NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|289629249|ref|NP_001166206|]
View 

protein phosphatase 1 regulatory inhibitor subunit 16B isoform 2 [Homo sapiens]

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 13328237)

ankyrin repeat (ANK) domain-containing protein mediates specific protein-protein interactions without necessarily recognizing specific primary sequences which allows for one ankyrin repeat domain to recognize and bind to a variety of intracellular substrates and may be involved in a wide array of functions

CATH:  1.25.40.20
Gene Ontology:  GO:0005515
PubMed:  33435370|15152081|17176038
SCOP:  4000366

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
71-199 3.07e-30

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 119.67  E-value: 3.07e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629249  71 ALLEASLRNDAEEVRYFLKNKVSPDLCNEDGLTALHQCCIDNFEEIVKLLLSHGANVNAKDNELWTPLHAAATCGHINLV 150
Cdd:COG0666  123 PLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 289629249 151 KILVQYGADLLAVNSDGNMPYDLCEDEPTLDVIETCMAYQGITQEKINE 199
Cdd:COG0666  203 KLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKD 251
PLN03192 super family cl33658
Voltage-dependent potassium channel; Provisional
 20-319 1.75e-10

Voltage-dependent potassium channel; Provisional


The actual alignment was detected with superfamily member PLN03192:

Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 63.73  E-value: 1.75e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629249  20 LERLRAAQKRRAQQLKKwaqyeQD--------LQHRKRKH-----ERKRSTGGRRKKVSFEASVaLLEASLRNDA--EEV 84
Cdd:PLN03192 471 LLRLKTSTLIEAMQTRQ-----EDnvvilknfLQHHKELHdlnvgDLLGDNGGEHDDPNMASNL-LTVASTGNAAllEEL 544

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629249  85 ryfLKNKVSPDLCNEDGLTALHQCCIDNFEEIVKLLLSHGANVNAKDNELWTPLHAAATCGHINLVKILVQYgadllAVN 164
Cdd:PLN03192 545 ---LKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHF-----ASI 616

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629249 165 SDGNMPYDLcedeptldvieTCMAyqgitqEKINEMRVAPEqqmiadihcMIAAGQDLDWIDAQGATLMQ---------M 235
Cdd:PLN03192 617 SDPHAAGDL-----------LCTA------AKRNDLTAMKE---------LLKQGLNVDSEDHQGATALQvamaedhvdM 670

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629249 236 AELLVSHGASLSARTSMDEM-PIDLCEEEEFKvlllELKHKHDV------IMKSQLRHKSSLSRRTSSAGSRGKVVRRAS 308
Cdd:PLN03192 671 VRLLIMNGADVDKANTDDDFsPTELRELLQKR----ELGHSITIvdsvpaDEPDLGRDGGSRPGRLQGTSSDNQCRPRVS 746

                        330
                 ....*....|.
gi 289629249 309 LSDRTNLYRKE 319
Cdd:PLN03192 747 IYKGHPLLRNE 757
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
71-199 3.07e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 119.67  E-value: 3.07e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629249  71 ALLEASLRNDAEEVRYFLKNKVSPDLCNEDGLTALHQCCIDNFEEIVKLLLSHGANVNAKDNELWTPLHAAATCGHINLV 150
Cdd:COG0666  123 PLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 289629249 151 KILVQYGADLLAVNSDGNMPYDLCEDEPTLDVIETCMAYQGITQEKINE 199
Cdd:COG0666  203 KLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKD 251
Ank_2 pfam12796
Ankyrin repeats (3 copies);
72-164 7.96e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.49  E-value: 7.96e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629249   72 LLEASLRNDAEEVRYFLKNKVSPDLCNEDGLTALHQCCIDNFEEIVKLLLSHgANVNAKDNElWTPLHAAATCGHINLVK 151
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNG-RTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 289629249  152 ILVQYGADLLAVN 164
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 78-170 3.61e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 71.23  E-value: 3.61e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629249  78 RNDAEEVRYFLKNKVSPDLCNEDGLTALHQ----CCIDNfeEIVKLLLSHGANVNAKDN-EL---------------WTP 137
Cdd:PHA03100 118 SNSYSIVEYLLDNGANVNIKNSDGENLLHLylesNKIDL--KILKLLIDKGVDINAKNRvNYllsygvpinikdvygFTP 195

                         90       100       110
                 ....*....|....*....|....*....|...
gi 289629249 138 LHAAATCGHINLVKILVQYGADLLAVNSDGNMP 170
Cdd:PHA03100 196 LHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTP 228
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 20-319 1.75e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 63.73  E-value: 1.75e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629249  20 LERLRAAQKRRAQQLKKwaqyeQD--------LQHRKRKH-----ERKRSTGGRRKKVSFEASVaLLEASLRNDA--EEV 84
Cdd:PLN03192 471 LLRLKTSTLIEAMQTRQ-----EDnvvilknfLQHHKELHdlnvgDLLGDNGGEHDDPNMASNL-LTVASTGNAAllEEL 544

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629249  85 ryfLKNKVSPDLCNEDGLTALHQCCIDNFEEIVKLLLSHGANVNAKDNELWTPLHAAATCGHINLVKILVQYgadllAVN 164
Cdd:PLN03192 545 ---LKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHF-----ASI 616

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629249 165 SDGNMPYDLcedeptldvieTCMAyqgitqEKINEMRVAPEqqmiadihcMIAAGQDLDWIDAQGATLMQ---------M 235
Cdd:PLN03192 617 SDPHAAGDL-----------LCTA------AKRNDLTAMKE---------LLKQGLNVDSEDHQGATALQvamaedhvdM 670

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629249 236 AELLVSHGASLSARTSMDEM-PIDLCEEEEFKvlllELKHKHDV------IMKSQLRHKSSLSRRTSSAGSRGKVVRRAS 308
Cdd:PLN03192 671 VRLLIMNGADVDKANTDDDFsPTELRELLQKR----ELGHSITIvdsvpaDEPDLGRDGGSRPGRLQGTSSDNQCRPRVS 746

                        330
                 ....*....|.
gi 289629249 309 LSDRTNLYRKE 319
Cdd:PLN03192 747 IYKGHPLLRNE 757
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 67-170 3.08e-06

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 50.01  E-value: 3.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629249  67 EASVALLEASlrndaeevryflknkvsPDLCNE-------DGLTALHQCCIDNFEEIVKLLLSHGANVNA---------- 129
Cdd:cd22192   65 EAAVVLMEAA-----------------PELVNEpmtsdlyQGETALHIAVVNQNLNLVRELIARGADVVSpratgtffrp 127

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 289629249 130 -KDNELW---TPLHAAATCGHINLVKILVQYGADLLAVNSDGNMP 170
Cdd:cd22192  128 gPKNLIYygeHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTV 172
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 100-129 1.08e-05

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.19  E-value: 1.08e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 289629249   100 DGLTALHQCCIDNFEEIVKLLLSHGANVNA 129
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 67-178 6.97e-04

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 42.38  E-value: 6.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629249   67 EASVALLEASLRndaEEVRYFLKNkvSPDLCNE-DGLTALHQCCIDNFEEIVKLLLSHGANVNAKDN------------- 132
Cdd:TIGR00870  98 EAILLHLLAAFR---KSGPLELAN--DQYTSEFtPGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsf 172

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 289629249  133 ---ELwtPLHAAATCGHINLVKILVQYGADLLAVNSDGNMPYDLCEDEP 178
Cdd:TIGR00870 173 yhgES--PLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVMEN 219
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
71-199 3.07e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 119.67  E-value: 3.07e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629249  71 ALLEASLRNDAEEVRYFLKNKVSPDLCNEDGLTALHQCCIDNFEEIVKLLLSHGANVNAKDNELWTPLHAAATCGHINLV 150
Cdd:COG0666  123 PLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 289629249 151 KILVQYGADLLAVNSDGNMPYDLCEDEPTLDVIETCMAYQGITQEKINE 199
Cdd:COG0666  203 KLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKD 251
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
71-170 3.98e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 113.90  E-value: 3.98e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629249  71 ALLEASLRNDAEEVRYFLKNKVSPDLCNEDGLTALHQCCIDNFEEIVKLLLSHGANVNAKDNELWTPLHAAATCGHINLV 150
Cdd:COG0666   90 LLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169

                         90       100
                 ....*....|....*....|
gi 289629249 151 KILVQYGADLLAVNSDGNMP 170
Cdd:COG0666  170 KLLLEAGADVNARDNDGETP 189
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
71-273 2.80e-25

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 105.81  E-value: 2.80e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629249  71 ALLEASLRNDAEEVRYFLKNKVSPDLCNEDGLTALHQCCIDNFEEIVKLLLSHGANVNAKDNELWTPLHAAATCGHINLV 150
Cdd:COG0666   57 LLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIV 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629249 151 KILVQYGADLLAVNSDGNMPYDLCEDEPTLDVIETcmayqgitqekinemrvapeqqmiadihcMIAAGQDLDWIDAQGA 230
Cdd:COG0666  137 KLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKL-----------------------------LLEAGADVNARDNDGE 187

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 289629249 231 T-LM--------QMAELLVSHGASLSARTSMDEMPIDLCEEEEFKVLLLELK 273
Cdd:COG0666  188 TpLHlaaenghlEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239
Ank_2 pfam12796
Ankyrin repeats (3 copies);
72-164 7.96e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.49  E-value: 7.96e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629249   72 LLEASLRNDAEEVRYFLKNKVSPDLCNEDGLTALHQCCIDNFEEIVKLLLSHgANVNAKDNElWTPLHAAATCGHINLVK 151
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNG-RTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 289629249  152 ILVQYGADLLAVN 164
Cdd:pfam12796  79 LLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
71-173 5.41e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 96.18  E-value: 5.41e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629249  71 ALLEASLRNDAEEVRYFLKNKVSPDLCNEDGLTALHQCCIDNFEEIVKLLLSHGANVNAKDNELWTPLHAAATCGHINLV 150
Cdd:COG0666  156 PLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIV 235

                         90       100
                 ....*....|....*....|...
gi 289629249 151 KILVQYGADLLAVNSDGNMPYDL 173
Cdd:COG0666  236 KLLLEAGADLNAKDKDGLTALLL 258
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 78-170 3.61e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 71.23  E-value: 3.61e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629249  78 RNDAEEVRYFLKNKVSPDLCNEDGLTALHQ----CCIDNfeEIVKLLLSHGANVNAKDN-EL---------------WTP 137
Cdd:PHA03100 118 SNSYSIVEYLLDNGANVNIKNSDGENLLHLylesNKIDL--KILKLLIDKGVDINAKNRvNYllsygvpinikdvygFTP 195

                         90       100       110
                 ....*....|....*....|....*....|...
gi 289629249 138 LHAAATCGHINLVKILVQYGADLLAVNSDGNMP 170
Cdd:PHA03100 196 LHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTP 228
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 84-269 1.60e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 69.31  E-value: 1.60e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629249  84 VRYFLKNKVSPDLCNEDGLTALHQCCIDNFE-----EIVKLLLSHGANVNAKDNELWTPLHAAATC--GHINLVKILVQY 156
Cdd:PHA03100  51 VKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDN 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629249 157 GADLLAVNSDGNMP--YDLCEDEPTLDVIETcMAYQGItqeKINEMRVapeqqmiadIHCMIAAGQDLDWIDAQGATLMQ 234
Cdd:PHA03100 131 GANVNIKNSDGENLlhLYLESNKIDLKILKL-LIDKGV---DINAKNR---------VNYLLSYGVPINIKDVYGFTPLH 197

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 289629249 235 MA---------ELLVSHGASLSARTSMDEMP----IDLCEEEEFKVLL 269
Cdd:PHA03100 198 YAvynnnpefvKYLLDLGANPNLVNKYGDTPlhiaILNNNKEIFKLLL 245
Ank_4 pfam13637
Ankyrin repeats (many copies);
101-154 4.02e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 61.14  E-value: 4.02e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 289629249  101 GLTALHQCCIDNFEEIVKLLLSHGANVNAKDNELWTPLHAAATCGHINLVKILV 154
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
71-168 1.31e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 65.36  E-value: 1.31e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629249  71 ALLEASLRNDAEEVRYFLKNKVSPDLCNEDGLTALHQCCIDNFEEIVKLLLSHGANVNAKDNELWTPLHAAATCGHINLV 150
Cdd:COG0666  189 PLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIV 268

                         90
                 ....*....|....*...
gi 289629249 151 KILVQYGADLLAVNSDGN 168
Cdd:COG0666  269 KLLLLALLLLAAALLDLL 286
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 117-189 3.66e-11

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 65.69  E-value: 3.66e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 289629249 117 VKLLLSHGANVNAKDNELWTPLHAAATCGHINLVKILVQYGADLLAVNSDGNMPYDLCEDEPTLDVIETCMAY 189
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PHA03095 PHA03095
ankyrin-like protein; Provisional
 71-172 8.55e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 64.28  E-value: 8.55e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629249  71 ALLEASLRNDAEEVRYFLKNKV---SPDLCnedGLTALHQC-CIDNFEEIVKLLLSHGANVNAKDNELWTPLHAAAT--C 144
Cdd:PHA03095  53 LYLHYSSEKVKDIVRLLLEAGAdvnAPERC---GFTPLHLYlYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVYLSgfN 129

                         90       100
                 ....*....|....*....|....*...
gi 289629249 145 GHINLVKILVQYGADLLAVNSDGNMPYD 172
Cdd:PHA03095 130 INPKVIRLLLRKGADVNALDLYGMTPLA 157
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 20-319 1.75e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 63.73  E-value: 1.75e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629249  20 LERLRAAQKRRAQQLKKwaqyeQD--------LQHRKRKH-----ERKRSTGGRRKKVSFEASVaLLEASLRNDA--EEV 84
Cdd:PLN03192 471 LLRLKTSTLIEAMQTRQ-----EDnvvilknfLQHHKELHdlnvgDLLGDNGGEHDDPNMASNL-LTVASTGNAAllEEL 544

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629249  85 ryfLKNKVSPDLCNEDGLTALHQCCIDNFEEIVKLLLSHGANVNAKDNELWTPLHAAATCGHINLVKILVQYgadllAVN 164
Cdd:PLN03192 545 ---LKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHF-----ASI 616

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629249 165 SDGNMPYDLcedeptldvieTCMAyqgitqEKINEMRVAPEqqmiadihcMIAAGQDLDWIDAQGATLMQ---------M 235
Cdd:PLN03192 617 SDPHAAGDL-----------LCTA------AKRNDLTAMKE---------LLKQGLNVDSEDHQGATALQvamaedhvdM 670

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629249 236 AELLVSHGASLSARTSMDEM-PIDLCEEEEFKvlllELKHKHDV------IMKSQLRHKSSLSRRTSSAGSRGKVVRRAS 308
Cdd:PLN03192 671 VRLLIMNGADVDKANTDDDFsPTELRELLQKR----ELGHSITIvdsvpaDEPDLGRDGGSRPGRLQGTSSDNQCRPRVS 746

                        330
                 ....*....|.
gi 289629249 309 LSDRTNLYRKE 319
Cdd:PLN03192 747 IYKGHPLLRNE 757
Ank_5 pfam13857
Ankyrin repeats (many copies);
120-174 9.32e-10

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 54.27  E-value: 9.32e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 289629249  120 LLSHG-ANVNAKDNELWTPLHAAATCGHINLVKILVQYGADLLAVNSDGNMPYDLC 174
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03095 PHA03095
ankyrin-like protein; Provisional
 77-259 2.63e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 59.27  E-value: 2.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629249  77 LRNDAEE--VRYFLKNKVSPDLCNEDGLTALHQC----CIDnfEEIVKLLLSHGANVNAKDNELWTPLHA-----AATcg 145
Cdd:PHA03095  91 LYNATTLdvIKLLIKAGADVNAKDKVGRTPLHVYlsgfNIN--PKVIRLLLRKGADVNALDLYGMTPLAVllksrNAN-- 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629249 146 hINLVKILVQYGADLLAVNSDGNMPydlcedeptLDVI-ETCMAYQGITQEKI---------NEMRVAPEQQMIADIHC- 214
Cdd:PHA03095 167 -VELLRLLIDAGADVYAVDDRFRSL---------LHHHlQSFKPRARIVRELIragcdpaatDMLGNTPLHSMATGSSCk 236

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629249 215 ------MIAAGQDLDWIDAQGATLMQMA---------ELLVSHGASLSARTSMDEMPIDL 259
Cdd:PHA03095 237 rslvlpLLIAGISINARNRYGQTPLHYAavfnnpracRRLIALGADINAVSSDGNTPLSL 296
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 79-159 3.27e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 58.91  E-value: 3.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629249  79 NDAEEVRYFLKNKVSPDLCNEDGLTALHQCCIDNFEEIVKLLLSHGANVNAKDNELWTPLHAAATCGHINLVKILVQYGA 158
Cdd:PHA03100 170 NAKNRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249


                 .
gi 289629249 159 D 159
Cdd:PHA03100 250 S 250
PHA03095 PHA03095
ankyrin-like protein; Provisional
 73-246 1.08e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 57.34  E-value: 1.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629249  73 LEASLRNDAEEVRYFLKNKVSPDLCNEDGLTALHQCC---IDNFEEIVKLLLSHGANVNAKDNELWTPLHAAATCGH-IN 148
Cdd:PHA03095  19 LLNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLhysSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLD 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629249 149 LVKILVQYGADLLAVNSDGNMPydlcedeptldvIETCMAyqgitqekinEMRVAPEQqmiadIHCMIAAGQDLDWIDAQ 228
Cdd:PHA03095  99 VIKLLIKAGADVNAKDKVGRTP------------LHVYLS----------GFNINPKV-----IRLLLRKGADVNALDLY 151

                        170
                 ....*....|....*...
gi 289629249 229 GATlmQMAELLVSHGASL 246
Cdd:PHA03095 152 GMT--PLAVLLKSRNANV 167
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 78-170 9.20e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 54.58  E-value: 9.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629249  78 RNDAEEVRYFLKNKVSPDLCNEDGLTALHQCCIDNFEEIVKLLLSHGANVNAKDNELWTPLHAAATCGHINLVKILVQYG 157
Cdd:PHA02874 134 KGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHG 213

                         90
                 ....*....|...
gi 289629249 158 ADLLAVNSDGNMP 170
Cdd:PHA02874 214 NHIMNKCKNGFTP 226
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 71-201 1.54e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 53.52  E-value: 1.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629249  71 ALLEASLRNDAEEVRYFLKNKVSPDLCNEDGLTALHQCCIDNFEEIVKLLLSHGANVNAKDNEL----WTPLHAaatcgh 146
Cdd:PHA03100 195 PLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIETLlyfkDKDLNT------ 268

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 289629249 147 INLVKILVQYGADLLAVNSD--GNMPYdLCEDEPTLDVIETCmayqgitQEKINEMR 201
Cdd:PHA03100 269 ITKIKMLKKSIMYMFLLDPGfyKNRKL-IENSKSLKDVINEC-------EKEIERMK 317
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 100-132 1.94e-07

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 47.28  E-value: 1.94e-07
                          10        20        30
                  ....*....|....*....|....*....|....
gi 289629249  100 DGLTALHQCCID-NFEEIVKLLLSHGANVNAKDN 132
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 116-355 3.86e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 52.76  E-value: 3.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629249 116 IVKLLLSHGANVNAKDNELWTPLHAAATCGHINLVKILVQYGADLLAVNSDGNMPYDLCEDEPTLDVIETCMAyqgiTQE 195
Cdd:PHA02876 160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIID----NRS 235

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629249 196 KINEmrvapeqqmiadihcmiaagQDLDWIDAQGATLMQMAELLVSHGASLSArtsmdempIDLCEeeefkvlllelkhk 275
Cdd:PHA02876 236 NINK--------------------NDLSLLKAIRNEDLETSLLLYDAGFSVNS--------IDDCK-------------- 273

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629249 276 hdvimKSQLRHKS---SLSRRTSSAGSRGKVVRRASLSDRTNLY---RKEYEGEAI--LWQRSAAEDQRTSTYNGDIRET 347
Cdd:PHA02876 274 -----NTPLHHASqapSLSRLVPKLLERGADVNAKNIKGETPLYlmaKNGYDTENIrtLIMLGADVNAADRLYITPLHQA 348


                 ....*...
gi 289629249 348 RTDQENKD 355
Cdd:PHA02876 349 STLDRNKD 356
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 84-170 3.87e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 52.57  E-value: 3.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629249  84 VRYFLKNKVSPDLCNEDGLTALHQC---CIDnfEEIVKLLLSHGANVNAKDNEL-WTPLHAAATCGHInlVKILVQYGAD 159
Cdd:PHA02878 217 VHILLENGASTDARDKCGNTPLHISvgyCKD--YDILKLLLEHGVDVNAKSYILgLTALHSSIKSERK--LKLLLEYGAD 292

                         90
                 ....*....|.
gi 289629249 160 LLAVNSDGNMP 170
Cdd:PHA02878 293 INSLNSYKLTP 303
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 80-182 7.31e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 51.99  E-value: 7.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629249  80 DAEEVRYFLKNKVSPDLCNEDGLTALHQCC-IDNFEEIVKLLLSHGANVNAKDNELWTPLHAAATCGHINLVKILVQYGA 158
Cdd:PHA02876 320 DTENIRTLIMLGADVNAADRLYITPLHQAStLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGA 399

                         90       100
                 ....*....|....*....|....*.
gi 289629249 159 DLLAVNSD--GNMPYDLCEDEPTLDV 182
Cdd:PHA02876 400 DIEALSQKigTALHFALCGTNPYMSV 425
PHA02798 PHA02798
ankyrin-like protein; Provisional
 115-170 8.37e-07

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 51.37  E-value: 8.37e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 289629249 115 EIVKLLLSHGANVNAKDNELWTPLHAAATC-----GHINLVKILVQYGADLLAVNSDGNMP 170
Cdd:PHA02798  52 DIVKLFINLGANVNGLDNEYSTPLCTILSNikdykHMLDIVKILIENGADINKKNSDGETP 112
Ank_4 pfam13637
Ankyrin repeats (many copies);
71-121 1.94e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.96  E-value: 1.94e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 289629249   71 ALLEASLRNDAEEVRYFLKNKVSPDLCNEDGLTALHQCCIDNFEEIVKLLL 121
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 72-160 2.14e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 49.99  E-value: 2.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629249  72 LLEASLRNDAEEVRYFLK-NKVSPDLCNEDGLTALHQCCIDNFEEIVKLLLSHGANVNAKDNELWTPLHAAATCGHINLV 150
Cdd:PHA02875  72 LHDAVEEGDVKAVEELLDlGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGI 151

                         90
                 ....*....|
gi 289629249 151 KILVQYGADL 160
Cdd:PHA02875 152 ELLIDHKACL 161
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 70-246 2.33e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 49.99  E-value: 2.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629249  70 VALLEASLRNDAEEVRYFLKNKVSPDLCNEDGLTALHQCCIDNFEEIVKLLLSHGANVNAKDNELWTPLHAAATCGHINL 149
Cdd:PHA02875   4 VALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629249 150 VKILV---QYGADLlaVNSDGNMPYDLCEDEPTLDVIETCMAYQGITQekinemrvAPEQQMIADIHCMIAAGQdldwid 226
Cdd:PHA02875  84 VEELLdlgKFADDV--FYKDGMTPLHLATILKKLDIMKLLIARGADPD--------IPNTDKFSPLHLAVMMGD------ 147

                        170       180
                 ....*....|....*....|
gi 289629249 227 aqgatlMQMAELLVSHGASL 246
Cdd:PHA02875 148 ------IKGIELLIDHKACL 161
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 67-170 3.08e-06

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 50.01  E-value: 3.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629249  67 EASVALLEASlrndaeevryflknkvsPDLCNE-------DGLTALHQCCIDNFEEIVKLLLSHGANVNA---------- 129
Cdd:cd22192   65 EAAVVLMEAA-----------------PELVNEpmtsdlyQGETALHIAVVNQNLNLVRELIARGADVVSpratgtffrp 127

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 289629249 130 -KDNELW---TPLHAAATCGHINLVKILVQYGADLLAVNSDGNMP 170
Cdd:cd22192  128 gPKNLIYygeHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTV 172
PHA02946 PHA02946
ankyin-like protein; Provisional
 80-188 4.56e-06

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 49.28  E-value: 4.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629249  80 DAEEVRYFLKNKVSPDLCNEDGLTALHQCCIDNFEEIVKLLLSHGANVNAKDNELWTPLHAAATCGH--INLVKILVQYG 157
Cdd:PHA02946  51 DERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYG 130

                         90       100       110
                 ....*....|....*....|....*....|..
gi 289629249 158 ADL-LAVNSDGNMPYDLCEDePTLDVIETCMA 188
Cdd:PHA02946 131 AKInNSVDEEGCGPLLACTD-PSERVFKKIMS 161
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 75-212 5.22e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 48.83  E-value: 5.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629249  75 ASLRNDAEEVRYFLKNKVSPDLCNEDGLTALHQCCIDNFEEIVKLLLSHGANVNAKDNELWTPLHAAATCGHINLVKILV 154
Cdd:PHA02875 109 ATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLL 188

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 289629249 155 QYGADLLAVNSDGN---MPYDLCEDEPTL-----------DVIETCMAYQGITQEKINEMRVAPEQQ----MIADI 212
Cdd:PHA02875 189 DSGANIDYFGKNGCvaaLCYAIENNKIDIvrlfikrgadcNIMFMIEGEECTILDMICNMCTNLESEaidaLIADI 264
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 135-164 6.79e-06

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 42.66  E-value: 6.79e-06
                          10        20        30
                  ....*....|....*....|....*....|.
gi 289629249  135 WTPLHAAAT-CGHINLVKILVQYGADLLAVN 164
Cdd:pfam00023   3 NTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 80-170 9.22e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 48.34  E-value: 9.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629249  80 DAEEVRYFLKNKVSPDLCNEDGL-TALHQCCIDNFEEIVKLLLSHGANVNAKDNELWTPLHAAATCGHINLVKILVQYGA 158
Cdd:PHA02878 146 EAEITKLLLSYGADINMKDRHKGnTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225

                         90
                 ....*....|..
gi 289629249 159 DLLAVNSDGNMP 170
Cdd:PHA02878 226 STDARDKCGNTP 237
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 100-129 1.08e-05

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.19  E-value: 1.08e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 289629249   100 DGLTALHQCCIDNFEEIVKLLLSHGANVNA 129
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 109-198 1.22e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 47.65  E-value: 1.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629249 109 CIDNfeEIVKLLLSHGANVNAKDNELWTPLHAAATCGHINLVKILVQYGADLLAVNSDGNMPYDLCEDEPTLDVIETCM- 187
Cdd:PHA02874 101 CIEK--DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLe 178

                         90
                 ....*....|...
gi 289629249 188 --AYQGITQEKIN 198
Cdd:PHA02874 179 kgAYANVKDNNGE 191
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 135-160 2.02e-05

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.42  E-value: 2.02e-05
                           10        20
                   ....*....|....*....|....*.
gi 289629249   135 WTPLHAAATCGHINLVKILVQYGADL 160
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADI 28
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 80-170 2.55e-05

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 47.21  E-value: 2.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629249  80 DAEEVRYFLKNKVSPDLCNEDGLTALHQCCIDNF--EEIVKLLLSHGANVNAKDNELWTPLHA------------AATCG 145
Cdd:PHA02716 296 DISVVYSFLQPGVKLHYKDSAGRTCLHQYILRHNisTDIIKLLHEYGNDLNEPDNIGNTVLHTylsmlsvvnildPETDN 375

                         90       100
                 ....*....|....*....|....*..
gi 289629249 146 HINL--VKILVQYGADLLAVNSDGNMP 170
Cdd:PHA02716 376 DIRLdvIQCLISLGADITAVNCLGYTP 402
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 100-129 2.66e-05

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 41.09  E-value: 2.66e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 289629249  100 DGLTALHQCCIDNFEEIVKLLLSHGANVNA 129
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA03095 PHA03095
ankyrin-like protein; Provisional
 76-170 2.79e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.56  E-value: 2.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629249  76 SLRNDAEEVRYFLKNKVSPDLCNEDGLTALHQCCIDNFEEIVKL--LLSHGANVNAKDNELWTPLHAAATCGHINLVKIL 153
Cdd:PHA03095 197 SFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRL 276

                         90
                 ....*....|....*..
gi 289629249 154 VQYGADLLAVNSDGNMP 170
Cdd:PHA03095 277 IALGADINAVSSDGNTP 293
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 82-170 3.33e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 46.50  E-value: 3.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629249  82 EEVRYFLKNKVSPDLCNEDGLTALHQCCIDNFEEIVKLLLSHGANVNAKDNELWTPLHAAATCGHINLVKILVQYGADLL 161
Cdd:PHA02874 105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184


                 ....*....
gi 289629249 162 AVNSDGNMP 170
Cdd:PHA02874 185 VKDNNGESP 193
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 69-160 3.97e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 46.03  E-value: 3.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629249  69 SVALLEASLRNDAEEVRYFL---KNKVSPDLCNEdglTALHQCCIDNFEEIVKLLLSHGANVNAKDNELWTPLH-AAATC 144
Cdd:PHA02878 169 NTALHYATENKDQRLTELLLsygANVNIPDKTNN---SPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHiSVGYC 245

                         90
                 ....*....|....*.
gi 289629249 145 GHINLVKILVQYGADL 160
Cdd:PHA02878 246 KDYDILKLLLEHGVDV 261
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 75-170 4.53e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.21  E-value: 4.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629249  75 ASLRNDAEEVRYFLKNKVSPDLCNEDGLTALH-QCCIDNFEEIVKLLLSHGANVNAKDNELWTPLHAAA--TCgHINLVK 151
Cdd:PHA02876 382 AAVRNNVVIINTLLDYGADIEALSQKIGTALHfALCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACkkNC-KLDVIE 460

                         90
                 ....*....|....*....
gi 289629249 152 ILVQYGADLLAVNSDGNMP 170
Cdd:PHA02876 461 MLLDNGADVNAINIQNQYP 479
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 37-159 8.75e-05

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 45.39  E-value: 8.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629249  37 WAQY--EQDLQHRKRKHErkrstggrrkkvsfeasVALLEASLRNDAEEVRYFLKNKvSPDLCNEDGL--TALHQCCIDN 112
Cdd:cd22192    1 WAQMldELHLLQQKRISE-----------------SPLLLAAKENDVQAIKKLLKCP-SCDLFQRGALgeTALHVAALYD 62

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 289629249 113 FEEIVKLLLSHGAN-VN-AKDNELW---TPLHAAATCGHINLVKILVQYGAD 159
Cdd:cd22192   63 NLEAAVVLMEAAPElVNePMTSDLYqgeTALHIAVVNQNLNLVRELIARGAD 114
Ank_4 pfam13637
Ankyrin repeats (many copies);
135-170 1.12e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.95  E-value: 1.12e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 289629249  135 WTPLHAAATCGHINLVKILVQYGADLLAVNSDGNMP 170
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETA 37
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 135-162 1.51e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 38.78  E-value: 1.51e-04
                          10        20
                  ....*....|....*....|....*...
gi 289629249  135 WTPLHAAATCGHINLVKILVQYGADLLA 162
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 78-171 4.42e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 41.73  E-value: 4.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629249  78 RNDAEEVRYFLKnkvSPDLCNEDGLTALHQCCIDNF--EEIVKLLLSHGANVNAK--DNELwTPLHAAATCG---HINLV 150
Cdd:PHA02859  31 KDDIEGVKKWIK---FVNDCNDLYETPIFSCLEKDKvnVEILKFLIENGADVNFKtrDNNL-SALHHYLSFNknvEPEIL 106

                         90       100
                 ....*....|....*....|.
gi 289629249 151 KILVQYGADLLAVNSDGNMPY 171
Cdd:PHA02859 107 KILIDSGSSITEEDEDGKNLL 127
Ank_5 pfam13857
Ankyrin repeats (many copies);
92-141 4.96e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.10  E-value: 4.96e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 289629249   92 VSPDLCNEDGLTALHQCCIDNFEEIVKLLLSHGANVNAKDNELWTPLHAA 141
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 67-178 6.97e-04

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 42.38  E-value: 6.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629249   67 EASVALLEASLRndaEEVRYFLKNkvSPDLCNE-DGLTALHQCCIDNFEEIVKLLLSHGANVNAKDN------------- 132
Cdd:TIGR00870  98 EAILLHLLAAFR---KSGPLELAN--DQYTSEFtPGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsf 172

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 289629249  133 ---ELwtPLHAAATCGHINLVKILVQYGADLLAVNSDGNMPYDLCEDEP 178
Cdd:TIGR00870 173 yhgES--PLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVMEN 219
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 98-160 7.38e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 42.36  E-value: 7.38e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 289629249  98 NEDGLTALHQCCIDNFE-EIVKLLLSHGANVNAKDNELWTPLHAAatCGHINLVKILVQYGADL 160
Cdd:PHA02876 439 NKDLSTPLHYACKKNCKlDVIEMLLDNGADVNAINIQNQYPLLIA--LEYHGIVNILLHYGAEL 500
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 117-173 1.97e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 40.35  E-value: 1.97e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 289629249 117 VKLLLSHGANVNAKDNEL-WTPLHAAATCGHINLVKILVQYGADLLAVNSDGNMPYDL 173
Cdd:PHA02884  86 AKLLIRYGADVNRYAEEAkITPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIEL 143
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 114-206 2.82e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 39.42  E-value: 2.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629249 114 EEIVKLLLSHGANVNAKDNELWTPLHAAAT-CG-HINLVKILVQYGADLLAVNSDGN---MPYDLCEDEptlDVIETCMA 188
Cdd:PHA02859 103 PEILKILIDSGSSITEEDEDGKNLLHMYMCnFNvRINVIKLLIDSGVSFLNKDFDNNnilYSYILFHSD---KKIFDFLT 179

                         90
                 ....*....|....*...
gi 289629249 189 YQGITQEKINEMRVAPEQ 206
Cdd:PHA02859 180 SLGIDINETNKSGYNCYD 197
Ank_5 pfam13857
Ankyrin repeats (many copies);
75-106 3.56e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.79  E-value: 3.56e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 289629249   75 ASLRNDAEEVRYFLKNKVSPDLCNEDGLTALH 106
Cdd:pfam13857  23 AAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH