|
Name |
Accession |
Description |
Interval |
E-value |
| eukary_SO_Moco |
cd02111 |
molybdopterin binding domain of sulfite oxidase (SO). SO catalyzes the terminal reaction in ... |
185-543 |
0e+00 |
|
molybdopterin binding domain of sulfite oxidase (SO). SO catalyzes the terminal reaction in the oxidative degradation of the sulfur-containing amino acids cysteine and methionine. Common features of all known members of the sulfite oxidase (SO) family of molybdopterin binding domains are that they contain one single pterin cofactor and part of the coordination of the metal (Mo) is a cysteine ligand of the protein and that they catalyze the transfer of an oxygen to or from a lone pair of electrons on the substrate.
Pssm-ID: 239029 [Multi-domain] Cd Length: 365 Bit Score: 598.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099694 185 ALKVNSQRPFNAEPPPELLTENYITPNPIFFTRNHLPVPNLDPDTYRLHVVGaPGGQSLSLSLDDLH-NFPRYEITVTLQ 263
Cdd:cd02111 1 ALKVNSKKPFNAEPPSSLLASSFITPNELFYVRNHLPVPVVDPDTYSLEVEG-PDGTTLSLSLEDLKsLFPKHEVTATLQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099694 264 CAGNRRSEMTQVKEVKGLEWRTGAISTARWAGARLCDVLAQAGHQLC--ETEAHVCFEGLDSDPTGTAYGASIPLARAMD 341
Cdd:cd02111 80 CAGNRRSEMTKVKKVKGLQWGDGAISNAEWGGARLRDVLLDAGIPEDdsQGGLHVHFEGLDVDPTGTPYGASIPLSKALD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099694 342 PEAEVLLAYEMNGQPLPRDHGFPVRVVVPGVVGARHVKWLGRVSVQPEESYSHWQRRDYKGFSPSVDWETVDFDSAPSIQ 421
Cdd:cd02111 160 PEADVLLAYEMNGTPLPRDHGFPLRVVVPGVVGARSVKWLDRIVVSDEESDSHWQQNDYKGFSPSVDWDNVDFSKAPAIQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099694 422 ELPVQSAITEPRDGE---TVESGEVTIKGYAWSGGGRAVIRVDVSLDGGLTWQVAKLDGEEQR--PRKAWAWRLWQLKAP 496
Cdd:cd02111 240 EMPVQSAICSPSVGApvvTVPPGKITVKGYAWSGGGRKIVRVDVSLDGGRTWKVAELEQEENVwpSGRKWAWTLWEATVP 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 74099694 497 VPAGqKELNIVCKAVDDGYNVQPDTVAPIWNLRGVLSNAWHRVHVYV 543
Cdd:cd02111 320 VPAG-KEAEIIAKAVDSAYNVQPETVEPIWNLRGVLNNAWHRVKVVV 365
|
|
| PLN00177 |
PLN00177 |
sulfite oxidase; Provisional |
168-543 |
2.70e-123 |
|
sulfite oxidase; Provisional
Pssm-ID: 177772 [Multi-domain] Cd Length: 393 Bit Score: 367.64 E-value: 2.70e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099694 168 PTVETSDPYADDPVRHPALKVNSQRPFNAEPPPELLTENYITPNPIFFTRNHLPVPNLDP-DTYRLHVVGAPGgQSLSLS 246
Cdd:PLN00177 2 PGLRGPSDYSQEPPRHPSLKINAKEPFNAEPPRSALVSSYITPVDLFYKRNHGPIPIVDDiERYSVTITGLIE-NPRKLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099694 247 LDDLHNFPRYEITVTLQCAGNRRSEMTQVKEVKGLEWRTGAISTARWAGARLCDVLAQAG-HQLCETEA----HVCFEGL 321
Cdd:PLN00177 81 MKDIRKLPKYNVTATLQCAGNRRTAMSKVRKVRGVGWDVSAIGNAVWGGAKLADVLELVGiPKLTSITSsggkHVEFVSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099694 322 DSDP--TGTAYGASIPLARAMDPEAEVLLAYEMNGQPLPRDHGFPVRVVVPGVVGARHVKWLGRVSVQPEESYSHWQRRD 399
Cdd:PLN00177 161 DKCKeeNGGPYKASIPLSQATNPEADVLLAYEMNGEVLNRDHGYPLRVVVPGVIGARSVKWLDSINIIAEECQGFFMQKD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099694 400 YKGFSPSVDWETVDFDSAPSIQELPVQSAITEPRDGETVESGEVTIKGYAWSGGGRAVIRVDVSLDGGLTWQVAKLDGEE 479
Cdd:PLN00177 241 YKMFPPSVNWDNINWSTRRPQMDFPVQSAICSLEDVNAIKPGKVTVAGYALSGGGRGIERVDISVDGGKTWVEASRYQKP 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74099694 480 QRPRKA-------WAWRLWQLKAPVPAGQKelnIVCKAVDDGYNVQPDTVAPIWNLRGVLSNAWHRVHVYV 543
Cdd:PLN00177 321 GVPYISddissdkWAWVLFEATVDVPQSTE---IVAKAVDSAANVQPESVESIWNLRGILNTSWHRVQLRV 388
|
|
| Oxidored_molyb |
pfam00174 |
Oxidoreductase molybdopterin binding domain; This domain is found in a variety of ... |
219-395 |
1.38e-64 |
|
Oxidoreductase molybdopterin binding domain; This domain is found in a variety of oxidoreductases. This domain binds to a molybdopterin cofactor. Xanthine dehydrogenases, that also bind molybdopterin, have essentially no similarity.
Pssm-ID: 459699 [Multi-domain] Cd Length: 168 Bit Score: 207.74 E-value: 1.38e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099694 219 HLPVPNLDPDTYRLHVVGApGGQSLSLSLDDLHNFPRYEITVTLQCAGNRRSEMTQVKevkGLEWRTGAISTARWAGARL 298
Cdd:pfam00174 1 HGPVPEIDPDTWRLRVDGL-VEKPLTLTLDDLKAFPQVTVTATLQCVGNRRKEMNRVK---GVQWGGGAIGNAEWTGVPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099694 299 CDVLAQAGhqLCETEAHVCFEGLDSDPTGtAYGASIPLARAMDPEaeVLLAYEMNGQPLPRDHGFPVRVVVPGVVGARHV 378
Cdd:pfam00174 77 RDLLERAG--VKPGAKHVLFEGADTLGDG-GYTTSLPLEKALDDD--VLLAYEMNGEPLPPDHGYPLRLVVPGWYGARSV 151
|
170
....*....|....*..
gi 74099694 379 KWLGRVSVQPEESYSHW 395
Cdd:pfam00174 152 KWLRRIEVTDEESPGFW 168
|
|
| MsrP |
COG2041 |
Molybdopterin-dependent catalytic subunit of periplasmic DMSO/TMAO and ... |
214-405 |
2.44e-35 |
|
Molybdopterin-dependent catalytic subunit of periplasmic DMSO/TMAO and protein-methionine-sulfoxide reductases [Energy production and conversion];
Pssm-ID: 441644 [Multi-domain] Cd Length: 183 Bit Score: 130.66 E-value: 2.44e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099694 214 FFTRNHLPVPNLDPDTYRLHVVGApGGQSLSLSLDDLHNFPRYEITVTLQCAGNrrsemtqvkevkgleWRTGaisTARW 293
Cdd:COG2041 19 FPVRTAGGVPEIDPADWRLRVDGL-VEKPLTLTLDDLLALPLEERIYRLHCVEN---------------WSGG---VAPW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099694 294 AGARLCDVLAQAGHQlceTEA-HVCFEGLDSDptgtaYGASIPLARAMDPEAevLLAYEMNGQPLPRDHGFPVRvvvpgv 372
Cdd:COG2041 80 TGVPLRDLLERAGPK---PGAkYVLFESADPG-----YTESLPLDEALDPDT--LLAYGMNGEPLPPEHGAPLR------ 143
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 74099694 373 vgAR--------HVKWLGRVSVQPEESYSHWQRRDYKGFSP 405
Cdd:COG2041 144 --LVvpglygfkSAKWLVRIEVTDEDPPGYWETRGYHFYAN 182
|
|
| Cyt-b5 |
pfam00173 |
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from ... |
86-160 |
1.95e-18 |
|
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from a diverse range of proteins. This family also includes proteins that bind to steroids. The family includes progesterone receptors. Many members of this subfamily are membrane anchored by an N-terminal transmembrane alpha helix. This family also includes a domain in some chitin synthases. There is no known ligand for this domain in the chitin synthases.
Pssm-ID: 459698 [Multi-domain] Cd Length: 74 Bit Score: 79.59 E-value: 1.95e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74099694 86 TKEEVSSHTSPEtGIWVTLGSEVFDVTEFVDLHPGGPSKLMLAAGGPL-EPFWALyaVHNQSHVRELLAQYKIGEL 160
Cdd:pfam00173 1 TLEELSKHNGDG-DCWVAINGKVYDVTKFLKEHPGGEDVILSAAGKDAtDAFEAI--GHSEDAAEKLLKKYRIGEL 73
|
|
| PLN03199 |
PLN03199 |
delta6-acyl-lipid desaturase-like protein; Provisional |
80-175 |
3.48e-06 |
|
delta6-acyl-lipid desaturase-like protein; Provisional
Pssm-ID: 178740 [Multi-domain] Cd Length: 485 Bit Score: 49.65 E-value: 3.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099694 80 ESTHIYTKEEVSSHTSPETGiWVTLGSEVFDVTEFVDlHPGGPSKLMLAAGGPLEPFWALYAVHNQShvreLLAQYKIGE 159
Cdd:PLN03199 21 EKPQKISWQEVKKHASPDDA-WIIHQNKVYDVSNWHD-HPGGAVIFTHAGDDMTDIFAAFHAPGSQA----LMKKFYIGD 94
|
90
....*....|....*.
gi 74099694 160 LNPEdkvapTVETSDP 175
Cdd:PLN03199 95 LIPE-----STEHKDP 105
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| eukary_SO_Moco |
cd02111 |
molybdopterin binding domain of sulfite oxidase (SO). SO catalyzes the terminal reaction in ... |
185-543 |
0e+00 |
|
molybdopterin binding domain of sulfite oxidase (SO). SO catalyzes the terminal reaction in the oxidative degradation of the sulfur-containing amino acids cysteine and methionine. Common features of all known members of the sulfite oxidase (SO) family of molybdopterin binding domains are that they contain one single pterin cofactor and part of the coordination of the metal (Mo) is a cysteine ligand of the protein and that they catalyze the transfer of an oxygen to or from a lone pair of electrons on the substrate.
Pssm-ID: 239029 [Multi-domain] Cd Length: 365 Bit Score: 598.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099694 185 ALKVNSQRPFNAEPPPELLTENYITPNPIFFTRNHLPVPNLDPDTYRLHVVGaPGGQSLSLSLDDLH-NFPRYEITVTLQ 263
Cdd:cd02111 1 ALKVNSKKPFNAEPPSSLLASSFITPNELFYVRNHLPVPVVDPDTYSLEVEG-PDGTTLSLSLEDLKsLFPKHEVTATLQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099694 264 CAGNRRSEMTQVKEVKGLEWRTGAISTARWAGARLCDVLAQAGHQLC--ETEAHVCFEGLDSDPTGTAYGASIPLARAMD 341
Cdd:cd02111 80 CAGNRRSEMTKVKKVKGLQWGDGAISNAEWGGARLRDVLLDAGIPEDdsQGGLHVHFEGLDVDPTGTPYGASIPLSKALD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099694 342 PEAEVLLAYEMNGQPLPRDHGFPVRVVVPGVVGARHVKWLGRVSVQPEESYSHWQRRDYKGFSPSVDWETVDFDSAPSIQ 421
Cdd:cd02111 160 PEADVLLAYEMNGTPLPRDHGFPLRVVVPGVVGARSVKWLDRIVVSDEESDSHWQQNDYKGFSPSVDWDNVDFSKAPAIQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099694 422 ELPVQSAITEPRDGE---TVESGEVTIKGYAWSGGGRAVIRVDVSLDGGLTWQVAKLDGEEQR--PRKAWAWRLWQLKAP 496
Cdd:cd02111 240 EMPVQSAICSPSVGApvvTVPPGKITVKGYAWSGGGRKIVRVDVSLDGGRTWKVAELEQEENVwpSGRKWAWTLWEATVP 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 74099694 497 VPAGqKELNIVCKAVDDGYNVQPDTVAPIWNLRGVLSNAWHRVHVYV 543
Cdd:cd02111 320 VPAG-KEAEIIAKAVDSAYNVQPETVEPIWNLRGVLNNAWHRVKVVV 365
|
|
| PLN00177 |
PLN00177 |
sulfite oxidase; Provisional |
168-543 |
2.70e-123 |
|
sulfite oxidase; Provisional
Pssm-ID: 177772 [Multi-domain] Cd Length: 393 Bit Score: 367.64 E-value: 2.70e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099694 168 PTVETSDPYADDPVRHPALKVNSQRPFNAEPPPELLTENYITPNPIFFTRNHLPVPNLDP-DTYRLHVVGAPGgQSLSLS 246
Cdd:PLN00177 2 PGLRGPSDYSQEPPRHPSLKINAKEPFNAEPPRSALVSSYITPVDLFYKRNHGPIPIVDDiERYSVTITGLIE-NPRKLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099694 247 LDDLHNFPRYEITVTLQCAGNRRSEMTQVKEVKGLEWRTGAISTARWAGARLCDVLAQAG-HQLCETEA----HVCFEGL 321
Cdd:PLN00177 81 MKDIRKLPKYNVTATLQCAGNRRTAMSKVRKVRGVGWDVSAIGNAVWGGAKLADVLELVGiPKLTSITSsggkHVEFVSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099694 322 DSDP--TGTAYGASIPLARAMDPEAEVLLAYEMNGQPLPRDHGFPVRVVVPGVVGARHVKWLGRVSVQPEESYSHWQRRD 399
Cdd:PLN00177 161 DKCKeeNGGPYKASIPLSQATNPEADVLLAYEMNGEVLNRDHGYPLRVVVPGVIGARSVKWLDSINIIAEECQGFFMQKD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099694 400 YKGFSPSVDWETVDFDSAPSIQELPVQSAITEPRDGETVESGEVTIKGYAWSGGGRAVIRVDVSLDGGLTWQVAKLDGEE 479
Cdd:PLN00177 241 YKMFPPSVNWDNINWSTRRPQMDFPVQSAICSLEDVNAIKPGKVTVAGYALSGGGRGIERVDISVDGGKTWVEASRYQKP 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74099694 480 QRPRKA-------WAWRLWQLKAPVPAGQKelnIVCKAVDDGYNVQPDTVAPIWNLRGVLSNAWHRVHVYV 543
Cdd:PLN00177 321 GVPYISddissdkWAWVLFEATVDVPQSTE---IVAKAVDSAANVQPESVESIWNLRGILNTSWHRVQLRV 388
|
|
| SO_family_Moco_dimer |
cd02110 |
Subgroup of sulfite oxidase (SO) family molybdopterin binding domains that contains conserved ... |
213-541 |
4.57e-112 |
|
Subgroup of sulfite oxidase (SO) family molybdopterin binding domains that contains conserved dimerization domain. This molybdopterin cofactor (Moco) binding domain is found in a variety of oxidoreductases, main members of this family are nitrate reductase (NR) and sulfite oxidase (SO).
Pssm-ID: 239028 [Multi-domain] Cd Length: 317 Bit Score: 335.81 E-value: 4.57e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099694 213 IFFTRNHLPVPNLDPDTYRLHVVGApGGQSLSLSLDDLHNFPRYEITVTLQCAGNRRSEMTqvKEVKGLEWRTGAISTAR 292
Cdd:cd02110 1 LFFVRNHGGVPDIDPDAWRLEIHGL-VERPLTLTLDDLKRLPSVEVVATLECSGNGRGGFI--PVRSGAQWGHGAVGNAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099694 293 WAGARLCDVLAQAGHQlcETEAHVCFEGLDSDPTGTA--YGASIPLARAMDPEaeVLLAYEMNGQPLPRDHGFPVRVVVP 370
Cdd:cd02110 78 WTGVPLKDLLEEAGVK--PGAKHVLFEGADVPPGEKAadYTRSVPLSKALDDD--ALLAYEMNGEPLPPDHGYPLRLVVP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099694 371 GVVGARHVKWLGRVSVQPEESYSHWQRRDYKGFSPSVDWetVDFDSAPSIQELPVQSAITEPRDGETVESGEVTIKGYAW 450
Cdd:cd02110 154 GWYGARSVKWLRRIEVTDQPSDGYWQTRDYTVPPPDVDA--VGGKARRPIGEMPVKSVITSPSPGAELVSGGRVEIGGVA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099694 451 SGGGRAVIRVDVSLDGGLTWQVAKLDGEEQRPrkaWAWRLWQLKAPVPAGqkELNIVCKAVDDGYNVQPDTVAPIWNLRG 530
Cdd:cd02110 232 WSGGRGIRRVEVSLDGGRTWQEARLEGPLAGP---RAWRQWELDWDLPPG--EYELVARATDSTGNVQPERAEWNWNPGG 306
|
330
....*....|.
gi 74099694 531 VLSNAWHRVHV 541
Cdd:cd02110 307 YGNNHWHRVQV 317
|
|
| PLN02252 |
PLN02252 |
nitrate reductase [NADPH] |
177-543 |
2.49e-97 |
|
nitrate reductase [NADPH]
Pssm-ID: 215141 [Multi-domain] Cd Length: 888 Bit Score: 314.69 E-value: 2.49e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099694 177 ADDPV-RHPAL-KVNSQRPFNAEPP-PELLTENYITPNPIFFTRNHLPVPNLDPDTYRLHVVGAPGgQSLSLSLDDLHNF 253
Cdd:PLN02252 78 PDEWIpRHPSLvRLTGKHPFNCEPPlARLMEHGFITPAPLHYVRNHGAVPRADWDEWTVEVTGLVK-RPARLTMDELVRF 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099694 254 PRYEITVTLQCAGNRRSEMTQVKEVKGLEWRTGAISTARWAGARLCDVLAQAGHQLCETEA-HVCFEGLDSDPTG--TAY 330
Cdd:PLN02252 157 PARELPVTLVCAGNRRKEQNMVKQTIGFNWGAAGVSTSVWRGVRLRDVLRRCGVMSRKGGAlNVCFEGAEDLPGGggSKY 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099694 331 GASIPLARAMDPEAEVLLAYEMNGQPLPRDHGFPVRVVVPGVVGARHVKWLGRVSVQPEESYSHWQRRDYKGFSPSVDWE 410
Cdd:PLN02252 237 GTSITLERAMDPARDVILAYMQNGEPLTPDHGFPVRLIIPGFIGGRMVKWLKRIIVTTAESDNYYHYRDNRVLPSHVDAE 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099694 411 TVDFDS---APS--IQELPVQSAITEPRDGETVESGEVTI------KGYAWSGGGRAVIRVDVSLDGGLTWQVAKLDGEE 479
Cdd:PLN02252 317 LANAEGwwyKPEyiINELNINSVITTPAHDEILPINASTTqrpytmKGYAYSGGGRKVTRVEVSLDGGETWRLCDLDHPE 396
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74099694 480 QRPR--KAWAWRLWQLKAPVP--AGQKElnIVCKAVDDGYNVQPDTvaPIWNLRGVLSNAWHRVHVYV 543
Cdd:PLN02252 397 KPTKygKYWCWCFWSLDVEVLdlLGAKE--IAVRAWDESMNTQPEK--LIWNLMGMMNNCWFRVKVNV 460
|
|
| eukary_NR_Moco |
cd02112 |
molybdopterin binding domain of eukaryotic nitrate reductase (NR). Assimilatory NRs catalyze ... |
182-541 |
5.09e-97 |
|
molybdopterin binding domain of eukaryotic nitrate reductase (NR). Assimilatory NRs catalyze the reduction of nitrate to nitrite which is subsequently converted to NH4+ by nitrite reductase. Eukaryotic assimilatory nitrate reductases are cytosolic homodimeric enzymes with three prosthetic groups, flavin adenine dinucleotide (FAD), cytochrome b557, and Mo cofactor, which are located in three functional domains. Common features of all known members of the sulfite oxidase (SO) family of molybdopterin binding domains are that they contain one single pterin cofactor and part of the coordination of the metal (Mo) is a cysteine ligand of the protein and that they catalyze the transfer of an oxygen to or from a lone pair of electrons on the substrate.
Pssm-ID: 239030 [Multi-domain] Cd Length: 386 Bit Score: 299.68 E-value: 5.09e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099694 182 RHPAL-KVNSQRPFNAEPPP-ELLTENYITPNPIFFTRNHLPVPNLDPDTYRLHVVG---APggqsLSLSLDDLHN-FPR 255
Cdd:cd02112 11 RDPRLiRLTGKHPFNSEPPLtELMDHGFITPSNLHYVRNHGPVPREKWEDWTVEVTGlveKP----TTLTMDELVAmFPS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099694 256 YEITVTLQCAGNRRSEMTQVKEVKGLEWRTGAISTARWAGARLCDVLAQAGHQLCETEA-HVCFEGLDSDPTG--TAYGA 332
Cdd:cd02112 87 VTFPVTLVCAGNRRKEQNMVKKTIGFNWGAAGTSTSLWTGVRLSDLLDRCGPKSPKGGArHVCFEGADDLLPGpnGKYGT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099694 333 SIPLARAMDPEAEVLLAYEMNGQPLPRDHGFPVRVVVPGVVGARHVKWLGRVSVQPEESYSHWQRRDYKGFSPSVDWETV 412
Cdd:cd02112 167 SITLSWAMDPSKDVMLAYKQNGELLHPDHGFPVRLIIPGQIGGRMVKWLKRIVVSDRESQNHYHFHDNRVLPSHVDAELA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099694 413 D-----FDSAPSIQELPVQSAITEPRDGETVE------SGEVTIKGYAWSGGGRAVIRVDVSLDGGLTWQVAKLDGEEQR 481
Cdd:cd02112 247 NeegwwYKPEYIINDLNVNSAITTPAHDEVLPlnglttAETYTMKGYAYAGGGRRVTRVEVSLDDGKSWKLASIDYPEDP 326
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74099694 482 PR--KAWAWRLWQLKAPVPAGQKELNIVCKAVDDGYNVQPDTvaPIWNLRGVLSNAWHRVHV 541
Cdd:cd02112 327 TKygKCWCWCFWSLDVPLSELLAAKEICVRAWDESMNTQPRD--MTWNVMGMMNNCWFRVKI 386
|
|
| Oxidored_molyb |
pfam00174 |
Oxidoreductase molybdopterin binding domain; This domain is found in a variety of ... |
219-395 |
1.38e-64 |
|
Oxidoreductase molybdopterin binding domain; This domain is found in a variety of oxidoreductases. This domain binds to a molybdopterin cofactor. Xanthine dehydrogenases, that also bind molybdopterin, have essentially no similarity.
Pssm-ID: 459699 [Multi-domain] Cd Length: 168 Bit Score: 207.74 E-value: 1.38e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099694 219 HLPVPNLDPDTYRLHVVGApGGQSLSLSLDDLHNFPRYEITVTLQCAGNRRSEMTQVKevkGLEWRTGAISTARWAGARL 298
Cdd:pfam00174 1 HGPVPEIDPDTWRLRVDGL-VEKPLTLTLDDLKAFPQVTVTATLQCVGNRRKEMNRVK---GVQWGGGAIGNAEWTGVPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099694 299 CDVLAQAGhqLCETEAHVCFEGLDSDPTGtAYGASIPLARAMDPEaeVLLAYEMNGQPLPRDHGFPVRVVVPGVVGARHV 378
Cdd:pfam00174 77 RDLLERAG--VKPGAKHVLFEGADTLGDG-GYTTSLPLEKALDDD--VLLAYEMNGEPLPPDHGYPLRLVVPGWYGARSV 151
|
170
....*....|....*..
gi 74099694 379 KWLGRVSVQPEESYSHW 395
Cdd:pfam00174 152 KWLRRIEVTDEESPGFW 168
|
|
| Mo-co_dimer |
pfam03404 |
Mo-co oxidoreductase dimerization domain; This domain is found in molybdopterin cofactor ... |
418-544 |
2.26e-58 |
|
Mo-co oxidoreductase dimerization domain; This domain is found in molybdopterin cofactor (Mo-co) oxidoreductases. It is involved in dimer formation, and has an Ig-fold structure.
Pssm-ID: 427280 [Multi-domain] Cd Length: 136 Bit Score: 190.65 E-value: 2.26e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099694 418 PSIQELPVQSAITEPRDGETVES----GEVTIKGYAWSGGGRAVIRVDVSLDGGLTWQVAKLDGEEQRPR------KAWA 487
Cdd:pfam03404 2 YAIYDLNVNSAICSPEHDEVVKLgaaqGTYTIKGYAYSGGGRRITRVEVSLDGGKTWRLAEIDYEEDPYRygewreKCWC 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 74099694 488 WRLWQLKAPVPAGQKELNIVCKAVDDGYNVQPDTvaPIWNLRGVLSNAWHRVHVYVS 544
Cdd:pfam03404 82 WCFWSLDIPVSDLLKAKEILVRAVDEAMNVQPED--MYWNVRGMMNNPWHRVKIHVE 136
|
|
| SO_family_Moco |
cd00321 |
Sulfite oxidase (SO) family, molybdopterin binding domain. This molybdopterin cofactor (Moco) ... |
215-389 |
7.13e-49 |
|
Sulfite oxidase (SO) family, molybdopterin binding domain. This molybdopterin cofactor (Moco) binding domain is found in a variety of oxidoreductases, main members of this family are nitrate reductase (NR) and sulfite oxidase (SO). SO catalyzes the terminal reaction in the oxidative degradation of the sulfur-containing amino acids cysteine and methionine. Assimilatory NRs catalyze the reduction of nitrate to nitrite which is subsequently converted to NH4+ by nitrite reductase. Common features of all known members of this family are that they contain one single pterin cofactor and part of the coordination of the metal (Mo) is a cysteine ligand of the protein and that they catalyze the transfer of an oxygen to or from a lone pair of electrons on the substrate.
Pssm-ID: 238198 [Multi-domain] Cd Length: 156 Bit Score: 166.21 E-value: 7.13e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099694 215 FTRNHLPVP-NLDPDTYRLHVVGApGGQSLSLSLDDLHNFPRYEITVTLQCAGNRrsemtqvkevkgleWRTGAISTARW 293
Cdd:cd00321 1 FVRNHGGVPpEIDPDDWRLEVDGL-VEKPLSLTLDDLKALPQVEVIATLHCVGNR--------------WGGGAVSNAEW 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099694 294 AGARLCDVLAQAGHQlcETEAHVCFEGLDsDPTGTAYGASIPLARAMDPEaeVLLAYEMNGQPLPRDHGFPVRVVVPGVV 373
Cdd:cd00321 66 TGVPLRDLLEEAGPK--PGARYVVFEGAD-DPGGDGYTTSLPLEKALDPD--VLLAYEMNGEPLPPDHGFPLRLVVPGLY 140
|
170
....*....|....*.
gi 74099694 374 GARHVKWLGRVSVQPE 389
Cdd:cd00321 141 GWKSVKWLRRIEVTDE 156
|
|
| bact_SorA_Moco |
cd02114 |
sulfite:cytochrome c oxidoreductase subunit A (SorA), molybdopterin binding domain. SorA is ... |
180-541 |
2.07e-48 |
|
sulfite:cytochrome c oxidoreductase subunit A (SorA), molybdopterin binding domain. SorA is involved in oxidation of sulfur compounds during chemolithothrophic growth. Together with SorB, a small c-type heme containing subunit, it forms a hetrodimer. It is a member of the sulfite oxidase (SO) family of molybdopterin binding domains. This molybdopterin cofactor (Moco) binding domain is found in a variety of oxidoreductases, main members of this family are nitrate reductase (NR) and sulfite oxidase (SO). Common features of all known members of this family are that they contain one single pterin cofactor and part of the coordination of the metal (Mo) is a cysteine ligand of the protein and that they catalyze the transfer of an oxygen to or from a lone pair of electrons on the substrate.
Pssm-ID: 239032 [Multi-domain] Cd Length: 367 Bit Score: 171.93 E-value: 2.07e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099694 180 PVRHPALKVNSqRPFNAEPPPELLTENYITPNPIFFTRNHLP-VP-NLDPDTYRLHVVGAPGgQSLSLSLDDLHNF-PRY 256
Cdd:cd02114 14 PQKRPLIRLTT-RPPHLETPFSVFNEGLITPNDAFFVRYHLAgIPlDIDPDAYTLTIDGKVR-TPLTLSLAELKRIePRF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099694 257 EITVTLQCAGNRRSEMTqvKEVKGLEWRTGAISTARWAGARLCDVLAQAGHQLCETEahVCFEGLDSDP--TGTAYGASI 334
Cdd:cd02114 92 EVVAVNQCSGNSRGFFQ--PRVQGAQLANGAMGNARWAGVPLKAVLAKAGVQDGARQ--VAFRGLDQPVldVTPDFVKSL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099694 335 PLARAMDPEaeVLLAYEMNGQPLPRDHGFPVRVVVPGVVGARHVKWLGRVSVQPEESYSHWQRRDYKgfSPSVDWETVDF 414
Cdd:cd02114 168 DIDHALDGE--VMLAWEMNGEPLPVLNGYPLRLVVPGFYATYWVKHLSHITVLDKEFDGFWASQAYR--IPDNADAGVEP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099694 415 DSAPS----IQELPVQSAITEPRDGETVES-GEVTIKGYAWSgGGRAVIRVDVSLDGGLTWQVAKLDGEEQRprkaWAWR 489
Cdd:cd02114 244 GTAPDrtapINRFKVRSFITSLENGAIVAPaGELALRGIAFD-GGSGIRRVDVSADGGDSWTQATLGPDLGR----FSFR 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 74099694 490 LWQLKAPVPAgQKELNIVCKAVDDGYNVQPDTVApiWNLRGVLSNAWHRVHV 541
Cdd:cd02114 319 GWKLTLDGVK-KGPLTLMVRATNNDGQTQPLRAP--WNPGGYMRNVVERTRI 367
|
|
| bact_SoxC_Moco |
cd02113 |
bacterial SoxC is a member of the sulfite oxidase (SO) family of molybdopterin binding domains. ... |
208-533 |
8.97e-39 |
|
bacterial SoxC is a member of the sulfite oxidase (SO) family of molybdopterin binding domains. SoxC is involved in oxidation of sulfur compounds during chemolithothrophic growth. Together with SoxD, a small c-type heme containing subunit, it forms a hetrotetrameric sulfite dehydrogenase. This molybdopterin cofactor (Moco) binding domain is found in a variety of oxidoreductases, main members of this family are nitrate reductase (NR) and sulfite oxidase (SO). Common features of all known members of this family are that they contain one single pterin cofactor and part of the coordination of the metal (Mo) is a cysteine ligand of the protein and that they catalyze the transfer of an oxygen to or from a lone pair of electrons on the substrate.
Pssm-ID: 239031 [Multi-domain] Cd Length: 326 Bit Score: 144.46 E-value: 8.97e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099694 208 ITPNPIFFTRNHLPVPNLDPDTYRLHVVGAPGgQSLSLSLDDLHNFPRYEITVTLQCAGNRRSEMTQVKeVKGLEWRTGA 287
Cdd:cd02113 9 ITPNGLHFERHHGGVPDIDPAQHRLMIHGMVK-KPLVFTMDDLKRFPSVSRIYFLECSGNGGTGWRGAP-LPTAQYTHGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099694 288 ISTARWAGARLCDVLAQAGhqLCETEAHVCFEGLDsdptGTAYGASIPLARAMDpeaEVLLAYEMNGQPLPRDHGFPVRV 367
Cdd:cd02113 87 LSCSEWTGVPLSTLLEEAG--VKPGAKWLLAEGAD----AAAMTRSIPLEKALD---DALVAYAQNGEALRPENGYPLRL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099694 368 VVPGVVGARHVKWLGRVSV--QPeesyshWQRRD----YKGFSPSVDWETVDFDSAPsiqelpvQSAITEPRDGETV-ES 440
Cdd:cd02113 158 VVPGWEGNTNVKWLRRIEVgdQP------WMTREetskYTDLLPDGRARQFSFVMEA-------KSVITSPSGGQRLrEP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099694 441 GEVTIKGYAWSGGGRaVIRVDVSLDGGLTWQVAKLDGEEQ-----RPRKAWAWrlwqlkapvpaGQKELNIVCKAVDDGY 515
Cdd:cd02113 225 GFHEISGLAWSGRGR-IRRVDVSFDGGRTWQDARLEGPVLpkaltRFRLPWKW-----------DGRPAVLQSRATDETG 292
|
330
....*....|....*...
gi 74099694 516 NVQPdTVAPIWNLRGVLS 533
Cdd:cd02113 293 YVQP-TRAELRAVRGTNS 309
|
|
| MsrP |
COG2041 |
Molybdopterin-dependent catalytic subunit of periplasmic DMSO/TMAO and ... |
214-405 |
2.44e-35 |
|
Molybdopterin-dependent catalytic subunit of periplasmic DMSO/TMAO and protein-methionine-sulfoxide reductases [Energy production and conversion];
Pssm-ID: 441644 [Multi-domain] Cd Length: 183 Bit Score: 130.66 E-value: 2.44e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099694 214 FFTRNHLPVPNLDPDTYRLHVVGApGGQSLSLSLDDLHNFPRYEITVTLQCAGNrrsemtqvkevkgleWRTGaisTARW 293
Cdd:COG2041 19 FPVRTAGGVPEIDPADWRLRVDGL-VEKPLTLTLDDLLALPLEERIYRLHCVEN---------------WSGG---VAPW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099694 294 AGARLCDVLAQAGHQlceTEA-HVCFEGLDSDptgtaYGASIPLARAMDPEAevLLAYEMNGQPLPRDHGFPVRvvvpgv 372
Cdd:COG2041 80 TGVPLRDLLERAGPK---PGAkYVLFESADPG-----YTESLPLDEALDPDT--LLAYGMNGEPLPPEHGAPLR------ 143
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 74099694 373 vgAR--------HVKWLGRVSVQPEESYSHWQRRDYKGFSP 405
Cdd:COG2041 144 --LVvpglygfkSAKWLVRIEVTDEDPPGYWETRGYHFYAN 182
|
|
| Cyt-b5 |
pfam00173 |
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from ... |
86-160 |
1.95e-18 |
|
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from a diverse range of proteins. This family also includes proteins that bind to steroids. The family includes progesterone receptors. Many members of this subfamily are membrane anchored by an N-terminal transmembrane alpha helix. This family also includes a domain in some chitin synthases. There is no known ligand for this domain in the chitin synthases.
Pssm-ID: 459698 [Multi-domain] Cd Length: 74 Bit Score: 79.59 E-value: 1.95e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74099694 86 TKEEVSSHTSPEtGIWVTLGSEVFDVTEFVDLHPGGPSKLMLAAGGPL-EPFWALyaVHNQSHVRELLAQYKIGEL 160
Cdd:pfam00173 1 TLEELSKHNGDG-DCWVAINGKVYDVTKFLKEHPGGEDVILSAAGKDAtDAFEAI--GHSEDAAEKLLKKYRIGEL 73
|
|
| arch_bact_SO_family_Moco |
cd02109 |
bacterial and archael members of the sulfite oxidase (SO) family of molybdopterin binding ... |
198-400 |
6.00e-17 |
|
bacterial and archael members of the sulfite oxidase (SO) family of molybdopterin binding domains. This molybdopterin cofactor (Moco) binding domain is found in a variety of oxidoreductases, main members of this family are nitrate reductase (NR) and sulfite oxidase (SO). Common features of all known members of this family are that they contain one single pterin cofactor and part of the coordination of the metal (Mo) is a cysteine ligand of the protein and that they catalyze the transfer of an oxygen to or from a lone pair of electrons on the substrate. The specific function of this subgroup is unknown.
Pssm-ID: 239027 [Multi-domain] Cd Length: 180 Bit Score: 78.83 E-value: 6.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099694 198 PPPELLTENYitpnPIFFTrnhLPVPNLDPDTYRLHVVGAPGGQsLSLSLDDLHNFPRYEITVTLQCagnrrsemtqvke 277
Cdd:cd02109 2 PPGQYLTEKF----PVLDA---GDVPEVDLEKWRLRVTGLVENP-LSLTYEDLLALPQTEYTADFHC------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099694 278 VKGleWrtgAISTARWAGARLCDVLAQAGhqLCETEAHVCFEGLDsdptgtAYGASIPLARAMDPEAevLLAYEMNGQPL 357
Cdd:cd02109 61 VTG--W---SKLDVVWEGVSLKDLLEAAR--PDPEATFVMAHSYD------GYTTNLPLEDLLREDS--LLATKMDGEPL 125
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 74099694 358 PRDHGFPVRVVVPGVVGARHVKWLGRVSVQPEESYSHWQRRDY 400
Cdd:cd02109 126 PPEHGGPARLVVPHLYFWKSAKWLRGIEFLDEDEPGFWERRGY 168
|
|
| bact_SO_family_Moco |
cd02108 |
bacterial subgroup of the sulfite oxidase (SO) family of molybdopterin binding domains. This ... |
215-363 |
2.77e-14 |
|
bacterial subgroup of the sulfite oxidase (SO) family of molybdopterin binding domains. This domain is found in a variety of oxidoreductases. Common features of all known members of this family, like sulfite oxidase and nitrite reductase, are that they contain one single pterin cofactor and part of the coordination of the metal (Mo) is a cysteine ligand of the protein and that they catalyze the transfer of an oxygen to or from a lone pair of electrons on the substrate. The specific function of this subgroup is unknown.
Pssm-ID: 239026 [Multi-domain] Cd Length: 185 Bit Score: 71.26 E-value: 2.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099694 215 FTRNHLPVPNL---------DPDTYRLHVvgapGG---QSLSLSLDDLHNFPRyeitvtlqcagnrRSEMTQVKEVKGle 282
Cdd:cd02108 5 FRRNGIRKPEAlaykaleanDFADYRLEV----GGlveHPLSLSLEELRALPQ-------------RTQITRHICVEG-- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099694 283 WrtGAIstARWAGARLCDVLAQAGhqlCETEA-HVCFEGLDSDPTGTAYGASIPLARAMDPEAevLLAYEMNGQPLPRDH 361
Cdd:cd02108 66 W--SAI--GKWGGVPLRTILELVG---PLPEAkYVVFKCADDFAGGDRYYESIDMASALHPQT--LLAYEMNGQPLPIKN 136
|
..
gi 74099694 362 GF 363
Cdd:cd02108 137 GA 138
|
|
| PLN02252 |
PLN02252 |
nitrate reductase [NADPH] |
77-246 |
1.20e-11 |
|
nitrate reductase [NADPH]
Pssm-ID: 215141 [Multi-domain] Cd Length: 888 Bit Score: 67.39 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099694 77 AAQESTHIYTKEEVSSHTSPETgIWVTLGSEVFDVTEFVDLHPGGPSKLMLAAGGP-LEPFwalYAVHNqSHVRELLAQY 155
Cdd:PLN02252 512 NTNTGSKQYTMSEVRKHNSEDS-CWIVVHGHVYDCTRFLKDHPGGADSILINAGTDcTEEF---DAIHS-DKAKKMLEDY 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099694 156 KIGELnpedkvaptVETSDPYADDPVRHPALKVNSQRPFNAEPPPellTENYITPNPifftRNHLPVP-----NLDPDTY 230
Cdd:PLN02252 587 RIGEL---------VTTGAAASSSASSHPLSAISTASALAAASPA---PGRPVALNP----REKIPCRlvekiSLSHDVR 650
|
170 180
....*....|....*....|....
gi 74099694 231 RL--------HVVGAPGGQSLSLS 246
Cdd:PLN02252 651 LFrfalpsedHVLGLPVGKHVFLC 674
|
|
| PLN03199 |
PLN03199 |
delta6-acyl-lipid desaturase-like protein; Provisional |
80-175 |
3.48e-06 |
|
delta6-acyl-lipid desaturase-like protein; Provisional
Pssm-ID: 178740 [Multi-domain] Cd Length: 485 Bit Score: 49.65 E-value: 3.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099694 80 ESTHIYTKEEVSSHTSPETGiWVTLGSEVFDVTEFVDlHPGGPSKLMLAAGGPLEPFWALYAVHNQShvreLLAQYKIGE 159
Cdd:PLN03199 21 EKPQKISWQEVKKHASPDDA-WIIHQNKVYDVSNWHD-HPGGAVIFTHAGDDMTDIFAAFHAPGSQA----LMKKFYIGD 94
|
90
....*....|....*.
gi 74099694 160 LNPEdkvapTVETSDP 175
Cdd:PLN03199 95 LIPE-----STEHKDP 105
|
|
| COG3915 |
COG3915 |
Uncharacterized conserved protein [Function unknown]; |
220-362 |
2.54e-05 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443120 Cd Length: 167 Bit Score: 44.88 E-value: 2.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099694 220 LPVPNLDPDtyrLHVVGAPG----GQSLSLSLDDLHNFPRYEITVTLqcagnrrsemtqvkevkglEWRTGAIstaRWAG 295
Cdd:COG3915 24 LPAPAGPVI---LTVSGKIGntnaGGAATFDLAMLEALPQTEITTTT-------------------PWTDGVQ---TFRG 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74099694 296 ARLCDVLAQAGhqlcETEAHVCFEGLDsdptgtAYGASIPLARAMdpEAEVLLAYEMNGQPLP-RDHG 362
Cdd:COG3915 79 VLLRDLLAAVG----AKGTTLRAVALN------DYAVEIPISDLE--EYGVILAYRMDGKPMSvRDKG 134
|
|
| PLN03198 |
PLN03198 |
delta6-acyl-lipid desaturase; Provisional |
49-178 |
3.16e-05 |
|
delta6-acyl-lipid desaturase; Provisional
Pssm-ID: 178739 [Multi-domain] Cd Length: 526 Bit Score: 46.61 E-value: 3.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099694 49 NSSTQGwrvmgTLLGLGAVLAYQDHRCRAAQESTHIYTKEEVSSHTSPeTGIWVTLGSEVFDVTEFVDLHPGGPSKLMLA 128
Cdd:PLN03198 75 NSNSQE-----AAEALAESVVKPTRRRSSKEKKSKSHLLSEVAAHNKP-NDCWIVIKNKVYDVSDFAAEHPGGSVISTYF 148
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 74099694 129 AGGPLEPFWALYAvhnqSHVRELLAQYKIGELnpeDKVAPTVETSDPYAD 178
Cdd:PLN03198 149 GRDGTDAFSSFHA----ASTWKILQDFYIGDV---DNVEPTPELLKDFRD 191
|
|
| Big_7 |
pfam17957 |
Bacterial Ig domain; This entry represents a bacterial ig-like domain that is found in ... |
428-469 |
9.89e-03 |
|
Bacterial Ig domain; This entry represents a bacterial ig-like domain that is found in glycosyl hydrolase enzymes.
Pssm-ID: 436171 [Multi-domain] Cd Length: 67 Bit Score: 34.89 E-value: 9.89e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 74099694 428 AITEPRDGETVESGEVTIKGYAwSGGGrAVIRVDVSLDGGLT 469
Cdd:pfam17957 2 SITSPANGATVSGGTVTISATA-SDDG-GVSKVEFYVDGTLV 41
|
|
| |
