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Conserved domains on  [gi|574279253|ref|NP_001276023|]
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histidine--tRNA ligase, cytoplasmic isoform 7 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02972 super family cl33611
Histidyl-tRNA synthetase
 28-472 0e+00

Histidyl-tRNA synthetase


The actual alignment was detected with superfamily member PLN02972:

Pssm-ID: 215525 [Multi-domain]  Cd Length: 763  Bit Score: 586.08  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253  28 KTPKGTRDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGEDSKLIYDLKDQGGELLSLRYDLTVPFA 107
Cdd:PLN02972 328 KIPKGTRDFAKEQMAIREKAFSIITSVFKRHGATALDTPVFELRETLMGKYGEDSKLIYDLADQGGELCSLRYDLTVPFA 407

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253 108 RYLAMNKLTNIKRYHIAKVYRRDNPamTRGRYREFYQCDFDIAGNFDPMIPDAECLKIMCEILSSLQIGDFLVKVNDRRI 187
Cdd:PLN02972 408 RYVAMNGITSFKRYQIAKVYRRDNP--SKGRYREFYQCDFDIAGVYEPMGPDFEIIKVLTELLDELDIGTYEVKLNHRKL 485

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253 188 LDGMFAICGVSDSKFRTICSSVDKLDKVSWEEVKNEMVGEKGLAPEVADRIGDYVQQHGG-VSLVEQLLQ-DPKLSQNKQ 265
Cdd:PLN02972 486 LDGMLEICGVPPEKFRTICSSIDKLDKQSFEQVKKEMVEEKGLSNETADKIGNFVKERGPpLELLSKLRQeGSEFLGNAS 565

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253 266 ALEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLLQTPaqageeplgVGSVAAGGRYDGLVGMFDpkG 345
Cdd:PLN02972 566 SRAALDELEIMFKALEKSKAIGKIVFDLSLARGLDYYTGVIYEAVFKGAQ---------VGSIAAGGRYDNLVGMFS--G 634

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253 346 RKVPCVGLSIGVERIFSIVEQRLEALEEKIRTTETQVLVASAQKKLLEERLKLVSELWDAGIKAEllYKKNPKLLNQLQY 425
Cdd:PLN02972 635 KQVPAVGVSLGIERVFAIMEQQEEEKSQVIRPTETEVLVSIIGDDKLALAAELVSELWNAGIKAE--YKVSTRKAKHLKR 712

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 574279253 426 CEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVDVRREDLVEEIKRR 472
Cdd:PLN02972 713 AKESGIPWMVLVGEKELSKGFVKLKNLEAGVEEEVDRTCFVQELKAE 759
S15_NS1_EPRS_RNA-bind super family cl00349
S15/NS1/EPRS_RNA-binding domain. This short domain consists of a helix-turn-helix structure, ...
 2-20 1.32e-04

S15/NS1/EPRS_RNA-binding domain. This short domain consists of a helix-turn-helix structure, which can bind to several types of RNA. It is found in the ribosomal protein S15, the influenza A viral nonstructural protein (NSA) and in several eukaryotic aminoacyl tRNA synthetases (aaRSs), where it occurs as a single or a repeated unit. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions in the formation of tRNA-synthetases into multienzyme complexes. While this domain lacks significant sequence similarity between the subgroups in which it is found, they share similar electrostatic surface potentials and thus are likely to bind to RNA via the same mechanism.


The actual alignment was detected with superfamily member cd00938:

Pssm-ID: 469733 [Multi-domain]  Cd Length: 45  Bit Score: 39.38  E-value: 1.32e-04
                         10
                 ....*....|....*....
gi 574279253   2 IEEEVAKLLKLKAQLGPDE 20
Cdd:cd00938   27 IAEEVAKLLELKAQLGGDE 45
 
Name Accession Description Interval E-value
PLN02972 PLN02972
Histidyl-tRNA synthetase
 28-472 0e+00

Histidyl-tRNA synthetase


Pssm-ID: 215525 [Multi-domain]  Cd Length: 763  Bit Score: 586.08  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253  28 KTPKGTRDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGEDSKLIYDLKDQGGELLSLRYDLTVPFA 107
Cdd:PLN02972 328 KIPKGTRDFAKEQMAIREKAFSIITSVFKRHGATALDTPVFELRETLMGKYGEDSKLIYDLADQGGELCSLRYDLTVPFA 407

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253 108 RYLAMNKLTNIKRYHIAKVYRRDNPamTRGRYREFYQCDFDIAGNFDPMIPDAECLKIMCEILSSLQIGDFLVKVNDRRI 187
Cdd:PLN02972 408 RYVAMNGITSFKRYQIAKVYRRDNP--SKGRYREFYQCDFDIAGVYEPMGPDFEIIKVLTELLDELDIGTYEVKLNHRKL 485

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253 188 LDGMFAICGVSDSKFRTICSSVDKLDKVSWEEVKNEMVGEKGLAPEVADRIGDYVQQHGG-VSLVEQLLQ-DPKLSQNKQ 265
Cdd:PLN02972 486 LDGMLEICGVPPEKFRTICSSIDKLDKQSFEQVKKEMVEEKGLSNETADKIGNFVKERGPpLELLSKLRQeGSEFLGNAS 565

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253 266 ALEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLLQTPaqageeplgVGSVAAGGRYDGLVGMFDpkG 345
Cdd:PLN02972 566 SRAALDELEIMFKALEKSKAIGKIVFDLSLARGLDYYTGVIYEAVFKGAQ---------VGSIAAGGRYDNLVGMFS--G 634

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253 346 RKVPCVGLSIGVERIFSIVEQRLEALEEKIRTTETQVLVASAQKKLLEERLKLVSELWDAGIKAEllYKKNPKLLNQLQY 425
Cdd:PLN02972 635 KQVPAVGVSLGIERVFAIMEQQEEEKSQVIRPTETEVLVSIIGDDKLALAAELVSELWNAGIKAE--YKVSTRKAKHLKR 712

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 574279253 426 CEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVDVRREDLVEEIKRR 472
Cdd:PLN02972 713 AKESGIPWMVLVGEKELSKGFVKLKNLEAGVEEEVDRTCFVQELKAE 759
HisS COG0124
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ...
 27-472 5.79e-119

Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


Pssm-ID: 439894 [Multi-domain]  Cd Length: 422  Bit Score: 355.20  E-value: 5.79e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253  27 LKTPKGTRDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGED--SKLIYDLKDQGGELLSLRYDLTV 104
Cdd:COG0124    4 IQAPRGTRDILPEESAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKIGEDivEKEMYTFEDRGGRSLTLRPEGTA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253 105 PFARYLAMNKLTN---IKRYHIAKVYRRDNPAmtRGRYREFYQCDFDIAGNFDPMIpDAECLKIMCEILSSLQIGDFLVK 181
Cdd:COG0124   84 PVARAVAEHGNELpfpFKLYYIGPVFRYERPQ--KGRYRQFHQFGVEVIGSDSPLA-DAEVIALAADLLKALGLKDFTLE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253 182 VNDRrildgmfaicGVSDSKFRTICSSVDKLDKVSWEEVknemvgekgLAPEVADRI------------GDYVQqhggvS 249
Cdd:COG0124  161 INSR----------GLPEERAEALLRYLDKLDKIGHEDV---------LDEDSQRRLetnplraildskGPDCQ-----E 216

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253 250 LVEQLlqdPKLSQNKqALEGLGDLKLLFEYLTLFGIDdkISFDLSLARGLDYYTGVIYEAVLLQTPAQageeplgvGSVA 329
Cdd:COG0124  217 VLADA---PKLLDYL-GEEGLAHFEEVLELLDALGIP--YVIDPRLVRGLDYYTGTVFEIVTDGLGAQ--------GSVC 282

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253 330 AGGRYDGLVGMFDpkGRKVPCVGLSIGVERIFSIVEQRLEALEEKirtTETQVLVASAQKKLLEERLKLVSELWDAGIKA 409
Cdd:COG0124  283 GGGRYDGLVEQLG--GPPTPAVGFAIGLERLLLLLEELGLLPAAE---PPPDVYVVPLGEEARAEALKLAQELRAAGIRV 357

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 574279253 410 EL-LYKKNPKllNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVDVRREDLVEEIKRR 472
Cdd:COG0124  358 ELdLGGRKLK--KQLKYADKSGAPFVLILGEDELANGTVTLKDLATGEQETVPLDELVEYLKEL 419
HisRS-like_core cd00773
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ...
 40-365 1.05e-104

Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. It is responsible for the attachment of histidine to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs. This domain is also found at the C-terminus of eukaryotic GCN2 protein kinase and at the N-terminus of the ATP phosphoribosyltransferase accessory subunit, HisZ. HisZ along with HisG catalyze the first reaction in histidine biosynthesis. HisZ is found only in a subset of bacteria and differs from HisRS in lacking a C-terminal anti-codon binding domain.


Pssm-ID: 238396 [Multi-domain]  Cd Length: 261  Bit Score: 312.61  E-value: 1.05e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253  40 QMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGED-SKLIYDLKDQGGELLSLRYDLTVPFARYLAMNKL--- 115
Cdd:cd00773    1 EAALRRYIEDTLREVFERYGYEEIDTPVFEYTELFLRKSGDEvSKEMYRFKDKGGRDLALRPDLTAPVARAVAENLLslp 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253 116 TNIKRYHIAKVYRRDNPAmtRGRYREFYQCDFDIAGnFDPMIPDAECLKIMCEILSSLQIGDFLVKVNDRRILDGmfaIC 195
Cdd:cd00773   81 LPLKLYYIGPVFRYERPQ--KGRYREFYQVGVEIIG-SDSPLADAEVIALAVEILEALGLKDFQIKINHRGILDG---IA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253 196 GVSDSKFRTICSSVDKLDKvsweevknemvgekglapevadrigdyvqqhggvslveqllqdpklsqnkqalEGLGDLKL 275
Cdd:cd00773  155 GLLEDREEYIERLIDKLDK-----------------------------------------------------EALAHLEK 181

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253 276 LFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLLQTPAQageeplgvGSVAAGGRYDGLVGMFDpkGRKVPCVGLSI 355
Cdd:cd00773  182 LLDYLEALGVDIKYSIDLSLVRGLDYYTGIVFEAVADGLGAQ--------GSIAGGGRYDGLLEEFG--GEDVPAVGFAI 251

                        330
                 ....*....|
gi 574279253 356 GVERIFSIVE 365
Cdd:cd00773  252 GLERLLLALE 261
hisS TIGR00442
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ...
 28-460 6.33e-104

histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed genome. Apparent second copies from Bacillus subtilis, Synechocystis sp., and Aquifex aeolicus are slightly shorter, more closely related to each other than to other hisS proteins, and actually serve as regulatory subunits for an enzyme of histidine biosynthesis. They were excluded from the seed alignment and score much lower than do single copy histidyl-tRNA synthetases of other genomes not included in the seed alignment. These putative second copies of HisS score below the trusted cutoff. The regulatory protein kinase GCN2 of Saccharomyces cerevisiae (YDR283c), and related proteins from other species designated eIF-2 alpha kinase, have a domain closely related to histidyl-tRNA synthetase that may serve to detect and respond to uncharged tRNA(his), an indicator of amino acid starvation; these regulatory proteins are not orthologous and so score below the noise cutoff. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 273080 [Multi-domain]  Cd Length: 404  Bit Score: 315.96  E-value: 6.33e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253   28 KTPKGTRDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGEDS----KLIYDLKDQGGELLSLRYDLT 103
Cdd:TIGR00442   1 QKPRGTRDFLPEEMIKWQYIEETIREVFERYGFKEIRTPIFEYTELFKRKVGEETdivsKEMYTFKDKGGRSLTLRPEGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253  104 VPFARYLAMNKLTN---IKRYHIAKVYRRDNPAmtRGRYREFYQCDFDIAGNFDPMIpDAECLKIMCEILSSLQIGDFLV 180
Cdd:TIGR00442  81 APVARAVIENKLLLpkpFKLYYIGPMFRYERPQ--KGRYRQFHQFGVEVIGSDSPLA-DAEIIALAADILKELGLKDFTL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253  181 KVNDRRILDGMFAicgvsdsKFRTICSSVDK-LDKVSWEEVKNEMVGEKGLAPEVADRIGDYVQQhggvslveqllqDPK 259
Cdd:TIGR00442 158 EINSLGILEGRLE-------YREALIRYLDKhKDKLGEDSVRRLEKNPLRILDSKNEKIQELLKN------------APK 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253  260 LSQNKQAlEGLGDLKLLFEYLTLFGIddKISFDLSLARGLDYYTGVIYEAVLLQTPAQageeplgvGSVAAGGRYDGLVG 339
Cdd:TIGR00442 219 ILDFLCE-ESRAHFEELKELLDALGI--PYKIDPSLVRGLDYYTGTVFEFVTDDLGAQ--------GSICGGGRYDGLVE 287

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253  340 MFDpkGRKVPCVGLSIGVERIFSIVEQRLEALEEKirtTETQVLVASAQKKLLEERLKLVSELWDAGIKAElLYKKNPKL 419
Cdd:TIGR00442 288 ELG--GPPTPAVGFAIGIERLILLLEELGLIPPPS---KKPDVYVVPLGEEAELEALKLAQKLRKAGIRVE-VDLGGRKL 361

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 574279253  420 LNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVDV 460
Cdd:TIGR00442 362 KKQLKYADKLGARFALIIGEDELENGTVTLKDLETGEQETV 402
tRNA-synt_His pfam13393
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ...
 32-360 1.33e-44

Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP phosphoribosyltransferase regulatory subunits.


Pssm-ID: 433170 [Multi-domain]  Cd Length: 309  Bit Score: 158.52  E-value: 1.33e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253   32 GTRDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGEDSKLIYDLKDQGGELLSLRYDLTVPFARYLA 111
Cdd:pfam13393   1 GIRDLLPPEARRIEELRRRLLDLFRSWGYELVMPPLLEYLDSLLTGTGADLDQTFKLVDQSGRLLGLRADITPQVARIDA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253  112 mnKLTNIKR----YHIAKVYRRDNPAMtrGRYREFYQCDFDIAGNFDPMiPDAECLKIMCEILSSLQIGDFLVKVNDRRI 187
Cdd:pfam13393  81 --HRLNRPGplrlCYAGSVLRTRPKGL--GRSREPLQVGAELIGHAGIE-ADAEIISLLLEALAAAGVPGVTLDLGHVGL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253  188 LDGMFAICGVSDSKFRTICSSVDKLDkvsWEEVKnEMVGEKGLAPEVADRIGDYVQQHGGVSLVEQLLQDpkLSQNKQAL 267
Cdd:pfam13393 156 VRALLEAAGLSEALEEALRAALQRKD---AAELA-ELAAEAGLPPALRRALLALPDLYGGPEVLDEARAA--LPGLPALQ 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253  268 EGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLlqtpAQAGEEplgvgsVAAGGRYDGLVGMFdpkGRK 347
Cdd:pfam13393 230 EALDELEALAALLEALGDGVRLTFDLAELRGYEYYTGIVFAAYA----PGVGEP------LARGGRYDDLGAAF---GRA 296

                         330
                  ....*....|...
gi 574279253  348 VPCVGLSIGVERI 360
Cdd:pfam13393 297 RPATGFSLDLEAL 309
HisRS_RNA cd00938
HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS ...
 2-20 1.32e-04

HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). This domain consists of a helix- turn- helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.


Pssm-ID: 238474 [Multi-domain]  Cd Length: 45  Bit Score: 39.38  E-value: 1.32e-04
                         10
                 ....*....|....*....
gi 574279253   2 IEEEVAKLLKLKAQLGPDE 20
Cdd:cd00938   27 IAEEVAKLLELKAQLGGDE 45
 
Name Accession Description Interval E-value
PLN02972 PLN02972
Histidyl-tRNA synthetase
 28-472 0e+00

Histidyl-tRNA synthetase


Pssm-ID: 215525 [Multi-domain]  Cd Length: 763  Bit Score: 586.08  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253  28 KTPKGTRDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGEDSKLIYDLKDQGGELLSLRYDLTVPFA 107
Cdd:PLN02972 328 KIPKGTRDFAKEQMAIREKAFSIITSVFKRHGATALDTPVFELRETLMGKYGEDSKLIYDLADQGGELCSLRYDLTVPFA 407

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253 108 RYLAMNKLTNIKRYHIAKVYRRDNPamTRGRYREFYQCDFDIAGNFDPMIPDAECLKIMCEILSSLQIGDFLVKVNDRRI 187
Cdd:PLN02972 408 RYVAMNGITSFKRYQIAKVYRRDNP--SKGRYREFYQCDFDIAGVYEPMGPDFEIIKVLTELLDELDIGTYEVKLNHRKL 485

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253 188 LDGMFAICGVSDSKFRTICSSVDKLDKVSWEEVKNEMVGEKGLAPEVADRIGDYVQQHGG-VSLVEQLLQ-DPKLSQNKQ 265
Cdd:PLN02972 486 LDGMLEICGVPPEKFRTICSSIDKLDKQSFEQVKKEMVEEKGLSNETADKIGNFVKERGPpLELLSKLRQeGSEFLGNAS 565

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253 266 ALEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLLQTPaqageeplgVGSVAAGGRYDGLVGMFDpkG 345
Cdd:PLN02972 566 SRAALDELEIMFKALEKSKAIGKIVFDLSLARGLDYYTGVIYEAVFKGAQ---------VGSIAAGGRYDNLVGMFS--G 634

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253 346 RKVPCVGLSIGVERIFSIVEQRLEALEEKIRTTETQVLVASAQKKLLEERLKLVSELWDAGIKAEllYKKNPKLLNQLQY 425
Cdd:PLN02972 635 KQVPAVGVSLGIERVFAIMEQQEEEKSQVIRPTETEVLVSIIGDDKLALAAELVSELWNAGIKAE--YKVSTRKAKHLKR 712

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 574279253 426 CEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVDVRREDLVEEIKRR 472
Cdd:PLN02972 713 AKESGIPWMVLVGEKELSKGFVKLKNLEAGVEEEVDRTCFVQELKAE 759
HisS COG0124
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ...
 27-472 5.79e-119

Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


Pssm-ID: 439894 [Multi-domain]  Cd Length: 422  Bit Score: 355.20  E-value: 5.79e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253  27 LKTPKGTRDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGED--SKLIYDLKDQGGELLSLRYDLTV 104
Cdd:COG0124    4 IQAPRGTRDILPEESAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKIGEDivEKEMYTFEDRGGRSLTLRPEGTA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253 105 PFARYLAMNKLTN---IKRYHIAKVYRRDNPAmtRGRYREFYQCDFDIAGNFDPMIpDAECLKIMCEILSSLQIGDFLVK 181
Cdd:COG0124   84 PVARAVAEHGNELpfpFKLYYIGPVFRYERPQ--KGRYRQFHQFGVEVIGSDSPLA-DAEVIALAADLLKALGLKDFTLE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253 182 VNDRrildgmfaicGVSDSKFRTICSSVDKLDKVSWEEVknemvgekgLAPEVADRI------------GDYVQqhggvS 249
Cdd:COG0124  161 INSR----------GLPEERAEALLRYLDKLDKIGHEDV---------LDEDSQRRLetnplraildskGPDCQ-----E 216

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253 250 LVEQLlqdPKLSQNKqALEGLGDLKLLFEYLTLFGIDdkISFDLSLARGLDYYTGVIYEAVLLQTPAQageeplgvGSVA 329
Cdd:COG0124  217 VLADA---PKLLDYL-GEEGLAHFEEVLELLDALGIP--YVIDPRLVRGLDYYTGTVFEIVTDGLGAQ--------GSVC 282

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253 330 AGGRYDGLVGMFDpkGRKVPCVGLSIGVERIFSIVEQRLEALEEKirtTETQVLVASAQKKLLEERLKLVSELWDAGIKA 409
Cdd:COG0124  283 GGGRYDGLVEQLG--GPPTPAVGFAIGLERLLLLLEELGLLPAAE---PPPDVYVVPLGEEARAEALKLAQELRAAGIRV 357

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 574279253 410 EL-LYKKNPKllNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVDVRREDLVEEIKRR 472
Cdd:COG0124  358 ELdLGGRKLK--KQLKYADKSGAPFVLILGEDELANGTVTLKDLATGEQETVPLDELVEYLKEL 419
HisRS-like_core cd00773
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ...
 40-365 1.05e-104

Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. It is responsible for the attachment of histidine to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs. This domain is also found at the C-terminus of eukaryotic GCN2 protein kinase and at the N-terminus of the ATP phosphoribosyltransferase accessory subunit, HisZ. HisZ along with HisG catalyze the first reaction in histidine biosynthesis. HisZ is found only in a subset of bacteria and differs from HisRS in lacking a C-terminal anti-codon binding domain.


Pssm-ID: 238396 [Multi-domain]  Cd Length: 261  Bit Score: 312.61  E-value: 1.05e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253  40 QMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGED-SKLIYDLKDQGGELLSLRYDLTVPFARYLAMNKL--- 115
Cdd:cd00773    1 EAALRRYIEDTLREVFERYGYEEIDTPVFEYTELFLRKSGDEvSKEMYRFKDKGGRDLALRPDLTAPVARAVAENLLslp 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253 116 TNIKRYHIAKVYRRDNPAmtRGRYREFYQCDFDIAGnFDPMIPDAECLKIMCEILSSLQIGDFLVKVNDRRILDGmfaIC 195
Cdd:cd00773   81 LPLKLYYIGPVFRYERPQ--KGRYREFYQVGVEIIG-SDSPLADAEVIALAVEILEALGLKDFQIKINHRGILDG---IA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253 196 GVSDSKFRTICSSVDKLDKvsweevknemvgekglapevadrigdyvqqhggvslveqllqdpklsqnkqalEGLGDLKL 275
Cdd:cd00773  155 GLLEDREEYIERLIDKLDK-----------------------------------------------------EALAHLEK 181

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253 276 LFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLLQTPAQageeplgvGSVAAGGRYDGLVGMFDpkGRKVPCVGLSI 355
Cdd:cd00773  182 LLDYLEALGVDIKYSIDLSLVRGLDYYTGIVFEAVADGLGAQ--------GSIAGGGRYDGLLEEFG--GEDVPAVGFAI 251

                        330
                 ....*....|
gi 574279253 356 GVERIFSIVE 365
Cdd:cd00773  252 GLERLLLALE 261
hisS TIGR00442
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ...
 28-460 6.33e-104

histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed genome. Apparent second copies from Bacillus subtilis, Synechocystis sp., and Aquifex aeolicus are slightly shorter, more closely related to each other than to other hisS proteins, and actually serve as regulatory subunits for an enzyme of histidine biosynthesis. They were excluded from the seed alignment and score much lower than do single copy histidyl-tRNA synthetases of other genomes not included in the seed alignment. These putative second copies of HisS score below the trusted cutoff. The regulatory protein kinase GCN2 of Saccharomyces cerevisiae (YDR283c), and related proteins from other species designated eIF-2 alpha kinase, have a domain closely related to histidyl-tRNA synthetase that may serve to detect and respond to uncharged tRNA(his), an indicator of amino acid starvation; these regulatory proteins are not orthologous and so score below the noise cutoff. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 273080 [Multi-domain]  Cd Length: 404  Bit Score: 315.96  E-value: 6.33e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253   28 KTPKGTRDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGEDS----KLIYDLKDQGGELLSLRYDLT 103
Cdd:TIGR00442   1 QKPRGTRDFLPEEMIKWQYIEETIREVFERYGFKEIRTPIFEYTELFKRKVGEETdivsKEMYTFKDKGGRSLTLRPEGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253  104 VPFARYLAMNKLTN---IKRYHIAKVYRRDNPAmtRGRYREFYQCDFDIAGNFDPMIpDAECLKIMCEILSSLQIGDFLV 180
Cdd:TIGR00442  81 APVARAVIENKLLLpkpFKLYYIGPMFRYERPQ--KGRYRQFHQFGVEVIGSDSPLA-DAEIIALAADILKELGLKDFTL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253  181 KVNDRRILDGMFAicgvsdsKFRTICSSVDK-LDKVSWEEVKNEMVGEKGLAPEVADRIGDYVQQhggvslveqllqDPK 259
Cdd:TIGR00442 158 EINSLGILEGRLE-------YREALIRYLDKhKDKLGEDSVRRLEKNPLRILDSKNEKIQELLKN------------APK 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253  260 LSQNKQAlEGLGDLKLLFEYLTLFGIddKISFDLSLARGLDYYTGVIYEAVLLQTPAQageeplgvGSVAAGGRYDGLVG 339
Cdd:TIGR00442 219 ILDFLCE-ESRAHFEELKELLDALGI--PYKIDPSLVRGLDYYTGTVFEFVTDDLGAQ--------GSICGGGRYDGLVE 287

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253  340 MFDpkGRKVPCVGLSIGVERIFSIVEQRLEALEEKirtTETQVLVASAQKKLLEERLKLVSELWDAGIKAElLYKKNPKL 419
Cdd:TIGR00442 288 ELG--GPPTPAVGFAIGIERLILLLEELGLIPPPS---KKPDVYVVPLGEEAELEALKLAQKLRKAGIRVE-VDLGGRKL 361

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 574279253  420 LNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVDV 460
Cdd:TIGR00442 362 KKQLKYADKLGARFALIIGEDELENGTVTLKDLETGEQETV 402
PRK12420 PRK12420
histidyl-tRNA synthetase; Provisional
 24-460 4.84e-83

histidyl-tRNA synthetase; Provisional


Pssm-ID: 237097 [Multi-domain]  Cd Length: 423  Bit Score: 262.74  E-value: 4.84e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253  24 KFVLKTPKGTRDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYG---EDSKLIYDLKDQGGELLSLRY 100
Cdd:PRK12420   1 MMEMRNVKGTKDYLPEEQVLRNKIKRALEDVFERYGCKPLETPTLNMYELMSSKYGggdEILKEIYTLTDQGKRDLALRY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253 101 DLTVPFARYLAMNKltNI----KRYHIAKVYrRDNPaMTRGRYREFYQCDFDIAGNFDPMiPDAECLKIMCEILSSLQIg 176
Cdd:PRK12420  81 DLTIPFAKVVAMNP--NIrlpfKRYEIGKVF-RDGP-IKQGRFREFIQCDVDIVGVESVM-AEAELMSMAFELFRRLNL- 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253 177 DFLVKVNDRRILDGMFAICGVSDSKFRTICSSVDKLDKVSWEEVKNEMVgEKGLAPEVADRIGDYVQQHGGVSLVEQllq 256
Cdd:PRK12420 155 EVTIQYNNRKLLNGILQAIGIPTELTSDVILSLDKIEKIGIDGVRKDLL-ERGISEEMADTICNTVLSCLQLSIADF--- 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253 257 dPKLSQNKQALEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEaVLLQTPAQAgeeplgvGSVAAGGRYDG 336
Cdd:PRK12420 231 -KEAFNNPLVAEGVNELQQLQQYLIALGINENCIFNPFLARGLTMYTGTVYE-IFLKDGSIT-------SSIGSGGRYDN 301

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253 337 LVGMFDPKGRKVPCVGLSIGVERIfsiveqrLEALEEKIRTTET-QVLVASAQKKLleERLKLVSELW-DAGIKAELLYk 414
Cdd:PRK12420 302 IIGAFRGDDMNYPTVGISFGLDVI-------YTALSQKETISSTaDVFIIPLGTEL--QCLQIAQQLRsTTGLKVELEL- 371

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 574279253 415 KNPKLLNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVDV 460
Cdd:PRK12420 372 AGRKLKKALNYANKENIPYVLIIGEEEVSTGTVMLRNMKEGSEVKV 417
PLN02530 PLN02530
histidine-tRNA ligase
 18-465 5.06e-52

histidine-tRNA ligase


Pssm-ID: 178145 [Multi-domain]  Cd Length: 487  Bit Score: 183.02  E-value: 5.06e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253  18 PDESKQKFVLKTPKGTRDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGED-SKLIYDLKDQGGELL 96
Cdd:PLN02530  61 QEDGKPKIDVNPPKGTRDFPPEDMRLRNWLFDHFREVSRLFGFEEVDAPVLESEELYIRKAGEEiTDQLYNFEDKGGRRV 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253  97 SLRYDLTVPFARyLAMNKLTNI----KRYHIAKVYRRDNpaMTRGRYREFYQCDFDIAGnFDPMIPDAECLKIMCEILSS 172
Cdd:PLN02530 141 ALRPELTPSLAR-LVLQKGKSLslplKWFAIGQCWRYER--MTRGRRREHYQWNMDIIG-VPGVEAEAELLAAIVTFFKR 216

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253 173 LQI--GDFLVKVNDRRILDGMFAICGVSDSKFRTICSSVDKLDKVSWEEVKNEMvGEKGLAPEVADRIGDyVQQHGGVSL 250
Cdd:PLN02530 217 VGItsSDVGIKVSSRKVLQAVLKSYGIPEESFAPVCVIVDKLEKLPREEIEKEL-DTLGVSEEAIEGILD-VLSLKSLDD 294

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253 251 VEQLLqdpklsqnKQALEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVllqtpAQAGEeplgVGSVAA 330
Cdd:PLN02530 295 LEALL--------GADSEAVADLKQLFSLAEAYGYQDWLVFDASVVRGLAYYTGIVFEGF-----DRAGK----LRAICG 357

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253 331 GGRYDGLVGMFDpkGRKVPCVGLSIGVERIFSIVEQRlEALEEKIRTTETqvLVASAQKKLLEERLKLVSELWDAGIKAE 410
Cdd:PLN02530 358 GGRYDRLLSTFG--GEDTPACGFGFGDAVIVELLKEK-GLLPELPHQVDD--VVFALDEDLQGAAAGVASRLREKGRSVD 432

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 574279253 411 L-LYKKNPKLLnqLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVDVRREDL 465
Cdd:PLN02530 433 LvLEPKKLKWV--FKHAERIGAKRLVLVGASEWERGMVRVKDLSSGEQTEVKLDEL 486
HisZ COG3705
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism];
38-360 1.58e-50

ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism];


Pssm-ID: 442919 [Multi-domain]  Cd Length: 312  Bit Score: 174.21  E-value: 1.58e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253  38 PRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGEDSKL-IYDLKDQGGELLSLRYDLTVPFARYLAmNKLT 116
Cdd:COG3705    2 PEEAARKEELRRRLLDVFRSWGYELVEPPLLEYLDSLLTGSGADLDLqTFKLVDQLGRTLGLRPDMTPQVARIAA-TRLA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253 117 NIKR----YHIAKVYRrdNPAMTRGRYREFYQC------DFDIAGnfdpmipDAECLKIMCEILSSLQIGDFLVKVNDRR 186
Cdd:COG3705   81 NRPGplrlCYAGNVFR--TRPSGLGRSREFLQAgaeligHAGLEA-------DAEVIALALEALKAAGLEDFTLDLGHVG 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253 187 ILDGMFAICGVSDSKFRTICSSVDKLDKVsweEVKnEMVGEKGLAPEVADRIGDYVQQHGGVSLVEQLLqdpKLSQNKQA 266
Cdd:COG3705  152 LFRALLEALGLSEEQREELRRALARKDAV---ELE-ELLAELGLSEELAEALLALPELYGGEEVLARAR---ALLLDAAI 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253 267 LEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLlqtpAQAGEEplgvgsVAAGGRYDGLVGMFdpkGR 346
Cdd:COG3705  225 RAALDELEALAEALAARGPDVRLTFDLSELRGYDYYTGIVFEAYA----PGVGDP------LARGGRYDGLLAAF---GR 291

                        330
                 ....*....|....
gi 574279253 347 KVPCVGLSIGVERI 360
Cdd:COG3705  292 ARPATGFSLDLDRL 305
hisZ_biosyn_reg TIGR00443
ATP phosphoribosyltransferase, regulatory subunit; Apparant second copies of histidyl-tRNA ...
 34-360 1.59e-50

ATP phosphoribosyltransferase, regulatory subunit; Apparant second copies of histidyl-tRNA synthetase, found in Bacillus subtilis, Synechocystis sp., Aquifex aeolicus, and others, are in fact a regulatory subunit of ATP phosphoribosyltransferase, and usually encoded by a gene adjacent to that encoding the catalytic subunit. [Amino acid biosynthesis, Histidine family]


Pssm-ID: 273081 [Multi-domain]  Cd Length: 313  Bit Score: 174.34  E-value: 1.59e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253   34 RDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGEDSKLIYDLKDQGGELLSLRYDLTVPFARyLAMN 113
Cdd:TIGR00443   1 RDLLPEEAARKEEIERQLQDVFRSWGYQEIITPTLEYLDTLSAGSGILNEDLFKLFDQLGRVLGLRPDMTAPIAR-LVST 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253  114 KLTNIKR----YHIAKVYRRDNPAmtRGRYREFYQCDFDIAGNfDPMIPDAECLKIMCEILSSLQIGDFLVKVNDRRILD 189
Cdd:TIGR00443  80 RLRDRPLplrlCYAGNVFRTNESG--GGRSREFTQAGVELIGA-GGPAADAEVIALLIEALKALGLKDFKIELGHVGLVR 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253  190 GMFAICGVSDSKFRTICSSVDKLDKVSWEEVknemVGEKGLAPEVADRIGDYVQQHGGVSLVEQLLQdpKLSQNKQALEG 269
Cdd:TIGR00443 157 ALLEEAGLPEEAREALREALARKDLVALEEL----VAELGLSPEVRERLLALPRLRGDGEEVLEEAR--ALAGSETAEAA 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253  270 LGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLLQTPAQageeplgvgsVAAGGRYDGLVGMFdpkGRKVP 349
Cdd:TIGR00443 231 LDELEAVLELLEARGVEEYISLDLGLVRGYHYYTGLIFEGYAPGLGAP----------LAGGGRYDELLGRF---GRPLP 297

                         330
                  ....*....|.
gi 574279253  350 CVGLSIGVERI 360
Cdd:TIGR00443 298 ATGFALNLERL 308
hisZ PRK12292
ATP phosphoribosyltransferase regulatory subunit; Provisional
 30-411 3.38e-48

ATP phosphoribosyltransferase regulatory subunit; Provisional


Pssm-ID: 237043 [Multi-domain]  Cd Length: 391  Bit Score: 170.43  E-value: 3.38e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253  30 PKGTRDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLM--GKYGEDSKLIYDLKDQGGELLSLRYDLTVPFA 107
Cdd:PRK12292   6 PEGIRDLLPEEARKIEEIRRRLLDLFRRWGYEEVITPTLEYLDTLLagGGAILDLRTFKLVDQLSGRTLGLRPDMTAQIA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253 108 RyLAMNKLTNIKR----YHIAKVYRrdNPAMTRGRYREFYQCDFDIAGnFDPMIPDAECLKIMCEILSSLQIGDFLVKVN 183
Cdd:PRK12292  86 R-IAATRLANRPGplrlCYAGNVFR--AQERGLGRSREFLQSGVELIG-DAGLEADAEVILLLLEALKALGLPNFTLDLG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253 184 DRRILDGMFAICGVSDSKFRTICSSVDKLDKVSWEEVknemvgEKGLAPEVADRIGDYVQQHGGVSLVEQLLQdpkLSQN 263
Cdd:PRK12292 162 HVGLFRALLEAAGLSEELEEVLRRALANKDYVALEEL------VLDLSEELRDALLALPRLRGGREVLEEARK---LLPS 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253 264 KQALEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLLQTPAqageeplgvgSVAAGGRYDGLVGMFdp 343
Cdd:PRK12292 233 LPIKRALDELEALAEALEKYGYGIPLSLDLGLLRHLDYYTGIVFEGYVDGVGN----------PIASGGRYDDLLGRF-- 300

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 574279253 344 kGRKVPCVGLSIGVERIfsiveqrLEALEEKiRTTETQVLVASAQKKLLEERLKLVSELWDAGIKAEL 411
Cdd:PRK12292 301 -GRARPATGFSLDLDRL-------LELQLEL-PVEARKDLVIAPDSEALAAALAAAQELRKKGEIVVL 359
tRNA-synt_His pfam13393
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ...
 32-360 1.33e-44

Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP phosphoribosyltransferase regulatory subunits.


Pssm-ID: 433170 [Multi-domain]  Cd Length: 309  Bit Score: 158.52  E-value: 1.33e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253   32 GTRDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGEDSKLIYDLKDQGGELLSLRYDLTVPFARYLA 111
Cdd:pfam13393   1 GIRDLLPPEARRIEELRRRLLDLFRSWGYELVMPPLLEYLDSLLTGTGADLDQTFKLVDQSGRLLGLRADITPQVARIDA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253  112 mnKLTNIKR----YHIAKVYRRDNPAMtrGRYREFYQCDFDIAGNFDPMiPDAECLKIMCEILSSLQIGDFLVKVNDRRI 187
Cdd:pfam13393  81 --HRLNRPGplrlCYAGSVLRTRPKGL--GRSREPLQVGAELIGHAGIE-ADAEIISLLLEALAAAGVPGVTLDLGHVGL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253  188 LDGMFAICGVSDSKFRTICSSVDKLDkvsWEEVKnEMVGEKGLAPEVADRIGDYVQQHGGVSLVEQLLQDpkLSQNKQAL 267
Cdd:pfam13393 156 VRALLEAAGLSEALEEALRAALQRKD---AAELA-ELAAEAGLPPALRRALLALPDLYGGPEVLDEARAA--LPGLPALQ 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253  268 EGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLlqtpAQAGEEplgvgsVAAGGRYDGLVGMFdpkGRK 347
Cdd:pfam13393 230 EALDELEALAALLEALGDGVRLTFDLAELRGYEYYTGIVFAAYA----PGVGEP------LARGGRYDDLGAAF---GRA 296

                         330
                  ....*....|...
gi 574279253  348 VPCVGLSIGVERI 360
Cdd:pfam13393 297 RPATGFSLDLEAL 309
HisRS_anticodon cd00859
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases ...
 379-470 4.66e-29

HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only.


Pssm-ID: 238436 [Multi-domain]  Cd Length: 91  Bit Score: 109.55  E-value: 4.66e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253 379 ETQVLVASAQKKLLEERLKLVSELWDAGIKAELLYKkNPKLLNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEV 458
Cdd:cd00859    1 EVDVYVVPLGEGALSEALELAEQLRDAGIKAEIDYG-GRKLKKQFKYADRSGARFAVILGEDELAAGVVTVKDLETGEQE 79

                         90
                 ....*....|..
gi 574279253 459 DVRREDLVEEIK 470
Cdd:cd00859   80 TVALDELVEELK 91
syh CHL00201
histidine-tRNA synthetase; Provisional
 31-469 7.07e-28

histidine-tRNA synthetase; Provisional


Pssm-ID: 164576 [Multi-domain]  Cd Length: 430  Bit Score: 115.38  E-value: 7.07e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253  31 KGTRDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGEDSKLI----YDLKDQGGELLSLRYDLTVPF 106
Cdd:CHL00201   8 RGTKDILPDEINYWQFIHDKALTLLSLANYSEIRTPIFENSSLYDRGIGETTDIVnkemYRFTDRSNRDITLRPEGTAGI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253 107 ARYLAMNKLT---NIKR-YHIAKVYRRDNPamTRGRYREFYQCDFDIAGNFDPMiPDAECLKIMCEILSSLQIGDFLVKV 182
Cdd:CHL00201  88 VRAFIENKMDyhsNLQRlWYSGPMFRYERP--QSGRQRQFHQLGIEFIGSIDAR-ADTEVIHLAMQIFNELQVKNLILDI 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253 183 N------DRRILDgmfaicgvsdSKFRTICSSV-DKLDKVSweevKNEMVGEkglaP-EVADRIGDYVQqhggvslvEQL 254
Cdd:CHL00201 165 NsigkleDRQSYQ----------LKLVEYLSQYqDDLDTDS----QNRLYSN----PiRILDSKNLKTQ--------EIL 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253 255 LQDPKLSQ--NKQALEGLGDLkllFEYLTLFGIDDKISFdlSLARGLDYYTGVIYEAVLLQTPAQageeplgvGSVAAGG 332
Cdd:CHL00201 219 DGAPKISDflSLESTEHFYDV---CTYLNLLNIPYKINY--KLVRGLDYYNDTAFEIKTLSSNGQ--------DTICGGG 285

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253 333 RYDGLVGMFDpkGRKVPCVGLSIGVERIFSIVEQRLEALEEKIrttetQVLVASAQKKLLEERLKLVSELWDAGIKAELL 412
Cdd:CHL00201 286 RYDSLIHQLG--GPKTPAVGCAIGLERLLLIAKDNIILPKQSI-----DVYIATQGLKAQKKGWEIIQFLEKQNIKFELD 358

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 574279253 413 YkKNPKLLNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVDVRREDLVEEI 469
Cdd:CHL00201 359 L-SSSNFHKQIKQAGKKRAKACIILGDNEIMDNCITIKWLDEQVQENAQYSNFKQEI 414
hisZ PRK12295
ATP phosphoribosyltransferase regulatory subunit; Provisional
 41-360 6.27e-23

ATP phosphoribosyltransferase regulatory subunit; Provisional


Pssm-ID: 183413 [Multi-domain]  Cd Length: 373  Bit Score: 100.01  E-value: 6.27e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253  41 MAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGED-SKLIYDLKDQGGELLSLRYDLTVPFAR-YLAMNKLTNI 118
Cdd:PRK12295   4 LSASAAAAEALLASFEAAGAVRVDPPILQPAEPFLDLSGEDiRRRIFVTSDENGEELCLRPDFTIPVCRrHIATAGGEPA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253 119 KRYHIAKVYRRdnpamTRGRYREFYQCDFDIAGNFDPMIPDAECLKIMCEILSSLQIGDFLVKVNDRRILDGMFAICGVS 198
Cdd:PRK12295  84 RYAYLGEVFRQ-----RRDRASEFLQAGIESFGRADPAAADAEVLALALEALAALGPGDLEVRLGDVGLFAALVDALGLP 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253 199 DS-KFRTIcssVDKLDKVSWEEVKNEMVGEKGLAPEVADRIGDYVQQHGGVS-LVEQLLQDPKLSQN------------- 263
Cdd:PRK12295 159 PGwKRRLL---RHFGRPRSLDALLARLAGPRVDPLDEHAGVLAALADEAAARaLVEDLMSIAGISPVggrspaeiarrll 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253 264 -----------------------------KQALEGL----GDLKL-------LFE----YLTLFGID-DKISFDLSLARG 298
Cdd:PRK12295 236 ekaalaaaarlpaealavlerflaisgppDAALAALralaADAGLdldaaldRFEarlaALAARGIDlERLRFSASFGRP 315

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 574279253 299 LDYYTGVIYEAvllqTPAQAGEEPLgvgsvAAGGRYDGLVGMFDpKGRKVPCVGLSIGVERI 360
Cdd:PRK12295 316 LDYYTGFVFEI----RAAGNGDPPL-----AGGGRYDGLLTRLG-AGEPIPAVGFSIWLDRL 367
HGTP_anticodon pfam03129
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ...
 381-472 1.32e-17

Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA synthetases it is probably the anticodon binding domain.


Pssm-ID: 460819 [Multi-domain]  Cd Length: 94  Bit Score: 77.63  E-value: 1.32e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253  381 QVLVASAQKK---LLEERLKLVSELWDAGIKAELLYKkNPKLLNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREE 457
Cdd:pfam03129   1 QVVVIPLGEKaeeLEEYAQKLAEELRAAGIRVELDDR-NESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQ 79

                          90
                  ....*....|....*
gi 574279253  458 VDVRREDLVEEIKRR 472
Cdd:pfam03129  80 ETVSLDELVEKLKEL 94
PRK12421 PRK12421
ATP phosphoribosyltransferase regulatory subunit; Provisional
 30-406 1.49e-11

ATP phosphoribosyltransferase regulatory subunit; Provisional


Pssm-ID: 237098  Cd Length: 392  Bit Score: 65.76  E-value: 1.49e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253  30 PKGTRDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGEDSKL-IYDLKDQ-GGELLSLRYDLTVPFA 107
Cdd:PRK12421  10 PDGVADVLPEEAQKIERLRRRLLDLFASRGYQLVMPPLIEYLESLLTGAGQDLKLqTFKLIDQlSGRLMGVRADITPQVA 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253 108 RYLA-MNKLTNIKRY-HIAKVY--RRDNPAMTRGRYR---EFYQCDfDIAGnfdpmipDAECLKIMCEILSSLQIGDFLV 180
Cdd:PRK12421  90 RIDAhLLNREGVARLcYAGSVLhtLPQGLFGSRTPLQlgaELYGHA-GIEA-------DLEIIRLMLGLLRNAGVPALHL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253 181 KVNDRRILDGMFAICGVSDSKFRTIcssVDKLDKVSWEEVKnEMVGEKGLAPEVADRIGDYVQQHGGVSLVEQLLQDpKL 260
Cdd:PRK12421 162 DLGHVGIFRRLAELAGLSPEEEEEL---FDLLQRKALPELA-EVCQNLGVGSDLRRMFYALARLNGGLEALDRALSV-LA 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253 261 SQNKQALEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYeAVLLQTPAQAgeeplgvgsVAAGGRYDGLVGM 340
Cdd:PRK12421 237 LQDAAIRQALDELKTLAAHLKNRWPELPVSIDLAELRGYHYHTGLVF-AAYIPGRGQA---------LARGGRYDGIGEA 306

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 574279253 341 FdpkGRKVPCVGlsigveriFSIVEQRLEALEEKIRTTETQVLVASAQKKLLEErlklVSELWDAG 406
Cdd:PRK12421 307 F---GRARPATG--------FSMDLKELLALQFLEEEAGAILAPWGDDPDLLAA----IAELRQQG 357
HGTP_anticodon2 pfam12745
Anticodon binding domain of tRNAs; This is an HGTP_anticodon binding domain, found largely on ...
 382-472 2.93e-08

Anticodon binding domain of tRNAs; This is an HGTP_anticodon binding domain, found largely on Gcn2 proteins which bind tRNA to down regulate translation in certain stress situations.


Pssm-ID: 432758  Cd Length: 259  Bit Score: 54.53  E-value: 2.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253  382 VLVASAQKKLL-EERLKLVSELWDAGIKAELLYKKNPKLLNQLQYCEEAGIPLVAIIGEQEL----KDGVIKLRSVTSRE 456
Cdd:pfam12745   8 VLVASFDASILrTTGVEILQELWAHGISADLAVDASYSPEDLVSRARDDGVSWIVIIKQQNKssdsKYKPLKVKNLLRKE 87

                          90       100
                  ....*....|....*....|
gi 574279253  457 EVDVRREDLV----EEIKRR 472
Cdd:pfam12745  88 DVDLDSDELVswlrGEIRER 107
PRK03991 PRK03991
threonyl-tRNA synthetase; Validated
 356-476 1.03e-05

threonyl-tRNA synthetase; Validated


Pssm-ID: 235190 [Multi-domain]  Cd Length: 613  Bit Score: 47.94  E-value: 1.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253 356 GVER-IFSIVE-QRLEALEEKIRT-----TETQVLVASAQKKLLEERLKLVSELWDAGIKAEL------LYKKnpkllnq 422
Cdd:PRK03991 469 SIERvIYALLEkAAKEEEEGKVPMlptwlSPTQVRVIPVSERHLDYAEEVADKLEAAGIRVDVddrdesLGKK------- 541

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 574279253 423 lqyCEEAG---IPLVAIIGEQELKDGVIklrSVTSREE---VDVRREDLVEEIKRRT-GQP 476
Cdd:PRK03991 542 ---IRDAGkewIPYVVVIGDKEMESGKL---TVTIREEsekVEMTLEELIERIKEETkGYP 596
HisRS_RNA cd00938
HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS ...
 2-20 1.32e-04

HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). This domain consists of a helix- turn- helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.


Pssm-ID: 238474 [Multi-domain]  Cd Length: 45  Bit Score: 39.38  E-value: 1.32e-04
                         10
                 ....*....|....*....
gi 574279253   2 IEEEVAKLLKLKAQLGPDE 20
Cdd:cd00938   27 IAEEVAKLLELKAQLGGDE 45
ThrRS_anticodon cd00860
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases ...
 380-470 6.55e-03

ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only.


Pssm-ID: 238437 [Multi-domain]  Cd Length: 91  Bit Score: 35.94  E-value: 6.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253 380 TQVLVASAQKKLLEERLKLVSELWDAGIKAELLYKkNPKLLNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVD 459
Cdd:cd00860    2 VQVVVIPVTDEHLDYAKEVAKKLSDAGIRVEVDLR-NEKLGKKIREAQLQKIPYILVVGDKEVETGTVSVRTRDGGDLGS 80

                         90
                 ....*....|.
gi 574279253 460 VRREDLVEEIK 470
Cdd:cd00860   81 MSLDEFIEKLK 91
PRK09194 PRK09194
prolyl-tRNA synthetase; Provisional
 342-471 8.62e-03

prolyl-tRNA synthetase; Provisional


Pssm-ID: 236405 [Multi-domain]  Cd Length: 565  Bit Score: 38.53  E-value: 8.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253 342 DPKGRKVP----CVGlsIGVERIFS-IVEQRLEaleEK--IRTTET---QV-LVAS-----AQKKLLEerlKLVSELWDA 405
Cdd:PRK09194 426 DENGKAQPlimgCYG--IGVSRLVAaAIEQNHD---EKgiIWPKAIapfDVhIVPVnmkdeEVKELAE---KLYAELQAA 497

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574279253 406 GIK----------------AELLykknpkllnqlqyceeaGIPLVAIIGEQELKDGVIKLRSVTSREEVDVRREDLVEEI 469
Cdd:PRK09194 498 GIEvllddrkerpgvkfadADLI-----------------GIPHRIVVGDRGLAEGIVEYKDRRTGEKEEVPVDELVEFL 560


                 ..
gi 574279253 470 KR 471
Cdd:PRK09194 561 KA 562
 
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.
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