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Conserved domains on  [gi|1958743144|ref|XP_038952791|]
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probable histidine--tRNA ligase, mitochondrial isoform X2 [Rattus norvegicus]

Protein Classification

histidine--tRNA ligase( domain architecture ID 1007767)

histidine--tRNA ligase (HisRS) is responsible for the attachment of histidine to the 3' OH group of ribose of the appropriate tRNA

CATH:  3.40.50.800|3.30.930.10
EC:  6.1.1.21
Gene Ontology:  GO:0003723|GO:0042802|GO:0004821|GO:0006427|GO:0005524|GO:0006412

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02972 super family cl33611
Histidyl-tRNA synthetase
 15-343 1.87e-106

Histidyl-tRNA synthetase


The actual alignment was detected with superfamily member PLN02972:

Pssm-ID: 215525 [Multi-domain]  Cd Length: 763  Bit Score: 328.38  E-value: 1.87e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743144  15 DFDIAGEFDPMIPDAECLRIMCEILSGLQLGDFLIKVNDRRVVDGMFAVCGVPESKFRTICSSMDKLDKMSWEDVRLEMV 94
Cdd:PLN02972  444 DFDIAGVYEPMGPDFEIIKVLTELLDELDIGTYEVKLNHRKLLDGMLEICGVPPEKFRTICSSIDKLDKQSFEQVKKEMV 523

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743144  95 AGKGLAPEVADRIGDYVQCHGG-ISLVEELFK-DPRLSQSQLALQGLGDLKLLFEYLRLFGIADKISLDLSLARGLDYYT 172
Cdd:PLN02972  524 EEKGLSNETADKIGNFVKERGPpLELLSKLRQeGSEFLGNASSRAALDELEIMFKALEKSKAIGKIVFDLSLARGLDYYT 603

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743144 173 GVIYEAVLLESpaqagketlNVGSVAAGGRYDRLVAQFDPKghSVPCVGLSIGVERIFYLVEQKMKISCEKVRTTETQVF 252
Cdd:PLN02972  604 GVIYEAVFKGA---------QVGSIAAGGRYDNLVGMFSGK--QVPAVGVSLGIERVFAIMEQQEEEKSQVIRPTETEVL 672

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743144 253 VATPQKNFLQERLKIIAQLWDAGIKAEmlYKNNPKLLTQLHYCEKEDIPLMVIIGEQEQNEGVVKLRSVASREEVTVNRE 332
Cdd:PLN02972  673 VSIIGDDKLALAAELVSELWNAGIKAE--YKVSTRKAKHLKRAKESGIPWMVLVGEKELSKGFVKLKNLEAGVEEEVDRT 750

                         330
                  ....*....|.
gi 1958743144 333 SLVAEIQKRLS 343
Cdd:PLN02972  751 CFVQELKAELL 761
 
Name Accession Description Interval E-value
PLN02972 PLN02972
Histidyl-tRNA synthetase
 15-343 1.87e-106

Histidyl-tRNA synthetase


Pssm-ID: 215525 [Multi-domain]  Cd Length: 763  Bit Score: 328.38  E-value: 1.87e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743144  15 DFDIAGEFDPMIPDAECLRIMCEILSGLQLGDFLIKVNDRRVVDGMFAVCGVPESKFRTICSSMDKLDKMSWEDVRLEMV 94
Cdd:PLN02972  444 DFDIAGVYEPMGPDFEIIKVLTELLDELDIGTYEVKLNHRKLLDGMLEICGVPPEKFRTICSSIDKLDKQSFEQVKKEMV 523

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743144  95 AGKGLAPEVADRIGDYVQCHGG-ISLVEELFK-DPRLSQSQLALQGLGDLKLLFEYLRLFGIADKISLDLSLARGLDYYT 172
Cdd:PLN02972  524 EEKGLSNETADKIGNFVKERGPpLELLSKLRQeGSEFLGNASSRAALDELEIMFKALEKSKAIGKIVFDLSLARGLDYYT 603

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743144 173 GVIYEAVLLESpaqagketlNVGSVAAGGRYDRLVAQFDPKghSVPCVGLSIGVERIFYLVEQKMKISCEKVRTTETQVF 252
Cdd:PLN02972  604 GVIYEAVFKGA---------QVGSIAAGGRYDNLVGMFSGK--QVPAVGVSLGIERVFAIMEQQEEEKSQVIRPTETEVL 672

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743144 253 VATPQKNFLQERLKIIAQLWDAGIKAEmlYKNNPKLLTQLHYCEKEDIPLMVIIGEQEQNEGVVKLRSVASREEVTVNRE 332
Cdd:PLN02972  673 VSIIGDDKLALAAELVSELWNAGIKAE--YKVSTRKAKHLKRAKESGIPWMVLVGEKELSKGFVKLKNLEAGVEEEVDRT 750

                         330
                  ....*....|.
gi 1958743144 333 SLVAEIQKRLS 343
Cdd:PLN02972  751 CFVQELKAELL 761
HisS COG0124
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ...
 15-344 1.84e-64

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: 209.98  E-value: 1.84e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743144  15 DFDIAGEFDPMIpDAECLRIMCEILSGLQLGDFLIKVNDRrvvdgmfavcGVPESKFRTICSSMDKLDKMSWEDVrlemv 94
Cdd:COG0124   126 GVEVIGSDSPLA-DAEVIALAADLLKALGLKDFTLEINSR----------GLPEERAEALLRYLDKLDKIGHEDV----- 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743144  95 agkgLAPEVADRIG-----DYVQCHGGIslVEELFKD-PRLSQSqLALQGLGDLKLLFEYLRLFGIadKISLDLSLARGL 168
Cdd:COG0124   190 ----LDEDSQRRLEtnplrAILDSKGPD--CQEVLADaPKLLDY-LGEEGLAHFEEVLELLDALGI--PYVIDPRLVRGL 260

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743144 169 DYYTGVIYEAVLLESPAQagketlnvGSVAAGGRYDRLVAQFDpkGHSVPCVGLSIGVERIFYLVEQKmkiSCEKVRTTE 248
Cdd:COG0124   261 DYYTGTVFEIVTDGLGAQ--------GSVCGGGRYDGLVEQLG--GPPTPAVGFAIGLERLLLLLEEL---GLLPAAEPP 327

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743144 249 TQVFVATPQKNFLQERLKIIAQLWDAGIKAEMLYKNNpKLLTQLHYCEKEDIPLMVIIGEQEQNEGVVKLRSVASREEVT 328
Cdd:COG0124   328 PDVYVVPLGEEARAEALKLAQELRAAGIRVELDLGGR-KLKKQLKYADKSGAPFVLILGEDELANGTVTLKDLATGEQET 406

                         330
                  ....*....|....*.
gi 1958743144 329 VNRESLVAEIQKRLSE 344
Cdd:COG0124   407 VPLDELVEYLKELLAE 422
hisS TIGR00442
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ...
 15-331 1.52e-49

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: 170.35  E-value: 1.52e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743144  15 DFDIAGEFDPMIpDAECLRIMCEILSGLQLGDFLIKVNDRRVVDGMFAvcgvpesKFRTICSSMDK-LDKMSWEDVRLEM 93
Cdd:TIGR00442 124 GVEVIGSDSPLA-DAEIIALAADILKELGLKDFTLEINSLGILEGRLE-------YREALIRYLDKhKDKLGEDSVRRLE 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743144  94 VAGKGLAPEVADRIGDYVQchGGISLVEELFKDprlsqsqlalqGLGDLKLLFEYLRLFGIadKISLDLSLARGLDYYTG 173
Cdd:TIGR00442 196 KNPLRILDSKNEKIQELLK--NAPKILDFLCEE-----------SRAHFEELKELLDALGI--PYKIDPSLVRGLDYYTG 260

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743144 174 VIYEAVLLESPAQagketlnvGSVAAGGRYDRLVAQFDpkGHSVPCVGLSIGVERIFYLVEQKMKISCEKvrtTETQVFV 253
Cdd:TIGR00442 261 TVFEFVTDDLGAQ--------GSICGGGRYDGLVEELG--GPPTPAVGFAIGIERLILLLEELGLIPPPS---KKPDVYV 327

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958743144 254 ATPQKNFLQERLKIIAQLWDAGIKAEMLYKNNpKLLTQLHYCEKEDIPLMVIIGEQEQNEGVVKLRSVASREEVTVNR 331
Cdd:TIGR00442 328 VPLGEEAELEALKLAQKLRKAGIRVEVDLGGR-KLKKQLKYADKLGARFALIIGEDELENGTVTLKDLETGEQETVPL 404
HisRS-like_core cd00773
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ...
 15-234 2.48e-45

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: 155.45  E-value: 2.48e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743144  15 DFDIAGEfDPMIPDAECLRIMCEILSGLQLGDFLIKVNDRRVVDGmfaVCGVPESKFRTICSSMDKLDKmswedvrlemv 94
Cdd:cd00773   109 GVEIIGS-DSPLADAEVIALAVEILEALGLKDFQIKINHRGILDG---IAGLLEDREEYIERLIDKLDK----------- 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743144  95 agkglapevadrigdyvqchggislveelfkdprlsqsqlalQGLGDLKLLFEYLRLFGIADKISLDLSLARGLDYYTGV 174
Cdd:cd00773   174 ------------------------------------------EALAHLEKLLDYLEALGVDIKYSIDLSLVRGLDYYTGI 211

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743144 175 IYEAVLLESPAQagketlnvGSVAAGGRYDRLVAQFDpkGHSVPCVGLSIGVERIFYLVE 234
Cdd:cd00773   212 VFEAVADGLGAQ--------GSIAGGGRYDGLLEEFG--GEDVPAVGFAIGLERLLLALE 261
tRNA-synt_His pfam13393
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ...
 28-229 9.90e-27

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: 107.29  E-value: 9.90e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743144  28 DAECLRIMCEILSGLQLGDFLIKVNDRRVVDGMFAVCGVPESKFRTIcssMDKLDKMSWEDVRlEMVAGKGLAPEVADRI 107
Cdd:pfam13393 127 DAEIISLLLEALAAAGVPGVTLDLGHVGLVRALLEAAGLSEALEEAL---RAALQRKDAAELA-ELAAEAGLPPALRRAL 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743144 108 GDYVQCHGGISLVEELFKdpRLSQSQLALQGLGDLKLLFEYLRLFGIADKISLDLSLARGLDYYTGVIYEAVLlespAQA 187
Cdd:pfam13393 203 LALPDLYGGPEVLDEARA--ALPGLPALQEALDELEALAALLEALGDGVRLTFDLAELRGYEYYTGIVFAAYA----PGV 276

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1958743144 188 GKEtlnvgsVAAGGRYDRLVAQFdpkGHSVPCVGLSIGVERI 229
Cdd:pfam13393 277 GEP------LARGGRYDDLGAAF---GRARPATGFSLDLEAL 309
 
Name Accession Description Interval E-value
PLN02972 PLN02972
Histidyl-tRNA synthetase
 15-343 1.87e-106

Histidyl-tRNA synthetase


Pssm-ID: 215525 [Multi-domain]  Cd Length: 763  Bit Score: 328.38  E-value: 1.87e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743144  15 DFDIAGEFDPMIPDAECLRIMCEILSGLQLGDFLIKVNDRRVVDGMFAVCGVPESKFRTICSSMDKLDKMSWEDVRLEMV 94
Cdd:PLN02972  444 DFDIAGVYEPMGPDFEIIKVLTELLDELDIGTYEVKLNHRKLLDGMLEICGVPPEKFRTICSSIDKLDKQSFEQVKKEMV 523

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743144  95 AGKGLAPEVADRIGDYVQCHGG-ISLVEELFK-DPRLSQSQLALQGLGDLKLLFEYLRLFGIADKISLDLSLARGLDYYT 172
Cdd:PLN02972  524 EEKGLSNETADKIGNFVKERGPpLELLSKLRQeGSEFLGNASSRAALDELEIMFKALEKSKAIGKIVFDLSLARGLDYYT 603

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743144 173 GVIYEAVLLESpaqagketlNVGSVAAGGRYDRLVAQFDPKghSVPCVGLSIGVERIFYLVEQKMKISCEKVRTTETQVF 252
Cdd:PLN02972  604 GVIYEAVFKGA---------QVGSIAAGGRYDNLVGMFSGK--QVPAVGVSLGIERVFAIMEQQEEEKSQVIRPTETEVL 672

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743144 253 VATPQKNFLQERLKIIAQLWDAGIKAEmlYKNNPKLLTQLHYCEKEDIPLMVIIGEQEQNEGVVKLRSVASREEVTVNRE 332
Cdd:PLN02972  673 VSIIGDDKLALAAELVSELWNAGIKAE--YKVSTRKAKHLKRAKESGIPWMVLVGEKELSKGFVKLKNLEAGVEEEVDRT 750

                         330
                  ....*....|.
gi 1958743144 333 SLVAEIQKRLS 343
Cdd:PLN02972  751 CFVQELKAELL 761
HisS COG0124
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ...
 15-344 1.84e-64

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: 209.98  E-value: 1.84e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743144  15 DFDIAGEFDPMIpDAECLRIMCEILSGLQLGDFLIKVNDRrvvdgmfavcGVPESKFRTICSSMDKLDKMSWEDVrlemv 94
Cdd:COG0124   126 GVEVIGSDSPLA-DAEVIALAADLLKALGLKDFTLEINSR----------GLPEERAEALLRYLDKLDKIGHEDV----- 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743144  95 agkgLAPEVADRIG-----DYVQCHGGIslVEELFKD-PRLSQSqLALQGLGDLKLLFEYLRLFGIadKISLDLSLARGL 168
Cdd:COG0124   190 ----LDEDSQRRLEtnplrAILDSKGPD--CQEVLADaPKLLDY-LGEEGLAHFEEVLELLDALGI--PYVIDPRLVRGL 260

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743144 169 DYYTGVIYEAVLLESPAQagketlnvGSVAAGGRYDRLVAQFDpkGHSVPCVGLSIGVERIFYLVEQKmkiSCEKVRTTE 248
Cdd:COG0124   261 DYYTGTVFEIVTDGLGAQ--------GSVCGGGRYDGLVEQLG--GPPTPAVGFAIGLERLLLLLEEL---GLLPAAEPP 327

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743144 249 TQVFVATPQKNFLQERLKIIAQLWDAGIKAEMLYKNNpKLLTQLHYCEKEDIPLMVIIGEQEQNEGVVKLRSVASREEVT 328
Cdd:COG0124   328 PDVYVVPLGEEARAEALKLAQELRAAGIRVELDLGGR-KLKKQLKYADKSGAPFVLILGEDELANGTVTLKDLATGEQET 406

                         330
                  ....*....|....*.
gi 1958743144 329 VNRESLVAEIQKRLSE 344
Cdd:COG0124   407 VPLDELVEYLKELLAE 422
hisS TIGR00442
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ...
 15-331 1.52e-49

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: 170.35  E-value: 1.52e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743144  15 DFDIAGEFDPMIpDAECLRIMCEILSGLQLGDFLIKVNDRRVVDGMFAvcgvpesKFRTICSSMDK-LDKMSWEDVRLEM 93
Cdd:TIGR00442 124 GVEVIGSDSPLA-DAEIIALAADILKELGLKDFTLEINSLGILEGRLE-------YREALIRYLDKhKDKLGEDSVRRLE 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743144  94 VAGKGLAPEVADRIGDYVQchGGISLVEELFKDprlsqsqlalqGLGDLKLLFEYLRLFGIadKISLDLSLARGLDYYTG 173
Cdd:TIGR00442 196 KNPLRILDSKNEKIQELLK--NAPKILDFLCEE-----------SRAHFEELKELLDALGI--PYKIDPSLVRGLDYYTG 260

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743144 174 VIYEAVLLESPAQagketlnvGSVAAGGRYDRLVAQFDpkGHSVPCVGLSIGVERIFYLVEQKMKISCEKvrtTETQVFV 253
Cdd:TIGR00442 261 TVFEFVTDDLGAQ--------GSICGGGRYDGLVEELG--GPPTPAVGFAIGIERLILLLEELGLIPPPS---KKPDVYV 327

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958743144 254 ATPQKNFLQERLKIIAQLWDAGIKAEMLYKNNpKLLTQLHYCEKEDIPLMVIIGEQEQNEGVVKLRSVASREEVTVNR 331
Cdd:TIGR00442 328 VPLGEEAELEALKLAQKLRKAGIRVEVDLGGR-KLKKQLKYADKLGARFALIIGEDELENGTVTLKDLETGEQETVPL 404
HisRS-like_core cd00773
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ...
 15-234 2.48e-45

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: 155.45  E-value: 2.48e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743144  15 DFDIAGEfDPMIPDAECLRIMCEILSGLQLGDFLIKVNDRRVVDGmfaVCGVPESKFRTICSSMDKLDKmswedvrlemv 94
Cdd:cd00773   109 GVEIIGS-DSPLADAEVIALAVEILEALGLKDFQIKINHRGILDG---IAGLLEDREEYIERLIDKLDK----------- 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743144  95 agkglapevadrigdyvqchggislveelfkdprlsqsqlalQGLGDLKLLFEYLRLFGIADKISLDLSLARGLDYYTGV 174
Cdd:cd00773   174 ------------------------------------------EALAHLEKLLDYLEALGVDIKYSIDLSLVRGLDYYTGI 211

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743144 175 IYEAVLLESPAQagketlnvGSVAAGGRYDRLVAQFDpkGHSVPCVGLSIGVERIFYLVE 234
Cdd:cd00773   212 VFEAVADGLGAQ--------GSIAGGGRYDGLLEEFG--GEDVPAVGFAIGLERLLLALE 261
PRK12420 PRK12420
histidyl-tRNA synthetase; Provisional
 15-329 5.61e-43

histidyl-tRNA synthetase; Provisional


Pssm-ID: 237097 [Multi-domain]  Cd Length: 423  Bit Score: 153.73  E-value: 5.61e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743144  15 DFDIAGEFDPMiPDAECLRIMCEILSGLQLgDFLIKVNDRRVVDGMFAVCGVPESKFRTICSSMDKLDKMSWEDVRLEmV 94
Cdd:PRK12420  126 DVDIVGVESVM-AEAELMSMAFELFRRLNL-EVTIQYNNRKLLNGILQAIGIPTELTSDVILSLDKIEKIGIDGVRKD-L 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743144  95 AGKGLAPEVADRIGDYVQCHGGISLveELFKDprLSQSQLALQGLGDLKLLFEYLRLFGIADKISLDLSLARGLDYYTGV 174
Cdd:PRK12420  203 LERGISEEMADTICNTVLSCLQLSI--ADFKE--AFNNPLVAEGVNELQQLQQYLIALGINENCIFNPFLARGLTMYTGT 278

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743144 175 IYEAVLlespaqagKETLNVGSVAAGGRYDRLVAQFDPKGHSVPCVGLSIGVERIFYLVEQKMKIScekvrtTETQVFVA 254
Cdd:PRK12420  279 VYEIFL--------KDGSITSSIGSGGRYDNIIGAFRGDDMNYPTVGISFGLDVIYTALSQKETIS------STADVFII 344

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958743144 255 TPQKNflQERLKIIAQLW-DAGIKAEMLYKNNpKLLTQLHYCEKEDIPLMVIIGEQEQNEGVVKLRSVASREEVTV 329
Cdd:PRK12420  345 PLGTE--LQCLQIAQQLRsTTGLKVELELAGR-KLKKALNYANKENIPYVLIIGEEEVSTGTVMLRNMKEGSEVKV 417
HisZ COG3705
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism];
28-229 1.44e-29

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


Pssm-ID: 442919 [Multi-domain]  Cd Length: 312  Bit Score: 115.27  E-value: 1.44e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743144  28 DAECLRIMCEILSGLQLGDFLIKVNDRRVVDGMFAVCGVPESKFRTICSSMDKLDKmswedVRLE-MVAGKGLAPEVADR 106
Cdd:COG3705   124 DAEVIALALEALKAAGLEDFTLDLGHVGLFRALLEALGLSEEQREELRRALARKDA-----VELEeLLAELGLSEELAEA 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743144 107 IGDYVQCHGGISLVEELFKdprLSQSQLALQGLGDLKLLFEYLRLFGIADKISLDLSLARGLDYYTGVIYEAVLlespAQ 186
Cdd:COG3705   199 LLALPELYGGEEVLARARA---LLLDAAIRAALDELEALAEALAARGPDVRLTFDLSELRGYDYYTGIVFEAYA----PG 271

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1958743144 187 AGKEtlnvgsVAAGGRYDRLVAQFdpkGHSVPCVGLSIGVERI 229
Cdd:COG3705   272 VGDP------LARGGRYDGLLAAF---GRARPATGFSLDLDRL 305
PLN02530 PLN02530
histidine-tRNA ligase
 28-334 4.27e-29

histidine-tRNA ligase


Pssm-ID: 178145 [Multi-domain]  Cd Length: 487  Bit Score: 116.77  E-value: 4.27e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743144  28 DAECLRIMCEILS--GLQLGDFLIKVNDRRVVDGMFAVCGVPESKFRTICSSMDKLDKMSWEDVRLEMvAGKGLAPEVAD 105
Cdd:PLN02530  203 EAELLAAIVTFFKrvGITSSDVGIKVSSRKVLQAVLKSYGIPEESFAPVCVIVDKLEKLPREEIEKEL-DTLGVSEEAIE 281

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743144 106 RIGDYVQCHGgISLVEELFKDprlsqsqlALQGLGDLKLLFEYLRLFGIADKISLDLSLARGLDYYTGVIYEAVllespA 185
Cdd:PLN02530  282 GILDVLSLKS-LDDLEALLGA--------DSEAVADLKQLFSLAEAYGYQDWLVFDASVVRGLAYYTGIVFEGF-----D 347

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743144 186 QAGKetlnVGSVAAGGRYDRLVAQFDpkGHSVPCVGLSIGVERIFYLVEQKmKISCEKVRTTETQVFvatPQKNFLQ-ER 264
Cdd:PLN02530  348 RAGK----LRAICGGGRYDRLLSTFG--GEDTPACGFGFGDAVIVELLKEK-GLLPELPHQVDDVVF---ALDEDLQgAA 417

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743144 265 LKIIAQLWDAGIKAEMLYKNNpKLLTQLHYCEKEDIPLMVIIGEQEQNEGVVKLRSVASREEVTVNRESL 334
Cdd:PLN02530  418 AGVASRLREKGRSVDLVLEPK-KLKWVFKHAERIGAKRLVLVGASEWERGMVRVKDLSSGEQTEVKLDEL 486
hisZ PRK12292
ATP phosphoribosyltransferase regulatory subunit; Provisional
 27-280 2.26e-27

ATP phosphoribosyltransferase regulatory subunit; Provisional


Pssm-ID: 237043 [Multi-domain]  Cd Length: 391  Bit Score: 110.73  E-value: 2.26e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743144  27 PDAECLRIMCEILSGLQLGDFLIKVNDRRVVDGMFAVCGVPESKFRTICSSMDKLDKmswedVRLEMVAgKGLAPEVADR 106
Cdd:PRK12292  136 ADAEVILLLLEALKALGLPNFTLDLGHVGLFRALLEAAGLSEELEEVLRRALANKDY-----VALEELV-LDLSEELRDA 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743144 107 IGDYVQCHGGISLVEELfkdPRLSQSQLALQGLGDLKLLFEYLRLFGIADKISLDLSLARGLDYYTGVIYEAVLLESPAq 186
Cdd:PRK12292  210 LLALPRLRGGREVLEEA---RKLLPSLPIKRALDELEALAEALEKYGYGIPLSLDLGLLRHLDYYTGIVFEGYVDGVGN- 285

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743144 187 agketlnvgSVAAGGRYDRLVAQFdpkGHSVPCVGLSIGVERIFYLVEQKmkiscekvRTTETQVFVATPQKNFLQERLK 266
Cdd:PRK12292  286 ---------PIASGGRYDDLLGRF---GRARPATGFSLDLDRLLELQLEL--------PVEARKDLVIAPDSEALAAALA 345

                         250
                  ....*....|....
gi 1958743144 267 IIAQLWDAGIKAEM 280
Cdd:PRK12292  346 AAQELRKKGEIVVL 359
HisRS_anticodon cd00859
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases ...
 248-339 3.09e-27

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: 102.62  E-value: 3.09e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743144 248 ETQVFVATPQKNFLQERLKIIAQLWDAGIKAEMLYKNnPKLLTQLHYCEKEDIPLMVIIGEQEQNEGVVKLRSVASREEV 327
Cdd:cd00859     1 EVDVYVVPLGEGALSEALELAEQLRDAGIKAEIDYGG-RKLKKQFKYADRSGARFAVILGEDELAAGVVTVKDLETGEQE 79

                          90
                  ....*....|..
gi 1958743144 328 TVNRESLVAEIQ 339
Cdd:cd00859    80 TVALDELVEELK 91
tRNA-synt_His pfam13393
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ...
 28-229 9.90e-27

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: 107.29  E-value: 9.90e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743144  28 DAECLRIMCEILSGLQLGDFLIKVNDRRVVDGMFAVCGVPESKFRTIcssMDKLDKMSWEDVRlEMVAGKGLAPEVADRI 107
Cdd:pfam13393 127 DAEIISLLLEALAAAGVPGVTLDLGHVGLVRALLEAAGLSEALEEAL---RAALQRKDAAELA-ELAAEAGLPPALRRAL 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743144 108 GDYVQCHGGISLVEELFKdpRLSQSQLALQGLGDLKLLFEYLRLFGIADKISLDLSLARGLDYYTGVIYEAVLlespAQA 187
Cdd:pfam13393 203 LALPDLYGGPEVLDEARA--ALPGLPALQEALDELEALAALLEALGDGVRLTFDLAELRGYEYYTGIVFAAYA----PGV 276

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1958743144 188 GKEtlnvgsVAAGGRYDRLVAQFdpkGHSVPCVGLSIGVERI 229
Cdd:pfam13393 277 GEP------LARGGRYDDLGAAF---GRARPATGFSLDLEAL 309
HGTP_anticodon pfam03129
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ...
 250-341 6.32e-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: 74.93  E-value: 6.32e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743144 250 QVFVATPQKN---FLQERLKIIAQLWDAGIKAEmLYKNNPKLLTQLHYCEKEDIPLMVIIGEQEQNEGVVKLRSVASREE 326
Cdd:pfam03129   1 QVVVIPLGEKaeeLEEYAQKLAEELRAAGIRVE-LDDRNESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQ 79

                          90
                  ....*....|....*
gi 1958743144 327 VTVNRESLVAEIQKR 341
Cdd:pfam03129  80 ETVSLDELVEKLKEL 94
syh CHL00201
histidine-tRNA synthetase; Provisional
 127-340 1.64e-13

histidine-tRNA synthetase; Provisional


Pssm-ID: 164576 [Multi-domain]  Cd Length: 430  Bit Score: 71.09  E-value: 1.64e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743144 127 PRLSQSqLALQGLGDLKLLFEYLRLFGIADKIslDLSLARGLDYYTGVIYEAVLLESPAQagketlnvGSVAAGGRYDRL 206
Cdd:CHL00201  222 PKISDF-LSLESTEHFYDVCTYLNLLNIPYKI--NYKLVRGLDYYNDTAFEIKTLSSNGQ--------DTICGGGRYDSL 290

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743144 207 VAQFDpkGHSVPCVGLSIGVERIFYLVEQKMKISCEKVrttetQVFVATPQKNFLQERLKIIAQLWDAGIKAEmLYKNNP 286
Cdd:CHL00201  291 IHQLG--GPKTPAVGCAIGLERLLLIAKDNIILPKQSI-----DVYIATQGLKAQKKGWEIIQFLEKQNIKFE-LDLSSS 362

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958743144 287 KLLTQLHYCEKEDIPLMVIIGEQEQNEGVVKLRSVASREEVTVNRESLVAEIQK 340
Cdd:CHL00201  363 NFHKQIKQAGKKRAKACIILGDNEIMDNCITIKWLDEQVQENAQYSNFKQEISY 416
hisZ PRK12295
ATP phosphoribosyltransferase regulatory subunit; Provisional
 95-229 4.38e-10

ATP phosphoribosyltransferase regulatory subunit; Provisional


Pssm-ID: 183413 [Multi-domain]  Cd Length: 373  Bit Score: 60.33  E-value: 4.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743144  95 AGKGLAPEVADRIGDY--VQCHGGISL--VEELFKDPRLSQSQlALQGLGDlkllfeylRLFGIA------DKISLDLSL 164
Cdd:PRK12295  242 AAARLPAEALAVLERFlaISGPPDAALaaLRALAADAGLDLDA-ALDRFEA--------RLAALAargidlERLRFSASF 312

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958743144 165 ARGLDYYTGVIYEaVLLESPAQAgketlnvgSVAAGGRYDRLVAQFDpKGHSVPCVGLSIGVERI 229
Cdd:PRK12295  313 GRPLDYYTGFVFE-IRAAGNGDP--------PLAGGGRYDGLLTRLG-AGEPIPAVGFSIWLDRL 367
HGTP_anticodon2 pfam12745
Anticodon binding domain of tRNAs; This is an HGTP_anticodon binding domain, found largely on ...
 251-341 3.89e-06

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: 47.60  E-value: 3.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743144 251 VFVATPQKNFL-QERLKIIAQLWDAGIKAEMLYKNNPKLLTQLHYCEKEDIPLMVIIGEQ----EQNEGVVKLRSVASRE 325
Cdd:pfam12745   8 VLVASFDASILrTTGVEILQELWAHGISADLAVDASYSPEDLVSRARDDGVSWIVIIKQQnkssDSKYKPLKVKNLLRKE 87

                          90       100
                  ....*....|....*....|
gi 1958743144 326 EVTVNRESLVA----EIQKR 341
Cdd:pfam12745  88 DVDLDSDELVSwlrgEIRER 107
PRK12421 PRK12421
ATP phosphoribosyltransferase regulatory subunit; Provisional
 92-229 2.22e-05

ATP phosphoribosyltransferase regulatory subunit; Provisional


Pssm-ID: 237098  Cd Length: 392  Bit Score: 45.73  E-value: 2.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743144  92 EMVAGKGLAPEVADRIGDYVQCHGGISLVEElfkdprlSQSQLALQG------LGDLKLLFEYLRLFGIADKISLDLSLA 165
Cdd:PRK12421  200 EVCQNLGVGSDLRRMFYALARLNGGLEALDR-------ALSVLALQDaairqaLDELKTLAAHLKNRWPELPVSIDLAEL 272

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958743144 166 RGLDYYTGVIYeAVLLESPAQAgketlnvgsVAAGGRYDRLVAQFdpkGHSVPCVGLSIGVERI 229
Cdd:PRK12421  273 RGYHYHTGLVF-AAYIPGRGQA---------LARGGRYDGIGEAF---GRARPATGFSMDLKEL 323
ProRS_anticodon_short cd00861
ProRS Prolyl-anticodon binding domain, short version found predominantly in bacteria. ProRS ...
 300-339 2.93e-04

ProRS Prolyl-anticodon binding domain, short version found predominantly in bacteria. ProRS 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: 238438 [Multi-domain]  Cd Length: 94  Bit Score: 39.50  E-value: 2.93e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1958743144 300 IPLMVIIGEQEQNEGVVKLRSVASREEVTVNRESLVAEIQ 339
Cdd:cd00861    55 IPYRIVVGKKSAAEGIVEIKVRKTGEKEEISIDELLEFLQ 94
ThrRS_anticodon cd00860
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases ...
 249-339 5.78e-04

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: 38.25  E-value: 5.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743144 249 TQVFVATPQKNFLQERLKIIAQLWDAGIKAEMLYKNNpKLLTQLHYCEKEDIPLMVIIGEQEQNEGVVKLRSVASREEVT 328
Cdd:cd00860     2 VQVVVIPVTDEHLDYAKEVAKKLSDAGIRVEVDLRNE-KLGKKIREAQLQKIPYILVVGDKEVETGTVSVRTRDGGDLGS 80

                          90
                  ....*....|.
gi 1958743144 329 VNRESLVAEIQ 339
Cdd:cd00860    81 MSLDEFIEKLK 91
 
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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