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Conserved domains on  [gi|119582425|gb|EAW62021|]
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histidyl-tRNA synthetase, isoform CRA_a [Homo sapiens]

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
 1-432 0e+00

Histidyl-tRNA synthetase


The actual alignment was detected with superfamily member PLN02972:

Pssm-ID: 215525 [Multi-domain]  Cd Length: 763  Bit Score: 565.67  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425   1 MAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGEDSKLIYDLKDQGGELLSLRYDLTVPFARYLAMNKLTNIKR 80
Cdd:PLN02972 341 MAIREKAFSIITSVFKRHGATALDTPVFELRETLMGKYGEDSKLIYDLADQGGELCSLRYDLTVPFARYVAMNGITSFKR 420

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425  81 YHIAKVYRRDNPamTRGRYREFYQCDFDIAGNFDPMIPDAECLKIMCEILSSLQIGDFLVKVNDRRILDGMFAICGVSDS 160
Cdd:PLN02972 421 YQIAKVYRRDNP--SKGRYREFYQCDFDIAGVYEPMGPDFEIIKVLTELLDELDIGTYEVKLNHRKLLDGMLEICGVPPE 498

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 161 KFRTICSSVDKLDKVSWEEVKNEMVGEKGLAPEVADRIGDYVQQHGG-VSLVEQLLQ-DPKLSQNKQALEGLGDLKLLFE 238
Cdd:PLN02972 499 KFRTICSSIDKLDKQSFEQVKKEMVEEKGLSNETADKIGNFVKERGPpLELLSKLRQeGSEFLGNASSRAALDELEIMFK 578

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 239 YLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLLQTPaqageeplgVGSVAAGGRYDGLVGMFDpkGRKVPCVGLSIGVE 318
Cdd:PLN02972 579 ALEKSKAIGKIVFDLSLARGLDYYTGVIYEAVFKGAQ---------VGSIAAGGRYDNLVGMFS--GKQVPAVGVSLGIE 647

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 319 RIFSIVEQRLEALEEKIRTTETQVLVASAQKKLLEERLKLVSELWDAGIKAEllYKKNPKLLNQLQYCEEAGIPLVAIIG 398
Cdd:PLN02972 648 RVFAIMEQQEEEKSQVIRPTETEVLVSIIGDDKLALAAELVSELWNAGIKAE--YKVSTRKAKHLKRAKESGIPWMVLVG 725

                        410       420       430
                 ....*....|....*....|....*....|....
gi 119582425 399 EQELKDGVIKLRSVTSREEVDVRREDLVEEIKRR 432
Cdd:PLN02972 726 EKELSKGFVKLKNLEAGVEEEVDRTCFVQELKAE 759
 
Name Accession Description Interval E-value
PLN02972 PLN02972
Histidyl-tRNA synthetase
 1-432 0e+00

Histidyl-tRNA synthetase


Pssm-ID: 215525 [Multi-domain]  Cd Length: 763  Bit Score: 565.67  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425   1 MAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGEDSKLIYDLKDQGGELLSLRYDLTVPFARYLAMNKLTNIKR 80
Cdd:PLN02972 341 MAIREKAFSIITSVFKRHGATALDTPVFELRETLMGKYGEDSKLIYDLADQGGELCSLRYDLTVPFARYVAMNGITSFKR 420

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425  81 YHIAKVYRRDNPamTRGRYREFYQCDFDIAGNFDPMIPDAECLKIMCEILSSLQIGDFLVKVNDRRILDGMFAICGVSDS 160
Cdd:PLN02972 421 YQIAKVYRRDNP--SKGRYREFYQCDFDIAGVYEPMGPDFEIIKVLTELLDELDIGTYEVKLNHRKLLDGMLEICGVPPE 498

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 161 KFRTICSSVDKLDKVSWEEVKNEMVGEKGLAPEVADRIGDYVQQHGG-VSLVEQLLQ-DPKLSQNKQALEGLGDLKLLFE 238
Cdd:PLN02972 499 KFRTICSSIDKLDKQSFEQVKKEMVEEKGLSNETADKIGNFVKERGPpLELLSKLRQeGSEFLGNASSRAALDELEIMFK 578

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 239 YLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLLQTPaqageeplgVGSVAAGGRYDGLVGMFDpkGRKVPCVGLSIGVE 318
Cdd:PLN02972 579 ALEKSKAIGKIVFDLSLARGLDYYTGVIYEAVFKGAQ---------VGSIAAGGRYDNLVGMFS--GKQVPAVGVSLGIE 647

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 319 RIFSIVEQRLEALEEKIRTTETQVLVASAQKKLLEERLKLVSELWDAGIKAEllYKKNPKLLNQLQYCEEAGIPLVAIIG 398
Cdd:PLN02972 648 RVFAIMEQQEEEKSQVIRPTETEVLVSIIGDDKLALAAELVSELWNAGIKAE--YKVSTRKAKHLKRAKESGIPWMVLVG 725

                        410       420       430
                 ....*....|....*....|....*....|....
gi 119582425 399 EQELKDGVIKLRSVTSREEVDVRREDLVEEIKRR 432
Cdd:PLN02972 726 EKELSKGFVKLKNLEAGVEEEVDRTCFVQELKAE 759
HisS COG0124
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ...
 1-432 2.99e-111

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: 333.63  E-value: 2.99e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425   1 MAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGED--SKLIYDLKDQGGELLSLRYDLTVPFARYLAMNKLTN- 77
Cdd:COG0124   18 SAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKIGEDivEKEMYTFEDRGGRSLTLRPEGTAPVARAVAEHGNELp 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425  78 --IKRYHIAKVYRRDNPAmtRGRYREFYQCDFDIAGNFDPMIpDAECLKIMCEILSSLQIGDFLVKVNDRrildgmfaic 155
Cdd:COG0124   98 fpFKLYYIGPVFRYERPQ--KGRYRQFHQFGVEVIGSDSPLA-DAEVIALAADLLKALGLKDFTLEINSR---------- 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 156 GVSDSKFRTICSSVDKLDKVSWEEVknemvgekgLAPEVADRI------------GDYVQqhggvSLVEQLlqdPKLSQN 223
Cdd:COG0124  165 GLPEERAEALLRYLDKLDKIGHEDV---------LDEDSQRRLetnplraildskGPDCQ-----EVLADA---PKLLDY 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 224 KqALEGLGDLKLLFEYLTLFGIDdkISFDLSLARGLDYYTGVIYEAVLLQTPAQageeplgvGSVAAGGRYDGLVGMFDp 303
Cdd:COG0124  228 L-GEEGLAHFEEVLELLDALGIP--YVIDPRLVRGLDYYTGTVFEIVTDGLGAQ--------GSVCGGGRYDGLVEQLG- 295

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 304 kGRKVPCVGLSIGVERIFSIVEQRLEALEEKirtTETQVLVASAQKKLLEERLKLVSELWDAGIKAEL-LYKKNPKllNQ 382
Cdd:COG0124  296 -GPPTPAVGFAIGLERLLLLLEELGLLPAAE---PPPDVYVVPLGEEARAEALKLAQELRAAGIRVELdLGGRKLK--KQ 369

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 119582425 383 LQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVDVRREDLVEEIKRR 432
Cdd:COG0124  370 LKYADKSGAPFVLILGEDELANGTVTLKDLATGEQETVPLDELVEYLKEL 419
HisRS-like_core cd00773
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ...
 1-325 2.40e-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: 310.30  E-value: 2.40e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425   1 MAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGED-SKLIYDLKDQGGELLSLRYDLTVPFARYLAMNKL---T 76
Cdd:cd00773    2 AALRRYIEDTLREVFERYGYEEIDTPVFEYTELFLRKSGDEvSKEMYRFKDKGGRDLALRPDLTAPVARAVAENLLslpL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425  77 NIKRYHIAKVYRRDNPAmtRGRYREFYQCDFDIAGnFDPMIPDAECLKIMCEILSSLQIGDFLVKVNDRRILDGmfaICG 156
Cdd:cd00773   82 PLKLYYIGPVFRYERPQ--KGRYREFYQVGVEIIG-SDSPLADAEVIALAVEILEALGLKDFQIKINHRGILDG---IAG 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 157 VSDSKFRTICSSVDKLDKvsweevknemvgekglapevadrigdyvqqhggvslveqllqdpklsqnkqalEGLGDLKLL 236
Cdd:cd00773  156 LLEDREEYIERLIDKLDK-----------------------------------------------------EALAHLEKL 182

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 237 FEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLLQTPAQageeplgvGSVAAGGRYDGLVGMFDpkGRKVPCVGLSIG 316
Cdd:cd00773  183 LDYLEALGVDIKYSIDLSLVRGLDYYTGIVFEAVADGLGAQ--------GSIAGGGRYDGLLEEFG--GEDVPAVGFAIG 252


                 ....*....
gi 119582425 317 VERIFSIVE 325
Cdd:cd00773  253 LERLLLALE 261
hisS TIGR00442
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ...
 1-420 3.53e-97

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: 297.08  E-value: 3.53e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425    1 MAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGEDS----KLIYDLKDQGGELLSLRYDLTVPFARYLAMNKLT 76
Cdd:TIGR00442  14 MIKWQYIEETIREVFERYGFKEIRTPIFEYTELFKRKVGEETdivsKEMYTFKDKGGRSLTLRPEGTAPVARAVIENKLL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425   77 N---IKRYHIAKVYRRDNPAmtRGRYREFYQCDFDIAGNFDPMIpDAECLKIMCEILSSLQIGDFLVKVNDRRILDGMFA 153
Cdd:TIGR00442  94 LpkpFKLYYIGPMFRYERPQ--KGRYRQFHQFGVEVIGSDSPLA-DAEIIALAADILKELGLKDFTLEINSLGILEGRLE 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425  154 icgvsdsKFRTICSSVDK-LDKVSWEEVKNEMVGEKGLAPEVADRIGDYVQQhggvslveqllqDPKLSQNKQAlEGLGD 232
Cdd:TIGR00442 171 -------YREALIRYLDKhKDKLGEDSVRRLEKNPLRILDSKNEKIQELLKN------------APKILDFLCE-ESRAH 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425  233 LKLLFEYLTLFGIddKISFDLSLARGLDYYTGVIYEAVLLQTPAQageeplgvGSVAAGGRYDGLVGMFDpkGRKVPCVG 312
Cdd:TIGR00442 231 FEELKELLDALGI--PYKIDPSLVRGLDYYTGTVFEFVTDDLGAQ--------GSICGGGRYDGLVEELG--GPPTPAVG 298

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425  313 LSIGVERIFSIVEQRLEALEEKirtTETQVLVASAQKKLLEERLKLVSELWDAGIKAElLYKKNPKLLNQLQYCEEAGIP 392
Cdd:TIGR00442 299 FAIGIERLILLLEELGLIPPPS---KKPDVYVVPLGEEAELEALKLAQKLRKAGIRVE-VDLGGRKLKKQLKYADKLGAR 374

                         410       420
                  ....*....|....*....|....*...
gi 119582425  393 LVAIIGEQELKDGVIKLRSVTSREEVDV 420
Cdd:TIGR00442 375 FALIIGEDELENGTVTLKDLETGEQETV 402
tRNA-synt_His pfam13393
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ...
 2-320 3.39e-42

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: 151.20  E-value: 3.39e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425    2 AVREKVFDViircFKRHGAEVIDTPVFELKETLMGKYGEDSKLIYDLKDQGGELLSLRYDLTVPFARYLAmnKLTNIKR- 80
Cdd:pfam13393  15 ELRRRLLDL----FRSWGYELVMPPLLEYLDSLLTGTGADLDQTFKLVDQSGRLLGLRADITPQVARIDA--HRLNRPGp 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425   81 ---YHIAKVYRRDNPAMtrGRYREFYQCDFDIAGNFDPMiPDAECLKIMCEILSSLQIGDFLVKVNDRRILDGMFAICGV 157
Cdd:pfam13393  89 lrlCYAGSVLRTRPKGL--GRSREPLQVGAELIGHAGIE-ADAEIISLLLEALAAAGVPGVTLDLGHVGLVRALLEAAGL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425  158 SDSKFRTICSSVDKLDkvsWEEVKnEMVGEKGLAPEVADRIGDYVQQHGGVSLVEQLLQDpkLSQNKQALEGLGDLKLLF 237
Cdd:pfam13393 166 SEALEEALRAALQRKD---AAELA-ELAAEAGLPPALRRALLALPDLYGGPEVLDEARAA--LPGLPALQEALDELEALA 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425  238 EYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLlqtpAQAGEEplgvgsVAAGGRYDGLVGMFdpkGRKVPCVGLSIGV 317
Cdd:pfam13393 240 ALLEALGDGVRLTFDLAELRGYEYYTGIVFAAYA----PGVGEP------LARGGRYDDLGAAF---GRARPATGFSLDL 306


                  ...
gi 119582425  318 ERI 320
Cdd:pfam13393 307 EAL 309
 
Name Accession Description Interval E-value
PLN02972 PLN02972
Histidyl-tRNA synthetase
 1-432 0e+00

Histidyl-tRNA synthetase


Pssm-ID: 215525 [Multi-domain]  Cd Length: 763  Bit Score: 565.67  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425   1 MAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGEDSKLIYDLKDQGGELLSLRYDLTVPFARYLAMNKLTNIKR 80
Cdd:PLN02972 341 MAIREKAFSIITSVFKRHGATALDTPVFELRETLMGKYGEDSKLIYDLADQGGELCSLRYDLTVPFARYVAMNGITSFKR 420

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425  81 YHIAKVYRRDNPamTRGRYREFYQCDFDIAGNFDPMIPDAECLKIMCEILSSLQIGDFLVKVNDRRILDGMFAICGVSDS 160
Cdd:PLN02972 421 YQIAKVYRRDNP--SKGRYREFYQCDFDIAGVYEPMGPDFEIIKVLTELLDELDIGTYEVKLNHRKLLDGMLEICGVPPE 498

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 161 KFRTICSSVDKLDKVSWEEVKNEMVGEKGLAPEVADRIGDYVQQHGG-VSLVEQLLQ-DPKLSQNKQALEGLGDLKLLFE 238
Cdd:PLN02972 499 KFRTICSSIDKLDKQSFEQVKKEMVEEKGLSNETADKIGNFVKERGPpLELLSKLRQeGSEFLGNASSRAALDELEIMFK 578

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 239 YLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLLQTPaqageeplgVGSVAAGGRYDGLVGMFDpkGRKVPCVGLSIGVE 318
Cdd:PLN02972 579 ALEKSKAIGKIVFDLSLARGLDYYTGVIYEAVFKGAQ---------VGSIAAGGRYDNLVGMFS--GKQVPAVGVSLGIE 647

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 319 RIFSIVEQRLEALEEKIRTTETQVLVASAQKKLLEERLKLVSELWDAGIKAEllYKKNPKLLNQLQYCEEAGIPLVAIIG 398
Cdd:PLN02972 648 RVFAIMEQQEEEKSQVIRPTETEVLVSIIGDDKLALAAELVSELWNAGIKAE--YKVSTRKAKHLKRAKESGIPWMVLVG 725

                        410       420       430
                 ....*....|....*....|....*....|....
gi 119582425 399 EQELKDGVIKLRSVTSREEVDVRREDLVEEIKRR 432
Cdd:PLN02972 726 EKELSKGFVKLKNLEAGVEEEVDRTCFVQELKAE 759
HisS COG0124
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ...
 1-432 2.99e-111

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: 333.63  E-value: 2.99e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425   1 MAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGED--SKLIYDLKDQGGELLSLRYDLTVPFARYLAMNKLTN- 77
Cdd:COG0124   18 SAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKIGEDivEKEMYTFEDRGGRSLTLRPEGTAPVARAVAEHGNELp 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425  78 --IKRYHIAKVYRRDNPAmtRGRYREFYQCDFDIAGNFDPMIpDAECLKIMCEILSSLQIGDFLVKVNDRrildgmfaic 155
Cdd:COG0124   98 fpFKLYYIGPVFRYERPQ--KGRYRQFHQFGVEVIGSDSPLA-DAEVIALAADLLKALGLKDFTLEINSR---------- 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 156 GVSDSKFRTICSSVDKLDKVSWEEVknemvgekgLAPEVADRI------------GDYVQqhggvSLVEQLlqdPKLSQN 223
Cdd:COG0124  165 GLPEERAEALLRYLDKLDKIGHEDV---------LDEDSQRRLetnplraildskGPDCQ-----EVLADA---PKLLDY 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 224 KqALEGLGDLKLLFEYLTLFGIDdkISFDLSLARGLDYYTGVIYEAVLLQTPAQageeplgvGSVAAGGRYDGLVGMFDp 303
Cdd:COG0124  228 L-GEEGLAHFEEVLELLDALGIP--YVIDPRLVRGLDYYTGTVFEIVTDGLGAQ--------GSVCGGGRYDGLVEQLG- 295

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 304 kGRKVPCVGLSIGVERIFSIVEQRLEALEEKirtTETQVLVASAQKKLLEERLKLVSELWDAGIKAEL-LYKKNPKllNQ 382
Cdd:COG0124  296 -GPPTPAVGFAIGLERLLLLLEELGLLPAAE---PPPDVYVVPLGEEARAEALKLAQELRAAGIRVELdLGGRKLK--KQ 369

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 119582425 383 LQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVDVRREDLVEEIKRR 432
Cdd:COG0124  370 LKYADKSGAPFVLILGEDELANGTVTLKDLATGEQETVPLDELVEYLKEL 419
HisRS-like_core cd00773
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ...
 1-325 2.40e-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: 310.30  E-value: 2.40e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425   1 MAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGED-SKLIYDLKDQGGELLSLRYDLTVPFARYLAMNKL---T 76
Cdd:cd00773    2 AALRRYIEDTLREVFERYGYEEIDTPVFEYTELFLRKSGDEvSKEMYRFKDKGGRDLALRPDLTAPVARAVAENLLslpL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425  77 NIKRYHIAKVYRRDNPAmtRGRYREFYQCDFDIAGnFDPMIPDAECLKIMCEILSSLQIGDFLVKVNDRRILDGmfaICG 156
Cdd:cd00773   82 PLKLYYIGPVFRYERPQ--KGRYREFYQVGVEIIG-SDSPLADAEVIALAVEILEALGLKDFQIKINHRGILDG---IAG 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 157 VSDSKFRTICSSVDKLDKvsweevknemvgekglapevadrigdyvqqhggvslveqllqdpklsqnkqalEGLGDLKLL 236
Cdd:cd00773  156 LLEDREEYIERLIDKLDK-----------------------------------------------------EALAHLEKL 182

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 237 FEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLLQTPAQageeplgvGSVAAGGRYDGLVGMFDpkGRKVPCVGLSIG 316
Cdd:cd00773  183 LDYLEALGVDIKYSIDLSLVRGLDYYTGIVFEAVADGLGAQ--------GSIAGGGRYDGLLEEFG--GEDVPAVGFAIG 252


                 ....*....
gi 119582425 317 VERIFSIVE 325
Cdd:cd00773  253 LERLLLALE 261
hisS TIGR00442
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ...
 1-420 3.53e-97

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: 297.08  E-value: 3.53e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425    1 MAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGEDS----KLIYDLKDQGGELLSLRYDLTVPFARYLAMNKLT 76
Cdd:TIGR00442  14 MIKWQYIEETIREVFERYGFKEIRTPIFEYTELFKRKVGEETdivsKEMYTFKDKGGRSLTLRPEGTAPVARAVIENKLL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425   77 N---IKRYHIAKVYRRDNPAmtRGRYREFYQCDFDIAGNFDPMIpDAECLKIMCEILSSLQIGDFLVKVNDRRILDGMFA 153
Cdd:TIGR00442  94 LpkpFKLYYIGPMFRYERPQ--KGRYRQFHQFGVEVIGSDSPLA-DAEIIALAADILKELGLKDFTLEINSLGILEGRLE 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425  154 icgvsdsKFRTICSSVDK-LDKVSWEEVKNEMVGEKGLAPEVADRIGDYVQQhggvslveqllqDPKLSQNKQAlEGLGD 232
Cdd:TIGR00442 171 -------YREALIRYLDKhKDKLGEDSVRRLEKNPLRILDSKNEKIQELLKN------------APKILDFLCE-ESRAH 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425  233 LKLLFEYLTLFGIddKISFDLSLARGLDYYTGVIYEAVLLQTPAQageeplgvGSVAAGGRYDGLVGMFDpkGRKVPCVG 312
Cdd:TIGR00442 231 FEELKELLDALGI--PYKIDPSLVRGLDYYTGTVFEFVTDDLGAQ--------GSICGGGRYDGLVEELG--GPPTPAVG 298

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425  313 LSIGVERIFSIVEQRLEALEEKirtTETQVLVASAQKKLLEERLKLVSELWDAGIKAElLYKKNPKLLNQLQYCEEAGIP 392
Cdd:TIGR00442 299 FAIGIERLILLLEELGLIPPPS---KKPDVYVVPLGEEAELEALKLAQKLRKAGIRVE-VDLGGRKLKKQLKYADKLGAR 374

                         410       420
                  ....*....|....*....|....*...
gi 119582425  393 LVAIIGEQELKDGVIKLRSVTSREEVDV 420
Cdd:TIGR00442 375 FALIIGEDELENGTVTLKDLETGEQETV 402
PRK12420 PRK12420
histidyl-tRNA synthetase; Provisional
 2-420 2.71e-77

histidyl-tRNA synthetase; Provisional


Pssm-ID: 237097 [Multi-domain]  Cd Length: 423  Bit Score: 246.57  E-value: 2.71e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425   2 AVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYG---EDSKLIYDLKDQGGELLSLRYDLTVPFARYLAMNKltNI 78
Cdd:PRK12420  19 VLRNKIKRALEDVFERYGCKPLETPTLNMYELMSSKYGggdEILKEIYTLTDQGKRDLALRYDLTIPFAKVVAMNP--NI 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425  79 ----KRYHIAKVYrRDNPaMTRGRYREFYQCDFDIAGNFDPMiPDAECLKIMCEILSSLQIgDFLVKVNDRRILDGMFAI 154
Cdd:PRK12420  97 rlpfKRYEIGKVF-RDGP-IKQGRFREFIQCDVDIVGVESVM-AEAELMSMAFELFRRLNL-EVTIQYNNRKLLNGILQA 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 155 CGVSDSKFRTICSSVDKLDKVSWEEVKNEMVgEKGLAPEVADRIGDYVQQHGGVSLVEQllqdPKLSQNKQALEGLGDLK 234
Cdd:PRK12420 173 IGIPTELTSDVILSLDKIEKIGIDGVRKDLL-ERGISEEMADTICNTVLSCLQLSIADF----KEAFNNPLVAEGVNELQ 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 235 LLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEaVLLQTPAQAgeeplgvGSVAAGGRYDGLVGMFDPKGRKVPCVGLS 314
Cdd:PRK12420 248 QLQQYLIALGINENCIFNPFLARGLTMYTGTVYE-IFLKDGSIT-------SSIGSGGRYDNIIGAFRGDDMNYPTVGIS 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 315 IGVERIfsiveqrLEALEEKIRTTET-QVLVASAQKKLleERLKLVSELW-DAGIKAELLYkKNPKLLNQLQYCEEAGIP 392
Cdd:PRK12420 320 FGLDVI-------YTALSQKETISSTaDVFIIPLGTEL--QCLQIAQQLRsTTGLKVELEL-AGRKLKKALNYANKENIP 389

                        410       420
                 ....*....|....*....|....*...
gi 119582425 393 LVAIIGEQELKDGVIKLRSVTSREEVDV 420
Cdd:PRK12420 390 YVLIIGEEEVSTGTVMLRNMKEGSEVKV 417
HisZ COG3705
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism];
2-320 3.74e-49

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


Pssm-ID: 442919 [Multi-domain]  Cd Length: 312  Bit Score: 169.59  E-value: 3.74e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425   2 AVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGEDSKL-IYDLKDQGGELLSLRYDLTVPFARYLAmNKLTNIKR 80
Cdd:COG3705    6 ARKEELRRRLLDVFRSWGYELVEPPLLEYLDSLLTGSGADLDLqTFKLVDQLGRTLGLRPDMTPQVARIAA-TRLANRPG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425  81 ----YHIAKVYRrdNPAMTRGRYREFYQC------DFDIAGnfdpmipDAECLKIMCEILSSLQIGDFLVKVNDRRILDG 150
Cdd:COG3705   85 plrlCYAGNVFR--TRPSGLGRSREFLQAgaeligHAGLEA-------DAEVIALALEALKAAGLEDFTLDLGHVGLFRA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 151 MFAICGVSDSKFRTICSSVDKLDKVsweEVKnEMVGEKGLAPEVADRIGDYVQQHGGVSLVEQLLqdpKLSQNKQALEGL 230
Cdd:COG3705  156 LLEALGLSEEQREELRRALARKDAV---ELE-ELLAELGLSEELAEALLALPELYGGEEVLARAR---ALLLDAAIRAAL 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 231 GDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLlqtpAQAGEEplgvgsVAAGGRYDGLVGMFdpkGRKVPC 310
Cdd:COG3705  229 DELEALAEALAARGPDVRLTFDLSELRGYDYYTGIVFEAYA----PGVGDP------LARGGRYDGLLAAF---GRARPA 295

                        330
                 ....*....|
gi 119582425 311 VGLSIGVERI 320
Cdd:COG3705  296 TGFSLDLDRL 305
hisZ_biosyn_reg TIGR00443
ATP phosphoribosyltransferase, regulatory subunit; Apparant second copies of histidyl-tRNA ...
 2-320 5.42e-47

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: 163.94  E-value: 5.42e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425    2 AVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGEDSKLIYDLKDQGGELLSLRYDLTVPFARyLAMNKLTNIKR- 80
Cdd:TIGR00443   9 ARKEEIERQLQDVFRSWGYQEIITPTLEYLDTLSAGSGILNEDLFKLFDQLGRVLGLRPDMTAPIAR-LVSTRLRDRPLp 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425   81 ---YHIAKVYRRDNPAmtRGRYREFYQCDFDIAGNfDPMIPDAECLKIMCEILSSLQIGDFLVKVNDRRILDGMFAICGV 157
Cdd:TIGR00443  88 lrlCYAGNVFRTNESG--GGRSREFTQAGVELIGA-GGPAADAEVIALLIEALKALGLKDFKIELGHVGLVRALLEEAGL 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425  158 SDSKFRTICSSVDKLDKVSWEEVknemVGEKGLAPEVADRIGDYVQQHGGVSLVEQLLQdpKLSQNKQALEGLGDLKLLF 237
Cdd:TIGR00443 165 PEEAREALREALARKDLVALEEL----VAELGLSPEVRERLLALPRLRGDGEEVLEEAR--ALAGSETAEAALDELEAVL 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425  238 EYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLLQTPAQageeplgvgsVAAGGRYDGLVGMFdpkGRKVPCVGLSIGV 317
Cdd:TIGR00443 239 ELLEARGVEEYISLDLGLVRGYHYYTGLIFEGYAPGLGAP----------LAGGGRYDELLGRF---GRPLPATGFALNL 305


                  ...
gi 119582425  318 ERI 320
Cdd:TIGR00443 306 ERL 308
PLN02530 PLN02530
histidine-tRNA ligase
 1-425 9.52e-45

histidine-tRNA ligase


Pssm-ID: 178145 [Multi-domain]  Cd Length: 487  Bit Score: 162.60  E-value: 9.52e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425   1 MAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGED-SKLIYDLKDQGGELLSLRYDLTVPFARyLAMNKLTNI- 78
Cdd:PLN02530  84 MRLRNWLFDHFREVSRLFGFEEVDAPVLESEELYIRKAGEEiTDQLYNFEDKGGRRVALRPELTPSLAR-LVLQKGKSLs 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425  79 ---KRYHIAKVYRRDNpaMTRGRYREFYQCDFDIAGnFDPMIPDAECLKIMCEILSSLQI--GDFLVKVNDRRILDGMFA 153
Cdd:PLN02530 163 lplKWFAIGQCWRYER--MTRGRRREHYQWNMDIIG-VPGVEAEAELLAAIVTFFKRVGItsSDVGIKVSSRKVLQAVLK 239

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 154 ICGVSDSKFRTICSSVDKLDKVSWEEVKNEMvGEKGLAPEVADRIGDyVQQHGGVSLVEQLLqdpklsqnKQALEGLGDL 233
Cdd:PLN02530 240 SYGIPEESFAPVCVIVDKLEKLPREEIEKEL-DTLGVSEEAIEGILD-VLSLKSLDDLEALL--------GADSEAVADL 309

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 234 KLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVllqtpAQAGEeplgVGSVAAGGRYDGLVGMFDpkGRKVPCVGL 313
Cdd:PLN02530 310 KQLFSLAEAYGYQDWLVFDASVVRGLAYYTGIVFEGF-----DRAGK----LRAICGGGRYDRLLSTFG--GEDTPACGF 378

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 314 SIGVERIFSIVEQRlEALEEKIRTTETqvLVASAQKKLLEERLKLVSELWDAGIKAEL-LYKKNPKLLnqLQYCEEAGIP 392
Cdd:PLN02530 379 GFGDAVIVELLKEK-GLLPELPHQVDD--VVFALDEDLQGAAAGVASRLREKGRSVDLvLEPKKLKWV--FKHAERIGAK 453

                        410       420       430
                 ....*....|....*....|....*....|...
gi 119582425 393 LVAIIGEQELKDGVIKLRSVTSREEVDVRREDL 425
Cdd:PLN02530 454 RLVLVGASEWERGMVRVKDLSSGEQTEVKLDEL 486
hisZ PRK12292
ATP phosphoribosyltransferase regulatory subunit; Provisional
 4-371 2.45e-43

ATP phosphoribosyltransferase regulatory subunit; Provisional


Pssm-ID: 237043 [Multi-domain]  Cd Length: 391  Bit Score: 156.56  E-value: 2.45e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425   4 REKVFDVIIRCFKRHGAEVIDTPVFELKETLM--GKYGEDSKLIYDLKDQGGELLSLRYDLTVPFARyLAMNKLTNIKR- 80
Cdd:PRK12292  20 IEEIRRRLLDLFRRWGYEEVITPTLEYLDTLLagGGAILDLRTFKLVDQLSGRTLGLRPDMTAQIAR-IAATRLANRPGp 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425  81 ---YHIAKVYRrdNPAMTRGRYREFYQCDFDIAGnFDPMIPDAECLKIMCEILSSLQIGDFLVKVNDRRILDGMFAICGV 157
Cdd:PRK12292  99 lrlCYAGNVFR--AQERGLGRSREFLQSGVELIG-DAGLEADAEVILLLLEALKALGLPNFTLDLGHVGLFRALLEAAGL 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 158 SDSKFRTICSSVDKLDKVSWEEVknemvgEKGLAPEVADRIGDYVQQHGGVSLVEQLLQdpkLSQNKQALEGLGDLKLLF 237
Cdd:PRK12292 176 SEELEEVLRRALANKDYVALEEL------VLDLSEELRDALLALPRLRGGREVLEEARK---LLPSLPIKRALDELEALA 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 238 EYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLLQTPAqageeplgvgSVAAGGRYDGLVGMFdpkGRKVPCVGLSIGV 317
Cdd:PRK12292 247 EALEKYGYGIPLSLDLGLLRHLDYYTGIVFEGYVDGVGN----------PIASGGRYDDLLGRF---GRARPATGFSLDL 313

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 119582425 318 ERIfsiveqrLEALEEKiRTTETQVLVASAQKKLLEERLKLVSELWDAGIKAEL 371
Cdd:PRK12292 314 DRL-------LELQLEL-PVEARKDLVIAPDSEALAAALAAAQELRKKGEIVVL 359
tRNA-synt_His pfam13393
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ...
 2-320 3.39e-42

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: 151.20  E-value: 3.39e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425    2 AVREKVFDViircFKRHGAEVIDTPVFELKETLMGKYGEDSKLIYDLKDQGGELLSLRYDLTVPFARYLAmnKLTNIKR- 80
Cdd:pfam13393  15 ELRRRLLDL----FRSWGYELVMPPLLEYLDSLLTGTGADLDQTFKLVDQSGRLLGLRADITPQVARIDA--HRLNRPGp 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425   81 ---YHIAKVYRRDNPAMtrGRYREFYQCDFDIAGNFDPMiPDAECLKIMCEILSSLQIGDFLVKVNDRRILDGMFAICGV 157
Cdd:pfam13393  89 lrlCYAGSVLRTRPKGL--GRSREPLQVGAELIGHAGIE-ADAEIISLLLEALAAAGVPGVTLDLGHVGLVRALLEAAGL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425  158 SDSKFRTICSSVDKLDkvsWEEVKnEMVGEKGLAPEVADRIGDYVQQHGGVSLVEQLLQDpkLSQNKQALEGLGDLKLLF 237
Cdd:pfam13393 166 SEALEEALRAALQRKD---AAELA-ELAAEAGLPPALRRALLALPDLYGGPEVLDEARAA--LPGLPALQEALDELEALA 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425  238 EYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLlqtpAQAGEEplgvgsVAAGGRYDGLVGMFdpkGRKVPCVGLSIGV 317
Cdd:pfam13393 240 ALLEALGDGVRLTFDLAELRGYEYYTGIVFAAYA----PGVGEP------LARGGRYDDLGAAF---GRARPATGFSLDL 306


                  ...
gi 119582425  318 ERI 320
Cdd:pfam13393 307 EAL 309
HisRS_anticodon cd00859
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases ...
 339-430 2.30e-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: 109.94  E-value: 2.30e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 339 ETQVLVASAQKKLLEERLKLVSELWDAGIKAELLYKkNPKLLNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEV 418
Cdd:cd00859    1 EVDVYVVPLGEGALSEALELAEQLRDAGIKAEIDYG-GRKLKKQFKYADRSGARFAVILGEDELAAGVVTVKDLETGEQE 79

                         90
                 ....*....|..
gi 119582425 419 DVRREDLVEEIK 430
Cdd:cd00859   80 TVALDELVEELK 91
syh CHL00201
histidine-tRNA synthetase; Provisional
 7-429 5.51e-26

histidine-tRNA synthetase; Provisional


Pssm-ID: 164576 [Multi-domain]  Cd Length: 430  Bit Score: 109.22  E-value: 5.51e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425   7 VFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGEDSKLI----YDLKDQGGELLSLRYDLTVPFARYLAMNKLT---NIK 79
Cdd:CHL00201  24 IHDKALTLLSLANYSEIRTPIFENSSLYDRGIGETTDIVnkemYRFTDRSNRDITLRPEGTAGIVRAFIENKMDyhsNLQ 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425  80 R-YHIAKVYRRDNPamTRGRYREFYQCDFDIAGNFDPMiPDAECLKIMCEILSSLQIGDFLVKVN------DRRILDgmf 152
Cdd:CHL00201 104 RlWYSGPMFRYERP--QSGRQRQFHQLGIEFIGSIDAR-ADTEVIHLAMQIFNELQVKNLILDINsigkleDRQSYQ--- 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 153 aicgvsdSKFRTICSSV-DKLDKVSweevKNEMVGEkglaP-EVADRIGDYVQqhggvslvEQLLQDPKLSQ--NKQALE 228
Cdd:CHL00201 178 -------LKLVEYLSQYqDDLDTDS----QNRLYSN----PiRILDSKNLKTQ--------EILDGAPKISDflSLESTE 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 229 GLGDLkllFEYLTLFGIDDKISFdlSLARGLDYYTGVIYEAVLLQTPAQageeplgvGSVAAGGRYDGLVGMFDpkGRKV 308
Cdd:CHL00201 235 HFYDV---CTYLNLLNIPYKINY--KLVRGLDYYNDTAFEIKTLSSNGQ--------DTICGGGRYDSLIHQLG--GPKT 299

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 309 PCVGLSIGVERIFSIVEQRLEALEEKIrttetQVLVASAQKKLLEERLKLVSELWDAGIKAELLYkKNPKLLNQLQYCEE 388
Cdd:CHL00201 300 PAVGCAIGLERLLLIAKDNIILPKQSI-----DVYIATQGLKAQKKGWEIIQFLEKQNIKFELDL-SSSNFHKQIKQAGK 373

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 119582425 389 AGIPLVAIIGEQELKDGVIKLRSVTSREEVDVRREDLVEEI 429
Cdd:CHL00201 374 KRAKACIILGDNEIMDNCITIKWLDEQVQENAQYSNFKQEI 414
hisZ PRK12295
ATP phosphoribosyltransferase regulatory subunit; Provisional
 1-320 7.59e-23

ATP phosphoribosyltransferase regulatory subunit; Provisional


Pssm-ID: 183413 [Multi-domain]  Cd Length: 373  Bit Score: 99.24  E-value: 7.59e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425   1 MAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGED-SKLIYDLKDQGGELLSLRYDLTVPFAR-YLAMNKLTNI 78
Cdd:PRK12295   4 LSASAAAAEALLASFEAAGAVRVDPPILQPAEPFLDLSGEDiRRRIFVTSDENGEELCLRPDFTIPVCRrHIATAGGEPA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425  79 KRYHIAKVYRRdnpamTRGRYREFYQCDFDIAGNFDPMIPDAECLKIMCEILSSLQIGDFLVKVNDRRILDGMFAICGVS 158
Cdd:PRK12295  84 RYAYLGEVFRQ-----RRDRASEFLQAGIESFGRADPAAADAEVLALALEALAALGPGDLEVRLGDVGLFAALVDALGLP 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 159 DS-KFRTIcssVDKLDKVSWEEVKNEMVGEKGLAPEVADRIGDYVQQHGGVS-LVEQLLQDPKLSQN------------- 223
Cdd:PRK12295 159 PGwKRRLL---RHFGRPRSLDALLARLAGPRVDPLDEHAGVLAALADEAAARaLVEDLMSIAGISPVggrspaeiarrll 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 224 -----------------------------KQALEGL----GDLKL-------LFE----YLTLFGID-DKISFDLSLARG 258
Cdd:PRK12295 236 ekaalaaaarlpaealavlerflaisgppDAALAALralaADAGLdldaaldRFEarlaALAARGIDlERLRFSASFGRP 315

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119582425 259 LDYYTGVIYEAvllqTPAQAGEEPLgvgsvAAGGRYDGLVGMFDpKGRKVPCVGLSIGVERI 320
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 ...
 341-432 9.86e-18

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: 78.01  E-value: 9.86e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425  341 QVLVASAQKK---LLEERLKLVSELWDAGIKAELLYKkNPKLLNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREE 417
Cdd:pfam03129   1 QVVVIPLGEKaeeLEEYAQKLAEELRAAGIRVELDDR-NESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQ 79

                          90
                  ....*....|....*
gi 119582425  418 VDVRREDLVEEIKRR 432
Cdd:pfam03129  80 ETVSLDELVEKLKEL 94
PRK12421 PRK12421
ATP phosphoribosyltransferase regulatory subunit; Provisional
 2-366 7.63e-10

ATP phosphoribosyltransferase regulatory subunit; Provisional


Pssm-ID: 237098  Cd Length: 392  Bit Score: 60.37  E-value: 7.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425   2 AVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGEDSKL-IYDLKDQ-GGELLSLRYDLTVPFARYLA-MNKLTNI 78
Cdd:PRK12421  22 QKIERLRRRLLDLFASRGYQLVMPPLIEYLESLLTGAGQDLKLqTFKLIDQlSGRLMGVRADITPQVARIDAhLLNREGV 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425  79 KRY-HIAKVY--RRDNPAMTRGRYR---EFYQCDfDIAGnfdpmipDAECLKIMCEILSSLQIGDFLVKVNDRRILDGMF 152
Cdd:PRK12421 102 ARLcYAGSVLhtLPQGLFGSRTPLQlgaELYGHA-GIEA-------DLEIIRLMLGLLRNAGVPALHLDLGHVGIFRRLA 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 153 AICGVSDSKFRTIcssVDKLDKVSWEEVKnEMVGEKGLAPEVADRIGDYVQQHGGVSLVEQLLQDpKLSQNKQALEGLGD 232
Cdd:PRK12421 174 ELAGLSPEEEEEL---FDLLQRKALPELA-EVCQNLGVGSDLRRMFYALARLNGGLEALDRALSV-LALQDAAIRQALDE 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 233 LKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYeAVLLQTPAQAgeeplgvgsVAAGGRYDGLVGMFdpkGRKVPCVG 312
Cdd:PRK12421 249 LKTLAAHLKNRWPELPVSIDLAELRGYHYHTGLVF-AAYIPGRGQA---------LARGGRYDGIGEAF---GRARPATG 315

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 119582425 313 lsigveriFSIVEQRLEALEEKIRTTETQVLVASAQKKLLEErlklVSELWDAG 366
Cdd:PRK12421 316 --------FSMDLKELLALQFLEEEAGAILAPWGDDPDLLAA----IAELRQQG 357
HGTP_anticodon2 pfam12745
Anticodon binding domain of tRNAs; This is an HGTP_anticodon binding domain, found largely on ...
 342-432 2.48e-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: 54.92  E-value: 2.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425  342 VLVASAQKKLL-EERLKLVSELWDAGIKAELLYKKNPKLLNQLQYCEEAGIPLVAIIGEQEL----KDGVIKLRSVTSRE 416
Cdd:pfam12745   8 VLVASFDASILrTTGVEILQELWAHGISADLAVDASYSPEDLVSRARDDGVSWIVIIKQQNKssdsKYKPLKVKNLLRKE 87

                          90       100
                  ....*....|....*....|
gi 119582425  417 EVDVRREDLV----EEIKRR 432
Cdd:pfam12745  88 DVDLDSDELVswlrGEIRER 107
PRK03991 PRK03991
threonyl-tRNA synthetase; Validated
 316-436 7.49e-06

threonyl-tRNA synthetase; Validated


Pssm-ID: 235190 [Multi-domain]  Cd Length: 613  Bit Score: 48.33  E-value: 7.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 316 GVER-IFSIVE-QRLEALEEKIRT-----TETQVLVASAQKKLLEERLKLVSELWDAGIKAEL------LYKKnpkllnq 382
Cdd:PRK03991 469 SIERvIYALLEkAAKEEEEGKVPMlptwlSPTQVRVIPVSERHLDYAEEVADKLEAAGIRVDVddrdesLGKK------- 541

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119582425 383 lqyCEEAG---IPLVAIIGEQELKDGVIklrSVTSREE---VDVRREDLVEEIKRRT-GQP 436
Cdd:PRK03991 542 ---IRDAGkewIPYVVVIGDKEMESGKL---TVTIREEsekVEMTLEELIERIKEETkGYP 596
ThrRS_anticodon cd00860
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases ...
 340-430 5.50e-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: 5.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 340 TQVLVASAQKKLLEERLKLVSELWDAGIKAELLYKkNPKLLNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVD 419
Cdd:cd00860    2 VQVVVIPVTDEHLDYAKEVAKKLSDAGIRVEVDLR-NEKLGKKIREAQLQKIPYILVVGDKEVETGTVSVRTRDGGDLGS 80

                         90
                 ....*....|.
gi 119582425 420 VRREDLVEEIK 430
Cdd:cd00860   81 MSLDEFIEKLK 91
PRK09194 PRK09194
prolyl-tRNA synthetase; Provisional
 302-431 8.22e-03

prolyl-tRNA synthetase; Provisional


Pssm-ID: 236405 [Multi-domain]  Cd Length: 565  Bit Score: 38.53  E-value: 8.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 302 DPKGRKVP----CVGlsIGVERIFS-IVEQRLEaleEK--IRTTET---QV-LVAS-----AQKKLLEerlKLVSELWDA 365
Cdd:PRK09194 426 DENGKAQPlimgCYG--IGVSRLVAaAIEQNHD---EKgiIWPKAIapfDVhIVPVnmkdeEVKELAE---KLYAELQAA 497

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 366 GIK----------------AELLykknpkllnqlqyceeaGIPLVAIIGEQELKDGVIKLRSVTSREEVDVRREDLVEEI 429
Cdd:PRK09194 498 GIEvllddrkerpgvkfadADLI-----------------GIPHRIVVGDRGLAEGIVEYKDRRTGEKEEVPVDELVEFL 560


                 ..
gi 119582425 430 KR 431
Cdd:PRK09194 561 KA 562
class_II_aaRS-like_core cd00768
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ...
 3-142 8.88e-03

Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA synthetases (aaRS) share a common fold and generally attach an amino acid to the 3' OH of ribose of the appropriate tRNA. PheRS is an exception in that it attaches the amino acid at the 2'-OH group, like class I aaRSs. These enzymes are usually homodimers. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. The substrate specificity of this reaction is further determined by additional domains. Intererestingly, this domain is also found is asparagine synthase A (AsnA), in the accessory subunit of mitochondrial polymerase gamma and in the bacterial ATP phosphoribosyltransferase regulatory subunit HisZ.


Pssm-ID: 238391 [Multi-domain]  Cd Length: 211  Bit Score: 37.48  E-value: 8.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425   3 VREKVFDVIIRCFKRHGAEVIDTPVFElKETLMGKYGEDSKLIYDLKDQGGELLSLRYDLTvPFARYLAMNKLTNI--KR 80
Cdd:cd00768    1 IRSKIEQKLRRFMAELGFQEVETPIVE-REPLLEKAGHEPKDLLPVGAENEEDLYLRPTLE-PGLVRLFVSHIRKLplRL 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119582425  81 YHIAKVYRRDNPAMTRGRYREFYQCDFDIAG-NFDPMIPDAECLKIMCEILSSLQIGDFLVKV 142
Cdd:cd00768   79 AEIGPAFRNEGGRRGLRRVREFTQLEGEVFGeDGEEASEFEELIELTEELLRALGIKLDIVFV 141
 
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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