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Conserved domains on  [gi|1622947319|ref|XP_028705592|]
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probable histidine--tRNA ligase, mitochondrial isoform X4 [Macaca mulatta]

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN02972 super family cl33611
Histidyl-tRNA synthetase
22-489 0e+00

Histidyl-tRNA synthetase


The actual alignment was detected with superfamily member PLN02972:

Pssm-ID: 215525 [Multi-domain]  Cd Length: 763  Bit Score: 538.70  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319  22 SFFCQVAEAVLTSQLKahqEKPnfiiKIPKGTRDLSPQHMVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGED 101
Cdd:PLN02972  309 SLVDKVKEIVESNEVR---RLP----KIPKGTRDFAKEQMAIREKAFSIITSVFKRHGATALDTPVFELRETLMGKYGED 381
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 102 SGLMYDLKDQGGELLSLRYDLTVPFARYLAMNKVKKMKRYHVGKVWRRESPSivQGRYREFCQCDFDIAGQFDPMIPDAE 181
Cdd:PLN02972  382 SKLIYDLADQGGELCSLRYDLTVPFARYVAMNGITSFKRYQIAKVYRRDNPS--KGRYREFYQCDFDIAGVYEPMGPDFE 459
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 182 CLKIMCEILSGLQLGDFLIKVNDRRIVDGMFAACGVPESKFRAICSSIDKLDKMAWKDVRHEMVAKKGLAPEVADRIGDY 261
Cdd:PLN02972  460 IIKVLTELLDELDIGTYEVKLNHRKLLDGMLEICGVPPEKFRTICSSIDKLDKQSFEQVKKEMVEEKGLSNETADKIGNF 539
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 262 VQCHGG-VSLVEQMFQ-DPRLSQNKQALEGLEDLKLLFEYLNLFGIAEKISFDLSLARGLDYYTGVIYEAVLLQTptqag 339
Cdd:PLN02972  540 VKERGPpLELLSKLRQeGSEFLGNASSRAALDELEIMFKALEKSKAIGKIVFDLSLARGLDYYTGVIYEAVFKGA----- 614
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 340 eeplNVGSVAAGGRYDGLVGMFDPKghKVPCVGLSIGVERIFYIVEQRMKTKGEKVRTTETQVFVATPQKNFLQERLKLI 419
Cdd:PLN02972  615 ----QVGSIAAGGRYDNLVGMFSGK--QVPAVGVSLGIERVFAIMEQQEEEKSQVIRPTETEVLVSIIGDDKLALAAELV 688
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 420 TELWDAGIKAEmlYKNNPKLLTQLHYCESTGIPLVVIIGEQELKEGIIKIRSVASREEVSGSSRNRRDEL 489
Cdd:PLN02972  689 SELWNAGIKAE--YKVSTRKAKHLKRAKESGIPWMVLVGEKELSKGFVKLKNLEAGVEEEVDRTCFVQEL 756
 
Name Accession Description Interval E-value
PLN02972 PLN02972
Histidyl-tRNA synthetase
22-489 0e+00

Histidyl-tRNA synthetase


Pssm-ID: 215525 [Multi-domain]  Cd Length: 763  Bit Score: 538.70  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319  22 SFFCQVAEAVLTSQLKahqEKPnfiiKIPKGTRDLSPQHMVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGED 101
Cdd:PLN02972  309 SLVDKVKEIVESNEVR---RLP----KIPKGTRDFAKEQMAIREKAFSIITSVFKRHGATALDTPVFELRETLMGKYGED 381
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 102 SGLMYDLKDQGGELLSLRYDLTVPFARYLAMNKVKKMKRYHVGKVWRRESPSivQGRYREFCQCDFDIAGQFDPMIPDAE 181
Cdd:PLN02972  382 SKLIYDLADQGGELCSLRYDLTVPFARYVAMNGITSFKRYQIAKVYRRDNPS--KGRYREFYQCDFDIAGVYEPMGPDFE 459
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 182 CLKIMCEILSGLQLGDFLIKVNDRRIVDGMFAACGVPESKFRAICSSIDKLDKMAWKDVRHEMVAKKGLAPEVADRIGDY 261
Cdd:PLN02972  460 IIKVLTELLDELDIGTYEVKLNHRKLLDGMLEICGVPPEKFRTICSSIDKLDKQSFEQVKKEMVEEKGLSNETADKIGNF 539
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 262 VQCHGG-VSLVEQMFQ-DPRLSQNKQALEGLEDLKLLFEYLNLFGIAEKISFDLSLARGLDYYTGVIYEAVLLQTptqag 339
Cdd:PLN02972  540 VKERGPpLELLSKLRQeGSEFLGNASSRAALDELEIMFKALEKSKAIGKIVFDLSLARGLDYYTGVIYEAVFKGA----- 614
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 340 eeplNVGSVAAGGRYDGLVGMFDPKghKVPCVGLSIGVERIFYIVEQRMKTKGEKVRTTETQVFVATPQKNFLQERLKLI 419
Cdd:PLN02972  615 ----QVGSIAAGGRYDNLVGMFSGK--QVPAVGVSLGIERVFAIMEQQEEEKSQVIRPTETEVLVSIIGDDKLALAAELV 688
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 420 TELWDAGIKAEmlYKNNPKLLTQLHYCESTGIPLVVIIGEQELKEGIIKIRSVASREEVSGSSRNRRDEL 489
Cdd:PLN02972  689 SELWNAGIKAE--YKVSTRKAKHLKRAKESGIPWMVLVGEKELSKGFVKLKNLEAGVEEEVDRTCFVQEL 756
HisS COG0124
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ...
47-479 2.89e-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: 337.48  E-value: 2.89e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319  47 IKIPKGTRDLSPQHMVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSG--LMYDLKDQGGELLSLRYDLTV 124
Cdd:COG0124     4 IQAPRGTRDILPEESAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKIGEDIVekEMYTFEDRGGRSLTLRPEGTA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 125 PFARYLAMNK---VKKMKRYHVGKVWRRESPsivQ-GRYREFCQCDFDIAGQFDPMIpDAECLKIMCEILSGLQLGDFLI 200
Cdd:COG0124    84 PVARAVAEHGnelPFPFKLYYIGPVFRYERP---QkGRYRQFHQFGVEVIGSDSPLA-DAEVIALAADLLKALGLKDFTL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 201 KVNDRrivdgmfaacGVPESKFRAICSSIDKLDKMAWKDVrhemvakkgLAPEVADRIG-----DYVQCHGGV--SLVEQ 273
Cdd:COG0124   160 EINSR----------GLPEERAEALLRYLDKLDKIGHEDV---------LDEDSQRRLEtnplrAILDSKGPDcqEVLAD 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 274 MfqdPRLSQNKqALEGLEDLKLLFEYLNLFGIaeKISFDLSLARGLDYYTGVIYEAVLLQTPTQageeplnvGSVAAGGR 353
Cdd:COG0124   221 A---PKLLDYL-GEEGLAHFEEVLELLDALGI--PYVIDPRLVRGLDYYTGTVFEIVTDGLGAQ--------GSVCGGGR 286
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 354 YDGLVGMFDpkGHKVPCVGLSIGVERIFYIVEQRmktKGEKVRTTETQVFVATPQKNFLQERLKLITELWDAGIKAEMLY 433
Cdd:COG0124   287 YDGLVEQLG--GPPTPAVGFAIGLERLLLLLEEL---GLLPAAEPPPDVYVVPLGEEARAEALKLAQELRAAGIRVELDL 361
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 1622947319 434 KNNpKLLTQLHYCESTGIPLVVIIGEQELKEGIIKIRSVASREEVS 479
Cdd:COG0124   362 GGR-KLKKQLKYADKSGAPFVLILGEDELANGTVTLKDLATGEQET 406
HisRS-like_core cd00773
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ...
61-385 9.46e-99

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: 299.52  E-value: 9.46e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319  61 MVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSG-LMYDLKDQGGELLSLRYDLTVPFARYLAMNKVKK-- 137
Cdd:cd00773     2 AALRRYIEDTLREVFERYGYEEIDTPVFEYTELFLRKSGDEVSkEMYRFKDKGGRDLALRPDLTAPVARAVAENLLSLpl 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 138 -MKRYHVGKVWRRESPSivQGRYREFCQCDFDIAGqFDPMIPDAECLKIMCEILSGLQLGDFLIKVNDRRIVDGmfaACG 216
Cdd:cd00773    82 pLKLYYIGPVFRYERPQ--KGRYREFYQVGVEIIG-SDSPLADAEVIALAVEILEALGLKDFQIKINHRGILDG---IAG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 217 VPESKFRAICSSIDKLDKmawkdvrhemvakkglapevadrigdyvqchggvslveqmfqdprlsqnkqalEGLEDLKLL 296
Cdd:cd00773   156 LLEDREEYIERLIDKLDK-----------------------------------------------------EALAHLEKL 182
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 297 FEYLNLFGIAEKISFDLSLARGLDYYTGVIYEAVLLQTPTQageeplnvGSVAAGGRYDGLVGMFDpkGHKVPCVGLSIG 376
Cdd:cd00773   183 LDYLEALGVDIKYSIDLSLVRGLDYYTGIVFEAVADGLGAQ--------GSIAGGGRYDGLLEEFG--GEDVPAVGFAIG 252

                  ....*....
gi 1622947319 377 VERIFYIVE 385
Cdd:cd00773   253 LERLLLALE 261
hisS TIGR00442
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ...
48-479 3.38e-95

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: 295.54  E-value: 3.38e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319  48 KIPKGTRDLSPQHMVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSGL----MYDLKDQGGELLSLRYDLT 123
Cdd:TIGR00442   1 QKPRGTRDFLPEEMIKWQYIEETIREVFERYGFKEIRTPIFEYTELFKRKVGEETDIvskeMYTFKDKGGRSLTLRPEGT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 124 VPFARYLAMNK---VKKMKRYHVGKVWRRESPsivQ-GRYREFCQCDFDIAGQFDPMIpDAECLKIMCEILSGLQLGDFL 199
Cdd:TIGR00442  81 APVARAVIENKlllPKPFKLYYIGPMFRYERP---QkGRYRQFHQFGVEVIGSDSPLA-DAEIIALAADILKELGLKDFT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 200 IKVNDRRIVDGMFAacgvpesKFRAICSSIDK-LDKMAWKDVRHEMVAKKGLAPEVADRIGDYVQchggvslveqmfQDP 278
Cdd:TIGR00442 157 LEINSLGILEGRLE-------YREALIRYLDKhKDKLGEDSVRRLEKNPLRILDSKNEKIQELLK------------NAP 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 279 RLSQNKQAlEGLEDLKLLFEYLNLFGIaeKISFDLSLARGLDYYTGVIYEAVLLQTPTQageeplnvGSVAAGGRYDGLV 358
Cdd:TIGR00442 218 KILDFLCE-ESRAHFEELKELLDALGI--PYKIDPSLVRGLDYYTGTVFEFVTDDLGAQ--------GSICGGGRYDGLV 286
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 359 GMFDpkGHKVPCVGLSIGVERIFYIVEQRmktKGEKVRTTETQVFVATPQKNFLQERLKLITELWDAGIKAEMLYKNNpK 438
Cdd:TIGR00442 287 EELG--GPPTPAVGFAIGIERLILLLEEL---GLIPPPSKKPDVYVVPLGEEAELEALKLAQKLRKAGIRVEVDLGGR-K 360
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 1622947319 439 LLTQLHYCESTGIPLVVIIGEQELKEGIIKIRSVASREEVS 479
Cdd:TIGR00442 361 LKKQLKYADKLGARFALIIGEDELENGTVTLKDLETGEQET 401
tRNA-synt_His pfam13393
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ...
52-380 4.89e-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: 152.74  E-value: 4.89e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319  52 GTRDLSPQHMVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSGLMYDLKDQGGELLSLRYDLTVPFARYLA 131
Cdd:pfam13393   1 GIRDLLPPEARRIEELRRRLLDLFRSWGYELVMPPLLEYLDSLLTGTGADLDQTFKLVDQSGRLLGLRADITPQVARIDA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 132 --MNKVKKMKRYHVGKVWRRESPSIvqGRYREFCQCDFDIAGQFDPMiPDAECLKIMCEILSGLQLGDFLIKVNDRRIVD 209
Cdd:pfam13393  81 hrLNRPGPLRLCYAGSVLRTRPKGL--GRSREPLQVGAELIGHAGIE-ADAEIISLLLEALAAAGVPGVTLDLGHVGLVR 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 210 GMFAACGVPESKFRAICSSIDKLDkmaWKDVRhEMVAKKGLAPEVADRIGDYVQCHGGVSLVEQMFQdpRLSQNKQALEG 289
Cdd:pfam13393 158 ALLEAAGLSEALEEALRAALQRKD---AAELA-ELAAEAGLPPALRRALLALPDLYGGPEVLDEARA--ALPGLPALQEA 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 290 LEDLKLLFEYLNLFGIAEKISFDLSLARGLDYYTGVIYEAVLLQTPtqageeplnvGSVAAGGRYDGLVGMFdpkGHKVP 369
Cdd:pfam13393 232 LDELEALAALLEALGDGVRLTFDLAELRGYEYYTGIVFAAYAPGVG----------EPLARGGRYDDLGAAF---GRARP 298
                         330
                  ....*....|.
gi 1622947319 370 CVGLSIGVERI 380
Cdd:pfam13393 299 ATGFSLDLEAL 309
 
Name Accession Description Interval E-value
PLN02972 PLN02972
Histidyl-tRNA synthetase
22-489 0e+00

Histidyl-tRNA synthetase


Pssm-ID: 215525 [Multi-domain]  Cd Length: 763  Bit Score: 538.70  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319  22 SFFCQVAEAVLTSQLKahqEKPnfiiKIPKGTRDLSPQHMVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGED 101
Cdd:PLN02972  309 SLVDKVKEIVESNEVR---RLP----KIPKGTRDFAKEQMAIREKAFSIITSVFKRHGATALDTPVFELRETLMGKYGED 381
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 102 SGLMYDLKDQGGELLSLRYDLTVPFARYLAMNKVKKMKRYHVGKVWRRESPSivQGRYREFCQCDFDIAGQFDPMIPDAE 181
Cdd:PLN02972  382 SKLIYDLADQGGELCSLRYDLTVPFARYVAMNGITSFKRYQIAKVYRRDNPS--KGRYREFYQCDFDIAGVYEPMGPDFE 459
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 182 CLKIMCEILSGLQLGDFLIKVNDRRIVDGMFAACGVPESKFRAICSSIDKLDKMAWKDVRHEMVAKKGLAPEVADRIGDY 261
Cdd:PLN02972  460 IIKVLTELLDELDIGTYEVKLNHRKLLDGMLEICGVPPEKFRTICSSIDKLDKQSFEQVKKEMVEEKGLSNETADKIGNF 539
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 262 VQCHGG-VSLVEQMFQ-DPRLSQNKQALEGLEDLKLLFEYLNLFGIAEKISFDLSLARGLDYYTGVIYEAVLLQTptqag 339
Cdd:PLN02972  540 VKERGPpLELLSKLRQeGSEFLGNASSRAALDELEIMFKALEKSKAIGKIVFDLSLARGLDYYTGVIYEAVFKGA----- 614
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 340 eeplNVGSVAAGGRYDGLVGMFDPKghKVPCVGLSIGVERIFYIVEQRMKTKGEKVRTTETQVFVATPQKNFLQERLKLI 419
Cdd:PLN02972  615 ----QVGSIAAGGRYDNLVGMFSGK--QVPAVGVSLGIERVFAIMEQQEEEKSQVIRPTETEVLVSIIGDDKLALAAELV 688
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 420 TELWDAGIKAEmlYKNNPKLLTQLHYCESTGIPLVVIIGEQELKEGIIKIRSVASREEVSGSSRNRRDEL 489
Cdd:PLN02972  689 SELWNAGIKAE--YKVSTRKAKHLKRAKESGIPWMVLVGEKELSKGFVKLKNLEAGVEEEVDRTCFVQEL 756
HisS COG0124
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ...
47-479 2.89e-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: 337.48  E-value: 2.89e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319  47 IKIPKGTRDLSPQHMVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSG--LMYDLKDQGGELLSLRYDLTV 124
Cdd:COG0124     4 IQAPRGTRDILPEESAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKIGEDIVekEMYTFEDRGGRSLTLRPEGTA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 125 PFARYLAMNK---VKKMKRYHVGKVWRRESPsivQ-GRYREFCQCDFDIAGQFDPMIpDAECLKIMCEILSGLQLGDFLI 200
Cdd:COG0124    84 PVARAVAEHGnelPFPFKLYYIGPVFRYERP---QkGRYRQFHQFGVEVIGSDSPLA-DAEVIALAADLLKALGLKDFTL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 201 KVNDRrivdgmfaacGVPESKFRAICSSIDKLDKMAWKDVrhemvakkgLAPEVADRIG-----DYVQCHGGV--SLVEQ 273
Cdd:COG0124   160 EINSR----------GLPEERAEALLRYLDKLDKIGHEDV---------LDEDSQRRLEtnplrAILDSKGPDcqEVLAD 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 274 MfqdPRLSQNKqALEGLEDLKLLFEYLNLFGIaeKISFDLSLARGLDYYTGVIYEAVLLQTPTQageeplnvGSVAAGGR 353
Cdd:COG0124   221 A---PKLLDYL-GEEGLAHFEEVLELLDALGI--PYVIDPRLVRGLDYYTGTVFEIVTDGLGAQ--------GSVCGGGR 286
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 354 YDGLVGMFDpkGHKVPCVGLSIGVERIFYIVEQRmktKGEKVRTTETQVFVATPQKNFLQERLKLITELWDAGIKAEMLY 433
Cdd:COG0124   287 YDGLVEQLG--GPPTPAVGFAIGLERLLLLLEEL---GLLPAAEPPPDVYVVPLGEEARAEALKLAQELRAAGIRVELDL 361
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 1622947319 434 KNNpKLLTQLHYCESTGIPLVVIIGEQELKEGIIKIRSVASREEVS 479
Cdd:COG0124   362 GGR-KLKKQLKYADKSGAPFVLILGEDELANGTVTLKDLATGEQET 406
HisRS-like_core cd00773
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ...
61-385 9.46e-99

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: 299.52  E-value: 9.46e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319  61 MVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSG-LMYDLKDQGGELLSLRYDLTVPFARYLAMNKVKK-- 137
Cdd:cd00773     2 AALRRYIEDTLREVFERYGYEEIDTPVFEYTELFLRKSGDEVSkEMYRFKDKGGRDLALRPDLTAPVARAVAENLLSLpl 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 138 -MKRYHVGKVWRRESPSivQGRYREFCQCDFDIAGqFDPMIPDAECLKIMCEILSGLQLGDFLIKVNDRRIVDGmfaACG 216
Cdd:cd00773    82 pLKLYYIGPVFRYERPQ--KGRYREFYQVGVEIIG-SDSPLADAEVIALAVEILEALGLKDFQIKINHRGILDG---IAG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 217 VPESKFRAICSSIDKLDKmawkdvrhemvakkglapevadrigdyvqchggvslveqmfqdprlsqnkqalEGLEDLKLL 296
Cdd:cd00773   156 LLEDREEYIERLIDKLDK-----------------------------------------------------EALAHLEKL 182
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 297 FEYLNLFGIAEKISFDLSLARGLDYYTGVIYEAVLLQTPTQageeplnvGSVAAGGRYDGLVGMFDpkGHKVPCVGLSIG 376
Cdd:cd00773   183 LDYLEALGVDIKYSIDLSLVRGLDYYTGIVFEAVADGLGAQ--------GSIAGGGRYDGLLEEFG--GEDVPAVGFAIG 252

                  ....*....
gi 1622947319 377 VERIFYIVE 385
Cdd:cd00773   253 LERLLLALE 261
hisS TIGR00442
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ...
48-479 3.38e-95

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: 295.54  E-value: 3.38e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319  48 KIPKGTRDLSPQHMVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSGL----MYDLKDQGGELLSLRYDLT 123
Cdd:TIGR00442   1 QKPRGTRDFLPEEMIKWQYIEETIREVFERYGFKEIRTPIFEYTELFKRKVGEETDIvskeMYTFKDKGGRSLTLRPEGT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 124 VPFARYLAMNK---VKKMKRYHVGKVWRRESPsivQ-GRYREFCQCDFDIAGQFDPMIpDAECLKIMCEILSGLQLGDFL 199
Cdd:TIGR00442  81 APVARAVIENKlllPKPFKLYYIGPMFRYERP---QkGRYRQFHQFGVEVIGSDSPLA-DAEIIALAADILKELGLKDFT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 200 IKVNDRRIVDGMFAacgvpesKFRAICSSIDK-LDKMAWKDVRHEMVAKKGLAPEVADRIGDYVQchggvslveqmfQDP 278
Cdd:TIGR00442 157 LEINSLGILEGRLE-------YREALIRYLDKhKDKLGEDSVRRLEKNPLRILDSKNEKIQELLK------------NAP 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 279 RLSQNKQAlEGLEDLKLLFEYLNLFGIaeKISFDLSLARGLDYYTGVIYEAVLLQTPTQageeplnvGSVAAGGRYDGLV 358
Cdd:TIGR00442 218 KILDFLCE-ESRAHFEELKELLDALGI--PYKIDPSLVRGLDYYTGTVFEFVTDDLGAQ--------GSICGGGRYDGLV 286
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 359 GMFDpkGHKVPCVGLSIGVERIFYIVEQRmktKGEKVRTTETQVFVATPQKNFLQERLKLITELWDAGIKAEMLYKNNpK 438
Cdd:TIGR00442 287 EELG--GPPTPAVGFAIGIERLILLLEEL---GLIPPPSKKPDVYVVPLGEEAELEALKLAQKLRKAGIRVEVDLGGR-K 360
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 1622947319 439 LLTQLHYCESTGIPLVVIIGEQELKEGIIKIRSVASREEVS 479
Cdd:TIGR00442 361 LKKQLKYADKLGARFALIIGEDELENGTVTLKDLETGEQET 401
PRK12420 PRK12420
histidyl-tRNA synthetase; Provisional
51-478 1.18e-83

histidyl-tRNA synthetase; Provisional


Pssm-ID: 237097 [Multi-domain]  Cd Length: 423  Bit Score: 266.21  E-value: 1.18e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319  51 KGTRDLSPQHMVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYG---EDSGLMYDLKDQGGELLSLRYDLTVPFA 127
Cdd:PRK12420    8 KGTKDYLPEEQVLRNKIKRALEDVFERYGCKPLETPTLNMYELMSSKYGggdEILKEIYTLTDQGKRDLALRYDLTIPFA 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 128 RYLAMNKVKKM--KRYHVGKVWrRESPsIVQGRYREFCQCDFDIAGQFDPMiPDAECLKIMCEILSGLQLgDFLIKVNDR 205
Cdd:PRK12420   88 KVVAMNPNIRLpfKRYEIGKVF-RDGP-IKQGRFREFIQCDVDIVGVESVM-AEAELMSMAFELFRRLNL-EVTIQYNNR 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 206 RIVDGMFAACGVPESKFRAICSSIDKLDKMAWKDVRHEmVAKKGLAPEVADRIGDYVQCHGGVSLVEqmFQDPRLSQNKQ 285
Cdd:PRK12420  164 KLLNGILQAIGIPTELTSDVILSLDKIEKIGIDGVRKD-LLERGISEEMADTICNTVLSCLQLSIAD--FKEAFNNPLVA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 286 alEGLEDLKLLFEYLNLFGIAEKISFDLSLARGLDYYTGVIYEAVLlqtptqagEEPLNVGSVAAGGRYDGLVGMFDPKG 365
Cdd:PRK12420  241 --EGVNELQQLQQYLIALGINENCIFNPFLARGLTMYTGTVYEIFL--------KDGSITSSIGSGGRYDNIIGAFRGDD 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 366 HKVPCVGLSIGVERIFYIVEQRmktkgekVRTTETQVFVATPQKNFLQERLKLITELWDAGIKAEMLYKNNpKLLTQLHY 445
Cdd:PRK12420  311 MNYPTVGISFGLDVIYTALSQK-------ETISSTADVFIIPLGTELQCLQIAQQLRSTTGLKVELELAGR-KLKKALNY 382
                         410       420       430
                  ....*....|....*....|....*....|...
gi 1622947319 446 CESTGIPLVVIIGEQELKEGIIKIRSVASREEV 478
Cdd:PRK12420  383 ANKENIPYVLIIGEEEVSTGTVMLRNMKEGSEV 415
hisZ_biosyn_reg TIGR00443
ATP phosphoribosyltransferase, regulatory subunit; Apparant second copies of histidyl-tRNA ...
54-380 5.70e-53

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: 182.43  E-value: 5.70e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319  54 RDLSPQHMVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSGLMYDLKDQGGELLSLRYDLTVPFARYLAmn 133
Cdd:TIGR00443   1 RDLLPEEAARKEEIERQLQDVFRSWGYQEIITPTLEYLDTLSAGSGILNEDLFKLFDQLGRVLGLRPDMTAPIARLVS-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 134 kvKKMKRYH-------VGKVWRRESPSIvqGRYREFCQCDFDIAGQfDPMIPDAECLKIMCEILSGLQLGDFLIKVNDRR 206
Cdd:TIGR00443  79 --TRLRDRPlplrlcyAGNVFRTNESGG--GRSREFTQAGVELIGA-GGPAADAEVIALLIEALKALGLKDFKIELGHVG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 207 IVDGMFAACGVPESKFRAICSSIDKLDKMAWKdvrhEMVAKKGLAPEVADRIGDYVQCHGGVSLVEQMFQdpRLSQNKQA 286
Cdd:TIGR00443 154 LVRALLEEAGLPEEAREALREALARKDLVALE----ELVAELGLSPEVRERLLALPRLRGDGEEVLEEAR--ALAGSETA 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 287 LEGLEDLKLLFEYLNLFGIAEKISFDLSLARGLDYYTGVIYEAVLlqtpTQAGEeplnvgSVAAGGRYDGLVGMFdpkGH 366
Cdd:TIGR00443 228 EAALDELEAVLELLEARGVEEYISLDLGLVRGYHYYTGLIFEGYA----PGLGA------PLAGGGRYDELLGRF---GR 294
                         330
                  ....*....|....
gi 1622947319 367 KVPCVGLSIGVERI 380
Cdd:TIGR00443 295 PLPATGFALNLERL 308
PLN02530 PLN02530
histidine-tRNA ligase
3-479 1.03e-48

histidine-tRNA ligase


Pssm-ID: 178145 [Multi-domain]  Cd Length: 487  Bit Score: 175.70  E-value: 1.03e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319   3 NGVRNATGLASVQRSHFSHSFFCQVAEAVLTSQLKAHQEKPNFIIKI----PKGTRDLSPQHMVVREKILDLVISCFKRH 78
Cdd:PLN02530   22 LSSRCSFLLSASSPRGGRCAASAAAGGGRSGGTTAPPSVQEDGKPKIdvnpPKGTRDFPPEDMRLRNWLFDHFREVSRLF 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319  79 GAKGMDTPAFELKETLTEKYGED-SGLMYDLKDQGGELLSLRYDLTVPFARyLAMNKVKKM----KRYHVGKVWRRESps 153
Cdd:PLN02530  102 GFEEVDAPVLESEELYIRKAGEEiTDQLYNFEDKGGRRVALRPELTPSLAR-LVLQKGKSLslplKWFAIGQCWRYER-- 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 154 IVQGRYREFCQCDFDIAGqFDPMIPDAECLKIMCEILS--GLQLGDFLIKVNDRRIVDGMFAACGVPESKFRAICSSIDK 231
Cdd:PLN02530  179 MTRGRRREHYQWNMDIIG-VPGVEAEAELLAAIVTFFKrvGITSSDVGIKVSSRKVLQAVLKSYGIPEESFAPVCVIVDK 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 232 LDKMAWKDVRHEMvAKKGLAPEVADRIGDYVQCHGGVSLVEQMFQDPrlsqnkqalEGLEDLKLLFEYLNLFGIAEKISF 311
Cdd:PLN02530  258 LEKLPREEIEKEL-DTLGVSEEAIEGILDVLSLKSLDDLEALLGADS---------EAVADLKQLFSLAEAYGYQDWLVF 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 312 DLSLARGLDYYTGVIYEAVllqtpTQAGEeplnVGSVAAGGRYDGLVGMFDpkGHKVPCVGLSIG--VerifyIVEqRMK 389
Cdd:PLN02530  328 DASVVRGLAYYTGIVFEGF-----DRAGK----LRAICGGGRYDRLLSTFG--GEDTPACGFGFGdaV-----IVE-LLK 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 390 TKG---EKVRTTETQVFvatPQKNFLQ-ERLKLITELWDAGIKAEMLYKNNpKLLTQLHYCESTGIPLVVIIGEQELKEG 465
Cdd:PLN02530  391 EKGllpELPHQVDDVVF---ALDEDLQgAAAGVASRLREKGRSVDLVLEPK-KLKWVFKHAERIGAKRLVLVGASEWERG 466
                         490
                  ....*....|....
gi 1622947319 466 IIKIRSVASREEVS 479
Cdd:PLN02530  467 MVRVKDLSSGEQTE 480
HisZ COG3705
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism];
64-380 5.49e-48

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


Pssm-ID: 442919 [Multi-domain]  Cd Length: 312  Bit Score: 168.82  E-value: 5.49e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319  64 REKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSGL-MYDLKDQGGELLSLRYDLTVPFARYLA--MNKVKKMKR 140
Cdd:COG3705     8 KEELRRRLLDVFRSWGYELVEPPLLEYLDSLLTGSGADLDLqTFKLVDQLGRTLGLRPDMTPQVARIAAtrLANRPGPLR 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 141 Y-HVGKVWRRESPSivQGRYREFCQC------DFDIAGqfdpmipDAECLKIMCEILSGLQLGDFLIKVNDRRIVDGMFA 213
Cdd:COG3705    88 LcYAGNVFRTRPSG--LGRSREFLQAgaeligHAGLEA-------DAEVIALALEALKAAGLEDFTLDLGHVGLFRALLE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 214 ACGVPESKFRAICSSIDKLDkmaWKDVRhEMVAKKGLAPEVADRIGDYVQCHGGVSLVEQMFQdprLSQNKQALEGLEDL 293
Cdd:COG3705   159 ALGLSEEQREELRRALARKD---AVELE-ELLAELGLSEELAEALLALPELYGGEEVLARARA---LLLDAAIRAALDEL 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 294 KLLFEYLNLFGIAEKISFDLSLARGLDYYTGVIYEAVllqTPTQAGEeplnvgsVAAGGRYDGLVGMFdpkGHKVPCVGL 373
Cdd:COG3705   232 EALAEALAARGPDVRLTFDLSELRGYDYYTGIVFEAY---APGVGDP-------LARGGRYDGLLAAF---GRARPATGF 298

                  ....*..
gi 1622947319 374 SIGVERI 380
Cdd:COG3705   299 SLDLDRL 305
hisZ PRK12292
ATP phosphoribosyltransferase regulatory subunit; Provisional
49-431 1.01e-46

ATP phosphoribosyltransferase regulatory subunit; Provisional


Pssm-ID: 237043 [Multi-domain]  Cd Length: 391  Bit Score: 167.74  E-value: 1.01e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319  49 IPKGTRDLSPQHMVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSGL-MYDLKDQG-GELLSLRYDLTVPF 126
Cdd:PRK12292    5 LPEGIRDLLPEEARKIEEIRRRLLDLFRRWGYEEVITPTLEYLDTLLAGGGAILDLrTFKLVDQLsGRTLGLRPDMTAQI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 127 ARyLAMNKVKKMKR-----YHvGKVWR-RESPSivqGRYREFCQCDFDIAGqFDPMIPDAECLKIMCEILSGLQLGDFLI 200
Cdd:PRK12292   85 AR-IAATRLANRPGplrlcYA-GNVFRaQERGL---GRSREFLQSGVELIG-DAGLEADAEVILLLLEALKALGLPNFTL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 201 KVNDRRIVDGMFAACGVPESKFRAICSSIDKLDKMAWKdvrhEMVAkkGLAPEVADRIGDYVQCHGGVSLVEQMfqdPRL 280
Cdd:PRK12292  159 DLGHVGLFRALLEAAGLSEELEEVLRRALANKDYVALE----ELVL--DLSEELRDALLALPRLRGGREVLEEA---RKL 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 281 SQNKQALEGLEDLKLLFEYLNLFGIAEKISFDLSLARGLDYYTGVIYEAVllqtptqAGEEPLNVGSvaaGGRYDGLVGM 360
Cdd:PRK12292  230 LPSLPIKRALDELEALAEALEKYGYGIPLSLDLGLLRHLDYYTGIVFEGY-------VDGVGNPIAS---GGRYDDLLGR 299
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622947319 361 FdpkGHKVPCVGLSIGVERifyIVEQRMKTKgekvrTTETQVFVATPQKNFLQERLKLITELWDAGIKAEM 431
Cdd:PRK12292  300 F---GRARPATGFSLDLDR---LLELQLELP-----VEARKDLVIAPDSEALAAALAAAQELRKKGEIVVL 359
tRNA-synt_His pfam13393
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ...
52-380 4.89e-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: 152.74  E-value: 4.89e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319  52 GTRDLSPQHMVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSGLMYDLKDQGGELLSLRYDLTVPFARYLA 131
Cdd:pfam13393   1 GIRDLLPPEARRIEELRRRLLDLFRSWGYELVMPPLLEYLDSLLTGTGADLDQTFKLVDQSGRLLGLRADITPQVARIDA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 132 --MNKVKKMKRYHVGKVWRRESPSIvqGRYREFCQCDFDIAGQFDPMiPDAECLKIMCEILSGLQLGDFLIKVNDRRIVD 209
Cdd:pfam13393  81 hrLNRPGPLRLCYAGSVLRTRPKGL--GRSREPLQVGAELIGHAGIE-ADAEIISLLLEALAAAGVPGVTLDLGHVGLVR 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 210 GMFAACGVPESKFRAICSSIDKLDkmaWKDVRhEMVAKKGLAPEVADRIGDYVQCHGGVSLVEQMFQdpRLSQNKQALEG 289
Cdd:pfam13393 158 ALLEAAGLSEALEEALRAALQRKD---AAELA-ELAAEAGLPPALRRALLALPDLYGGPEVLDEARA--ALPGLPALQEA 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 290 LEDLKLLFEYLNLFGIAEKISFDLSLARGLDYYTGVIYEAVLLQTPtqageeplnvGSVAAGGRYDGLVGMFdpkGHKVP 369
Cdd:pfam13393 232 LDELEALAALLEALGDGVRLTFDLAELRGYEYYTGIVFAAYAPGVG----------EPLARGGRYDDLGAAF---GRARP 298
                         330
                  ....*....|.
gi 1622947319 370 CVGLSIGVERI 380
Cdd:pfam13393 299 ATGFSLDLEAL 309
syh CHL00201
histidine-tRNA synthetase; Provisional
51-477 1.11e-27

histidine-tRNA synthetase; Provisional


Pssm-ID: 164576 [Multi-domain]  Cd Length: 430  Bit Score: 115.38  E-value: 1.11e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319  51 KGTRDLSPQHMVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSGL----MYDLKDQGGELLSLRYDLTVPF 126
Cdd:CHL00201    8 RGTKDILPDEINYWQFIHDKALTLLSLANYSEIRTPIFENSSLYDRGIGETTDIvnkeMYRFTDRSNRDITLRPEGTAGI 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 127 ARYLAMNKVKKMKR----YHVGKVWRRESPSivQGRYREFCQCDFDIAGQFDPMiPDAECLKIMCEILSGLQLGDFLIKV 202
Cdd:CHL00201   88 VRAFIENKMDYHSNlqrlWYSGPMFRYERPQ--SGRQRQFHQLGIEFIGSIDAR-ADTEVIHLAMQIFNELQVKNLILDI 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 203 N------DRRIVdgmfaacgvpESKFRAICSSI-DKLDKmawkDVRHEMVAKkglaP-EVADRIGDYVQchggvslvEQM 274
Cdd:CHL00201  165 NsigkleDRQSY----------QLKLVEYLSQYqDDLDT----DSQNRLYSN----PiRILDSKNLKTQ--------EIL 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 275 FQDPRLSqNKQALEGLEDLKLLFEYLNLFGIAEKISFdlSLARGLDYYTGVIYEavlLQTPTQAGEEplnvgSVAAGGRY 354
Cdd:CHL00201  219 DGAPKIS-DFLSLESTEHFYDVCTYLNLLNIPYKINY--KLVRGLDYYNDTAFE---IKTLSSNGQD-----TICGGGRY 287
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 355 DGLVGMFDpkGHKVPCVGLSIGVERIFYIVEQRMKTKGEKVrttetQVFVATPQKNFLQERLKLITELWDAGIKAEmLYK 434
Cdd:CHL00201  288 DSLIHQLG--GPKTPAVGCAIGLERLLLIAKDNIILPKQSI-----DVYIATQGLKAQKKGWEIIQFLEKQNIKFE-LDL 359
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 1622947319 435 NNPKLLTQLHYCESTGIPLVVIIGEQELKEGIIKIRSVASREE 477
Cdd:CHL00201  360 SSSNFHKQIKQAGKKRAKACIILGDNEIMDNCITIKWLDEQVQ 402
HisRS_anticodon cd00859
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases ...
399-479 2.67e-24

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: 96.84  E-value: 2.67e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 399 ETQVFVATPQKNFLQERLKLITELWDAGIKAEMLYKNnPKLLTQLHYCESTGIPLVVIIGEQELKEGIIKIRSVASREEV 478
Cdd:cd00859     1 EVDVYVVPLGEGALSEALELAEQLRDAGIKAEIDYGG-RKLKKQFKYADRSGARFAVILGEDELAAGVVTVKDLETGEQE 79

                  .
gi 1622947319 479 S 479
Cdd:cd00859    80 T 80
hisZ PRK12295
ATP phosphoribosyltransferase regulatory subunit; Provisional
67-380 5.68e-22

ATP phosphoribosyltransferase regulatory subunit; Provisional


Pssm-ID: 183413 [Multi-domain]  Cd Length: 373  Bit Score: 97.70  E-value: 5.68e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319  67 ILDLVISCFKRHGAKGMDTPAFELKETLTEKYGED-SGLMYDLKDQGGELLSLRYDLTVPFAR-YLAMNKVKKMKRYHVG 144
Cdd:PRK12295   10 AAEALLASFEAAGAVRVDPPILQPAEPFLDLSGEDiRRRIFVTSDENGEELCLRPDFTIPVCRrHIATAGGEPARYAYLG 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 145 KVWRRESpsivqGRYREFCQCDFDIAGQFDPMIPDAECLKIMCEILSGLQLGDFLIKVNDRRIVDGMFAACGVPE----- 219
Cdd:PRK12295   90 EVFRQRR-----DRASEFLQAGIESFGRADPAAADAEVLALALEALAALGPGDLEVRLGDVGLFAALVDALGLPPgwkrr 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 220 --------SKFRAIcssIDKL-------------------DKMAWKDVRHEMVAKKGLAP-------EVADRIGDYVQCH 265
Cdd:PRK12295  165 llrhfgrpRSLDAL---LARLagprvdpldehagvlaalaDEAAARALVEDLMSIAGISPvggrspaEIARRLLEKAALA 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 266 GGVSLVEQMFQ----------DPrlsqnKQALEGLEDL----KL-LFEYLNLF----------GIA-EKISFDLSLARGL 319
Cdd:PRK12295  242 AAARLPAEALAvlerflaisgPP-----DAALAALRALaadaGLdLDAALDRFearlaalaarGIDlERLRFSASFGRPL 316
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622947319 320 DYYTGVIYEAvllqTPTQAGEEPLnvgsvAAGGRYDGLVGMFDpKGHKVPCVGLSIGVERI 380
Cdd:PRK12295  317 DYYTGFVFEI----RAAGNGDPPL-----AGGGRYDGLLTRLG-AGEPIPAVGFSIWLDRL 367
HGTP_anticodon pfam03129
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ...
401-489 5.82e-14

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: 67.61  E-value: 5.82e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 401 QVFVATPQKN---FLQERLKLITELWDAGIKAEmLYKNNPKLLTQLHYCESTGIPLVVIIGEQELKEGIIKIRSVASREE 477
Cdd:pfam03129   1 QVVVIPLGEKaeeLEEYAQKLAEELRAAGIRVE-LDDRNESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQ 79
                          90
                  ....*....|..
gi 1622947319 478 VSGSsrnrRDEL 489
Cdd:pfam03129  80 ETVS----LDEL 87
PRK12421 PRK12421
ATP phosphoribosyltransferase regulatory subunit; Provisional
50-380 1.91e-07

ATP phosphoribosyltransferase regulatory subunit; Provisional


Pssm-ID: 237098  Cd Length: 392  Bit Score: 53.43  E-value: 1.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319  50 PKGTRDLSP---QHM-VVREKILDLVIScfkrHGAKGMDTPAFELKETLTEKYGEDSGLM-YDLKDQ-GGELLSLRYDLT 123
Cdd:PRK12421   10 PDGVADVLPeeaQKIeRLRRRLLDLFAS----RGYQLVMPPLIEYLESLLTGAGQDLKLQtFKLIDQlSGRLMGVRADIT 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 124 VPFARYLA-MNKVKKMKRY-HVGKVWRRESPSIvqGRYREFCQCDFDIAGQfDPMIPDAECLKIMCEILSGLQLGDFLIK 201
Cdd:PRK12421   86 PQVARIDAhLLNREGVARLcYAGSVLHTLPQGL--FGSRTPLQLGAELYGH-AGIEADLEIIRLMLGLLRNAGVPALHLD 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 202 VNDRRIVDGMFAACGVPESKFRAIcssidkLDKMAWKDVR--HEMVAKKGLAPEVADRIGDYVQCHGGV-SLVEQMFQDP 278
Cdd:PRK12421  163 LGHVGIFRRLAELAGLSPEEEEEL------FDLLQRKALPelAEVCQNLGVGSDLRRMFYALARLNGGLeALDRALSVLA 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 279 RlsQNKQALEGLEDLKLLFEYLNLFGIAEKISFDLSLARGLDYYTGVIYeAVLLQTPTQAgeeplnvgsVAAGGRYDGLV 358
Cdd:PRK12421  237 L--QDAAIRQALDELKTLAAHLKNRWPELPVSIDLAELRGYHYHTGLVF-AAYIPGRGQA---------LARGGRYDGIG 304
                         330       340
                  ....*....|....*....|..
gi 1622947319 359 GMFdpkGHKVPCVGLSIGVERI 380
Cdd:PRK12421  305 EAF---GRARPATGFSMDLKEL 323
HGTP_anticodon2 pfam12745
Anticodon binding domain of tRNAs; This is an HGTP_anticodon binding domain, found largely on ...
402-478 9.61e-05

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: 44.13  E-value: 9.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947319 402 VFVATPQKNFL-QERLKLITELWDAGIKAEMLYKNNPKLLTQLHYCESTGIPLVVIIGEQEL----KEGIIKIRSVASRE 476
Cdd:pfam12745   8 VLVASFDASILrTTGVEILQELWAHGISADLAVDASYSPEDLVSRARDDGVSWIVIIKQQNKssdsKYKPLKVKNLLRKE 87

                  ..
gi 1622947319 477 EV 478
Cdd:pfam12745  88 DV 89
 
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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