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Conserved domains on  [gi|1391723599|ref|NP_001350464|]
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histidine--tRNA ligase, mitochondrial isoform 4 precursor [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

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
PLN02972 super family cl33611
Histidyl-tRNA synthetase
 12-510 0e+00

Histidyl-tRNA synthetase


The actual alignment was detected with superfamily member PLN02972:

Pssm-ID: 215525 [Multi-domain]  Cd Length: 763  Bit Score: 540.24  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599  12 WASLLSQLLRPPCASCTGAVRcqsqgeeslQVAEAVLTSQLKahqEKPnfiiKTPKGTRDLSPQHMVVREKILDLVISCF 91
Cdd:PLN02972  292 WATQLLLLFDPKCPGFDSLVD---------KVKEIVESNEVR---RLP----KIPKGTRDFAKEQMAIREKAFSIITSVF 355

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599  92 KRHGAKGMDTPAFELKETLTEKYGEDSGLMYDLKDQGGELLSLRYDLTVPFARYLAMNKVKKMKRYHVGKVWRRESPTiv 171
Cdd:PLN02972  356 KRHGATALDTPVFELRETLMGKYGEDSKLIYDLADQGGELCSLRYDLTVPFARYVAMNGITSFKRYQIAKVYRRDNPS-- 433

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 172 QGRYREFCQCDFDIAGQFDPMIPDAECLKIMCEILSGLQLGDFLIKVNDRRIVDGMFAVCGVPESKFRAICSSIDKLDKM 251
Cdd:PLN02972  434 KGRYREFYQCDFDIAGVYEPMGPDFEIIKVLTELLDELDIGTYEVKLNHRKLLDGMLEICGVPPEKFRTICSSIDKLDKQ 513

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 252 AWKDVRHEMVVKKGLAPEVADRIGDYVQCHGG-VSLVEQMFQ-DPRLSQNKQALEGLGDLKLLFEYLTLFGIADKISFDL 329
Cdd:PLN02972  514 SFEQVKKEMVEEKGLSNETADKIGNFVKERGPpLELLSKLRQeGSEFLGNASSRAALDELEIMFKALEKSKAIGKIVFDL 593

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 330 SLARGLDYYTGVIYEAVLLQTptqageeplNVGSVAAGGRYDGLVGMFDPKghKVPCVGLSIGVERIFYIVEQRMKTKGE 409
Cdd:PLN02972  594 SLARGLDYYTGVIYEAVFKGA---------QVGSIAAGGRYDNLVGMFSGK--QVPAVGVSLGIERVFAIMEQQEEEKSQ 662

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 410 KVRTTETQVFVATPQKNFLQERLKLIAELWDSGIKAEmlYKNNPKLLTQLHYCESTGIPLVVIIGEQELKEGVIKIRSVA 489
Cdd:PLN02972  663 VIRPTETEVLVSIIGDDKLALAAELVSELWNAGIKAE--YKVSTRKAKHLKRAKESGIPWMVLVGEKELSKGFVKLKNLE 740

                         490       500
                  ....*....|....*....|.
gi 1391723599 490 SREEVAIKRENFVAEIQKRLS 510
Cdd:PLN02972  741 AGVEEEVDRTCFVQELKAELL 761
 
Name Accession Description Interval E-value
PLN02972 PLN02972
Histidyl-tRNA synthetase
 12-510 0e+00

Histidyl-tRNA synthetase


Pssm-ID: 215525 [Multi-domain]  Cd Length: 763  Bit Score: 540.24  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599  12 WASLLSQLLRPPCASCTGAVRcqsqgeeslQVAEAVLTSQLKahqEKPnfiiKTPKGTRDLSPQHMVVREKILDLVISCF 91
Cdd:PLN02972  292 WATQLLLLFDPKCPGFDSLVD---------KVKEIVESNEVR---RLP----KIPKGTRDFAKEQMAIREKAFSIITSVF 355

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599  92 KRHGAKGMDTPAFELKETLTEKYGEDSGLMYDLKDQGGELLSLRYDLTVPFARYLAMNKVKKMKRYHVGKVWRRESPTiv 171
Cdd:PLN02972  356 KRHGATALDTPVFELRETLMGKYGEDSKLIYDLADQGGELCSLRYDLTVPFARYVAMNGITSFKRYQIAKVYRRDNPS-- 433

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 172 QGRYREFCQCDFDIAGQFDPMIPDAECLKIMCEILSGLQLGDFLIKVNDRRIVDGMFAVCGVPESKFRAICSSIDKLDKM 251
Cdd:PLN02972  434 KGRYREFYQCDFDIAGVYEPMGPDFEIIKVLTELLDELDIGTYEVKLNHRKLLDGMLEICGVPPEKFRTICSSIDKLDKQ 513

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 252 AWKDVRHEMVVKKGLAPEVADRIGDYVQCHGG-VSLVEQMFQ-DPRLSQNKQALEGLGDLKLLFEYLTLFGIADKISFDL 329
Cdd:PLN02972  514 SFEQVKKEMVEEKGLSNETADKIGNFVKERGPpLELLSKLRQeGSEFLGNASSRAALDELEIMFKALEKSKAIGKIVFDL 593

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 330 SLARGLDYYTGVIYEAVLLQTptqageeplNVGSVAAGGRYDGLVGMFDPKghKVPCVGLSIGVERIFYIVEQRMKTKGE 409
Cdd:PLN02972  594 SLARGLDYYTGVIYEAVFKGA---------QVGSIAAGGRYDNLVGMFSGK--QVPAVGVSLGIERVFAIMEQQEEEKSQ 662

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 410 KVRTTETQVFVATPQKNFLQERLKLIAELWDSGIKAEmlYKNNPKLLTQLHYCESTGIPLVVIIGEQELKEGVIKIRSVA 489
Cdd:PLN02972  663 VIRPTETEVLVSIIGDDKLALAAELVSELWNAGIKAE--YKVSTRKAKHLKRAKESGIPWMVLVGEKELSKGFVKLKNLE 740

                         490       500
                  ....*....|....*....|.
gi 1391723599 490 SREEVAIKRENFVAEIQKRLS 510
Cdd:PLN02972  741 AGVEEEVDRTCFVQELKAELL 761
HisS COG0124
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ...
 63-511 8.59e-115

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: 345.57  E-value: 8.59e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599  63 IKTPKGTRDLSPQHMVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSG--LMYDLKDQGGELLSLRYDLTV 140
Cdd:COG0124     4 IQAPRGTRDILPEESAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKIGEDIVekEMYTFEDRGGRSLTLRPEGTA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 141 PFARYLAMNK---VKKMKRYHVGKVWRRESPtivQ-GRYREFCQCDFDIAGQFDPMIpDAECLKIMCEILSGLQLGDFLI 216
Cdd:COG0124    84 PVARAVAEHGnelPFPFKLYYIGPVFRYERP---QkGRYRQFHQFGVEVIGSDSPLA-DAEVIALAADLLKALGLKDFTL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 217 KVNDRrivdgmfavcGVPESKFRAICSSIDKLDKMAWKDVrhemvvkkgLAPEVADRIG-----DYVQCHGGV--SLVEQ 289
Cdd:COG0124   160 EINSR----------GLPEERAEALLRYLDKLDKIGHEDV---------LDEDSQRRLEtnplrAILDSKGPDcqEVLAD 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 290 MfqdPRLSQNKqALEGLGDLKLLFEYLTLFGIadKISFDLSLARGLDYYTGVIYEAVLLQTPTQageeplnvGSVAAGGR 369
Cdd:COG0124   221 A---PKLLDYL-GEEGLAHFEEVLELLDALGI--PYVIDPRLVRGLDYYTGTVFEIVTDGLGAQ--------GSVCGGGR 286

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 370 YDGLVGMFDpkGHKVPCVGLSIGVERIFYIVEQRmktKGEKVRTTETQVFVATPQKNFLQERLKLIAELWDSGIKAEMLY 449
Cdd:COG0124   287 YDGLVEQLG--GPPTPAVGFAIGLERLLLLLEEL---GLLPAAEPPPDVYVVPLGEEARAEALKLAQELRAAGIRVELDL 361

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1391723599 450 KNNpKLLTQLHYCESTGIPLVVIIGEQELKEGVIKIRSVASREEVAIKRENFVAEIQKRLSE 511
Cdd:COG0124   362 GGR-KLKKQLKYADKSGAPFVLILGEDELANGTVTLKDLATGEQETVPLDELVEYLKELLAE 422
HisRS-like_core cd00773
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ...
 77-401 1.34e-97

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: 295.67  E-value: 1.34e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599  77 MVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSG-LMYDLKDQGGELLSLRYDLTVPFARYLAMNKVKK-- 153
Cdd:cd00773     2 AALRRYIEDTLREVFERYGYEEIDTPVFEYTELFLRKSGDEVSkEMYRFKDKGGRDLALRPDLTAPVARAVAENLLSLpl 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 154 -MKRYHVGKVWRRESPTivQGRYREFCQCDFDIAGqFDPMIPDAECLKIMCEILSGLQLGDFLIKVNDRRIVDGmfaVCG 232
Cdd:cd00773    82 pLKLYYIGPVFRYERPQ--KGRYREFYQVGVEIIG-SDSPLADAEVIALAVEILEALGLKDFQIKINHRGILDG---IAG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 233 VPESKFRAICSSIDKLDKmawkdvrhemvvkkglapevadrigdyvqchggvslveqmfqdprlsqnkqalEGLGDLKLL 312
Cdd:cd00773   156 LLEDREEYIERLIDKLDK-----------------------------------------------------EALAHLEKL 182

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 313 FEYLTLFGIADKISFDLSLARGLDYYTGVIYEAVLLQTPTQageeplnvGSVAAGGRYDGLVGMFDpkGHKVPCVGLSIG 392
Cdd:cd00773   183 LDYLEALGVDIKYSIDLSLVRGLDYYTGIVFEAVADGLGAQ--------GSIAGGGRYDGLLEEFG--GEDVPAVGFAIG 252


                  ....*....
gi 1391723599 393 VERIFYIVE 401
Cdd:cd00773   253 LERLLLALE 261
hisS TIGR00442
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ...
 64-498 7.76e-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: 293.62  E-value: 7.76e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599  64 KTPKGTRDLSPQHMVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSGL----MYDLKDQGGELLSLRYDLT 139
Cdd:TIGR00442   1 QKPRGTRDFLPEEMIKWQYIEETIREVFERYGFKEIRTPIFEYTELFKRKVGEETDIvskeMYTFKDKGGRSLTLRPEGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 140 VPFARYLAMNK---VKKMKRYHVGKVWRRESPtivQ-GRYREFCQCDFDIAGQFDPMIpDAECLKIMCEILSGLQLGDFL 215
Cdd:TIGR00442  81 APVARAVIENKlllPKPFKLYYIGPMFRYERP---QkGRYRQFHQFGVEVIGSDSPLA-DAEIIALAADILKELGLKDFT 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 216 IKVNDRRIVDGMFAvcgvpesKFRAICSSIDK-LDKMAWKDVRHEMVVKKGLAPEVADRIGDYVQchggvslveqmfQDP 294
Cdd:TIGR00442 157 LEINSLGILEGRLE-------YREALIRYLDKhKDKLGEDSVRRLEKNPLRILDSKNEKIQELLK------------NAP 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 295 RLSQNKQAlEGLGDLKLLFEYLTLFGIadKISFDLSLARGLDYYTGVIYEAVLLQTPTQageeplnvGSVAAGGRYDGLV 374
Cdd:TIGR00442 218 KILDFLCE-ESRAHFEELKELLDALGI--PYKIDPSLVRGLDYYTGTVFEFVTDDLGAQ--------GSICGGGRYDGLV 286

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 375 GMFDpkGHKVPCVGLSIGVERIFYIVEQRmktKGEKVRTTETQVFVATPQKNFLQERLKLIAELWDSGIKAEMLYKNNpK 454
Cdd:TIGR00442 287 EELG--GPPTPAVGFAIGIERLILLLEEL---GLIPPPSKKPDVYVVPLGEEAELEALKLAQKLRKAGIRVEVDLGGR-K 360

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 1391723599 455 LLTQLHYCESTGIPLVVIIGEQELKEGVIKIRSVASREEVAIKR 498
Cdd:TIGR00442 361 LKKQLKYADKLGARFALIIGEDELENGTVTLKDLETGEQETVPL 404
tRNA-synt_His pfam13393
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ...
 68-396 1.56e-38

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: 142.72  E-value: 1.56e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599  68 GTRDLSPQHMVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSGLMYDLKDQGGELLSLRYDLTVPFARYLA 147
Cdd:pfam13393   1 GIRDLLPPEARRIEELRRRLLDLFRSWGYELVMPPLLEYLDSLLTGTGADLDQTFKLVDQSGRLLGLRADITPQVARIDA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 148 --MNKVKKMKRYHVGKVWRRESPTIvqGRYREFCQCDFDIAGQFDPMiPDAECLKIMCEILSGLQLGDFLIKVNDRRIVD 225
Cdd:pfam13393  81 hrLNRPGPLRLCYAGSVLRTRPKGL--GRSREPLQVGAELIGHAGIE-ADAEIISLLLEALAAAGVPGVTLDLGHVGLVR 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 226 GMFAVCGVPESKFRAICSSIDKLDkmaWKDVRhEMVVKKGLAPEVADRIGDYVQCHGGVSLVEQMFQdpRLSQNKQALEG 305
Cdd:pfam13393 158 ALLEAAGLSEALEEALRAALQRKD---AAELA-ELAAEAGLPPALRRALLALPDLYGGPEVLDEARA--ALPGLPALQEA 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 306 LGDLKLLFEYLTLFGIADKISFDLSLARGLDYYTGVIYEAVLLQTPtqageeplnvGSVAAGGRYDGLVGMFdpkGHKVP 385
Cdd:pfam13393 232 LDELEALAALLEALGDGVRLTFDLAELRGYEYYTGIVFAAYAPGVG----------EPLARGGRYDDLGAAF---GRARP 298

                         330
                  ....*....|.
gi 1391723599 386 CVGLSIGVERI 396
Cdd:pfam13393 299 ATGFSLDLEAL 309
 
Name Accession Description Interval E-value
PLN02972 PLN02972
Histidyl-tRNA synthetase
 12-510 0e+00

Histidyl-tRNA synthetase


Pssm-ID: 215525 [Multi-domain]  Cd Length: 763  Bit Score: 540.24  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599  12 WASLLSQLLRPPCASCTGAVRcqsqgeeslQVAEAVLTSQLKahqEKPnfiiKTPKGTRDLSPQHMVVREKILDLVISCF 91
Cdd:PLN02972  292 WATQLLLLFDPKCPGFDSLVD---------KVKEIVESNEVR---RLP----KIPKGTRDFAKEQMAIREKAFSIITSVF 355

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599  92 KRHGAKGMDTPAFELKETLTEKYGEDSGLMYDLKDQGGELLSLRYDLTVPFARYLAMNKVKKMKRYHVGKVWRRESPTiv 171
Cdd:PLN02972  356 KRHGATALDTPVFELRETLMGKYGEDSKLIYDLADQGGELCSLRYDLTVPFARYVAMNGITSFKRYQIAKVYRRDNPS-- 433

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 172 QGRYREFCQCDFDIAGQFDPMIPDAECLKIMCEILSGLQLGDFLIKVNDRRIVDGMFAVCGVPESKFRAICSSIDKLDKM 251
Cdd:PLN02972  434 KGRYREFYQCDFDIAGVYEPMGPDFEIIKVLTELLDELDIGTYEVKLNHRKLLDGMLEICGVPPEKFRTICSSIDKLDKQ 513

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 252 AWKDVRHEMVVKKGLAPEVADRIGDYVQCHGG-VSLVEQMFQ-DPRLSQNKQALEGLGDLKLLFEYLTLFGIADKISFDL 329
Cdd:PLN02972  514 SFEQVKKEMVEEKGLSNETADKIGNFVKERGPpLELLSKLRQeGSEFLGNASSRAALDELEIMFKALEKSKAIGKIVFDL 593

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 330 SLARGLDYYTGVIYEAVLLQTptqageeplNVGSVAAGGRYDGLVGMFDPKghKVPCVGLSIGVERIFYIVEQRMKTKGE 409
Cdd:PLN02972  594 SLARGLDYYTGVIYEAVFKGA---------QVGSIAAGGRYDNLVGMFSGK--QVPAVGVSLGIERVFAIMEQQEEEKSQ 662

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 410 KVRTTETQVFVATPQKNFLQERLKLIAELWDSGIKAEmlYKNNPKLLTQLHYCESTGIPLVVIIGEQELKEGVIKIRSVA 489
Cdd:PLN02972  663 VIRPTETEVLVSIIGDDKLALAAELVSELWNAGIKAE--YKVSTRKAKHLKRAKESGIPWMVLVGEKELSKGFVKLKNLE 740

                         490       500
                  ....*....|....*....|.
gi 1391723599 490 SREEVAIKRENFVAEIQKRLS 510
Cdd:PLN02972  741 AGVEEEVDRTCFVQELKAELL 761
HisS COG0124
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ...
 63-511 8.59e-115

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: 345.57  E-value: 8.59e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599  63 IKTPKGTRDLSPQHMVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSG--LMYDLKDQGGELLSLRYDLTV 140
Cdd:COG0124     4 IQAPRGTRDILPEESAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKIGEDIVekEMYTFEDRGGRSLTLRPEGTA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 141 PFARYLAMNK---VKKMKRYHVGKVWRRESPtivQ-GRYREFCQCDFDIAGQFDPMIpDAECLKIMCEILSGLQLGDFLI 216
Cdd:COG0124    84 PVARAVAEHGnelPFPFKLYYIGPVFRYERP---QkGRYRQFHQFGVEVIGSDSPLA-DAEVIALAADLLKALGLKDFTL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 217 KVNDRrivdgmfavcGVPESKFRAICSSIDKLDKMAWKDVrhemvvkkgLAPEVADRIG-----DYVQCHGGV--SLVEQ 289
Cdd:COG0124   160 EINSR----------GLPEERAEALLRYLDKLDKIGHEDV---------LDEDSQRRLEtnplrAILDSKGPDcqEVLAD 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 290 MfqdPRLSQNKqALEGLGDLKLLFEYLTLFGIadKISFDLSLARGLDYYTGVIYEAVLLQTPTQageeplnvGSVAAGGR 369
Cdd:COG0124   221 A---PKLLDYL-GEEGLAHFEEVLELLDALGI--PYVIDPRLVRGLDYYTGTVFEIVTDGLGAQ--------GSVCGGGR 286

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 370 YDGLVGMFDpkGHKVPCVGLSIGVERIFYIVEQRmktKGEKVRTTETQVFVATPQKNFLQERLKLIAELWDSGIKAEMLY 449
Cdd:COG0124   287 YDGLVEQLG--GPPTPAVGFAIGLERLLLLLEEL---GLLPAAEPPPDVYVVPLGEEARAEALKLAQELRAAGIRVELDL 361

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1391723599 450 KNNpKLLTQLHYCESTGIPLVVIIGEQELKEGVIKIRSVASREEVAIKRENFVAEIQKRLSE 511
Cdd:COG0124   362 GGR-KLKKQLKYADKSGAPFVLILGEDELANGTVTLKDLATGEQETVPLDELVEYLKELLAE 422
HisRS-like_core cd00773
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ...
 77-401 1.34e-97

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: 295.67  E-value: 1.34e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599  77 MVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSG-LMYDLKDQGGELLSLRYDLTVPFARYLAMNKVKK-- 153
Cdd:cd00773     2 AALRRYIEDTLREVFERYGYEEIDTPVFEYTELFLRKSGDEVSkEMYRFKDKGGRDLALRPDLTAPVARAVAENLLSLpl 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 154 -MKRYHVGKVWRRESPTivQGRYREFCQCDFDIAGqFDPMIPDAECLKIMCEILSGLQLGDFLIKVNDRRIVDGmfaVCG 232
Cdd:cd00773    82 pLKLYYIGPVFRYERPQ--KGRYREFYQVGVEIIG-SDSPLADAEVIALAVEILEALGLKDFQIKINHRGILDG---IAG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 233 VPESKFRAICSSIDKLDKmawkdvrhemvvkkglapevadrigdyvqchggvslveqmfqdprlsqnkqalEGLGDLKLL 312
Cdd:cd00773   156 LLEDREEYIERLIDKLDK-----------------------------------------------------EALAHLEKL 182

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 313 FEYLTLFGIADKISFDLSLARGLDYYTGVIYEAVLLQTPTQageeplnvGSVAAGGRYDGLVGMFDpkGHKVPCVGLSIG 392
Cdd:cd00773   183 LDYLEALGVDIKYSIDLSLVRGLDYYTGIVFEAVADGLGAQ--------GSIAGGGRYDGLLEEFG--GEDVPAVGFAIG 252


                  ....*....
gi 1391723599 393 VERIFYIVE 401
Cdd:cd00773   253 LERLLLALE 261
hisS TIGR00442
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ...
 64-498 7.76e-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: 293.62  E-value: 7.76e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599  64 KTPKGTRDLSPQHMVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSGL----MYDLKDQGGELLSLRYDLT 139
Cdd:TIGR00442   1 QKPRGTRDFLPEEMIKWQYIEETIREVFERYGFKEIRTPIFEYTELFKRKVGEETDIvskeMYTFKDKGGRSLTLRPEGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 140 VPFARYLAMNK---VKKMKRYHVGKVWRRESPtivQ-GRYREFCQCDFDIAGQFDPMIpDAECLKIMCEILSGLQLGDFL 215
Cdd:TIGR00442  81 APVARAVIENKlllPKPFKLYYIGPMFRYERP---QkGRYRQFHQFGVEVIGSDSPLA-DAEIIALAADILKELGLKDFT 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 216 IKVNDRRIVDGMFAvcgvpesKFRAICSSIDK-LDKMAWKDVRHEMVVKKGLAPEVADRIGDYVQchggvslveqmfQDP 294
Cdd:TIGR00442 157 LEINSLGILEGRLE-------YREALIRYLDKhKDKLGEDSVRRLEKNPLRILDSKNEKIQELLK------------NAP 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 295 RLSQNKQAlEGLGDLKLLFEYLTLFGIadKISFDLSLARGLDYYTGVIYEAVLLQTPTQageeplnvGSVAAGGRYDGLV 374
Cdd:TIGR00442 218 KILDFLCE-ESRAHFEELKELLDALGI--PYKIDPSLVRGLDYYTGTVFEFVTDDLGAQ--------GSICGGGRYDGLV 286

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 375 GMFDpkGHKVPCVGLSIGVERIFYIVEQRmktKGEKVRTTETQVFVATPQKNFLQERLKLIAELWDSGIKAEMLYKNNpK 454
Cdd:TIGR00442 287 EELG--GPPTPAVGFAIGIERLILLLEEL---GLIPPPSKKPDVYVVPLGEEAELEALKLAQKLRKAGIRVEVDLGGR-K 360

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 1391723599 455 LLTQLHYCESTGIPLVVIIGEQELKEGVIKIRSVASREEVAIKR 498
Cdd:TIGR00442 361 LKKQLKYADKLGARFALIIGEDELENGTVTLKDLETGEQETVPL 404
PRK12420 PRK12420
histidyl-tRNA synthetase; Provisional
 64-497 1.13e-84

histidyl-tRNA synthetase; Provisional


Pssm-ID: 237097 [Multi-domain]  Cd Length: 423  Bit Score: 268.14  E-value: 1.13e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599  64 KTPKGTRDLSPQHMVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYG---EDSGLMYDLKDQGGELLSLRYDLTV 140
Cdd:PRK12420    5 RNVKGTKDYLPEEQVLRNKIKRALEDVFERYGCKPLETPTLNMYELMSSKYGggdEILKEIYTLTDQGKRDLALRYDLTI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 141 PFARYLAMNKVKKM--KRYHVGKVWrRESPtIVQGRYREFCQCDFDIAGQFDPMiPDAECLKIMCEILSGLQLgDFLIKV 218
Cdd:PRK12420   85 PFAKVVAMNPNIRLpfKRYEIGKVF-RDGP-IKQGRFREFIQCDVDIVGVESVM-AEAELMSMAFELFRRLNL-EVTIQY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 219 NDRRIVDGMFAVCGVPESKFRAICSSIDKLDKMAWKDVRHEmVVKKGLAPEVADRIGDYVQCHGGVSLVEqmFQDPRLSQ 298
Cdd:PRK12420  161 NNRKLLNGILQAIGIPTELTSDVILSLDKIEKIGIDGVRKD-LLERGISEEMADTICNTVLSCLQLSIAD--FKEAFNNP 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 299 NKQalEGLGDLKLLFEYLTLFGIADKISFDLSLARGLDYYTGVIYEAVLlqtptqagEEPLNVGSVAAGGRYDGLVGMFD 378
Cdd:PRK12420  238 LVA--EGVNELQQLQQYLIALGINENCIFNPFLARGLTMYTGTVYEIFL--------KDGSITSSIGSGGRYDNIIGAFR 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 379 PKGHKVPCVGLSIGVERIFYIVEQRmktkgekVRTTETQVFVATPQKNFLQErLKLIAELW-DSGIKAEMLYKNNpKLLT 457
Cdd:PRK12420  308 GDDMNYPTVGISFGLDVIYTALSQK-------ETISSTADVFIIPLGTELQC-LQIAQQLRsTTGLKVELELAGR-KLKK 378

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 1391723599 458 QLHYCESTGIPLVVIIGEQELKEGVIKIRSVASREEVAIK 497
Cdd:PRK12420  379 ALNYANKENIPYVLIIGEEEVSTGTVMLRNMKEGSEVKVP 418
PLN02530 PLN02530
histidine-tRNA ligase
 2-497 6.74e-50

histidine-tRNA ligase


Pssm-ID: 178145 [Multi-domain]  Cd Length: 487  Bit Score: 178.01  E-value: 6.74e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599   2 PLLGLLPRRAWASLLSQLLRPPCASCTGAvrcqSQGEESLQVAEAVLtsqlkahQEKPNFIIKT--PKGTRDLSPQHMVV 79
Cdd:PLN02530   18 PSLPLSSRCSFLLSASSPRGGRCAASAAA----GGGRSGGTTAPPSV-------QEDGKPKIDVnpPKGTRDFPPEDMRL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599  80 REKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGED-SGLMYDLKDQGGELLSLRYDLTVPFARyLAMNKVKKM---- 154
Cdd:PLN02530   87 RNWLFDHFREVSRLFGFEEVDAPVLESEELYIRKAGEEiTDQLYNFEDKGGRRVALRPELTPSLAR-LVLQKGKSLslpl 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 155 KRYHVGKVWRRESPTivQGRYREFCQCDFDIAGqFDPMIPDAECLKIMCEILS--GLQLGDFLIKVNDRRIVDGMFAVCG 232
Cdd:PLN02530  166 KWFAIGQCWRYERMT--RGRRREHYQWNMDIIG-VPGVEAEAELLAAIVTFFKrvGITSSDVGIKVSSRKVLQAVLKSYG 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 233 VPESKFRAICSSIDKLDKMAWKDVRHEMVvKKGLAPEVADRIGDYVQCHGGVSLVEQMFQDPrlsqnkqalEGLGDLKLL 312
Cdd:PLN02530  243 IPEESFAPVCVIVDKLEKLPREEIEKELD-TLGVSEEAIEGILDVLSLKSLDDLEALLGADS---------EAVADLKQL 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 313 FEYLTLFGIADKISFDLSLARGLDYYTGVIYEAVllqtpTQAGEeplnVGSVAAGGRYDGLVGMFDpkGHKVPCVGLSIG 392
Cdd:PLN02530  313 FSLAEAYGYQDWLVFDASVVRGLAYYTGIVFEGF-----DRAGK----LRAICGGGRYDRLLSTFG--GEDTPACGFGFG 381

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 393 --VerifyIVEqRMKTKG---EKVRTTETQVFvatPQKNFLQ-ERLKLIAELWDSGIKAEMLYKNNpKLLTQLHYCESTG 466
Cdd:PLN02530  382 daV-----IVE-LLKEKGllpELPHQVDDVVF---ALDEDLQgAAAGVASRLREKGRSVDLVLEPK-KLKWVFKHAERIG 451

                         490       500       510
                  ....*....|....*....|....*....|.
gi 1391723599 467 IPLVVIIGEQELKEGVIKIRSVASREEVAIK 497
Cdd:PLN02530  452 AKRLVLVGASEWERGMVRVKDLSSGEQTEVK 482
hisZ_biosyn_reg TIGR00443
ATP phosphoribosyltransferase, regulatory subunit; Apparant second copies of histidyl-tRNA ...
 70-396 3.06e-49

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: 171.64  E-value: 3.06e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599  70 RDLSPQHMVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSGLMYDLKDQGGELLSLRYDLTVPFARYLAmn 149
Cdd:TIGR00443   1 RDLLPEEAARKEEIERQLQDVFRSWGYQEIITPTLEYLDTLSAGSGILNEDLFKLFDQLGRVLGLRPDMTAPIARLVS-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 150 kvKKMKRYH-------VGKVWRRESPTIvqGRYREFCQCDFDIAGQfDPMIPDAECLKIMCEILSGLQLGDFLIKVNDRR 222
Cdd:TIGR00443  79 --TRLRDRPlplrlcyAGNVFRTNESGG--GRSREFTQAGVELIGA-GGPAADAEVIALLIEALKALGLKDFKIELGHVG 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 223 IVDGMFAVCGVPESKFRAICSSIDKLDKMAWKdvrhEMVVKKGLAPEVADRIGDYVQCHGGVSLVEQMFQdpRLSQNKQA 302
Cdd:TIGR00443 154 LVRALLEEAGLPEEAREALREALARKDLVALE----ELVAELGLSPEVRERLLALPRLRGDGEEVLEEAR--ALAGSETA 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 303 LEGLGDLKLLFEYLTLFGIADKISFDLSLARGLDYYTGVIYEAVLlqtpTQAGEeplnvgSVAAGGRYDGLVGMFdpkGH 382
Cdd:TIGR00443 228 EAALDELEAVLELLEARGVEEYISLDLGLVRGYHYYTGLIFEGYA----PGLGA------PLAGGGRYDELLGRF---GR 294

                         330
                  ....*....|....
gi 1391723599 383 KVPCVGLSIGVERI 396
Cdd:TIGR00443 295 PLPATGFALNLERL 308
HisZ COG3705
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism];
80-396 2.78e-44

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


Pssm-ID: 442919 [Multi-domain]  Cd Length: 312  Bit Score: 158.42  E-value: 2.78e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599  80 REKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSGL-MYDLKDQGGELLSLRYDLTVPFARYLA--MNKVKKMKR 156
Cdd:COG3705     8 KEELRRRLLDVFRSWGYELVEPPLLEYLDSLLTGSGADLDLqTFKLVDQLGRTLGLRPDMTPQVARIAAtrLANRPGPLR 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 157 Y-HVGKVWR-RESPtivQGRYREFCQC------DFDIAGqfdpmipDAECLKIMCEILSGLQLGDFLIKVNDRRIVDGMF 228
Cdd:COG3705    88 LcYAGNVFRtRPSG---LGRSREFLQAgaeligHAGLEA-------DAEVIALALEALKAAGLEDFTLDLGHVGLFRALL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 229 AVCGVPESKFRAICSSIDKLDkmaWKDVRhEMVVKKGLAPEVADRIGDYVQCHGGVSLVEQMFQdprLSQNKQALEGLGD 308
Cdd:COG3705   158 EALGLSEEQREELRRALARKD---AVELE-ELLAELGLSEELAEALLALPELYGGEEVLARARA---LLLDAAIRAALDE 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 309 LKLLFEYLTLFGIADKISFDLSLARGLDYYTGVIYEAVllqTPTQAGEeplnvgsVAAGGRYDGLVGMFdpkGHKVPCVG 388
Cdd:COG3705   231 LEALAEALAARGPDVRLTFDLSELRGYDYYTGIVFEAY---APGVGDP-------LARGGRYDGLLAAF---GRARPATG 297


                  ....*...
gi 1391723599 389 LSIGVERI 396
Cdd:COG3705   298 FSLDLDRL 305
hisZ PRK12292
ATP phosphoribosyltransferase regulatory subunit; Provisional
 66-447 4.45e-43

ATP phosphoribosyltransferase regulatory subunit; Provisional


Pssm-ID: 237043 [Multi-domain]  Cd Length: 391  Bit Score: 157.34  E-value: 4.45e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599  66 PKGTRDLSPQHMVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSGL-MYDLKDQG-GELLSLRYDLTVPFA 143
Cdd:PRK12292    6 PEGIRDLLPEEARKIEEIRRRLLDLFRRWGYEEVITPTLEYLDTLLAGGGAILDLrTFKLVDQLsGRTLGLRPDMTAQIA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 144 RyLAMNKVKKMKR-----YHvGKVWR---RESptivqGRYREFCQCDFDIAGqFDPMIPDAECLKIMCEILSGLQLGDFL 215
Cdd:PRK12292   86 R-IAATRLANRPGplrlcYA-GNVFRaqeRGL-----GRSREFLQSGVELIG-DAGLEADAEVILLLLEALKALGLPNFT 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 216 IKVNDRRIVDGMFAVCGVPESKFRAICSSIDKLDKMAWKdvrhEMVvkKGLAPEVADRIGDYVQCHGGVSLVEQMfqdPR 295
Cdd:PRK12292  158 LDLGHVGLFRALLEAAGLSEELEEVLRRALANKDYVALE----ELV--LDLSEELRDALLALPRLRGGREVLEEA---RK 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 296 LSQNKQALEGLGDLKLLFEYLTLFGIADKISFDLSLARGLDYYTGVIYEAVllqtptqAGEEPLNVGSvaaGGRYDGLVG 375
Cdd:PRK12292  229 LLPSLPIKRALDELEALAEALEKYGYGIPLSLDLGLLRHLDYYTGIVFEGY-------VDGVGNPIAS---GGRYDDLLG 298

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1391723599 376 MFdpkGHKVPCVGLSIGVERifyIVEQRMKTKgekvrTTETQVFVATPQKNFLQERLKLIAELWDSGIKAEM 447
Cdd:PRK12292  299 RF---GRARPATGFSLDLDR---LLELQLELP-----VEARKDLVIAPDSEALAAALAAAQELRKKGEIVVL 359
tRNA-synt_His pfam13393
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ...
 68-396 1.56e-38

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: 142.72  E-value: 1.56e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599  68 GTRDLSPQHMVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSGLMYDLKDQGGELLSLRYDLTVPFARYLA 147
Cdd:pfam13393   1 GIRDLLPPEARRIEELRRRLLDLFRSWGYELVMPPLLEYLDSLLTGTGADLDQTFKLVDQSGRLLGLRADITPQVARIDA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 148 --MNKVKKMKRYHVGKVWRRESPTIvqGRYREFCQCDFDIAGQFDPMiPDAECLKIMCEILSGLQLGDFLIKVNDRRIVD 225
Cdd:pfam13393  81 hrLNRPGPLRLCYAGSVLRTRPKGL--GRSREPLQVGAELIGHAGIE-ADAEIISLLLEALAAAGVPGVTLDLGHVGLVR 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 226 GMFAVCGVPESKFRAICSSIDKLDkmaWKDVRhEMVVKKGLAPEVADRIGDYVQCHGGVSLVEQMFQdpRLSQNKQALEG 305
Cdd:pfam13393 158 ALLEAAGLSEALEEALRAALQRKD---AAELA-ELAAEAGLPPALRRALLALPDLYGGPEVLDEARA--ALPGLPALQEA 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 306 LGDLKLLFEYLTLFGIADKISFDLSLARGLDYYTGVIYEAVLLQTPtqageeplnvGSVAAGGRYDGLVGMFdpkGHKVP 385
Cdd:pfam13393 232 LDELEALAALLEALGDGVRLTFDLAELRGYEYYTGIVFAAYAPGVG----------EPLARGGRYDDLGAAF---GRARP 298

                         330
                  ....*....|.
gi 1391723599 386 CVGLSIGVERI 396
Cdd:pfam13393 299 ATGFSLDLEAL 309
syh CHL00201
histidine-tRNA synthetase; Provisional
 63-507 1.35e-28

histidine-tRNA synthetase; Provisional


Pssm-ID: 164576 [Multi-domain]  Cd Length: 430  Bit Score: 117.69  E-value: 1.35e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599  63 IKTPKGTRDLSPQHMVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSGL----MYDLKDQGGELLSLRYDL 138
Cdd:CHL00201    4 IQAIRGTKDILPDEINYWQFIHDKALTLLSLANYSEIRTPIFENSSLYDRGIGETTDIvnkeMYRFTDRSNRDITLRPEG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 139 TVPFARYLAMNKVKKMKR----YHVGKVWRRESPTivQGRYREFCQCDFDIAGQFDPMiPDAECLKIMCEILSGLQLGDF 214
Cdd:CHL00201   84 TAGIVRAFIENKMDYHSNlqrlWYSGPMFRYERPQ--SGRQRQFHQLGIEFIGSIDAR-ADTEVIHLAMQIFNELQVKNL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 215 LIKVN------DRRIVdgmfavcgvpESKFRAICSSI-DKLDKmawkDVRHEMVVKkglaP-EVADRIGDYVQchggvsl 286
Cdd:CHL00201  161 ILDINsigkleDRQSY----------QLKLVEYLSQYqDDLDT----DSQNRLYSN----PiRILDSKNLKTQ------- 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 287 vEQMFQDPRLSQ--NKQALEGLGDLkllFEYLTLFGIADKISFdlSLARGLDYYTGVIYEavlLQTPTQAGEEplnvgSV 364
Cdd:CHL00201  216 -EILDGAPKISDflSLESTEHFYDV---CTYLNLLNIPYKINY--KLVRGLDYYNDTAFE---IKTLSSNGQD-----TI 281

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 365 AAGGRYDGLVGMFDpkGHKVPCVGLSIGVERIFYIVEQRMKTKGEKVrttetQVFVATPQKNFLQERLKLIAELWDSGIK 444
Cdd:CHL00201  282 CGGGRYDSLIHQLG--GPKTPAVGCAIGLERLLLIAKDNIILPKQSI-----DVYIATQGLKAQKKGWEIIQFLEKQNIK 354

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1391723599 445 AEmLYKNNPKLLTQLHYCESTGIPLVVIIGEQELKEGVIKIRSVASREEVAIKRENFVAEIQK 507
Cdd:CHL00201  355 FE-LDLSSSNFHKQIKQAGKKRAKACIILGDNEIMDNCITIKWLDEQVQENAQYSNFKQEISY 416
HisRS_anticodon cd00859
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases ...
 415-506 4.62e-28

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: 107.24  E-value: 4.62e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 415 ETQVFVATPQKNFLQERLKLIAELWDSGIKAEMLYKNnPKLLTQLHYCESTGIPLVVIIGEQELKEGVIKIRSVASREEV 494
Cdd:cd00859     1 EVDVYVVPLGEGALSEALELAEQLRDAGIKAEIDYGG-RKLKKQFKYADRSGARFAVILGEDELAAGVVTVKDLETGEQE 79

                          90
                  ....*....|..
gi 1391723599 495 AIKRENFVAEIQ 506
Cdd:cd00859    80 TVALDELVEELK 91
hisZ PRK12295
ATP phosphoribosyltransferase regulatory subunit; Provisional
 83-396 1.32e-20

ATP phosphoribosyltransferase regulatory subunit; Provisional


Pssm-ID: 183413 [Multi-domain]  Cd Length: 373  Bit Score: 93.46  E-value: 1.32e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599  83 ILDLVISCFKRHGAKGMDTPAFELKETLTEKYGED-SGLMYDLKDQGGELLSLRYDLTVPFAR-YLAMNKVKKMKRYHVG 160
Cdd:PRK12295   10 AAEALLASFEAAGAVRVDPPILQPAEPFLDLSGEDiRRRIFVTSDENGEELCLRPDFTIPVCRrHIATAGGEPARYAYLG 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 161 KVWRRESptivqGRYREFCQCDFDIAGQFDPMIPDAECLKIMCEILSGLQLGDFLIKVNDRRIVDGMFAVCGVPE----- 235
Cdd:PRK12295   90 EVFRQRR-----DRASEFLQAGIESFGRADPAAADAEVLALALEALAALGPGDLEVRLGDVGLFAALVDALGLPPgwkrr 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 236 --------SKFRAIcssIDKL-------------------DKMAWKDVRHEMVVKKGLAP-------EVADRIGDYVQCH 281
Cdd:PRK12295  165 llrhfgrpRSLDAL---LARLagprvdpldehagvlaalaDEAAARALVEDLMSIAGISPvggrspaEIARRLLEKAALA 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 282 GGVSLVEQMFQ--------DPRLSQNKQALEGL-GDLKL-------LFE----YLTLFGIA-DKISFDLSLARGLDYYTG 340
Cdd:PRK12295  242 AAARLPAEALAvlerflaiSGPPDAALAALRALaADAGLdldaaldRFEarlaALAARGIDlERLRFSASFGRPLDYYTG 321

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1391723599 341 VIYEAvllqTPTQAGEEPLnvgsvAAGGRYDGLVGMFDpKGHKVPCVGLSIGVERI 396
Cdd:PRK12295  322 FVFEI----RAAGNGDPPL-----AGGGRYDGLLTRLG-AGEPIPAVGFSIWLDRL 367
HGTP_anticodon pfam03129
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ...
 417-508 8.59e-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: 78.40  E-value: 8.59e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 417 QVFVATPQKN---FLQERLKLIAELWDSGIKAEmLYKNNPKLLTQLHYCESTGIPLVVIIGEQELKEGVIKIRSVASREE 493
Cdd:pfam03129   1 QVVVIPLGEKaeeLEEYAQKLAEELRAAGIRVE-LDDRNESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQ 79

                          90
                  ....*....|....*
gi 1391723599 494 VAIKRENFVAEIQKR 508
Cdd:pfam03129  80 ETVSLDELVEKLKEL 94
HGTP_anticodon2 pfam12745
Anticodon binding domain of tRNAs; This is an HGTP_anticodon binding domain, found largely on ...
 418-508 6.25e-07

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: 50.68  E-value: 6.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 418 VFVATPQKNFL-QERLKLIAELWDSGIKAEMLYKNNPKLLTQLHYCESTGIPLVVIIGEQEL----KEGVIKIRSVASRE 492
Cdd:pfam12745   8 VLVASFDASILrTTGVEILQELWAHGISADLAVDASYSPEDLVSRARDDGVSWIVIIKQQNKssdsKYKPLKVKNLLRKE 87

                          90       100
                  ....*....|....*....|
gi 1391723599 493 EVAIKRENFVA----EIQKR 508
Cdd:pfam12745  88 DVDLDSDELVSwlrgEIRER 107
PRK12421 PRK12421
ATP phosphoribosyltransferase regulatory subunit; Provisional
 66-396 2.30e-05

ATP phosphoribosyltransferase regulatory subunit; Provisional


Pssm-ID: 237098  Cd Length: 392  Bit Score: 46.50  E-value: 2.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599  66 PKGTRDLSP---QHM-VVREKILDLVIScfkrHGAKGMDTPAFELKETLTEKYGEDSGLM-YDLKDQ-GGELLSLRYDLT 139
Cdd:PRK12421   10 PDGVADVLPeeaQKIeRLRRRLLDLFAS----RGYQLVMPPLIEYLESLLTGAGQDLKLQtFKLIDQlSGRLMGVRADIT 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 140 VPFARYLA-MNKVKKMKRY-HVGKVWRrespTIVQG--RYREFCQCDFDIAGQfDPMIPDAECLKIMCEILSGLQLGDFL 215
Cdd:PRK12421   86 PQVARIDAhLLNREGVARLcYAGSVLH----TLPQGlfGSRTPLQLGAELYGH-AGIEADLEIIRLMLGLLRNAGVPALH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 216 IKVNDRRIVDGMFAVCGVPESKFRAIcssidkLDKMAWKDVR--HEMVVKKGLAPEVADRIGDYVQCHGGV-SLVEQMFQ 292
Cdd:PRK12421  161 LDLGHVGIFRRLAELAGLSPEEEEEL------FDLLQRKALPelAEVCQNLGVGSDLRRMFYALARLNGGLeALDRALSV 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 293 DPRlsQNKQALEGLGDLKLLFEYLTLFGIADKISFDLSLARGLDYYTGVIYeAVLLQTPTQAgeeplnvgsVAAGGRYDG 372
Cdd:PRK12421  235 LAL--QDAAIRQALDELKTLAAHLKNRWPELPVSIDLAELRGYHYHTGLVF-AAYIPGRGQA---------LARGGRYDG 302

                         330       340
                  ....*....|....*....|....
gi 1391723599 373 LVGMFdpkGHKVPCVGLSIGVERI 396
Cdd:PRK12421  303 IGEAF---GRARPATGFSMDLKEL 323
ProRS_anticodon_short cd00861
ProRS Prolyl-anticodon binding domain, short version found predominantly in bacteria. ProRS ...
 466-506 4.50e-04

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


Pssm-ID: 238438 [Multi-domain]  Cd Length: 94  Bit Score: 39.50  E-value: 4.50e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1391723599 466 GIPLVVIIGEQELKEGVIKIRSVASREEVAIKRENFVAEIQ 506
Cdd:cd00861    54 GIPYRIVVGKKSAAEGIVEIKVRKTGEKEEISIDELLEFLQ 94
PRK09194 PRK09194
prolyl-tRNA synthetase; Provisional
 466-510 5.02e-03

prolyl-tRNA synthetase; Provisional


Pssm-ID: 236405 [Multi-domain]  Cd Length: 565  Bit Score: 39.30  E-value: 5.02e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1391723599 466 GIPLVVIIGEQELKEGVIKIRSVASREEVAIKRENFVAEIQKRLS 510
Cdd:PRK09194  521 GIPHRIVVGDRGLAEGIVEYKDRRTGEKEEVPVDELVEFLKALKK 565
ThrRS_anticodon cd00860
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases ...
 416-506 9.05e-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: 35.56  E-value: 9.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723599 416 TQVFVATPQKNFLQERLKLIAELWDSGIKAEMLYKNNpKL-----LTQLHycestGIPLVVIIGEQELKEGVIKIRSVAS 490
Cdd:cd00860     2 VQVVVIPVTDEHLDYAKEVAKKLSDAGIRVEVDLRNE-KLgkkirEAQLQ-----KIPYILVVGDKEVETGTVSVRTRDG 75

                          90
                  ....*....|....*.
gi 1391723599 491 REEVAIKRENFVAEIQ 506
Cdd:cd00860    76 GDLGSMSLDEFIEKLK 91
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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