|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02972 |
PLN02972 |
Histidyl-tRNA synthetase |
12-509 |
0e+00 |
|
Histidyl-tRNA synthetase
Pssm-ID: 215525 [Multi-domain] Cd Length: 763 Bit Score: 535.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 12 WAALLSQLLRPPCASCTGAVrcqSQVAEAVLTSQLKahqEKPnfiiKIPKGTRDLSPQHMVVREKILDLVISCFKRHGAK 91
Cdd:PLN02972 292 WATQLLLLFDPKCPGFDSLV---DKVKEIVESNEVR---RLP----KIPKGTRDFAKEQMAIREKAFSIITSVFKRHGAT 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 92 GMDTPAFELKETLTEKYGEDSGLMYDLKDQGGELLSLRYDLTypssltdlceVPFARYLAMNKVKKMKRYHVGKVWRRES 171
Cdd:PLN02972 362 ALDTPVFELRETLMGKYGEDSKLIYDLADQGGELCSLRYDLT----------VPFARYVAMNGITSFKRYQIAKVYRRDN 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 172 PSivQGRYREFCQCDFDIAGQFDPMIPDAECLKIMCEILSGLQLGDFLIKVNDRRIVDGMFAACGVPESKFRAICSSIDK 251
Cdd:PLN02972 432 PS--KGRYREFYQCDFDIAGVYEPMGPDFEIIKVLTELLDELDIGTYEVKLNHRKLLDGMLEICGVPPEKFRTICSSIDK 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 252 LDKMAWKDVRHEMVAKKGLAPEVADRIGDYVQCHGG-VSLVEQMFQ-DPRLSQNKQALEGLEDLKLLFEYLNLFGIAEKI 329
Cdd:PLN02972 510 LDKQSFEQVKKEMVEEKGLSNETADKIGNFVKERGPpLELLSKLRQeGSEFLGNASSRAALDELEIMFKALEKSKAIGKI 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 330 SFDLSLARGLDYYTGVIYEAVLLQTptqageeplNVGSVAAGGRYDGLVGMFDPKghKVPCVGLSIGVERIFYIVEQRMK 409
Cdd:PLN02972 590 VFDLSLARGLDYYTGVIYEAVFKGA---------QVGSIAAGGRYDNLVGMFSGK--QVPAVGVSLGIERVFAIMEQQEE 658
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 410 TKGEKVRTTETQVFVATPQKNFLQERLKLITELWDAGIKAEmlYKNNPKLLTQLHYCESTGIPLVVIIGEQELKEGIIKI 489
Cdd:PLN02972 659 EKSQVIRPTETEVLVSIIGDDKLALAAELVSELWNAGIKAE--YKVSTRKAKHLKRAKESGIPWMVLVGEKELSKGFVKL 736
|
490 500
....*....|....*....|
gi 1622947310 490 RSVASREEVSGSSRNRRDEL 509
Cdd:PLN02972 737 KNLEAGVEEEVDRTCFVQEL 756
|
|
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
57-499 |
6.83e-108 |
|
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: 329.39 E-value: 6.83e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 57 IKIPKGTRDLSPQHMVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSG--LMYDLKDQGGELLSLRYDLTy 134
Cdd:COG0124 4 IQAPRGTRDILPEESAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKIGEDIVekEMYTFEDRGGRSLTLRPEGT- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 135 pssltdlceVPFARYLAMNK---VKKMKRYHVGKVWRRESPsivQ-GRYREFCQCDFDIAGQFDPMIpDAECLKIMCEIL 210
Cdd:COG0124 83 ---------APVARAVAEHGnelPFPFKLYYIGPVFRYERP---QkGRYRQFHQFGVEVIGSDSPLA-DAEVIALAADLL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 211 SGLQLGDFLIKVNDRrivdgmfaacGVPESKFRAICSSIDKLDKMAWKDVrhemvakkgLAPEVADRIG-----DYVQCH 285
Cdd:COG0124 150 KALGLKDFTLEINSR----------GLPEERAEALLRYLDKLDKIGHEDV---------LDEDSQRRLEtnplrAILDSK 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 286 GGV--SLVEQMfqdPRLSQNKqALEGLEDLKLLFEYLNLFGIaeKISFDLSLARGLDYYTGVIYEAVLLQTPTQageepl 363
Cdd:COG0124 211 GPDcqEVLADA---PKLLDYL-GEEGLAHFEEVLELLDALGI--PYVIDPRLVRGLDYYTGTVFEIVTDGLGAQ------ 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 364 nvGSVAAGGRYDGLVGMFDpkGHKVPCVGLSIGVERIFYIVEQRmktKGEKVRTTETQVFVATPQKNFLQERLKLITELW 443
Cdd:COG0124 279 --GSVCGGGRYDGLVEQLG--GPPTPAVGFAIGLERLLLLLEEL---GLLPAAEPPPDVYVVPLGEEARAEALKLAQELR 351
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622947310 444 DAGIKAEMLYKNNpKLLTQLHYCESTGIPLVVIIGEQELKEGIIKIRSVASREEVS 499
Cdd:COG0124 352 AAGIRVELDLGGR-KLKKQLKYADKSGAPFVLILGEDELANGTVTLKDLATGEQET 406
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
71-405 |
8.58e-96 |
|
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: 292.58 E-value: 8.58e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 71 MVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSG-LMYDLKDQGGELLSLRYDLTypssltdlceVPFARY 149
Cdd:cd00773 2 AALRRYIEDTLREVFERYGYEEIDTPVFEYTELFLRKSGDEVSkEMYRFKDKGGRDLALRPDLT----------APVARA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 150 LAMNKVKK---MKRYHVGKVWRRESPSivQGRYREFCQCDFDIAGqFDPMIPDAECLKIMCEILSGLQLGDFLIKVNDRR 226
Cdd:cd00773 72 VAENLLSLplpLKLYYIGPVFRYERPQ--KGRYREFYQVGVEIIG-SDSPLADAEVIALAVEILEALGLKDFQIKINHRG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 227 IVDGmfaACGVPESKFRAICSSIDKLDKmawkdvrhemvakkglapevadrigdyvqchggvslveqmfqdprlsqnkqa 306
Cdd:cd00773 149 ILDG---IAGLLEDREEYIERLIDKLDK---------------------------------------------------- 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 307 lEGLEDLKLLFEYLNLFGIAEKISFDLSLARGLDYYTGVIYEAVLLQTPTQageeplnvGSVAAGGRYDGLVGMFDpkGH 386
Cdd:cd00773 174 -EALAHLEKLLDYLEALGVDIKYSIDLSLVRGLDYYTGIVFEAVADGLGAQ--------GSIAGGGRYDGLLEEFG--GE 242
|
330
....*....|....*....
gi 1622947310 387 KVPCVGLSIGVERIFYIVE 405
Cdd:cd00773 243 DVPAVGFAIGLERLLLALE 261
|
|
| hisS |
TIGR00442 |
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ... |
58-499 |
2.91e-92 |
|
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: 288.61 E-value: 2.91e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 58 KIPKGTRDLSPQHMVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSGL----MYDLKDQGGELLSLRYDLT 133
Cdd:TIGR00442 1 QKPRGTRDFLPEEMIKWQYIEETIREVFERYGFKEIRTPIFEYTELFKRKVGEETDIvskeMYTFKDKGGRSLTLRPEGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 134 ypssltdlceVPFARYLAMNK---VKKMKRYHVGKVWRRESPsivQ-GRYREFCQCDFDIAGQFDPMIpDAECLKIMCEI 209
Cdd:TIGR00442 81 ----------APVARAVIENKlllPKPFKLYYIGPMFRYERP---QkGRYRQFHQFGVEVIGSDSPLA-DAEIIALAADI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 210 LSGLQLGDFLIKVNDRRIVDGMFAacgvpesKFRAICSSIDK-LDKMAWKDVRHEMVAKKGLAPEVADRIGDYVQchggv 288
Cdd:TIGR00442 147 LKELGLKDFTLEINSLGILEGRLE-------YREALIRYLDKhKDKLGEDSVRRLEKNPLRILDSKNEKIQELLK----- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 289 slveqmfQDPRLSQNKQAlEGLEDLKLLFEYLNLFGIaeKISFDLSLARGLDYYTGVIYEAVLLQTPTQageeplnvGSV 368
Cdd:TIGR00442 215 -------NAPKILDFLCE-ESRAHFEELKELLDALGI--PYKIDPSLVRGLDYYTGTVFEFVTDDLGAQ--------GSI 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 369 AAGGRYDGLVGMFDpkGHKVPCVGLSIGVERIFYIVEQRmktKGEKVRTTETQVFVATPQKNFLQERLKLITELWDAGIK 448
Cdd:TIGR00442 277 CGGGRYDGLVEELG--GPPTPAVGFAIGIERLILLLEEL---GLIPPPSKKPDVYVVPLGEEAELEALKLAQKLRKAGIR 351
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1622947310 449 AEMLYKNNpKLLTQLHYCESTGIPLVVIIGEQELKEGIIKIRSVASREEVS 499
Cdd:TIGR00442 352 VEVDLGGR-KLKKQLKYADKLGARFALIIGEDELENGTVTLKDLETGEQET 401
|
|
| tRNA-synt_His |
pfam13393 |
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ... |
62-400 |
2.89e-39 |
|
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: 145.42 E-value: 2.89e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 62 GTRDLSPQHMVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSGLMYDLKDQGGELLSLRYDLTyPSsltdl 141
Cdd:pfam13393 1 GIRDLLPPEARRIEELRRRLLDLFRSWGYELVMPPLLEYLDSLLTGTGADLDQTFKLVDQSGRLLGLRADIT-PQ----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 142 cevpFARYLA--MNKVKKMKRYHVGKVWRRESPSIvqGRYREFCQCDFDIAGQFDPMiPDAECLKIMCEILSGLQLGDFL 219
Cdd:pfam13393 75 ----VARIDAhrLNRPGPLRLCYAGSVLRTRPKGL--GRSREPLQVGAELIGHAGIE-ADAEIISLLLEALAAAGVPGVT 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 220 IKVNDRRIVDGMFAACGVPESKFRAICSSIDKLDkmaWKDVRhEMVAKKGLAPEVADRIGDYVQCHGGVSLVEQMFQdpR 299
Cdd:pfam13393 148 LDLGHVGLVRALLEAAGLSEALEEALRAALQRKD---AAELA-ELAAEAGLPPALRRALLALPDLYGGPEVLDEARA--A 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 300 LSQNKQALEGLEDLKLLFEYLNLFGIAEKISFDLSLARGLDYYTGVIYEAVLLQTPtqageeplnvGSVAAGGRYDGLVG 379
Cdd:pfam13393 222 LPGLPALQEALDELEALAALLEALGDGVRLTFDLAELRGYEYYTGIVFAAYAPGVG----------EPLARGGRYDDLGA 291
|
330 340
....*....|....*....|.
gi 1622947310 380 MFdpkGHKVPCVGLSIGVERI 400
Cdd:pfam13393 292 AF---GRARPATGFSLDLEAL 309
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02972 |
PLN02972 |
Histidyl-tRNA synthetase |
12-509 |
0e+00 |
|
Histidyl-tRNA synthetase
Pssm-ID: 215525 [Multi-domain] Cd Length: 763 Bit Score: 535.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 12 WAALLSQLLRPPCASCTGAVrcqSQVAEAVLTSQLKahqEKPnfiiKIPKGTRDLSPQHMVVREKILDLVISCFKRHGAK 91
Cdd:PLN02972 292 WATQLLLLFDPKCPGFDSLV---DKVKEIVESNEVR---RLP----KIPKGTRDFAKEQMAIREKAFSIITSVFKRHGAT 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 92 GMDTPAFELKETLTEKYGEDSGLMYDLKDQGGELLSLRYDLTypssltdlceVPFARYLAMNKVKKMKRYHVGKVWRRES 171
Cdd:PLN02972 362 ALDTPVFELRETLMGKYGEDSKLIYDLADQGGELCSLRYDLT----------VPFARYVAMNGITSFKRYQIAKVYRRDN 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 172 PSivQGRYREFCQCDFDIAGQFDPMIPDAECLKIMCEILSGLQLGDFLIKVNDRRIVDGMFAACGVPESKFRAICSSIDK 251
Cdd:PLN02972 432 PS--KGRYREFYQCDFDIAGVYEPMGPDFEIIKVLTELLDELDIGTYEVKLNHRKLLDGMLEICGVPPEKFRTICSSIDK 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 252 LDKMAWKDVRHEMVAKKGLAPEVADRIGDYVQCHGG-VSLVEQMFQ-DPRLSQNKQALEGLEDLKLLFEYLNLFGIAEKI 329
Cdd:PLN02972 510 LDKQSFEQVKKEMVEEKGLSNETADKIGNFVKERGPpLELLSKLRQeGSEFLGNASSRAALDELEIMFKALEKSKAIGKI 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 330 SFDLSLARGLDYYTGVIYEAVLLQTptqageeplNVGSVAAGGRYDGLVGMFDPKghKVPCVGLSIGVERIFYIVEQRMK 409
Cdd:PLN02972 590 VFDLSLARGLDYYTGVIYEAVFKGA---------QVGSIAAGGRYDNLVGMFSGK--QVPAVGVSLGIERVFAIMEQQEE 658
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 410 TKGEKVRTTETQVFVATPQKNFLQERLKLITELWDAGIKAEmlYKNNPKLLTQLHYCESTGIPLVVIIGEQELKEGIIKI 489
Cdd:PLN02972 659 EKSQVIRPTETEVLVSIIGDDKLALAAELVSELWNAGIKAE--YKVSTRKAKHLKRAKESGIPWMVLVGEKELSKGFVKL 736
|
490 500
....*....|....*....|
gi 1622947310 490 RSVASREEVSGSSRNRRDEL 509
Cdd:PLN02972 737 KNLEAGVEEEVDRTCFVQEL 756
|
|
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
57-499 |
6.83e-108 |
|
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: 329.39 E-value: 6.83e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 57 IKIPKGTRDLSPQHMVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSG--LMYDLKDQGGELLSLRYDLTy 134
Cdd:COG0124 4 IQAPRGTRDILPEESAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKIGEDIVekEMYTFEDRGGRSLTLRPEGT- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 135 pssltdlceVPFARYLAMNK---VKKMKRYHVGKVWRRESPsivQ-GRYREFCQCDFDIAGQFDPMIpDAECLKIMCEIL 210
Cdd:COG0124 83 ---------APVARAVAEHGnelPFPFKLYYIGPVFRYERP---QkGRYRQFHQFGVEVIGSDSPLA-DAEVIALAADLL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 211 SGLQLGDFLIKVNDRrivdgmfaacGVPESKFRAICSSIDKLDKMAWKDVrhemvakkgLAPEVADRIG-----DYVQCH 285
Cdd:COG0124 150 KALGLKDFTLEINSR----------GLPEERAEALLRYLDKLDKIGHEDV---------LDEDSQRRLEtnplrAILDSK 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 286 GGV--SLVEQMfqdPRLSQNKqALEGLEDLKLLFEYLNLFGIaeKISFDLSLARGLDYYTGVIYEAVLLQTPTQageepl 363
Cdd:COG0124 211 GPDcqEVLADA---PKLLDYL-GEEGLAHFEEVLELLDALGI--PYVIDPRLVRGLDYYTGTVFEIVTDGLGAQ------ 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 364 nvGSVAAGGRYDGLVGMFDpkGHKVPCVGLSIGVERIFYIVEQRmktKGEKVRTTETQVFVATPQKNFLQERLKLITELW 443
Cdd:COG0124 279 --GSVCGGGRYDGLVEQLG--GPPTPAVGFAIGLERLLLLLEEL---GLLPAAEPPPDVYVVPLGEEARAEALKLAQELR 351
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622947310 444 DAGIKAEMLYKNNpKLLTQLHYCESTGIPLVVIIGEQELKEGIIKIRSVASREEVS 499
Cdd:COG0124 352 AAGIRVELDLGGR-KLKKQLKYADKSGAPFVLILGEDELANGTVTLKDLATGEQET 406
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
71-405 |
8.58e-96 |
|
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: 292.58 E-value: 8.58e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 71 MVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSG-LMYDLKDQGGELLSLRYDLTypssltdlceVPFARY 149
Cdd:cd00773 2 AALRRYIEDTLREVFERYGYEEIDTPVFEYTELFLRKSGDEVSkEMYRFKDKGGRDLALRPDLT----------APVARA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 150 LAMNKVKK---MKRYHVGKVWRRESPSivQGRYREFCQCDFDIAGqFDPMIPDAECLKIMCEILSGLQLGDFLIKVNDRR 226
Cdd:cd00773 72 VAENLLSLplpLKLYYIGPVFRYERPQ--KGRYREFYQVGVEIIG-SDSPLADAEVIALAVEILEALGLKDFQIKINHRG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 227 IVDGmfaACGVPESKFRAICSSIDKLDKmawkdvrhemvakkglapevadrigdyvqchggvslveqmfqdprlsqnkqa 306
Cdd:cd00773 149 ILDG---IAGLLEDREEYIERLIDKLDK---------------------------------------------------- 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 307 lEGLEDLKLLFEYLNLFGIAEKISFDLSLARGLDYYTGVIYEAVLLQTPTQageeplnvGSVAAGGRYDGLVGMFDpkGH 386
Cdd:cd00773 174 -EALAHLEKLLDYLEALGVDIKYSIDLSLVRGLDYYTGIVFEAVADGLGAQ--------GSIAGGGRYDGLLEEFG--GE 242
|
330
....*....|....*....
gi 1622947310 387 KVPCVGLSIGVERIFYIVE 405
Cdd:cd00773 243 DVPAVGFAIGLERLLLALE 261
|
|
| hisS |
TIGR00442 |
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ... |
58-499 |
2.91e-92 |
|
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: 288.61 E-value: 2.91e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 58 KIPKGTRDLSPQHMVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSGL----MYDLKDQGGELLSLRYDLT 133
Cdd:TIGR00442 1 QKPRGTRDFLPEEMIKWQYIEETIREVFERYGFKEIRTPIFEYTELFKRKVGEETDIvskeMYTFKDKGGRSLTLRPEGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 134 ypssltdlceVPFARYLAMNK---VKKMKRYHVGKVWRRESPsivQ-GRYREFCQCDFDIAGQFDPMIpDAECLKIMCEI 209
Cdd:TIGR00442 81 ----------APVARAVIENKlllPKPFKLYYIGPMFRYERP---QkGRYRQFHQFGVEVIGSDSPLA-DAEIIALAADI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 210 LSGLQLGDFLIKVNDRRIVDGMFAacgvpesKFRAICSSIDK-LDKMAWKDVRHEMVAKKGLAPEVADRIGDYVQchggv 288
Cdd:TIGR00442 147 LKELGLKDFTLEINSLGILEGRLE-------YREALIRYLDKhKDKLGEDSVRRLEKNPLRILDSKNEKIQELLK----- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 289 slveqmfQDPRLSQNKQAlEGLEDLKLLFEYLNLFGIaeKISFDLSLARGLDYYTGVIYEAVLLQTPTQageeplnvGSV 368
Cdd:TIGR00442 215 -------NAPKILDFLCE-ESRAHFEELKELLDALGI--PYKIDPSLVRGLDYYTGTVFEFVTDDLGAQ--------GSI 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 369 AAGGRYDGLVGMFDpkGHKVPCVGLSIGVERIFYIVEQRmktKGEKVRTTETQVFVATPQKNFLQERLKLITELWDAGIK 448
Cdd:TIGR00442 277 CGGGRYDGLVEELG--GPPTPAVGFAIGIERLILLLEEL---GLIPPPSKKPDVYVVPLGEEAELEALKLAQKLRKAGIR 351
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1622947310 449 AEMLYKNNpKLLTQLHYCESTGIPLVVIIGEQELKEGIIKIRSVASREEVS 499
Cdd:TIGR00442 352 VEVDLGGR-KLKKQLKYADKLGARFALIIGEDELENGTVTLKDLETGEQET 401
|
|
| PRK12420 |
PRK12420 |
histidyl-tRNA synthetase; Provisional |
61-498 |
2.48e-80 |
|
histidyl-tRNA synthetase; Provisional
Pssm-ID: 237097 [Multi-domain] Cd Length: 423 Bit Score: 258.12 E-value: 2.48e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 61 KGTRDLSPQHMVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYG---EDSGLMYDLKDQGGELLSLRYDLTypss 137
Cdd:PRK12420 8 KGTKDYLPEEQVLRNKIKRALEDVFERYGCKPLETPTLNMYELMSSKYGggdEILKEIYTLTDQGKRDLALRYDLT---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 138 ltdlceVPFARYLAMNKVKKM--KRYHVGKVWRrESPsIVQGRYREFCQCDFDIAGQFDPMiPDAECLKIMCEILSGLQL 215
Cdd:PRK12420 84 ------IPFAKVVAMNPNIRLpfKRYEIGKVFR-DGP-IKQGRFREFIQCDVDIVGVESVM-AEAELMSMAFELFRRLNL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 216 gDFLIKVNDRRIVDGMFAACGVPESKFRAICSSIDKLDKMAWKDVRHEmVAKKGLAPEVADRIGDYVQCHGGVSLVEqmF 295
Cdd:PRK12420 155 -EVTIQYNNRKLLNGILQAIGIPTELTSDVILSLDKIEKIGIDGVRKD-LLERGISEEMADTICNTVLSCLQLSIAD--F 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 296 QDPRLSQNKQalEGLEDLKLLFEYLNLFGIAEKISFDLSLARGLDYYTGVIYEAVLlqtptqagEEPLNVGSVAAGGRYD 375
Cdd:PRK12420 231 KEAFNNPLVA--EGVNELQQLQQYLIALGINENCIFNPFLARGLTMYTGTVYEIFL--------KDGSITSSIGSGGRYD 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 376 GLVGMFDPKGHKVPCVGLSIGVERIFYIVEQRmktkgekVRTTETQVFVATPQKNFLQERLKLITELWDAGIKAEMLYKN 455
Cdd:PRK12420 301 NIIGAFRGDDMNYPTVGISFGLDVIYTALSQK-------ETISSTADVFIIPLGTELQCLQIAQQLRSTTGLKVELELAG 373
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1622947310 456 NpKLLTQLHYCESTGIPLVVIIGEQELKEGIIKIRSVASREEV 498
Cdd:PRK12420 374 R-KLKKALNYANKENIPYVLIIGEEEVSTGTVMLRNMKEGSEV 415
|
|
| hisZ_biosyn_reg |
TIGR00443 |
ATP phosphoribosyltransferase, regulatory subunit; Apparant second copies of histidyl-tRNA ... |
64-400 |
1.58e-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: 173.57 E-value: 1.58e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 64 RDLSPQHMVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSGLMYDLKDQGGELLSLRYDLTYP------SS 137
Cdd:TIGR00443 1 RDLLPEEAARKEEIERQLQDVFRSWGYQEIITPTLEYLDTLSAGSGILNEDLFKLFDQLGRVLGLRPDMTAPiarlvsTR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 138 LTDlCEVPFarylamnkvkkmKRYHVGKVWRRESPSIvqGRYREFCQCDFDIAGQfDPMIPDAECLKIMCEILSGLQLGD 217
Cdd:TIGR00443 81 LRD-RPLPL------------RLCYAGNVFRTNESGG--GRSREFTQAGVELIGA-GGPAADAEVIALLIEALKALGLKD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 218 FLIKVNDRRIVDGMFAACGVPESKFRAICSSIDKLDKMAWKdvrhEMVAKKGLAPEVADRIGDYVQCHGGVSLVEQMFQd 297
Cdd:TIGR00443 145 FKIELGHVGLVRALLEEAGLPEEAREALREALARKDLVALE----ELVAELGLSPEVRERLLALPRLRGDGEEVLEEAR- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 298 pRLSQNKQALEGLEDLKLLFEYLNLFGIAEKISFDLSLARGLDYYTGVIYEAVLlqtpTQAGEeplnvgSVAAGGRYDGL 377
Cdd:TIGR00443 220 -ALAGSETAEAALDELEAVLELLEARGVEEYISLDLGLVRGYHYYTGLIFEGYA----PGLGA------PLAGGGRYDEL 288
|
330 340
....*....|....*....|...
gi 1622947310 378 VGMFdpkGHKVPCVGLSIGVERI 400
Cdd:TIGR00443 289 LGRF---GRPLPATGFALNLERL 308
|
|
| PLN02530 |
PLN02530 |
histidine-tRNA ligase |
2-499 |
2.47e-48 |
|
histidine-tRNA ligase
Pssm-ID: 178145 [Multi-domain] Cd Length: 487 Bit Score: 174.93 E-value: 2.47e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 2 PLLGLLPRRAWAALLSQLLRPPCASCTGAVRCQSQVAEAVLTSQLKAhqeKPNFIIKIPKGTRDLSPQHMVVREKILDLV 81
Cdd:PLN02530 18 PSLPLSSRCSFLLSASSPRGGRCAASAAAGGGRSGGTTAPPSVQEDG---KPKIDVNPPKGTRDFPPEDMRLRNWLFDHF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 82 ISCFKRHGAKGMDTPAFELKETLTEKYGED-SGLMYDLKDQGGELLSLRYDLTyPSsltdlcevpFARyLAMNKVKKM-- 158
Cdd:PLN02530 95 REVSRLFGFEEVDAPVLESEELYIRKAGEEiTDQLYNFEDKGGRRVALRPELT-PS---------LAR-LVLQKGKSLsl 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 159 --KRYHVGKVWRRESpsIVQGRYREFCQCDFDIAGqFDPMIPDAECLKIMCEILS--GLQLGDFLIKVNDRRIVDGMFAA 234
Cdd:PLN02530 164 plKWFAIGQCWRYER--MTRGRRREHYQWNMDIIG-VPGVEAEAELLAAIVTFFKrvGITSSDVGIKVSSRKVLQAVLKS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 235 CGVPESKFRAICSSIDKLDKMAWKDVRHEMvAKKGLAPEVADRIGDYVQCHGGVSLVEQMFQDPrlsqnkqalEGLEDLK 314
Cdd:PLN02530 241 YGIPEESFAPVCVIVDKLEKLPREEIEKEL-DTLGVSEEAIEGILDVLSLKSLDDLEALLGADS---------EAVADLK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 315 LLFEYLNLFGIAEKISFDLSLARGLDYYTGVIYEAVllqtpTQAGEeplnVGSVAAGGRYDGLVGMFDpkGHKVPCVGLS 394
Cdd:PLN02530 311 QLFSLAEAYGYQDWLVFDASVVRGLAYYTGIVFEGF-----DRAGK----LRAICGGGRYDRLLSTFG--GEDTPACGFG 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 395 IG--VerifyIVEQrMKTKG---EKVRTTETQVFvatPQKNFLQ-ERLKLITELWDAGIKAEMLYKNNpKLLTQLHYCES 468
Cdd:PLN02530 380 FGdaV-----IVEL-LKEKGllpELPHQVDDVVF---ALDEDLQgAAAGVASRLREKGRSVDLVLEPK-KLKWVFKHAER 449
|
490 500 510
....*....|....*....|....*....|.
gi 1622947310 469 TGIPLVVIIGEQELKEGIIKIRSVASREEVS 499
Cdd:PLN02530 450 IGAKRLVLVGASEWERGMVRVKDLSSGEQTE 480
|
|
| HisZ |
COG3705 |
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism]; |
74-400 |
2.69e-44 |
|
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism];
Pssm-ID: 442919 [Multi-domain] Cd Length: 312 Bit Score: 159.19 E-value: 2.69e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 74 REKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSGL-MYDLKDQGGELLSLRYDLTypssltdlceVPFARYLA- 151
Cdd:COG3705 8 KEELRRRLLDVFRSWGYELVEPPLLEYLDSLLTGSGADLDLqTFKLVDQLGRTLGLRPDMT----------PQVARIAAt 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 152 -MNKVKKMKRY-HVGKVWRRESPSivQGRYREFCQC------DFDIAGqfdpmipDAECLKIMCEILSGLQLGDFLIKVN 223
Cdd:COG3705 78 rLANRPGPLRLcYAGNVFRTRPSG--LGRSREFLQAgaeligHAGLEA-------DAEVIALALEALKAAGLEDFTLDLG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 224 DRRIVDGMFAACGVPESKFRAICSSIDKLDkmaWKDVRhEMVAKKGLAPEVADRIGDYVQCHGGVSLVEQMFQdprLSQN 303
Cdd:COG3705 149 HVGLFRALLEALGLSEEQREELRRALARKD---AVELE-ELLAELGLSEELAEALLALPELYGGEEVLARARA---LLLD 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 304 KQALEGLEDLKLLFEYLNLFGIAEKISFDLSLARGLDYYTGVIYEAVllqTPTQAGEeplnvgsVAAGGRYDGLVGMFdp 383
Cdd:COG3705 222 AAIRAALDELEALAEALAARGPDVRLTFDLSELRGYDYYTGIVFEAY---APGVGDP-------LARGGRYDGLLAAF-- 289
|
330
....*....|....*..
gi 1622947310 384 kGHKVPCVGLSIGVERI 400
Cdd:COG3705 290 -GRARPATGFSLDLDRL 305
|
|
| hisZ |
PRK12292 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
59-451 |
5.33e-43 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 237043 [Multi-domain] Cd Length: 391 Bit Score: 158.11 E-value: 5.33e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 59 IPKGTRDLSPQHMVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSGL-MYDLKDQG-GELLSLRYDLTyps 136
Cdd:PRK12292 5 LPEGIRDLLPEEARKIEEIRRRLLDLFRRWGYEEVITPTLEYLDTLLAGGGAILDLrTFKLVDQLsGRTLGLRPDMT--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 137 sltdlceVPFARyLAMNKVKKMKR-----YHvGKVWR-RESPSivqGRYREFCQCDFDIAGqFDPMIPDAECLKIMCEIL 210
Cdd:PRK12292 82 -------AQIAR-IAATRLANRPGplrlcYA-GNVFRaQERGL---GRSREFLQSGVELIG-DAGLEADAEVILLLLEAL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 211 SGLQLGDFLIKVNDRRIVDGMFAACGVPESKFRAICSSIDKLDKMAWKdvrhEMVAkkGLAPEVADRIGDYVQCHGGVSL 290
Cdd:PRK12292 149 KALGLPNFTLDLGHVGLFRALLEAAGLSEELEEVLRRALANKDYVALE----ELVL--DLSEELRDALLALPRLRGGREV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 291 VEQMfqdPRLSQNKQALEGLEDLKLLFEYLNLFGIAEKISFDLSLARGLDYYTGVIYEAVllqtptqAGEEPLNVGSvaa 370
Cdd:PRK12292 223 LEEA---RKLLPSLPIKRALDELEALAEALEKYGYGIPLSLDLGLLRHLDYYTGIVFEGY-------VDGVGNPIAS--- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 371 GGRYDGLVGMFdpkGHKVPCVGLSIGVERifyIVEQRMKTKgekvrTTETQVFVATPQKNFLQERLKLITELWDAGIKAE 450
Cdd:PRK12292 290 GGRYDDLLGRF---GRARPATGFSLDLDR---LLELQLELP-----VEARKDLVIAPDSEALAAALAAAQELRKKGEIVV 358
|
.
gi 1622947310 451 M 451
Cdd:PRK12292 359 L 359
|
|
| tRNA-synt_His |
pfam13393 |
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ... |
62-400 |
2.89e-39 |
|
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: 145.42 E-value: 2.89e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 62 GTRDLSPQHMVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSGLMYDLKDQGGELLSLRYDLTyPSsltdl 141
Cdd:pfam13393 1 GIRDLLPPEARRIEELRRRLLDLFRSWGYELVMPPLLEYLDSLLTGTGADLDQTFKLVDQSGRLLGLRADIT-PQ----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 142 cevpFARYLA--MNKVKKMKRYHVGKVWRRESPSIvqGRYREFCQCDFDIAGQFDPMiPDAECLKIMCEILSGLQLGDFL 219
Cdd:pfam13393 75 ----VARIDAhrLNRPGPLRLCYAGSVLRTRPKGL--GRSREPLQVGAELIGHAGIE-ADAEIISLLLEALAAAGVPGVT 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 220 IKVNDRRIVDGMFAACGVPESKFRAICSSIDKLDkmaWKDVRhEMVAKKGLAPEVADRIGDYVQCHGGVSLVEQMFQdpR 299
Cdd:pfam13393 148 LDLGHVGLVRALLEAAGLSEALEEALRAALQRKD---AAELA-ELAAEAGLPPALRRALLALPDLYGGPEVLDEARA--A 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 300 LSQNKQALEGLEDLKLLFEYLNLFGIAEKISFDLSLARGLDYYTGVIYEAVLLQTPtqageeplnvGSVAAGGRYDGLVG 379
Cdd:pfam13393 222 LPGLPALQEALDELEALAALLEALGDGVRLTFDLAELRGYEYYTGIVFAAYAPGVG----------EPLARGGRYDDLGA 291
|
330 340
....*....|....*....|.
gi 1622947310 380 MFdpkGHKVPCVGLSIGVERI 400
Cdd:pfam13393 292 AF---GRARPATGFSLDLEAL 309
|
|
| syh |
CHL00201 |
histidine-tRNA synthetase; Provisional |
61-497 |
7.05e-25 |
|
histidine-tRNA synthetase; Provisional
Pssm-ID: 164576 [Multi-domain] Cd Length: 430 Bit Score: 107.29 E-value: 7.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 61 KGTRDLSPQHMVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSGL----MYDLKDQGGELLSLRYDLTyps 136
Cdd:CHL00201 8 RGTKDILPDEINYWQFIHDKALTLLSLANYSEIRTPIFENSSLYDRGIGETTDIvnkeMYRFTDRSNRDITLRPEGT--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 137 sltdlceVPFARYLAMNKVKKMKR----YHVGKVWRRESPSivQGRYREFCQCDFDIAGQFDPMiPDAECLKIMCEILSG 212
Cdd:CHL00201 85 -------AGIVRAFIENKMDYHSNlqrlWYSGPMFRYERPQ--SGRQRQFHQLGIEFIGSIDAR-ADTEVIHLAMQIFNE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 213 LQLGDFLIKVN------DRRIVdgmfaacgvpESKFRAICSSI-DKLDKmawkDVRHEMVAKkglaP-EVADRIGDYVQc 284
Cdd:CHL00201 155 LQVKNLILDINsigkleDRQSY----------QLKLVEYLSQYqDDLDT----DSQNRLYSN----PiRILDSKNLKTQ- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 285 hggvslvEQMFQDPRLSqNKQALEGLEDLKLLFEYLNLFGIAEKISFdlSLARGLDYYTGVIYEavlLQTPTQAGEEpln 364
Cdd:CHL00201 216 -------EILDGAPKIS-DFLSLESTEHFYDVCTYLNLLNIPYKINY--KLVRGLDYYNDTAFE---IKTLSSNGQD--- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 365 vgSVAAGGRYDGLVGMFDpkGHKVPCVGLSIGVERIFYIVEQRMKTKGEKVrttetQVFVATPQKNFLQERLKLITELWD 444
Cdd:CHL00201 280 --TICGGGRYDSLIHQLG--GPKTPAVGCAIGLERLLLIAKDNIILPKQSI-----DVYIATQGLKAQKKGWEIIQFLEK 350
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1622947310 445 AGIKAEmLYKNNPKLLTQLHYCESTGIPLVVIIGEQELKEGIIKIRSVASREE 497
Cdd:CHL00201 351 QNIKFE-LDLSSSNFHKQIKQAGKKRAKACIILGDNEIMDNCITIKWLDEQVQ 402
|
|
| HisRS_anticodon |
cd00859 |
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases ... |
419-499 |
1.59e-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: 97.61 E-value: 1.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 419 ETQVFVATPQKNFLQERLKLITELWDAGIKAEMLYKNnPKLLTQLHYCESTGIPLVVIIGEQELKEGIIKIRSVASREEV 498
Cdd:cd00859 1 EVDVYVVPLGEGALSEALELAEQLRDAGIKAEIDYGG-RKLKKQFKYADRSGARFAVILGEDELAAGVVTVKDLETGEQE 79
|
.
gi 1622947310 499 S 499
Cdd:cd00859 80 T 80
|
|
| hisZ |
PRK12295 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
77-400 |
3.85e-19 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 183413 [Multi-domain] Cd Length: 373 Bit Score: 89.22 E-value: 3.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 77 ILDLVISCFKRHGAKGMDTPAFELKETLTEKYGED-SGLMYDLKDQGGELLSLRYDLTYPSSLtdlcevpfaRYLAMNKV 155
Cdd:PRK12295 10 AAEALLASFEAAGAVRVDPPILQPAEPFLDLSGEDiRRRIFVTSDENGEELCLRPDFTIPVCR---------RHIATAGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 156 KKMKRYHVGKVWRRESpsivqGRYREFCQCDFDIAGQFDPMIPDAECLKIMCEILSGLQLGDFLIKVNDRRIVDGMFAAC 235
Cdd:PRK12295 81 EPARYAYLGEVFRQRR-----DRASEFLQAGIESFGRADPAAADAEVLALALEALAALGPGDLEVRLGDVGLFAALVDAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 236 GVPE-------------SKFRAIcssIDKL-------------------DKMAWKDVRHEMVAKKGLAP-------EVAD 276
Cdd:PRK12295 156 GLPPgwkrrllrhfgrpRSLDAL---LARLagprvdpldehagvlaalaDEAAARALVEDLMSIAGISPvggrspaEIAR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 277 RIGDYVQCHGGVSLVEQMFQ----------DPrlsqnKQALEGLEDL----KL-LFEYLNLF----------GIA-EKIS 330
Cdd:PRK12295 233 RLLEKAALAAAARLPAEALAvlerflaisgPP-----DAALAALRALaadaGLdLDAALDRFearlaalaarGIDlERLR 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 331 FDLSLARGLDYYTGVIYEAvllqTPTQAGEEPLnvgsvAAGGRYDGLVGMFDpKGHKVPCVGLSIGVERI 400
Cdd:PRK12295 308 FSASFGRPLDYYTGFVFEI----RAAGNGDPPL-----AGGGRYDGLLTRLG-AGEPIPAVGFSIWLDRL 367
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
421-509 |
3.18e-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: 68.38 E-value: 3.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 421 QVFVATPQKN---FLQERLKLITELWDAGIKAEmLYKNNPKLLTQLHYCESTGIPLVVIIGEQELKEGIIKIRSVASREE 497
Cdd:pfam03129 1 QVVVIPLGEKaeeLEEYAQKLAEELRAAGIRVE-LDDRNESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQ 79
|
90
....*....|..
gi 1622947310 498 VSGSsrnrRDEL 509
Cdd:pfam03129 80 ETVS----LDEL 87
|
|
| PRK12421 |
PRK12421 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
262-400 |
1.22e-05 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 237098 Cd Length: 392 Bit Score: 47.66 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 262 HEMVAKKGLAPEVADRIGDYVQCHGGV-SLVEQMFQDPRlsQNKQALEGLEDLKLLFEYLNLFGIAEKISFDLSLARGLD 340
Cdd:PRK12421 199 AEVCQNLGVGSDLRRMFYALARLNGGLeALDRALSVLAL--QDAAIRQALDELKTLAAHLKNRWPELPVSIDLAELRGYH 276
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 341 YYTGVIYeAVLLQTPTQAgeeplnvgsVAAGGRYDGLVGMFdpkGHKVPCVGLSIGVERI 400
Cdd:PRK12421 277 YHTGLVF-AAYIPGRGQA---------LARGGRYDGIGEAF---GRARPATGFSMDLKEL 323
|
|
| HGTP_anticodon2 |
pfam12745 |
Anticodon binding domain of tRNAs; This is an HGTP_anticodon binding domain, found largely on ... |
422-498 |
1.01e-04 |
|
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: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947310 422 VFVATPQKNFL-QERLKLITELWDAGIKAEMLYKNNPKLLTQLHYCESTGIPLVVIIGEQEL----KEGIIKIRSVASRE 496
Cdd:pfam12745 8 VLVASFDASILrTTGVEILQELWAHGISADLAVDASYSPEDLVSRARDDGVSWIVIIKQQNKssdsKYKPLKVKNLLRKE 87
|
..
gi 1622947310 497 EV 498
Cdd:pfam12745 88 DV 89
|
|
|