|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02972 |
PLN02972 |
Histidyl-tRNA synthetase |
59-505 |
5.69e-174 |
|
Histidyl-tRNA synthetase
Pssm-ID: 215525 [Multi-domain] Cd Length: 763 Bit Score: 508.66 E-value: 5.69e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 59 KVPKGTRDLSPQQMVVREKILDKIISCFKRHGAKGLDTPAFELKEMLTEKYEDNFGLMYDLEDQGGELLSLRYDLTVPFA 138
Cdd:PLN02972 328 KIPKGTRDFAKEQMAIREKAFSIITSVFKRHGATALDTPVFELRETLMGKYGEDSKLIYDLADQGGELCSLRYDLTVPFA 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 139 RYLAMNKLKRMKRYQVGKVWRRESPAivQGRYREFCQCDFDIAGEFDPMIPDAECLRIMCEILSGLQLGDFLIKVNDRRV 218
Cdd:PLN02972 408 RYVAMNGITSFKRYQIAKVYRRDNPS--KGRYREFYQCDFDIAGVYEPMGPDFEIIKVLTELLDELDIGTYEVKLNHRKL 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 219 VDGMFAVCGVPESKFRTICSSMDKLDKMSWEDVRLEMVAGKGLAPEVADRIGDYVQCHGG-ISLVEELFK-DPRLSQSQL 296
Cdd:PLN02972 486 LDGMLEICGVPPEKFRTICSSIDKLDKQSFEQVKKEMVEEKGLSNETADKIGNFVKERGPpLELLSKLRQeGSEFLGNAS 565
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 297 ALQGLGDLKLLFEYLRLFGIADKISLDLSLARGLDYYTGVIYEAVLLESpaqagketlNVGSVAAGGRYDRLVAQFDPKg 376
Cdd:PLN02972 566 SRAALDELEIMFKALEKSKAIGKIVFDLSLARGLDYYTGVIYEAVFKGA---------QVGSIAAGGRYDNLVGMFSGK- 635
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 377 hSVPCVGLSIGVERIFYLVEQKMKISCEKVRTTETQVFVATPQKNFLQERLKIIAQLWDAGIKAEmlYKNNPKLLTQLHY 456
Cdd:PLN02972 636 -QVPAVGVSLGIERVFAIMEQQEEEKSQVIRPTETEVLVSIIGDDKLALAAELVSELWNAGIKAE--YKVSTRKAKHLKR 712
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 207445692 457 CEKEDIPLMVIIGEQEQNEGVVKLRSVASREEVTVNRESLVAEIQKRLS 505
Cdd:PLN02972 713 AKESGIPWMVLVGEKELSKGFVKLKNLEAGVEEEVDRTCFVQELKAELL 761
|
|
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
58-506 |
1.43e-113 |
|
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: 342.10 E-value: 1.43e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 58 IKVPKGTRDLSPQQMVVREKILDKIISCFKRHGAKGLDTPAFELKEMLTEKYEDNFG--LMYDLEDQGGELLSLRYDLTV 135
Cdd:COG0124 4 IQAPRGTRDILPEESAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKIGEDIVekEMYTFEDRGGRSLTLRPEGTA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 136 PFARYLAMNKLKR---MKRYQVGKVWRRESPAivQGRYREFCQCDFDIAGEFDPMIpDAECLRIMCEILSGLQLGDFLIK 212
Cdd:COG0124 84 PVARAVAEHGNELpfpFKLYYIGPVFRYERPQ--KGRYRQFHQFGVEVIGSDSPLA-DAEVIALAADLLKALGLKDFTLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 213 VNDRrvvdgmfavcGVPESKFRTICSSMDKLDKMSWEDVrlemvagkgLAPEVADRIG-----DYVQCHGGIslVEELFK 287
Cdd:COG0124 161 INSR----------GLPEERAEALLRYLDKLDKIGHEDV---------LDEDSQRRLEtnplrAILDSKGPD--CQEVLA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 288 D-PRLSQSqLALQGLGDLKLLFEYLRLFGIadKISLDLSLARGLDYYTGVIYEAVLLESPAQagketlnvGSVAAGGRYD 366
Cdd:COG0124 220 DaPKLLDY-LGEEGLAHFEEVLELLDALGI--PYVIDPRLVRGLDYYTGTVFEIVTDGLGAQ--------GSVCGGGRYD 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 367 RLVAQFDpkGHSVPCVGLSIGVERIFYLVEQKmkiSCEKVRTTETQVFVATPQKNFLQERLKIIAQLWDAGIKAEMLYKN 446
Cdd:COG0124 289 GLVEQLG--GPPTPAVGFAIGLERLLLLLEEL---GLLPAAEPPPDVYVVPLGEEARAEALKLAQELRAAGIRVELDLGG 363
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 447 NpKLLTQLHYCEKEDIPLMVIIGEQEQNEGVVKLRSVASREEVTVNRESLVAEIQKRLSE 506
Cdd:COG0124 364 R-KLKKQLKYADKSGAPFVLILGEDELANGTVTLKDLATGEQETVPLDELVEYLKELLAE 422
|
|
| hisS |
TIGR00442 |
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ... |
59-493 |
3.39e-94 |
|
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: 291.69 E-value: 3.39e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 59 KVPKGTRDLSPQQMVVREKILDKIISCFKRHGAKGLDTPAFELKEMLTEKYEDN----FGLMYDLEDQGGELLSLRYDLT 134
Cdd:TIGR00442 1 QKPRGTRDFLPEEMIKWQYIEETIREVFERYGFKEIRTPIFEYTELFKRKVGEEtdivSKEMYTFKDKGGRSLTLRPEGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 135 VPFARYLAMNKLKR---MKRYQVGKVWRRESPaivQ-GRYREFCQCDFDIAGEFDPMIpDAECLRIMCEILSGLQLGDFL 210
Cdd:TIGR00442 81 APVARAVIENKLLLpkpFKLYYIGPMFRYERP---QkGRYRQFHQFGVEVIGSDSPLA-DAEIIALAADILKELGLKDFT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 211 IKVNDRRVVDGMFAvcgvpesKFRTICSSMDK-LDKMSWEDVRLEMVAGKGLAPEVADRIGDYVQchGGISLVEELFKDp 289
Cdd:TIGR00442 157 LEINSLGILEGRLE-------YREALIRYLDKhKDKLGEDSVRRLEKNPLRILDSKNEKIQELLK--NAPKILDFLCEE- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 290 rlsqsqlalqGLGDLKLLFEYLRLFGIadKISLDLSLARGLDYYTGVIYEAVLLESPAQagketlnvGSVAAGGRYDRLV 369
Cdd:TIGR00442 227 ----------SRAHFEELKELLDALGI--PYKIDPSLVRGLDYYTGTVFEFVTDDLGAQ--------GSICGGGRYDGLV 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 370 AQFDpkGHSVPCVGLSIGVERIFYLVEQKMKISCEKvrtTETQVFVATPQKNFLQERLKIIAQLWDAGIKAEMLYKNNpK 449
Cdd:TIGR00442 287 EELG--GPPTPAVGFAIGIERLILLLEELGLIPPPS---KKPDVYVVPLGEEAELEALKLAQKLRKAGIRVEVDLGGR-K 360
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 207445692 450 LLTQLHYCEKEDIPLMVIIGEQEQNEGVVKLRSVASREEVTVNR 493
Cdd:TIGR00442 361 LKKQLKYADKLGARFALIIGEDELENGTVTLKDLETGEQETVPL 404
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
71-396 |
1.58e-93 |
|
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: 284.88 E-value: 1.58e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 71 QMVVREKILDKIISCFKRHGAKGLDTPAFELKEMLTEK-YEDNFGLMYDLEDQGGELLSLRYDLTVPFARYLAMNKLKR- 148
Cdd:cd00773 1 EAALRRYIEDTLREVFERYGYEEIDTPVFEYTELFLRKsGDEVSKEMYRFKDKGGRDLALRPDLTAPVARAVAENLLSLp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 149 --MKRYQVGKVWRRESPAivQGRYREFCQCDFDIAGEfDPMIPDAECLRIMCEILSGLQLGDFLIKVNDRRVVDGmfaVC 226
Cdd:cd00773 81 lpLKLYYIGPVFRYERPQ--KGRYREFYQVGVEIIGS-DSPLADAEVIALAVEILEALGLKDFQIKINHRGILDG---IA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 227 GVPESKFRTICSSMDKLDKmswedvrlemvagkglapevadrigdyvqchggislveelfkdprlsqsqlalQGLGDLKL 306
Cdd:cd00773 155 GLLEDREEYIERLIDKLDK-----------------------------------------------------EALAHLEK 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 307 LFEYLRLFGIADKISLDLSLARGLDYYTGVIYEAVLLESPAQagketlnvGSVAAGGRYDRLVAQFDpkGHSVPCVGLSI 386
Cdd:cd00773 182 LLDYLEALGVDIKYSIDLSLVRGLDYYTGIVFEAVADGLGAQ--------GSIAGGGRYDGLLEEFG--GEDVPAVGFAI 251
|
330
....*....|
gi 207445692 387 GVERIFYLVE 396
Cdd:cd00773 252 GLERLLLALE 261
|
|
| tRNA-synt_His |
pfam13393 |
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ... |
63-391 |
3.81e-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: 144.27 E-value: 3.81e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 63 GTRDLSPQQMVVREKILDKIISCFKRHGAKGLDTPAFELKEMLTEKYEDNFGLMYDLEDQGGELLSLRYDLTVPFARYLA 142
Cdd:pfam13393 1 GIRDLLPPEARRIEELRRRLLDLFRSWGYELVMPPLLEYLDSLLTGTGADLDQTFKLVDQSGRLLGLRADITPQVARIDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 143 mnklKRMKRYQV------GKVWRRESPAIvqGRYREFCQCDFDIAGEFDPMiPDAECLRIMCEILSGLQLGDFLIKVNDR 216
Cdd:pfam13393 81 ----HRLNRPGPlrlcyaGSVLRTRPKGL--GRSREPLQVGAELIGHAGIE-ADAEIISLLLEALAAAGVPGVTLDLGHV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 217 RVVDGMFAVCGVPESKFRTIcssMDKLDKMSWEDVRlEMVAGKGLAPEVADRIGDYVQCHGGISLVEELFKdpRLSQSQL 296
Cdd:pfam13393 154 GLVRALLEAAGLSEALEEAL---RAALQRKDAAELA-ELAAEAGLPPALRRALLALPDLYGGPEVLDEARA--ALPGLPA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 297 ALQGLGDLKLLFEYLRLFGIADKISLDLSLARGLDYYTGVIYEAVLlespAQAGKEtlnvgsVAAGGRYDRLVAQFdpkG 376
Cdd:pfam13393 228 LQEALDELEALAALLEALGDGVRLTFDLAELRGYEYYTGIVFAAYA----PGVGEP------LARGGRYDDLGAAF---G 294
|
330
....*....|....*
gi 207445692 377 HSVPCVGLSIGVERI 391
Cdd:pfam13393 295 RARPATGFSLDLEAL 309
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02972 |
PLN02972 |
Histidyl-tRNA synthetase |
59-505 |
5.69e-174 |
|
Histidyl-tRNA synthetase
Pssm-ID: 215525 [Multi-domain] Cd Length: 763 Bit Score: 508.66 E-value: 5.69e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 59 KVPKGTRDLSPQQMVVREKILDKIISCFKRHGAKGLDTPAFELKEMLTEKYEDNFGLMYDLEDQGGELLSLRYDLTVPFA 138
Cdd:PLN02972 328 KIPKGTRDFAKEQMAIREKAFSIITSVFKRHGATALDTPVFELRETLMGKYGEDSKLIYDLADQGGELCSLRYDLTVPFA 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 139 RYLAMNKLKRMKRYQVGKVWRRESPAivQGRYREFCQCDFDIAGEFDPMIPDAECLRIMCEILSGLQLGDFLIKVNDRRV 218
Cdd:PLN02972 408 RYVAMNGITSFKRYQIAKVYRRDNPS--KGRYREFYQCDFDIAGVYEPMGPDFEIIKVLTELLDELDIGTYEVKLNHRKL 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 219 VDGMFAVCGVPESKFRTICSSMDKLDKMSWEDVRLEMVAGKGLAPEVADRIGDYVQCHGG-ISLVEELFK-DPRLSQSQL 296
Cdd:PLN02972 486 LDGMLEICGVPPEKFRTICSSIDKLDKQSFEQVKKEMVEEKGLSNETADKIGNFVKERGPpLELLSKLRQeGSEFLGNAS 565
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 297 ALQGLGDLKLLFEYLRLFGIADKISLDLSLARGLDYYTGVIYEAVLLESpaqagketlNVGSVAAGGRYDRLVAQFDPKg 376
Cdd:PLN02972 566 SRAALDELEIMFKALEKSKAIGKIVFDLSLARGLDYYTGVIYEAVFKGA---------QVGSIAAGGRYDNLVGMFSGK- 635
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 377 hSVPCVGLSIGVERIFYLVEQKMKISCEKVRTTETQVFVATPQKNFLQERLKIIAQLWDAGIKAEmlYKNNPKLLTQLHY 456
Cdd:PLN02972 636 -QVPAVGVSLGIERVFAIMEQQEEEKSQVIRPTETEVLVSIIGDDKLALAAELVSELWNAGIKAE--YKVSTRKAKHLKR 712
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 207445692 457 CEKEDIPLMVIIGEQEQNEGVVKLRSVASREEVTVNRESLVAEIQKRLS 505
Cdd:PLN02972 713 AKESGIPWMVLVGEKELSKGFVKLKNLEAGVEEEVDRTCFVQELKAELL 761
|
|
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
58-506 |
1.43e-113 |
|
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: 342.10 E-value: 1.43e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 58 IKVPKGTRDLSPQQMVVREKILDKIISCFKRHGAKGLDTPAFELKEMLTEKYEDNFG--LMYDLEDQGGELLSLRYDLTV 135
Cdd:COG0124 4 IQAPRGTRDILPEESAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKIGEDIVekEMYTFEDRGGRSLTLRPEGTA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 136 PFARYLAMNKLKR---MKRYQVGKVWRRESPAivQGRYREFCQCDFDIAGEFDPMIpDAECLRIMCEILSGLQLGDFLIK 212
Cdd:COG0124 84 PVARAVAEHGNELpfpFKLYYIGPVFRYERPQ--KGRYRQFHQFGVEVIGSDSPLA-DAEVIALAADLLKALGLKDFTLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 213 VNDRrvvdgmfavcGVPESKFRTICSSMDKLDKMSWEDVrlemvagkgLAPEVADRIG-----DYVQCHGGIslVEELFK 287
Cdd:COG0124 161 INSR----------GLPEERAEALLRYLDKLDKIGHEDV---------LDEDSQRRLEtnplrAILDSKGPD--CQEVLA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 288 D-PRLSQSqLALQGLGDLKLLFEYLRLFGIadKISLDLSLARGLDYYTGVIYEAVLLESPAQagketlnvGSVAAGGRYD 366
Cdd:COG0124 220 DaPKLLDY-LGEEGLAHFEEVLELLDALGI--PYVIDPRLVRGLDYYTGTVFEIVTDGLGAQ--------GSVCGGGRYD 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 367 RLVAQFDpkGHSVPCVGLSIGVERIFYLVEQKmkiSCEKVRTTETQVFVATPQKNFLQERLKIIAQLWDAGIKAEMLYKN 446
Cdd:COG0124 289 GLVEQLG--GPPTPAVGFAIGLERLLLLLEEL---GLLPAAEPPPDVYVVPLGEEARAEALKLAQELRAAGIRVELDLGG 363
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 447 NpKLLTQLHYCEKEDIPLMVIIGEQEQNEGVVKLRSVASREEVTVNRESLVAEIQKRLSE 506
Cdd:COG0124 364 R-KLKKQLKYADKSGAPFVLILGEDELANGTVTLKDLATGEQETVPLDELVEYLKELLAE 422
|
|
| hisS |
TIGR00442 |
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ... |
59-493 |
3.39e-94 |
|
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: 291.69 E-value: 3.39e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 59 KVPKGTRDLSPQQMVVREKILDKIISCFKRHGAKGLDTPAFELKEMLTEKYEDN----FGLMYDLEDQGGELLSLRYDLT 134
Cdd:TIGR00442 1 QKPRGTRDFLPEEMIKWQYIEETIREVFERYGFKEIRTPIFEYTELFKRKVGEEtdivSKEMYTFKDKGGRSLTLRPEGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 135 VPFARYLAMNKLKR---MKRYQVGKVWRRESPaivQ-GRYREFCQCDFDIAGEFDPMIpDAECLRIMCEILSGLQLGDFL 210
Cdd:TIGR00442 81 APVARAVIENKLLLpkpFKLYYIGPMFRYERP---QkGRYRQFHQFGVEVIGSDSPLA-DAEIIALAADILKELGLKDFT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 211 IKVNDRRVVDGMFAvcgvpesKFRTICSSMDK-LDKMSWEDVRLEMVAGKGLAPEVADRIGDYVQchGGISLVEELFKDp 289
Cdd:TIGR00442 157 LEINSLGILEGRLE-------YREALIRYLDKhKDKLGEDSVRRLEKNPLRILDSKNEKIQELLK--NAPKILDFLCEE- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 290 rlsqsqlalqGLGDLKLLFEYLRLFGIadKISLDLSLARGLDYYTGVIYEAVLLESPAQagketlnvGSVAAGGRYDRLV 369
Cdd:TIGR00442 227 ----------SRAHFEELKELLDALGI--PYKIDPSLVRGLDYYTGTVFEFVTDDLGAQ--------GSICGGGRYDGLV 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 370 AQFDpkGHSVPCVGLSIGVERIFYLVEQKMKISCEKvrtTETQVFVATPQKNFLQERLKIIAQLWDAGIKAEMLYKNNpK 449
Cdd:TIGR00442 287 EELG--GPPTPAVGFAIGIERLILLLEELGLIPPPS---KKPDVYVVPLGEEAELEALKLAQKLRKAGIRVEVDLGGR-K 360
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 207445692 450 LLTQLHYCEKEDIPLMVIIGEQEQNEGVVKLRSVASREEVTVNR 493
Cdd:TIGR00442 361 LKKQLKYADKLGARFALIIGEDELENGTVTLKDLETGEQETVPL 404
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
71-396 |
1.58e-93 |
|
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: 284.88 E-value: 1.58e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 71 QMVVREKILDKIISCFKRHGAKGLDTPAFELKEMLTEK-YEDNFGLMYDLEDQGGELLSLRYDLTVPFARYLAMNKLKR- 148
Cdd:cd00773 1 EAALRRYIEDTLREVFERYGYEEIDTPVFEYTELFLRKsGDEVSKEMYRFKDKGGRDLALRPDLTAPVARAVAENLLSLp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 149 --MKRYQVGKVWRRESPAivQGRYREFCQCDFDIAGEfDPMIPDAECLRIMCEILSGLQLGDFLIKVNDRRVVDGmfaVC 226
Cdd:cd00773 81 lpLKLYYIGPVFRYERPQ--KGRYREFYQVGVEIIGS-DSPLADAEVIALAVEILEALGLKDFQIKINHRGILDG---IA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 227 GVPESKFRTICSSMDKLDKmswedvrlemvagkglapevadrigdyvqchggislveelfkdprlsqsqlalQGLGDLKL 306
Cdd:cd00773 155 GLLEDREEYIERLIDKLDK-----------------------------------------------------EALAHLEK 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 307 LFEYLRLFGIADKISLDLSLARGLDYYTGVIYEAVLLESPAQagketlnvGSVAAGGRYDRLVAQFDpkGHSVPCVGLSI 386
Cdd:cd00773 182 LLDYLEALGVDIKYSIDLSLVRGLDYYTGIVFEAVADGLGAQ--------GSIAGGGRYDGLLEEFG--GEDVPAVGFAI 251
|
330
....*....|
gi 207445692 387 GVERIFYLVE 396
Cdd:cd00773 252 GLERLLLALE 261
|
|
| PRK12420 |
PRK12420 |
histidyl-tRNA synthetase; Provisional |
62-491 |
6.35e-84 |
|
histidyl-tRNA synthetase; Provisional
Pssm-ID: 237097 [Multi-domain] Cd Length: 423 Bit Score: 265.83 E-value: 6.35e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 62 KGTRDLSPQQMVVREKILDKIISCFKRHGAKGLDTPAFELKEMLTEKY---EDNFGLMYDLEDQGGELLSLRYDLTVPFA 138
Cdd:PRK12420 8 KGTKDYLPEEQVLRNKIKRALEDVFERYGCKPLETPTLNMYELMSSKYgggDEILKEIYTLTDQGKRDLALRYDLTIPFA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 139 RYLAMNKLKRM--KRYQVGKVWrRESPaIVQGRYREFCQCDFDIAGEFDPMiPDAECLRIMCEILSGLQLgDFLIKVNDR 216
Cdd:PRK12420 88 KVVAMNPNIRLpfKRYEIGKVF-RDGP-IKQGRFREFIQCDVDIVGVESVM-AEAELMSMAFELFRRLNL-EVTIQYNNR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 217 RVVDGMFAVCGVPESKFRTICSSMDKLDKMSWEDVRLEmVAGKGLAPEVADRIGDYVQCHGGISLveELFKDprLSQSQL 296
Cdd:PRK12420 164 KLLNGILQAIGIPTELTSDVILSLDKIEKIGIDGVRKD-LLERGISEEMADTICNTVLSCLQLSI--ADFKE--AFNNPL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 297 ALQGLGDLKLLFEYLRLFGIADKISLDLSLARGLDYYTGVIYEAVLlespaqagKETLNVGSVAAGGRYDRLVAQFDPKG 376
Cdd:PRK12420 239 VAEGVNELQQLQQYLIALGINENCIFNPFLARGLTMYTGTVYEIFL--------KDGSITSSIGSGGRYDNIIGAFRGDD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 377 HSVPCVGLSIGVERIFYLVEQKMKIScekvrtTETQVFVATPQKNflQERLKIIAQLW-DAGIKAEMLYKNNpKLLTQLH 455
Cdd:PRK12420 311 MNYPTVGISFGLDVIYTALSQKETIS------STADVFIIPLGTE--LQCLQIAQQLRsTTGLKVELELAGR-KLKKALN 381
|
410 420 430
....*....|....*....|....*....|....*.
gi 207445692 456 YCEKEDIPLMVIIGEQEQNEGVVKLRSVASREEVTV 491
Cdd:PRK12420 382 YANKENIPYVLIIGEEEVSTGTVMLRNMKEGSEVKV 417
|
|
| PLN02530 |
PLN02530 |
histidine-tRNA ligase |
61-496 |
5.91e-49 |
|
histidine-tRNA ligase
Pssm-ID: 178145 [Multi-domain] Cd Length: 487 Bit Score: 175.32 E-value: 5.91e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 61 PKGTRDLSPQQMVVREKILDKIISCFKRHGAKGLDTPAFELKEMLTEKY-EDNFGLMYDLEDQGGELLSLRYDLTVPFAR 139
Cdd:PLN02530 73 PKGTRDFPPEDMRLRNWLFDHFREVSRLFGFEEVDAPVLESEELYIRKAgEEITDQLYNFEDKGGRRVALRPELTPSLAR 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 140 yLAMNKLKRM----KRYQVGKVWRRESpaIVQGRYREFCQCDFDIAGeFDPMIPDAECLRIMCEILS--GLQLGDFLIKV 213
Cdd:PLN02530 153 -LVLQKGKSLslplKWFAIGQCWRYER--MTRGRRREHYQWNMDIIG-VPGVEAEAELLAAIVTFFKrvGITSSDVGIKV 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 214 NDRRVVDGMFAVCGVPESKFRTICSSMDKLDKMSWEDVRLEMvAGKGLAPEVADRIGDYVQCHGgISLVEELFKDprlsq 293
Cdd:PLN02530 229 SSRKVLQAVLKSYGIPEESFAPVCVIVDKLEKLPREEIEKEL-DTLGVSEEAIEGILDVLSLKS-LDDLEALLGA----- 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 294 sqlALQGLGDLKLLFEYLRLFGIADKISLDLSLARGLDYYTGVIYEAVllespAQAGKetlnVGSVAAGGRYDRLVAQFD 373
Cdd:PLN02530 302 ---DSEAVADLKQLFSLAEAYGYQDWLVFDASVVRGLAYYTGIVFEGF-----DRAGK----LRAICGGGRYDRLLSTFG 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 374 pkGHSVPCVGLSIGVERIFYLVEQKmKISCEKVRTTETQVFvatPQKNFLQ-ERLKIIAQLWDAGIKAEMLYKNNpKLLT 452
Cdd:PLN02530 370 --GEDTPACGFGFGDAVIVELLKEK-GLLPELPHQVDDVVF---ALDEDLQgAAAGVASRLREKGRSVDLVLEPK-KLKW 442
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 207445692 453 QLHYCEKEDIPLMVIIGEQEQNEGVVKLRSVASREEVTVNRESL 496
Cdd:PLN02530 443 VFKHAERIGAKRLVLVGASEWERGMVRVKDLSSGEQTEVKLDEL 486
|
|
| hisZ |
PRK12292 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
61-442 |
1.51e-42 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 237043 [Multi-domain] Cd Length: 391 Bit Score: 155.79 E-value: 1.51e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 61 PKGTRDLSPQQMVVREKILDKIISCFKRHGAKGLDTPAFElkemltekYEDNFGL---------MYDLEDQG-GELLSLR 130
Cdd:PRK12292 6 PEGIRDLLPEEARKIEEIRRRLLDLFRRWGYEEVITPTLE--------YLDTLLAgggaildlrTFKLVDQLsGRTLGLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 131 YDLTVPFARyLAMNKLKRMKR-----YQvGKVWR---RESpaivqGRYREFCQCDFDIAGeFDPMIPDAECLRIMCEILS 202
Cdd:PRK12292 78 PDMTAQIAR-IAATRLANRPGplrlcYA-GNVFRaqeRGL-----GRSREFLQSGVELIG-DAGLEADAEVILLLLEALK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 203 GLQLGDFLIKVNDRRVVDGMFAVCGVPESKFRTICSSMDKLDKmswedVRLEMVAgKGLAPEVADRIGDYVQCHGGISLV 282
Cdd:PRK12292 150 ALGLPNFTLDLGHVGLFRALLEAAGLSEELEEVLRRALANKDY-----VALEELV-LDLSEELRDALLALPRLRGGREVL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 283 EELfkdPRLSQSQLALQGLGDLKLLFEYLRLFGIADKISLDLSLARGLDYYTGVIYEAVLLESPAqagketlnvgSVAAG 362
Cdd:PRK12292 224 EEA---RKLLPSLPIKRALDELEALAEALEKYGYGIPLSLDLGLLRHLDYYTGIVFEGYVDGVGN----------PIASG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 363 GRYDRLVAQFdpkGHSVPCVGLSIGVERIFYLVEQKmkiscekvRTTETQVFVATPQKNFLQERLKIIAQLWDAGIKAEM 442
Cdd:PRK12292 291 GRYDDLLGRF---GRARPATGFSLDLDRLLELQLEL--------PVEARKDLVIAPDSEALAAALAAAQELRKKGEIVVL 359
|
|
| HisZ |
COG3705 |
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism]; |
69-391 |
2.53e-42 |
|
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism];
Pssm-ID: 442919 [Multi-domain] Cd Length: 312 Bit Score: 153.02 E-value: 2.53e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 69 PQQMVVREKILDKIISCFKRHGAKGLDTPAFELKEMLTEKYEDNFGL-MYDLEDQGGELLSLRYDLTVPFARYLAmNKLK 147
Cdd:COG3705 2 PEEAARKEELRRRLLDVFRSWGYELVEPPLLEYLDSLLTGSGADLDLqTFKLVDQLGRTLGLRPDMTPQVARIAA-TRLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 148 RMKRYQ----VGKVWR-RESPAivqGRYREFCQC------DFDIAGefdpmipDAECLRIMCEILSGLQLGDFLIKVNDR 216
Cdd:COG3705 81 NRPGPLrlcyAGNVFRtRPSGL---GRSREFLQAgaeligHAGLEA-------DAEVIALALEALKAAGLEDFTLDLGHV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 217 RVVDGMFAVCGVPESKFRTICSSMDKLDKmswedVRLE-MVAGKGLAPEVADRIGDYVQCHGGISLVEELFKdprLSQSQ 295
Cdd:COG3705 151 GLFRALLEALGLSEEQREELRRALARKDA-----VELEeLLAELGLSEELAEALLALPELYGGEEVLARARA---LLLDA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 296 LALQGLGDLKLLFEYLRLFGIADKISLDLSLARGLDYYTGVIYEAVLlespAQAGKEtlnvgsVAAGGRYDRLVAQFdpk 375
Cdd:COG3705 223 AIRAALDELEALAEALAARGPDVRLTFDLSELRGYDYYTGIVFEAYA----PGVGDP------LARGGRYDGLLAAF--- 289
|
330
....*....|....*.
gi 207445692 376 GHSVPCVGLSIGVERI 391
Cdd:COG3705 290 GRARPATGFSLDLDRL 305
|
|
| tRNA-synt_His |
pfam13393 |
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ... |
63-391 |
3.81e-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: 144.27 E-value: 3.81e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 63 GTRDLSPQQMVVREKILDKIISCFKRHGAKGLDTPAFELKEMLTEKYEDNFGLMYDLEDQGGELLSLRYDLTVPFARYLA 142
Cdd:pfam13393 1 GIRDLLPPEARRIEELRRRLLDLFRSWGYELVMPPLLEYLDSLLTGTGADLDQTFKLVDQSGRLLGLRADITPQVARIDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 143 mnklKRMKRYQV------GKVWRRESPAIvqGRYREFCQCDFDIAGEFDPMiPDAECLRIMCEILSGLQLGDFLIKVNDR 216
Cdd:pfam13393 81 ----HRLNRPGPlrlcyaGSVLRTRPKGL--GRSREPLQVGAELIGHAGIE-ADAEIISLLLEALAAAGVPGVTLDLGHV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 217 RVVDGMFAVCGVPESKFRTIcssMDKLDKMSWEDVRlEMVAGKGLAPEVADRIGDYVQCHGGISLVEELFKdpRLSQSQL 296
Cdd:pfam13393 154 GLVRALLEAAGLSEALEEAL---RAALQRKDAAELA-ELAAEAGLPPALRRALLALPDLYGGPEVLDEARA--ALPGLPA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 297 ALQGLGDLKLLFEYLRLFGIADKISLDLSLARGLDYYTGVIYEAVLlespAQAGKEtlnvgsVAAGGRYDRLVAQFdpkG 376
Cdd:pfam13393 228 LQEALDELEALAALLEALGDGVRLTFDLAELRGYEYYTGIVFAAYA----PGVGEP------LARGGRYDDLGAAF---G 294
|
330
....*....|....*
gi 207445692 377 HSVPCVGLSIGVERI 391
Cdd:pfam13393 295 RARPATGFSLDLEAL 309
|
|
| syh |
CHL00201 |
histidine-tRNA synthetase; Provisional |
58-502 |
3.69e-27 |
|
histidine-tRNA synthetase; Provisional
Pssm-ID: 164576 [Multi-domain] Cd Length: 430 Bit Score: 113.46 E-value: 3.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 58 IKVPKGTRDLSPQQMVVREKILDKIISCFKRHGAKGLDTPAFELKEMLTEKYEDNFGL----MYDLEDQGGELLSLRYDL 133
Cdd:CHL00201 4 IQAIRGTKDILPDEINYWQFIHDKALTLLSLANYSEIRTPIFENSSLYDRGIGETTDIvnkeMYRFTDRSNRDITLRPEG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 134 TVPFARYLAMNKLKRMKRYQ----VGKVWRRESPAivQGRYREFCQCDFDIAGEFDPMiPDAECLRIMCEILSGLQLGDF 209
Cdd:CHL00201 84 TAGIVRAFIENKMDYHSNLQrlwySGPMFRYERPQ--SGRQRQFHQLGIEFIGSIDAR-ADTEVIHLAMQIFNELQVKNL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 210 LIKVN------DRRVVdgmfavcgvpESKFRTICSS-MDKLD-----KMSWEDVRlemvagkglapeVADRIGDYVQchg 277
Cdd:CHL00201 161 ILDINsigkleDRQSY----------QLKLVEYLSQyQDDLDtdsqnRLYSNPIR------------ILDSKNLKTQ--- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 278 gislvEELFKDPRLSQSqLALQGLGDLKLLFEYLRLFGIADKIslDLSLARGLDYYTGVIYEAVLLESPAQagketlnvG 357
Cdd:CHL00201 216 -----EILDGAPKISDF-LSLESTEHFYDVCTYLNLLNIPYKI--NYKLVRGLDYYNDTAFEIKTLSSNGQ--------D 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 358 SVAAGGRYDRLVAQFDpkGHSVPCVGLSIGVERIFYLVEQKMKISCEKVrttetQVFVATPQKNFLQERLKIIAQLWDAG 437
Cdd:CHL00201 280 TICGGGRYDSLIHQLG--GPKTPAVGCAIGLERLLLIAKDNIILPKQSI-----DVYIATQGLKAQKKGWEIIQFLEKQN 352
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 207445692 438 IKAEmLYKNNPKLLTQLHYCEKEDIPLMVIIGEQEQNEGVVKLRSVASREEVTVNRESLVAEIQK 502
Cdd:CHL00201 353 IKFE-LDLSSSNFHKQIKQAGKKRAKACIILGDNEIMDNCITIKWLDEQVQENAQYSNFKQEISY 416
|
|
| HisRS_anticodon |
cd00859 |
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases ... |
410-501 |
5.13e-27 |
|
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only.
Pssm-ID: 238436 [Multi-domain] Cd Length: 91 Bit Score: 104.16 E-value: 5.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 410 ETQVFVATPQKNFLQERLKIIAQLWDAGIKAEMLYKNnPKLLTQLHYCEKEDIPLMVIIGEQEQNEGVVKLRSVASREEV 489
Cdd:cd00859 1 EVDVYVVPLGEGALSEALELAEQLRDAGIKAEIDYGG-RKLKKQFKYADRSGARFAVILGEDELAAGVVTVKDLETGEQE 79
|
90
....*....|..
gi 207445692 490 TVNRESLVAEIQ 501
Cdd:cd00859 80 TVALDELVEELK 91
|
|
| hisZ |
PRK12295 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
78-391 |
6.55e-18 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 183413 [Multi-domain] Cd Length: 373 Bit Score: 85.37 E-value: 6.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 78 ILDKIISCFKRHGAKGLDTPAFELKEMLTEKY-EDNFGLMYDLEDQGGELLSLRYDLTVPFAR-YLAMNkLKRMKRYQ-V 154
Cdd:PRK12295 10 AAEALLASFEAAGAVRVDPPILQPAEPFLDLSgEDIRRRIFVTSDENGEELCLRPDFTIPVCRrHIATA-GGEPARYAyL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 155 GKVWRRESpaivqGRYREFCQCDFDIAGEFDPMIPDAECLRIMCEILSGLQLGDFLIKVNDRRVVDGMFAVCGVPES-KF 233
Cdd:PRK12295 89 GEVFRQRR-----DRASEFLQAGIESFGRADPAAADAEVLALALEALAALGPGDLEVRLGDVGLFAALVDALGLPPGwKR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 234 RTICS-----SMDKL-----------------------DKMSWEDVRLEM--------VAGKGLApEVADRIGDYVQCHG 277
Cdd:PRK12295 164 RLLRHfgrprSLDALlarlagprvdpldehagvlaalaDEAAARALVEDLmsiagispVGGRSPA-EIARRLLEKAALAA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 278 GISL-------VEELFK-DPRLSQSQLALQGL-GDLKL-------LFEYlRLFGIA------DKISLDLSLARGLDYYTG 335
Cdd:PRK12295 243 AARLpaealavLERFLAiSGPPDAALAALRALaADAGLdldaaldRFEA-RLAALAargidlERLRFSASFGRPLDYYTG 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 207445692 336 VIYEaVLLESPAQAgketlnvgSVAAGGRYDRLVAQFDpKGHSVPCVGLSIGVERI 391
Cdd:PRK12295 322 FVFE-IRAAGNGDP--------PLAGGGRYDGLLTRLG-AGEPIPAVGFSIWLDRL 367
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
412-503 |
5.80e-17 |
|
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA synthetases it is probably the anticodon binding domain.
Pssm-ID: 460819 [Multi-domain] Cd Length: 94 Bit Score: 76.09 E-value: 5.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 412 QVFVATPQKN---FLQERLKIIAQLWDAGIKAEmLYKNNPKLLTQLHYCEKEDIPLMVIIGEQEQNEGVVKLRSVASREE 488
Cdd:pfam03129 1 QVVVIPLGEKaeeLEEYAQKLAEELRAAGIRVE-LDDRNESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQ 79
|
90
....*....|....*
gi 207445692 489 VTVNRESLVAEIQKR 503
Cdd:pfam03129 80 ETVSLDELVEKLKEL 94
|
|
| HGTP_anticodon2 |
pfam12745 |
Anticodon binding domain of tRNAs; This is an HGTP_anticodon binding domain, found largely on ... |
413-503 |
5.29e-06 |
|
Anticodon binding domain of tRNAs; This is an HGTP_anticodon binding domain, found largely on Gcn2 proteins which bind tRNA to down regulate translation in certain stress situations.
Pssm-ID: 432758 Cd Length: 259 Bit Score: 47.99 E-value: 5.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 413 VFVATPQKNFL-QERLKIIAQLWDAGIKAEMLYKNNPKLLTQLHYCEKEDIPLMVIIGEQ----EQNEGVVKLRSVASRE 487
Cdd:pfam12745 8 VLVASFDASILrTTGVEILQELWAHGISADLAVDASYSPEDLVSRARDDGVSWIVIIKQQnkssDSKYKPLKVKNLLRKE 87
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90 100
....*....|....*....|
gi 207445692 488 EVTVNRESLVA----EIQKR 503
Cdd:pfam12745 88 DVDLDSDELVSwlrgEIRER 107
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| PRK12421 |
PRK12421 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
254-391 |
5.74e-05 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 237098 Cd Length: 392 Bit Score: 45.35 E-value: 5.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 254 EMVAGKGLAPEVADRIGDYVQCHGGISLVEElfkdprlSQSQLALQG------LGDLKLLFEYLRLFGIADKISLDLSLA 327
Cdd:PRK12421 200 EVCQNLGVGSDLRRMFYALARLNGGLEALDR-------ALSVLALQDaairqaLDELKTLAAHLKNRWPELPVSIDLAEL 272
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 207445692 328 RGLDYYTGVIYeAVLLESPAQAgketlnvgsVAAGGRYDRLVAQFdpkGHSVPCVGLSIGVERI 391
Cdd:PRK12421 273 RGYHYHTGLVF-AAYIPGRGQA---------LARGGRYDGIGEAF---GRARPATGFSMDLKEL 323
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|
| ProRS_anticodon_short |
cd00861 |
ProRS Prolyl-anticodon binding domain, short version found predominantly in bacteria. ProRS ... |
462-501 |
2.96e-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: 39.88 E-value: 2.96e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 207445692 462 IPLMVIIGEQEQNEGVVKLRSVASREEVTVNRESLVAEIQ 501
Cdd:cd00861 55 IPYRIVVGKKSAAEGIVEIKVRKTGEKEEISIDELLEFLQ 94
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| ThrRS_anticodon |
cd00860 |
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases ... |
411-501 |
6.53e-04 |
|
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only.
Pssm-ID: 238437 [Multi-domain] Cd Length: 91 Bit Score: 38.64 E-value: 6.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207445692 411 TQVFVATPQKNFLQERLKIIAQLWDAGIKAEMLYKNNpKLLTQLHYCEKEDIPLMVIIGEQEQNEGVVKLRSVASREEVT 490
Cdd:cd00860 2 VQVVVIPVTDEHLDYAKEVAKKLSDAGIRVEVDLRNE-KLGKKIREAQLQKIPYILVVGDKEVETGTVSVRTRDGGDLGS 80
|
90
....*....|.
gi 207445692 491 VNRESLVAEIQ 501
Cdd:cd00860 81 MSLDEFIEKLK 91
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