|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02972 |
PLN02972 |
Histidyl-tRNA synthetase |
12-504 |
0e+00 |
|
Histidyl-tRNA synthetase
Pssm-ID: 215525 [Multi-domain] Cd Length: 763 Bit Score: 538.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 12 WAALLSQLLRPPCASCTGAVrcqSQVAEAVLTSQLKahqEKPnfiiKIPKGTRDLSPQHMVVREKILDLVISCFKRHGAK 91
Cdd:PLN02972 292 WATQLLLLFDPKCPGFDSLV---DKVKEIVESNEVR---RLP----KIPKGTRDFAKEQMAIREKAFSIITSVFKRHGAT 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 92 GMDTPAFELKETLTEKYGEDSGLMYDLKDQGGELLSLRYDLTVPFARYLAMSKVKKMKRYHVGKVWRRESPSivQGRYRE 171
Cdd:PLN02972 362 ALDTPVFELRETLMGKYGEDSKLIYDLADQGGELCSLRYDLTVPFARYVAMNGITSFKRYQIAKVYRRDNPS--KGRYRE 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 172 FCQCDFDIAGQFDPMIPDAECLKIMCEILSGLQLGDFLIKVNDRRIVDGMFAACGVPESKFRAICSSIDKLDKMAWKDVR 251
Cdd:PLN02972 440 FYQCDFDIAGVYEPMGPDFEIIKVLTELLDELDIGTYEVKLNHRKLLDGMLEICGVPPEKFRTICSSIDKLDKQSFEQVK 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 252 HEMVAKKGLAPEVADRIGDYVQCHGG-VSLVEQMFQ-DPRLSQNKQALEGLEDLKLLFEYLNLFGIAEKISFDLSLARGL 329
Cdd:PLN02972 520 KEMVEEKGLSNETADKIGNFVKERGPpLELLSKLRQeGSEFLGNASSRAALDELEIMFKALEKSKAIGKIVFDLSLARGL 599
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 330 DYYTGVIYEAVLLQTptqageeplNVGSVAAGGRYDGLVGMFDPKghKVPCVGLSIGVERIFYIVEQRMKTKGEKVRTTE 409
Cdd:PLN02972 600 DYYTGVIYEAVFKGA---------QVGSIAAGGRYDNLVGMFSGK--QVPAVGVSLGIERVFAIMEQQEEEKSQVIRPTE 668
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 410 TQVFVATPQKNFLQERLKLITELWDAGIKAEmlYKNNPKLLTQLHYCESTGIPLVVIIGEQELKEGIIKIRSVASREEVA 489
Cdd:PLN02972 669 TEVLVSIIGDDKLALAAELVSELWNAGIKAE--YKVSTRKAKHLKRAKESGIPWMVLVGEKELSKGFVKLKNLEAGVEEE 746
|
490
....*....|....*
gi 384943856 490 IKRENLVAEIQKRLS 504
Cdd:PLN02972 747 VDRTCFVQELKAELL 761
|
|
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
57-505 |
8.80e-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: 345.18 E-value: 8.80e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 57 IKIPKGTRDLSPQHMVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSG--LMYDLKDQGGELLSLRYDLTV 134
Cdd:COG0124 4 IQAPRGTRDILPEESAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKIGEDIVekEMYTFEDRGGRSLTLRPEGTA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 135 PFARYLAMSK---VKKMKRYHVGKVWRRESPsivQ-GRYREFCQCDFDIAGQFDPMIpDAECLKIMCEILSGLQLGDFLI 210
Cdd:COG0124 84 PVARAVAEHGnelPFPFKLYYIGPVFRYERP---QkGRYRQFHQFGVEVIGSDSPLA-DAEVIALAADLLKALGLKDFTL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 211 KVNDRrivdgmfaacGVPESKFRAICSSIDKLDKMAWKDVrhemvakkgLAPEVADRIG-----DYVQCHGGV--SLVEQ 283
Cdd:COG0124 160 EINSR----------GLPEERAEALLRYLDKLDKIGHEDV---------LDEDSQRRLEtnplrAILDSKGPDcqEVLAD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 284 MfqdPRLSQNKqALEGLEDLKLLFEYLNLFGIaeKISFDLSLARGLDYYTGVIYEAVLLQTPTQageeplnvGSVAAGGR 363
Cdd:COG0124 221 A---PKLLDYL-GEEGLAHFEEVLELLDALGI--PYVIDPRLVRGLDYYTGTVFEIVTDGLGAQ--------GSVCGGGR 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 364 YDGLVGMFDpkGHKVPCVGLSIGVERIFYIVEQRmktKGEKVRTTETQVFVATPQKNFLQERLKLITELWDAGIKAEMLY 443
Cdd:COG0124 287 YDGLVEQLG--GPPTPAVGFAIGLERLLLLLEEL---GLLPAAEPPPDVYVVPLGEEARAEALKLAQELRAAGIRVELDL 361
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 384943856 444 KNNpKLLTQLHYCESTGIPLVVIIGEQELKEGIIKIRSVASREEVAIKRENLVAEIQKRLSE 505
Cdd:COG0124 362 GGR-KLKKQLKYADKSGAPFVLILGEDELANGTVTLKDLATGEQETVPLDELVEYLKELLAE 422
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
71-395 |
2.03e-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: 294.90 E-value: 2.03e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 71 MVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSG-LMYDLKDQGGELLSLRYDLTVPFARYLAMSKVKK-- 147
Cdd:cd00773 2 AALRRYIEDTLREVFERYGYEEIDTPVFEYTELFLRKSGDEVSkEMYRFKDKGGRDLALRPDLTAPVARAVAENLLSLpl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 148 -MKRYHVGKVWRRESPSivQGRYREFCQCDFDIAGqFDPMIPDAECLKIMCEILSGLQLGDFLIKVNDRRIVDGmfaACG 226
Cdd:cd00773 82 pLKLYYIGPVFRYERPQ--KGRYREFYQVGVEIIG-SDSPLADAEVIALAVEILEALGLKDFQIKINHRGILDG---IAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 227 VPESKFRAICSSIDKLDKmawkdvrhemvakkglapevadrigdyvqchggvslveqmfqdprlsqnkqalEGLEDLKLL 306
Cdd:cd00773 156 LLEDREEYIERLIDKLDK-----------------------------------------------------EALAHLEKL 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 307 FEYLNLFGIAEKISFDLSLARGLDYYTGVIYEAVLLQTPTQageeplnvGSVAAGGRYDGLVGMFDpkGHKVPCVGLSIG 386
Cdd:cd00773 183 LDYLEALGVDIKYSIDLSLVRGLDYYTGIVFEAVADGLGAQ--------GSIAGGGRYDGLLEEFG--GEDVPAVGFAIG 252
|
....*....
gi 384943856 387 VERIFYIVE 395
Cdd:cd00773 253 LERLLLALE 261
|
|
| hisS |
TIGR00442 |
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ... |
58-492 |
2.16e-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: 292.07 E-value: 2.16e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 58 KIPKGTRDLSPQHMVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSGL----MYDLKDQGGELLSLRYDLT 133
Cdd:TIGR00442 1 QKPRGTRDFLPEEMIKWQYIEETIREVFERYGFKEIRTPIFEYTELFKRKVGEETDIvskeMYTFKDKGGRSLTLRPEGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 134 VPFARYLAMSK---VKKMKRYHVGKVWRRESPsivQ-GRYREFCQCDFDIAGQFDPMIpDAECLKIMCEILSGLQLGDFL 209
Cdd:TIGR00442 81 APVARAVIENKlllPKPFKLYYIGPMFRYERP---QkGRYRQFHQFGVEVIGSDSPLA-DAEIIALAADILKELGLKDFT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 210 IKVNDRRIVDGMFAacgvpesKFRAICSSIDK-LDKMAWKDVRHEMVAKKGLAPEVADRIGDYVQchggvslveqmfQDP 288
Cdd:TIGR00442 157 LEINSLGILEGRLE-------YREALIRYLDKhKDKLGEDSVRRLEKNPLRILDSKNEKIQELLK------------NAP 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 289 RLSQNKQAlEGLEDLKLLFEYLNLFGIaeKISFDLSLARGLDYYTGVIYEAVLLQTPTQageeplnvGSVAAGGRYDGLV 368
Cdd:TIGR00442 218 KILDFLCE-ESRAHFEELKELLDALGI--PYKIDPSLVRGLDYYTGTVFEFVTDDLGAQ--------GSICGGGRYDGLV 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 369 GMFDpkGHKVPCVGLSIGVERIFYIVEQRmktKGEKVRTTETQVFVATPQKNFLQERLKLITELWDAGIKAEMLYKNNpK 448
Cdd:TIGR00442 287 EELG--GPPTPAVGFAIGIERLILLLEEL---GLIPPPSKKPDVYVVPLGEEAELEALKLAQKLRKAGIRVEVDLGGR-K 360
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 384943856 449 LLTQLHYCESTGIPLVVIIGEQELKEGIIKIRSVASREEVAIKR 492
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 ... |
62-390 |
3.12e-41 |
|
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: 150.04 E-value: 3.12e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 62 GTRDLSPQHMVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSGLMYDLKDQGGELLSLRYDLTVPFARYLA 141
Cdd:pfam13393 1 GIRDLLPPEARRIEELRRRLLDLFRSWGYELVMPPLLEYLDSLLTGTGADLDQTFKLVDQSGRLLGLRADITPQVARIDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 142 -MSKVKKMKR-YHVGKVWRRESPSIvqGRYREFCQCDFDIAGQFDPMiPDAECLKIMCEILSGLQLGDFLIKVNDRRIVD 219
Cdd:pfam13393 81 hRLNRPGPLRlCYAGSVLRTRPKGL--GRSREPLQVGAELIGHAGIE-ADAEIISLLLEALAAAGVPGVTLDLGHVGLVR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 220 GMFAACGVPESKFRAICSSIDKLDkmaWKDVRhEMVAKKGLAPEVADRIGDYVQCHGGVSLVEQMFQdpRLSQNKQALEG 299
Cdd:pfam13393 158 ALLEAAGLSEALEEALRAALQRKD---AAELA-ELAAEAGLPPALRRALLALPDLYGGPEVLDEARA--ALPGLPALQEA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 300 LEDLKLLFEYLNLFGIAEKISFDLSLARGLDYYTGVIYEAVLLQTPtqageeplnvGSVAAGGRYDGLVGMFdpkGHKVP 379
Cdd:pfam13393 232 LDELEALAALLEALGDGVRLTFDLAELRGYEYYTGIVFAAYAPGVG----------EPLARGGRYDDLGAAF---GRARP 298
|
330
....*....|.
gi 384943856 380 CVGLSIGVERI 390
Cdd:pfam13393 299 ATGFSLDLEAL 309
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02972 |
PLN02972 |
Histidyl-tRNA synthetase |
12-504 |
0e+00 |
|
Histidyl-tRNA synthetase
Pssm-ID: 215525 [Multi-domain] Cd Length: 763 Bit Score: 538.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 12 WAALLSQLLRPPCASCTGAVrcqSQVAEAVLTSQLKahqEKPnfiiKIPKGTRDLSPQHMVVREKILDLVISCFKRHGAK 91
Cdd:PLN02972 292 WATQLLLLFDPKCPGFDSLV---DKVKEIVESNEVR---RLP----KIPKGTRDFAKEQMAIREKAFSIITSVFKRHGAT 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 92 GMDTPAFELKETLTEKYGEDSGLMYDLKDQGGELLSLRYDLTVPFARYLAMSKVKKMKRYHVGKVWRRESPSivQGRYRE 171
Cdd:PLN02972 362 ALDTPVFELRETLMGKYGEDSKLIYDLADQGGELCSLRYDLTVPFARYVAMNGITSFKRYQIAKVYRRDNPS--KGRYRE 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 172 FCQCDFDIAGQFDPMIPDAECLKIMCEILSGLQLGDFLIKVNDRRIVDGMFAACGVPESKFRAICSSIDKLDKMAWKDVR 251
Cdd:PLN02972 440 FYQCDFDIAGVYEPMGPDFEIIKVLTELLDELDIGTYEVKLNHRKLLDGMLEICGVPPEKFRTICSSIDKLDKQSFEQVK 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 252 HEMVAKKGLAPEVADRIGDYVQCHGG-VSLVEQMFQ-DPRLSQNKQALEGLEDLKLLFEYLNLFGIAEKISFDLSLARGL 329
Cdd:PLN02972 520 KEMVEEKGLSNETADKIGNFVKERGPpLELLSKLRQeGSEFLGNASSRAALDELEIMFKALEKSKAIGKIVFDLSLARGL 599
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 330 DYYTGVIYEAVLLQTptqageeplNVGSVAAGGRYDGLVGMFDPKghKVPCVGLSIGVERIFYIVEQRMKTKGEKVRTTE 409
Cdd:PLN02972 600 DYYTGVIYEAVFKGA---------QVGSIAAGGRYDNLVGMFSGK--QVPAVGVSLGIERVFAIMEQQEEEKSQVIRPTE 668
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 410 TQVFVATPQKNFLQERLKLITELWDAGIKAEmlYKNNPKLLTQLHYCESTGIPLVVIIGEQELKEGIIKIRSVASREEVA 489
Cdd:PLN02972 669 TEVLVSIIGDDKLALAAELVSELWNAGIKAE--YKVSTRKAKHLKRAKESGIPWMVLVGEKELSKGFVKLKNLEAGVEEE 746
|
490
....*....|....*
gi 384943856 490 IKRENLVAEIQKRLS 504
Cdd:PLN02972 747 VDRTCFVQELKAELL 761
|
|
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
57-505 |
8.80e-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: 345.18 E-value: 8.80e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 57 IKIPKGTRDLSPQHMVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSG--LMYDLKDQGGELLSLRYDLTV 134
Cdd:COG0124 4 IQAPRGTRDILPEESAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKIGEDIVekEMYTFEDRGGRSLTLRPEGTA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 135 PFARYLAMSK---VKKMKRYHVGKVWRRESPsivQ-GRYREFCQCDFDIAGQFDPMIpDAECLKIMCEILSGLQLGDFLI 210
Cdd:COG0124 84 PVARAVAEHGnelPFPFKLYYIGPVFRYERP---QkGRYRQFHQFGVEVIGSDSPLA-DAEVIALAADLLKALGLKDFTL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 211 KVNDRrivdgmfaacGVPESKFRAICSSIDKLDKMAWKDVrhemvakkgLAPEVADRIG-----DYVQCHGGV--SLVEQ 283
Cdd:COG0124 160 EINSR----------GLPEERAEALLRYLDKLDKIGHEDV---------LDEDSQRRLEtnplrAILDSKGPDcqEVLAD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 284 MfqdPRLSQNKqALEGLEDLKLLFEYLNLFGIaeKISFDLSLARGLDYYTGVIYEAVLLQTPTQageeplnvGSVAAGGR 363
Cdd:COG0124 221 A---PKLLDYL-GEEGLAHFEEVLELLDALGI--PYVIDPRLVRGLDYYTGTVFEIVTDGLGAQ--------GSVCGGGR 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 364 YDGLVGMFDpkGHKVPCVGLSIGVERIFYIVEQRmktKGEKVRTTETQVFVATPQKNFLQERLKLITELWDAGIKAEMLY 443
Cdd:COG0124 287 YDGLVEQLG--GPPTPAVGFAIGLERLLLLLEEL---GLLPAAEPPPDVYVVPLGEEARAEALKLAQELRAAGIRVELDL 361
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 384943856 444 KNNpKLLTQLHYCESTGIPLVVIIGEQELKEGIIKIRSVASREEVAIKRENLVAEIQKRLSE 505
Cdd:COG0124 362 GGR-KLKKQLKYADKSGAPFVLILGEDELANGTVTLKDLATGEQETVPLDELVEYLKELLAE 422
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
71-395 |
2.03e-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: 294.90 E-value: 2.03e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 71 MVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSG-LMYDLKDQGGELLSLRYDLTVPFARYLAMSKVKK-- 147
Cdd:cd00773 2 AALRRYIEDTLREVFERYGYEEIDTPVFEYTELFLRKSGDEVSkEMYRFKDKGGRDLALRPDLTAPVARAVAENLLSLpl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 148 -MKRYHVGKVWRRESPSivQGRYREFCQCDFDIAGqFDPMIPDAECLKIMCEILSGLQLGDFLIKVNDRRIVDGmfaACG 226
Cdd:cd00773 82 pLKLYYIGPVFRYERPQ--KGRYREFYQVGVEIIG-SDSPLADAEVIALAVEILEALGLKDFQIKINHRGILDG---IAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 227 VPESKFRAICSSIDKLDKmawkdvrhemvakkglapevadrigdyvqchggvslveqmfqdprlsqnkqalEGLEDLKLL 306
Cdd:cd00773 156 LLEDREEYIERLIDKLDK-----------------------------------------------------EALAHLEKL 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 307 FEYLNLFGIAEKISFDLSLARGLDYYTGVIYEAVLLQTPTQageeplnvGSVAAGGRYDGLVGMFDpkGHKVPCVGLSIG 386
Cdd:cd00773 183 LDYLEALGVDIKYSIDLSLVRGLDYYTGIVFEAVADGLGAQ--------GSIAGGGRYDGLLEEFG--GEDVPAVGFAIG 252
|
....*....
gi 384943856 387 VERIFYIVE 395
Cdd:cd00773 253 LERLLLALE 261
|
|
| hisS |
TIGR00442 |
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ... |
58-492 |
2.16e-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: 292.07 E-value: 2.16e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 58 KIPKGTRDLSPQHMVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSGL----MYDLKDQGGELLSLRYDLT 133
Cdd:TIGR00442 1 QKPRGTRDFLPEEMIKWQYIEETIREVFERYGFKEIRTPIFEYTELFKRKVGEETDIvskeMYTFKDKGGRSLTLRPEGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 134 VPFARYLAMSK---VKKMKRYHVGKVWRRESPsivQ-GRYREFCQCDFDIAGQFDPMIpDAECLKIMCEILSGLQLGDFL 209
Cdd:TIGR00442 81 APVARAVIENKlllPKPFKLYYIGPMFRYERP---QkGRYRQFHQFGVEVIGSDSPLA-DAEIIALAADILKELGLKDFT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 210 IKVNDRRIVDGMFAacgvpesKFRAICSSIDK-LDKMAWKDVRHEMVAKKGLAPEVADRIGDYVQchggvslveqmfQDP 288
Cdd:TIGR00442 157 LEINSLGILEGRLE-------YREALIRYLDKhKDKLGEDSVRRLEKNPLRILDSKNEKIQELLK------------NAP 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 289 RLSQNKQAlEGLEDLKLLFEYLNLFGIaeKISFDLSLARGLDYYTGVIYEAVLLQTPTQageeplnvGSVAAGGRYDGLV 368
Cdd:TIGR00442 218 KILDFLCE-ESRAHFEELKELLDALGI--PYKIDPSLVRGLDYYTGTVFEFVTDDLGAQ--------GSICGGGRYDGLV 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 369 GMFDpkGHKVPCVGLSIGVERIFYIVEQRmktKGEKVRTTETQVFVATPQKNFLQERLKLITELWDAGIKAEMLYKNNpK 448
Cdd:TIGR00442 287 EELG--GPPTPAVGFAIGIERLILLLEEL---GLIPPPSKKPDVYVVPLGEEAELEALKLAQKLRKAGIRVEVDLGGR-K 360
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 384943856 449 LLTQLHYCESTGIPLVVIIGEQELKEGIIKIRSVASREEVAIKR 492
Cdd:TIGR00442 361 LKKQLKYADKLGARFALIIGEDELENGTVTLKDLETGEQETVPL 404
|
|
| PRK12420 |
PRK12420 |
histidyl-tRNA synthetase; Provisional |
61-491 |
1.02e-82 |
|
histidyl-tRNA synthetase; Provisional
Pssm-ID: 237097 [Multi-domain] Cd Length: 423 Bit Score: 262.74 E-value: 1.02e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 61 KGTRDLSPQHMVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYG---EDSGLMYDLKDQGGELLSLRYDLTVPFA 137
Cdd:PRK12420 8 KGTKDYLPEEQVLRNKIKRALEDVFERYGCKPLETPTLNMYELMSSKYGggdEILKEIYTLTDQGKRDLALRYDLTIPFA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 138 RYLAMSKVKKM--KRYHVGKVWrRESPsIVQGRYREFCQCDFDIAGQFDPMiPDAECLKIMCEILSGLQLgDFLIKVNDR 215
Cdd:PRK12420 88 KVVAMNPNIRLpfKRYEIGKVF-RDGP-IKQGRFREFIQCDVDIVGVESVM-AEAELMSMAFELFRRLNL-EVTIQYNNR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 216 RIVDGMFAACGVPESKFRAICSSIDKLDKMAWKDVRHEmVAKKGLAPEVADRIGDYVQCHGGVSLVEqmFQDprLSQNKQ 295
Cdd:PRK12420 164 KLLNGILQAIGIPTELTSDVILSLDKIEKIGIDGVRKD-LLERGISEEMADTICNTVLSCLQLSIAD--FKE--AFNNPL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 296 ALEGLEDLKLLFEYLNLFGIAEKISFDLSLARGLDYYTGVIYEAVLlqtptqagEEPLNVGSVAAGGRYDGLVGMFDPKG 375
Cdd:PRK12420 239 VAEGVNELQQLQQYLIALGINENCIFNPFLARGLTMYTGTVYEIFL--------KDGSITSSIGSGGRYDNIIGAFRGDD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 376 HKVPCVGLSIGVERIFYIVEQRmktkgekVRTTETQVFVATPQKNFLQERLKLITELWDAGIKAEMLYKNNpKLLTQLHY 455
Cdd:PRK12420 311 MNYPTVGISFGLDVIYTALSQK-------ETISSTADVFIIPLGTELQCLQIAQQLRSTTGLKVELELAGR-KLKKALNY 382
|
410 420 430
....*....|....*....|....*....|....*.
gi 384943856 456 CESTGIPLVVIIGEQELKEGIIKIRSVASREEVAIK 491
Cdd:PRK12420 383 ANKENIPYVLIIGEEEVSTGTVMLRNMKEGSEVKVP 418
|
|
| hisZ_biosyn_reg |
TIGR00443 |
ATP phosphoribosyltransferase, regulatory subunit; Apparant second copies of histidyl-tRNA ... |
64-390 |
3.26e-52 |
|
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: 179.35 E-value: 3.26e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 64 RDLSPQHMVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSGLMYDLKDQGGELLSLRYDLTVPFARyLAMS 143
Cdd:TIGR00443 1 RDLLPEEAARKEEIERQLQDVFRSWGYQEIITPTLEYLDTLSAGSGILNEDLFKLFDQLGRVLGLRPDMTAPIAR-LVST 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 144 KVKKMKR----YHVGKVWRRESPSIvqGRYREFCQCDFDIAGQfDPMIPDAECLKIMCEILSGLQLGDFLIKVNDRRIVD 219
Cdd:TIGR00443 80 RLRDRPLplrlCYAGNVFRTNESGG--GRSREFTQAGVELIGA-GGPAADAEVIALLIEALKALGLKDFKIELGHVGLVR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 220 GMFAACGVPESKFRAICSSIDKLDKMAWKdvrhEMVAKKGLAPEVADRIGDYVQCHGGVSLVEQMFQdpRLSQNKQALEG 299
Cdd:TIGR00443 157 ALLEEAGLPEEAREALREALARKDLVALE----ELVAELGLSPEVRERLLALPRLRGDGEEVLEEAR--ALAGSETAEAA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 300 LEDLKLLFEYLNLFGIAEKISFDLSLARGLDYYTGVIYEAVLlqtpTQAGEeplnvgSVAAGGRYDGLVGMFdpkGHKVP 379
Cdd:TIGR00443 231 LDELEAVLELLEARGVEEYISLDLGLVRGYHYYTGLIFEGYA----PGLGA------PLAGGGRYDELLGRF---GRPLP 297
|
330
....*....|.
gi 384943856 380 CVGLSIGVERI 390
Cdd:TIGR00443 298 ATGFALNLERL 308
|
|
| PLN02530 |
PLN02530 |
histidine-tRNA ligase |
2-495 |
3.08e-51 |
|
histidine-tRNA ligase
Pssm-ID: 178145 [Multi-domain] Cd Length: 487 Bit Score: 181.48 E-value: 3.08e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 2 PLLGLLPRRAWAALLSQLLRPPCASCTGAVRCQSQVAEAVLTSQLKAhqeKPNFIIKIPKGTRDLSPQHMVVREKILDLV 81
Cdd:PLN02530 18 PSLPLSSRCSFLLSASSPRGGRCAASAAAGGGRSGGTTAPPSVQEDG---KPKIDVNPPKGTRDFPPEDMRLRNWLFDHF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 82 ISCFKRHGAKGMDTPAFELKETLTEKYGED-SGLMYDLKDQGGELLSLRYDLTVPFARyLAMSKVKKM----KRYHVGKV 156
Cdd:PLN02530 95 REVSRLFGFEEVDAPVLESEELYIRKAGEEiTDQLYNFEDKGGRRVALRPELTPSLAR-LVLQKGKSLslplKWFAIGQC 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 157 WRRESpsIVQGRYREFCQCDFDIAGqFDPMIPDAECLKIMCEILS--GLQLGDFLIKVNDRRIVDGMFAACGVPESKFRA 234
Cdd:PLN02530 174 WRYER--MTRGRRREHYQWNMDIIG-VPGVEAEAELLAAIVTFFKrvGITSSDVGIKVSSRKVLQAVLKSYGIPEESFAP 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 235 ICSSIDKLDKMAWKDVRHEMvAKKGLAPEVADRIGDYVQCHGGVSLVEQMFQDPrlsqnkqalEGLEDLKLLFEYLNLFG 314
Cdd:PLN02530 251 VCVIVDKLEKLPREEIEKEL-DTLGVSEEAIEGILDVLSLKSLDDLEALLGADS---------EAVADLKQLFSLAEAYG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 315 IAEKISFDLSLARGLDYYTGVIYEAVllqtpTQAGEeplnVGSVAAGGRYDGLVGMFDpkGHKVPCVGLSIG--Verify 392
Cdd:PLN02530 321 YQDWLVFDASVVRGLAYYTGIVFEGF-----DRAGK----LRAICGGGRYDRLLSTFG--GEDTPACGFGFGdaV----- 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 393 IVEqRMKTKG---EKVRTTETQVFvatPQKNFLQ-ERLKLITELWDAGIKAEMLYKNNpKLLTQLHYCESTGIPLVVIIG 468
Cdd:PLN02530 385 IVE-LLKEKGllpELPHQVDDVVF---ALDEDLQgAAAGVASRLREKGRSVDLVLEPK-KLKWVFKHAERIGAKRLVLVG 459
|
490 500
....*....|....*....|....*..
gi 384943856 469 EQELKEGIIKIRSVASREEVAIKRENL 495
Cdd:PLN02530 460 ASEWERGMVRVKDLSSGEQTEVKLDEL 486
|
|
| HisZ |
COG3705 |
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism]; |
74-390 |
3.75e-47 |
|
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism];
Pssm-ID: 442919 [Multi-domain] Cd Length: 312 Bit Score: 166.12 E-value: 3.75e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 74 REKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSGL-MYDLKDQGGELLSLRYDLTVPFARYLAmSKVKKMKR-- 150
Cdd:COG3705 8 KEELRRRLLDVFRSWGYELVEPPLLEYLDSLLTGSGADLDLqTFKLVDQLGRTLGLRPDMTPQVARIAA-TRLANRPGpl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 151 --YHVGKVWRRESPSivQGRYREFCQC------DFDIAGqfdpmipDAECLKIMCEILSGLQLGDFLIKVNDRRIVDGMF 222
Cdd:COG3705 87 rlCYAGNVFRTRPSG--LGRSREFLQAgaeligHAGLEA-------DAEVIALALEALKAAGLEDFTLDLGHVGLFRALL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 223 AACGVPESKFRAICSSIDKLDkmaWKDVRhEMVAKKGLAPEVADRIGDYVQCHGGVSLVEQMFQdprLSQNKQALEGLED 302
Cdd:COG3705 158 EALGLSEEQREELRRALARKD---AVELE-ELLAELGLSEELAEALLALPELYGGEEVLARARA---LLLDAAIRAALDE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 303 LKLLFEYLNLFGIAEKISFDLSLARGLDYYTGVIYEAVllqTPTQAGEeplnvgsVAAGGRYDGLVGMFdpkGHKVPCVG 382
Cdd:COG3705 231 LEALAEALAARGPDVRLTFDLSELRGYDYYTGIVFEAY---APGVGDP-------LARGGRYDGLLAAF---GRARPATG 297
|
....*...
gi 384943856 383 LSIGVERI 390
Cdd:COG3705 298 FSLDLDRL 305
|
|
| hisZ |
PRK12292 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
59-441 |
2.10e-46 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 237043 [Multi-domain] Cd Length: 391 Bit Score: 166.19 E-value: 2.10e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 59 IPKGTRDLSPQHMVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSGL-MYDLKDQG-GELLSLRYDLTVPF 136
Cdd:PRK12292 5 LPEGIRDLLPEEARKIEEIRRRLLDLFRRWGYEEVITPTLEYLDTLLAGGGAILDLrTFKLVDQLsGRTLGLRPDMTAQI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 137 ARyLAMSKVKKMKR-----YHvGKVWR-RESPSivqGRYREFCQCDFDIAGqFDPMIPDAECLKIMCEILSGLQLGDFLI 210
Cdd:PRK12292 85 AR-IAATRLANRPGplrlcYA-GNVFRaQERGL---GRSREFLQSGVELIG-DAGLEADAEVILLLLEALKALGLPNFTL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 211 KVNDRRIVDGMFAACGVPESKFRAICSSIDKLDKMAWKdvrhEMVAkkGLAPEVADRIGDYVQCHGGVSLVEQMfqdPRL 290
Cdd:PRK12292 159 DLGHVGLFRALLEAAGLSEELEEVLRRALANKDYVALE----ELVL--DLSEELRDALLALPRLRGGREVLEEA---RKL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 291 SQNKQALEGLEDLKLLFEYLNLFGIAEKISFDLSLARGLDYYTGVIYEAVllqtptqAGEEPLNVGSvaaGGRYDGLVGM 370
Cdd:PRK12292 230 LPSLPIKRALDELEALAEALEKYGYGIPLSLDLGLLRHLDYYTGIVFEGY-------VDGVGNPIAS---GGRYDDLLGR 299
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 384943856 371 FdpkGHKVPCVGLSIGVERifyIVEQRMKTKgekvrTTETQVFVATPQKNFLQERLKLITELWDAGIKAEM 441
Cdd:PRK12292 300 F---GRARPATGFSLDLDR---LLELQLELP-----VEARKDLVIAPDSEALAAALAAAQELRKKGEIVVL 359
|
|
| tRNA-synt_His |
pfam13393 |
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ... |
62-390 |
3.12e-41 |
|
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: 150.04 E-value: 3.12e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 62 GTRDLSPQHMVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSGLMYDLKDQGGELLSLRYDLTVPFARYLA 141
Cdd:pfam13393 1 GIRDLLPPEARRIEELRRRLLDLFRSWGYELVMPPLLEYLDSLLTGTGADLDQTFKLVDQSGRLLGLRADITPQVARIDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 142 -MSKVKKMKR-YHVGKVWRRESPSIvqGRYREFCQCDFDIAGQFDPMiPDAECLKIMCEILSGLQLGDFLIKVNDRRIVD 219
Cdd:pfam13393 81 hRLNRPGPLRlCYAGSVLRTRPKGL--GRSREPLQVGAELIGHAGIE-ADAEIISLLLEALAAAGVPGVTLDLGHVGLVR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 220 GMFAACGVPESKFRAICSSIDKLDkmaWKDVRhEMVAKKGLAPEVADRIGDYVQCHGGVSLVEQMFQdpRLSQNKQALEG 299
Cdd:pfam13393 158 ALLEAAGLSEALEEALRAALQRKD---AAELA-ELAAEAGLPPALRRALLALPDLYGGPEVLDEARA--ALPGLPALQEA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 300 LEDLKLLFEYLNLFGIAEKISFDLSLARGLDYYTGVIYEAVLLQTPtqageeplnvGSVAAGGRYDGLVGMFdpkGHKVP 379
Cdd:pfam13393 232 LDELEALAALLEALGDGVRLTFDLAELRGYEYYTGIVFAAYAPGVG----------EPLARGGRYDDLGAAF---GRARP 298
|
330
....*....|.
gi 384943856 380 CVGLSIGVERI 390
Cdd:pfam13393 299 ATGFSLDLEAL 309
|
|
| HisRS_anticodon |
cd00859 |
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases ... |
409-500 |
2.70e-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: 107.63 E-value: 2.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 409 ETQVFVATPQKNFLQERLKLITELWDAGIKAEMLYKNnPKLLTQLHYCESTGIPLVVIIGEQELKEGIIKIRSVASREEV 488
Cdd:cd00859 1 EVDVYVVPLGEGALSEALELAEQLRDAGIKAEIDYGG-RKLKKQFKYADRSGARFAVILGEDELAAGVVTVKDLETGEQE 79
|
90
....*....|..
gi 384943856 489 AIKRENLVAEIQ 500
Cdd:cd00859 80 TVALDELVEELK 91
|
|
| syh |
CHL00201 |
histidine-tRNA synthetase; Provisional |
61-501 |
4.60e-28 |
|
histidine-tRNA synthetase; Provisional
Pssm-ID: 164576 [Multi-domain] Cd Length: 430 Bit Score: 116.15 E-value: 4.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 61 KGTRDLSPQHMVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSGL----MYDLKDQGGELLSLRYDLTVPF 136
Cdd:CHL00201 8 RGTKDILPDEINYWQFIHDKALTLLSLANYSEIRTPIFENSSLYDRGIGETTDIvnkeMYRFTDRSNRDITLRPEGTAGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 137 ARYLAMSKVKKMKR----YHVGKVWRRESPSivQGRYREFCQCDFDIAGQFDPMiPDAECLKIMCEILSGLQLGDFLIKV 212
Cdd:CHL00201 88 VRAFIENKMDYHSNlqrlWYSGPMFRYERPQ--SGRQRQFHQLGIEFIGSIDAR-ADTEVIHLAMQIFNELQVKNLILDI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 213 N------DRRIVdgmfaacgvpESKFRAICSSI-DKLDKmawkDVRHEMVAKkglaP-EVADRIGDYVQchggvslvEQM 284
Cdd:CHL00201 165 NsigkleDRQSY----------QLKLVEYLSQYqDDLDT----DSQNRLYSN----PiRILDSKNLKTQ--------EIL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 285 FQDPRLSqNKQALEGLEDLKLLFEYLNLFGIAEKISFdlSLARGLDYYTGVIYEavlLQTPTQAGEEplnvgSVAAGGRY 364
Cdd:CHL00201 219 DGAPKIS-DFLSLESTEHFYDVCTYLNLLNIPYKINY--KLVRGLDYYNDTAFE---IKTLSSNGQD-----TICGGGRY 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 365 DGLVGMFDpkGHKVPCVGLSIGVERIFYIVEQRMKTKGEKVrttetQVFVATPQKNFLQERLKLITELWDAGIKAEmLYK 444
Cdd:CHL00201 288 DSLIHQLG--GPKTPAVGCAIGLERLLLIAKDNIILPKQSI-----DVYIATQGLKAQKKGWEIIQFLEKQNIKFE-LDL 359
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 384943856 445 NNPKLLTQLHYCESTGIPLVVIIGEQELKEGIIKIRSVASREEVAIKRENLVAEIQK 501
Cdd:CHL00201 360 SSSNFHKQIKQAGKKRAKACIILGDNEIMDNCITIKWLDEQVQENAQYSNFKQEISY 416
|
|
| hisZ |
PRK12295 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
77-390 |
9.31e-21 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 183413 [Multi-domain] Cd Length: 373 Bit Score: 93.84 E-value: 9.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 77 ILDLVISCFKRHGAKGMDTPAFELKETLTEKYGED-SGLMYDLKDQGGELLSLRYDLTVPFAR-YLAMSKVKKMKRYHVG 154
Cdd:PRK12295 10 AAEALLASFEAAGAVRVDPPILQPAEPFLDLSGEDiRRRIFVTSDENGEELCLRPDFTIPVCRrHIATAGGEPARYAYLG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 155 KVWRRESpsivqGRYREFCQCDFDIAGQFDPMIPDAECLKIMCEILSGLQLGDFLIKVNDRRIVDGMFAACGVPE----- 229
Cdd:PRK12295 90 EVFRQRR-----DRASEFLQAGIESFGRADPAAADAEVLALALEALAALGPGDLEVRLGDVGLFAALVDALGLPPgwkrr 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 230 --------SKFRAIcssIDKL-------------------DKMAWKDVRHEMVAKKGLAP-------EVADRIGDYVQCH 275
Cdd:PRK12295 165 llrhfgrpRSLDAL---LARLagprvdpldehagvlaalaDEAAARALVEDLMSIAGISPvggrspaEIARRLLEKAALA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 276 GGVSLVEQMFQdpRLSQ-------NKQALEGLEDL----KL-LFEYLNLF----------GIA-EKISFDLSLARGLDYY 332
Cdd:PRK12295 242 AAARLPAEALA--VLERflaisgpPDAALAALRALaadaGLdLDAALDRFearlaalaarGIDlERLRFSASFGRPLDYY 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 384943856 333 TGVIYEAvllqTPTQAGEEPLnvgsvAAGGRYDGLVGMFDpKGHKVPCVGLSIGVERI 390
Cdd:PRK12295 320 TGFVFEI----RAAGNGDPPL-----AGGGRYDGLLTRLG-AGEPIPAVGFSIWLDRL 367
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
411-502 |
3.84e-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: 79.17 E-value: 3.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 411 QVFVATPQKN---FLQERLKLITELWDAGIKAEmLYKNNPKLLTQLHYCESTGIPLVVIIGEQELKEGIIKIRSVASREE 487
Cdd:pfam03129 1 QVVVIPLGEKaeeLEEYAQKLAEELRAAGIRVE-LDDRNESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQ 79
|
90
....*....|....*
gi 384943856 488 VAIKRENLVAEIQKR 502
Cdd:pfam03129 80 ETVSLDELVEKLKEL 94
|
|
| HGTP_anticodon2 |
pfam12745 |
Anticodon binding domain of tRNAs; This is an HGTP_anticodon binding domain, found largely on ... |
412-502 |
7.52e-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: 7.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 412 VFVATPQKNFL-QERLKLITELWDAGIKAEMLYKNNPKLLTQLHYCESTGIPLVVIIGEQEL----KEGIIKIRSVASRE 486
Cdd:pfam12745 8 VLVASFDASILrTTGVEILQELWAHGISADLAVDASYSPEDLVSRARDDGVSWIVIIKQQNKssdsKYKPLKVKNLLRKE 87
|
90 100
....*....|....*....|
gi 384943856 487 EVAIKRENLVA----EIQKR 502
Cdd:pfam12745 88 DVDLDSDELVSwlrgEIRER 107
|
|
| PRK12421 |
PRK12421 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
60-390 |
8.68e-07 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 237098 Cd Length: 392 Bit Score: 51.12 E-value: 8.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 60 PKGTRDLSP---QHM-VVREKILDLVIScfkrHGAKGMDTPAFELKETLTEKYGEDSGLM-YDLKDQ-GGELLSLRYDLT 133
Cdd:PRK12421 10 PDGVADVLPeeaQKIeRLRRRLLDLFAS----RGYQLVMPPLIEYLESLLTGAGQDLKLQtFKLIDQlSGRLMGVRADIT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 134 VPFARYLA-MSKVKKMKRY-HVGKVWRRESPSIvqGRYREFCQCDFDIAGQfDPMIPDAECLKIMCEILSGLQLGDFLIK 211
Cdd:PRK12421 86 PQVARIDAhLLNREGVARLcYAGSVLHTLPQGL--FGSRTPLQLGAELYGH-AGIEADLEIIRLMLGLLRNAGVPALHLD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 212 VNDRRIVDGMFAACGVPESKFRAIcssidkLDKMAWKDVR--HEMVAKKGLAPEVADRIGDYVQCHGGV-SLVEQMFQDP 288
Cdd:PRK12421 163 LGHVGIFRRLAELAGLSPEEEEEL------FDLLQRKALPelAEVCQNLGVGSDLRRMFYALARLNGGLeALDRALSVLA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 289 RlsQNKQALEGLEDLKLLFEYLNLFGIAEKISFDLSLARGLDYYTGVIYeAVLLQTPTQAgeeplnvgsVAAGGRYDGLV 368
Cdd:PRK12421 237 L--QDAAIRQALDELKTLAAHLKNRWPELPVSIDLAELRGYHYHTGLVF-AAYIPGRGQA---------LARGGRYDGIG 304
|
330 340
....*....|....*....|..
gi 384943856 369 GMFdpkGHKVPCVGLSIGVERI 390
Cdd:PRK12421 305 EAF---GRARPATGFSMDLKEL 323
|
|
| ProRS_anticodon_short |
cd00861 |
ProRS Prolyl-anticodon binding domain, short version found predominantly in bacteria. ProRS ... |
460-500 |
2.22e-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: 40.27 E-value: 2.22e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 384943856 460 GIPLVVIIGEQELKEGIIKIRSVASREEVAIKRENLVAEIQ 500
Cdd:cd00861 54 GIPYRIVVGKKSAAEGIVEIKVRKTGEKEEISIDELLEFLQ 94
|
|
| PRK09194 |
PRK09194 |
prolyl-tRNA synthetase; Provisional |
460-504 |
1.91e-03 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 236405 [Multi-domain] Cd Length: 565 Bit Score: 40.84 E-value: 1.91e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 384943856 460 GIPLVVIIGEQELKEGIIKIRSVASREEVAIKRENLVAEIQKRLS 504
Cdd:PRK09194 521 GIPHRIVVGDRGLAEGIVEYKDRRTGEKEEVPVDELVEFLKALKK 565
|
|
| HGTP_anticodon |
cd00738 |
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ... |
427-500 |
4.20e-03 |
|
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and prolyl tRNA synthetases, which are classified as a group of class II aminoacyl-tRNA synthetases (aaRS). In aaRSs, the anticodon binding domain 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. This domain is also found in the accessory subunit of mitochondrial polymerase gamma (Pol gamma b).
Pssm-ID: 238379 [Multi-domain] Cd Length: 94 Bit Score: 36.61 E-value: 4.20e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 384943856 427 KLITELWDAGIKAEMLYKNNpKLLTQLHYCESTGIPLVVIIGEQELKEGIIKIRSVASREEVAIKRENLVAEIQ 500
Cdd:cd00738 22 KLLNALLANGIRVLYDDRER-KIGKKFREADLRGVPFAVVVGEDELENGKVTVKSRDTGESETLHVDELPEFLV 94
|
|
| ThrRS_anticodon |
cd00860 |
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases ... |
410-500 |
8.43e-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: 8.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384943856 410 TQVFVATPQKNFLQERLKLITELWDAGIKAEMLYKNNpKL-----LTQLHycestGIPLVVIIGEQELKEGIIKIRSVAS 484
Cdd:cd00860 2 VQVVVIPVTDEHLDYAKEVAKKLSDAGIRVEVDLRNE-KLgkkirEAQLQ-----KIPYILVVGDKEVETGTVSVRTRDG 75
|
90
....*....|....*.
gi 384943856 485 REEVAIKRENLVAEIQ 500
Cdd:cd00860 76 GDLGSMSLDEFIEKLK 91
|
|
| |
