|
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: 542.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 12 WASLLSQLLRPPCASCTGAVrcqSQVAEAVLTSQLKahqEKPnfiiKTPKGTRDLSPQHMVVREKILDLVISCFKRHGAK 91
Cdd:PLN02972 292 WATQLLLLFDPKCPGFDSLV---DKVKEIVESNEVR---RLP----KIPKGTRDFAKEQMAIREKAFSIITSVFKRHGAT 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 92 GMDTPAFELKETLTEKYGEDSGLMYDLKDQGGELLSLRYDLTVPFARYLAMNKVKKMKRYHVGKVWRRESPTivQGRYRE 171
Cdd:PLN02972 362 ALDTPVFELRETLMGKYGEDSKLIYDLADQGGELCSLRYDLTVPFARYVAMNGITSFKRYQIAKVYRRDNPS--KGRYRE 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 172 FCQCDFDIAGQFDPMIPDAECLKIMCEILSGLQLGDFLIKVNDRRIVDGMFAVCGVPESKFRAICSSIDKLDKMAWKDVR 251
Cdd:PLN02972 440 FYQCDFDIAGVYEPMGPDFEIIKVLTELLDELDIGTYEVKLNHRKLLDGMLEICGVPPEKFRTICSSIDKLDKQSFEQVK 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 252 HEMVVKKGLAPEVADRIGDYVQCHGG-VSLVEQMFQ-DPRLSQNKQALEGLGDLKLLFEYLTLFGIADKISFDLSLARGL 329
Cdd:PLN02972 520 KEMVEEKGLSNETADKIGNFVKERGPpLELLSKLRQeGSEFLGNASSRAALDELEIMFKALEKSKAIGKIVFDLSLARGL 599
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 330 DYYTGVIYEAVLLQTptqageeplNVGSVAAGGRYDGLVGMFDPKghKVPCVGLSIGVERIFYIVEQRMKTKGEKVRTTE 409
Cdd:PLN02972 600 DYYTGVIYEAVFKGA---------QVGSIAAGGRYDNLVGMFSGK--QVPAVGVSLGIERVFAIMEQQEEEKSQVIRPTE 668
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 410 TQVFVATPQKNFLQERLKLIAELWDSGIKAEmlYKNNPKLLTQLHYCESTGIPLVVIIGEQELKEGVIKIRSVASREEVA 489
Cdd:PLN02972 669 TEVLVSIIGDDKLALAAELVSELWNAGIKAE--YKVSTRKAKHLKRAKESGIPWMVLVGEKELSKGFVKLKNLEAGVEEE 746
|
490
....*....|....*
gi 15029520 490 IKRENFVAEIQKRLS 504
Cdd:PLN02972 747 VDRTCFVQELKAELL 761
|
|
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
57-505 |
5.47e-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: 345.95 E-value: 5.47e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 57 IKTPKGTRDLSPQHMVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSG--LMYDLKDQGGELLSLRYDLTV 134
Cdd:COG0124 4 IQAPRGTRDILPEESAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKIGEDIVekEMYTFEDRGGRSLTLRPEGTA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 135 PFARYLAMNK---VKKMKRYHVGKVWRRESPtivQ-GRYREFCQCDFDIAGQFDPMIpDAECLKIMCEILSGLQLGDFLI 210
Cdd:COG0124 84 PVARAVAEHGnelPFPFKLYYIGPVFRYERP---QkGRYRQFHQFGVEVIGSDSPLA-DAEVIALAADLLKALGLKDFTL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 211 KVNDRrivdgmfavcGVPESKFRAICSSIDKLDKMAWKDVrhemvvkkgLAPEVADRIG-----DYVQCHGGV--SLVEQ 283
Cdd:COG0124 160 EINSR----------GLPEERAEALLRYLDKLDKIGHEDV---------LDEDSQRRLEtnplrAILDSKGPDcqEVLAD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 284 MfqdPRLSQNKqALEGLGDLKLLFEYLTLFGIadKISFDLSLARGLDYYTGVIYEAVLLQTPTQageeplnvGSVAAGGR 363
Cdd:COG0124 221 A---PKLLDYL-GEEGLAHFEEVLELLDALGI--PYVIDPRLVRGLDYYTGTVFEIVTDGLGAQ--------GSVCGGGR 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 364 YDGLVGMFDpkGHKVPCVGLSIGVERIFYIVEQRmktKGEKVRTTETQVFVATPQKNFLQERLKLIAELWDSGIKAEMLY 443
Cdd:COG0124 287 YDGLVEQLG--GPPTPAVGFAIGLERLLLLLEEL---GLLPAAEPPPDVYVVPLGEEARAEALKLAQELRAAGIRVELDL 361
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15029520 444 KNNpKLLTQLHYCESTGIPLVVIIGEQELKEGVIKIRSVASREEVAIKRENFVAEIQKRLSE 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 |
1.02e-97 |
|
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. It is responsible for the attachment of histidine to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs. This domain is also found at the C-terminus of eukaryotic GCN2 protein kinase and at the N-terminus of the ATP phosphoribosyltransferase accessory subunit, HisZ. HisZ along with HisG catalyze the first reaction in histidine biosynthesis. HisZ is found only in a subset of bacteria and differs from HisRS in lacking a C-terminal anti-codon binding domain.
Pssm-ID: 238396 [Multi-domain] Cd Length: 261 Bit Score: 295.67 E-value: 1.02e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 71 MVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSG-LMYDLKDQGGELLSLRYDLTVPFARYLAMNKVKK-- 147
Cdd:cd00773 2 AALRRYIEDTLREVFERYGYEEIDTPVFEYTELFLRKSGDEVSkEMYRFKDKGGRDLALRPDLTAPVARAVAENLLSLpl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 148 -MKRYHVGKVWRRESPTivQGRYREFCQCDFDIAGqFDPMIPDAECLKIMCEILSGLQLGDFLIKVNDRRIVDGmfaVCG 226
Cdd:cd00773 82 pLKLYYIGPVFRYERPQ--KGRYREFYQVGVEIIG-SDSPLADAEVIALAVEILEALGLKDFQIKINHRGILDG---IAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 227 VPESKFRAICSSIDKLDKmawkdvrhemvvkkglapevadrigdyvqchggvslveqmfqdprlsqnkqalEGLGDLKLL 306
Cdd:cd00773 156 LLEDREEYIERLIDKLDK-----------------------------------------------------EALAHLEKL 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 307 FEYLTLFGIADKISFDLSLARGLDYYTGVIYEAVLLQTPTQageeplnvGSVAAGGRYDGLVGMFDpkGHKVPCVGLSIG 386
Cdd:cd00773 183 LDYLEALGVDIKYSIDLSLVRGLDYYTGIVFEAVADGLGAQ--------GSIAGGGRYDGLLEEFG--GEDVPAVGFAIG 252
|
....*....
gi 15029520 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 |
5.35e-95 |
|
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed genome. Apparent second copies from Bacillus subtilis, Synechocystis sp., and Aquifex aeolicus are slightly shorter, more closely related to each other than to other hisS proteins, and actually serve as regulatory subunits for an enzyme of histidine biosynthesis. They were excluded from the seed alignment and score much lower than do single copy histidyl-tRNA synthetases of other genomes not included in the seed alignment. These putative second copies of HisS score below the trusted cutoff. The regulatory protein kinase GCN2 of Saccharomyces cerevisiae (YDR283c), and related proteins from other species designated eIF-2 alpha kinase, have a domain closely related to histidyl-tRNA synthetase that may serve to detect and respond to uncharged tRNA(his), an indicator of amino acid starvation; these regulatory proteins are not orthologous and so score below the noise cutoff. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273080 [Multi-domain] Cd Length: 404 Bit Score: 294.00 E-value: 5.35e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 58 KTPKGTRDLSPQHMVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSGL----MYDLKDQGGELLSLRYDLT 133
Cdd:TIGR00442 1 QKPRGTRDFLPEEMIKWQYIEETIREVFERYGFKEIRTPIFEYTELFKRKVGEETDIvskeMYTFKDKGGRSLTLRPEGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 134 VPFARYLAMNK---VKKMKRYHVGKVWRRESPtivQ-GRYREFCQCDFDIAGQFDPMIpDAECLKIMCEILSGLQLGDFL 209
Cdd:TIGR00442 81 APVARAVIENKlllPKPFKLYYIGPMFRYERP---QkGRYRQFHQFGVEVIGSDSPLA-DAEIIALAADILKELGLKDFT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 210 IKVNDRRIVDGMFAvcgvpesKFRAICSSIDK-LDKMAWKDVRHEMVVKKGLAPEVADRIGDYVQchggvslveqmfQDP 288
Cdd:TIGR00442 157 LEINSLGILEGRLE-------YREALIRYLDKhKDKLGEDSVRRLEKNPLRILDSKNEKIQELLK------------NAP 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 289 RLSQNKQAlEGLGDLKLLFEYLTLFGIadKISFDLSLARGLDYYTGVIYEAVLLQTPTQageeplnvGSVAAGGRYDGLV 368
Cdd:TIGR00442 218 KILDFLCE-ESRAHFEELKELLDALGI--PYKIDPSLVRGLDYYTGTVFEFVTDDLGAQ--------GSICGGGRYDGLV 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 369 GMFDpkGHKVPCVGLSIGVERIFYIVEQRmktKGEKVRTTETQVFVATPQKNFLQERLKLIAELWDSGIKAEMLYKNNpK 448
Cdd:TIGR00442 287 EELG--GPPTPAVGFAIGIERLILLLEEL---GLIPPPSKKPDVYVVPLGEEAELEALKLAQKLRKAGIRVEVDLGGR-K 360
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 15029520 449 LLTQLHYCESTGIPLVVIIGEQELKEGVIKIRSVASREEVAIKR 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 |
1.18e-38 |
|
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP phosphoribosyltransferase regulatory subunits.
Pssm-ID: 433170 [Multi-domain] Cd Length: 309 Bit Score: 143.11 E-value: 1.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 62 GTRDLSPQHMVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSGLMYDLKDQGGELLSLRYDLTVPFARYLA 141
Cdd:pfam13393 1 GIRDLLPPEARRIEELRRRLLDLFRSWGYELVMPPLLEYLDSLLTGTGADLDQTFKLVDQSGRLLGLRADITPQVARIDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 142 --MNKVKKMKRYHVGKVWRRESPTIvqGRYREFCQCDFDIAGQFDPMiPDAECLKIMCEILSGLQLGDFLIKVNDRRIVD 219
Cdd:pfam13393 81 hrLNRPGPLRLCYAGSVLRTRPKGL--GRSREPLQVGAELIGHAGIE-ADAEIISLLLEALAAAGVPGVTLDLGHVGLVR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 220 GMFAVCGVPESKFRAICSSIDKLDkmaWKDVRhEMVVKKGLAPEVADRIGDYVQCHGGVSLVEQMFQdpRLSQNKQALEG 299
Cdd:pfam13393 158 ALLEAAGLSEALEEALRAALQRKD---AAELA-ELAAEAGLPPALRRALLALPDLYGGPEVLDEARA--ALPGLPALQEA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 300 LGDLKLLFEYLTLFGIADKISFDLSLARGLDYYTGVIYEAVLLQTPtqageeplnvGSVAAGGRYDGLVGMFdpkGHKVP 379
Cdd:pfam13393 232 LDELEALAALLEALGDGVRLTFDLAELRGYEYYTGIVFAAYAPGVG----------EPLARGGRYDDLGAAF---GRARP 298
|
330
....*....|.
gi 15029520 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: 542.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 12 WASLLSQLLRPPCASCTGAVrcqSQVAEAVLTSQLKahqEKPnfiiKTPKGTRDLSPQHMVVREKILDLVISCFKRHGAK 91
Cdd:PLN02972 292 WATQLLLLFDPKCPGFDSLV---DKVKEIVESNEVR---RLP----KIPKGTRDFAKEQMAIREKAFSIITSVFKRHGAT 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 92 GMDTPAFELKETLTEKYGEDSGLMYDLKDQGGELLSLRYDLTVPFARYLAMNKVKKMKRYHVGKVWRRESPTivQGRYRE 171
Cdd:PLN02972 362 ALDTPVFELRETLMGKYGEDSKLIYDLADQGGELCSLRYDLTVPFARYVAMNGITSFKRYQIAKVYRRDNPS--KGRYRE 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 172 FCQCDFDIAGQFDPMIPDAECLKIMCEILSGLQLGDFLIKVNDRRIVDGMFAVCGVPESKFRAICSSIDKLDKMAWKDVR 251
Cdd:PLN02972 440 FYQCDFDIAGVYEPMGPDFEIIKVLTELLDELDIGTYEVKLNHRKLLDGMLEICGVPPEKFRTICSSIDKLDKQSFEQVK 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 252 HEMVVKKGLAPEVADRIGDYVQCHGG-VSLVEQMFQ-DPRLSQNKQALEGLGDLKLLFEYLTLFGIADKISFDLSLARGL 329
Cdd:PLN02972 520 KEMVEEKGLSNETADKIGNFVKERGPpLELLSKLRQeGSEFLGNASSRAALDELEIMFKALEKSKAIGKIVFDLSLARGL 599
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 330 DYYTGVIYEAVLLQTptqageeplNVGSVAAGGRYDGLVGMFDPKghKVPCVGLSIGVERIFYIVEQRMKTKGEKVRTTE 409
Cdd:PLN02972 600 DYYTGVIYEAVFKGA---------QVGSIAAGGRYDNLVGMFSGK--QVPAVGVSLGIERVFAIMEQQEEEKSQVIRPTE 668
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 410 TQVFVATPQKNFLQERLKLIAELWDSGIKAEmlYKNNPKLLTQLHYCESTGIPLVVIIGEQELKEGVIKIRSVASREEVA 489
Cdd:PLN02972 669 TEVLVSIIGDDKLALAAELVSELWNAGIKAE--YKVSTRKAKHLKRAKESGIPWMVLVGEKELSKGFVKLKNLEAGVEEE 746
|
490
....*....|....*
gi 15029520 490 IKRENFVAEIQKRLS 504
Cdd:PLN02972 747 VDRTCFVQELKAELL 761
|
|
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
57-505 |
5.47e-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: 345.95 E-value: 5.47e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 57 IKTPKGTRDLSPQHMVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSG--LMYDLKDQGGELLSLRYDLTV 134
Cdd:COG0124 4 IQAPRGTRDILPEESAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKIGEDIVekEMYTFEDRGGRSLTLRPEGTA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 135 PFARYLAMNK---VKKMKRYHVGKVWRRESPtivQ-GRYREFCQCDFDIAGQFDPMIpDAECLKIMCEILSGLQLGDFLI 210
Cdd:COG0124 84 PVARAVAEHGnelPFPFKLYYIGPVFRYERP---QkGRYRQFHQFGVEVIGSDSPLA-DAEVIALAADLLKALGLKDFTL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 211 KVNDRrivdgmfavcGVPESKFRAICSSIDKLDKMAWKDVrhemvvkkgLAPEVADRIG-----DYVQCHGGV--SLVEQ 283
Cdd:COG0124 160 EINSR----------GLPEERAEALLRYLDKLDKIGHEDV---------LDEDSQRRLEtnplrAILDSKGPDcqEVLAD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 284 MfqdPRLSQNKqALEGLGDLKLLFEYLTLFGIadKISFDLSLARGLDYYTGVIYEAVLLQTPTQageeplnvGSVAAGGR 363
Cdd:COG0124 221 A---PKLLDYL-GEEGLAHFEEVLELLDALGI--PYVIDPRLVRGLDYYTGTVFEIVTDGLGAQ--------GSVCGGGR 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 364 YDGLVGMFDpkGHKVPCVGLSIGVERIFYIVEQRmktKGEKVRTTETQVFVATPQKNFLQERLKLIAELWDSGIKAEMLY 443
Cdd:COG0124 287 YDGLVEQLG--GPPTPAVGFAIGLERLLLLLEEL---GLLPAAEPPPDVYVVPLGEEARAEALKLAQELRAAGIRVELDL 361
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15029520 444 KNNpKLLTQLHYCESTGIPLVVIIGEQELKEGVIKIRSVASREEVAIKRENFVAEIQKRLSE 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 |
1.02e-97 |
|
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. It is responsible for the attachment of histidine to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs. This domain is also found at the C-terminus of eukaryotic GCN2 protein kinase and at the N-terminus of the ATP phosphoribosyltransferase accessory subunit, HisZ. HisZ along with HisG catalyze the first reaction in histidine biosynthesis. HisZ is found only in a subset of bacteria and differs from HisRS in lacking a C-terminal anti-codon binding domain.
Pssm-ID: 238396 [Multi-domain] Cd Length: 261 Bit Score: 295.67 E-value: 1.02e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 71 MVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSG-LMYDLKDQGGELLSLRYDLTVPFARYLAMNKVKK-- 147
Cdd:cd00773 2 AALRRYIEDTLREVFERYGYEEIDTPVFEYTELFLRKSGDEVSkEMYRFKDKGGRDLALRPDLTAPVARAVAENLLSLpl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 148 -MKRYHVGKVWRRESPTivQGRYREFCQCDFDIAGqFDPMIPDAECLKIMCEILSGLQLGDFLIKVNDRRIVDGmfaVCG 226
Cdd:cd00773 82 pLKLYYIGPVFRYERPQ--KGRYREFYQVGVEIIG-SDSPLADAEVIALAVEILEALGLKDFQIKINHRGILDG---IAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 227 VPESKFRAICSSIDKLDKmawkdvrhemvvkkglapevadrigdyvqchggvslveqmfqdprlsqnkqalEGLGDLKLL 306
Cdd:cd00773 156 LLEDREEYIERLIDKLDK-----------------------------------------------------EALAHLEKL 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 307 FEYLTLFGIADKISFDLSLARGLDYYTGVIYEAVLLQTPTQageeplnvGSVAAGGRYDGLVGMFDpkGHKVPCVGLSIG 386
Cdd:cd00773 183 LDYLEALGVDIKYSIDLSLVRGLDYYTGIVFEAVADGLGAQ--------GSIAGGGRYDGLLEEFG--GEDVPAVGFAIG 252
|
....*....
gi 15029520 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 |
5.35e-95 |
|
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed genome. Apparent second copies from Bacillus subtilis, Synechocystis sp., and Aquifex aeolicus are slightly shorter, more closely related to each other than to other hisS proteins, and actually serve as regulatory subunits for an enzyme of histidine biosynthesis. They were excluded from the seed alignment and score much lower than do single copy histidyl-tRNA synthetases of other genomes not included in the seed alignment. These putative second copies of HisS score below the trusted cutoff. The regulatory protein kinase GCN2 of Saccharomyces cerevisiae (YDR283c), and related proteins from other species designated eIF-2 alpha kinase, have a domain closely related to histidyl-tRNA synthetase that may serve to detect and respond to uncharged tRNA(his), an indicator of amino acid starvation; these regulatory proteins are not orthologous and so score below the noise cutoff. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273080 [Multi-domain] Cd Length: 404 Bit Score: 294.00 E-value: 5.35e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 58 KTPKGTRDLSPQHMVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSGL----MYDLKDQGGELLSLRYDLT 133
Cdd:TIGR00442 1 QKPRGTRDFLPEEMIKWQYIEETIREVFERYGFKEIRTPIFEYTELFKRKVGEETDIvskeMYTFKDKGGRSLTLRPEGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 134 VPFARYLAMNK---VKKMKRYHVGKVWRRESPtivQ-GRYREFCQCDFDIAGQFDPMIpDAECLKIMCEILSGLQLGDFL 209
Cdd:TIGR00442 81 APVARAVIENKlllPKPFKLYYIGPMFRYERP---QkGRYRQFHQFGVEVIGSDSPLA-DAEIIALAADILKELGLKDFT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 210 IKVNDRRIVDGMFAvcgvpesKFRAICSSIDK-LDKMAWKDVRHEMVVKKGLAPEVADRIGDYVQchggvslveqmfQDP 288
Cdd:TIGR00442 157 LEINSLGILEGRLE-------YREALIRYLDKhKDKLGEDSVRRLEKNPLRILDSKNEKIQELLK------------NAP 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 289 RLSQNKQAlEGLGDLKLLFEYLTLFGIadKISFDLSLARGLDYYTGVIYEAVLLQTPTQageeplnvGSVAAGGRYDGLV 368
Cdd:TIGR00442 218 KILDFLCE-ESRAHFEELKELLDALGI--PYKIDPSLVRGLDYYTGTVFEFVTDDLGAQ--------GSICGGGRYDGLV 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 369 GMFDpkGHKVPCVGLSIGVERIFYIVEQRmktKGEKVRTTETQVFVATPQKNFLQERLKLIAELWDSGIKAEMLYKNNpK 448
Cdd:TIGR00442 287 EELG--GPPTPAVGFAIGIERLILLLEEL---GLIPPPSKKPDVYVVPLGEEAELEALKLAQKLRKAGIRVEVDLGGR-K 360
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 15029520 449 LLTQLHYCESTGIPLVVIIGEQELKEGVIKIRSVASREEVAIKR 492
Cdd:TIGR00442 361 LKKQLKYADKLGARFALIIGEDELENGTVTLKDLETGEQETVPL 404
|
|
| PRK12420 |
PRK12420 |
histidyl-tRNA synthetase; Provisional |
58-491 |
5.56e-85 |
|
histidyl-tRNA synthetase; Provisional
Pssm-ID: 237097 [Multi-domain] Cd Length: 423 Bit Score: 268.52 E-value: 5.56e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 58 KTPKGTRDLSPQHMVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYG---EDSGLMYDLKDQGGELLSLRYDLTV 134
Cdd:PRK12420 5 RNVKGTKDYLPEEQVLRNKIKRALEDVFERYGCKPLETPTLNMYELMSSKYGggdEILKEIYTLTDQGKRDLALRYDLTI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 135 PFARYLAMNKVKKM--KRYHVGKVWrRESPtIVQGRYREFCQCDFDIAGQFDPMiPDAECLKIMCEILSGLQLgDFLIKV 212
Cdd:PRK12420 85 PFAKVVAMNPNIRLpfKRYEIGKVF-RDGP-IKQGRFREFIQCDVDIVGVESVM-AEAELMSMAFELFRRLNL-EVTIQY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 213 NDRRIVDGMFAVCGVPESKFRAICSSIDKLDKMAWKDVRHEmVVKKGLAPEVADRIGDYVQCHGGVSLVEqmFQDprLSQ 292
Cdd:PRK12420 161 NNRKLLNGILQAIGIPTELTSDVILSLDKIEKIGIDGVRKD-LLERGISEEMADTICNTVLSCLQLSIAD--FKE--AFN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 293 NKQALEGLGDLKLLFEYLTLFGIADKISFDLSLARGLDYYTGVIYEAVLlqtptqagEEPLNVGSVAAGGRYDGLVGMFD 372
Cdd:PRK12420 236 NPLVAEGVNELQQLQQYLIALGINENCIFNPFLARGLTMYTGTVYEIFL--------KDGSITSSIGSGGRYDNIIGAFR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 373 PKGHKVPCVGLSIGVERIFYIVEQRmktkgekVRTTETQVFVATPQKNFLQErLKLIAELW-DSGIKAEMLYKNNpKLLT 451
Cdd:PRK12420 308 GDDMNYPTVGISFGLDVIYTALSQK-------ETISSTADVFIIPLGTELQC-LQIAQQLRsTTGLKVELELAGR-KLKK 378
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 15029520 452 QLHYCESTGIPLVVIIGEQELKEGVIKIRSVASREEVAIK 491
Cdd:PRK12420 379 ALNYANKENIPYVLIIGEEEVSTGTVMLRNMKEGSEVKVP 418
|
|
| PLN02530 |
PLN02530 |
histidine-tRNA ligase |
2-491 |
3.11e-51 |
|
histidine-tRNA ligase
Pssm-ID: 178145 [Multi-domain] Cd Length: 487 Bit Score: 181.48 E-value: 3.11e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 2 PLLGLLPRRAWASLLSQLLRPPCASCTGAVRCQSQVAEAVLTSQLKAhqeKPNFIIKTPKGTRDLSPQHMVVREKILDLV 81
Cdd:PLN02530 18 PSLPLSSRCSFLLSASSPRGGRCAASAAAGGGRSGGTTAPPSVQEDG---KPKIDVNPPKGTRDFPPEDMRLRNWLFDHF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 82 ISCFKRHGAKGMDTPAFELKETLTEKYGED-SGLMYDLKDQGGELLSLRYDLTVPFARyLAMNKVKKM----KRYHVGKV 156
Cdd:PLN02530 95 REVSRLFGFEEVDAPVLESEELYIRKAGEEiTDQLYNFEDKGGRRVALRPELTPSLAR-LVLQKGKSLslplKWFAIGQC 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 157 WRRESPTivQGRYREFCQCDFDIAGqFDPMIPDAECLKIMCEILS--GLQLGDFLIKVNDRRIVDGMFAVCGVPESKFRA 234
Cdd:PLN02530 174 WRYERMT--RGRRREHYQWNMDIIG-VPGVEAEAELLAAIVTFFKrvGITSSDVGIKVSSRKVLQAVLKSYGIPEESFAP 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 235 ICSSIDKLDKMAWKDVRHEMVvKKGLAPEVADRIGDYVQCHGGVSLVEQMFQDPrlsqnkqalEGLGDLKLLFEYLTLFG 314
Cdd:PLN02530 251 VCVIVDKLEKLPREEIEKELD-TLGVSEEAIEGILDVLSLKSLDDLEALLGADS---------EAVADLKQLFSLAEAYG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 315 IADKISFDLSLARGLDYYTGVIYEAVllqtpTQAGEeplnVGSVAAGGRYDGLVGMFDpkGHKVPCVGLSIG--Verify 392
Cdd:PLN02530 321 YQDWLVFDASVVRGLAYYTGIVFEGF-----DRAGK----LRAICGGGRYDRLLSTFG--GEDTPACGFGFGdaV----- 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 393 IVEqRMKTKG---EKVRTTETQVFvatPQKNFLQ-ERLKLIAELWDSGIKAEMLYKNNpKLLTQLHYCESTGIPLVVIIG 468
Cdd:PLN02530 385 IVE-LLKEKGllpELPHQVDDVVF---ALDEDLQgAAAGVASRLREKGRSVDLVLEPK-KLKWVFKHAERIGAKRLVLVG 459
|
490 500
....*....|....*....|...
gi 15029520 469 EQELKEGVIKIRSVASREEVAIK 491
Cdd:PLN02530 460 ASEWERGMVRVKDLSSGEQTEVK 482
|
|
| hisZ_biosyn_reg |
TIGR00443 |
ATP phosphoribosyltransferase, regulatory subunit; Apparant second copies of histidyl-tRNA ... |
64-390 |
2.02e-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: 172.03 E-value: 2.02e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 64 RDLSPQHMVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSGLMYDLKDQGGELLSLRYDLTVPFARYLAmn 143
Cdd:TIGR00443 1 RDLLPEEAARKEEIERQLQDVFRSWGYQEIITPTLEYLDTLSAGSGILNEDLFKLFDQLGRVLGLRPDMTAPIARLVS-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 144 kvKKMKRYH-------VGKVWRRESPTIvqGRYREFCQCDFDIAGQfDPMIPDAECLKIMCEILSGLQLGDFLIKVNDRR 216
Cdd:TIGR00443 79 --TRLRDRPlplrlcyAGNVFRTNESGG--GRSREFTQAGVELIGA-GGPAADAEVIALLIEALKALGLKDFKIELGHVG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 217 IVDGMFAVCGVPESKFRAICSSIDKLDKMAWKdvrhEMVVKKGLAPEVADRIGDYVQCHGGVSLVEQMFQdpRLSQNKQA 296
Cdd:TIGR00443 154 LVRALLEEAGLPEEAREALREALARKDLVALE----ELVAELGLSPEVRERLLALPRLRGDGEEVLEEAR--ALAGSETA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 297 LEGLGDLKLLFEYLTLFGIADKISFDLSLARGLDYYTGVIYEAVLlqtpTQAGEeplnvgSVAAGGRYDGLVGMFdpkGH 376
Cdd:TIGR00443 228 EAALDELEAVLELLEARGVEEYISLDLGLVRGYHYYTGLIFEGYA----PGLGA------PLAGGGRYDELLGRF---GR 294
|
330
....*....|....
gi 15029520 377 KVPCVGLSIGVERI 390
Cdd:TIGR00443 295 PLPATGFALNLERL 308
|
|
| HisZ |
COG3705 |
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism]; |
74-390 |
2.10e-44 |
|
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism];
Pssm-ID: 442919 [Multi-domain] Cd Length: 312 Bit Score: 158.80 E-value: 2.10e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 74 REKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSGL-MYDLKDQGGELLSLRYDLTVPFARYLA--MNKVKKMKR 150
Cdd:COG3705 8 KEELRRRLLDVFRSWGYELVEPPLLEYLDSLLTGSGADLDLqTFKLVDQLGRTLGLRPDMTPQVARIAAtrLANRPGPLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 151 Y-HVGKVWR-RESPtivQGRYREFCQC------DFDIAGqfdpmipDAECLKIMCEILSGLQLGDFLIKVNDRRIVDGMF 222
Cdd:COG3705 88 LcYAGNVFRtRPSG---LGRSREFLQAgaeligHAGLEA-------DAEVIALALEALKAAGLEDFTLDLGHVGLFRALL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 223 AVCGVPESKFRAICSSIDKLDkmaWKDVRhEMVVKKGLAPEVADRIGDYVQCHGGVSLVEQMFQdprLSQNKQALEGLGD 302
Cdd:COG3705 158 EALGLSEEQREELRRALARKD---AVELE-ELLAELGLSEELAEALLALPELYGGEEVLARARA---LLLDAAIRAALDE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 303 LKLLFEYLTLFGIADKISFDLSLARGLDYYTGVIYEAVllqTPTQAGEeplnvgsVAAGGRYDGLVGMFdpkGHKVPCVG 382
Cdd:COG3705 231 LEALAEALAARGPDVRLTFDLSELRGYDYYTGIVFEAY---APGVGDP-------LARGGRYDGLLAAF---GRARPATG 297
|
....*...
gi 15029520 383 LSIGVERI 390
Cdd:COG3705 298 FSLDLDRL 305
|
|
| hisZ |
PRK12292 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
60-441 |
3.04e-43 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 237043 [Multi-domain] Cd Length: 391 Bit Score: 157.72 E-value: 3.04e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 60 PKGTRDLSPQHMVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSGL-MYDLKDQG-GELLSLRYDLTVPFA 137
Cdd:PRK12292 6 PEGIRDLLPEEARKIEEIRRRLLDLFRRWGYEEVITPTLEYLDTLLAGGGAILDLrTFKLVDQLsGRTLGLRPDMTAQIA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 138 RyLAMNKVKKMKR-----YHvGKVWR---RESptivqGRYREFCQCDFDIAGqFDPMIPDAECLKIMCEILSGLQLGDFL 209
Cdd:PRK12292 86 R-IAATRLANRPGplrlcYA-GNVFRaqeRGL-----GRSREFLQSGVELIG-DAGLEADAEVILLLLEALKALGLPNFT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 210 IKVNDRRIVDGMFAVCGVPESKFRAICSSIDKLDKMAWKdvrhEMVvkKGLAPEVADRIGDYVQCHGGVSLVEQMfqdPR 289
Cdd:PRK12292 158 LDLGHVGLFRALLEAAGLSEELEEVLRRALANKDYVALE----ELV--LDLSEELRDALLALPRLRGGREVLEEA---RK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 290 LSQNKQALEGLGDLKLLFEYLTLFGIADKISFDLSLARGLDYYTGVIYEAVllqtptqAGEEPLNVGSvaaGGRYDGLVG 369
Cdd:PRK12292 229 LLPSLPIKRALDELEALAEALEKYGYGIPLSLDLGLLRHLDYYTGIVFEGY-------VDGVGNPIAS---GGRYDDLLG 298
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15029520 370 MFdpkGHKVPCVGLSIGVERifyIVEQRMKTKgekvrTTETQVFVATPQKNFLQERLKLIAELWDSGIKAEM 441
Cdd:PRK12292 299 RF---GRARPATGFSLDLDR---LLELQLELP-----VEARKDLVIAPDSEALAAALAAAQELRKKGEIVVL 359
|
|
| tRNA-synt_His |
pfam13393 |
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ... |
62-390 |
1.18e-38 |
|
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP phosphoribosyltransferase regulatory subunits.
Pssm-ID: 433170 [Multi-domain] Cd Length: 309 Bit Score: 143.11 E-value: 1.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 62 GTRDLSPQHMVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSGLMYDLKDQGGELLSLRYDLTVPFARYLA 141
Cdd:pfam13393 1 GIRDLLPPEARRIEELRRRLLDLFRSWGYELVMPPLLEYLDSLLTGTGADLDQTFKLVDQSGRLLGLRADITPQVARIDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 142 --MNKVKKMKRYHVGKVWRRESPTIvqGRYREFCQCDFDIAGQFDPMiPDAECLKIMCEILSGLQLGDFLIKVNDRRIVD 219
Cdd:pfam13393 81 hrLNRPGPLRLCYAGSVLRTRPKGL--GRSREPLQVGAELIGHAGIE-ADAEIISLLLEALAAAGVPGVTLDLGHVGLVR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 220 GMFAVCGVPESKFRAICSSIDKLDkmaWKDVRhEMVVKKGLAPEVADRIGDYVQCHGGVSLVEQMFQdpRLSQNKQALEG 299
Cdd:pfam13393 158 ALLEAAGLSEALEEALRAALQRKD---AAELA-ELAAEAGLPPALRRALLALPDLYGGPEVLDEARA--ALPGLPALQEA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 300 LGDLKLLFEYLTLFGIADKISFDLSLARGLDYYTGVIYEAVLLQTPtqageeplnvGSVAAGGRYDGLVGMFdpkGHKVP 379
Cdd:pfam13393 232 LDELEALAALLEALGDGVRLTFDLAELRGYEYYTGIVFAAYAPGVG----------EPLARGGRYDDLGAAF---GRARP 298
|
330
....*....|.
gi 15029520 380 CVGLSIGVERI 390
Cdd:pfam13393 299 ATGFSLDLEAL 309
|
|
| syh |
CHL00201 |
histidine-tRNA synthetase; Provisional |
57-501 |
1.27e-28 |
|
histidine-tRNA synthetase; Provisional
Pssm-ID: 164576 [Multi-domain] Cd Length: 430 Bit Score: 117.69 E-value: 1.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 57 IKTPKGTRDLSPQHMVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSGL----MYDLKDQGGELLSLRYDL 132
Cdd:CHL00201 4 IQAIRGTKDILPDEINYWQFIHDKALTLLSLANYSEIRTPIFENSSLYDRGIGETTDIvnkeMYRFTDRSNRDITLRPEG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 133 TVPFARYLAMNKVKKMKR----YHVGKVWRRESPTivQGRYREFCQCDFDIAGQFDPMiPDAECLKIMCEILSGLQLGDF 208
Cdd:CHL00201 84 TAGIVRAFIENKMDYHSNlqrlWYSGPMFRYERPQ--SGRQRQFHQLGIEFIGSIDAR-ADTEVIHLAMQIFNELQVKNL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 209 LIKVN------DRRIVdgmfavcgvpESKFRAICSSI-DKLDKmawkDVRHEMVVKkglaP-EVADRIGDYVQchggvsl 280
Cdd:CHL00201 161 ILDINsigkleDRQSY----------QLKLVEYLSQYqDDLDT----DSQNRLYSN----PiRILDSKNLKTQ------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 281 vEQMFQDPRLSQ--NKQALEGLGDLkllFEYLTLFGIADKISFdlSLARGLDYYTGVIYEavlLQTPTQAGEEplnvgSV 358
Cdd:CHL00201 216 -EILDGAPKISDflSLESTEHFYDV---CTYLNLLNIPYKINY--KLVRGLDYYNDTAFE---IKTLSSNGQD-----TI 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 359 AAGGRYDGLVGMFDpkGHKVPCVGLSIGVERIFYIVEQRMKTKGEKVrttetQVFVATPQKNFLQERLKLIAELWDSGIK 438
Cdd:CHL00201 282 CGGGRYDSLIHQLG--GPKTPAVGCAIGLERLLLIAKDNIILPKQSI-----DVYIATQGLKAQKKGWEIIQFLEKQNIK 354
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15029520 439 AEmLYKNNPKLLTQLHYCESTGIPLVVIIGEQELKEGVIKIRSVASREEVAIKRENFVAEIQK 501
Cdd:CHL00201 355 FE-LDLSSSNFHKQIKQAGKKRAKACIILGDNEIMDNCITIKWLDEQVQENAQYSNFKQEISY 416
|
|
| HisRS_anticodon |
cd00859 |
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases ... |
409-500 |
4.04e-28 |
|
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only.
Pssm-ID: 238436 [Multi-domain] Cd Length: 91 Bit Score: 107.24 E-value: 4.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 409 ETQVFVATPQKNFLQERLKLIAELWDSGIKAEMLYKNnPKLLTQLHYCESTGIPLVVIIGEQELKEGVIKIRSVASREEV 488
Cdd:cd00859 1 EVDVYVVPLGEGALSEALELAEQLRDAGIKAEIDYGG-RKLKKQFKYADRSGARFAVILGEDELAAGVVTVKDLETGEQE 79
|
90
....*....|..
gi 15029520 489 AIKRENFVAEIQ 500
Cdd:cd00859 80 TVALDELVEELK 91
|
|
| hisZ |
PRK12295 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
77-390 |
1.13e-20 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 183413 [Multi-domain] Cd Length: 373 Bit Score: 93.46 E-value: 1.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 77 ILDLVISCFKRHGAKGMDTPAFELKETLTEKYGED-SGLMYDLKDQGGELLSLRYDLTVPFAR-YLAMNKVKKMKRYHVG 154
Cdd:PRK12295 10 AAEALLASFEAAGAVRVDPPILQPAEPFLDLSGEDiRRRIFVTSDENGEELCLRPDFTIPVCRrHIATAGGEPARYAYLG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 155 KVWRRESptivqGRYREFCQCDFDIAGQFDPMIPDAECLKIMCEILSGLQLGDFLIKVNDRRIVDGMFAVCGVPE----- 229
Cdd:PRK12295 90 EVFRQRR-----DRASEFLQAGIESFGRADPAAADAEVLALALEALAALGPGDLEVRLGDVGLFAALVDALGLPPgwkrr 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 230 --------SKFRAIcssIDKL-------------------DKMAWKDVRHEMVVKKGLAP-------EVADRIGDYVQCH 275
Cdd:PRK12295 165 llrhfgrpRSLDAL---LARLagprvdpldehagvlaalaDEAAARALVEDLMSIAGISPvggrspaEIARRLLEKAALA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 276 GGVSLVEQMFQ--------DPRLSQNKQALEGL-GDLKL-------LFE----YLTLFGIA-DKISFDLSLARGLDYYTG 334
Cdd:PRK12295 242 AAARLPAEALAvlerflaiSGPPDAALAALRALaADAGLdldaaldRFEarlaALAARGIDlERLRFSASFGRPLDYYTG 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 15029520 335 VIYEAvllqTPTQAGEEPLnvgsvAAGGRYDGLVGMFDpKGHKVPCVGLSIGVERI 390
Cdd:PRK12295 322 FVFEI----RAAGNGDPPL-----AGGGRYDGLLTRLG-AGEPIPAVGFSIWLDRL 367
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
411-502 |
8.06e-18 |
|
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA synthetases it is probably the anticodon binding domain.
Pssm-ID: 460819 [Multi-domain] Cd Length: 94 Bit Score: 78.40 E-value: 8.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 411 QVFVATPQKN---FLQERLKLIAELWDSGIKAEmLYKNNPKLLTQLHYCESTGIPLVVIIGEQELKEGVIKIRSVASREE 487
Cdd:pfam03129 1 QVVVIPLGEKaeeLEEYAQKLAEELRAAGIRVE-LDDRNESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQ 79
|
90
....*....|....*
gi 15029520 488 VAIKRENFVAEIQKR 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 |
6.15e-07 |
|
Anticodon binding domain of tRNAs; This is an HGTP_anticodon binding domain, found largely on Gcn2 proteins which bind tRNA to down regulate translation in certain stress situations.
Pssm-ID: 432758 Cd Length: 259 Bit Score: 50.68 E-value: 6.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 412 VFVATPQKNFL-QERLKLIAELWDSGIKAEMLYKNNPKLLTQLHYCESTGIPLVVIIGEQEL----KEGVIKIRSVASRE 486
Cdd:pfam12745 8 VLVASFDASILrTTGVEILQELWAHGISADLAVDASYSPEDLVSRARDDGVSWIVIIKQQNKssdsKYKPLKVKNLLRKE 87
|
90 100
....*....|....*....|
gi 15029520 487 EVAIKRENFVA----EIQKR 502
Cdd:pfam12745 88 DVDLDSDELVSwlrgEIRER 107
|
|
| PRK12421 |
PRK12421 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
60-390 |
2.11e-05 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 237098 Cd Length: 392 Bit Score: 46.89 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 60 PKGTRDLSP---QHM-VVREKILDLVIScfkrHGAKGMDTPAFELKETLTEKYGEDSGLM-YDLKDQ-GGELLSLRYDLT 133
Cdd:PRK12421 10 PDGVADVLPeeaQKIeRLRRRLLDLFAS----RGYQLVMPPLIEYLESLLTGAGQDLKLQtFKLIDQlSGRLMGVRADIT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 134 VPFARYLA-MNKVKKMKRY-HVGKVWRrespTIVQG--RYREFCQCDFDIAGQfDPMIPDAECLKIMCEILSGLQLGDFL 209
Cdd:PRK12421 86 PQVARIDAhLLNREGVARLcYAGSVLH----TLPQGlfGSRTPLQLGAELYGH-AGIEADLEIIRLMLGLLRNAGVPALH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 210 IKVNDRRIVDGMFAVCGVPESKFRAIcssidkLDKMAWKDVR--HEMVVKKGLAPEVADRIGDYVQCHGGV-SLVEQMFQ 286
Cdd:PRK12421 161 LDLGHVGIFRRLAELAGLSPEEEEEL------FDLLQRKALPelAEVCQNLGVGSDLRRMFYALARLNGGLeALDRALSV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 287 DPRlsQNKQALEGLGDLKLLFEYLTLFGIADKISFDLSLARGLDYYTGVIYeAVLLQTPTQAgeeplnvgsVAAGGRYDG 366
Cdd:PRK12421 235 LAL--QDAAIRQALDELKTLAAHLKNRWPELPVSIDLAELRGYHYHTGLVF-AAYIPGRGQA---------LARGGRYDG 302
|
330 340
....*....|....*....|....
gi 15029520 367 LVGMFdpkGHKVPCVGLSIGVERI 390
Cdd:PRK12421 303 IGEAF---GRARPATGFSMDLKEL 323
|
|
| ProRS_anticodon_short |
cd00861 |
ProRS Prolyl-anticodon binding domain, short version found predominantly in bacteria. ProRS ... |
460-500 |
4.44e-04 |
|
ProRS Prolyl-anticodon binding domain, short version found predominantly in bacteria. ProRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only.
Pssm-ID: 238438 [Multi-domain] Cd Length: 94 Bit Score: 39.50 E-value: 4.44e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 15029520 460 GIPLVVIIGEQELKEGVIKIRSVASREEVAIKRENFVAEIQ 500
Cdd:cd00861 54 GIPYRIVVGKKSAAEGIVEIKVRKTGEKEEISIDELLEFLQ 94
|
|
| PRK09194 |
PRK09194 |
prolyl-tRNA synthetase; Provisional |
460-504 |
4.90e-03 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 236405 [Multi-domain] Cd Length: 565 Bit Score: 39.30 E-value: 4.90e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 15029520 460 GIPLVVIIGEQELKEGVIKIRSVASREEVAIKRENFVAEIQKRLS 504
Cdd:PRK09194 521 GIPHRIVVGDRGLAEGIVEYKDRRTGEKEEVPVDELVEFLKALKK 565
|
|
| ThrRS_anticodon |
cd00860 |
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases ... |
410-500 |
8.94e-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: 8.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15029520 410 TQVFVATPQKNFLQERLKLIAELWDSGIKAEMLYKNNpKL-----LTQLHycestGIPLVVIIGEQELKEGVIKIRSVAS 484
Cdd:cd00860 2 VQVVVIPVTDEHLDYAKEVAKKLSDAGIRVEVDLRNE-KLgkkirEAQLQ-----KIPYILVVGDKEVETGTVSVRTRDG 75
|
90
....*....|....*.
gi 15029520 485 REEVAIKRENFVAEIQ 500
Cdd:cd00860 76 GDLGSMSLDEFIEKLK 91
|
|
| |
