|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02972 |
PLN02972 |
Histidyl-tRNA synthetase |
1-432 |
0e+00 |
|
Histidyl-tRNA synthetase
Pssm-ID: 215525 [Multi-domain] Cd Length: 763 Bit Score: 565.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 1 MAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGEDSKLIYDLKDQGGELLSLRYDLTVPFARYLAMNKLTNIKR 80
Cdd:PLN02972 341 MAIREKAFSIITSVFKRHGATALDTPVFELRETLMGKYGEDSKLIYDLADQGGELCSLRYDLTVPFARYVAMNGITSFKR 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 81 YHIAKVYRRDNPamTRGRYREFYQCDFDIAGNFDPMIPDAECLKIMCEILSSLQIGDFLVKVNDRRILDGMFAICGVSDS 160
Cdd:PLN02972 421 YQIAKVYRRDNP--SKGRYREFYQCDFDIAGVYEPMGPDFEIIKVLTELLDELDIGTYEVKLNHRKLLDGMLEICGVPPE 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 161 KFRTICSSVDKLDKVSWEEVKNEMVGEKGLAPEVADRIGDYVQQHGG-VSLVEQLLQ-DPKLSQNKQALEGLGDLKLLFE 238
Cdd:PLN02972 499 KFRTICSSIDKLDKQSFEQVKKEMVEEKGLSNETADKIGNFVKERGPpLELLSKLRQeGSEFLGNASSRAALDELEIMFK 578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 239 YLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLLQTPaqageeplgVGSVAAGGRYDGLVGMFDpkGRKVPCVGLSIGVE 318
Cdd:PLN02972 579 ALEKSKAIGKIVFDLSLARGLDYYTGVIYEAVFKGAQ---------VGSIAAGGRYDNLVGMFS--GKQVPAVGVSLGIE 647
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 319 RIFSIVEQRLEALEEKIRTTETQVLVASAQKKLLEERLKLVSELWDAGIKAEllYKKNPKLLNQLQYCEEAGIPLVAIIG 398
Cdd:PLN02972 648 RVFAIMEQQEEEKSQVIRPTETEVLVSIIGDDKLALAAELVSELWNAGIKAE--YKVSTRKAKHLKRAKESGIPWMVLVG 725
|
410 420 430
....*....|....*....|....*....|....
gi 119582425 399 EQELKDGVIKLRSVTSREEVDVRREDLVEEIKRR 432
Cdd:PLN02972 726 EKELSKGFVKLKNLEAGVEEEVDRTCFVQELKAE 759
|
|
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
1-432 |
2.99e-111 |
|
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: 333.63 E-value: 2.99e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 1 MAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGED--SKLIYDLKDQGGELLSLRYDLTVPFARYLAMNKLTN- 77
Cdd:COG0124 18 SAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKIGEDivEKEMYTFEDRGGRSLTLRPEGTAPVARAVAEHGNELp 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 78 --IKRYHIAKVYRRDNPAmtRGRYREFYQCDFDIAGNFDPMIpDAECLKIMCEILSSLQIGDFLVKVNDRrildgmfaic 155
Cdd:COG0124 98 fpFKLYYIGPVFRYERPQ--KGRYRQFHQFGVEVIGSDSPLA-DAEVIALAADLLKALGLKDFTLEINSR---------- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 156 GVSDSKFRTICSSVDKLDKVSWEEVknemvgekgLAPEVADRI------------GDYVQqhggvSLVEQLlqdPKLSQN 223
Cdd:COG0124 165 GLPEERAEALLRYLDKLDKIGHEDV---------LDEDSQRRLetnplraildskGPDCQ-----EVLADA---PKLLDY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 224 KqALEGLGDLKLLFEYLTLFGIDdkISFDLSLARGLDYYTGVIYEAVLLQTPAQageeplgvGSVAAGGRYDGLVGMFDp 303
Cdd:COG0124 228 L-GEEGLAHFEEVLELLDALGIP--YVIDPRLVRGLDYYTGTVFEIVTDGLGAQ--------GSVCGGGRYDGLVEQLG- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 304 kGRKVPCVGLSIGVERIFSIVEQRLEALEEKirtTETQVLVASAQKKLLEERLKLVSELWDAGIKAEL-LYKKNPKllNQ 382
Cdd:COG0124 296 -GPPTPAVGFAIGLERLLLLLEELGLLPAAE---PPPDVYVVPLGEEARAEALKLAQELRAAGIRVELdLGGRKLK--KQ 369
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 119582425 383 LQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVDVRREDLVEEIKRR 432
Cdd:COG0124 370 LKYADKSGAPFVLILGEDELANGTVTLKDLATGEQETVPLDELVEYLKEL 419
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
1-325 |
2.40e-104 |
|
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: 310.30 E-value: 2.40e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 1 MAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGED-SKLIYDLKDQGGELLSLRYDLTVPFARYLAMNKL---T 76
Cdd:cd00773 2 AALRRYIEDTLREVFERYGYEEIDTPVFEYTELFLRKSGDEvSKEMYRFKDKGGRDLALRPDLTAPVARAVAENLLslpL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 77 NIKRYHIAKVYRRDNPAmtRGRYREFYQCDFDIAGnFDPMIPDAECLKIMCEILSSLQIGDFLVKVNDRRILDGmfaICG 156
Cdd:cd00773 82 PLKLYYIGPVFRYERPQ--KGRYREFYQVGVEIIG-SDSPLADAEVIALAVEILEALGLKDFQIKINHRGILDG---IAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 157 VSDSKFRTICSSVDKLDKvsweevknemvgekglapevadrigdyvqqhggvslveqllqdpklsqnkqalEGLGDLKLL 236
Cdd:cd00773 156 LLEDREEYIERLIDKLDK-----------------------------------------------------EALAHLEKL 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 237 FEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLLQTPAQageeplgvGSVAAGGRYDGLVGMFDpkGRKVPCVGLSIG 316
Cdd:cd00773 183 LDYLEALGVDIKYSIDLSLVRGLDYYTGIVFEAVADGLGAQ--------GSIAGGGRYDGLLEEFG--GEDVPAVGFAIG 252
|
....*....
gi 119582425 317 VERIFSIVE 325
Cdd:cd00773 253 LERLLLALE 261
|
|
| hisS |
TIGR00442 |
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ... |
1-420 |
3.53e-97 |
|
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: 297.08 E-value: 3.53e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 1 MAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGEDS----KLIYDLKDQGGELLSLRYDLTVPFARYLAMNKLT 76
Cdd:TIGR00442 14 MIKWQYIEETIREVFERYGFKEIRTPIFEYTELFKRKVGEETdivsKEMYTFKDKGGRSLTLRPEGTAPVARAVIENKLL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 77 N---IKRYHIAKVYRRDNPAmtRGRYREFYQCDFDIAGNFDPMIpDAECLKIMCEILSSLQIGDFLVKVNDRRILDGMFA 153
Cdd:TIGR00442 94 LpkpFKLYYIGPMFRYERPQ--KGRYRQFHQFGVEVIGSDSPLA-DAEIIALAADILKELGLKDFTLEINSLGILEGRLE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 154 icgvsdsKFRTICSSVDK-LDKVSWEEVKNEMVGEKGLAPEVADRIGDYVQQhggvslveqllqDPKLSQNKQAlEGLGD 232
Cdd:TIGR00442 171 -------YREALIRYLDKhKDKLGEDSVRRLEKNPLRILDSKNEKIQELLKN------------APKILDFLCE-ESRAH 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 233 LKLLFEYLTLFGIddKISFDLSLARGLDYYTGVIYEAVLLQTPAQageeplgvGSVAAGGRYDGLVGMFDpkGRKVPCVG 312
Cdd:TIGR00442 231 FEELKELLDALGI--PYKIDPSLVRGLDYYTGTVFEFVTDDLGAQ--------GSICGGGRYDGLVEELG--GPPTPAVG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 313 LSIGVERIFSIVEQRLEALEEKirtTETQVLVASAQKKLLEERLKLVSELWDAGIKAElLYKKNPKLLNQLQYCEEAGIP 392
Cdd:TIGR00442 299 FAIGIERLILLLEELGLIPPPS---KKPDVYVVPLGEEAELEALKLAQKLRKAGIRVE-VDLGGRKLKKQLKYADKLGAR 374
|
410 420
....*....|....*....|....*...
gi 119582425 393 LVAIIGEQELKDGVIKLRSVTSREEVDV 420
Cdd:TIGR00442 375 FALIIGEDELENGTVTLKDLETGEQETV 402
|
|
| tRNA-synt_His |
pfam13393 |
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ... |
2-320 |
3.39e-42 |
|
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: 151.20 E-value: 3.39e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 2 AVREKVFDViircFKRHGAEVIDTPVFELKETLMGKYGEDSKLIYDLKDQGGELLSLRYDLTVPFARYLAmnKLTNIKR- 80
Cdd:pfam13393 15 ELRRRLLDL----FRSWGYELVMPPLLEYLDSLLTGTGADLDQTFKLVDQSGRLLGLRADITPQVARIDA--HRLNRPGp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 81 ---YHIAKVYRRDNPAMtrGRYREFYQCDFDIAGNFDPMiPDAECLKIMCEILSSLQIGDFLVKVNDRRILDGMFAICGV 157
Cdd:pfam13393 89 lrlCYAGSVLRTRPKGL--GRSREPLQVGAELIGHAGIE-ADAEIISLLLEALAAAGVPGVTLDLGHVGLVRALLEAAGL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 158 SDSKFRTICSSVDKLDkvsWEEVKnEMVGEKGLAPEVADRIGDYVQQHGGVSLVEQLLQDpkLSQNKQALEGLGDLKLLF 237
Cdd:pfam13393 166 SEALEEALRAALQRKD---AAELA-ELAAEAGLPPALRRALLALPDLYGGPEVLDEARAA--LPGLPALQEALDELEALA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 238 EYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLlqtpAQAGEEplgvgsVAAGGRYDGLVGMFdpkGRKVPCVGLSIGV 317
Cdd:pfam13393 240 ALLEALGDGVRLTFDLAELRGYEYYTGIVFAAYA----PGVGEP------LARGGRYDDLGAAF---GRARPATGFSLDL 306
|
...
gi 119582425 318 ERI 320
Cdd:pfam13393 307 EAL 309
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02972 |
PLN02972 |
Histidyl-tRNA synthetase |
1-432 |
0e+00 |
|
Histidyl-tRNA synthetase
Pssm-ID: 215525 [Multi-domain] Cd Length: 763 Bit Score: 565.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 1 MAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGEDSKLIYDLKDQGGELLSLRYDLTVPFARYLAMNKLTNIKR 80
Cdd:PLN02972 341 MAIREKAFSIITSVFKRHGATALDTPVFELRETLMGKYGEDSKLIYDLADQGGELCSLRYDLTVPFARYVAMNGITSFKR 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 81 YHIAKVYRRDNPamTRGRYREFYQCDFDIAGNFDPMIPDAECLKIMCEILSSLQIGDFLVKVNDRRILDGMFAICGVSDS 160
Cdd:PLN02972 421 YQIAKVYRRDNP--SKGRYREFYQCDFDIAGVYEPMGPDFEIIKVLTELLDELDIGTYEVKLNHRKLLDGMLEICGVPPE 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 161 KFRTICSSVDKLDKVSWEEVKNEMVGEKGLAPEVADRIGDYVQQHGG-VSLVEQLLQ-DPKLSQNKQALEGLGDLKLLFE 238
Cdd:PLN02972 499 KFRTICSSIDKLDKQSFEQVKKEMVEEKGLSNETADKIGNFVKERGPpLELLSKLRQeGSEFLGNASSRAALDELEIMFK 578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 239 YLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLLQTPaqageeplgVGSVAAGGRYDGLVGMFDpkGRKVPCVGLSIGVE 318
Cdd:PLN02972 579 ALEKSKAIGKIVFDLSLARGLDYYTGVIYEAVFKGAQ---------VGSIAAGGRYDNLVGMFS--GKQVPAVGVSLGIE 647
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 319 RIFSIVEQRLEALEEKIRTTETQVLVASAQKKLLEERLKLVSELWDAGIKAEllYKKNPKLLNQLQYCEEAGIPLVAIIG 398
Cdd:PLN02972 648 RVFAIMEQQEEEKSQVIRPTETEVLVSIIGDDKLALAAELVSELWNAGIKAE--YKVSTRKAKHLKRAKESGIPWMVLVG 725
|
410 420 430
....*....|....*....|....*....|....
gi 119582425 399 EQELKDGVIKLRSVTSREEVDVRREDLVEEIKRR 432
Cdd:PLN02972 726 EKELSKGFVKLKNLEAGVEEEVDRTCFVQELKAE 759
|
|
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
1-432 |
2.99e-111 |
|
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: 333.63 E-value: 2.99e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 1 MAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGED--SKLIYDLKDQGGELLSLRYDLTVPFARYLAMNKLTN- 77
Cdd:COG0124 18 SAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKIGEDivEKEMYTFEDRGGRSLTLRPEGTAPVARAVAEHGNELp 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 78 --IKRYHIAKVYRRDNPAmtRGRYREFYQCDFDIAGNFDPMIpDAECLKIMCEILSSLQIGDFLVKVNDRrildgmfaic 155
Cdd:COG0124 98 fpFKLYYIGPVFRYERPQ--KGRYRQFHQFGVEVIGSDSPLA-DAEVIALAADLLKALGLKDFTLEINSR---------- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 156 GVSDSKFRTICSSVDKLDKVSWEEVknemvgekgLAPEVADRI------------GDYVQqhggvSLVEQLlqdPKLSQN 223
Cdd:COG0124 165 GLPEERAEALLRYLDKLDKIGHEDV---------LDEDSQRRLetnplraildskGPDCQ-----EVLADA---PKLLDY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 224 KqALEGLGDLKLLFEYLTLFGIDdkISFDLSLARGLDYYTGVIYEAVLLQTPAQageeplgvGSVAAGGRYDGLVGMFDp 303
Cdd:COG0124 228 L-GEEGLAHFEEVLELLDALGIP--YVIDPRLVRGLDYYTGTVFEIVTDGLGAQ--------GSVCGGGRYDGLVEQLG- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 304 kGRKVPCVGLSIGVERIFSIVEQRLEALEEKirtTETQVLVASAQKKLLEERLKLVSELWDAGIKAEL-LYKKNPKllNQ 382
Cdd:COG0124 296 -GPPTPAVGFAIGLERLLLLLEELGLLPAAE---PPPDVYVVPLGEEARAEALKLAQELRAAGIRVELdLGGRKLK--KQ 369
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 119582425 383 LQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVDVRREDLVEEIKRR 432
Cdd:COG0124 370 LKYADKSGAPFVLILGEDELANGTVTLKDLATGEQETVPLDELVEYLKEL 419
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
1-325 |
2.40e-104 |
|
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: 310.30 E-value: 2.40e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 1 MAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGED-SKLIYDLKDQGGELLSLRYDLTVPFARYLAMNKL---T 76
Cdd:cd00773 2 AALRRYIEDTLREVFERYGYEEIDTPVFEYTELFLRKSGDEvSKEMYRFKDKGGRDLALRPDLTAPVARAVAENLLslpL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 77 NIKRYHIAKVYRRDNPAmtRGRYREFYQCDFDIAGnFDPMIPDAECLKIMCEILSSLQIGDFLVKVNDRRILDGmfaICG 156
Cdd:cd00773 82 PLKLYYIGPVFRYERPQ--KGRYREFYQVGVEIIG-SDSPLADAEVIALAVEILEALGLKDFQIKINHRGILDG---IAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 157 VSDSKFRTICSSVDKLDKvsweevknemvgekglapevadrigdyvqqhggvslveqllqdpklsqnkqalEGLGDLKLL 236
Cdd:cd00773 156 LLEDREEYIERLIDKLDK-----------------------------------------------------EALAHLEKL 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 237 FEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLLQTPAQageeplgvGSVAAGGRYDGLVGMFDpkGRKVPCVGLSIG 316
Cdd:cd00773 183 LDYLEALGVDIKYSIDLSLVRGLDYYTGIVFEAVADGLGAQ--------GSIAGGGRYDGLLEEFG--GEDVPAVGFAIG 252
|
....*....
gi 119582425 317 VERIFSIVE 325
Cdd:cd00773 253 LERLLLALE 261
|
|
| hisS |
TIGR00442 |
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ... |
1-420 |
3.53e-97 |
|
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: 297.08 E-value: 3.53e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 1 MAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGEDS----KLIYDLKDQGGELLSLRYDLTVPFARYLAMNKLT 76
Cdd:TIGR00442 14 MIKWQYIEETIREVFERYGFKEIRTPIFEYTELFKRKVGEETdivsKEMYTFKDKGGRSLTLRPEGTAPVARAVIENKLL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 77 N---IKRYHIAKVYRRDNPAmtRGRYREFYQCDFDIAGNFDPMIpDAECLKIMCEILSSLQIGDFLVKVNDRRILDGMFA 153
Cdd:TIGR00442 94 LpkpFKLYYIGPMFRYERPQ--KGRYRQFHQFGVEVIGSDSPLA-DAEIIALAADILKELGLKDFTLEINSLGILEGRLE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 154 icgvsdsKFRTICSSVDK-LDKVSWEEVKNEMVGEKGLAPEVADRIGDYVQQhggvslveqllqDPKLSQNKQAlEGLGD 232
Cdd:TIGR00442 171 -------YREALIRYLDKhKDKLGEDSVRRLEKNPLRILDSKNEKIQELLKN------------APKILDFLCE-ESRAH 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 233 LKLLFEYLTLFGIddKISFDLSLARGLDYYTGVIYEAVLLQTPAQageeplgvGSVAAGGRYDGLVGMFDpkGRKVPCVG 312
Cdd:TIGR00442 231 FEELKELLDALGI--PYKIDPSLVRGLDYYTGTVFEFVTDDLGAQ--------GSICGGGRYDGLVEELG--GPPTPAVG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 313 LSIGVERIFSIVEQRLEALEEKirtTETQVLVASAQKKLLEERLKLVSELWDAGIKAElLYKKNPKLLNQLQYCEEAGIP 392
Cdd:TIGR00442 299 FAIGIERLILLLEELGLIPPPS---KKPDVYVVPLGEEAELEALKLAQKLRKAGIRVE-VDLGGRKLKKQLKYADKLGAR 374
|
410 420
....*....|....*....|....*...
gi 119582425 393 LVAIIGEQELKDGVIKLRSVTSREEVDV 420
Cdd:TIGR00442 375 FALIIGEDELENGTVTLKDLETGEQETV 402
|
|
| PRK12420 |
PRK12420 |
histidyl-tRNA synthetase; Provisional |
2-420 |
2.71e-77 |
|
histidyl-tRNA synthetase; Provisional
Pssm-ID: 237097 [Multi-domain] Cd Length: 423 Bit Score: 246.57 E-value: 2.71e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 2 AVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYG---EDSKLIYDLKDQGGELLSLRYDLTVPFARYLAMNKltNI 78
Cdd:PRK12420 19 VLRNKIKRALEDVFERYGCKPLETPTLNMYELMSSKYGggdEILKEIYTLTDQGKRDLALRYDLTIPFAKVVAMNP--NI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 79 ----KRYHIAKVYrRDNPaMTRGRYREFYQCDFDIAGNFDPMiPDAECLKIMCEILSSLQIgDFLVKVNDRRILDGMFAI 154
Cdd:PRK12420 97 rlpfKRYEIGKVF-RDGP-IKQGRFREFIQCDVDIVGVESVM-AEAELMSMAFELFRRLNL-EVTIQYNNRKLLNGILQA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 155 CGVSDSKFRTICSSVDKLDKVSWEEVKNEMVgEKGLAPEVADRIGDYVQQHGGVSLVEQllqdPKLSQNKQALEGLGDLK 234
Cdd:PRK12420 173 IGIPTELTSDVILSLDKIEKIGIDGVRKDLL-ERGISEEMADTICNTVLSCLQLSIADF----KEAFNNPLVAEGVNELQ 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 235 LLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEaVLLQTPAQAgeeplgvGSVAAGGRYDGLVGMFDPKGRKVPCVGLS 314
Cdd:PRK12420 248 QLQQYLIALGINENCIFNPFLARGLTMYTGTVYE-IFLKDGSIT-------SSIGSGGRYDNIIGAFRGDDMNYPTVGIS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 315 IGVERIfsiveqrLEALEEKIRTTET-QVLVASAQKKLleERLKLVSELW-DAGIKAELLYkKNPKLLNQLQYCEEAGIP 392
Cdd:PRK12420 320 FGLDVI-------YTALSQKETISSTaDVFIIPLGTEL--QCLQIAQQLRsTTGLKVELEL-AGRKLKKALNYANKENIP 389
|
410 420
....*....|....*....|....*...
gi 119582425 393 LVAIIGEQELKDGVIKLRSVTSREEVDV 420
Cdd:PRK12420 390 YVLIIGEEEVSTGTVMLRNMKEGSEVKV 417
|
|
| HisZ |
COG3705 |
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism]; |
2-320 |
3.74e-49 |
|
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism];
Pssm-ID: 442919 [Multi-domain] Cd Length: 312 Bit Score: 169.59 E-value: 3.74e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 2 AVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGEDSKL-IYDLKDQGGELLSLRYDLTVPFARYLAmNKLTNIKR 80
Cdd:COG3705 6 ARKEELRRRLLDVFRSWGYELVEPPLLEYLDSLLTGSGADLDLqTFKLVDQLGRTLGLRPDMTPQVARIAA-TRLANRPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 81 ----YHIAKVYRrdNPAMTRGRYREFYQC------DFDIAGnfdpmipDAECLKIMCEILSSLQIGDFLVKVNDRRILDG 150
Cdd:COG3705 85 plrlCYAGNVFR--TRPSGLGRSREFLQAgaeligHAGLEA-------DAEVIALALEALKAAGLEDFTLDLGHVGLFRA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 151 MFAICGVSDSKFRTICSSVDKLDKVsweEVKnEMVGEKGLAPEVADRIGDYVQQHGGVSLVEQLLqdpKLSQNKQALEGL 230
Cdd:COG3705 156 LLEALGLSEEQREELRRALARKDAV---ELE-ELLAELGLSEELAEALLALPELYGGEEVLARAR---ALLLDAAIRAAL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 231 GDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLlqtpAQAGEEplgvgsVAAGGRYDGLVGMFdpkGRKVPC 310
Cdd:COG3705 229 DELEALAEALAARGPDVRLTFDLSELRGYDYYTGIVFEAYA----PGVGDP------LARGGRYDGLLAAF---GRARPA 295
|
330
....*....|
gi 119582425 311 VGLSIGVERI 320
Cdd:COG3705 296 TGFSLDLDRL 305
|
|
| hisZ_biosyn_reg |
TIGR00443 |
ATP phosphoribosyltransferase, regulatory subunit; Apparant second copies of histidyl-tRNA ... |
2-320 |
5.42e-47 |
|
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: 163.94 E-value: 5.42e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 2 AVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGEDSKLIYDLKDQGGELLSLRYDLTVPFARyLAMNKLTNIKR- 80
Cdd:TIGR00443 9 ARKEEIERQLQDVFRSWGYQEIITPTLEYLDTLSAGSGILNEDLFKLFDQLGRVLGLRPDMTAPIAR-LVSTRLRDRPLp 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 81 ---YHIAKVYRRDNPAmtRGRYREFYQCDFDIAGNfDPMIPDAECLKIMCEILSSLQIGDFLVKVNDRRILDGMFAICGV 157
Cdd:TIGR00443 88 lrlCYAGNVFRTNESG--GGRSREFTQAGVELIGA-GGPAADAEVIALLIEALKALGLKDFKIELGHVGLVRALLEEAGL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 158 SDSKFRTICSSVDKLDKVSWEEVknemVGEKGLAPEVADRIGDYVQQHGGVSLVEQLLQdpKLSQNKQALEGLGDLKLLF 237
Cdd:TIGR00443 165 PEEAREALREALARKDLVALEEL----VAELGLSPEVRERLLALPRLRGDGEEVLEEAR--ALAGSETAEAALDELEAVL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 238 EYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLLQTPAQageeplgvgsVAAGGRYDGLVGMFdpkGRKVPCVGLSIGV 317
Cdd:TIGR00443 239 ELLEARGVEEYISLDLGLVRGYHYYTGLIFEGYAPGLGAP----------LAGGGRYDELLGRF---GRPLPATGFALNL 305
|
...
gi 119582425 318 ERI 320
Cdd:TIGR00443 306 ERL 308
|
|
| PLN02530 |
PLN02530 |
histidine-tRNA ligase |
1-425 |
9.52e-45 |
|
histidine-tRNA ligase
Pssm-ID: 178145 [Multi-domain] Cd Length: 487 Bit Score: 162.60 E-value: 9.52e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 1 MAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGED-SKLIYDLKDQGGELLSLRYDLTVPFARyLAMNKLTNI- 78
Cdd:PLN02530 84 MRLRNWLFDHFREVSRLFGFEEVDAPVLESEELYIRKAGEEiTDQLYNFEDKGGRRVALRPELTPSLAR-LVLQKGKSLs 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 79 ---KRYHIAKVYRRDNpaMTRGRYREFYQCDFDIAGnFDPMIPDAECLKIMCEILSSLQI--GDFLVKVNDRRILDGMFA 153
Cdd:PLN02530 163 lplKWFAIGQCWRYER--MTRGRRREHYQWNMDIIG-VPGVEAEAELLAAIVTFFKRVGItsSDVGIKVSSRKVLQAVLK 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 154 ICGVSDSKFRTICSSVDKLDKVSWEEVKNEMvGEKGLAPEVADRIGDyVQQHGGVSLVEQLLqdpklsqnKQALEGLGDL 233
Cdd:PLN02530 240 SYGIPEESFAPVCVIVDKLEKLPREEIEKEL-DTLGVSEEAIEGILD-VLSLKSLDDLEALL--------GADSEAVADL 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 234 KLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVllqtpAQAGEeplgVGSVAAGGRYDGLVGMFDpkGRKVPCVGL 313
Cdd:PLN02530 310 KQLFSLAEAYGYQDWLVFDASVVRGLAYYTGIVFEGF-----DRAGK----LRAICGGGRYDRLLSTFG--GEDTPACGF 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 314 SIGVERIFSIVEQRlEALEEKIRTTETqvLVASAQKKLLEERLKLVSELWDAGIKAEL-LYKKNPKLLnqLQYCEEAGIP 392
Cdd:PLN02530 379 GFGDAVIVELLKEK-GLLPELPHQVDD--VVFALDEDLQGAAAGVASRLREKGRSVDLvLEPKKLKWV--FKHAERIGAK 453
|
410 420 430
....*....|....*....|....*....|...
gi 119582425 393 LVAIIGEQELKDGVIKLRSVTSREEVDVRREDL 425
Cdd:PLN02530 454 RLVLVGASEWERGMVRVKDLSSGEQTEVKLDEL 486
|
|
| hisZ |
PRK12292 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
4-371 |
2.45e-43 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 237043 [Multi-domain] Cd Length: 391 Bit Score: 156.56 E-value: 2.45e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 4 REKVFDVIIRCFKRHGAEVIDTPVFELKETLM--GKYGEDSKLIYDLKDQGGELLSLRYDLTVPFARyLAMNKLTNIKR- 80
Cdd:PRK12292 20 IEEIRRRLLDLFRRWGYEEVITPTLEYLDTLLagGGAILDLRTFKLVDQLSGRTLGLRPDMTAQIAR-IAATRLANRPGp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 81 ---YHIAKVYRrdNPAMTRGRYREFYQCDFDIAGnFDPMIPDAECLKIMCEILSSLQIGDFLVKVNDRRILDGMFAICGV 157
Cdd:PRK12292 99 lrlCYAGNVFR--AQERGLGRSREFLQSGVELIG-DAGLEADAEVILLLLEALKALGLPNFTLDLGHVGLFRALLEAAGL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 158 SDSKFRTICSSVDKLDKVSWEEVknemvgEKGLAPEVADRIGDYVQQHGGVSLVEQLLQdpkLSQNKQALEGLGDLKLLF 237
Cdd:PRK12292 176 SEELEEVLRRALANKDYVALEEL------VLDLSEELRDALLALPRLRGGREVLEEARK---LLPSLPIKRALDELEALA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 238 EYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLLQTPAqageeplgvgSVAAGGRYDGLVGMFdpkGRKVPCVGLSIGV 317
Cdd:PRK12292 247 EALEKYGYGIPLSLDLGLLRHLDYYTGIVFEGYVDGVGN----------PIASGGRYDDLLGRF---GRARPATGFSLDL 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 119582425 318 ERIfsiveqrLEALEEKiRTTETQVLVASAQKKLLEERLKLVSELWDAGIKAEL 371
Cdd:PRK12292 314 DRL-------LELQLEL-PVEARKDLVIAPDSEALAAALAAAQELRKKGEIVVL 359
|
|
| tRNA-synt_His |
pfam13393 |
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ... |
2-320 |
3.39e-42 |
|
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: 151.20 E-value: 3.39e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 2 AVREKVFDViircFKRHGAEVIDTPVFELKETLMGKYGEDSKLIYDLKDQGGELLSLRYDLTVPFARYLAmnKLTNIKR- 80
Cdd:pfam13393 15 ELRRRLLDL----FRSWGYELVMPPLLEYLDSLLTGTGADLDQTFKLVDQSGRLLGLRADITPQVARIDA--HRLNRPGp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 81 ---YHIAKVYRRDNPAMtrGRYREFYQCDFDIAGNFDPMiPDAECLKIMCEILSSLQIGDFLVKVNDRRILDGMFAICGV 157
Cdd:pfam13393 89 lrlCYAGSVLRTRPKGL--GRSREPLQVGAELIGHAGIE-ADAEIISLLLEALAAAGVPGVTLDLGHVGLVRALLEAAGL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 158 SDSKFRTICSSVDKLDkvsWEEVKnEMVGEKGLAPEVADRIGDYVQQHGGVSLVEQLLQDpkLSQNKQALEGLGDLKLLF 237
Cdd:pfam13393 166 SEALEEALRAALQRKD---AAELA-ELAAEAGLPPALRRALLALPDLYGGPEVLDEARAA--LPGLPALQEALDELEALA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 238 EYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLlqtpAQAGEEplgvgsVAAGGRYDGLVGMFdpkGRKVPCVGLSIGV 317
Cdd:pfam13393 240 ALLEALGDGVRLTFDLAELRGYEYYTGIVFAAYA----PGVGEP------LARGGRYDDLGAAF---GRARPATGFSLDL 306
|
...
gi 119582425 318 ERI 320
Cdd:pfam13393 307 EAL 309
|
|
| HisRS_anticodon |
cd00859 |
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases ... |
339-430 |
2.30e-29 |
|
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: 109.94 E-value: 2.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 339 ETQVLVASAQKKLLEERLKLVSELWDAGIKAELLYKkNPKLLNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEV 418
Cdd:cd00859 1 EVDVYVVPLGEGALSEALELAEQLRDAGIKAEIDYG-GRKLKKQFKYADRSGARFAVILGEDELAAGVVTVKDLETGEQE 79
|
90
....*....|..
gi 119582425 419 DVRREDLVEEIK 430
Cdd:cd00859 80 TVALDELVEELK 91
|
|
| syh |
CHL00201 |
histidine-tRNA synthetase; Provisional |
7-429 |
5.51e-26 |
|
histidine-tRNA synthetase; Provisional
Pssm-ID: 164576 [Multi-domain] Cd Length: 430 Bit Score: 109.22 E-value: 5.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 7 VFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGEDSKLI----YDLKDQGGELLSLRYDLTVPFARYLAMNKLT---NIK 79
Cdd:CHL00201 24 IHDKALTLLSLANYSEIRTPIFENSSLYDRGIGETTDIVnkemYRFTDRSNRDITLRPEGTAGIVRAFIENKMDyhsNLQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 80 R-YHIAKVYRRDNPamTRGRYREFYQCDFDIAGNFDPMiPDAECLKIMCEILSSLQIGDFLVKVN------DRRILDgmf 152
Cdd:CHL00201 104 RlWYSGPMFRYERP--QSGRQRQFHQLGIEFIGSIDAR-ADTEVIHLAMQIFNELQVKNLILDINsigkleDRQSYQ--- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 153 aicgvsdSKFRTICSSV-DKLDKVSweevKNEMVGEkglaP-EVADRIGDYVQqhggvslvEQLLQDPKLSQ--NKQALE 228
Cdd:CHL00201 178 -------LKLVEYLSQYqDDLDTDS----QNRLYSN----PiRILDSKNLKTQ--------EILDGAPKISDflSLESTE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 229 GLGDLkllFEYLTLFGIDDKISFdlSLARGLDYYTGVIYEAVLLQTPAQageeplgvGSVAAGGRYDGLVGMFDpkGRKV 308
Cdd:CHL00201 235 HFYDV---CTYLNLLNIPYKINY--KLVRGLDYYNDTAFEIKTLSSNGQ--------DTICGGGRYDSLIHQLG--GPKT 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 309 PCVGLSIGVERIFSIVEQRLEALEEKIrttetQVLVASAQKKLLEERLKLVSELWDAGIKAELLYkKNPKLLNQLQYCEE 388
Cdd:CHL00201 300 PAVGCAIGLERLLLIAKDNIILPKQSI-----DVYIATQGLKAQKKGWEIIQFLEKQNIKFELDL-SSSNFHKQIKQAGK 373
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 119582425 389 AGIPLVAIIGEQELKDGVIKLRSVTSREEVDVRREDLVEEI 429
Cdd:CHL00201 374 KRAKACIILGDNEIMDNCITIKWLDEQVQENAQYSNFKQEI 414
|
|
| hisZ |
PRK12295 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
1-320 |
7.59e-23 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 183413 [Multi-domain] Cd Length: 373 Bit Score: 99.24 E-value: 7.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 1 MAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGED-SKLIYDLKDQGGELLSLRYDLTVPFAR-YLAMNKLTNI 78
Cdd:PRK12295 4 LSASAAAAEALLASFEAAGAVRVDPPILQPAEPFLDLSGEDiRRRIFVTSDENGEELCLRPDFTIPVCRrHIATAGGEPA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 79 KRYHIAKVYRRdnpamTRGRYREFYQCDFDIAGNFDPMIPDAECLKIMCEILSSLQIGDFLVKVNDRRILDGMFAICGVS 158
Cdd:PRK12295 84 RYAYLGEVFRQ-----RRDRASEFLQAGIESFGRADPAAADAEVLALALEALAALGPGDLEVRLGDVGLFAALVDALGLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 159 DS-KFRTIcssVDKLDKVSWEEVKNEMVGEKGLAPEVADRIGDYVQQHGGVS-LVEQLLQDPKLSQN------------- 223
Cdd:PRK12295 159 PGwKRRLL---RHFGRPRSLDALLARLAGPRVDPLDEHAGVLAALADEAAARaLVEDLMSIAGISPVggrspaeiarrll 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 224 -----------------------------KQALEGL----GDLKL-------LFE----YLTLFGID-DKISFDLSLARG 258
Cdd:PRK12295 236 ekaalaaaarlpaealavlerflaisgppDAALAALralaADAGLdldaaldRFEarlaALAARGIDlERLRFSASFGRP 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119582425 259 LDYYTGVIYEAvllqTPAQAGEEPLgvgsvAAGGRYDGLVGMFDpKGRKVPCVGLSIGVERI 320
Cdd:PRK12295 316 LDYYTGFVFEI----RAAGNGDPPL-----AGGGRYDGLLTRLG-AGEPIPAVGFSIWLDRL 367
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
341-432 |
9.86e-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: 78.01 E-value: 9.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 341 QVLVASAQKK---LLEERLKLVSELWDAGIKAELLYKkNPKLLNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREE 417
Cdd:pfam03129 1 QVVVIPLGEKaeeLEEYAQKLAEELRAAGIRVELDDR-NESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQ 79
|
90
....*....|....*
gi 119582425 418 VDVRREDLVEEIKRR 432
Cdd:pfam03129 80 ETVSLDELVEKLKEL 94
|
|
| PRK12421 |
PRK12421 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
2-366 |
7.63e-10 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 237098 Cd Length: 392 Bit Score: 60.37 E-value: 7.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 2 AVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGEDSKL-IYDLKDQ-GGELLSLRYDLTVPFARYLA-MNKLTNI 78
Cdd:PRK12421 22 QKIERLRRRLLDLFASRGYQLVMPPLIEYLESLLTGAGQDLKLqTFKLIDQlSGRLMGVRADITPQVARIDAhLLNREGV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 79 KRY-HIAKVY--RRDNPAMTRGRYR---EFYQCDfDIAGnfdpmipDAECLKIMCEILSSLQIGDFLVKVNDRRILDGMF 152
Cdd:PRK12421 102 ARLcYAGSVLhtLPQGLFGSRTPLQlgaELYGHA-GIEA-------DLEIIRLMLGLLRNAGVPALHLDLGHVGIFRRLA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 153 AICGVSDSKFRTIcssVDKLDKVSWEEVKnEMVGEKGLAPEVADRIGDYVQQHGGVSLVEQLLQDpKLSQNKQALEGLGD 232
Cdd:PRK12421 174 ELAGLSPEEEEEL---FDLLQRKALPELA-EVCQNLGVGSDLRRMFYALARLNGGLEALDRALSV-LALQDAAIRQALDE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 233 LKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYeAVLLQTPAQAgeeplgvgsVAAGGRYDGLVGMFdpkGRKVPCVG 312
Cdd:PRK12421 249 LKTLAAHLKNRWPELPVSIDLAELRGYHYHTGLVF-AAYIPGRGQA---------LARGGRYDGIGEAF---GRARPATG 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 119582425 313 lsigveriFSIVEQRLEALEEKIRTTETQVLVASAQKKLLEErlklVSELWDAG 366
Cdd:PRK12421 316 --------FSMDLKELLALQFLEEEAGAILAPWGDDPDLLAA----IAELRQQG 357
|
|
| HGTP_anticodon2 |
pfam12745 |
Anticodon binding domain of tRNAs; This is an HGTP_anticodon binding domain, found largely on ... |
342-432 |
2.48e-08 |
|
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: 54.92 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 342 VLVASAQKKLL-EERLKLVSELWDAGIKAELLYKKNPKLLNQLQYCEEAGIPLVAIIGEQEL----KDGVIKLRSVTSRE 416
Cdd:pfam12745 8 VLVASFDASILrTTGVEILQELWAHGISADLAVDASYSPEDLVSRARDDGVSWIVIIKQQNKssdsKYKPLKVKNLLRKE 87
|
90 100
....*....|....*....|
gi 119582425 417 EVDVRREDLV----EEIKRR 432
Cdd:pfam12745 88 DVDLDSDELVswlrGEIRER 107
|
|
| PRK03991 |
PRK03991 |
threonyl-tRNA synthetase; Validated |
316-436 |
7.49e-06 |
|
threonyl-tRNA synthetase; Validated
Pssm-ID: 235190 [Multi-domain] Cd Length: 613 Bit Score: 48.33 E-value: 7.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 316 GVER-IFSIVE-QRLEALEEKIRT-----TETQVLVASAQKKLLEERLKLVSELWDAGIKAEL------LYKKnpkllnq 382
Cdd:PRK03991 469 SIERvIYALLEkAAKEEEEGKVPMlptwlSPTQVRVIPVSERHLDYAEEVADKLEAAGIRVDVddrdesLGKK------- 541
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119582425 383 lqyCEEAG---IPLVAIIGEQELKDGVIklrSVTSREE---VDVRREDLVEEIKRRT-GQP 436
Cdd:PRK03991 542 ---IRDAGkewIPYVVVIGDKEMESGKL---TVTIREEsekVEMTLEELIERIKEETkGYP 596
|
|
| ThrRS_anticodon |
cd00860 |
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases ... |
340-430 |
5.50e-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: 35.94 E-value: 5.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 340 TQVLVASAQKKLLEERLKLVSELWDAGIKAELLYKkNPKLLNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVD 419
Cdd:cd00860 2 VQVVVIPVTDEHLDYAKEVAKKLSDAGIRVEVDLR-NEKLGKKIREAQLQKIPYILVVGDKEVETGTVSVRTRDGGDLGS 80
|
90
....*....|.
gi 119582425 420 VRREDLVEEIK 430
Cdd:cd00860 81 MSLDEFIEKLK 91
|
|
| PRK09194 |
PRK09194 |
prolyl-tRNA synthetase; Provisional |
302-431 |
8.22e-03 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 236405 [Multi-domain] Cd Length: 565 Bit Score: 38.53 E-value: 8.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 302 DPKGRKVP----CVGlsIGVERIFS-IVEQRLEaleEK--IRTTET---QV-LVAS-----AQKKLLEerlKLVSELWDA 365
Cdd:PRK09194 426 DENGKAQPlimgCYG--IGVSRLVAaAIEQNHD---EKgiIWPKAIapfDVhIVPVnmkdeEVKELAE---KLYAELQAA 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 366 GIK----------------AELLykknpkllnqlqyceeaGIPLVAIIGEQELKDGVIKLRSVTSREEVDVRREDLVEEI 429
Cdd:PRK09194 498 GIEvllddrkerpgvkfadADLI-----------------GIPHRIVVGDRGLAEGIVEYKDRRTGEKEEVPVDELVEFL 560
|
..
gi 119582425 430 KR 431
Cdd:PRK09194 561 KA 562
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
3-142 |
8.88e-03 |
|
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA synthetases (aaRS) share a common fold and generally attach an amino acid to the 3' OH of ribose of the appropriate tRNA. PheRS is an exception in that it attaches the amino acid at the 2'-OH group, like class I aaRSs. These enzymes are usually homodimers. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. The substrate specificity of this reaction is further determined by additional domains. Intererestingly, this domain is also found is asparagine synthase A (AsnA), in the accessory subunit of mitochondrial polymerase gamma and in the bacterial ATP phosphoribosyltransferase regulatory subunit HisZ.
Pssm-ID: 238391 [Multi-domain] Cd Length: 211 Bit Score: 37.48 E-value: 8.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119582425 3 VREKVFDVIIRCFKRHGAEVIDTPVFElKETLMGKYGEDSKLIYDLKDQGGELLSLRYDLTvPFARYLAMNKLTNI--KR 80
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVE-REPLLEKAGHEPKDLLPVGAENEEDLYLRPTLE-PGLVRLFVSHIRKLplRL 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119582425 81 YHIAKVYRRDNPAMTRGRYREFYQCDFDIAG-NFDPMIPDAECLKIMCEILSSLQIGDFLVKV 142
Cdd:cd00768 79 AEIGPAFRNEGGRRGLRRVREFTQLEGEVFGeDGEEASEFEELIELTEELLRALGIKLDIVFV 141
|
|
|