|
Name |
Accession |
Description |
Interval |
E-value |
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
2-428 |
0e+00 |
|
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: 627.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 2 SKSLQAIRGMNDILPEQTPAWRYLERTFAGLLDGYGYSEIRLPILEFTELFARGIGEgtDVVDKEMYTFLDRNGESLTMR 81
Cdd:COG0124 1 MMKIQAPRGTRDILPEESAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKIGE--DIVEKEMYTFEDRGGRSLTLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 82 PEGTAGCVRAVLEHGLsGGGQVQKLWYTGPMFRYEKPQKGRYRQFHQIGVEVFNLPGPDIDAELIILTWRLWQKLGMADa 161
Cdd:COG0124 79 PEGTAPVARAVAEHGN-ELPFPFKLYYIGPVFRYERPQKGRYRQFHQFGVEVIGSDSPLADAEVIALAADLLKALGLKD- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 162 VTLQLNTLGSSEARAryrEALVAYLQ-----ERFEQLDEDSQRRMTTNPLR-ILDSKVESTQALLVGAPTLHDYLDEESI 235
Cdd:COG0124 157 FTLEINSRGLPEERA---EALLRYLDkldkiGHEDVLDEDSQRRLETNPLRaILDSKGPDCQEVLADAPKLLDYLGEEGL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 236 AHFEGLKARLDAVGLRYEINQKLVRGLDYYCRTAFEWVTDKLGAQGTVCGGGRYDGLVSQFGGKPTPGVGFAMGVERLVL 315
Cdd:COG0124 234 AHFEEVLELLDALGIPYVIDPRLVRGLDYYTGTVFEIVTDGLGAQGSVCGGGRYDGLVEQLGGPPTPAVGFAIGLERLLL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 316 LLETLGVIPAElNRPADLYVCAFGEPAELAALTLAEQLRSAipGIRLLVNAGAGSFKSQFKKADKSGARFALILGEDEVA 395
Cdd:COG0124 314 LLEELGLLPAA-EPPPDVYVVPLGEEARAEALKLAQELRAA--GIRVELDLGGRKLKKQLKYADKSGAPFVLILGEDELA 390
|
410 420 430
....*....|....*....|....*....|...
gi 15598997 396 NRVVGFKPLRDeGEQQSIAWDALPEHLAACLAQ 428
Cdd:COG0124 391 NGTVTLKDLAT-GEQETVPLDELVEYLKELLAE 422
|
|
| hisS |
TIGR00442 |
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ... |
6-415 |
0e+00 |
|
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: 616.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 6 QAIRGMNDILPEQTPAWRYLERTFAGLLDGYGYSEIRLPILEFTELFARGIGEGTDVVDKEMYTFLDRNGESLTMRPEGT 85
Cdd:TIGR00442 1 QKPRGTRDFLPEEMIKWQYIEETIREVFERYGFKEIRTPIFEYTELFKRKVGEETDIVSKEMYTFKDKGGRSLTLRPEGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 86 AGCVRAVLEHGLSGGGQvQKLWYTGPMFRYEKPQKGRYRQFHQIGVEVFNLPGPDIDAELIILTWRLWQKLGMADaVTLQ 165
Cdd:TIGR00442 81 APVARAVIENKLLLPKP-FKLYYIGPMFRYERPQKGRYRQFHQFGVEVIGSDSPLADAEIIALAADILKELGLKD-FTLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 166 LNTLGSSEARARYREALVAYLQERFEQLDEDSQRRMTTNPLRILDSKVESTQALLVGAPTLHDYLDEESIAHFEGLKARL 245
Cdd:TIGR00442 159 INSLGILEGRLEYREALIRYLDKHKDKLGEDSVRRLEKNPLRILDSKNEKIQELLKNAPKILDFLCEESRAHFEELKELL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 246 DAVGLRYEINQKLVRGLDYYCRTAFEWVTDKLGAQGTVCGGGRYDGLVSQFGGKPTPGVGFAMGVERLVLLLETLGVIPA 325
Cdd:TIGR00442 239 DALGIPYKIDPSLVRGLDYYTGTVFEFVTDDLGAQGSICGGGRYDGLVEELGGPPTPAVGFAIGIERLILLLEELGLIPP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 326 ELNRPaDLYVCAFGEPAELAALTLAEQLRSAipGIRLLVNAGAGSFKSQFKKADKSGARFALILGEDEVANRVVGFKPLR 405
Cdd:TIGR00442 319 PSKKP-DVYVVPLGEEAELEALKLAQKLRKA--GIRVEVDLGGRKLKKQLKYADKLGARFALIIGEDELENGTVTLKDLE 395
|
410
....*....|
gi 15598997 406 DeGEQQSIAW 415
Cdd:TIGR00442 396 T-GEQETVPL 404
|
|
| syh |
CHL00201 |
histidine-tRNA synthetase; Provisional |
5-413 |
3.69e-134 |
|
histidine-tRNA synthetase; Provisional
Pssm-ID: 164576 [Multi-domain] Cd Length: 430 Bit Score: 392.34 E-value: 3.69e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 5 LQAIRGMNDILPEQTPAWRYLERTFAGLLDGYGYSEIRLPILEFTELFARGIGEGTDVVDKEMYTFLDRNGESLTMRPEG 84
Cdd:CHL00201 4 IQAIRGTKDILPDEINYWQFIHDKALTLLSLANYSEIRTPIFENSSLYDRGIGETTDIVNKEMYRFTDRSNRDITLRPEG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 85 TAGCVRAVLEHGLSGGGQVQKLWYTGPMFRYEKPQKGRYRQFHQIGVEVFNLPGPDIDAELIILTWRLWQKLGMADaVTL 164
Cdd:CHL00201 84 TAGIVRAFIENKMDYHSNLQRLWYSGPMFRYERPQSGRQRQFHQLGIEFIGSIDARADTEVIHLAMQIFNELQVKN-LIL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 165 QLNTLGSSEARARYREALVAYLQERFEQLDEDSQRRMTTNPLRILDSKVESTQALLVGAPTLHDYLDEESIAHFEGLKAR 244
Cdd:CHL00201 163 DINSIGKLEDRQSYQLKLVEYLSQYQDDLDTDSQNRLYSNPIRILDSKNLKTQEILDGAPKISDFLSLESTEHFYDVCTY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 245 LDAVGLRYEINQKLVRGLDYYCRTAFEWVTDKLGAQGTVCGGGRYDGLVSQFGGKPTPGVGFAMGVERLVLLLETLGVIP 324
Cdd:CHL00201 243 LNLLNIPYKINYKLVRGLDYYNDTAFEIKTLSSNGQDTICGGGRYDSLIHQLGGPKTPAVGCAIGLERLLLIAKDNIILP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 325 aelNRPADLYVCAFGEPAELAALTLAEQLRSAIpgIRLLVNAGAGSFKSQFKKADKSGARFALILGEDEVANRVVGFKPL 404
Cdd:CHL00201 323 ---KQSIDVYIATQGLKAQKKGWEIIQFLEKQN--IKFELDLSSSNFHKQIKQAGKKRAKACIILGDNEIMDNCITIKWL 397
|
....*....
gi 15598997 405 rDEGEQQSI 413
Cdd:CHL00201 398 -DEQVQENA 405
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
22-318 |
1.91e-96 |
|
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. It is responsible for the attachment of histidine to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs. This domain is also found at the C-terminus of eukaryotic GCN2 protein kinase and at the N-terminus of the ATP phosphoribosyltransferase accessory subunit, HisZ. HisZ along with HisG catalyze the first reaction in histidine biosynthesis. HisZ is found only in a subset of bacteria and differs from HisRS in lacking a C-terminal anti-codon binding domain.
Pssm-ID: 238396 [Multi-domain] Cd Length: 261 Bit Score: 289.89 E-value: 1.91e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 22 WRYLERTFAGLLDGYGYSEIRLPILEFTELFARGIGegtDVVDKEMYTFLDRNGESLTMRPEGTAGCVRAVLEHGLSGGg 101
Cdd:cd00773 5 RRYIEDTLREVFERYGYEEIDTPVFEYTELFLRKSG---DEVSKEMYRFKDKGGRDLALRPDLTAPVARAVAENLLSLP- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 102 QVQKLWYTGPMFRYEKPQKGRYRQFHQIGVEVFNLPGPDIDAELIILTWRLWQKLGMADaVTLQLNTLGSseararyrea 181
Cdd:cd00773 81 LPLKLYYIGPVFRYERPQKGRYREFYQVGVEIIGSDSPLADAEVIALAVEILEALGLKD-FQIKINHRGI---------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 182 lvayLQERFEQLDEDSQRRMttnplrildskvestqallvgapTLHDYLDEESIAHFEGLKARLDAVGL--RYEINQKLV 259
Cdd:cd00773 150 ----LDGIAGLLEDREEYIE-----------------------RLIDKLDKEALAHLEKLLDYLEALGVdiKYSIDLSLV 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 15598997 260 RGLDYYCRTAFEWVTDKLGAQGTVCGGGRYDGLVSQFGGKPTPGVGFAMGVERLVLLLE 318
Cdd:cd00773 203 RGLDYYTGIVFEAVADGLGAQGSIAGGGRYDGLLEEFGGEDVPAVGFAIGLERLLLALE 261
|
|
| tRNA-synt_His |
pfam13393 |
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ... |
10-313 |
2.91e-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: 140.41 E-value: 2.91e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 10 GMNDILPEQTPAWRYLERTFAGLLDGYGYSEIRLPILEFTELFARGIGEGTDvvdkEMYTFLDRNGESLTMRPEGTAGCV 89
Cdd:pfam13393 1 GIRDLLPPEARRIEELRRRLLDLFRSWGYELVMPPLLEYLDSLLTGTGADLD----QTFKLVDQSGRLLGLRADITPQVA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 90 RAVlEHGLSGGGqVQKLWYTGPMFRYEKPQKGRYRQFHQIGVEVFNLPGPDIDAELIIL-----------TWRLwqKLGM 158
Cdd:pfam13393 77 RID-AHRLNRPG-PLRLCYAGSVLRTRPKGLGRSREPLQVGAELIGHAGIEADAEIISLllealaaagvpGVTL--DLGH 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 159 ADAVTLQLNTLGSSEA-RARYREAL----VAYLQERFEQLDEDSQRRMTTNPLRIL---DSKVESTQALLVGAPTLHDYL 230
Cdd:pfam13393 153 VGLVRALLEAAGLSEAlEEALRAALqrkdAAELAELAAEAGLPPALRRALLALPDLyggPEVLDEARAALPGLPALQEAL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 231 DEesiahFEGLKARLDAVG--LRYEINQKLVRGLDYYCRTAFEWVTDklGAQGTVCGGGRYDGLVSQFgGKPTPGVGFAM 308
Cdd:pfam13393 233 DE-----LEALAALLEALGdgVRLTFDLAELRGYEYYTGIVFAAYAP--GVGEPLARGGRYDDLGAAF-GRARPATGFSL 304
|
....*
gi 15598997 309 GVERL 313
Cdd:pfam13393 305 DLEAL 309
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
2-428 |
0e+00 |
|
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: 627.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 2 SKSLQAIRGMNDILPEQTPAWRYLERTFAGLLDGYGYSEIRLPILEFTELFARGIGEgtDVVDKEMYTFLDRNGESLTMR 81
Cdd:COG0124 1 MMKIQAPRGTRDILPEESAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKIGE--DIVEKEMYTFEDRGGRSLTLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 82 PEGTAGCVRAVLEHGLsGGGQVQKLWYTGPMFRYEKPQKGRYRQFHQIGVEVFNLPGPDIDAELIILTWRLWQKLGMADa 161
Cdd:COG0124 79 PEGTAPVARAVAEHGN-ELPFPFKLYYIGPVFRYERPQKGRYRQFHQFGVEVIGSDSPLADAEVIALAADLLKALGLKD- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 162 VTLQLNTLGSSEARAryrEALVAYLQ-----ERFEQLDEDSQRRMTTNPLR-ILDSKVESTQALLVGAPTLHDYLDEESI 235
Cdd:COG0124 157 FTLEINSRGLPEERA---EALLRYLDkldkiGHEDVLDEDSQRRLETNPLRaILDSKGPDCQEVLADAPKLLDYLGEEGL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 236 AHFEGLKARLDAVGLRYEINQKLVRGLDYYCRTAFEWVTDKLGAQGTVCGGGRYDGLVSQFGGKPTPGVGFAMGVERLVL 315
Cdd:COG0124 234 AHFEEVLELLDALGIPYVIDPRLVRGLDYYTGTVFEIVTDGLGAQGSVCGGGRYDGLVEQLGGPPTPAVGFAIGLERLLL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 316 LLETLGVIPAElNRPADLYVCAFGEPAELAALTLAEQLRSAipGIRLLVNAGAGSFKSQFKKADKSGARFALILGEDEVA 395
Cdd:COG0124 314 LLEELGLLPAA-EPPPDVYVVPLGEEARAEALKLAQELRAA--GIRVELDLGGRKLKKQLKYADKSGAPFVLILGEDELA 390
|
410 420 430
....*....|....*....|....*....|...
gi 15598997 396 NRVVGFKPLRDeGEQQSIAWDALPEHLAACLAQ 428
Cdd:COG0124 391 NGTVTLKDLAT-GEQETVPLDELVEYLKELLAE 422
|
|
| hisS |
TIGR00442 |
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ... |
6-415 |
0e+00 |
|
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: 616.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 6 QAIRGMNDILPEQTPAWRYLERTFAGLLDGYGYSEIRLPILEFTELFARGIGEGTDVVDKEMYTFLDRNGESLTMRPEGT 85
Cdd:TIGR00442 1 QKPRGTRDFLPEEMIKWQYIEETIREVFERYGFKEIRTPIFEYTELFKRKVGEETDIVSKEMYTFKDKGGRSLTLRPEGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 86 AGCVRAVLEHGLSGGGQvQKLWYTGPMFRYEKPQKGRYRQFHQIGVEVFNLPGPDIDAELIILTWRLWQKLGMADaVTLQ 165
Cdd:TIGR00442 81 APVARAVIENKLLLPKP-FKLYYIGPMFRYERPQKGRYRQFHQFGVEVIGSDSPLADAEIIALAADILKELGLKD-FTLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 166 LNTLGSSEARARYREALVAYLQERFEQLDEDSQRRMTTNPLRILDSKVESTQALLVGAPTLHDYLDEESIAHFEGLKARL 245
Cdd:TIGR00442 159 INSLGILEGRLEYREALIRYLDKHKDKLGEDSVRRLEKNPLRILDSKNEKIQELLKNAPKILDFLCEESRAHFEELKELL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 246 DAVGLRYEINQKLVRGLDYYCRTAFEWVTDKLGAQGTVCGGGRYDGLVSQFGGKPTPGVGFAMGVERLVLLLETLGVIPA 325
Cdd:TIGR00442 239 DALGIPYKIDPSLVRGLDYYTGTVFEFVTDDLGAQGSICGGGRYDGLVEELGGPPTPAVGFAIGIERLILLLEELGLIPP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 326 ELNRPaDLYVCAFGEPAELAALTLAEQLRSAipGIRLLVNAGAGSFKSQFKKADKSGARFALILGEDEVANRVVGFKPLR 405
Cdd:TIGR00442 319 PSKKP-DVYVVPLGEEAELEALKLAQKLRKA--GIRVEVDLGGRKLKKQLKYADKLGARFALIIGEDELENGTVTLKDLE 395
|
410
....*....|
gi 15598997 406 DeGEQQSIAW 415
Cdd:TIGR00442 396 T-GEQETVPL 404
|
|
| syh |
CHL00201 |
histidine-tRNA synthetase; Provisional |
5-413 |
3.69e-134 |
|
histidine-tRNA synthetase; Provisional
Pssm-ID: 164576 [Multi-domain] Cd Length: 430 Bit Score: 392.34 E-value: 3.69e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 5 LQAIRGMNDILPEQTPAWRYLERTFAGLLDGYGYSEIRLPILEFTELFARGIGEGTDVVDKEMYTFLDRNGESLTMRPEG 84
Cdd:CHL00201 4 IQAIRGTKDILPDEINYWQFIHDKALTLLSLANYSEIRTPIFENSSLYDRGIGETTDIVNKEMYRFTDRSNRDITLRPEG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 85 TAGCVRAVLEHGLSGGGQVQKLWYTGPMFRYEKPQKGRYRQFHQIGVEVFNLPGPDIDAELIILTWRLWQKLGMADaVTL 164
Cdd:CHL00201 84 TAGIVRAFIENKMDYHSNLQRLWYSGPMFRYERPQSGRQRQFHQLGIEFIGSIDARADTEVIHLAMQIFNELQVKN-LIL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 165 QLNTLGSSEARARYREALVAYLQERFEQLDEDSQRRMTTNPLRILDSKVESTQALLVGAPTLHDYLDEESIAHFEGLKAR 244
Cdd:CHL00201 163 DINSIGKLEDRQSYQLKLVEYLSQYQDDLDTDSQNRLYSNPIRILDSKNLKTQEILDGAPKISDFLSLESTEHFYDVCTY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 245 LDAVGLRYEINQKLVRGLDYYCRTAFEWVTDKLGAQGTVCGGGRYDGLVSQFGGKPTPGVGFAMGVERLVLLLETLGVIP 324
Cdd:CHL00201 243 LNLLNIPYKINYKLVRGLDYYNDTAFEIKTLSSNGQDTICGGGRYDSLIHQLGGPKTPAVGCAIGLERLLLIAKDNIILP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 325 aelNRPADLYVCAFGEPAELAALTLAEQLRSAIpgIRLLVNAGAGSFKSQFKKADKSGARFALILGEDEVANRVVGFKPL 404
Cdd:CHL00201 323 ---KQSIDVYIATQGLKAQKKGWEIIQFLEKQN--IKFELDLSSSNFHKQIKQAGKKRAKACIILGDNEIMDNCITIKWL 397
|
....*....
gi 15598997 405 rDEGEQQSI 413
Cdd:CHL00201 398 -DEQVQENA 405
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
22-318 |
1.91e-96 |
|
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. It is responsible for the attachment of histidine to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs. This domain is also found at the C-terminus of eukaryotic GCN2 protein kinase and at the N-terminus of the ATP phosphoribosyltransferase accessory subunit, HisZ. HisZ along with HisG catalyze the first reaction in histidine biosynthesis. HisZ is found only in a subset of bacteria and differs from HisRS in lacking a C-terminal anti-codon binding domain.
Pssm-ID: 238396 [Multi-domain] Cd Length: 261 Bit Score: 289.89 E-value: 1.91e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 22 WRYLERTFAGLLDGYGYSEIRLPILEFTELFARGIGegtDVVDKEMYTFLDRNGESLTMRPEGTAGCVRAVLEHGLSGGg 101
Cdd:cd00773 5 RRYIEDTLREVFERYGYEEIDTPVFEYTELFLRKSG---DEVSKEMYRFKDKGGRDLALRPDLTAPVARAVAENLLSLP- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 102 QVQKLWYTGPMFRYEKPQKGRYRQFHQIGVEVFNLPGPDIDAELIILTWRLWQKLGMADaVTLQLNTLGSseararyrea 181
Cdd:cd00773 81 LPLKLYYIGPVFRYERPQKGRYREFYQVGVEIIGSDSPLADAEVIALAVEILEALGLKD-FQIKINHRGI---------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 182 lvayLQERFEQLDEDSQRRMttnplrildskvestqallvgapTLHDYLDEESIAHFEGLKARLDAVGL--RYEINQKLV 259
Cdd:cd00773 150 ----LDGIAGLLEDREEYIE-----------------------RLIDKLDKEALAHLEKLLDYLEALGVdiKYSIDLSLV 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 15598997 260 RGLDYYCRTAFEWVTDKLGAQGTVCGGGRYDGLVSQFGGKPTPGVGFAMGVERLVLLLE 318
Cdd:cd00773 203 RGLDYYTGIVFEAVADGLGAQGSIAGGGRYDGLLEEFGGEDVPAVGFAIGLERLLLALE 261
|
|
| hisZ_biosyn_reg |
TIGR00443 |
ATP phosphoribosyltransferase, regulatory subunit; Apparant second copies of histidyl-tRNA ... |
13-318 |
4.71e-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: 169.33 E-value: 4.71e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 13 DILPEQTPAWRYLERTFAGLLDGYGYSEIRLPILEFTELFARGIGEGtdvvDKEMYTFLDRNGESLTMRPEGTAGCVRAV 92
Cdd:TIGR00443 2 DLLPEEAARKEEIERQLQDVFRSWGYQEIITPTLEYLDTLSAGSGIL----NEDLFKLFDQLGRVLGLRPDMTAPIARLV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 93 LEHgLSGGGQVQKLWYTGPMFRYEKPQKGRYRQFHQIGVEVFNLPGPDIDAELIILTWRLWQKLGMADA---------VT 163
Cdd:TIGR00443 78 STR-LRDRPLPLRLCYAGNVFRTNESGGGRSREFTQAGVELIGAGGPAADAEVIALLIEALKALGLKDFkielghvglVR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 164 LQLNTLG-SSEARARYREALVAYLQERFEQL-------DEDSQRRMTTNPLRILDSKVESTQALLVGAPTLhdyldEESI 235
Cdd:TIGR00443 157 ALLEEAGlPEEAREALREALARKDLVALEELvaelglsPEVRERLLALPRLRGDGEEVLEEARALAGSETA-----EAAL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 236 AHFEGLKARLDAVGLRYEINQKL--VRGLDYYCRTAFEWVTDKLGAqgTVCGGGRYDGLVSQFgGKPTPGVGFAMGVERL 313
Cdd:TIGR00443 232 DELEAVLELLEARGVEEYISLDLglVRGYHYYTGLIFEGYAPGLGA--PLAGGGRYDELLGRF-GRPLPATGFALNLERL 308
|
....*
gi 15598997 314 VLLLE 318
Cdd:TIGR00443 309 LEALT 313
|
|
| hisZ |
PRK12292 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
10-356 |
3.53e-43 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 237043 [Multi-domain] Cd Length: 391 Bit Score: 155.79 E-value: 3.53e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 10 GMNDILPEQTPAWRYLERTFAGLLDGYGYSEIRLPILEFTELFARGIGEGtdvVDKEMYTFLDR-NGESLTMRPEGTAGC 88
Cdd:PRK12292 8 GIRDLLPEEARKIEEIRRRLLDLFRRWGYEEVITPTLEYLDTLLAGGGAI---LDLRTFKLVDQlSGRTLGLRPDMTAQI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 89 VRAVlEHGLSGGGQVQKLWYTGPMFRYEKPQKGRYRQFHQIGVEVFNLPGPDIDAELIILTWRLWQKLGMADaVTLQL-- 166
Cdd:PRK12292 85 ARIA-ATRLANRPGPLRLCYAGNVFRAQERGLGRSREFLQSGVELIGDAGLEADAEVILLLLEALKALGLPN-FTLDLgh 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 167 ---------NTLGSSEARARYREAL----VAYLQERFEQLDEDSQRRmttnpLRIL-----DSKVESTQALLVGAPTLHD 228
Cdd:PRK12292 163 vglfralleAAGLSEELEEVLRRALankdYVALEELVLDLSEELRDA-----LLALprlrgGREVLEEARKLLPSLPIKR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 229 YLDE-ESIahFEGLKARLDAVGLRYEINqkLVRGLDYYCRTAFEWVTDKLGAQgtVCGGGRYDGLVSQFgGKPTPGVGFA 307
Cdd:PRK12292 238 ALDElEAL--AEALEKYGYGIPLSLDLG--LLRHLDYYTGIVFEGYVDGVGNP--IASGGRYDDLLGRF-GRARPATGFS 310
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 15598997 308 MGVERLVLLLetlgvIPAELNRPADLyVCAFGEPAELAALTLAEQLRSA 356
Cdd:PRK12292 311 LDLDRLLELQ-----LELPVEARKDL-VIAPDSEALAAALAAAQELRKK 353
|
|
| PLN02530 |
PLN02530 |
histidine-tRNA ligase |
4-418 |
1.69e-41 |
|
histidine-tRNA ligase
Pssm-ID: 178145 [Multi-domain] Cd Length: 487 Bit Score: 153.36 E-value: 1.69e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 4 SLQAIRGMNDILPEQTPAWRYLERTFAGLLDGYGYSEIRLPILEFTELFARGIGEgtDVVDkEMYTFLDRNGESLTMRPE 83
Cdd:PLN02530 69 DVNPPKGTRDFPPEDMRLRNWLFDHFREVSRLFGFEEVDAPVLESEELYIRKAGE--EITD-QLYNFEDKGGRRVALRPE 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 84 GTAGCVRAVLEHGlsgGGQVQKL-WYT-GPMFRYEKPQKGRYRQFHQIGVEVFNLPGPDIDAELIILTWRLWQKLGM-AD 160
Cdd:PLN02530 146 LTPSLARLVLQKG---KSLSLPLkWFAiGQCWRYERMTRGRRREHYQWNMDIIGVPGVEAEAELLAAIVTFFKRVGItSS 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 161 AVTLQLNTlgsseararyREALVAYLqERFEqLDEDSQRRMTTnplrILDS--KV--ESTQALL----VGAPTLHDYLDE 232
Cdd:PLN02530 223 DVGIKVSS----------RKVLQAVL-KSYG-IPEESFAPVCV----IVDKleKLprEEIEKELdtlgVSEEAIEGILDV 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 233 ESIAHFEGLKARL----DAVGlryEINQ------------------KLVRGLDYYCRTAFEWVtDKLGAQGTVCGGGRYD 290
Cdd:PLN02530 287 LSLKSLDDLEALLgadsEAVA---DLKQlfslaeaygyqdwlvfdaSVVRGLAYYTGIVFEGF-DRAGKLRAICGGGRYD 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 291 GLVSQFGGKPTPGVGFAMGVERLVLLLETLGVIPaELNRPADLYVCAFGEPAELAALTLAEQLRSAIPGIRLLVNagAGS 370
Cdd:PLN02530 363 RLLSTFGGEDTPACGFGFGDAVIVELLKEKGLLP-ELPHQVDDVVFALDEDLQGAAAGVASRLREKGRSVDLVLE--PKK 439
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 15598997 371 FKSQFKKADKSGARFALILGEDEVANRVVGFKPLRdEGEQQSIAWDAL 418
Cdd:PLN02530 440 LKWVFKHAERIGAKRLVLVGASEWERGMVRVKDLS-SGEQTEVKLDEL 486
|
|
| HisZ |
COG3705 |
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism]; |
15-318 |
3.90e-40 |
|
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism];
Pssm-ID: 442919 [Multi-domain] Cd Length: 312 Bit Score: 145.70 E-value: 3.90e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 15 LPEQTPAWRYLERTFAGLLDGYGYSEIRLPILEFTELFARGIGEgtdVVDKEMYTFLDRNGESLTMRPEGTAGCVRAVLe 94
Cdd:COG3705 1 LPEEAARKEELRRRLLDVFRSWGYELVEPPLLEYLDSLLTGSGA---DLDLQTFKLVDQLGRTLGLRPDMTPQVARIAA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 95 HGLSGGGQVQKLWYTGPMFRYEKPQKGRYRQFHQIGVEVFNLPGPDIDAELIILTWRLWQKLGMADaVTLQLNTLG---- 170
Cdd:COG3705 77 TRLANRPGPLRLCYAGNVFRTRPSGLGRSREFLQAGAELIGHAGLEADAEVIALALEALKAAGLED-FTLDLGHVGlfra 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 171 -------SSEARARYREAL----VAYLQE--RFEQLDEDSQRRMTTNP-LRILDSKVESTQALLvgaptlhdyLDEESIA 236
Cdd:COG3705 156 llealglSEEQREELRRALarkdAVELEEllAELGLSEELAEALLALPeLYGGEEVLARARALL---------LDAAIRA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 237 HFEGLKARLDAVGLRYeINQKL------VRGLDYYCRTAFEWVTDKLGaqGTVCGGGRYDGLVSQFgGKPTPGVGFAMGV 310
Cdd:COG3705 227 ALDELEALAEALAARG-PDVRLtfdlseLRGYDYYTGIVFEAYAPGVG--DPLARGGRYDGLLAAF-GRARPATGFSLDL 302
|
....*...
gi 15598997 311 ERLVLLLE 318
Cdd:COG3705 303 DRLLRALP 310
|
|
| tRNA-synt_His |
pfam13393 |
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ... |
10-313 |
2.91e-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: 140.41 E-value: 2.91e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 10 GMNDILPEQTPAWRYLERTFAGLLDGYGYSEIRLPILEFTELFARGIGEGTDvvdkEMYTFLDRNGESLTMRPEGTAGCV 89
Cdd:pfam13393 1 GIRDLLPPEARRIEELRRRLLDLFRSWGYELVMPPLLEYLDSLLTGTGADLD----QTFKLVDQSGRLLGLRADITPQVA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 90 RAVlEHGLSGGGqVQKLWYTGPMFRYEKPQKGRYRQFHQIGVEVFNLPGPDIDAELIIL-----------TWRLwqKLGM 158
Cdd:pfam13393 77 RID-AHRLNRPG-PLRLCYAGSVLRTRPKGLGRSREPLQVGAELIGHAGIEADAEIISLllealaaagvpGVTL--DLGH 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 159 ADAVTLQLNTLGSSEA-RARYREAL----VAYLQERFEQLDEDSQRRMTTNPLRIL---DSKVESTQALLVGAPTLHDYL 230
Cdd:pfam13393 153 VGLVRALLEAAGLSEAlEEALRAALqrkdAAELAELAAEAGLPPALRRALLALPDLyggPEVLDEARAALPGLPALQEAL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 231 DEesiahFEGLKARLDAVG--LRYEINQKLVRGLDYYCRTAFEWVTDklGAQGTVCGGGRYDGLVSQFgGKPTPGVGFAM 308
Cdd:pfam13393 233 DE-----LEALAALLEALGdgVRLTFDLAELRGYEYYTGIVFAAYAP--GVGEPLARGGRYDDLGAAF-GRARPATGFSL 304
|
....*
gi 15598997 309 GVERL 313
Cdd:pfam13393 305 DLEAL 309
|
|
| PRK12420 |
PRK12420 |
histidyl-tRNA synthetase; Provisional |
5-413 |
2.87e-36 |
|
histidyl-tRNA synthetase; Provisional
Pssm-ID: 237097 [Multi-domain] Cd Length: 423 Bit Score: 137.94 E-value: 2.87e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 5 LQAIRGMNDILPEQTPAWRYLERTFAGLLDGYGYSEIRLPILEFTELFARGIGEGTDVVdKEMYTFLDRNGESLTMRPEG 84
Cdd:PRK12420 4 MRNVKGTKDYLPEEQVLRNKIKRALEDVFERYGCKPLETPTLNMYELMSSKYGGGDEIL-KEIYTLTDQGKRDLALRYDL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 85 TAGCVRAV-LEHGLSgggQVQKLWYTGPMFRYEKPQKGRYRQFHQIGVEVFNLPGPDIDAELIILTWRLWQKLGMAdaVT 163
Cdd:PRK12420 83 TIPFAKVVaMNPNIR---LPFKRYEIGKVFRDGPIKQGRFREFIQCDVDIVGVESVMAEAELMSMAFELFRRLNLE--VT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 164 LQLN-------TLGSSEARARYREALVAYLQE---------RFEQLDEDSQRRMTTNPLRILDSKVESTQALLVGAPTlh 227
Cdd:PRK12420 158 IQYNnrkllngILQAIGIPTELTSDVILSLDKiekigidgvRKDLLERGISEEMADTICNTVLSCLQLSIADFKEAFN-- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 228 DYLDEESIAHFEGLKARLDAVGLRYEI--NQKLVRGLDYYCRTAFEwVTDKLGA-QGTVCGGGRYDGLVSQFGGK--PTP 302
Cdd:PRK12420 236 NPLVAEGVNELQQLQQYLIALGINENCifNPFLARGLTMYTGTVYE-IFLKDGSiTSSIGSGGRYDNIIGAFRGDdmNYP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 303 GVGFAMGVERLVLLLETLGVIpaelNRPADLYVCAFGEPAElaALTLAEQLRSAiPGIRLLVNAGAGSFKSQFKKADKSG 382
Cdd:PRK12420 315 TVGISFGLDVIYTALSQKETI----SSTADVFIIPLGTELQ--CLQIAQQLRST-TGLKVELELAGRKLKKALNYANKEN 387
|
410 420 430
....*....|....*....|....*....|.
gi 15598997 383 ARFALILGEDEVANRVVGFKPLRdEGEQQSI 413
Cdd:PRK12420 388 IPYVLIIGEEEVSTGTVMLRNMK-EGSEVKV 417
|
|
| Gly_His_Pro_Ser_Thr_tRS_core |
cd00670 |
Gly_His_Pro_Ser_Thr_tRNA synthetase class II core domain. This domain is the core catalytic ... |
22-203 |
1.42e-30 |
|
Gly_His_Pro_Ser_Thr_tRNA synthetase class II core domain. This domain is the core catalytic domain of tRNA synthetases of the subgroup containing glycyl, histidyl, prolyl, seryl and threonyl tRNA synthetases. It is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. These enzymes belong to class II aminoacyl-tRNA synthetases (aaRS) based upon their structure and the presence of three characteristic sequence motifs in the core domain. 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 and the accessory subunit of mitochondrial polymerase gamma (Pol gamma b) . Most class II tRNA synthetases are dimers, with this subgroup consisting of mostly homodimers. These enzymes attach a specific amino acid to the 3' OH group of ribose of the appropriate tRNA.
Pssm-ID: 238359 [Multi-domain] Cd Length: 235 Bit Score: 117.49 E-value: 1.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 22 WRYLERTFAGLLDGYGYSEIRLPILEFTELFARGIGegTDVVDKEMYTFLDRNGE----SLTMRPEGTAGCVRAVLEHGL 97
Cdd:cd00670 5 WRALERFLDDRMAEYGYQEILFPFLAPTVLFFKGGH--LDGYRKEMYTFEDKGRElrdtDLVLRPAACEPIYQIFSGEIL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 98 SGGGQVQKLWYTGPMFRYEKPQ---KGRYRQFHQIGVEVFNLPG--PDIDAELIILTWRLWQKLGMadAVTLQLNTLGSS 172
Cdd:cd00670 83 SYRALPLRLDQIGPCFRHEPSGrrgLMRVREFRQVEYVVFGEPEeaEEERREWLELAEEIARELGL--PVRVVVADDPFF 160
|
170 180 190
....*....|....*....|....*....|.
gi 15598997 173 EARARYREALVAYLQERFEQLDEDSQRRMTT 203
Cdd:cd00670 161 GRGGKRGLDAGRETVVEFELLLPLPGRAKET 191
|
|
| HisRS_anticodon |
cd00859 |
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases ... |
330-423 |
2.03e-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: 2.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 330 PADLYVCAFGEPAELAALTLAEQLRSAipGIRLLVNAGAGSFKSQFKKADKSGARFALILGEDEVANRVVGFKPLRdEGE 409
Cdd:cd00859 1 EVDVYVVPLGEGALSEALELAEQLRDA--GIKAEIDYGGRKLKKQFKYADRSGARFAVILGEDELAAGVVTVKDLE-TGE 77
|
90
....*....|....
gi 15598997 410 QQSIAWDALPEHLA 423
Cdd:cd00859 78 QETVALDELVEELK 91
|
|
| PLN02972 |
PLN02972 |
Histidyl-tRNA synthetase |
9-411 |
3.20e-26 |
|
Histidyl-tRNA synthetase
Pssm-ID: 215525 [Multi-domain] Cd Length: 763 Bit Score: 111.52 E-value: 3.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 9 RGMNDILPEQTpAWRylERTFA---GLLDGYGYSEIRLPILEFTELFARGIGEGTdvvdKEMYTFLDRNGESLTMRPEGT 85
Cdd:PLN02972 331 KGTRDFAKEQM-AIR--EKAFSiitSVFKRHGATALDTPVFELRETLMGKYGEDS----KLIYDLADQGGELCSLRYDLT 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 86 AGCVRAVLEHGLSGggqvQKLWYTGPMFRYEKPQKGRYRQFHQIGVEVFNLPGP-DIDAELI-ILTWRLwqklgmadavt 163
Cdd:PLN02972 404 VPFARYVAMNGITS----FKRYQIAKVYRRDNPSKGRYREFYQCDFDIAGVYEPmGPDFEIIkVLTELL----------- 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 164 LQLNtLGSSEARARYREALVAYLQ------ERF-------EQLDEDS----QRRMTTN--------------------PL 206
Cdd:PLN02972 469 DELD-IGTYEVKLNHRKLLDGMLEicgvppEKFrticssiDKLDKQSfeqvKKEMVEEkglsnetadkignfvkergpPL 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 207 RILdSKVESTQALLVGAPTLHDYLDEESIAhFEGLKaRLDAVGlRYEINQKLVRGLDYYCRTAFEWVTdkLGAQ-GTVCG 285
Cdd:PLN02972 548 ELL-SKLRQEGSEFLGNASSRAALDELEIM-FKALE-KSKAIG-KIVFDLSLARGLDYYTGVIYEAVF--KGAQvGSIAA 621
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 286 GGRYDGLVSQFGGKPTPGVGFAMGVERLVLLLETLGVIPAELNRPAD--LYVCAFGEPAELAALTLAEQLRSAIPGIRLL 363
Cdd:PLN02972 622 GGRYDNLVGMFSGKQVPAVGVSLGIERVFAIMEQQEEEKSQVIRPTEteVLVSIIGDDKLALAAELVSELWNAGIKAEYK 701
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 15598997 364 VNAgagSFKSQFKKADKSGARFALILGEDEVANRVVGFKPLRDEGEQQ 411
Cdd:PLN02972 702 VST---RKAKHLKRAKESGIPWMVLVGEKELSKGFVKLKNLEAGVEEE 746
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
22-174 |
7.73e-23 |
|
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: 95.65 E-value: 7.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 22 WRYLERTFAGLLDGYGYSEIRLPILEFTELFARGIGEGtdvvdKEMYTFLDRNGESLTMRPEGTAGCVRAVLEHGLSGGg 101
Cdd:cd00768 2 RSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGHEP-----KDLLPVGAENEEDLYLRPTLEPGLVRLFVSHIRKLP- 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598997 102 qvQKLWYTGPMFRYEKPQKG--RYRQFHQIGVEVFNLPGPD--IDAELIILTWRLWQKLGMADAVTLQLNTLGSSEA 174
Cdd:cd00768 76 --LRLAEIGPAFRNEGGRRGlrRVREFTQLEGEVFGEDGEEasEFEELIELTEELLRALGIKLDIVFVEKTPGEFSP 150
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
68-226 |
7.96e-22 |
|
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely threonyl-tRNA members.
Pssm-ID: 395469 [Multi-domain] Cd Length: 181 Bit Score: 92.09 E-value: 7.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 68 YTFLDRNGESLTMRPEGTAGCVRAVLEHGLSGGGQVQKLWYTGPMFRYEKP--QKG--RYRQFHQIGVEVFNLPG--PDI 141
Cdd:pfam00587 1 YKVEDENGDELALKPTNEPGHTLLFREEGLRSKDLPLKLAQFGTCFRHEASgdTRGliRVRQFHQDDAHIFHAPGqsPDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 142 DAELIILTWRLWQKLGMADAVTLQLNTLGSSEARARYR-----EALVAYLQERFEQLDEDSQ-RRMTtnpLRILDSKVES 215
Cdd:pfam00587 81 LEDYIKLIDRVYSRLGLEVRVVRLSNSDGSAFYGPKLDfevvfPSLGKQRQTGTIQNDGFRLpRRLG---IRYKDEDNES 157
|
170
....*....|.
gi 15598997 216 TQALLVGAPTL 226
Cdd:pfam00587 158 KFPYMIHRAGL 168
|
|
| hisZ |
PRK12295 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
37-313 |
1.30e-15 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 183413 [Multi-domain] Cd Length: 373 Bit Score: 77.67 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 37 GYSEIRLPILEFTELFARGIGEGtdvVDKEMYTFLDRNGESLTMRPEGTAGCVRAVLEhglSGGGQVQKLWYTGPMFRYe 116
Cdd:PRK12295 22 GAVRVDPPILQPAEPFLDLSGED---IRRRIFVTSDENGEELCLRPDFTIPVCRRHIA---TAGGEPARYAYLGEVFRQ- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 117 kpQKGRYRQFHQIGVEVFNLPGP-DIDAELIILTWRLWQKLGM------------------------------------- 158
Cdd:PRK12295 95 --RRDRASEFLQAGIESFGRADPaAADAEVLALALEALAALGPgdlevrlgdvglfaalvdalglppgwkrrllrhfgrp 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 159 ----ADAVTLQLNTLGSSEARARY------REALVAYLQE--------------------RF-EQLDEDSQRRMTTNPLR 207
Cdd:PRK12295 173 rsldALLARLAGPRVDPLDEHAGVlaaladEAAARALVEDlmsiagispvggrspaeiarRLlEKAALAAAARLPAEALA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 208 IL----------DSKVESTQALLVGAPtlhdyLD-EESIAHFEGLKARLDAVGL---RYEINQKLVRGLDYYCRTAFEwV 273
Cdd:PRK12295 253 VLerflaisgppDAALAALRALAADAG-----LDlDAALDRFEARLAALAARGIdleRLRFSASFGRPLDYYTGFVFE-I 326
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 15598997 274 TDKLGAQGTVCGGGRYDGLVSQFG-GKPTPGVGFAMGVERL 313
Cdd:PRK12295 327 RAAGNGDPPLAGGGRYDGLLTRLGaGEPIPAVGFSIWLDRL 367
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
332-420 |
6.87e-10 |
|
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: 55.67 E-value: 6.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 332 DLYVCAFGEPAELA---ALTLAEQLRSAipGIRLLVNAGAGSFKSQFKKADKSGARFALILGEDEVANRVVGFKPlRDEG 408
Cdd:pfam03129 1 QVVVIPLGEKAEELeeyAQKLAEELRAA--GIRVELDDRNESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRR-RDTG 77
|
90
....*....|..
gi 15598997 409 EQQSIAWDALPE 420
Cdd:pfam03129 78 EQETVSLDELVE 89
|
|
| HGTP_anticodon |
cd00738 |
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ... |
330-422 |
8.66e-07 |
|
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: 47.01 E-value: 8.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 330 PADLYVCAFGEPAELA---ALTLAEQLRSAipGIRLLVNAGAGSFKSQFKKADKSGARFALILGEDEVANRVVGFKpLRD 406
Cdd:cd00738 1 PIDVAIVPLTDPRVEAreyAQKLLNALLAN--GIRVLYDDRERKIGKKFREADLRGVPFAVVVGEDELENGKVTVK-SRD 77
|
90
....*....|....*.
gi 15598997 407 EGEQQSIAWDALPEHL 422
Cdd:cd00738 78 TGESETLHVDELPEFL 93
|
|
| hisZ |
PRK12293 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
23-166 |
2.92e-05 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 183411 Cd Length: 281 Bit Score: 45.37 E-value: 2.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598997 23 RYLERTFAGLLDGYGYSEIRLPILEFTELFArgigegtDVVDKEMYTFLDRNGESLTMRPEGTAGCVRAVLEHgLSGGGQ 102
Cdd:PRK12293 23 REIENVASEILYENGFEEIVTPFFSYHQHQS-------IADEKELIRFSDEKNHQISLRADSTLDVVRIVTKR-LGRSTE 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598997 103 VQKLWYTGPMFRYekPQkgryRQFHQIGVEVfnLPGPDIdAELIILTWRLWQKLGMADavTLQL 166
Cdd:PRK12293 95 HKKWFYIQPVFRY--PS----NEIYQIGAEL--IGEEDL-SEILNIAAEIFEELELEP--ILQI 147
|
|
| |
