|
Name |
Accession |
Description |
Interval |
E-value |
| hisZ |
PRK12292 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
3-390 |
7.30e-133 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 237043 [Multi-domain] Cd Length: 391 Bit Score: 386.14 E-value: 7.30e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502716242 3 LNKNLPTGTRDKLFREARAAYKIEQQVNHYFEKRGFKRIETPVIEFEDVFSSE--HQADAKLYRFFDE-KGRLTVLRPDM 79
Cdd:PRK12292 1 MMWQLPEGIRDLLPEEARKIEEIRRRLLDLFRRWGYEEVITPTLEYLDTLLAGggAILDLRTFKLVDQlSGRTLGLRPDM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502716242 80 TLPIGRVVSTT--GVMLPLKLSYSGKIFRANEDFGGEQNEQTQAGIEIIGYPSIKAEIECILIGIGVLNALEIPNFQIEL 157
Cdd:PRK12292 81 TAQIARIAATRlaNRPGPLRLCYAGNVFRAQERGLGRSREFLQSGVELIGDAGLEADAEVILLLLEALKALGLPNFTLDL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502716242 158 GHAAIYRRVTNLLNLSETAEIDFRLLIQNKSLTGIKRFVADNPSTLDDFILVLPRLFGPAtAILKQAKNLTTDKGILTAL 237
Cdd:PRK12292 161 GHVGLFRALLEAAGLSEELEEVLRRALANKDYVALEELVLDLSEELRDALLALPRLRGGR-EVLEEARKLLPSLPIKRAL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502716242 238 REMETIVEAVS---YTADISVDLGLVQDFHYYTGIIFRGYADLAADNFLSGGRYDHLLEQFTSAsSPAVGLALNLDSLTT 314
Cdd:PRK12292 240 DELEALAEALEkygYGIPLSLDLGLLRHLDYYTGIVFEGYVDGVGNPIASGGRYDDLLGRFGRA-RPATGFSLDLDRLLE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502716242 315 LQnraGVIKKQVSTSLLIHYDLDAIQQAEKLMQETPNS----ELSFF-ETPTNAISFAKKWHIpavihVSRQGIQTIFQR 389
Cdd:PRK12292 319 LQ---LELPVEARKDLVIAPDSEALAAALAAAQELRKKgeivVLALPgRNFEDAREYARDRQI-----VEADGEWQVEPL 390
|
.
gi 502716242 390 E 390
Cdd:PRK12292 391 A 391
|
|
| hisZ_biosyn_reg |
TIGR00443 |
ATP phosphoribosyltransferase, regulatory subunit; Apparant second copies of histidyl-tRNA ... |
12-317 |
1.74e-127 |
|
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: 369.25 E-value: 1.74e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502716242 12 RDKLFREARAAYKIEQQVNHYFEKRGFKRIETPVIEFEDVFSSEHQ-ADAKLYRFFDEKGRLTVLRPDMTLPIGRVVSTT 90
Cdd:TIGR00443 1 RDLLPEEAARKEEIERQLQDVFRSWGYQEIITPTLEYLDTLSAGSGiLNEDLFKLFDQLGRVLGLRPDMTAPIARLVSTR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502716242 91 --GVMLPLKLSYSGKIFRANEDFGGEQNEQTQAGIEIIGYPSIKAEIECILIGIGVLNALEIPNFQIELGHAAIYRRVTN 168
Cdd:TIGR00443 81 lrDRPLPLRLCYAGNVFRTNESGGGRSREFTQAGVELIGAGGPAADAEVIALLIEALKALGLKDFKIELGHVGLVRALLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502716242 169 LLNLSETAEIDFRLLIQNKSLTGIKRFVADNPST--LDDFILVLPRLFGPATAILKQAKNLTTDKGILTALREMET---I 243
Cdd:TIGR00443 161 EAGLPEEAREALREALARKDLVALEELVAELGLSpeVRERLLALPRLRGDGEEVLEEARALAGSETAEAALDELEAvleL 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502716242 244 VEAVSYTADISVDLGLVQDFHYYTGIIFRGYADLAADNFLSGGRYDHLLEQFtSASSPAVGLALNLDSLTTLQN 317
Cdd:TIGR00443 241 LEARGVEEYISLDLGLVRGYHYYTGLIFEGYAPGLGAPLAGGGRYDELLGRF-GRPLPATGFALNLERLLEALT 313
|
|
| HisZ |
COG3705 |
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism]; |
15-319 |
3.57e-102 |
|
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism];
Pssm-ID: 442919 [Multi-domain] Cd Length: 312 Bit Score: 304.79 E-value: 3.57e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502716242 15 LFREARAAYKIEQQVNHYFEKRGFKRIETPVIEFEDVFSSEHQAD--AKLYRFFDEKGRLTVLRPDMTLPIGRVVST--T 90
Cdd:COG3705 1 LPEEAARKEELRRRLLDVFRSWGYELVEPPLLEYLDSLLTGSGADldLQTFKLVDQLGRTLGLRPDMTPQVARIAATrlA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502716242 91 GVMLPLKLSYSGKIFRANEDFGGEQNEQTQAGIEIIGYPSIKAEIECILIGIGVLNALEIPNFQIELGHAAIYRRVTNLL 170
Cdd:COG3705 81 NRPGPLRLCYAGNVFRTRPSGLGRSREFLQAGAELIGHAGLEADAEVIALALEALKAAGLEDFTLDLGHVGLFRALLEAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502716242 171 NLSETAEIDFRLLIQNKSLTGIKRFVADN--PSTLDDFILVLPRLFGPATAiLKQAKNLTTDKGILTALREMETIVEAVS 248
Cdd:COG3705 161 GLSEEQREELRRALARKDAVELEELLAELglSEELAEALLALPELYGGEEV-LARARALLLDAAIRAALDELEALAEALA 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502716242 249 ---YTADISVDLGLVQDFHYYTGIIFRGYADLAADNFLSGGRYDHLLEQFtSASSPAVGLALNLDSLTTLQNRA 319
Cdd:COG3705 240 argPDVRLTFDLSELRGYDYYTGIVFEAYAPGVGDPLARGGRYDGLLAAF-GRARPATGFSLDLDRLLRALPAA 312
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
18-312 |
2.74e-79 |
|
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: 244.82 E-value: 2.74e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502716242 18 EARAAYKIEQQVNHYFEKRGFKRIETPVIEFEDVF--SSEHQADAKLYRFFDEKGRLTVLRPDMTLPIGRVVSTTGVML- 94
Cdd:cd00773 1 EAALRRYIEDTLREVFERYGYEEIDTPVFEYTELFlrKSGDEVSKEMYRFKDKGGRDLALRPDLTAPVARAVAENLLSLp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502716242 95 -PLKLSYSGKIFRANEDFGGEQNEQTQAGIEIIGYPSIKAEIECILIGIGVLNALEIPNFQIELGHAAIYRRVTNLLNLS 173
Cdd:cd00773 81 lPLKLYYIGPVFRYERPQKGRYREFYQVGVEIIGSDSPLADAEVIALAVEILEALGLKDFQIKINHRGILDGIAGLLEDR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502716242 174 ETAEIDFRLLIQNKSLTgikrfvadnpstlddfilvlprlfgpatailkqaknlttdkgiltALREMETIVEAVSYTADI 253
Cdd:cd00773 161 EEYIERLIDKLDKEALA---------------------------------------------HLEKLLDYLEALGVDIKY 195
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502716242 254 SVDLGLVQDFHYYTGIIFRGYAD--LAADNFLSGGRYDHLLEQFTSASSPAVGLALNLDSL 312
Cdd:cd00773 196 SIDLSLVRGLDYYTGIVFEAVADglGAQGSIAGGGRYDGLLEEFGGEDVPAVGFAIGLERL 256
|
|
| tRNA-synt_His |
pfam13393 |
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ... |
10-312 |
3.65e-72 |
|
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: 227.85 E-value: 3.65e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502716242 10 GTRDKLFREARAAYKIEQQVNHYFEKRGFKRIETPVIEFEDVFSSEHQADAK-LYRFFDEKGRLTVLRPDMTLPIGRVVS 88
Cdd:pfam13393 1 GIRDLLPPEARRIEELRRRLLDLFRSWGYELVMPPLLEYLDSLLTGTGADLDqTFKLVDQSGRLLGLRADITPQVARIDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502716242 89 TtgvML----PLKLSYSGKIFRANEDFGGEQNEQTQAGIEIIGYPSIKAEIECILIGIGVLNALEIPNFQIELGHAAIYR 164
Cdd:pfam13393 81 H---RLnrpgPLRLCYAGSVLRTRPKGLGRSREPLQVGAELIGHAGIEADAEIISLLLEALAAAGVPGVTLDLGHVGLVR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502716242 165 RVTNLLNLSETAEIDFRLLIQNKSLTGIKRFVADN--PSTLDDFILVLPRLFGPATAILKQAKNLTTDKGI---LTALRE 239
Cdd:pfam13393 158 ALLEAAGLSEALEEALRAALQRKDAAELAELAAEAglPPALRRALLALPDLYGGPEVLDEARAALPGLPALqeaLDELEA 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502716242 240 METIVEAVSYTADISVDLGLVQDFHYYTGIIFRGYADLAADNFLSGGRYDHLLEQFTSAsSPAVGLALNLDSL 312
Cdd:pfam13393 238 LAALLEALGDGVRLTFDLAELRGYEYYTGIVFAAYAPGVGEPLARGGRYDDLGAAFGRA-RPATGFSLDLEAL 309
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| hisZ |
PRK12292 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
3-390 |
7.30e-133 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 237043 [Multi-domain] Cd Length: 391 Bit Score: 386.14 E-value: 7.30e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502716242 3 LNKNLPTGTRDKLFREARAAYKIEQQVNHYFEKRGFKRIETPVIEFEDVFSSE--HQADAKLYRFFDE-KGRLTVLRPDM 79
Cdd:PRK12292 1 MMWQLPEGIRDLLPEEARKIEEIRRRLLDLFRRWGYEEVITPTLEYLDTLLAGggAILDLRTFKLVDQlSGRTLGLRPDM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502716242 80 TLPIGRVVSTT--GVMLPLKLSYSGKIFRANEDFGGEQNEQTQAGIEIIGYPSIKAEIECILIGIGVLNALEIPNFQIEL 157
Cdd:PRK12292 81 TAQIARIAATRlaNRPGPLRLCYAGNVFRAQERGLGRSREFLQSGVELIGDAGLEADAEVILLLLEALKALGLPNFTLDL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502716242 158 GHAAIYRRVTNLLNLSETAEIDFRLLIQNKSLTGIKRFVADNPSTLDDFILVLPRLFGPAtAILKQAKNLTTDKGILTAL 237
Cdd:PRK12292 161 GHVGLFRALLEAAGLSEELEEVLRRALANKDYVALEELVLDLSEELRDALLALPRLRGGR-EVLEEARKLLPSLPIKRAL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502716242 238 REMETIVEAVS---YTADISVDLGLVQDFHYYTGIIFRGYADLAADNFLSGGRYDHLLEQFTSAsSPAVGLALNLDSLTT 314
Cdd:PRK12292 240 DELEALAEALEkygYGIPLSLDLGLLRHLDYYTGIVFEGYVDGVGNPIASGGRYDDLLGRFGRA-RPATGFSLDLDRLLE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502716242 315 LQnraGVIKKQVSTSLLIHYDLDAIQQAEKLMQETPNS----ELSFF-ETPTNAISFAKKWHIpavihVSRQGIQTIFQR 389
Cdd:PRK12292 319 LQ---LELPVEARKDLVIAPDSEALAAALAAAQELRKKgeivVLALPgRNFEDAREYARDRQI-----VEADGEWQVEPL 390
|
.
gi 502716242 390 E 390
Cdd:PRK12292 391 A 391
|
|
| hisZ_biosyn_reg |
TIGR00443 |
ATP phosphoribosyltransferase, regulatory subunit; Apparant second copies of histidyl-tRNA ... |
12-317 |
1.74e-127 |
|
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: 369.25 E-value: 1.74e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502716242 12 RDKLFREARAAYKIEQQVNHYFEKRGFKRIETPVIEFEDVFSSEHQ-ADAKLYRFFDEKGRLTVLRPDMTLPIGRVVSTT 90
Cdd:TIGR00443 1 RDLLPEEAARKEEIERQLQDVFRSWGYQEIITPTLEYLDTLSAGSGiLNEDLFKLFDQLGRVLGLRPDMTAPIARLVSTR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502716242 91 --GVMLPLKLSYSGKIFRANEDFGGEQNEQTQAGIEIIGYPSIKAEIECILIGIGVLNALEIPNFQIELGHAAIYRRVTN 168
Cdd:TIGR00443 81 lrDRPLPLRLCYAGNVFRTNESGGGRSREFTQAGVELIGAGGPAADAEVIALLIEALKALGLKDFKIELGHVGLVRALLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502716242 169 LLNLSETAEIDFRLLIQNKSLTGIKRFVADNPST--LDDFILVLPRLFGPATAILKQAKNLTTDKGILTALREMET---I 243
Cdd:TIGR00443 161 EAGLPEEAREALREALARKDLVALEELVAELGLSpeVRERLLALPRLRGDGEEVLEEARALAGSETAEAALDELEAvleL 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502716242 244 VEAVSYTADISVDLGLVQDFHYYTGIIFRGYADLAADNFLSGGRYDHLLEQFtSASSPAVGLALNLDSLTTLQN 317
Cdd:TIGR00443 241 LEARGVEEYISLDLGLVRGYHYYTGLIFEGYAPGLGAPLAGGGRYDELLGRF-GRPLPATGFALNLERLLEALT 313
|
|
| HisZ |
COG3705 |
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism]; |
15-319 |
3.57e-102 |
|
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism];
Pssm-ID: 442919 [Multi-domain] Cd Length: 312 Bit Score: 304.79 E-value: 3.57e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502716242 15 LFREARAAYKIEQQVNHYFEKRGFKRIETPVIEFEDVFSSEHQAD--AKLYRFFDEKGRLTVLRPDMTLPIGRVVST--T 90
Cdd:COG3705 1 LPEEAARKEELRRRLLDVFRSWGYELVEPPLLEYLDSLLTGSGADldLQTFKLVDQLGRTLGLRPDMTPQVARIAATrlA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502716242 91 GVMLPLKLSYSGKIFRANEDFGGEQNEQTQAGIEIIGYPSIKAEIECILIGIGVLNALEIPNFQIELGHAAIYRRVTNLL 170
Cdd:COG3705 81 NRPGPLRLCYAGNVFRTRPSGLGRSREFLQAGAELIGHAGLEADAEVIALALEALKAAGLEDFTLDLGHVGLFRALLEAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502716242 171 NLSETAEIDFRLLIQNKSLTGIKRFVADN--PSTLDDFILVLPRLFGPATAiLKQAKNLTTDKGILTALREMETIVEAVS 248
Cdd:COG3705 161 GLSEEQREELRRALARKDAVELEELLAELglSEELAEALLALPELYGGEEV-LARARALLLDAAIRAALDELEALAEALA 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502716242 249 ---YTADISVDLGLVQDFHYYTGIIFRGYADLAADNFLSGGRYDHLLEQFtSASSPAVGLALNLDSLTTLQNRA 319
Cdd:COG3705 240 argPDVRLTFDLSELRGYDYYTGIVFEAYAPGVGDPLARGGRYDGLLAAF-GRARPATGFSLDLDRLLRALPAA 312
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
18-312 |
2.74e-79 |
|
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: 244.82 E-value: 2.74e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502716242 18 EARAAYKIEQQVNHYFEKRGFKRIETPVIEFEDVF--SSEHQADAKLYRFFDEKGRLTVLRPDMTLPIGRVVSTTGVML- 94
Cdd:cd00773 1 EAALRRYIEDTLREVFERYGYEEIDTPVFEYTELFlrKSGDEVSKEMYRFKDKGGRDLALRPDLTAPVARAVAENLLSLp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502716242 95 -PLKLSYSGKIFRANEDFGGEQNEQTQAGIEIIGYPSIKAEIECILIGIGVLNALEIPNFQIELGHAAIYRRVTNLLNLS 173
Cdd:cd00773 81 lPLKLYYIGPVFRYERPQKGRYREFYQVGVEIIGSDSPLADAEVIALAVEILEALGLKDFQIKINHRGILDGIAGLLEDR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502716242 174 ETAEIDFRLLIQNKSLTgikrfvadnpstlddfilvlprlfgpatailkqaknlttdkgiltALREMETIVEAVSYTADI 253
Cdd:cd00773 161 EEYIERLIDKLDKEALA---------------------------------------------HLEKLLDYLEALGVDIKY 195
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502716242 254 SVDLGLVQDFHYYTGIIFRGYAD--LAADNFLSGGRYDHLLEQFTSASSPAVGLALNLDSL 312
Cdd:cd00773 196 SIDLSLVRGLDYYTGIVFEAVADglGAQGSIAGGGRYDGLLEEFGGEDVPAVGFAIGLERL 256
|
|
| tRNA-synt_His |
pfam13393 |
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ... |
10-312 |
3.65e-72 |
|
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: 227.85 E-value: 3.65e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502716242 10 GTRDKLFREARAAYKIEQQVNHYFEKRGFKRIETPVIEFEDVFSSEHQADAK-LYRFFDEKGRLTVLRPDMTLPIGRVVS 88
Cdd:pfam13393 1 GIRDLLPPEARRIEELRRRLLDLFRSWGYELVMPPLLEYLDSLLTGTGADLDqTFKLVDQSGRLLGLRADITPQVARIDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502716242 89 TtgvML----PLKLSYSGKIFRANEDFGGEQNEQTQAGIEIIGYPSIKAEIECILIGIGVLNALEIPNFQIELGHAAIYR 164
Cdd:pfam13393 81 H---RLnrpgPLRLCYAGSVLRTRPKGLGRSREPLQVGAELIGHAGIEADAEIISLLLEALAAAGVPGVTLDLGHVGLVR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502716242 165 RVTNLLNLSETAEIDFRLLIQNKSLTGIKRFVADN--PSTLDDFILVLPRLFGPATAILKQAKNLTTDKGI---LTALRE 239
Cdd:pfam13393 158 ALLEAAGLSEALEEALRAALQRKDAAELAELAAEAglPPALRRALLALPDLYGGPEVLDEARAALPGLPALqeaLDELEA 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502716242 240 METIVEAVSYTADISVDLGLVQDFHYYTGIIFRGYADLAADNFLSGGRYDHLLEQFTSAsSPAVGLALNLDSL 312
Cdd:pfam13393 238 LAALLEALGDGVRLTFDLAELRGYEYYTGIVFAAYAPGVGEPLARGGRYDDLGAAFGRA-RPATGFSLDLEAL 309
|
|
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
6-348 |
1.53e-45 |
|
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: 161.83 E-value: 1.53e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502716242 6 NLPTGTRDKLFREARAAYKIEQQVNHYFEKRGFKRIETPVIEFEDVF---SSEHQADAKLYRFFDEKGRLTVLRPDMTLP 82
Cdd:COG0124 5 QAPRGTRDILPEESAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFarkIGEDIVEKEMYTFEDRGGRSLTLRPEGTAP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502716242 83 IGRVVSTTGVML--PLKLSYSGKIFRAnedfggeqnEQ---------TQAGIEIIGYPSIKAEIECILIGIGVLNALEIP 151
Cdd:COG0124 85 VARAVAEHGNELpfPFKLYYIGPVFRY---------ERpqkgryrqfHQFGVEVIGSDSPLADAEVIALAADLLKALGLK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502716242 152 NFQIELGHaaiyrrvtnlLNLSETAEIDFRLLIQNKSLTGIKRFVAD--------NPstlddfILVLPRLFGPAT-AILK 222
Cdd:COG0124 156 DFTLEINS----------RGLPEERAEALLRYLDKLDKIGHEDVLDEdsqrrletNP------LRAILDSKGPDCqEVLA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502716242 223 QAKNLtTDKGILTALREMETIVEAV-SYTADISVDLGLVQDFHYYTGIIFRGYAD-LAADN-FLSGGRYDHLLEQFTSAS 299
Cdd:COG0124 220 DAPKL-LDYLGEEGLAHFEEVLELLdALGIPYVIDPRLVRGLDYYTGTVFEIVTDgLGAQGsVCGGGRYDGLVEQLGGPP 298
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 502716242 300 SPAVGLALNLDSLTTLQNRAGVIKKQVSTS--LLIHYDLDAIQQAEKLMQE 348
Cdd:COG0124 299 TPAVGFAIGLERLLLLLEELGLLPAAEPPPdvYVVPLGEEARAEALKLAQE 349
|
|
| PRK12421 |
PRK12421 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
7-316 |
5.89e-37 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 237098 Cd Length: 392 Bit Score: 138.18 E-value: 5.89e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502716242 7 LPTGTRDKLFREARAAYKIEQQVNHYFEKRGFKRIETPVIEFEDVFSSEHQADAKL--YRFFDE-KGRLTVLRPDMTLPI 83
Cdd:PRK12421 9 LPDGVADVLPEEAQKIERLRRRLLDLFASRGYQLVMPPLIEYLESLLTGAGQDLKLqtFKLIDQlSGRLMGVRADITPQV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502716242 84 GRVVS-TTGVMLPLKLSYSGKIFRANED-FGGEQNEqTQAGIEIIGYPSIKAEIECILIGIGVLNALEIPNFQIELGHAA 161
Cdd:PRK12421 89 ARIDAhLLNREGVARLCYAGSVLHTLPQgLFGSRTP-LQLGAELYGHAGIEADLEIIRLMLGLLRNAGVPALHLDLGHVG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502716242 162 IYRRVTNLLNLSETAEIDFRLLIQNKSLTGIKRFVADNP--STLDDFILVLPRLFGPATAIL-KQAKNLTTDKGILTALR 238
Cdd:PRK12421 168 IFRRLAELAGLSPEEEEELFDLLQRKALPELAEVCQNLGvgSDLRRMFYALARLNGGLEALDrALSVLALQDAAIRQALD 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502716242 239 EMETIVEAVSYTAD---ISVDLGLVQDFHYYTGIIFRGYADLAADNFLSGGRYDHLLEQFTSAsSPAVGLALNLDSLTTL 315
Cdd:PRK12421 248 ELKTLAAHLKNRWPelpVSIDLAELRGYHYHTGLVFAAYIPGRGQALARGGRYDGIGEAFGRA-RPATGFSMDLKELLAL 326
|
.
gi 502716242 316 Q 316
Cdd:PRK12421 327 Q 327
|
|
| PLN02972 |
PLN02972 |
Histidyl-tRNA synthetase |
7-384 |
7.15e-23 |
|
Histidyl-tRNA synthetase
Pssm-ID: 215525 [Multi-domain] Cd Length: 763 Bit Score: 100.73 E-value: 7.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502716242 7 LPTGTRDkLFREARA----AYKIEQQVnhyFEKRGFKRIETPVIEFEDVFSSEHQADAKL-YRFFDEKGRLTVLRPDMTL 81
Cdd:PLN02972 329 IPKGTRD-FAKEQMAirekAFSIITSV---FKRHGATALDTPVFELRETLMGKYGEDSKLiYDLADQGGELCSLRYDLTV 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502716242 82 PIGRVVSTTGVMlPLKLSYSGKIFRANEDFGGEQNEQTQAGIEIIG-YPSIKAEIECILIGIGVLNALEIPNFQIELGHA 160
Cdd:PLN02972 405 PFARYVAMNGIT-SFKRYQIAKVYRRDNPSKGRYREFYQCDFDIAGvYEPMGPDFEIIKVLTELLDELDIGTYEVKLNHR 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502716242 161 AIyrrVTNLLNLSETAEIDFRLL------IQNKSLTGIKRFVADN---PSTLDDFILVLPRLFGPATAILKQAKN----L 227
Cdd:PLN02972 484 KL---LDGMLEICGVPPEKFRTIcssidkLDKQSFEQVKKEMVEEkglSNETADKIGNFVKERGPPLELLSKLRQegseF 560
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502716242 228 TTDKGILTALREMETIVEAVSYTA---DISVDLGLVQDFHYYTGIIFRGYADLA-ADNFLSGGRYDHLLEQFTSASSPAV 303
Cdd:PLN02972 561 LGNASSRAALDELEIMFKALEKSKaigKIVFDLSLARGLDYYTGVIYEAVFKGAqVGSIAAGGRYDNLVGMFSGKQVPAV 640
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502716242 304 GLALNLDSLTT----LQNRAGVIKKQVSTSLLIHYDLDAIQ-QAEKLMQETPNSELSFFETPT----NAISFAKKWHIPA 374
Cdd:PLN02972 641 GVSLGIERVFAimeqQEEEKSQVIRPTETEVLVSIIGDDKLaLAAELVSELWNAGIKAEYKVStrkaKHLKRAKESGIPW 720
|
410
....*....|
gi 502716242 375 VIHVSRQGIQ 384
Cdd:PLN02972 721 MVLVGEKELS 730
|
|
| hisZ |
PRK12295 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
33-315 |
6.27e-18 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 183413 [Multi-domain] Cd Length: 373 Bit Score: 84.21 E-value: 6.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502716242 33 FEKRGFKRIETPVIEFEDVF---SSEhqaD--AKLYRFFDEKGRLTVLRPDMTLPIGRVVSTTGVMLPLKLSYSGKIFRA 107
Cdd:PRK12295 18 FEAAGAVRVDPPILQPAEPFldlSGE---DirRRIFVTSDENGEELCLRPDFTIPVCRRHIATAGGEPARYAYLGEVFRQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502716242 108 NedfGGEQNEQTQAGIEIIGYPSI-KAEIECILIGIGVLNALEIPNFQIELGHAAIYRRVTNLLNLSE------------ 174
Cdd:PRK12295 95 R---RDRASEFLQAGIESFGRADPaAADAEVLALALEALAALGPGDLEVRLGDVGLFAALVDALGLPPgwkrrllrhfgr 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502716242 175 -------------------------------------------------------TAEIDFRLLIQnKSLTGIKRFVADN 199
Cdd:PRK12295 172 prsldallarlagprvdpldehagvlaaladeaaaralvedlmsiagispvggrsPAEIARRLLEK-AALAAAARLPAEA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502716242 200 PSTLDDFIlvlpRLFGPATAILKQAKNLTTDKG--ILTALREMETIVEAVsytADISVDLGLV-------QDFHYYTGII 270
Cdd:PRK12295 251 LAVLERFL----AISGPPDAALAALRALAADAGldLDAALDRFEARLAAL---AARGIDLERLrfsasfgRPLDYYTGFV 323
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 502716242 271 FRGY-ADLAADNFLSGGRYDHLLEQFTSASS-PAVGLALNLDSLTTL 315
Cdd:PRK12295 324 FEIRaAGNGDPPLAGGGRYDGLLTRLGAGEPiPAVGFSIWLDRLAAL 370
|
|
| PRK12420 |
PRK12420 |
histidyl-tRNA synthetase; Provisional |
10-318 |
1.42e-16 |
|
histidyl-tRNA synthetase; Provisional
Pssm-ID: 237097 [Multi-domain] Cd Length: 423 Bit Score: 80.93 E-value: 1.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502716242 10 GTRDKLFREARAAYKIEQQVNHYFEKRGFKRIETPVIEFEDVFSSEHQADA----KLYRFFDEKGRLTVLRPDMTLPIGR 85
Cdd:PRK12420 9 GTKDYLPEEQVLRNKIKRALEDVFERYGCKPLETPTLNMYELMSSKYGGGDeilkEIYTLTDQGKRDLALRYDLTIPFAK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502716242 86 VVSTT-GVMLPLKLSYSGKIFRANEDFGGEQNEQTQAGIEIIGYPSIKAEIECILIGIGVLNALEIPnfqielghaaIYR 164
Cdd:PRK12420 89 VVAMNpNIRLPFKRYEIGKVFRDGPIKQGRFREFIQCDVDIVGVESVMAEAELMSMAFELFRRLNLE----------VTI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502716242 165 RVTNLLNLSETAEI---------DFRLL---IQNKSLTGIKRFVAD---NPSTLDDFI-LVLPRLFGPATAILKQAKNLT 228
Cdd:PRK12420 159 QYNNRKLLNGILQAigipteltsDVILSldkIEKIGIDGVRKDLLErgiSEEMADTICnTVLSCLQLSIADFKEAFNNPL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502716242 229 TDKGIlTALREMETIVEAVSYTADISVDLGLVQDFHYYTGIIFRGY-ADLA-ADNFLSGGRYDHLLEQFTSASS--PAVG 304
Cdd:PRK12420 239 VAEGV-NELQQLQQYLIALGINENCIFNPFLARGLTMYTGTVYEIFlKDGSiTSSIGSGGRYDNIIGAFRGDDMnyPTVG 317
|
330
....*....|....*
gi 502716242 305 LALNLDSLTT-LQNR 318
Cdd:PRK12420 318 ISFGLDVIYTaLSQK 332
|
|
| syh |
CHL00201 |
histidine-tRNA synthetase; Provisional |
10-312 |
8.80e-16 |
|
histidine-tRNA synthetase; Provisional
Pssm-ID: 164576 [Multi-domain] Cd Length: 430 Bit Score: 78.40 E-value: 8.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502716242 10 GTRDKLFREARAAYKIEQQVNHYFEKRGFKRIETPVIEFEDVFSSEHQADA-----KLYRFFDEKGRLTVLRPDMTLPIG 84
Cdd:CHL00201 9 GTKDILPDEINYWQFIHDKALTLLSLANYSEIRTPIFENSSLYDRGIGETTdivnkEMYRFTDRSNRDITLRPEGTAGIV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502716242 85 RVVSTTGVMLP---LKLSYSGKIFRANEDFGGEQNEQTQAGIEIIGYPSIKAEIECILIGIGVLNALEIPNFQIELGH-A 160
Cdd:CHL00201 89 RAFIENKMDYHsnlQRLWYSGPMFRYERPQSGRQRQFHQLGIEFIGSIDARADTEVIHLAMQIFNELQVKNLILDINSiG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502716242 161 AIYRRVTNLLNLSETAEIDFRLLIQNKsltgiKRFVADNPSTLDDfilvlprlfgpatailkqAKNLTTDKgILT----- 235
Cdd:CHL00201 169 KLEDRQSYQLKLVEYLSQYQDDLDTDS-----QNRLYSNPIRILD------------------SKNLKTQE-ILDgapki 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502716242 236 ----ALREMETIVEAVSYTADISV----DLGLVQDFHYYTGIIF--RGYADLAADNFLSGGRYDHLLEQFTSASSPAVGL 305
Cdd:CHL00201 225 sdflSLESTEHFYDVCTYLNLLNIpykiNYKLVRGLDYYNDTAFeiKTLSSNGQDTICGGGRYDSLIHQLGGPKTPAVGC 304
|
....*..
gi 502716242 306 ALNLDSL 312
Cdd:CHL00201 305 AIGLERL 311
|
|
| PLN02530 |
PLN02530 |
histidine-tRNA ligase |
6-304 |
1.50e-15 |
|
histidine-tRNA ligase
Pssm-ID: 178145 [Multi-domain] Cd Length: 487 Bit Score: 77.86 E-value: 1.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502716242 6 NLPTGTRD------KL-------FREARAAYkieqqvnhyfekrGFKRIETPVIEFEDVF---SSEHQADaKLYRFFDEK 69
Cdd:PLN02530 71 NPPKGTRDfppedmRLrnwlfdhFREVSRLF-------------GFEEVDAPVLESEELYirkAGEEITD-QLYNFEDKG 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502716242 70 GRLTVLRPDMTLPIGRVVSTTG--VMLPLKLSYSGKIFRANEDFGGEQNEQTQAGIEIIGYPSIKAEIECIL-------- 139
Cdd:PLN02530 137 GRRVALRPELTPSLARLVLQKGksLSLPLKWFAIGQCWRYERMTRGRRREHYQWNMDIIGVPGVEAEAELLAaivtffkr 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502716242 140 IGI----------------GVLNALEIPN--F--------QIE-LGHAAIYRRVTNLLNLSETAEidfrLLIQNKSLTgi 192
Cdd:PLN02530 217 VGItssdvgikvssrkvlqAVLKSYGIPEesFapvcvivdKLEkLPREEIEKELDTLGVSEEAIE----GILDVLSLK-- 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502716242 193 krfvadnpsTLDDfilvLPRLFGPATAILKQaknlttdkgiltaLREMETIVEAVSYTADISVDLGLVQDFHYYTGIIFR 272
Cdd:PLN02530 291 ---------SLDD----LEALLGADSEAVAD-------------LKQLFSLAEAYGYQDWLVFDASVVRGLAYYTGIVFE 344
|
330 340 350
....*....|....*....|....*....|....*
gi 502716242 273 GY---ADLAAdnFLSGGRYDHLLEQFTSASSPAVG 304
Cdd:PLN02530 345 GFdraGKLRA--ICGGGRYDRLLSTFGGEDTPACG 377
|
|
| hisZ |
PRK12293 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
1-312 |
7.64e-13 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 183411 Cd Length: 281 Bit Score: 68.10 E-value: 7.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502716242 1 MNLNKNLPTGTRDKLFREARAAYKIEQQVNHYFEKRGFKRIETPVIEFedvfsSEHQADA---KLYRFFDEKGRLTVLRP 77
Cdd:PRK12293 1 MILEHEIPQGSKLYFGKSAKLKREIENVASEILYENGFEEIVTPFFSY-----HQHQSIAdekELIRFSDEKNHQISLRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502716242 78 DMTLPIGRVV------STTgvmlPLKLSYSGKIFRAnedfggEQNEQTQAGIEIIGYPSIKaeiECILIGIGVLNALEI- 150
Cdd:PRK12293 76 DSTLDVVRIVtkrlgrSTE----HKKWFYIQPVFRY------PSNEIYQIGAELIGEEDLS---EILNIAAEIFEELELe 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502716242 151 PNFQIElgHAAIYRRVTNLLNLS----ETAEIDfRLLIQN----KSLTGIKrfvadNPSTLDDFILVLPrlfgpatAILK 222
Cdd:PRK12293 143 PILQIS--NIKIPKLVAEILGLDievfKKGQIE-KLLAQNvpwlNKLVRIK-----TLEDLDEVIELVP-------DEIK 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502716242 223 QaknlttdkgiltALREMETIVEAVSYTADISVDLGLVQdFHYYTGIIFRgyadLAADNF--LSGGRYDhlleqftSASS 300
Cdd:PRK12293 208 E------------ELEKLKELAESIKYENLVIAPLYYAK-MRYYDDLFFR----FFDGNStlASGGNYE-------IDGI 263
|
330
....*....|..
gi 502716242 301 PAVGLALNLDSL 312
Cdd:PRK12293 264 SSSGFALYTDNL 275
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
23-142 |
2.09e-06 |
|
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: 48.27 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502716242 23 YKIEQQVNHYFEKRGFKRIETPVIEFEDVFSSEHQADAKLYRFFDEKGRLTVLRPDMTLPIGRVVSTTGVMLPLKLSYSG 102
Cdd:cd00768 3 SKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGHEPKDLLPVGAENEEDLYLRPTLEPGLVRLFVSHIRKLPLRLAEIG 82
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 502716242 103 KIFRANED--FGGEQNEQTQAGIEIIGYPSIKAEIECILIGI 142
Cdd:cd00768 83 PAFRNEGGrrGLRRVREFTQLEGEVFGEDGEEASEFEELIEL 124
|
|
|