|
Name |
Accession |
Description |
Interval |
E-value |
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
1-408 |
1.38e-161 |
|
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: 460.74 E-value: 1.38e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 1 MTVNRPRGTRDFLPADTARRRYVESVMRDVARKWGYSEIITPTFEHLDLFTLKSGEGIIG-ELYNFTDKGGREMTLRPEL 79
Cdd:COG0124 2 MKIQAPRGTRDILPEESAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKIGEDIVEkEMYTFEDRGGRSLTLRPEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 80 TAPVMRLYINELQPFPKPLKLFYFENCFRYERPQKGRFREFWQFGVELIGSGKPDSDAEVIALADAMLKAAGVKG-DMKL 158
Cdd:COG0124 82 TAPVARAVAEHGNELPFPFKLYYIGPVFRYERPQKGRYRQFHQFGVEVIGSDSPLADAEVIALAADLLKALGLKDfTLEI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 159 GNLavirtllsGLEPEIVSKVMRLVDKKEYAGLEALLEEIGAEEQLKSDLFHLIKLEGkrilPEVIKIVGNIPELVS--- 235
Cdd:COG0124 162 NSR--------GLPEERAEALLRYLDKLDKIGHEDVLDEDSQRRLETNPLRAILDSKG----PDCQEVLADAPKLLDylg 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 236 ------FEKTLKLLDAYGVDYSLDFGIARGLDYYTGMVFEVYAEGLGAQKQVCGGGSY-QLIKLFGGGDVPSTGFGIGFD 308
Cdd:COG0124 230 eeglahFEEVLELLDALGIPYVIDPRLVRGLDYYTGTVFEIVTDGLGAQGSVCGGGRYdGLVEQLGGPPTPAVGFAIGLE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 309 RIMEIC------PLTPPAPKTLMLISKPDLHLKAIGFANKLRKY-VPVHVDLMQRNFKAQLSYANTINADYVVIVGEKEL 381
Cdd:COG0124 310 RLLLLLeelgllPAAEPPPDVYVVPLGEEARAEALKLAQELRAAgIRVELDLGGRKLKKQLKYADKSGAPFVLILGEDEL 389
|
410 420
....*....|....*....|....*..
gi 499627630 382 EVGKLTLRDMVSGEQELLTLEEIIEKV 408
Cdd:COG0124 390 ANGTVTLKDLATGEQETVPLDELVEYL 416
|
|
| hisS |
TIGR00442 |
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ... |
4-401 |
6.49e-159 |
|
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: 453.47 E-value: 6.49e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 4 NRPRGTRDFLPADTARRRYVESVMRDVARKWGYSEIITPTFEHLDLFTLKSGEG---IIGELYNFTDKGGREMTLRPELT 80
Cdd:TIGR00442 1 QKPRGTRDFLPEEMIKWQYIEETIREVFERYGFKEIRTPIFEYTELFKRKVGEEtdiVSKEMYTFKDKGGRSLTLRPEGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 81 APVMRLYINELQPFPKPLKLFYFENCFRYERPQKGRFREFWQFGVELIGSGKPDSDAEVIALADAMLKAAGVKG-DMKLG 159
Cdd:TIGR00442 81 APVARAVIENKLLLPKPFKLYYIGPMFRYERPQKGRYRQFHQFGVEVIGSDSPLADAEIIALAADILKELGLKDfTLEIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 160 NLAVIRTLLsglepEIVSKVMRLVDKKeyaglealleeigaEEQLKSDLFHLIKLEGKRIL----PEVIKIVGNIPELVS 235
Cdd:TIGR00442 161 SLGILEGRL-----EYREALIRYLDKH--------------KDKLGEDSVRRLEKNPLRILdsknEKIQELLKNAPKILD 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 236 ---------FEKTLKLLDAYGVDYSLDFGIARGLDYYTGMVFEVYAEGLGAQKQVCGGGSY-QLIKLFGGGDVPSTGFGI 305
Cdd:TIGR00442 222 flceesrahFEELKELLDALGIPYKIDPSLVRGLDYYTGTVFEFVTDDLGAQGSICGGGRYdGLVEELGGPPTPAVGFAI 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 306 GFDRIMEICP-----LTPPAPKTLMLIS-KPDLHLKAIGFANKLRKY-VPVHVDLMQRNFKAQLSYANTINADYVVIVGE 378
Cdd:TIGR00442 302 GIERLILLLEelgliPPPSKKPDVYVVPlGEEAELEALKLAQKLRKAgIRVEVDLGGRKLKKQLKYADKLGARFALIIGE 381
|
410 420
....*....|....*....|...
gi 499627630 379 KELEVGKLTLRDMVSGEQELLTL 401
Cdd:TIGR00442 382 DELENGTVTLKDLETGEQETVPL 404
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
16-315 |
3.77e-109 |
|
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: 321.47 E-value: 3.77e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 16 DTARRRYVESVMRDVARKWGYSEIITPTFEHLDLFTLKSGEGIIGELYNFTDKGGREMTLRPELTAPVMRLYINELQPFP 95
Cdd:cd00773 1 EAALRRYIEDTLREVFERYGYEEIDTPVFEYTELFLRKSGDEVSKEMYRFKDKGGRDLALRPDLTAPVARAVAENLLSLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 96 KPLKLFYFENCFRYERPQKGRFREFWQFGVELIGSGKPDSDAEVIALADAMLKAAGVKG-DMKLGNLAVIRTLLSGLEpE 174
Cdd:cd00773 81 LPLKLYYIGPVFRYERPQKGRYREFYQVGVEIIGSDSPLADAEVIALAVEILEALGLKDfQIKINHRGILDGIAGLLE-D 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 175 IVSKVMRLVDKKEYAGLEAlleeigaeeqlksdlfhliklegkrilpevikivgnipelvsFEKTLKLLDAYGVD--YSL 252
Cdd:cd00773 160 REEYIERLIDKLDKEALAH------------------------------------------LEKLLDYLEALGVDikYSI 197
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499627630 253 DFGIARGLDYYTGMVFEVYAEGLGAQKQVCGGGSY-QLIKLFGGGDVPSTGFGIGFDRIMEICP 315
Cdd:cd00773 198 DLSLVRGLDYYTGIVFEAVADGLGAQGSIAGGGRYdGLLEEFGGEDVPAVGFAIGLERLLLALE 261
|
|
| hisZ |
PRK12292 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
6-365 |
1.62e-79 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 237043 [Multi-domain] Cd Length: 391 Bit Score: 250.17 E-value: 1.62e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 6 PRGTRDFLPADTARRRYVESVMRDVARKWGYSEIITPTFEHLDlfTLKSGEGIIGE--LYNFTDKG-GREMTLRPELTAP 82
Cdd:PRK12292 6 PEGIRDLLPEEARKIEEIRRRLLDLFRRWGYEEVITPTLEYLD--TLLAGGGAILDlrTFKLVDQLsGRTLGLRPDMTAQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 83 VMRLYINELQPFPKPLKLFYFENCFRYERPQKGRFREFWQFGVELIGSGKPDSDAEVIALADAMLKAAGVKgDMKL--GN 160
Cdd:PRK12292 84 IARIAATRLANRPGPLRLCYAGNVFRAQERGLGRSREFLQSGVELIGDAGLEADAEVILLLLEALKALGLP-NFTLdlGH 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 161 LAVIRTLLS--GLEPEIVSKVMRLVDKKEYAGLEALLEEIgaEEQLKSDLFHLIKLEGKR-ILPEVIKIVGNIPELVSFE 237
Cdd:PRK12292 163 VGLFRALLEaaGLSEELEEVLRRALANKDYVALEELVLDL--SEELRDALLALPRLRGGReVLEEARKLLPSLPIKRALD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 238 KTLKLLDA-----YGVDYSLDFGIARGLDYYTGMVFEVYAEGLGAqkQVCGGGSY-QLIKLFgGGDVPSTGFGIGFDRIM 311
Cdd:PRK12292 241 ELEALAEAlekygYGIPLSLDLGLLRHLDYYTGIVFEGYVDGVGN--PIASGGRYdDLLGRF-GRARPATGFSLDLDRLL 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 499627630 312 EIC-PLTPPAPKTLMLISKPDLHLKAIGFANKLRKY-VPVHVDLMQRNFKAQLSYA 365
Cdd:PRK12292 318 ELQlELPVEARKDLVIAPDSEALAAALAAAQELRKKgEIVVLALPGRNFEDAREYA 373
|
|
| tRNA-synt_His |
pfam13393 |
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ... |
8-310 |
2.43e-66 |
|
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: 213.60 E-value: 2.43e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 8 GTRDFLPADTARRRYVESVMRDVARKWGYSEIITPTFEHLDlfTLKSGEGI-IGELYNFTDKGGREMTLRPELTAPVMRL 86
Cdd:pfam13393 1 GIRDLLPPEARRIEELRRRLLDLFRSWGYELVMPPLLEYLD--SLLTGTGAdLDQTFKLVDQSGRLLGLRADITPQVARI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 87 YINELQPfPKPLKLFYFENCFRYERPQKGRFREFWQFGVELIGSGKPDSDAEVIALADAMLKAAGVKG-DMKLGNLAVIR 165
Cdd:pfam13393 79 DAHRLNR-PGPLRLCYAGSVLRTRPKGLGRSREPLQVGAELIGHAGIEADAEIISLLLEALAAAGVPGvTLDLGHVGLVR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 166 TLLS--GLEPEIVSKVMRLVDKKEYAGLEALLEEIGAEEQLKSDLFHLIKLEGK--------RILPEVIKIVGNIPELvs 235
Cdd:pfam13393 158 ALLEaaGLSEALEEALRAALQRKDAAELAELAAEAGLPPALRRALLALPDLYGGpevldearAALPGLPALQEALDEL-- 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499627630 236 fEKTLKLLDA--YGVDYSLDFGIARGLDYYTGMVFEVYAEGLGaqKQVCGGGSY-QLIKLFGGGdVPSTGFGIGFDRI 310
Cdd:pfam13393 236 -EALAALLEAlgDGVRLTFDLAELRGYEYYTGIVFAAYAPGVG--EPLARGGRYdDLGAAFGRA-RPATGFSLDLEAL 309
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
1-408 |
1.38e-161 |
|
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: 460.74 E-value: 1.38e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 1 MTVNRPRGTRDFLPADTARRRYVESVMRDVARKWGYSEIITPTFEHLDLFTLKSGEGIIG-ELYNFTDKGGREMTLRPEL 79
Cdd:COG0124 2 MKIQAPRGTRDILPEESAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKIGEDIVEkEMYTFEDRGGRSLTLRPEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 80 TAPVMRLYINELQPFPKPLKLFYFENCFRYERPQKGRFREFWQFGVELIGSGKPDSDAEVIALADAMLKAAGVKG-DMKL 158
Cdd:COG0124 82 TAPVARAVAEHGNELPFPFKLYYIGPVFRYERPQKGRYRQFHQFGVEVIGSDSPLADAEVIALAADLLKALGLKDfTLEI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 159 GNLavirtllsGLEPEIVSKVMRLVDKKEYAGLEALLEEIGAEEQLKSDLFHLIKLEGkrilPEVIKIVGNIPELVS--- 235
Cdd:COG0124 162 NSR--------GLPEERAEALLRYLDKLDKIGHEDVLDEDSQRRLETNPLRAILDSKG----PDCQEVLADAPKLLDylg 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 236 ------FEKTLKLLDAYGVDYSLDFGIARGLDYYTGMVFEVYAEGLGAQKQVCGGGSY-QLIKLFGGGDVPSTGFGIGFD 308
Cdd:COG0124 230 eeglahFEEVLELLDALGIPYVIDPRLVRGLDYYTGTVFEIVTDGLGAQGSVCGGGRYdGLVEQLGGPPTPAVGFAIGLE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 309 RIMEIC------PLTPPAPKTLMLISKPDLHLKAIGFANKLRKY-VPVHVDLMQRNFKAQLSYANTINADYVVIVGEKEL 381
Cdd:COG0124 310 RLLLLLeelgllPAAEPPPDVYVVPLGEEARAEALKLAQELRAAgIRVELDLGGRKLKKQLKYADKSGAPFVLILGEDEL 389
|
410 420
....*....|....*....|....*..
gi 499627630 382 EVGKLTLRDMVSGEQELLTLEEIIEKV 408
Cdd:COG0124 390 ANGTVTLKDLATGEQETVPLDELVEYL 416
|
|
| hisS |
TIGR00442 |
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ... |
4-401 |
6.49e-159 |
|
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: 453.47 E-value: 6.49e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 4 NRPRGTRDFLPADTARRRYVESVMRDVARKWGYSEIITPTFEHLDLFTLKSGEG---IIGELYNFTDKGGREMTLRPELT 80
Cdd:TIGR00442 1 QKPRGTRDFLPEEMIKWQYIEETIREVFERYGFKEIRTPIFEYTELFKRKVGEEtdiVSKEMYTFKDKGGRSLTLRPEGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 81 APVMRLYINELQPFPKPLKLFYFENCFRYERPQKGRFREFWQFGVELIGSGKPDSDAEVIALADAMLKAAGVKG-DMKLG 159
Cdd:TIGR00442 81 APVARAVIENKLLLPKPFKLYYIGPMFRYERPQKGRYRQFHQFGVEVIGSDSPLADAEIIALAADILKELGLKDfTLEIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 160 NLAVIRTLLsglepEIVSKVMRLVDKKeyaglealleeigaEEQLKSDLFHLIKLEGKRIL----PEVIKIVGNIPELVS 235
Cdd:TIGR00442 161 SLGILEGRL-----EYREALIRYLDKH--------------KDKLGEDSVRRLEKNPLRILdsknEKIQELLKNAPKILD 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 236 ---------FEKTLKLLDAYGVDYSLDFGIARGLDYYTGMVFEVYAEGLGAQKQVCGGGSY-QLIKLFGGGDVPSTGFGI 305
Cdd:TIGR00442 222 flceesrahFEELKELLDALGIPYKIDPSLVRGLDYYTGTVFEFVTDDLGAQGSICGGGRYdGLVEELGGPPTPAVGFAI 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 306 GFDRIMEICP-----LTPPAPKTLMLIS-KPDLHLKAIGFANKLRKY-VPVHVDLMQRNFKAQLSYANTINADYVVIVGE 378
Cdd:TIGR00442 302 GIERLILLLEelgliPPPSKKPDVYVVPlGEEAELEALKLAQKLRKAgIRVEVDLGGRKLKKQLKYADKLGARFALIIGE 381
|
410 420
....*....|....*....|...
gi 499627630 379 KELEVGKLTLRDMVSGEQELLTL 401
Cdd:TIGR00442 382 DELENGTVTLKDLETGEQETVPL 404
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
16-315 |
3.77e-109 |
|
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: 321.47 E-value: 3.77e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 16 DTARRRYVESVMRDVARKWGYSEIITPTFEHLDLFTLKSGEGIIGELYNFTDKGGREMTLRPELTAPVMRLYINELQPFP 95
Cdd:cd00773 1 EAALRRYIEDTLREVFERYGYEEIDTPVFEYTELFLRKSGDEVSKEMYRFKDKGGRDLALRPDLTAPVARAVAENLLSLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 96 KPLKLFYFENCFRYERPQKGRFREFWQFGVELIGSGKPDSDAEVIALADAMLKAAGVKG-DMKLGNLAVIRTLLSGLEpE 174
Cdd:cd00773 81 LPLKLYYIGPVFRYERPQKGRYREFYQVGVEIIGSDSPLADAEVIALAVEILEALGLKDfQIKINHRGILDGIAGLLE-D 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 175 IVSKVMRLVDKKEYAGLEAlleeigaeeqlksdlfhliklegkrilpevikivgnipelvsFEKTLKLLDAYGVD--YSL 252
Cdd:cd00773 160 REEYIERLIDKLDKEALAH------------------------------------------LEKLLDYLEALGVDikYSI 197
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499627630 253 DFGIARGLDYYTGMVFEVYAEGLGAQKQVCGGGSY-QLIKLFGGGDVPSTGFGIGFDRIMEICP 315
Cdd:cd00773 198 DLSLVRGLDYYTGIVFEAVADGLGAQGSIAGGGRYdGLLEEFGGEDVPAVGFAIGLERLLLALE 261
|
|
| HisZ |
COG3705 |
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism]; |
13-315 |
2.29e-81 |
|
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism];
Pssm-ID: 442919 [Multi-domain] Cd Length: 312 Bit Score: 252.40 E-value: 2.29e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 13 LPADTARRRYVESVMRDVARKWGYSEIITPTFEHLDLFTLKSGEGIIGELYNFTDKGGREMTLRPELTAPVMRLYINELQ 92
Cdd:COG3705 1 LPEEAARKEELRRRLLDVFRSWGYELVEPPLLEYLDSLLTGSGADLDLQTFKLVDQLGRTLGLRPDMTPQVARIAATRLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 93 PFPKPLKLFYFENCFRYERPQKGRFREFWQFGVELIGSGKPDSDAEVIALADAMLKAAGVKG---DmkLGNLAVIRTLLS 169
Cdd:COG3705 81 NRPGPLRLCYAGNVFRTRPSGLGRSREFLQAGAELIGHAGLEADAEVIALALEALKAAGLEDftlD--LGHVGLFRALLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 170 --GLEPEIVSKVMRLVDKKEYAGLEALLEEIGAEEQLKSDLFHLIKLEGKR-ILPEVIKIVGNIP---ELVSFEKTLKLL 243
Cdd:COG3705 159 alGLSEEQREELRRALARKDAVELEELLAELGLSEELAEALLALPELYGGEeVLARARALLLDAAiraALDELEALAEAL 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499627630 244 DAYGVD--YSLDFGIARGLDYYTGMVFEVYAEGLGaqKQVCGGGSY-QLIKLFgGGDVPSTGFGIGFDRIMEICP 315
Cdd:COG3705 239 AARGPDvrLTFDLSELRGYDYYTGIVFEAYAPGVG--DPLARGGRYdGLLAAF-GRARPATGFSLDLDRLLRALP 310
|
|
| hisZ_biosyn_reg |
TIGR00443 |
ATP phosphoribosyltransferase, regulatory subunit; Apparant second copies of histidyl-tRNA ... |
10-313 |
2.95e-81 |
|
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: 252.15 E-value: 2.95e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 10 RDFLPADTARRRYVESVMRDVARKWGYSEIITPTFEHLDLFTLKSGEGIiGELYNFTDKGGREMTLRPELTAPVMRLYIN 89
Cdd:TIGR00443 1 RDLLPEEAARKEEIERQLQDVFRSWGYQEIITPTLEYLDTLSAGSGILN-EDLFKLFDQLGRVLGLRPDMTAPIARLVST 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 90 ELQPFPKPLKLFYFENCFRYERPQKGRFREFWQFGVELIGSGKPDSDAEVIALADAMLKAAGVKG-DMKLGNLAVIRTLL 168
Cdd:TIGR00443 80 RLRDRPLPLRLCYAGNVFRTNESGGGRSREFTQAGVELIGAGGPAADAEVIALLIEALKALGLKDfKIELGHVGLVRALL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 169 --SGLEPEIVSKVMRLVDKKEYAGLEALLEEIGAEEQLKSDLFHLIKL--EGKRILPEVIKIVGNIPELVSF---EKTLK 241
Cdd:TIGR00443 160 eeAGLPEEAREALREALARKDLVALEELVAELGLSPEVRERLLALPRLrgDGEEVLEEARALAGSETAEAALdelEAVLE 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499627630 242 LLDAYGVD--YSLDFGIARGLDYYTGMVFEVYAEGLGAqkQVCGGGSY-QLIKLFgGGDVPSTGFGIGFDRIMEI 313
Cdd:TIGR00443 240 LLEARGVEeyISLDLGLVRGYHYYTGLIFEGYAPGLGA--PLAGGGRYdELLGRF-GRPLPATGFALNLERLLEA 311
|
|
| hisZ |
PRK12292 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
6-365 |
1.62e-79 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 237043 [Multi-domain] Cd Length: 391 Bit Score: 250.17 E-value: 1.62e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 6 PRGTRDFLPADTARRRYVESVMRDVARKWGYSEIITPTFEHLDlfTLKSGEGIIGE--LYNFTDKG-GREMTLRPELTAP 82
Cdd:PRK12292 6 PEGIRDLLPEEARKIEEIRRRLLDLFRRWGYEEVITPTLEYLD--TLLAGGGAILDlrTFKLVDQLsGRTLGLRPDMTAQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 83 VMRLYINELQPFPKPLKLFYFENCFRYERPQKGRFREFWQFGVELIGSGKPDSDAEVIALADAMLKAAGVKgDMKL--GN 160
Cdd:PRK12292 84 IARIAATRLANRPGPLRLCYAGNVFRAQERGLGRSREFLQSGVELIGDAGLEADAEVILLLLEALKALGLP-NFTLdlGH 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 161 LAVIRTLLS--GLEPEIVSKVMRLVDKKEYAGLEALLEEIgaEEQLKSDLFHLIKLEGKR-ILPEVIKIVGNIPELVSFE 237
Cdd:PRK12292 163 VGLFRALLEaaGLSEELEEVLRRALANKDYVALEELVLDL--SEELRDALLALPRLRGGReVLEEARKLLPSLPIKRALD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 238 KTLKLLDA-----YGVDYSLDFGIARGLDYYTGMVFEVYAEGLGAqkQVCGGGSY-QLIKLFgGGDVPSTGFGIGFDRIM 311
Cdd:PRK12292 241 ELEALAEAlekygYGIPLSLDLGLLRHLDYYTGIVFEGYVDGVGN--PIASGGRYdDLLGRF-GRARPATGFSLDLDRLL 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 499627630 312 EIC-PLTPPAPKTLMLISKPDLHLKAIGFANKLRKY-VPVHVDLMQRNFKAQLSYA 365
Cdd:PRK12292 318 ELQlELPVEARKDLVIAPDSEALAAALAAAQELRKKgEIVVLALPGRNFEDAREYA 373
|
|
| PLN02530 |
PLN02530 |
histidine-tRNA ligase |
1-405 |
2.45e-73 |
|
histidine-tRNA ligase
Pssm-ID: 178145 [Multi-domain] Cd Length: 487 Bit Score: 237.33 E-value: 2.45e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 1 MTVNRPRGTRDFLPADTARRRYVESVMRDVARKWGYSEIITPTFEHLDLFTLKSGEGIIGELYNFTDKGGREMTLRPELT 80
Cdd:PLN02530 68 IDVNPPKGTRDFPPEDMRLRNWLFDHFREVSRLFGFEEVDAPVLESEELYIRKAGEEITDQLYNFEDKGGRRVALRPELT 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 81 APVMRLYINELQPFPKPLKLFYFENCFRYERPQKGRFREFWQFGVELIGSGKPDSDAEVIALADAMLKAAGVKGD---MK 157
Cdd:PLN02530 148 PSLARLVLQKGKSLSLPLKWFAIGQCWRYERMTRGRRREHYQWNMDIIGVPGVEAEAELLAAIVTFFKRVGITSSdvgIK 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 158 LGNLAVIRTLLS--GLEPEIVSKVMRLVDKKEYAGLEAL---LEEIGAEEQLKSDLFHLIKLegkRILPEVIKIVGNIPE 232
Cdd:PLN02530 228 VSSRKVLQAVLKsyGIPEESFAPVCVIVDKLEKLPREEIekeLDTLGVSEEAIEGILDVLSL---KSLDDLEALLGADSE 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 233 LVSFEKTL-KLLDAYGVDYSLDF--GIARGLDYYTGMVFEVYAEGlGAQKQVCGGGSY-QLIKLFGGGDVPSTGFGIGFD 308
Cdd:PLN02530 305 AVADLKQLfSLAEAYGYQDWLVFdaSVVRGLAYYTGIVFEGFDRA-GKLRAICGGGRYdRLLSTFGGEDTPACGFGFGDA 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 309 RIME------ICPLTPPAPKTLMLISKPDLHLKAIGFANKLRKYVPVhVDLMQRNFKAQ--LSYANTINADYVVIVGEKE 380
Cdd:PLN02530 384 VIVEllkekgLLPELPHQVDDVVFALDEDLQGAAAGVASRLREKGRS-VDLVLEPKKLKwvFKHAERIGAKRLVLVGASE 462
|
410 420
....*....|....*....|....*
gi 499627630 381 LEVGKLTLRDMVSGEQELLTLEEII 405
Cdd:PLN02530 463 WERGMVRVKDLSSGEQTEVKLDELE 487
|
|
| tRNA-synt_His |
pfam13393 |
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ... |
8-310 |
2.43e-66 |
|
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: 213.60 E-value: 2.43e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 8 GTRDFLPADTARRRYVESVMRDVARKWGYSEIITPTFEHLDlfTLKSGEGI-IGELYNFTDKGGREMTLRPELTAPVMRL 86
Cdd:pfam13393 1 GIRDLLPPEARRIEELRRRLLDLFRSWGYELVMPPLLEYLD--SLLTGTGAdLDQTFKLVDQSGRLLGLRADITPQVARI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 87 YINELQPfPKPLKLFYFENCFRYERPQKGRFREFWQFGVELIGSGKPDSDAEVIALADAMLKAAGVKG-DMKLGNLAVIR 165
Cdd:pfam13393 79 DAHRLNR-PGPLRLCYAGSVLRTRPKGLGRSREPLQVGAELIGHAGIEADAEIISLLLEALAAAGVPGvTLDLGHVGLVR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 166 TLLS--GLEPEIVSKVMRLVDKKEYAGLEALLEEIGAEEQLKSDLFHLIKLEGK--------RILPEVIKIVGNIPELvs 235
Cdd:pfam13393 158 ALLEaaGLSEALEEALRAALQRKDAAELAELAAEAGLPPALRRALLALPDLYGGpevldearAALPGLPALQEALDEL-- 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499627630 236 fEKTLKLLDA--YGVDYSLDFGIARGLDYYTGMVFEVYAEGLGaqKQVCGGGSY-QLIKLFGGGdVPSTGFGIGFDRI 310
Cdd:pfam13393 236 -EALAALLEAlgDGVRLTFDLAELRGYEYYTGIVFAAYAPGVG--EPLARGGRYdDLGAAFGRA-RPATGFSLDLEAL 309
|
|
| syh |
CHL00201 |
histidine-tRNA synthetase; Provisional |
7-408 |
9.59e-54 |
|
histidine-tRNA synthetase; Provisional
Pssm-ID: 164576 [Multi-domain] Cd Length: 430 Bit Score: 184.33 E-value: 9.59e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 7 RGTRDFLPADTARRRYVESVMRDVARKWGYSEIITPTFEHLDLFTLKSGEG---IIGELYNFTDKGGREMTLRPELTAPV 83
Cdd:CHL00201 8 RGTKDILPDEINYWQFIHDKALTLLSLANYSEIRTPIFENSSLYDRGIGETtdiVNKEMYRFTDRSNRDITLRPEGTAGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 84 MRLYI-NELQPFPKPLKLFYFENCFRYERPQKGRFREFWQFGVELIGSGKPDSDAEVIALADAMLKaagvkgDMKLGNLA 162
Cdd:CHL00201 88 VRAFIeNKMDYHSNLQRLWYSGPMFRYERPQSGRQRQFHQLGIEFIGSIDARADTEVIHLAMQIFN------ELQVKNLI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 163 VIRTLLSGLEPEIVSKvmrlVDKKEYagLEALLEEIGAEEQ--LKSDLFHLI---KLEGKRILPEVIKivgnIPELVSFE 237
Cdd:CHL00201 162 LDINSIGKLEDRQSYQ----LKLVEY--LSQYQDDLDTDSQnrLYSNPIRILdskNLKTQEILDGAPK----ISDFLSLE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 238 KT---------LKLLDaygVDYSLDFGIARGLDYYTGMVFEVYAEGLGAQKQVCGGGSY-QLIKLFGGGDVPSTGFGIGF 307
Cdd:CHL00201 232 STehfydvctyLNLLN---IPYKINYKLVRGLDYYNDTAFEIKTLSSNGQDTICGGGRYdSLIHQLGGPKTPAVGCAIGL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 308 DRIMEICP--LTPPAPKTLMLISKPDLHLKAIGF--ANKLR-KYVPVHVDLMQRNFKAQLSYANTINADYVVIVGEKELE 382
Cdd:CHL00201 309 ERLLLIAKdnIILPKQSIDVYIATQGLKAQKKGWeiIQFLEkQNIKFELDLSSSNFHKQIKQAGKKRAKACIILGDNEIM 388
|
410 420
....*....|....*....|....*.
gi 499627630 383 VGKLTLRDMVSGEQELLTLEEIIEKV 408
Cdd:CHL00201 389 DNCITIKWLDEQVQENAQYSNFKQEI 414
|
|
| PRK12420 |
PRK12420 |
histidyl-tRNA synthetase; Provisional |
7-404 |
1.82e-51 |
|
histidyl-tRNA synthetase; Provisional
Pssm-ID: 237097 [Multi-domain] Cd Length: 423 Bit Score: 178.00 E-value: 1.82e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 7 RGTRDFLPADTARRRYVESVMRDVARKWGYSEIITPTFEHLDLFTLKSGEG--IIGELYNFTDKGGREMTLRPELTAP-- 82
Cdd:PRK12420 8 KGTKDYLPEEQVLRNKIKRALEDVFERYGCKPLETPTLNMYELMSSKYGGGdeILKEIYTLTDQGKRDLALRYDLTIPfa 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 83 -VMRLYINELQPFpkplKLFYFENCFRYERPQKGRFREFWQFGVELIGSGKPDSDAEVIALADAMLKAAGVKGDMKLGNl 161
Cdd:PRK12420 88 kVVAMNPNIRLPF----KRYEIGKVFRDGPIKQGRFREFIQCDVDIVGVESVMAEAELMSMAFELFRRLNLEVTIQYNN- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 162 aviRTLLSGL------EPEIVSKVMRLVDKKEYAGLEALLEEI---GAEEQLKSDLFHLIKLEGKRILPEVIKIVGN--- 229
Cdd:PRK12420 163 ---RKLLNGIlqaigiPTELTSDVILSLDKIEKIGIDGVRKDLlerGISEEMADTICNTVLSCLQLSIADFKEAFNNplv 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 230 ---IPELvsfEKTLKLLDAYGVDYSLDFG--IARGLDYYTGMVFEVYAEGLGAQKQVCGGGSY-QLIKLFGGGDV--PST 301
Cdd:PRK12420 240 aegVNEL---QQLQQYLIALGINENCIFNpfLARGLTMYTGTVYEIFLKDGSITSSIGSGGRYdNIIGAFRGDDMnyPTV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 302 GFGIGFDRIMEIC---PLTPPAPKTLML-ISKPdlhLKAIGFANKLRKY--VPVHVDLMQRNFKAQLSYANTINADYVVI 375
Cdd:PRK12420 317 GISFGLDVIYTALsqkETISSTADVFIIpLGTE---LQCLQIAQQLRSTtgLKVELELAGRKLKKALNYANKENIPYVLI 393
|
410 420
....*....|....*....|....*....
gi 499627630 376 VGEKELEVGKLTLRDMVSGEQELLTLEEI 404
Cdd:PRK12420 394 IGEEEVSTGTVMLRNMKEGSEVKVPLSSL 422
|
|
| PLN02972 |
PLN02972 |
Histidyl-tRNA synthetase |
6-409 |
6.42e-35 |
|
Histidyl-tRNA synthetase
Pssm-ID: 215525 [Multi-domain] Cd Length: 763 Bit Score: 136.94 E-value: 6.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 6 PRGTRDFLPADTARRRYVESVMRDVARKWGYSEIITPTFEHLDLFTLKSGEGIiGELYNFTDKGGREMTLRPELTAPVMR 85
Cdd:PLN02972 330 PKGTRDFAKEQMAIREKAFSIITSVFKRHGATALDTPVFELRETLMGKYGEDS-KLIYDLADQGGELCSLRYDLTVPFAR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 86 -LYINELQPFpkplKLFYFENCFRYERPQKGRFREFWQFGVELIGSGKP-DSDAEVIALADAMLKAAGV-KGDMKLGNLA 162
Cdd:PLN02972 409 yVAMNGITSF----KRYQIAKVYRRDNPSKGRYREFYQCDFDIAGVYEPmGPDFEIIKVLTELLDELDIgTYEVKLNHRK 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 163 VIRTLLS--GLEPEIVSKVMRLVDKKEYAGLE----ALLEEIGAEEQLKSDLFHLIKLEG------KRILPEVIKIVGN- 229
Cdd:PLN02972 485 LLDGMLEicGVPPEKFRTICSSIDKLDKQSFEqvkkEMVEEKGLSNETADKIGNFVKERGpplellSKLRQEGSEFLGNa 564
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 230 --IPELVSFEKTLKLLDAYGVDYSL--DFGIARGLDYYTGMVFEvyAEGLGAQ-KQVCGGGSY-QLIKLFGGGDVPSTGF 303
Cdd:PLN02972 565 ssRAALDELEIMFKALEKSKAIGKIvfDLSLARGLDYYTGVIYE--AVFKGAQvGSIAAGGRYdNLVGMFSGKQVPAVGV 642
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 304 GIGFDRIMEIC---------PLTPPAPKTLMLISKPDLHLKAIGFANKLRKYVPVHVDLMQRNFKAQLSYANTINADYVV 374
Cdd:PLN02972 643 SLGIERVFAIMeqqeeeksqVIRPTETEVLVSIIGDDKLALAAELVSELWNAGIKAEYKVSTRKAKHLKRAKESGIPWMV 722
|
410 420 430
....*....|....*....|....*....|....*
gi 499627630 375 IVGEKELEVGKLTLRDMVSGEQELLTLEEIIEKVC 409
Cdd:PLN02972 723 LVGEKELSKGFVKLKNLEAGVEEEVDRTCFVQELK 757
|
|
| hisZ |
PRK12295 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
35-310 |
8.77e-29 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 183413 [Multi-domain] Cd Length: 373 Bit Score: 115.80 E-value: 8.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 35 GYSEIITPTFEHLDLFTLKSGEGIIGELYNFTDKGGREMTLRPELTAPVMRLYInELQPfPKPLKLFYFENCFRYerpQK 114
Cdd:PRK12295 22 GAVRVDPPILQPAEPFLDLSGEDIRRRIFVTSDENGEELCLRPDFTIPVCRRHI-ATAG-GEPARYAYLGEVFRQ---RR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 115 GRFREFWQFGVELIGSG-KPDSDAEVIALADAMLKAAGVK-GDMKLGNLAVIRTLLSGLE--PEIVSKVMRLVDKKEYag 190
Cdd:PRK12295 97 DRASEFLQAGIESFGRAdPAAADAEVLALALEALAALGPGdLEVRLGDVGLFAALVDALGlpPGWKRRLLRHFGRPRS-- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 191 LEALLEE------------------IGAEEQLKSDLFHLIKLEG-------------KRILP---------------EVI 224
Cdd:PRK12295 175 LDALLARlagprvdpldehagvlaaLADEAAARALVEDLMSIAGispvggrspaeiaRRLLEkaalaaaarlpaealAVL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 225 K----IVGNIPE-------------------LVSFEKTLKLLDAYGVD-----YSLDFGiaRGLDYYTGMVFEVYAEGLG 276
Cdd:PRK12295 255 ErflaISGPPDAalaalralaadagldldaaLDRFEARLAALAARGIDlerlrFSASFG--RPLDYYTGFVFEIRAAGNG 332
|
330 340 350
....*....|....*....|....*....|....*.
gi 499627630 277 AQKqVCGGGSY-QLIKLFGGGD-VPSTGFGIGFDRI 310
Cdd:PRK12295 333 DPP-LAGGGRYdGLLTRLGAGEpIPAVGFSIWLDRL 367
|
|
| PRK12421 |
PRK12421 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
6-303 |
3.07e-21 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 237098 Cd Length: 392 Bit Score: 94.65 E-value: 3.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 6 PRGTRDFLPADTARrryVESVMR---DVARKWGYSEIITPTFEHLDLFTLKSGEGIIGELYNFTDK-GGREMTLRPELTA 81
Cdd:PRK12421 10 PDGVADVLPEEAQK---IERLRRrllDLFASRGYQLVMPPLIEYLESLLTGAGQDLKLQTFKLIDQlSGRLMGVRADITP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 82 PVMRlyIN-ELQPFPKPLKLFYFENCFRyERPQK-GRFREFWQFGVELIGSGKPDSDAEVIALADAMLKAAGVKG-DMKL 158
Cdd:PRK12421 87 QVAR--IDaHLLNREGVARLCYAGSVLH-TLPQGlFGSRTPLQLGAELYGHAGIEADLEIIRLMLGLLRNAGVPAlHLDL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 159 GNLAVIRTL--LSGLEPEIVSKVMRLVDKKEYAGLEALLEEIGAEEQLKSDLFHLIKLEGKrilPEVIK----------- 225
Cdd:PRK12421 164 GHVGIFRRLaeLAGLSPEEEEELFDLLQRKALPELAEVCQNLGVGSDLRRMFYALARLNGG---LEALDralsvlalqda 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 226 -IVGNIPELvsfEKTLKLLDAYGVDYSLDFGIA--RGLDYYTGMVFEVYAEGLGAqkQVCGGGSYQLIKLFGGGDVPSTG 302
Cdd:PRK12421 241 aIRQALDEL---KTLAAHLKNRWPELPVSIDLAelRGYHYHTGLVFAAYIPGRGQ--ALARGGRYDGIGEAFGRARPATG 315
|
.
gi 499627630 303 F 303
Cdd:PRK12421 316 F 316
|
|
| HisRS_anticodon |
cd00859 |
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases ... |
331-408 |
4.18e-17 |
|
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: 76.04 E-value: 4.18e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499627630 331 DLHLKAIGFANKLRK-YVPVHVDLMQRNFKAQLSYANTINADYVVIVGEKELEVGKLTLRDMVSGEQELLTLEEIIEKV 408
Cdd:cd00859 12 GALSEALELAEQLRDaGIKAEIDYGGRKLKKQFKYADRSGARFAVILGEDELAAGVVTVKDLETGEQETVALDELVEEL 90
|
|
| 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 ... |
16-149 |
3.22e-16 |
|
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: 77.43 E-value: 3.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 16 DTARRRYVESVMRDVARKWGYSEIITPTFEHLDLFtLKSG--EGIIGELYNFTDKG----GREMTLRPELTAPVMRLYIN 89
Cdd:cd00670 1 GTALWRALERFLDDRMAEYGYQEILFPFLAPTVLF-FKGGhlDGYRKEMYTFEDKGrelrDTDLVLRPAACEPIYQIFSG 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499627630 90 ELQPFPK-PLKLFYFENCFRYERPQ---KGRFREFWQFGVELIGSGK--PDSDAEVIALADAMLKA 149
Cdd:cd00670 80 EILSYRAlPLRLDQIGPCFRHEPSGrrgLMRVREFRQVEYVVFGEPEeaEEERREWLELAEEIARE 145
|
|
| hisZ |
PRK12293 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
6-313 |
1.52e-15 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 183411 Cd Length: 281 Bit Score: 76.19 E-value: 1.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 6 PRGTRDFLpADTAR-RRYVESVMRDVARKWGYSEIITPTF---EHLDLFTLKsgegiigELYNFTDKGGREMTLRPELTA 81
Cdd:PRK12293 8 PQGSKLYF-GKSAKlKREIENVASEILYENGFEEIVTPFFsyhQHQSIADEK-------ELIRFSDEKNHQISLRADSTL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 82 PVMRLYINELQPFPKPLKLFYFENCFRYerPQkgrfREFWQFGVELIGSgkpDSDAEVIALADAMLKAAGVKGDMKLGNL 161
Cdd:PRK12293 80 DVVRIVTKRLGRSTEHKKWFYIQPVFRY--PS----NEIYQIGAELIGE---EDLSEILNIAAEIFEELELEPILQISNI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 162 AVirtllsglePEIVSKVMRLvdkkeyaGLEaLLEEIGAEEQLKSD---LFHLIKLEGKRILPEVIKIVgniPELVSfEK 238
Cdd:PRK12293 151 KI---------PKLVAEILGL-------DIE-VFKKGQIEKLLAQNvpwLNKLVRIKTLEDLDEVIELV---PDEIK-EE 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 239 TLKLLD-AYGVDYSlDFGIA----RGLDYYTGMVFEVyaegLGAQKQVCGGGSYQLiklfggGDVPSTGFGIGFDRIMEI 313
Cdd:PRK12293 210 LEKLKElAESIKYE-NLVIAplyyAKMRYYDDLFFRF----FDGNSTLASGGNYEI------DGISSSGFALYTDNLIEI 278
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
20-224 |
8.21e-12 |
|
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: 64.06 E-value: 8.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 20 RRYVESVMRDVARKWGYSEIITPTFEHlDLFTLKSGEgIIGELYNFTDKGGREMTLRPELTAPVMRLYINELqpFPKPLK 99
Cdd:cd00768 2 RSKIEQKLRRFMAELGFQEVETPIVER-EPLLEKAGH-EPKDLLPVGAENEEDLYLRPTLEPGLVRLFVSHI--RKLPLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 100 LFYFENCFRYERPQKG--RFREFWQFGVELIGSGKPDSD--AEVIALADAMLKAAGVKGDMKLgnlaVIRTLLSGLEPEI 175
Cdd:cd00768 78 LAEIGPAFRNEGGRRGlrRVREFTQLEGEVFGEDGEEASefEELIELTEELLRALGIKLDIVF----VEKTPGEFSPGGA 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499627630 176 VSKVMRLVDKKEYAGLEalLEEIGAEEQLKSDLFHLIKL--EGKRILPEVI 224
Cdd:cd00768 154 GPGFEIEVDHPEGRGLE--IGSGGYRQDEQARAADLYFLdeALEYRYPPTI 202
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
63-154 |
3.86e-11 |
|
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: 61.66 E-value: 3.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 63 YNFTDKGGREMTLRPELTAPVMRLYINE-LQPFPKPLKLFYFENCFRYERP--QKG--RFREFWQFGVELIGSGK--PDS 135
Cdd:pfam00587 1 YKVEDENGDELALKPTNEPGHTLLFREEgLRSKDLPLKLAQFGTCFRHEASgdTRGliRVRQFHQDDAHIFHAPGqsPDE 80
|
90
....*....|....*....
gi 499627630 136 DAEVIALADAMLKAAGVKG 154
Cdd:pfam00587 81 LEDYIKLIDRVYSRLGLEV 99
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
331-408 |
6.96e-11 |
|
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: 58.37 E-value: 6.96e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499627630 331 DLHLKAIGFANKLRKY-VPVHVDLMQRNFKAQLSYANTINADYVVIVGEKELEVGKLTLRDMVSGEQELLTLEEIIEKV 408
Cdd:pfam03129 13 ELEEYAQKLAEELRAAgIRVELDDRNESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQETVSLDELVEKL 91
|
|
| HGTP_anticodon |
cd00738 |
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ... |
336-407 |
2.38e-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: 48.55 E-value: 2.38e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499627630 336 AIGFANKLR-KYVPVHVDLMQRNFKAQLSYANTINADYVVIVGEKELEVGKLTLRDMVSGEQELLTLEEIIEK 407
Cdd:cd00738 20 AQKLLNALLaNGIRVLYDDRERKIGKKFREADLRGVPFAVVVGEDELENGKVTVKSRDTGESETLHVDELPEF 92
|
|
| PRK03991 |
PRK03991 |
threonyl-tRNA synthetase; Validated |
372-408 |
6.14e-06 |
|
threonyl-tRNA synthetase; Validated
Pssm-ID: 235190 [Multi-domain] Cd Length: 613 Bit Score: 48.33 E-value: 6.14e-06
10 20 30
....*....|....*....|....*....|....*..
gi 499627630 372 YVVIVGEKELEVGKLTLRDMVSGEQELLTLEEIIEKV 408
Cdd:PRK03991 552 YVVVIGDKEMESGKLTVTIREESEKVEMTLEELIERI 588
|
|
| PRK14938 |
PRK14938 |
Ser-tRNA(Thr) hydrolase; Provisional |
325-408 |
2.59e-05 |
|
Ser-tRNA(Thr) hydrolase; Provisional
Pssm-ID: 184902 [Multi-domain] Cd Length: 387 Bit Score: 45.99 E-value: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499627630 325 MLISKPDLHLKAIGFANKLRKY-VPVHVDLMQRNFKAQLSYANTINADYVVIVGEKELEVGKLTLRDMVSGEQELLTLEE 403
Cdd:PRK14938 279 ILPVKKDFLDFSIQVAERLRKEgIRVNVDDLDDSLGNKIRRAGTEWIPFVIIIGEREVKTSTLTVKIRANNEQKSMTVEE 358
|
....*
gi 499627630 404 IIEKV 408
Cdd:PRK14938 359 LVKEI 363
|
|
| ThrRS_anticodon |
cd00860 |
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases ... |
372-408 |
5.51e-05 |
|
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: 41.72 E-value: 5.51e-05
10 20 30
....*....|....*....|....*....|....*..
gi 499627630 372 YVVIVGEKELEVGKLTLRDMVSGEQELLTLEEIIEKV 408
Cdd:cd00860 54 YILVVGDKEVETGTVSVRTRDGGDLGSMSLDEFIEKL 90
|
|
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
340-409 |
5.32e-03 |
|
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440210 [Multi-domain] Cd Length: 639 Bit Score: 38.86 E-value: 5.32e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499627630 340 ANKLRKY-VPVHVDLmqRN----FK---AQLSYANtinadYVVIVGEKELEVGKLTLRDMVSGEQELLTLEEIIEKVC 409
Cdd:COG0441 559 AKKLRAAgIRVEVDL--RNekigYKireAQLQKVP-----YMLVVGDKEVENGTVSVRRRGGGDLGTMSLDEFIARLK 629
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