|
Name |
Accession |
Description |
Interval |
E-value |
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
1-440 |
9.78e-126 |
|
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: 371.38 E-value: 9.78e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 1 MEFETLPGFRDFLPDACSARNSIFDHWRLAAESFNFQEYDAPVLEPLELFIEKSGEEIVG-QLFNFTDRGDRSVALRPEM 79
Cdd:COG0124 2 MKIQAPRGTRDILPEESAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKIGEDIVEkEMYTFEDRGGRSLTLRPEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 80 TPTLARLVGARANSLKRPVKWFTIGEHYRYERPQKGRLRAFYQFNADILGESGPGADAELIALLAHTLRSFGLaaDDFVI 159
Cdd:COG0124 82 TAPVARAVAEHGNELPFPFKLYYIGPVFRYERPQKGRYRQFHQFGVEVIGSDSPLADAEVIALAADLLKALGL--KDFTL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 160 RLSDRNLwwsilaaedlETEKAIEVLGIIDKMDRMGRERLLEkladavgsragEVCARIDAVREIRDFA-----ALESMI 234
Cdd:COG0124 160 EINSRGL----------PEERAEALLRYLDKLDKIGHEDVLD-----------EDSQRRLETNPLRAILdskgpDCQEVL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 235 RSLP--LEGASAEALharvEDWRCLMELLSHLGVgdSVRIDLSIVRGLAYYTGFVFEAFeasgagRALAGGGR------- 305
Cdd:COG0124 219 ADAPklLDYLGEEGL----AHFEEVLELLDALGI--PYVIDPRLVRGLDYYTGTVFEIV------TDGLGAQGsvcgggr 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 306 YDDLVQKLGGPAMPAVGFAMGDVTLADLLQEKSIDLEPPAKADFVCVIGGVEEQCFALQDVACLRHLGYRVEYPLKSQNF 385
Cdd:COG0124 287 YDGLVEQLGGPPTPAVGFAIGLERLLLLLEELGLLPAAEPPPDVYVVPLGEEARAEALKLAQELRAAGIRVELDLGGRKL 366
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1519714025 386 GKQLKAAVQSGASFALIYGSEEREQGVVRVRDLRTATELVLPREKLASAVSGIIA 440
Cdd:COG0124 367 KKQLKYADKSGAPFVLILGEDELANGTVTLKDLATGEQETVPLDELVEYLKELLA 421
|
|
| hisS |
TIGR00442 |
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ... |
4-428 |
1.16e-108 |
|
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: 326.74 E-value: 1.16e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 4 ETLPGFRDFLPDACSARNSIFDHWRLAAESFNFQEYDAPVLEPLELFIEKSGEE--IVG-QLFNFTDRGDRSVALRPEMT 80
Cdd:TIGR00442 1 QKPRGTRDFLPEEMIKWQYIEETIREVFERYGFKEIRTPIFEYTELFKRKVGEEtdIVSkEMYTFKDKGGRSLTLRPEGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 81 PTLARLVGARANSLKRPVKWFTIGEHYRYERPQKGRLRAFYQFNADILGESGPGADAELIALLAHTLRSFGLaaDDFVIR 160
Cdd:TIGR00442 81 APVARAVIENKLLLPKPFKLYYIGPMFRYERPQKGRYRQFHQFGVEVIGSDSPLADAEIIALAADILKELGL--KDFTLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 161 LSDRNlwwsilaaeDLET--EKAIEVLGIIDKmdrmgrerLLEKLADAVGSRAGEVCARI--DAVREIRDFAALESMIrs 236
Cdd:TIGR00442 159 INSLG---------ILEGrlEYREALIRYLDK--------HKDKLGEDSVRRLEKNPLRIldSKNEKIQELLKNAPKI-- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 237 lpLEGASAEALhARVEDwrcLMELLSHLGVgdSVRIDLSIVRGLAYYTGFVFEAFeasgagRALAGGGR-------YDDL 309
Cdd:TIGR00442 220 --LDFLCEESR-AHFEE---LKELLDALGI--PYKIDPSLVRGLDYYTGTVFEFV------TDDLGAQGsicgggrYDGL 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 310 VQKLGGPAMPAVGFAMGDVTLADLLQEKSIDLEPPAKAD-FVCVIgGVEEQCFALQDVACLRHLGYRVEYPLKSQNFGKQ 388
Cdd:TIGR00442 286 VEELGGPPTPAVGFAIGIERLILLLEELGLIPPPSKKPDvYVVPL-GEEAELEALKLAQKLRKAGIRVEVDLGGRKLKKQ 364
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1519714025 389 LKAAVQSGASFALIYGSEEREQGVVRVRDLRTATELVLPR 428
Cdd:TIGR00442 365 LKYADKLGARFALIIGEDELENGTVTLKDLETGEQETVPL 404
|
|
| PLN02530 |
PLN02530 |
histidine-tRNA ligase |
7-431 |
2.33e-103 |
|
histidine-tRNA ligase
Pssm-ID: 178145 [Multi-domain] Cd Length: 487 Bit Score: 316.30 E-value: 2.33e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 7 PGFRDFLPDACSARNSIFDHWRLAAESFNFQEYDAPVLEPLELFIEKSGEEIVGQLFNFTDRGDRSVALRPEMTPTLARL 86
Cdd:PLN02530 74 KGTRDFPPEDMRLRNWLFDHFREVSRLFGFEEVDAPVLESEELYIRKAGEEITDQLYNFEDKGGRRVALRPELTPSLARL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 87 VGARANSLKRPVKWFTIGEHYRYERPQKGRLRAFYQFNADILGESGPGADAELIALLAHTLRSFGLAADDFVIRLSDRNL 166
Cdd:PLN02530 154 VLQKGKSLSLPLKWFAIGQCWRYERMTRGRRREHYQWNMDIIGVPGVEAEAELLAAIVTFFKRVGITSSDVGIKVSSRKV 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 167 WWSILAAEDLETEKAIEVLGIIDKMDRMGRERLLEKLaDAVGSRAgEVCARIDAVREIRDFAALESMIrslpleGASAEA 246
Cdd:PLN02530 234 LQAVLKSYGIPEESFAPVCVIVDKLEKLPREEIEKEL-DTLGVSE-EAIEGILDVLSLKSLDDLEALL------GADSEA 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 247 lharVEDWRCLMELLSHLGVGDSVRIDLSIVRGLAYYTGFVFEAFEASGAGRALAGGGRYDDLVQKLGGPAMPAVGFAMG 326
Cdd:PLN02530 306 ----VADLKQLFSLAEAYGYQDWLVFDASVVRGLAYYTGIVFEGFDRAGKLRAICGGGRYDRLLSTFGGEDTPACGFGFG 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 327 DVTLADLLQEKSIDLEPPAKADFVCVIGGVEEQCFALQDVACLRHLGYRVEYPLKSQNFGKQLKAAVQSGASFALIYGSE 406
Cdd:PLN02530 382 DAVIVELLKEKGLLPELPHQVDDVVFALDEDLQGAAAGVASRLREKGRSVDLVLEPKKLKWVFKHAERIGAKRLVLVGAS 461
|
410 420
....*....|....*....|....*
gi 1519714025 407 EREQGVVRVRDLRTATELVLPREKL 431
Cdd:PLN02530 462 EWERGMVRVKDLSSGEQTEVKLDEL 486
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
17-335 |
6.57e-67 |
|
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: 214.77 E-value: 6.57e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 17 CSARNSIFDHWRLAAESFNFQEYDAPVLEPLELFIEKSGEEIVGQLFNFTDRGDRSVALRPEMTPTLARLVGARANSLKR 96
Cdd:cd00773 2 AALRRYIEDTLREVFERYGYEEIDTPVFEYTELFLRKSGDEVSKEMYRFKDKGGRDLALRPDLTAPVARAVAENLLSLPL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 97 PVKWFTIGEHYRYERPQKGRLRAFYQFNADILGESGPGADAELIALLAHTLRSFGLaaDDFVIRLSDRNLWWSILAAEDL 176
Cdd:cd00773 82 PLKLYYIGPVFRYERPQKGRYREFYQVGVEIIGSDSPLADAEVIALAVEILEALGL--KDFQIKINHRGILDGIAGLLED 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 177 ETEKaievlgiidkmdrmgRERLLEKLADAvgsragevcaridavrEIRDFAALEsmirslplegasaealharvedwrc 256
Cdd:cd00773 160 REEY---------------IERLIDKLDKE----------------ALAHLEKLL------------------------- 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 257 lmELLSHLGVGDSVRIDLSIVRGLAYYTGFVFEAF-EASGAGRALAGGGRYDDLVQKLGGPAMPAVGFAMGDVTLADLLQ 335
Cdd:cd00773 184 --DYLEALGVDIKYSIDLSLVRGLDYYTGIVFEAVaDGLGAQGSIAGGGRYDGLLEEFGGEDVPAVGFAIGLERLLLALE 261
|
|
| tRNA-synt_His |
pfam13393 |
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ... |
8-325 |
3.75e-35 |
|
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: 132.32 E-value: 3.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 8 GFRDFLPDACSARNSIFDHWRLAAESFNFQEYDAPVLEPLELFIEKSGEEIvGQLFNFTDRGDRSVALRPEMTPTLARLV 87
Cdd:pfam13393 1 GIRDLLPPEARRIEELRRRLLDLFRSWGYELVMPPLLEYLDSLLTGTGADL-DQTFKLVDQSGRLLGLRADITPQVARID 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 88 GARANSlKRPVKWFTIGEHYRYERPQKGRLRAFYQFNADILGESGPGADAELIALLAHTLRSFGLaaDDFVIRLSDRNLW 167
Cdd:pfam13393 80 AHRLNR-PGPLRLCYAGSVLRTRPKGLGRSREPLQVGAELIGHAGIEADAEIISLLLEALAAAGV--PGVTLDLGHVGLV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 168 WSILAAEDLETEKAIEVLGIIDKMDRMGrerlLEKLADAVGSRAgEVCARIDAVREIR-DFAALESMIRSLPLEGASAEA 246
Cdd:pfam13393 157 RALLEAAGLSEALEEALRAALQRKDAAE----LAELAAEAGLPP-ALRRALLALPDLYgGPEVLDEARAALPGLPALQEA 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1519714025 247 LHarveDWRCLMELLSHLGVGDSVRIDLSIVRGLAYYTGFVFEAFeASGAGRALAGGGRYDDLVQKLGGPAmPAVGFAM 325
Cdd:pfam13393 232 LD----ELEALAALLEALGDGVRLTFDLAELRGYEYYTGIVFAAY-APGVGEPLARGGRYDDLGAAFGRAR-PATGFSL 304
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
1-440 |
9.78e-126 |
|
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: 371.38 E-value: 9.78e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 1 MEFETLPGFRDFLPDACSARNSIFDHWRLAAESFNFQEYDAPVLEPLELFIEKSGEEIVG-QLFNFTDRGDRSVALRPEM 79
Cdd:COG0124 2 MKIQAPRGTRDILPEESAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKIGEDIVEkEMYTFEDRGGRSLTLRPEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 80 TPTLARLVGARANSLKRPVKWFTIGEHYRYERPQKGRLRAFYQFNADILGESGPGADAELIALLAHTLRSFGLaaDDFVI 159
Cdd:COG0124 82 TAPVARAVAEHGNELPFPFKLYYIGPVFRYERPQKGRYRQFHQFGVEVIGSDSPLADAEVIALAADLLKALGL--KDFTL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 160 RLSDRNLwwsilaaedlETEKAIEVLGIIDKMDRMGRERLLEkladavgsragEVCARIDAVREIRDFA-----ALESMI 234
Cdd:COG0124 160 EINSRGL----------PEERAEALLRYLDKLDKIGHEDVLD-----------EDSQRRLETNPLRAILdskgpDCQEVL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 235 RSLP--LEGASAEALharvEDWRCLMELLSHLGVgdSVRIDLSIVRGLAYYTGFVFEAFeasgagRALAGGGR------- 305
Cdd:COG0124 219 ADAPklLDYLGEEGL----AHFEEVLELLDALGI--PYVIDPRLVRGLDYYTGTVFEIV------TDGLGAQGsvcgggr 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 306 YDDLVQKLGGPAMPAVGFAMGDVTLADLLQEKSIDLEPPAKADFVCVIGGVEEQCFALQDVACLRHLGYRVEYPLKSQNF 385
Cdd:COG0124 287 YDGLVEQLGGPPTPAVGFAIGLERLLLLLEELGLLPAAEPPPDVYVVPLGEEARAEALKLAQELRAAGIRVELDLGGRKL 366
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1519714025 386 GKQLKAAVQSGASFALIYGSEEREQGVVRVRDLRTATELVLPREKLASAVSGIIA 440
Cdd:COG0124 367 KKQLKYADKSGAPFVLILGEDELANGTVTLKDLATGEQETVPLDELVEYLKELLA 421
|
|
| hisS |
TIGR00442 |
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ... |
4-428 |
1.16e-108 |
|
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: 326.74 E-value: 1.16e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 4 ETLPGFRDFLPDACSARNSIFDHWRLAAESFNFQEYDAPVLEPLELFIEKSGEE--IVG-QLFNFTDRGDRSVALRPEMT 80
Cdd:TIGR00442 1 QKPRGTRDFLPEEMIKWQYIEETIREVFERYGFKEIRTPIFEYTELFKRKVGEEtdIVSkEMYTFKDKGGRSLTLRPEGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 81 PTLARLVGARANSLKRPVKWFTIGEHYRYERPQKGRLRAFYQFNADILGESGPGADAELIALLAHTLRSFGLaaDDFVIR 160
Cdd:TIGR00442 81 APVARAVIENKLLLPKPFKLYYIGPMFRYERPQKGRYRQFHQFGVEVIGSDSPLADAEIIALAADILKELGL--KDFTLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 161 LSDRNlwwsilaaeDLET--EKAIEVLGIIDKmdrmgrerLLEKLADAVGSRAGEVCARI--DAVREIRDFAALESMIrs 236
Cdd:TIGR00442 159 INSLG---------ILEGrlEYREALIRYLDK--------HKDKLGEDSVRRLEKNPLRIldSKNEKIQELLKNAPKI-- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 237 lpLEGASAEALhARVEDwrcLMELLSHLGVgdSVRIDLSIVRGLAYYTGFVFEAFeasgagRALAGGGR-------YDDL 309
Cdd:TIGR00442 220 --LDFLCEESR-AHFEE---LKELLDALGI--PYKIDPSLVRGLDYYTGTVFEFV------TDDLGAQGsicgggrYDGL 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 310 VQKLGGPAMPAVGFAMGDVTLADLLQEKSIDLEPPAKAD-FVCVIgGVEEQCFALQDVACLRHLGYRVEYPLKSQNFGKQ 388
Cdd:TIGR00442 286 VEELGGPPTPAVGFAIGIERLILLLEELGLIPPPSKKPDvYVVPL-GEEAELEALKLAQKLRKAGIRVEVDLGGRKLKKQ 364
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1519714025 389 LKAAVQSGASFALIYGSEEREQGVVRVRDLRTATELVLPR 428
Cdd:TIGR00442 365 LKYADKLGARFALIIGEDELENGTVTLKDLETGEQETVPL 404
|
|
| PLN02530 |
PLN02530 |
histidine-tRNA ligase |
7-431 |
2.33e-103 |
|
histidine-tRNA ligase
Pssm-ID: 178145 [Multi-domain] Cd Length: 487 Bit Score: 316.30 E-value: 2.33e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 7 PGFRDFLPDACSARNSIFDHWRLAAESFNFQEYDAPVLEPLELFIEKSGEEIVGQLFNFTDRGDRSVALRPEMTPTLARL 86
Cdd:PLN02530 74 KGTRDFPPEDMRLRNWLFDHFREVSRLFGFEEVDAPVLESEELYIRKAGEEITDQLYNFEDKGGRRVALRPELTPSLARL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 87 VGARANSLKRPVKWFTIGEHYRYERPQKGRLRAFYQFNADILGESGPGADAELIALLAHTLRSFGLAADDFVIRLSDRNL 166
Cdd:PLN02530 154 VLQKGKSLSLPLKWFAIGQCWRYERMTRGRRREHYQWNMDIIGVPGVEAEAELLAAIVTFFKRVGITSSDVGIKVSSRKV 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 167 WWSILAAEDLETEKAIEVLGIIDKMDRMGRERLLEKLaDAVGSRAgEVCARIDAVREIRDFAALESMIrslpleGASAEA 246
Cdd:PLN02530 234 LQAVLKSYGIPEESFAPVCVIVDKLEKLPREEIEKEL-DTLGVSE-EAIEGILDVLSLKSLDDLEALL------GADSEA 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 247 lharVEDWRCLMELLSHLGVGDSVRIDLSIVRGLAYYTGFVFEAFEASGAGRALAGGGRYDDLVQKLGGPAMPAVGFAMG 326
Cdd:PLN02530 306 ----VADLKQLFSLAEAYGYQDWLVFDASVVRGLAYYTGIVFEGFDRAGKLRAICGGGRYDRLLSTFGGEDTPACGFGFG 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 327 DVTLADLLQEKSIDLEPPAKADFVCVIGGVEEQCFALQDVACLRHLGYRVEYPLKSQNFGKQLKAAVQSGASFALIYGSE 406
Cdd:PLN02530 382 DAVIVELLKEKGLLPELPHQVDDVVFALDEDLQGAAAGVASRLREKGRSVDLVLEPKKLKWVFKHAERIGAKRLVLVGAS 461
|
410 420
....*....|....*....|....*
gi 1519714025 407 EREQGVVRVRDLRTATELVLPREKL 431
Cdd:PLN02530 462 EWERGMVRVKDLSSGEQTEVKLDEL 486
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
17-335 |
6.57e-67 |
|
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: 214.77 E-value: 6.57e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 17 CSARNSIFDHWRLAAESFNFQEYDAPVLEPLELFIEKSGEEIVGQLFNFTDRGDRSVALRPEMTPTLARLVGARANSLKR 96
Cdd:cd00773 2 AALRRYIEDTLREVFERYGYEEIDTPVFEYTELFLRKSGDEVSKEMYRFKDKGGRDLALRPDLTAPVARAVAENLLSLPL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 97 PVKWFTIGEHYRYERPQKGRLRAFYQFNADILGESGPGADAELIALLAHTLRSFGLaaDDFVIRLSDRNLWWSILAAEDL 176
Cdd:cd00773 82 PLKLYYIGPVFRYERPQKGRYREFYQVGVEIIGSDSPLADAEVIALAVEILEALGL--KDFQIKINHRGILDGIAGLLED 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 177 ETEKaievlgiidkmdrmgRERLLEKLADAvgsragevcaridavrEIRDFAALEsmirslplegasaealharvedwrc 256
Cdd:cd00773 160 REEY---------------IERLIDKLDKE----------------ALAHLEKLL------------------------- 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 257 lmELLSHLGVGDSVRIDLSIVRGLAYYTGFVFEAF-EASGAGRALAGGGRYDDLVQKLGGPAMPAVGFAMGDVTLADLLQ 335
Cdd:cd00773 184 --DYLEALGVDIKYSIDLSLVRGLDYYTGIVFEAVaDGLGAQGSIAGGGRYDGLLEEFGGEDVPAVGFAIGLERLLLALE 261
|
|
| PRK12420 |
PRK12420 |
histidyl-tRNA synthetase; Provisional |
1-427 |
1.73e-52 |
|
histidyl-tRNA synthetase; Provisional
Pssm-ID: 237097 [Multi-domain] Cd Length: 423 Bit Score: 181.85 E-value: 1.73e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 1 MEFETLPGFRDFLPDACSARNSIFDHWRLAAESFNFQEYDAPVLEPLELFIEK--SGEEIVGQLFNFTDRGDRSVALRPE 78
Cdd:PRK12420 2 MEMRNVKGTKDYLPEEQVLRNKIKRALEDVFERYGCKPLETPTLNMYELMSSKygGGDEILKEIYTLTDQGKRDLALRYD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 79 MTPTLARLVGARANsLKRPVKWFTIGEHYRYERPQKGRLRAFYQFNADILGESGPGADAELIALLAHTLRSFGLaadDFV 158
Cdd:PRK12420 82 LTIPFAKVVAMNPN-IRLPFKRYEIGKVFRDGPIKQGRFREFIQCDVDIVGVESVMAEAELMSMAFELFRRLNL---EVT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 159 IRLSDRNLWWSILAAEDLETEKAIEVLGIIDKMDRMGRERLLEKLADAVGSraGEVCARIDAVREIRDFAALESmIRSLP 238
Cdd:PRK12420 158 IQYNNRKLLNGILQAIGIPTELTSDVILSLDKIEKIGIDGVRKDLLERGIS--EEMADTICNTVLSCLQLSIAD-FKEAF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 239 LEGASAEAlharVEDWRCLMELLSHLGVGDSVRIDLSIVRGLAYYTGFVFEAFEASGAGRALAGGG-RYDDLVQKLGGP- 316
Cdd:PRK12420 235 NNPLVAEG----VNELQQLQQYLIALGINENCIFNPFLARGLTMYTGTVYEIFLKDGSITSSIGSGgRYDNIIGAFRGDd 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 317 -AMPAVGFAMG-DVTLADLLQEKsidlEPPAKADFVCVIGGVEEQCFALQDvACLRHLGYRVEYPLKSQNFGKQLKAAVQ 394
Cdd:PRK12420 311 mNYPTVGISFGlDVIYTALSQKE----TISSTADVFIIPLGTELQCLQIAQ-QLRSTTGLKVELELAGRKLKKALNYANK 385
|
410 420 430
....*....|....*....|....*....|...
gi 1519714025 395 SGASFALIYGSEEREQGVVRVRDLRTATELVLP 427
Cdd:PRK12420 386 ENIPYVLIIGEEEVSTGTVMLRNMKEGSEVKVP 418
|
|
| hisZ_biosyn_reg |
TIGR00443 |
ATP phosphoribosyltransferase, regulatory subunit; Apparant second copies of histidyl-tRNA ... |
10-326 |
1.61e-44 |
|
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: 157.78 E-value: 1.61e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 10 RDFLPDACSARNSIFDHWRLAAESFNFQEYDAPVLEPLELFIEKSGEEiVGQLFNFTDRGDRSVALRPEMTPTLARLVGA 89
Cdd:TIGR00443 1 RDLLPEEAARKEEIERQLQDVFRSWGYQEIITPTLEYLDTLSAGSGIL-NEDLFKLFDQLGRVLGLRPDMTAPIARLVST 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 90 RANSLKRPVKWFTIGEHYRYERPQKGRLRAFYQFNADILGESGPGADAELIALLAHTLRSFGLaaDDFVIRLSDRNLWWS 169
Cdd:TIGR00443 80 RLRDRPLPLRLCYAGNVFRTNESGGGRSREFTQAGVELIGAGGPAADAEVIALLIEALKALGL--KDFKIELGHVGLVRA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 170 ILAAEDLETEKAIEVLGIIDKMDRMGRERLLEKLadavgSRAGEVCARIDAVREIR-DFAALESMIRSLPLEGASAEALh 248
Cdd:TIGR00443 158 LLEEAGLPEEAREALREALARKDLVALEELVAEL-----GLSPEVRERLLALPRLRgDGEEVLEEARALAGSETAEAAL- 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1519714025 249 arvEDWRCLMELLSHLGVGDSVRIDLSIVRGLAYYTGFVFEAFEaSGAGRALAGGGRYDDLVQKLGGPAmPAVGFAMG 326
Cdd:TIGR00443 232 ---DELEAVLELLEARGVEEYISLDLGLVRGYHYYTGLIFEGYA-PGLGAPLAGGGRYDELLGRFGRPL-PATGFALN 304
|
|
| HisZ |
COG3705 |
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism]; |
13-325 |
1.75e-44 |
|
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism];
Pssm-ID: 442919 [Multi-domain] Cd Length: 312 Bit Score: 157.65 E-value: 1.75e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 13 LPDACSARNSIFDHWRLAAESFNFQEYDAPVLEPLELFIEKSGEEIVGQLFNFTDRGDRSVALRPEMTPTLARLVGARAN 92
Cdd:COG3705 1 LPEEAARKEELRRRLLDVFRSWGYELVEPPLLEYLDSLLTGSGADLDLQTFKLVDQLGRTLGLRPDMTPQVARIAATRLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 93 SLKRPVKWFTIGEHYRYERPQKGRLRAFYQFNADILGESGPGADAELIALLAHTLRSFGLaaDDFVIRLSDRNLWWSILA 172
Cdd:COG3705 81 NRPGPLRLCYAGNVFRTRPSGLGRSREFLQAGAELIGHAGLEADAEVIALALEALKAAGL--EDFTLDLGHVGLFRALLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 173 AEDLETEKAIEVLGIIDKMDRMGRERLLEKLADavgsrAGEVCARIDAVREIR-DFAALESmIRSLPLEGASAEALharv 251
Cdd:COG3705 159 ALGLSEEQREELRRALARKDAVELEELLAELGL-----SEELAEALLALPELYgGEEVLAR-ARALLLDAAIRAAL---- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 252 EDWRCLMELLSHLGVGDSVRIDLSIVRGLAYYTGFVFEAFeasgagrALAGGGR------YDDLVQKLGGPaMPAVGFAM 325
Cdd:COG3705 229 DELEALAEALAARGPDVRLTFDLSELRGYDYYTGIVFEAY-------APGVGDPlarggrYDGLLAAFGRA-RPATGFSL 300
|
|
| syh |
CHL00201 |
histidine-tRNA synthetase; Provisional |
4-420 |
1.01e-41 |
|
histidine-tRNA synthetase; Provisional
Pssm-ID: 164576 [Multi-domain] Cd Length: 430 Bit Score: 153.13 E-value: 1.01e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 4 ETLPGFRDFLPDACSARNSIFDHWRLAAESFNFQEYDAPVLEPLELFIEKSGE--EIVG-QLFNFTDRGDRSVALRPEMT 80
Cdd:CHL00201 5 QAIRGTKDILPDEINYWQFIHDKALTLLSLANYSEIRTPIFENSSLYDRGIGEttDIVNkEMYRFTDRSNRDITLRPEGT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 81 PTLAR-LVGARA---NSLKRpvKWFTiGEHYRYERPQKGRLRAFYQFNADILGESGPGADAELIALLAHTLRSfgLAADD 156
Cdd:CHL00201 85 AGIVRaFIENKMdyhSNLQR--LWYS-GPMFRYERPQSGRQRQFHQLGIEFIGSIDARADTEVIHLAMQIFNE--LQVKN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 157 FVIRLSdrnlwwSILAAEDLETEKA--IEVLG-IIDKMDRMGRERLLE---KLADAVGSRAGEVcarIDAVREIRDFAAL 230
Cdd:CHL00201 160 LILDIN------SIGKLEDRQSYQLklVEYLSqYQDDLDTDSQNRLYSnpiRILDSKNLKTQEI---LDGAPKISDFLSL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 231 ESMirslplegasaealharvEDWRCLMELLSHLGVgdSVRIDLSIVRGLAYYTGFVFE-AFEASGAGRALAGGGRYDDL 309
Cdd:CHL00201 231 EST------------------EHFYDVCTYLNLLNI--PYKINYKLVRGLDYYNDTAFEiKTLSSNGQDTICGGGRYDSL 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 310 VQKLGGPAMPAVGFAMGDVTLAdLLQEKSIDLePPAKADFVCVIGGVEEQCFALQDVACLRHLGYRVEYPLKSQNFGKQL 389
Cdd:CHL00201 291 IHQLGGPKTPAVGCAIGLERLL-LIAKDNIIL-PKQSIDVYIATQGLKAQKKGWEIIQFLEKQNIKFELDLSSSNFHKQI 368
|
410 420 430
....*....|....*....|....*....|.
gi 1519714025 390 KAAVQSGASFALIYGSEEREQGVVRVRDLRT 420
Cdd:CHL00201 369 KQAGKKRAKACIILGDNEIMDNCITIKWLDE 399
|
|
| hisZ |
PRK12292 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
1-396 |
7.53e-38 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 237043 [Multi-domain] Cd Length: 391 Bit Score: 141.93 E-value: 7.53e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 1 MEFEtLP-GFRDFLPDACSARNSIFDhwRLAA--ESFNFQEYDAPVLEPLELFIEKSGEEIVGQLFNFTDRG-DRSVALR 76
Cdd:PRK12292 1 MMWQ-LPeGIRDLLPEEARKIEEIRR--RLLDlfRRWGYEEVITPTLEYLDTLLAGGGAILDLRTFKLVDQLsGRTLGLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 77 PEMTPTLARLVGARANSLKRPVKWFTIGEHYRYERPQKGRLRAFYQFNADILGESGPGADAELIALLAHTLRSFGLaaDD 156
Cdd:PRK12292 78 PDMTAQIARIAATRLANRPGPLRLCYAGNVFRAQERGLGRSREFLQSGVELIGDAGLEADAEVILLLLEALKALGL--PN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 157 FVIRLSDRNLWWSILAAEDLETEKAIEVLGIIDKMDRMGRERLLEKLADAVGSRA---------GEVCARIdavreirdf 227
Cdd:PRK12292 156 FTLDLGHVGLFRALLEAAGLSEELEEVLRRALANKDYVALEELVLDLSEELRDALlalprlrggREVLEEA--------- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 228 aalesmiRSLPLegaSAEALHArVEDWRCLMELLSHLGVGDSVRIDLSIVRGLAYYTGFVFEAFeASGAGRALAGGGRYD 307
Cdd:PRK12292 227 -------RKLLP---SLPIKRA-LDELEALAEALEKYGYGIPLSLDLGLLRHLDYYTGIVFEGY-VDGVGNPIASGGRYD 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 308 DLVQKLGGPAmPAVGFAMGDVTLADLLQEksidlEPPAKADFVCVIGGVEEQCFALQDVACLRHLGYRVEYPLKSQNFGK 387
Cdd:PRK12292 295 DLLGRFGRAR-PATGFSLDLDRLLELQLE-----LPVEARKDLVIAPDSEALAAALAAAQELRKKGEIVVLALPGRNFED 368
|
....*....
gi 1519714025 388 QLKAAVQSG 396
Cdd:PRK12292 369 AREYARDRQ 377
|
|
| tRNA-synt_His |
pfam13393 |
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ... |
8-325 |
3.75e-35 |
|
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: 132.32 E-value: 3.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 8 GFRDFLPDACSARNSIFDHWRLAAESFNFQEYDAPVLEPLELFIEKSGEEIvGQLFNFTDRGDRSVALRPEMTPTLARLV 87
Cdd:pfam13393 1 GIRDLLPPEARRIEELRRRLLDLFRSWGYELVMPPLLEYLDSLLTGTGADL-DQTFKLVDQSGRLLGLRADITPQVARID 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 88 GARANSlKRPVKWFTIGEHYRYERPQKGRLRAFYQFNADILGESGPGADAELIALLAHTLRSFGLaaDDFVIRLSDRNLW 167
Cdd:pfam13393 80 AHRLNR-PGPLRLCYAGSVLRTRPKGLGRSREPLQVGAELIGHAGIEADAEIISLLLEALAAAGV--PGVTLDLGHVGLV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 168 WSILAAEDLETEKAIEVLGIIDKMDRMGrerlLEKLADAVGSRAgEVCARIDAVREIR-DFAALESMIRSLPLEGASAEA 246
Cdd:pfam13393 157 RALLEAAGLSEALEEALRAALQRKDAAE----LAELAAEAGLPP-ALRRALLALPDLYgGPEVLDEARAALPGLPALQEA 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1519714025 247 LHarveDWRCLMELLSHLGVGDSVRIDLSIVRGLAYYTGFVFEAFeASGAGRALAGGGRYDDLVQKLGGPAmPAVGFAM 325
Cdd:pfam13393 232 LD----ELEALAALLEALGDGVRLTFDLAELRGYEYYTGIVFAAY-APGVGEPLARGGRYDDLGAAFGRAR-PATGFSL 304
|
|
| PLN02972 |
PLN02972 |
Histidyl-tRNA synthetase |
8-428 |
1.20e-34 |
|
Histidyl-tRNA synthetase
Pssm-ID: 215525 [Multi-domain] Cd Length: 763 Bit Score: 136.94 E-value: 1.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 8 GFRDFLPDACSARNSIFDHWRLAAESFNFQEYDAPVLEPLELFIEKSGEEiVGQLFNFTDRGDRSVALRPEMTPTLARLV 87
Cdd:PLN02972 332 GTRDFAKEQMAIREKAFSIITSVFKRHGATALDTPVFELRETLMGKYGED-SKLIYDLADQGGELCSLRYDLTVPFARYV 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 88 GARA-NSLKRpvkwFTIGEHYRYERPQKGRLRAFYQFNADILGESGP-GADAELIALLAHTLRSFGLAadDFVIRLSDRN 165
Cdd:PLN02972 411 AMNGiTSFKR----YQIAKVYRRDNPSKGRYREFYQCDFDIAGVYEPmGPDFEIIKVLTELLDELDIG--TYEVKLNHRK 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 166 LWWSILAAEDLETEKAIEVLGIIDKMDRMGRERLLEKLADAVGsRAGEVCARIDAVREIRDfAALEsMIRSLPLEGA--- 242
Cdd:PLN02972 485 LLDGMLEICGVPPEKFRTICSSIDKLDKQSFEQVKKEMVEEKG-LSNETADKIGNFVKERG-PPLE-LLSKLRQEGSefl 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 243 ----SAEALharvEDWRCLMELLSHLGVGDSVRIDLSIVRGLAYYTGFVFEAFEASGAGRALAGGGRYDDLVQKLGGPAM 318
Cdd:PLN02972 562 gnasSRAAL----DELEIMFKALEKSKAIGKIVFDLSLARGLDYYTGVIYEAVFKGAQVGSIAAGGRYDNLVGMFSGKQV 637
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 319 PAVGFAMGD---VTLADLLQEKSIDLEPPAKADFVCVIGGVEEQCFALQDVACLRHLGYRVEYPLkSQNFGKQLKAAVQS 395
Cdd:PLN02972 638 PAVGVSLGIervFAIMEQQEEEKSQVIRPTETEVLVSIIGDDKLALAAELVSELWNAGIKAEYKV-STRKAKHLKRAKES 716
|
410 420 430
....*....|....*....|....*....|...
gi 1519714025 396 GASFALIYGSEEREQGVVRVRDLRTATELVLPR 428
Cdd:PLN02972 717 GIPWMVLVGEKELSKGFVKLKNLEAGVEEEVDR 749
|
|
| hisZ |
PRK12295 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
35-325 |
2.57e-19 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 183413 [Multi-domain] Cd Length: 373 Bit Score: 89.22 E-value: 2.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 35 NFQEYDAPVLEPLELFIEKSGEEIVGQLFNFTDRGDRSVALRPEMTPTLARLVgaRANSLKRPVKWFTIGEHYRYerpQK 114
Cdd:PRK12295 22 GAVRVDPPILQPAEPFLDLSGEDIRRRIFVTSDENGEELCLRPDFTIPVCRRH--IATAGGEPARYAYLGEVFRQ---RR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 115 GRLRAFYQFNADILGESGP-GADAELIALLAHTLRSFGLAadDFVIRLSD----------------------RNLWWSIL 171
Cdd:PRK12295 97 DRASEFLQAGIESFGRADPaAADAEVLALALEALAALGPG--DLEVRLGDvglfaalvdalglppgwkrrllRHFGRPRS 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 172 AAEDLETEKAIEVLGIIDKMDRM--------------------------GR------ERLLEKLADA-VGSRAGEVCARI 218
Cdd:PRK12295 175 LDALLARLAGPRVDPLDEHAGVLaaladeaaaralvedlmsiagispvgGRspaeiaRRLLEKAALAaAARLPAEALAVL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 219 DAVREIRD-----FAALESMIRSLPLegasaeALHARVEDWRCLMELLSHLGVG-DSVRIDLSIVRGLAYYTGFVFEAFE 292
Cdd:PRK12295 255 ERFLAISGppdaaLAALRALAADAGL------DLDAALDRFEARLAALAARGIDlERLRFSASFGRPLDYYTGFVFEIRA 328
|
330 340 350
....*....|....*....|....*....|....
gi 1519714025 293 ASGAGRALAGGGRYDDLVQKLGGPA-MPAVGFAM 325
Cdd:PRK12295 329 AGNGDPPLAGGGRYDGLLTRLGAGEpIPAVGFSI 362
|
|
| HisRS_anticodon |
cd00859 |
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases ... |
349-435 |
8.18e-16 |
|
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: 72.57 E-value: 8.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 349 FVCVIGGvEEQCFALQDVACLRHLGYRVEYPLKSQNFGKQLKAAVQSGASFALIYGSEEREQGVVRVRDLRTATELVLPR 428
Cdd:cd00859 5 YVVPLGE-GALSEALELAEQLRDAGIKAEIDYGGRKLKKQFKYADRSGARFAVILGEDELAAGVVTVKDLETGEQETVAL 83
|
....*..
gi 1519714025 429 EKLASAV 435
Cdd:cd00859 84 DELVEEL 90
|
|
| PRK12421 |
PRK12421 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
42-383 |
3.35e-11 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 237098 Cd Length: 392 Bit Score: 64.61 E-value: 3.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 42 PVLEPLELFIEKSGEEIVGQLFNFTDR-GDRSVALRPEMTPTLARlVGARANSLKRPVKWFTIGeHYRYERPQK-GRLRA 119
Cdd:PRK12421 46 PLIEYLESLLTGAGQDLKLQTFKLIDQlSGRLMGVRADITPQVAR-IDAHLLNREGVARLCYAG-SVLHTLPQGlFGSRT 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 120 FYQFNADILGESGPGADAELIALLAHTLRSFGLAADDfvIRLSDRNLWWSILAAEDLETEKAIEVLGIIDKMDRMGRERL 199
Cdd:PRK12421 124 PLQLGAELYGHAGIEADLEIIRLMLGLLRNAGVPALH--LDLGHVGIFRRLAELAGLSPEEEEELFDLLQRKALPELAEV 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 200 LEKLAdaVGSRAGEVCARIdaVREIRDFAALESMIRSLPLEGAsaeALHARVEDWRCLMELLSHLGVGDSVRIDLSIVRG 279
Cdd:PRK12421 202 CQNLG--VGSDLRRMFYAL--ARLNGGLEALDRALSVLALQDA---AIRQALDELKTLAAHLKNRWPELPVSIDLAELRG 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 280 LAYYTGFVFEAFeASGAGRALAGGGRYDDlVQKLGGPAMPAVGFAMgdvTLADLLQEKSIDLEPPAkadfvcVIGGVEEQ 359
Cdd:PRK12421 275 YHYHTGLVFAAY-IPGRGQALARGGRYDG-IGEAFGRARPATGFSM---DLKELLALQFLEEEAGA------ILAPWGDD 343
|
330 340
....*....|....*....|....
gi 1519714025 360 CFALQDVACLRHLGYRVEYPLKSQ 383
Cdd:PRK12421 344 PDLLAAIAELRQQGERVVQLLPGD 367
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
351-435 |
4.07e-08 |
|
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: 50.66 E-value: 4.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 351 CVIGGVEEQCFALQDVAC-----LRHLGYRVEYPLKSQNFGKQLKAAVQSGASFALIYGSEEREQGVVRVRDLRTATELV 425
Cdd:pfam03129 2 VVVIPLGEKAEELEEYAQklaeeLRAAGIRVELDDRNESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQET 81
|
90
....*....|
gi 1519714025 426 LPREKLASAV 435
Cdd:pfam03129 82 VSLDELVEKL 91
|
|
| 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 ... |
35-164 |
1.32e-07 |
|
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: 52.39 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 35 NFQEYDAPVLEPLELFiEKSG--EEIVGQLFNFTDRG----DRSVALRPEMTPTLARLVGARANSLKRPVKWFT-IGEHY 107
Cdd:cd00670 20 GYQEILFPFLAPTVLF-FKGGhlDGYRKEMYTFEDKGrelrDTDLVLRPAACEPIYQIFSGEILSYRALPLRLDqIGPCF 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1519714025 108 RYERPQ---KGRLRAFYQFNADILG--ESGPGADAELIALLAHTLRSFGLaadDFVIRLSDR 164
Cdd:cd00670 99 RHEPSGrrgLMRVREFRQVEYVVFGepEEAEEERREWLELAEEIARELGL---PVRVVVADD 157
|
|
| pylS |
PRK09537 |
pyrrolysine--tRNA(Pyl) ligase; |
36-159 |
1.50e-06 |
|
pyrrolysine--tRNA(Pyl) ligase;
Pssm-ID: 236555 [Multi-domain] Cd Length: 417 Bit Score: 50.22 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 36 FQEYDAPVLEPLElFIEKSG----EEIVGQLFnftdRGDRSVALRPEMTPTLARLVGARANSLKRPVKWFTIGEHYRYER 111
Cdd:PRK09537 222 FLEIKSPILIPAE-YIERMGidndTELSKQIF----RVDKNFCLRPMLAPGLYNYLRKLDRILPDPIKIFEIGPCYRKES 296
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1519714025 112 PQKGRLRAFYQFNadiLGESGPGADAE-LIALLAHTLRSFGLaadDFVI 159
Cdd:PRK09537 297 DGKEHLEEFTMVN---FCQMGSGCTREnLENIIDDFLKHLGI---DYEI 339
|
|
| HGTP_anticodon |
cd00738 |
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ... |
369-431 |
4.03e-06 |
|
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: 45.08 E-value: 4.03e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1519714025 369 LRHLGYRVEYPLKSQNFGKQLKAAVQSGASFALIYGSEEREQGVVRVRDLRTATELVLPREKL 431
Cdd:cd00738 27 LLANGIRVLYDDRERKIGKKFREADLRGVPFAVVVGEDELENGKVTVKSRDTGESETLHVDEL 89
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
63-162 |
8.08e-06 |
|
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: 46.25 E-value: 8.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714025 63 FNFTDRGDRSVALRPEMTPTLARLVGAR-ANSLKRPVKWFTIGEHYRYERP--QKG--RLRAFYQFNADI--LGESGPGA 135
Cdd:pfam00587 1 YKVEDENGDELALKPTNEPGHTLLFREEgLRSKDLPLKLAQFGTCFRHEASgdTRGliRVRQFHQDDAHIfhAPGQSPDE 80
|
90 100
....*....|....*....|....*..
gi 1519714025 136 DAELIALLAHTLRSFGLAAddFVIRLS 162
Cdd:pfam00587 81 LEDYIKLIDRVYSRLGLEV--RVVRLS 105
|
|
| |
