|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02972 |
PLN02972 |
Histidyl-tRNA synthetase |
1-363 |
9.53e-123 |
|
Histidyl-tRNA synthetase
Pssm-ID: 215525 [Multi-domain] Cd Length: 763 Bit Score: 371.53 E-value: 9.53e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561263 1 MNKLKKMKRYQVGKVWRRESPAiaQGRYREFCQCDFDIAGEFDPMIPDAECLRIMCEILSGLQLGDFLIKVNDRRVVDGI 80
Cdd:PLN02972 412 MNGITSFKRYQIAKVYRRDNPS--KGRYREFYQCDFDIAGVYEPMGPDFEIIKVLTELLDELDIGTYEVKLNHRKLLDGM 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561263 81 FAVCGVPESKLRTICSSMDKLDKMSWEGVRHEMVAKKGLAPEVADRIGDFVQYHGG-ISLVEDLFK-DPRLSQSQLALQG 158
Cdd:PLN02972 490 LEICGVPPEKFRTICSSIDKLDKQSFEQVKKEMVEEKGLSNETADKIGNFVKERGPpLELLSKLRQeGSEFLGNASSRAA 569
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561263 159 LGDLKLLFEYLRLFGIADKISLDLSLARGLDYYTGVIYEAVLLESpaqagketlSVGSVAAGGRYDNLVAQFDPKghHVP 238
Cdd:PLN02972 570 LDELEIMFKALEKSKAIGKIVFDLSLARGLDYYTGVIYEAVFKGA---------QVGSIAAGGRYDNLVGMFSGK--QVP 638
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561263 239 CVGLSIGVERIFYLVEQKMKMSGEKVRTTETQVFVATPQKNFLQERLKIIAELWDAGIKAEmlYKNNPKLLTQLHYCEKA 318
Cdd:PLN02972 639 AVGVSLGIERVFAIMEQQEEEKSQVIRPTETEVLVSIIGDDKLALAAELVSELWNAGIKAE--YKVSTRKAKHLKRAKES 716
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 755561263 319 DIPLMVIIGEQERNEGVIKLRSVASREEVTINRESLVAEIQKRLS 363
Cdd:PLN02972 717 GIPWMVLVGEKELSKGFVKLKNLEAGVEEEVDRTCFVQELKAELL 761
|
|
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
8-364 |
1.33e-79 |
|
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: 249.65 E-value: 1.33e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561263 8 KRYQVGKVWRRESPAiaQGRYREFCQCDFDIAGEFDPMIpDAECLRIMCEILSGLQLGDFLIKVNDRrvvdgifavcGVP 87
Cdd:COG0124 101 KLYYIGPVFRYERPQ--KGRYRQFHQFGVEVIGSDSPLA-DAEVIALAADLLKALGLKDFTLEINSR----------GLP 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561263 88 ESKLRTICSSMDKLDKMSWEGVrhemvakkgLAPEVADRI------------GDFVQyhggiSLVEDLfkdPRLSQSqLA 155
Cdd:COG0124 168 EERAEALLRYLDKLDKIGHEDV---------LDEDSQRRLetnplraildskGPDCQ-----EVLADA---PKLLDY-LG 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561263 156 LQGLGDLKLLFEYLRLFGIadKISLDLSLARGLDYYTGVIYEAVLLESPAQagketlsvGSVAAGGRYDNLVAQFDpkGH 235
Cdd:COG0124 230 EEGLAHFEEVLELLDALGI--PYVIDPRLVRGLDYYTGTVFEIVTDGLGAQ--------GSVCGGGRYDGLVEQLG--GP 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561263 236 HVPCVGLSIGVERIFYLVEQKmkmSGEKVRTTETQVFVATPQKNFLQERLKIIAELWDAGIKAEMLYKNNpKLLTQLHYC 315
Cdd:COG0124 298 PTPAVGFAIGLERLLLLLEEL---GLLPAAEPPPDVYVVPLGEEARAEALKLAQELRAAGIRVELDLGGR-KLKKQLKYA 373
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 755561263 316 EKADIPLMVIIGEQERNEGVIKLRSVASREEVTINRESLVAEIQKRLSE 364
Cdd:COG0124 374 DKSGAPFVLILGEDELANGTVTLKDLATGEQETVPLDELVEYLKELLAE 422
|
|
| hisS |
TIGR00442 |
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ... |
8-351 |
9.99e-65 |
|
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: 210.80 E-value: 9.99e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561263 8 KRYQVGKVWRRESPaiaQ-GRYREFCQCDFDIAGEFDPMIpDAECLRIMCEILSGLQLGDFLIKVNDRRVVDGIFAvcgv 86
Cdd:TIGR00442 99 KLYYIGPMFRYERP---QkGRYRQFHQFGVEVIGSDSPLA-DAEIIALAADILKELGLKDFTLEINSLGILEGRLE---- 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561263 87 pesKLRTICSSMDK-LDKMSWEGVRHEMVAKKGLAPEVADRIGDFVQyhGGISLVEDLFKDprlsqsqlalqGLGDLKLL 165
Cdd:TIGR00442 171 ---YREALIRYLDKhKDKLGEDSVRRLEKNPLRILDSKNEKIQELLK--NAPKILDFLCEE-----------SRAHFEEL 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561263 166 FEYLRLFGIadKISLDLSLARGLDYYTGVIYEAVLLESPAQagketlsvGSVAAGGRYDNLVAQFDpkGHHVPCVGLSIG 245
Cdd:TIGR00442 235 KELLDALGI--PYKIDPSLVRGLDYYTGTVFEFVTDDLGAQ--------GSICGGGRYDGLVEELG--GPPTPAVGFAIG 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561263 246 VERIFYLVEQKmkmSGEKVRTTETQVFVATPQKNFLQERLKIIAELWDAGIKAEMLYKNNpKLLTQLHYCEKADIPLMVI 325
Cdd:TIGR00442 303 IERLILLLEEL---GLIPPPSKKPDVYVVPLGEEAELEALKLAQKLRKAGIRVEVDLGGR-KLKKQLKYADKLGARFALI 378
|
330 340
....*....|....*....|....*.
gi 755561263 326 IGEQERNEGVIKLRSVASREEVTINR 351
Cdd:TIGR00442 379 IGEDELENGTVTLKDLETGEQETVPL 404
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
8-254 |
1.98e-58 |
|
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: 190.12 E-value: 1.98e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561263 8 KRYQVGKVWRRESPAiaQGRYREFCQCDFDIAGEfDPMIPDAECLRIMCEILSGLQLGDFLIKVNDRRVVDGIFAVCGVP 87
Cdd:cd00773 84 KLYYIGPVFRYERPQ--KGRYREFYQVGVEIIGS-DSPLADAEVIALAVEILEALGLKDFQIKINHRGILDGIAGLLEDR 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561263 88 EsklRTICSSMDKLDKmswegvrhemvakkglapevadrigdfvqyhggislvedlfkdprlsqsqlalQGLGDLKLLFE 167
Cdd:cd00773 161 E---EYIERLIDKLDK-----------------------------------------------------EALAHLEKLLD 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561263 168 YLRLFGIADKISLDLSLARGLDYYTGVIYEAVLLESPAQagketlsvGSVAAGGRYDNLVAQFDpkGHHVPCVGLSIGVE 247
Cdd:cd00773 185 YLEALGVDIKYSIDLSLVRGLDYYTGIVFEAVADGLGAQ--------GSIAGGGRYDGLLEEFG--GEDVPAVGFAIGLE 254
|
....*..
gi 755561263 248 RIFYLVE 254
Cdd:cd00773 255 RLLLALE 261
|
|
| tRNA-synt_His |
pfam13393 |
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ... |
13-249 |
3.66e-27 |
|
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: 109.21 E-value: 3.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561263 13 GKVWRReSPAIAqGRYREFCQCDFDIAGEFDPMiPDAECLRIMCEILSGLQLGDFLIKVNDRRVVDGIFAVCGVPESKLR 92
Cdd:pfam13393 95 GSVLRT-RPKGL-GRSREPLQVGAELIGHAGIE-ADAEIISLLLEALAAAGVPGVTLDLGHVGLVRALLEAAGLSEALEE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561263 93 TIcssMDKLDKMSWEGVRhEMVAKKGLAPEVADRIGDFVQYHGGISLVEDLFKdpRLSQSQLALQGLGDLKLLFEYLRLF 172
Cdd:pfam13393 172 AL---RAALQRKDAAELA-ELAAEAGLPPALRRALLALPDLYGGPEVLDEARA--ALPGLPALQEALDELEALAALLEAL 245
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755561263 173 GIADKISLDLSLARGLDYYTGVIYEAVLlespAQAGKEtlsvgsVAAGGRYDNLVAQFdpkGHHVPCVGLSIGVERI 249
Cdd:pfam13393 246 GDGVRLTFDLAELRGYEYYTGIVFAAYA----PGVGEP------LARGGRYDDLGAAF---GRARPATGFSLDLEAL 309
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02972 |
PLN02972 |
Histidyl-tRNA synthetase |
1-363 |
9.53e-123 |
|
Histidyl-tRNA synthetase
Pssm-ID: 215525 [Multi-domain] Cd Length: 763 Bit Score: 371.53 E-value: 9.53e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561263 1 MNKLKKMKRYQVGKVWRRESPAiaQGRYREFCQCDFDIAGEFDPMIPDAECLRIMCEILSGLQLGDFLIKVNDRRVVDGI 80
Cdd:PLN02972 412 MNGITSFKRYQIAKVYRRDNPS--KGRYREFYQCDFDIAGVYEPMGPDFEIIKVLTELLDELDIGTYEVKLNHRKLLDGM 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561263 81 FAVCGVPESKLRTICSSMDKLDKMSWEGVRHEMVAKKGLAPEVADRIGDFVQYHGG-ISLVEDLFK-DPRLSQSQLALQG 158
Cdd:PLN02972 490 LEICGVPPEKFRTICSSIDKLDKQSFEQVKKEMVEEKGLSNETADKIGNFVKERGPpLELLSKLRQeGSEFLGNASSRAA 569
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561263 159 LGDLKLLFEYLRLFGIADKISLDLSLARGLDYYTGVIYEAVLLESpaqagketlSVGSVAAGGRYDNLVAQFDPKghHVP 238
Cdd:PLN02972 570 LDELEIMFKALEKSKAIGKIVFDLSLARGLDYYTGVIYEAVFKGA---------QVGSIAAGGRYDNLVGMFSGK--QVP 638
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561263 239 CVGLSIGVERIFYLVEQKMKMSGEKVRTTETQVFVATPQKNFLQERLKIIAELWDAGIKAEmlYKNNPKLLTQLHYCEKA 318
Cdd:PLN02972 639 AVGVSLGIERVFAIMEQQEEEKSQVIRPTETEVLVSIIGDDKLALAAELVSELWNAGIKAE--YKVSTRKAKHLKRAKES 716
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 755561263 319 DIPLMVIIGEQERNEGVIKLRSVASREEVTINRESLVAEIQKRLS 363
Cdd:PLN02972 717 GIPWMVLVGEKELSKGFVKLKNLEAGVEEEVDRTCFVQELKAELL 761
|
|
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
8-364 |
1.33e-79 |
|
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: 249.65 E-value: 1.33e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561263 8 KRYQVGKVWRRESPAiaQGRYREFCQCDFDIAGEFDPMIpDAECLRIMCEILSGLQLGDFLIKVNDRrvvdgifavcGVP 87
Cdd:COG0124 101 KLYYIGPVFRYERPQ--KGRYRQFHQFGVEVIGSDSPLA-DAEVIALAADLLKALGLKDFTLEINSR----------GLP 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561263 88 ESKLRTICSSMDKLDKMSWEGVrhemvakkgLAPEVADRI------------GDFVQyhggiSLVEDLfkdPRLSQSqLA 155
Cdd:COG0124 168 EERAEALLRYLDKLDKIGHEDV---------LDEDSQRRLetnplraildskGPDCQ-----EVLADA---PKLLDY-LG 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561263 156 LQGLGDLKLLFEYLRLFGIadKISLDLSLARGLDYYTGVIYEAVLLESPAQagketlsvGSVAAGGRYDNLVAQFDpkGH 235
Cdd:COG0124 230 EEGLAHFEEVLELLDALGI--PYVIDPRLVRGLDYYTGTVFEIVTDGLGAQ--------GSVCGGGRYDGLVEQLG--GP 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561263 236 HVPCVGLSIGVERIFYLVEQKmkmSGEKVRTTETQVFVATPQKNFLQERLKIIAELWDAGIKAEMLYKNNpKLLTQLHYC 315
Cdd:COG0124 298 PTPAVGFAIGLERLLLLLEEL---GLLPAAEPPPDVYVVPLGEEARAEALKLAQELRAAGIRVELDLGGR-KLKKQLKYA 373
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 755561263 316 EKADIPLMVIIGEQERNEGVIKLRSVASREEVTINRESLVAEIQKRLSE 364
Cdd:COG0124 374 DKSGAPFVLILGEDELANGTVTLKDLATGEQETVPLDELVEYLKELLAE 422
|
|
| hisS |
TIGR00442 |
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ... |
8-351 |
9.99e-65 |
|
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: 210.80 E-value: 9.99e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561263 8 KRYQVGKVWRRESPaiaQ-GRYREFCQCDFDIAGEFDPMIpDAECLRIMCEILSGLQLGDFLIKVNDRRVVDGIFAvcgv 86
Cdd:TIGR00442 99 KLYYIGPMFRYERP---QkGRYRQFHQFGVEVIGSDSPLA-DAEIIALAADILKELGLKDFTLEINSLGILEGRLE---- 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561263 87 pesKLRTICSSMDK-LDKMSWEGVRHEMVAKKGLAPEVADRIGDFVQyhGGISLVEDLFKDprlsqsqlalqGLGDLKLL 165
Cdd:TIGR00442 171 ---YREALIRYLDKhKDKLGEDSVRRLEKNPLRILDSKNEKIQELLK--NAPKILDFLCEE-----------SRAHFEEL 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561263 166 FEYLRLFGIadKISLDLSLARGLDYYTGVIYEAVLLESPAQagketlsvGSVAAGGRYDNLVAQFDpkGHHVPCVGLSIG 245
Cdd:TIGR00442 235 KELLDALGI--PYKIDPSLVRGLDYYTGTVFEFVTDDLGAQ--------GSICGGGRYDGLVEELG--GPPTPAVGFAIG 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561263 246 VERIFYLVEQKmkmSGEKVRTTETQVFVATPQKNFLQERLKIIAELWDAGIKAEMLYKNNpKLLTQLHYCEKADIPLMVI 325
Cdd:TIGR00442 303 IERLILLLEEL---GLIPPPSKKPDVYVVPLGEEAELEALKLAQKLRKAGIRVEVDLGGR-KLKKQLKYADKLGARFALI 378
|
330 340
....*....|....*....|....*.
gi 755561263 326 IGEQERNEGVIKLRSVASREEVTINR 351
Cdd:TIGR00442 379 IGEDELENGTVTLKDLETGEQETVPL 404
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
8-254 |
1.98e-58 |
|
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: 190.12 E-value: 1.98e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561263 8 KRYQVGKVWRRESPAiaQGRYREFCQCDFDIAGEfDPMIPDAECLRIMCEILSGLQLGDFLIKVNDRRVVDGIFAVCGVP 87
Cdd:cd00773 84 KLYYIGPVFRYERPQ--KGRYREFYQVGVEIIGS-DSPLADAEVIALAVEILEALGLKDFQIKINHRGILDGIAGLLEDR 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561263 88 EsklRTICSSMDKLDKmswegvrhemvakkglapevadrigdfvqyhggislvedlfkdprlsqsqlalQGLGDLKLLFE 167
Cdd:cd00773 161 E---EYIERLIDKLDK-----------------------------------------------------EALAHLEKLLD 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561263 168 YLRLFGIADKISLDLSLARGLDYYTGVIYEAVLLESPAQagketlsvGSVAAGGRYDNLVAQFDpkGHHVPCVGLSIGVE 247
Cdd:cd00773 185 YLEALGVDIKYSIDLSLVRGLDYYTGIVFEAVADGLGAQ--------GSIAGGGRYDGLLEEFG--GEDVPAVGFAIGLE 254
|
....*..
gi 755561263 248 RIFYLVE 254
Cdd:cd00773 255 RLLLALE 261
|
|
| PRK12420 |
PRK12420 |
histidyl-tRNA synthetase; Provisional |
1-349 |
4.37e-58 |
|
histidyl-tRNA synthetase; Provisional
Pssm-ID: 237097 [Multi-domain] Cd Length: 423 Bit Score: 194.18 E-value: 4.37e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561263 1 MNKLKKM--KRYQVGKVWRrESPaIAQGRYREFCQCDFDIAGEFDPMiPDAECLRIMCEILSGLQLgDFLIKVNDRRVVD 78
Cdd:PRK12420 92 MNPNIRLpfKRYEIGKVFR-DGP-IKQGRFREFIQCDVDIVGVESVM-AEAELMSMAFELFRRLNL-EVTIQYNNRKLLN 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561263 79 GIFAVCGVPESKLRTICSSMDKLDKMSWEGVRHEmVAKKGLAPEVADRIGDFVQYHGGISLveDLFKDprLSQSQLALQG 158
Cdd:PRK12420 168 GILQAIGIPTELTSDVILSLDKIEKIGIDGVRKD-LLERGISEEMADTICNTVLSCLQLSI--ADFKE--AFNNPLVAEG 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561263 159 LGDLKLLFEYLRLFGIADKISLDLSLARGLDYYTGVIYEAVLlespaQAGKETLSVGSvaaGGRYDNLVAQFDPKGHHVP 238
Cdd:PRK12420 243 VNELQQLQQYLIALGINENCIFNPFLARGLTMYTGTVYEIFL-----KDGSITSSIGS---GGRYDNIIGAFRGDDMNYP 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561263 239 CVGLSIGVERIfylveqkMKMSGEKVRTTETQVFVATPQKNFLQErLKIIAELW-DAGIKAEMLYKNNpKLLTQLHYCEK 317
Cdd:PRK12420 315 TVGISFGLDVI-------YTALSQKETISSTADVFIIPLGTELQC-LQIAQQLRsTTGLKVELELAGR-KLKKALNYANK 385
|
330 340 350
....*....|....*....|....*....|..
gi 755561263 318 ADIPLMVIIGEQERNEGVIKLRSVASREEVTI 349
Cdd:PRK12420 386 ENIPYVLIIGEEEVSTGTVMLRNMKEGSEVKV 417
|
|
| hisZ_biosyn_reg |
TIGR00443 |
ATP phosphoribosyltransferase, regulatory subunit; Apparant second copies of histidyl-tRNA ... |
12-249 |
3.62e-33 |
|
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: 125.42 E-value: 3.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561263 12 VGKVWRRESPAIaqGRYREFCQCDFDIAGEfDPMIPDAECLRIMCEILSGLQLGDFLIKVNDRRVVDGIFAVCGVPESKL 91
Cdd:TIGR00443 93 AGNVFRTNESGG--GRSREFTQAGVELIGA-GGPAADAEVIALLIEALKALGLKDFKIELGHVGLVRALLEEAGLPEEAR 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561263 92 RTICSSMDKLDKMSWEgvrhEMVAKKGLAPEVADRIGDFVQYHGGISLVEDLFKdpRLSQSQLALQGLGDLKLLFEYLRL 171
Cdd:TIGR00443 170 EALREALARKDLVALE----ELVAELGLSPEVRERLLALPRLRGDGEEVLEEAR--ALAGSETAEAALDELEAVLELLEA 243
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755561263 172 FGIADKISLDLSLARGLDYYTGVIYEAVLLESPAQagketlsvgsVAAGGRYDNLVAQFdpkGHHVPCVGLSIGVERI 249
Cdd:TIGR00443 244 RGVEEYISLDLGLVRGYHYYTGLIFEGYAPGLGAP----------LAGGGRYDELLGRF---GRPLPATGFALNLERL 308
|
|
| PLN02530 |
PLN02530 |
histidine-tRNA ligase |
7-354 |
2.57e-30 |
|
histidine-tRNA ligase
Pssm-ID: 178145 [Multi-domain] Cd Length: 487 Bit Score: 120.62 E-value: 2.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561263 7 MKRYQVGKVWRRESpaIAQGRYREFCQCDFDIAGeFDPMIPDAECLRIMCEILS--GLQLGDFLIKVNDRRVVDGIFAVC 84
Cdd:PLN02530 165 LKWFAIGQCWRYER--MTRGRRREHYQWNMDIIG-VPGVEAEAELLAAIVTFFKrvGITSSDVGIKVSSRKVLQAVLKSY 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561263 85 GVPESKLRTICSSMDKLDKMSWEGVRHEMvAKKGLAPEVADRIGDFVQyhggISLVEDLfkdprlsqSQL---ALQGLGD 161
Cdd:PLN02530 242 GIPEESFAPVCVIVDKLEKLPREEIEKEL-DTLGVSEEAIEGILDVLS----LKSLDDL--------EALlgaDSEAVAD 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561263 162 LKLLFEYLRLFGIADKISLDLSLARGLDYYTGVIYEAVllespAQAGKetlsVGSVAAGGRYDNLVAQFDpkGHHVPCVG 241
Cdd:PLN02530 309 LKQLFSLAEAYGYQDWLVFDASVVRGLAYYTGIVFEGF-----DRAGK----LRAICGGGRYDRLLSTFG--GEDTPACG 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561263 242 LSIGVERIFYLVEQKMKMSgEKVRTTETQVFvatPQKNFLQ-ERLKIIAELWDAGIKAEMLYKNNpKLLTQLHYCEKADI 320
Cdd:PLN02530 378 FGFGDAVIVELLKEKGLLP-ELPHQVDDVVF---ALDEDLQgAAAGVASRLREKGRSVDLVLEPK-KLKWVFKHAERIGA 452
|
330 340 350
....*....|....*....|....*....|....
gi 755561263 321 PLMVIIGEQERNEGVIKLRSVASREEVTINRESL 354
Cdd:PLN02530 453 KRLVLVGASEWERGMVRVKDLSSGEQTEVKLDEL 486
|
|
| HisZ |
COG3705 |
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism]; |
25-249 |
6.05e-29 |
|
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism];
Pssm-ID: 442919 [Multi-domain] Cd Length: 312 Bit Score: 114.12 E-value: 6.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561263 25 QGRYREFCQC------DFDIAGefdpmipDAECLRIMCEILSGLQLGDFLIKVNDRRVVDGIFAVCGVPESKLRTICSSM 98
Cdd:COG3705 102 LGRSREFLQAgaeligHAGLEA-------DAEVIALALEALKAAGLEDFTLDLGHVGLFRALLEALGLSEEQREELRRAL 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561263 99 DKLDkmsWEGVRhEMVAKKGLAPEVADRIGDFVQYHGGISLVEDLFKdprLSQSQLALQGLGDLKLLFEYLRLFGIADKI 178
Cdd:COG3705 175 ARKD---AVELE-ELLAELGLSEELAEALLALPELYGGEEVLARARA---LLLDAAIRAALDELEALAEALAARGPDVRL 247
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755561263 179 SLDLSLARGLDYYTGVIYEAVLlespAQAGKEtlsvgsVAAGGRYDNLVAQFdpkGHHVPCVGLSIGVERI 249
Cdd:COG3705 248 TFDLSELRGYDYYTGIVFEAYA----PGVGDP------LARGGRYDGLLAAF---GRARPATGFSLDLDRL 305
|
|
| hisZ |
PRK12292 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
13-300 |
9.78e-28 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 237043 [Multi-domain] Cd Length: 391 Bit Score: 112.27 E-value: 9.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561263 13 GKVWR---RESpaiaqGRYREFCQCDFDIAGeFDPMIPDAECLRIMCEILSGLQLGDFLIKVNDRRVVDGIFAVCGVPES 89
Cdd:PRK12292 105 GNVFRaqeRGL-----GRSREFLQSGVELIG-DAGLEADAEVILLLLEALKALGLPNFTLDLGHVGLFRALLEAAGLSEE 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561263 90 KLRTICSSMDKLDKmswEGVRhEMVAkkGLAPEVADRIGDFVQYHGGISLVEDLfkdPRLSQSQLALQGLGDLKLLFEYL 169
Cdd:PRK12292 179 LEEVLRRALANKDY---VALE-ELVL--DLSEELRDALLALPRLRGGREVLEEA---RKLLPSLPIKRALDELEALAEAL 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561263 170 RLFGIADKISLDLSLARGLDYYTGVIYEAVLLESPAqagketlsvgSVAAGGRYDNLVAQFdpkGHHVPCVGLSIGVERI 249
Cdd:PRK12292 250 EKYGYGIPLSLDLGLLRHLDYYTGIVFEGYVDGVGN----------PIASGGRYDDLLGRF---GRARPATGFSLDLDRL 316
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 755561263 250 FYLVEQKmkmsgekvRTTETQVFVATPQKNFLQERLKIIAELWDAGIKAEM 300
Cdd:PRK12292 317 LELQLEL--------PVEARKDLVIAPDSEALAAALAAAQELRKKGEIVVL 359
|
|
| tRNA-synt_His |
pfam13393 |
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ... |
13-249 |
3.66e-27 |
|
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: 109.21 E-value: 3.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561263 13 GKVWRReSPAIAqGRYREFCQCDFDIAGEFDPMiPDAECLRIMCEILSGLQLGDFLIKVNDRRVVDGIFAVCGVPESKLR 92
Cdd:pfam13393 95 GSVLRT-RPKGL-GRSREPLQVGAELIGHAGIE-ADAEIISLLLEALAAAGVPGVTLDLGHVGLVRALLEAAGLSEALEE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561263 93 TIcssMDKLDKMSWEGVRhEMVAKKGLAPEVADRIGDFVQYHGGISLVEDLFKdpRLSQSQLALQGLGDLKLLFEYLRLF 172
Cdd:pfam13393 172 AL---RAALQRKDAAELA-ELAAEAGLPPALRRALLALPDLYGGPEVLDEARA--ALPGLPALQEALDELEALAALLEAL 245
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755561263 173 GIADKISLDLSLARGLDYYTGVIYEAVLlespAQAGKEtlsvgsVAAGGRYDNLVAQFdpkGHHVPCVGLSIGVERI 249
Cdd:pfam13393 246 GDGVRLTFDLAELRGYEYYTGIVFAAYA----PGVGEP------LARGGRYDDLGAAF---GRARPATGFSLDLEAL 309
|
|
| HisRS_anticodon |
cd00859 |
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases ... |
268-359 |
5.32e-26 |
|
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: 99.54 E-value: 5.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561263 268 ETQVFVATPQKNFLQERLKIIAELWDAGIKAEMLYKNnPKLLTQLHYCEKADIPLMVIIGEQERNEGVIKLRSVASREEV 347
Cdd:cd00859 1 EVDVYVVPLGEGALSEALELAEQLRDAGIKAEIDYGG-RKLKKQFKYADRSGARFAVILGEDELAAGVVTVKDLETGEQE 79
|
90
....*....|..
gi 755561263 348 TINRESLVAEIQ 359
Cdd:cd00859 80 TVALDELVEELK 91
|
|
| syh |
CHL00201 |
histidine-tRNA synthetase; Provisional |
2-360 |
1.45e-17 |
|
histidine-tRNA synthetase; Provisional
Pssm-ID: 164576 [Multi-domain] Cd Length: 430 Bit Score: 83.41 E-value: 1.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561263 2 NKLKKMKRYQ----VGKVWRRESPAiaQGRYREFCQCDFDIAGEFDPMiPDAECLRIMCEILSGLQLGDFLIKVN----- 72
Cdd:CHL00201 94 NKMDYHSNLQrlwySGPMFRYERPQ--SGRQRQFHQLGIEFIGSIDAR-ADTEVIHLAMQIFNELQVKNLILDINsigkl 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561263 73 -DRRVVdgifavcgvpESKLRTICSS-MDKLD-----KMSWEGVRhemvakkglapeVADRIGDFVQyhggislvEDLFK 145
Cdd:CHL00201 171 eDRQSY----------QLKLVEYLSQyQDDLDtdsqnRLYSNPIR------------ILDSKNLKTQ--------EILDG 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561263 146 DPRLSQSqLALQGLGDLKLLFEYLRLFGIADKIslDLSLARGLDYYTGVIYEAVLLESPAQagketlsvGSVAAGGRYDN 225
Cdd:CHL00201 221 APKISDF-LSLESTEHFYDVCTYLNLLNIPYKI--NYKLVRGLDYYNDTAFEIKTLSSNGQ--------DTICGGGRYDS 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561263 226 LVAQFDpkGHHVPCVGLSIGVERIFYLVEQKMKMSGEKVrttetQVFVATPQKNFLQERLKIIAELWDAGIKAEmLYKNN 305
Cdd:CHL00201 290 LIHQLG--GPKTPAVGCAIGLERLLLIAKDNIILPKQSI-----DVYIATQGLKAQKKGWEIIQFLEKQNIKFE-LDLSS 361
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 755561263 306 PKLLTQLHYCEKADIPLMVIIGEQERNEGVIKLRSVASREEVTINRESLVAEIQK 360
Cdd:CHL00201 362 SNFHKQIKQAGKKRAKACIILGDNEIMDNCITIKWLDEQVQENAQYSNFKQEISY 416
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
270-361 |
3.92e-16 |
|
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: 73.00 E-value: 3.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561263 270 QVFVATPQKN---FLQERLKIIAELWDAGIKAEmLYKNNPKLLTQLHYCEKADIPLMVIIGEQERNEGVIKLRSVASREE 346
Cdd:pfam03129 1 QVVVIPLGEKaeeLEEYAQKLAEELRAAGIRVE-LDDRNESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQ 79
|
90
....*....|....*
gi 755561263 347 VTINRESLVAEIQKR 361
Cdd:pfam03129 80 ETVSLDELVEKLKEL 94
|
|
| hisZ |
PRK12295 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
118-249 |
5.95e-09 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 183413 [Multi-domain] Cd Length: 373 Bit Score: 56.87 E-value: 5.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561263 118 GLAPEVADRIGDFVQYHG----GISLVEDLFKDPRLSQSQlALQGLGDlkllfeylRLFGIA------DKISLDLSLARG 187
Cdd:PRK12295 245 RLPAEALAVLERFLAISGppdaALAALRALAADAGLDLDA-ALDRFEA--------RLAALAargidlERLRFSASFGRP 315
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755561263 188 LDYYTGVIYEavlLESPAqagketLSVGSVAAGGRYDNLVAQFDpKGHHVPCVGLSIGVERI 249
Cdd:PRK12295 316 LDYYTGFVFE---IRAAG------NGDPPLAGGGRYDGLLTRLG-AGEPIPAVGFSIWLDRL 367
|
|
| HGTP_anticodon2 |
pfam12745 |
Anticodon binding domain of tRNAs; This is an HGTP_anticodon binding domain, found largely on ... |
271-361 |
1.20e-05 |
|
Anticodon binding domain of tRNAs; This is an HGTP_anticodon binding domain, found largely on Gcn2 proteins which bind tRNA to down regulate translation in certain stress situations.
Pssm-ID: 432758 Cd Length: 259 Bit Score: 46.06 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561263 271 VFVATPQKNFL-QERLKIIAELWDAGIKAEMLYKNNPKLLTQLHYCEKADIPLMVIIGEQ----ERNEGVIKLRSVASRE 345
Cdd:pfam12745 8 VLVASFDASILrTTGVEILQELWAHGISADLAVDASYSPEDLVSRARDDGVSWIVIIKQQnkssDSKYKPLKVKNLLRKE 87
|
90 100
....*....|....*....|
gi 755561263 346 EVTINRESLVA----EIQKR 361
Cdd:pfam12745 88 DVDLDSDELVSwlrgEIRER 107
|
|
| PRK12421 |
PRK12421 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
111-224 |
3.12e-05 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 237098 Cd Length: 392 Bit Score: 45.35 E-value: 3.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561263 111 HEMVAKKGLAPEVADRIGDFVQYHGGISLVEDlfkdprlSQSQLALQG------LGDLKLLFEYLRLFGIADKISLDLSL 184
Cdd:PRK12421 199 AEVCQNLGVGSDLRRMFYALARLNGGLEALDR-------ALSVLALQDaairqaLDELKTLAAHLKNRWPELPVSIDLAE 271
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 755561263 185 ARGLDYYTGVIYeAVLLESPAQAgketlsvgsVAAGGRYD 224
Cdd:PRK12421 272 LRGYHYHTGLVF-AAYIPGRGQA---------LARGGRYD 301
|
|
| ThrRS_anticodon |
cd00860 |
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases ... |
269-359 |
2.64e-03 |
|
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only.
Pssm-ID: 238437 [Multi-domain] Cd Length: 91 Bit Score: 36.71 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561263 269 TQVFVATPQKNFLQERLKIIAELWDAGIKAEMLYKNNpKLLTQLHYCEKADIPLMVIIGEQERNEGVIKLRSVASREEVT 348
Cdd:cd00860 2 VQVVVIPVTDEHLDYAKEVAKKLSDAGIRVEVDLRNE-KLGKKIREAQLQKIPYILVVGDKEVETGTVSVRTRDGGDLGS 80
|
90
....*....|.
gi 755561263 349 INRESLVAEIQ 359
Cdd:cd00860 81 MSLDEFIEKLK 91
|
|
| ProRS_anticodon_short |
cd00861 |
ProRS Prolyl-anticodon binding domain, short version found predominantly in bacteria. ProRS ... |
320-359 |
3.07e-03 |
|
ProRS Prolyl-anticodon binding domain, short version found predominantly in bacteria. ProRS 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: 238438 [Multi-domain] Cd Length: 94 Bit Score: 36.41 E-value: 3.07e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 755561263 320 IPLMVIIGEQERNEGVIKLRSVASREEVTINRESLVAEIQ 359
Cdd:cd00861 55 IPYRIVVGKKSAAEGIVEIKVRKTGEKEEISIDELLEFLQ 94
|
|
| HGTP_anticodon |
cd00738 |
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ... |
286-359 |
9.63e-03 |
|
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: 35.07 E-value: 9.63e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755561263 286 KIIAELWDAGIKAEMLYKNNpKLLTQLHYCEKADIPLMVIIGEQERNEGVIKLRSVASREEVTINRESLVAEIQ 359
Cdd:cd00738 22 KLLNALLANGIRVLYDDRER-KIGKKFREADLRGVPFAVVVGEDELENGKVTVKSRDTGESETLHVDELPEFLV 94
|
|
| |
