|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02972 |
PLN02972 |
Histidyl-tRNA synthetase |
1-434 |
6.74e-178 |
|
Histidyl-tRNA synthetase
Pssm-ID: 215525 [Multi-domain] Cd Length: 763 Bit Score: 515.98 E-value: 6.74e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 1 MVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSGLMYDLKDQGGELLSLRYDLTVPFARYLAMNKVKKMKR 80
Cdd:PLN02972 341 MAIREKAFSIITSVFKRHGATALDTPVFELRETLMGKYGEDSKLIYDLADQGGELCSLRYDLTVPFARYVAMNGITSFKR 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 81 YHVGKVWRRESPTivQGRYREFCQCDFDIAGQFDPMIPDAECLKIMCEILSGLQLGDFLIKVNDRRIVDGMFAVCGVPES 160
Cdd:PLN02972 421 YQIAKVYRRDNPS--KGRYREFYQCDFDIAGVYEPMGPDFEIIKVLTELLDELDIGTYEVKLNHRKLLDGMLEICGVPPE 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 161 KFRAICSSIDKLDKMAWKDVRHEMVVKKGLAPEVADRIGDYVQCHGG-VSLVEQMFQ-DPRLSQNKQALEGLGDLKLLFE 238
Cdd:PLN02972 499 KFRTICSSIDKLDKQSFEQVKKEMVEEKGLSNETADKIGNFVKERGPpLELLSKLRQeGSEFLGNASSRAALDELEIMFK 578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 239 YLTLFGIADKISFDLSLARGLDYYTGVIYEAVLLQTptqageeplNVGSVAAGGRYDGLVGMFDPKghKVPCVGLSIGVE 318
Cdd:PLN02972 579 ALEKSKAIGKIVFDLSLARGLDYYTGVIYEAVFKGA---------QVGSIAAGGRYDNLVGMFSGK--QVPAVGVSLGIE 647
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 319 RIFYIVEQRMKTKGEKVRTTETQVFVATPQKNFLQERLKLIAELWDSGIKAEmlYKNNPKLLTQLHYCESTGIPLVVIIG 398
Cdd:PLN02972 648 RVFAIMEQQEEEKSQVIRPTETEVLVSIIGDDKLALAAELVSELWNAGIKAE--YKVSTRKAKHLKRAKESGIPWMVLVG 725
|
410 420 430
....*....|....*....|....*....|....*.
gi 1391723582 399 EQELKEGVIKIRSVASREEVAIKRENFVAEIQKRLS 434
Cdd:PLN02972 726 EKELSKGFVKLKNLEAGVEEEVDRTCFVQELKAELL 761
|
|
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
1-435 |
2.02e-106 |
|
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: 321.30 E-value: 2.02e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 1 MVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSG--LMYDLKDQGGELLSLRYDLTVPFARYLAMNK---V 75
Cdd:COG0124 18 SAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKIGEDIVekEMYTFEDRGGRSLTLRPEGTAPVARAVAEHGnelP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 76 KKMKRYHVGKVWRRESPtivQ-GRYREFCQCDFDIAGQFDPMIpDAECLKIMCEILSGLQLGDFLIKVNDRrivdgmfav 154
Cdd:COG0124 98 FPFKLYYIGPVFRYERP---QkGRYRQFHQFGVEVIGSDSPLA-DAEVIALAADLLKALGLKDFTLEINSR--------- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 155 cGVPESKFRAICSSIDKLDKMAWKDVrhemvvkkgLAPEVADRIG-----DYVQCHGGV--SLVEQMfqdPRLSQNKqAL 227
Cdd:COG0124 165 -GLPEERAEALLRYLDKLDKIGHEDV---------LDEDSQRRLEtnplrAILDSKGPDcqEVLADA---PKLLDYL-GE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 228 EGLGDLKLLFEYLTLFGIadKISFDLSLARGLDYYTGVIYEAVLLQTPTQageeplnvGSVAAGGRYDGLVGMFDpkGHK 307
Cdd:COG0124 231 EGLAHFEEVLELLDALGI--PYVIDPRLVRGLDYYTGTVFEIVTDGLGAQ--------GSVCGGGRYDGLVEQLG--GPP 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 308 VPCVGLSIGVERIFYIVEQRmktKGEKVRTTETQVFVATPQKNFLQERLKLIAELWDSGIKAEMLYKNNpKLLTQLHYCE 387
Cdd:COG0124 299 TPAVGFAIGLERLLLLLEEL---GLLPAAEPPPDVYVVPLGEEARAEALKLAQELRAAGIRVELDLGGR-KLKKQLKYAD 374
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1391723582 388 STGIPLVVIIGEQELKEGVIKIRSVASREEVAIKRENFVAEIQKRLSE 435
Cdd:COG0124 375 KSGAPFVLILGEDELANGTVTLKDLATGEQETVPLDELVEYLKELLAE 422
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
1-325 |
7.56e-97 |
|
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: 291.04 E-value: 7.56e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 1 MVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSG-LMYDLKDQGGELLSLRYDLTVPFARYLAMNKVKK-- 77
Cdd:cd00773 2 AALRRYIEDTLREVFERYGYEEIDTPVFEYTELFLRKSGDEVSkEMYRFKDKGGRDLALRPDLTAPVARAVAENLLSLpl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 78 -MKRYHVGKVWRRESPTivQGRYREFCQCDFDIAGqFDPMIPDAECLKIMCEILSGLQLGDFLIKVNDRRIVDGmfaVCG 156
Cdd:cd00773 82 pLKLYYIGPVFRYERPQ--KGRYREFYQVGVEIIG-SDSPLADAEVIALAVEILEALGLKDFQIKINHRGILDG---IAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 157 VPESKFRAICSSIDKLDKmawkdvrhemvvkkglapevadrigdyvqchggvslveqmfqdprlsqnkqalEGLGDLKLL 236
Cdd:cd00773 156 LLEDREEYIERLIDKLDK-----------------------------------------------------EALAHLEKL 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 237 FEYLTLFGIADKISFDLSLARGLDYYTGVIYEAVLLQTPTQageeplnvGSVAAGGRYDGLVGMFDpkGHKVPCVGLSIG 316
Cdd:cd00773 183 LDYLEALGVDIKYSIDLSLVRGLDYYTGIVFEAVADGLGAQ--------GSIAGGGRYDGLLEEFG--GEDVPAVGFAIG 252
|
....*....
gi 1391723582 317 VERIFYIVE 325
Cdd:cd00773 253 LERLLLALE 261
|
|
| hisS |
TIGR00442 |
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ... |
1-422 |
3.24e-87 |
|
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: 271.27 E-value: 3.24e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 1 MVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSGL----MYDLKDQGGELLSLRYDLTVPFARYLAMNK-- 74
Cdd:TIGR00442 14 MIKWQYIEETIREVFERYGFKEIRTPIFEYTELFKRKVGEETDIvskeMYTFKDKGGRSLTLRPEGTAPVARAVIENKll 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 75 -VKKMKRYHVGKVWRRESPtivQ-GRYREFCQCDFDIAGQFDPMIpDAECLKIMCEILSGLQLGDFLIKVNDRRIVDGMF 152
Cdd:TIGR00442 94 lPKPFKLYYIGPMFRYERP---QkGRYRQFHQFGVEVIGSDSPLA-DAEIIALAADILKELGLKDFTLEINSLGILEGRL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 153 AvcgvpesKFRAICSSIDK-LDKMAWKDVRHEMVVKKGLAPEVADRIGDYVQchggvslveqmfQDPRLSQNKQAlEGLG 231
Cdd:TIGR00442 170 E-------YREALIRYLDKhKDKLGEDSVRRLEKNPLRILDSKNEKIQELLK------------NAPKILDFLCE-ESRA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 232 DLKLLFEYLTLFGIadKISFDLSLARGLDYYTGVIYEAVLLQTPTQageeplnvGSVAAGGRYDGLVGMFDpkGHKVPCV 311
Cdd:TIGR00442 230 HFEELKELLDALGI--PYKIDPSLVRGLDYYTGTVFEFVTDDLGAQ--------GSICGGGRYDGLVEELG--GPPTPAV 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 312 GLSIGVERIFYIVEQRmktKGEKVRTTETQVFVATPQKNFLQERLKLIAELWDSGIKAEMLYKNNpKLLTQLHYCESTGI 391
Cdd:TIGR00442 298 GFAIGIERLILLLEEL---GLIPPPSKKPDVYVVPLGEEAELEALKLAQKLRKAGIRVEVDLGGR-KLKKQLKYADKLGA 373
|
410 420 430
....*....|....*....|....*....|.
gi 1391723582 392 PLVVIIGEQELKEGVIKIRSVASREEVAIKR 422
Cdd:TIGR00442 374 RFALIIGEDELENGTVTLKDLETGEQETVPL 404
|
|
| tRNA-synt_His |
pfam13393 |
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ... |
3-320 |
1.29e-37 |
|
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: 138.87 E-value: 1.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 3 VREKILDLviscFKRHGAKGMDTPAFELKETLTEKYGEDSGLMYDLKDQGGELLSLRYDLTVPFARYLA--MNKVKKMKR 80
Cdd:pfam13393 16 LRRRLLDL----FRSWGYELVMPPLLEYLDSLLTGTGADLDQTFKLVDQSGRLLGLRADITPQVARIDAhrLNRPGPLRL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 81 YHVGKVWRRESPTIvqGRYREFCQCDFDIAGQFDPMiPDAECLKIMCEILSGLQLGDFLIKVNDRRIVDGMFAVCGVPES 160
Cdd:pfam13393 92 CYAGSVLRTRPKGL--GRSREPLQVGAELIGHAGIE-ADAEIISLLLEALAAAGVPGVTLDLGHVGLVRALLEAAGLSEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 161 KFRAICSSIDKLDkmaWKDVRhEMVVKKGLAPEVADRIGDYVQCHGGVSLVEQMFQdpRLSQNKQALEGLGDLKLLFEYL 240
Cdd:pfam13393 169 LEEALRAALQRKD---AAELA-ELAAEAGLPPALRRALLALPDLYGGPEVLDEARA--ALPGLPALQEALDELEALAALL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 241 TLFGIADKISFDLSLARGLDYYTGVIYEAVLLQTPtqageeplnvGSVAAGGRYDGLVGMFdpkGHKVPCVGLSIGVERI 320
Cdd:pfam13393 243 EALGDGVRLTFDLAELRGYEYYTGIVFAAYAPGVG----------EPLARGGRYDDLGAAF---GRARPATGFSLDLEAL 309
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02972 |
PLN02972 |
Histidyl-tRNA synthetase |
1-434 |
6.74e-178 |
|
Histidyl-tRNA synthetase
Pssm-ID: 215525 [Multi-domain] Cd Length: 763 Bit Score: 515.98 E-value: 6.74e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 1 MVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSGLMYDLKDQGGELLSLRYDLTVPFARYLAMNKVKKMKR 80
Cdd:PLN02972 341 MAIREKAFSIITSVFKRHGATALDTPVFELRETLMGKYGEDSKLIYDLADQGGELCSLRYDLTVPFARYVAMNGITSFKR 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 81 YHVGKVWRRESPTivQGRYREFCQCDFDIAGQFDPMIPDAECLKIMCEILSGLQLGDFLIKVNDRRIVDGMFAVCGVPES 160
Cdd:PLN02972 421 YQIAKVYRRDNPS--KGRYREFYQCDFDIAGVYEPMGPDFEIIKVLTELLDELDIGTYEVKLNHRKLLDGMLEICGVPPE 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 161 KFRAICSSIDKLDKMAWKDVRHEMVVKKGLAPEVADRIGDYVQCHGG-VSLVEQMFQ-DPRLSQNKQALEGLGDLKLLFE 238
Cdd:PLN02972 499 KFRTICSSIDKLDKQSFEQVKKEMVEEKGLSNETADKIGNFVKERGPpLELLSKLRQeGSEFLGNASSRAALDELEIMFK 578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 239 YLTLFGIADKISFDLSLARGLDYYTGVIYEAVLLQTptqageeplNVGSVAAGGRYDGLVGMFDPKghKVPCVGLSIGVE 318
Cdd:PLN02972 579 ALEKSKAIGKIVFDLSLARGLDYYTGVIYEAVFKGA---------QVGSIAAGGRYDNLVGMFSGK--QVPAVGVSLGIE 647
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 319 RIFYIVEQRMKTKGEKVRTTETQVFVATPQKNFLQERLKLIAELWDSGIKAEmlYKNNPKLLTQLHYCESTGIPLVVIIG 398
Cdd:PLN02972 648 RVFAIMEQQEEEKSQVIRPTETEVLVSIIGDDKLALAAELVSELWNAGIKAE--YKVSTRKAKHLKRAKESGIPWMVLVG 725
|
410 420 430
....*....|....*....|....*....|....*.
gi 1391723582 399 EQELKEGVIKIRSVASREEVAIKRENFVAEIQKRLS 434
Cdd:PLN02972 726 EKELSKGFVKLKNLEAGVEEEVDRTCFVQELKAELL 761
|
|
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
1-435 |
2.02e-106 |
|
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: 321.30 E-value: 2.02e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 1 MVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSG--LMYDLKDQGGELLSLRYDLTVPFARYLAMNK---V 75
Cdd:COG0124 18 SAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKIGEDIVekEMYTFEDRGGRSLTLRPEGTAPVARAVAEHGnelP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 76 KKMKRYHVGKVWRRESPtivQ-GRYREFCQCDFDIAGQFDPMIpDAECLKIMCEILSGLQLGDFLIKVNDRrivdgmfav 154
Cdd:COG0124 98 FPFKLYYIGPVFRYERP---QkGRYRQFHQFGVEVIGSDSPLA-DAEVIALAADLLKALGLKDFTLEINSR--------- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 155 cGVPESKFRAICSSIDKLDKMAWKDVrhemvvkkgLAPEVADRIG-----DYVQCHGGV--SLVEQMfqdPRLSQNKqAL 227
Cdd:COG0124 165 -GLPEERAEALLRYLDKLDKIGHEDV---------LDEDSQRRLEtnplrAILDSKGPDcqEVLADA---PKLLDYL-GE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 228 EGLGDLKLLFEYLTLFGIadKISFDLSLARGLDYYTGVIYEAVLLQTPTQageeplnvGSVAAGGRYDGLVGMFDpkGHK 307
Cdd:COG0124 231 EGLAHFEEVLELLDALGI--PYVIDPRLVRGLDYYTGTVFEIVTDGLGAQ--------GSVCGGGRYDGLVEQLG--GPP 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 308 VPCVGLSIGVERIFYIVEQRmktKGEKVRTTETQVFVATPQKNFLQERLKLIAELWDSGIKAEMLYKNNpKLLTQLHYCE 387
Cdd:COG0124 299 TPAVGFAIGLERLLLLLEEL---GLLPAAEPPPDVYVVPLGEEARAEALKLAQELRAAGIRVELDLGGR-KLKKQLKYAD 374
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1391723582 388 STGIPLVVIIGEQELKEGVIKIRSVASREEVAIKRENFVAEIQKRLSE 435
Cdd:COG0124 375 KSGAPFVLILGEDELANGTVTLKDLATGEQETVPLDELVEYLKELLAE 422
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
1-325 |
7.56e-97 |
|
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: 291.04 E-value: 7.56e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 1 MVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSG-LMYDLKDQGGELLSLRYDLTVPFARYLAMNKVKK-- 77
Cdd:cd00773 2 AALRRYIEDTLREVFERYGYEEIDTPVFEYTELFLRKSGDEVSkEMYRFKDKGGRDLALRPDLTAPVARAVAENLLSLpl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 78 -MKRYHVGKVWRRESPTivQGRYREFCQCDFDIAGqFDPMIPDAECLKIMCEILSGLQLGDFLIKVNDRRIVDGmfaVCG 156
Cdd:cd00773 82 pLKLYYIGPVFRYERPQ--KGRYREFYQVGVEIIG-SDSPLADAEVIALAVEILEALGLKDFQIKINHRGILDG---IAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 157 VPESKFRAICSSIDKLDKmawkdvrhemvvkkglapevadrigdyvqchggvslveqmfqdprlsqnkqalEGLGDLKLL 236
Cdd:cd00773 156 LLEDREEYIERLIDKLDK-----------------------------------------------------EALAHLEKL 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 237 FEYLTLFGIADKISFDLSLARGLDYYTGVIYEAVLLQTPTQageeplnvGSVAAGGRYDGLVGMFDpkGHKVPCVGLSIG 316
Cdd:cd00773 183 LDYLEALGVDIKYSIDLSLVRGLDYYTGIVFEAVADGLGAQ--------GSIAGGGRYDGLLEEFG--GEDVPAVGFAIG 252
|
....*....
gi 1391723582 317 VERIFYIVE 325
Cdd:cd00773 253 LERLLLALE 261
|
|
| hisS |
TIGR00442 |
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ... |
1-422 |
3.24e-87 |
|
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: 271.27 E-value: 3.24e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 1 MVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSGL----MYDLKDQGGELLSLRYDLTVPFARYLAMNK-- 74
Cdd:TIGR00442 14 MIKWQYIEETIREVFERYGFKEIRTPIFEYTELFKRKVGEETDIvskeMYTFKDKGGRSLTLRPEGTAPVARAVIENKll 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 75 -VKKMKRYHVGKVWRRESPtivQ-GRYREFCQCDFDIAGQFDPMIpDAECLKIMCEILSGLQLGDFLIKVNDRRIVDGMF 152
Cdd:TIGR00442 94 lPKPFKLYYIGPMFRYERP---QkGRYRQFHQFGVEVIGSDSPLA-DAEIIALAADILKELGLKDFTLEINSLGILEGRL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 153 AvcgvpesKFRAICSSIDK-LDKMAWKDVRHEMVVKKGLAPEVADRIGDYVQchggvslveqmfQDPRLSQNKQAlEGLG 231
Cdd:TIGR00442 170 E-------YREALIRYLDKhKDKLGEDSVRRLEKNPLRILDSKNEKIQELLK------------NAPKILDFLCE-ESRA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 232 DLKLLFEYLTLFGIadKISFDLSLARGLDYYTGVIYEAVLLQTPTQageeplnvGSVAAGGRYDGLVGMFDpkGHKVPCV 311
Cdd:TIGR00442 230 HFEELKELLDALGI--PYKIDPSLVRGLDYYTGTVFEFVTDDLGAQ--------GSICGGGRYDGLVEELG--GPPTPAV 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 312 GLSIGVERIFYIVEQRmktKGEKVRTTETQVFVATPQKNFLQERLKLIAELWDSGIKAEMLYKNNpKLLTQLHYCESTGI 391
Cdd:TIGR00442 298 GFAIGIERLILLLEEL---GLIPPPSKKPDVYVVPLGEEAELEALKLAQKLRKAGIRVEVDLGGR-KLKKQLKYADKLGA 373
|
410 420 430
....*....|....*....|....*....|.
gi 1391723582 392 PLVVIIGEQELKEGVIKIRSVASREEVAIKR 422
Cdd:TIGR00442 374 RFALIIGEDELENGTVTLKDLETGEQETVPL 404
|
|
| PRK12420 |
PRK12420 |
histidyl-tRNA synthetase; Provisional |
2-421 |
1.27e-79 |
|
histidyl-tRNA synthetase; Provisional
Pssm-ID: 237097 [Multi-domain] Cd Length: 423 Bit Score: 252.34 E-value: 1.27e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 2 VVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYG---EDSGLMYDLKDQGGELLSLRYDLTVPFARYLAMNKVKKM 78
Cdd:PRK12420 19 VLRNKIKRALEDVFERYGCKPLETPTLNMYELMSSKYGggdEILKEIYTLTDQGKRDLALRYDLTIPFAKVVAMNPNIRL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 79 --KRYHVGKVWrRESPtIVQGRYREFCQCDFDIAGQFDPMiPDAECLKIMCEILSGLQLgDFLIKVNDRRIVDGMFAVCG 156
Cdd:PRK12420 99 pfKRYEIGKVF-RDGP-IKQGRFREFIQCDVDIVGVESVM-AEAELMSMAFELFRRLNL-EVTIQYNNRKLLNGILQAIG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 157 VPESKFRAICSSIDKLDKMAWKDVRHEmVVKKGLAPEVADRIGDYVQCHGGVSLVEqmFQDPRLSQNKQalEGLGDLKLL 236
Cdd:PRK12420 175 IPTELTSDVILSLDKIEKIGIDGVRKD-LLERGISEEMADTICNTVLSCLQLSIAD--FKEAFNNPLVA--EGVNELQQL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 237 FEYLTLFGIADKISFDLSLARGLDYYTGVIYEAVLlqtptqagEEPLNVGSVAAGGRYDGLVGMFDPKGHKVPCVGLSIG 316
Cdd:PRK12420 250 QQYLIALGINENCIFNPFLARGLTMYTGTVYEIFL--------KDGSITSSIGSGGRYDNIIGAFRGDDMNYPTVGISFG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 317 VERIFYIVEQRmktkgekVRTTETQVFVATPQKNFLQErLKLIAELW-DSGIKAEMLYKNNpKLLTQLHYCESTGIPLVV 395
Cdd:PRK12420 322 LDVIYTALSQK-------ETISSTADVFIIPLGTELQC-LQIAQQLRsTTGLKVELELAGR-KLKKALNYANKENIPYVL 392
|
410 420
....*....|....*....|....*.
gi 1391723582 396 IIGEQELKEGVIKIRSVASREEVAIK 421
Cdd:PRK12420 393 IIGEEEVSTGTVMLRNMKEGSEVKVP 418
|
|
| hisZ_biosyn_reg |
TIGR00443 |
ATP phosphoribosyltransferase, regulatory subunit; Apparant second copies of histidyl-tRNA ... |
4-320 |
7.48e-47 |
|
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: 163.55 E-value: 7.48e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 4 REKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSGLMYDLKDQGGELLSLRYDLTVPFARYLAmnkvKKMKRYH- 82
Cdd:TIGR00443 11 KEEIERQLQDVFRSWGYQEIITPTLEYLDTLSAGSGILNEDLFKLFDQLGRVLGLRPDMTAPIARLVS----TRLRDRPl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 83 ------VGKVWRRESPTIvqGRYREFCQCDFDIAGQfDPMIPDAECLKIMCEILSGLQLGDFLIKVNDRRIVDGMFAVCG 156
Cdd:TIGR00443 87 plrlcyAGNVFRTNESGG--GRSREFTQAGVELIGA-GGPAADAEVIALLIEALKALGLKDFKIELGHVGLVRALLEEAG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 157 VPESKFRAICSSIDKLDKMAWKdvrhEMVVKKGLAPEVADRIGDYVQCHGGVSLVEQMFQdpRLSQNKQALEGLGDLKLL 236
Cdd:TIGR00443 164 LPEEAREALREALARKDLVALE----ELVAELGLSPEVRERLLALPRLRGDGEEVLEEAR--ALAGSETAEAALDELEAV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 237 FEYLTLFGIADKISFDLSLARGLDYYTGVIYEAVLlqtpTQAGEeplnvgSVAAGGRYDGLVGMFdpkGHKVPCVGLSIG 316
Cdd:TIGR00443 238 LELLEARGVEEYISLDLGLVRGYHYYTGLIFEGYA----PGLGA------PLAGGGRYDELLGRF---GRPLPATGFALN 304
|
....
gi 1391723582 317 VERI 320
Cdd:TIGR00443 305 LERL 308
|
|
| HisZ |
COG3705 |
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism]; |
4-320 |
7.51e-45 |
|
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism];
Pssm-ID: 442919 [Multi-domain] Cd Length: 312 Bit Score: 158.42 E-value: 7.51e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 4 REKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSGL-MYDLKDQGGELLSLRYDLTVPFARYLA--MNKVKKMKR 80
Cdd:COG3705 8 KEELRRRLLDVFRSWGYELVEPPLLEYLDSLLTGSGADLDLqTFKLVDQLGRTLGLRPDMTPQVARIAAtrLANRPGPLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 81 Y-HVGKVWR-RESPtivQGRYREFCQC------DFDIAGqfdpmipDAECLKIMCEILSGLQLGDFLIKVNDRRIVDGMF 152
Cdd:COG3705 88 LcYAGNVFRtRPSG---LGRSREFLQAgaeligHAGLEA-------DAEVIALALEALKAAGLEDFTLDLGHVGLFRALL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 153 AVCGVPESKFRAICSSIDKLDkmaWKDVRhEMVVKKGLAPEVADRIGDYVQCHGGVSLVEQMFQdprLSQNKQALEGLGD 232
Cdd:COG3705 158 EALGLSEEQREELRRALARKD---AVELE-ELLAELGLSEELAEALLALPELYGGEEVLARARA---LLLDAAIRAALDE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 233 LKLLFEYLTLFGIADKISFDLSLARGLDYYTGVIYEAVllqTPTQAGEeplnvgsVAAGGRYDGLVGMFdpkGHKVPCVG 312
Cdd:COG3705 231 LEALAEALAARGPDVRLTFDLSELRGYDYYTGIVFEAY---APGVGDP-------LARGGRYDGLLAAF---GRARPATG 297
|
....*...
gi 1391723582 313 LSIGVERI 320
Cdd:COG3705 298 FSLDLDRL 305
|
|
| PLN02530 |
PLN02530 |
histidine-tRNA ligase |
24-421 |
1.64e-42 |
|
histidine-tRNA ligase
Pssm-ID: 178145 [Multi-domain] Cd Length: 487 Bit Score: 156.06 E-value: 1.64e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 24 DTPAFELKETLTEKYGED-SGLMYDLKDQGGELLSLRYDLTVPFARyLAMNKVKKM----KRYHVGKVWRRESPTivQGR 98
Cdd:PLN02530 107 DAPVLESEELYIRKAGEEiTDQLYNFEDKGGRRVALRPELTPSLAR-LVLQKGKSLslplKWFAIGQCWRYERMT--RGR 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 99 YREFCQCDFDIAGqFDPMIPDAECLKIMCEILS--GLQLGDFLIKVNDRRIVDGMFAVCGVPESKFRAICSSIDKLDKMA 176
Cdd:PLN02530 184 RREHYQWNMDIIG-VPGVEAEAELLAAIVTFFKrvGITSSDVGIKVSSRKVLQAVLKSYGIPEESFAPVCVIVDKLEKLP 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 177 WKDVRHEMVvKKGLAPEVADRIGDYVQCHGGVSLVEQMFQDPrlsqnkqalEGLGDLKLLFEYLTLFGIADKISFDLSLA 256
Cdd:PLN02530 263 REEIEKELD-TLGVSEEAIEGILDVLSLKSLDDLEALLGADS---------EAVADLKQLFSLAEAYGYQDWLVFDASVV 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 257 RGLDYYTGVIYEAVllqtpTQAGEeplnVGSVAAGGRYDGLVGMFDpkGHKVPCVGLSIG--VerifyIVEQrMKTKG-- 332
Cdd:PLN02530 333 RGLAYYTGIVFEGF-----DRAGK----LRAICGGGRYDRLLSTFG--GEDTPACGFGFGdaV-----IVEL-LKEKGll 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 333 -EKVRTTETQVFvatPQKNFLQ-ERLKLIAELWDSGIKAEMLYKNNpKLLTQLHYCESTGIPLVVIIGEQELKEGVIKIR 410
Cdd:PLN02530 396 pELPHQVDDVVF---ALDEDLQgAAAGVASRLREKGRSVDLVLEPK-KLKWVFKHAERIGAKRLVLVGASEWERGMVRVK 471
|
410
....*....|.
gi 1391723582 411 SVASREEVAIK 421
Cdd:PLN02530 472 DLSSGEQTEVK 482
|
|
| hisZ |
PRK12292 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
4-371 |
3.96e-40 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 237043 [Multi-domain] Cd Length: 391 Bit Score: 147.71 E-value: 3.96e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 4 REKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSGL-MYDLKDQG-GELLSLRYDLTVPFARyLAMNKVKKMKR- 80
Cdd:PRK12292 20 IEEIRRRLLDLFRRWGYEEVITPTLEYLDTLLAGGGAILDLrTFKLVDQLsGRTLGLRPDMTAQIAR-IAATRLANRPGp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 81 ----YHvGKVWR---RESptivqGRYREFCQCDFDIAGqFDPMIPDAECLKIMCEILSGLQLGDFLIKVNDRRIVDGMFA 153
Cdd:PRK12292 99 lrlcYA-GNVFRaqeRGL-----GRSREFLQSGVELIG-DAGLEADAEVILLLLEALKALGLPNFTLDLGHVGLFRALLE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 154 VCGVPESKFRAICSSIDKLDKMAWKdvrhEMVvkKGLAPEVADRIGDYVQCHGGVSLVEQMfqdPRLSQNKQALEGLGDL 233
Cdd:PRK12292 172 AAGLSEELEEVLRRALANKDYVALE----ELV--LDLSEELRDALLALPRLRGGREVLEEA---RKLLPSLPIKRALDEL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 234 KLLFEYLTLFGIADKISFDLSLARGLDYYTGVIYEAVllqtptqAGEEPLNVGSvaaGGRYDGLVGMFdpkGHKVPCVGL 313
Cdd:PRK12292 243 EALAEALEKYGYGIPLSLDLGLLRHLDYYTGIVFEGY-------VDGVGNPIAS---GGRYDDLLGRF---GRARPATGF 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1391723582 314 SIGVERifyIVEQRMKTKgekvrTTETQVFVATPQKNFLQERLKLIAELWDSGIKAEM 371
Cdd:PRK12292 310 SLDLDR---LLELQLELP-----VEARKDLVIAPDSEALAAALAAAQELRKKGEIVVL 359
|
|
| tRNA-synt_His |
pfam13393 |
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ... |
3-320 |
1.29e-37 |
|
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: 138.87 E-value: 1.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 3 VREKILDLviscFKRHGAKGMDTPAFELKETLTEKYGEDSGLMYDLKDQGGELLSLRYDLTVPFARYLA--MNKVKKMKR 80
Cdd:pfam13393 16 LRRRLLDL----FRSWGYELVMPPLLEYLDSLLTGTGADLDQTFKLVDQSGRLLGLRADITPQVARIDAhrLNRPGPLRL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 81 YHVGKVWRRESPTIvqGRYREFCQCDFDIAGQFDPMiPDAECLKIMCEILSGLQLGDFLIKVNDRRIVDGMFAVCGVPES 160
Cdd:pfam13393 92 CYAGSVLRTRPKGL--GRSREPLQVGAELIGHAGIE-ADAEIISLLLEALAAAGVPGVTLDLGHVGLVRALLEAAGLSEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 161 KFRAICSSIDKLDkmaWKDVRhEMVVKKGLAPEVADRIGDYVQCHGGVSLVEQMFQdpRLSQNKQALEGLGDLKLLFEYL 240
Cdd:pfam13393 169 LEEALRAALQRKD---AAELA-ELAAEAGLPPALRRALLALPDLYGGPEVLDEARA--ALPGLPALQEALDELEALAALL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 241 TLFGIADKISFDLSLARGLDYYTGVIYEAVLLQTPtqageeplnvGSVAAGGRYDGLVGMFdpkGHKVPCVGLSIGVERI 320
Cdd:pfam13393 243 EALGDGVRLTFDLAELRGYEYYTGIVFAAYAPGVG----------EPLARGGRYDDLGAAF---GRARPATGFSLDLEAL 309
|
|
| HisRS_anticodon |
cd00859 |
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases ... |
339-430 |
8.15e-28 |
|
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only.
Pssm-ID: 238436 [Multi-domain] Cd Length: 91 Bit Score: 105.70 E-value: 8.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 339 ETQVFVATPQKNFLQERLKLIAELWDSGIKAEMLYKNnPKLLTQLHYCESTGIPLVVIIGEQELKEGVIKIRSVASREEV 418
Cdd:cd00859 1 EVDVYVVPLGEGALSEALELAEQLRDAGIKAEIDYGG-RKLKKQFKYADRSGARFAVILGEDELAAGVVTVKDLETGEQE 79
|
90
....*....|..
gi 1391723582 419 AIKRENFVAEIQ 430
Cdd:cd00859 80 TVALDELVEELK 91
|
|
| syh |
CHL00201 |
histidine-tRNA synthetase; Provisional |
7-431 |
4.50e-26 |
|
histidine-tRNA synthetase; Provisional
Pssm-ID: 164576 [Multi-domain] Cd Length: 430 Bit Score: 109.61 E-value: 4.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 7 ILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSGL----MYDLKDQGGELLSLRYDLTVPFARYLAMNKVKKMKR-- 80
Cdd:CHL00201 24 IHDKALTLLSLANYSEIRTPIFENSSLYDRGIGETTDIvnkeMYRFTDRSNRDITLRPEGTAGIVRAFIENKMDYHSNlq 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 81 --YHVGKVWRRESPTivQGRYREFCQCDFDIAGQFDPMiPDAECLKIMCEILSGLQLGDFLIKVN------DRRIVdgmf 152
Cdd:CHL00201 104 rlWYSGPMFRYERPQ--SGRQRQFHQLGIEFIGSIDAR-ADTEVIHLAMQIFNELQVKNLILDINsigkleDRQSY---- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 153 avcgvpESKFRAICSSI-DKLDKmawkDVRHEMVVKkglaP-EVADRIGDYVQchggvslvEQMFQDPRLSQ--NKQALE 228
Cdd:CHL00201 177 ------QLKLVEYLSQYqDDLDT----DSQNRLYSN----PiRILDSKNLKTQ--------EILDGAPKISDflSLESTE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 229 GLGDLkllFEYLTLFGIADKISFdlSLARGLDYYTGVIYEavlLQTPTQAGEEplnvgSVAAGGRYDGLVGMFDpkGHKV 308
Cdd:CHL00201 235 HFYDV---CTYLNLLNIPYKINY--KLVRGLDYYNDTAFE---IKTLSSNGQD-----TICGGGRYDSLIHQLG--GPKT 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 309 PCVGLSIGVERIFYIVEQRMKTKGEKVrttetQVFVATPQKNFLQERLKLIAELWDSGIKAEmLYKNNPKLLTQLHYCES 388
Cdd:CHL00201 300 PAVGCAIGLERLLLIAKDNIILPKQSI-----DVYIATQGLKAQKKGWEIIQFLEKQNIKFE-LDLSSSNFHKQIKQAGK 373
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1391723582 389 TGIPLVVIIGEQELKEGVIKIRSVASREEVAIKRENFVAEIQK 431
Cdd:CHL00201 374 KRAKACIILGDNEIMDNCITIKWLDEQVQENAQYSNFKQEISY 416
|
|
| hisZ |
PRK12295 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
7-320 |
3.83e-21 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 183413 [Multi-domain] Cd Length: 373 Bit Score: 94.23 E-value: 3.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 7 ILDLVISCFKRHGAKGMDTPAFELKETLTEKYGED-SGLMYDLKDQGGELLSLRYDLTVPFAR-YLAMNKVKKMKRYHVG 84
Cdd:PRK12295 10 AAEALLASFEAAGAVRVDPPILQPAEPFLDLSGEDiRRRIFVTSDENGEELCLRPDFTIPVCRrHIATAGGEPARYAYLG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 85 KVWRRESptivqGRYREFCQCDFDIAGQFDPMIPDAECLKIMCEILSGLQLGDFLIKVNDRRIVDGMFAVCGVPE----- 159
Cdd:PRK12295 90 EVFRQRR-----DRASEFLQAGIESFGRADPAAADAEVLALALEALAALGPGDLEVRLGDVGLFAALVDALGLPPgwkrr 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 160 --------SKFRAIcssIDKL-------------------DKMAWKDVRHEMVVKKGLAP-------EVADRIGDYVQCH 205
Cdd:PRK12295 165 llrhfgrpRSLDAL---LARLagprvdpldehagvlaalaDEAAARALVEDLMSIAGISPvggrspaEIARRLLEKAALA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 206 GGVSLVEQMFQ--------DPRLSQNKQALEGL-GDLKL-------LFE----YLTLFGIA-DKISFDLSLARGLDYYTG 264
Cdd:PRK12295 242 AAARLPAEALAvlerflaiSGPPDAALAALRALaADAGLdldaaldRFEarlaALAARGIDlERLRFSASFGRPLDYYTG 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1391723582 265 VIYEAvllqTPTQAGEEPLnvgsvAAGGRYDGLVGMFDpKGHKVPCVGLSIGVERI 320
Cdd:PRK12295 322 FVFEI----RAAGNGDPPL-----AGGGRYDGLLTRLG-AGEPIPAVGFSIWLDRL 367
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
341-432 |
2.78e-17 |
|
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: 76.47 E-value: 2.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 341 QVFVATPQKN---FLQERLKLIAELWDSGIKAEmLYKNNPKLLTQLHYCESTGIPLVVIIGEQELKEGVIKIRSVASREE 417
Cdd:pfam03129 1 QVVVIPLGEKaeeLEEYAQKLAEELRAAGIRVE-LDDRNESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQ 79
|
90
....*....|....*
gi 1391723582 418 VAIKRENFVAEIQKR 432
Cdd:pfam03129 80 ETVSLDELVEKLKEL 94
|
|
| HGTP_anticodon2 |
pfam12745 |
Anticodon binding domain of tRNAs; This is an HGTP_anticodon binding domain, found largely on ... |
342-432 |
4.95e-07 |
|
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: 50.68 E-value: 4.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 342 VFVATPQKNFL-QERLKLIAELWDSGIKAEMLYKNNPKLLTQLHYCESTGIPLVVIIGEQEL----KEGVIKIRSVASRE 416
Cdd:pfam12745 8 VLVASFDASILrTTGVEILQELWAHGISADLAVDASYSPEDLVSRARDDGVSWIVIIKQQNKssdsKYKPLKVKNLLRKE 87
|
90 100
....*....|....*....|
gi 1391723582 417 EVAIKRENFVA----EIQKR 432
Cdd:pfam12745 88 DVDLDSDELVSwlrgEIRER 107
|
|
| PRK12421 |
PRK12421 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
4-320 |
6.48e-05 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 237098 Cd Length: 392 Bit Score: 44.96 E-value: 6.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 4 REKILDLVIScfkrHGAKGMDTPAFELKETLTEKYGEDSGLM-YDLKDQ-GGELLSLRYDLTVPFARYLA-MNKVKKMKR 80
Cdd:PRK12421 28 RRRLLDLFAS----RGYQLVMPPLIEYLESLLTGAGQDLKLQtFKLIDQlSGRLMGVRADITPQVARIDAhLLNREGVAR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 81 Y-HVGKVWRrespTIVQG--RYREFCQCDFDIAGQfDPMIPDAECLKIMCEILSGLQLGDFLIKVNDRRIVDGMFAVCGV 157
Cdd:PRK12421 104 LcYAGSVLH----TLPQGlfGSRTPLQLGAELYGH-AGIEADLEIIRLMLGLLRNAGVPALHLDLGHVGIFRRLAELAGL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 158 PESKFRAIcssidkLDKMAWKDVR--HEMVVKKGLAPEVADRIGDYVQCHGGV-SLVEQMFQDPRlsQNKQALEGLGDLK 234
Cdd:PRK12421 179 SPEEEEEL------FDLLQRKALPelAEVCQNLGVGSDLRRMFYALARLNGGLeALDRALSVLAL--QDAAIRQALDELK 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 235 LLFEYLTLFGIADKISFDLSLARGLDYYTGVIYeAVLLQTPTQAgeeplnvgsVAAGGRYDGLVGMFdpkGHKVPCVGLS 314
Cdd:PRK12421 251 TLAAHLKNRWPELPVSIDLAELRGYHYHTGLVF-AAYIPGRGQA---------LARGGRYDGIGEAF---GRARPATGFS 317
|
....*.
gi 1391723582 315 IGVERI 320
Cdd:PRK12421 318 MDLKEL 323
|
|
| ProRS_anticodon_short |
cd00861 |
ProRS Prolyl-anticodon binding domain, short version found predominantly in bacteria. ProRS ... |
390-430 |
6.09e-04 |
|
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: 38.72 E-value: 6.09e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1391723582 390 GIPLVVIIGEQELKEGVIKIRSVASREEVAIKRENFVAEIQ 430
Cdd:cd00861 54 GIPYRIVVGKKSAAEGIVEIKVRKTGEKEEISIDELLEFLQ 94
|
|
| PRK09194 |
PRK09194 |
prolyl-tRNA synthetase; Provisional |
390-434 |
5.21e-03 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 236405 [Multi-domain] Cd Length: 565 Bit Score: 38.91 E-value: 5.21e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1391723582 390 GIPLVVIIGEQELKEGVIKIRSVASREEVAIKRENFVAEIQKRLS 434
Cdd:PRK09194 521 GIPHRIVVGDRGLAEGIVEYKDRRTGEKEEVPVDELVEFLKALKK 565
|
|
|