|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02972 |
PLN02972 |
Histidyl-tRNA synthetase |
57-481 |
0e+00 |
|
Histidyl-tRNA synthetase
Pssm-ID: 215525 [Multi-domain] Cd Length: 763 Bit Score: 528.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 57 KTPKGTRDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGEDSKLIYDLKDQGGELLSLRYDLTVPFA 136
Cdd:PLN02972 328 KIPKGTRDFAKEQMAIREKAFSIITSVFKRHGATALDTPVFELRETLMGKYGEDSKLIYDLADQGGELCSLRYDLTVPFA 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 137 RYLAMNKLTNIKRYHIAK------------------DFDIAGNFDPMIPDAECLKIMCEILSSLQIGDFLVKVNDRRILD 198
Cdd:PLN02972 408 RYVAMNGITSFKRYQIAKvyrrdnpskgryrefyqcDFDIAGVYEPMGPDFEIIKVLTELLDELDIGTYEVKLNHRKLLD 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 199 GMFAICGVSDSKFRTICSSVDKLDKVSWEEVKNEMVGEKGLAPEVADRIGDYVQQHGG-VSLVEQLLQ-DPKLSQNKQAL 276
Cdd:PLN02972 488 GMLEICGVPPEKFRTICSSIDKLDKQSFEQVKKEMVEEKGLSNETADKIGNFVKERGPpLELLSKLRQeGSEFLGNASSR 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 277 EGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLLQTPaqageeplgVGSVAAGGRYDGLVGMFDpkGRK 356
Cdd:PLN02972 568 AALDELEIMFKALEKSKAIGKIVFDLSLARGLDYYTGVIYEAVFKGAQ---------VGSIAAGGRYDNLVGMFS--GKQ 636
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 357 VPCVGLSIGVERIFSIVEQRLEALEEKIRTTETQVLVASAQKKLLEERLKLVSELWDAGIKAEllYKKNPKLLNQLQYCE 436
Cdd:PLN02972 637 VPAVGVSLGIERVFAIMEQQEEEKSQVIRPTETEVLVSIIGDDKLALAAELVSELWNAGIKAE--YKVSTRKAKHLKRAK 714
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 384475554 437 EAGIPLVAIIGEQELKDGVIKLRSVTSREEVDVRREDLVEEIKRR 481
Cdd:PLN02972 715 ESGIPWMVLVGEKELSKGFVKLKNLEAGVEEEVDRTCFVQELKAE 759
|
|
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
56-481 |
1.18e-101 |
|
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: 310.90 E-value: 1.18e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 56 LKTPKGTRDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGED--SKLIYDLKDQGGELLSLRYDLTV 133
Cdd:COG0124 4 IQAPRGTRDILPEESAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKIGEDivEKEMYTFEDRGGRSLTLRPEGTA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 134 PFARYLAMNKLTN---IKRYHIAK------------------DFDIAGNFDPMIpDAECLKIMCEILSSLQIGDFLVKVN 192
Cdd:COG0124 84 PVARAVAEHGNELpfpFKLYYIGPvfryerpqkgryrqfhqfGVEVIGSDSPLA-DAEVIALAADLLKALGLKDFTLEIN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 193 DRrildgmfaicGVSDSKFRTICSSVDKLDKVSWEEVknemvgekgLAPEVADRI------------GDYVQqhggvSLV 260
Cdd:COG0124 163 SR----------GLPEERAEALLRYLDKLDKIGHEDV---------LDEDSQRRLetnplraildskGPDCQ-----EVL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 261 EQLlqdPKLSQNKqALEGLGDLKLLFEYLTLFGIDdkISFDLSLARGLDYYTGVIYEAVLLQTPAQageeplgvGSVAAG 340
Cdd:COG0124 219 ADA---PKLLDYL-GEEGLAHFEEVLELLDALGIP--YVIDPRLVRGLDYYTGTVFEIVTDGLGAQ--------GSVCGG 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 341 GRYDGLVGMFDpkGRKVPCVGLSIGVERIFSIVEQRLEALEEKirtTETQVLVASAQKKLLEERLKLVSELWDAGIKAEL 420
Cdd:COG0124 285 GRYDGLVEQLG--GPPTPAVGFAIGLERLLLLLEELGLLPAAE---PPPDVYVVPLGEEARAEALKLAQELRAAGIRVEL 359
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 384475554 421 -LYKKNPKllNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVDVRREDLVEEIKRR 481
Cdd:COG0124 360 dLGGRKLK--KQLKYADKSGAPFVLILGEDELANGTVTLKDLATGEQETVPLDELVEYLKEL 419
|
|
| hisS |
TIGR00442 |
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ... |
57-469 |
5.86e-88 |
|
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: 275.13 E-value: 5.86e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 57 KTPKGTRDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGEDS----KLIYDLKDQGGELLSLRYDLT 132
Cdd:TIGR00442 1 QKPRGTRDFLPEEMIKWQYIEETIREVFERYGFKEIRTPIFEYTELFKRKVGEETdivsKEMYTFKDKGGRSLTLRPEGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 133 VPFARYLAMNKLTN---IKRYHIAK------------------DFDIAGNFDPMIpDAECLKIMCEILSSLQIGDFLVKV 191
Cdd:TIGR00442 81 APVARAVIENKLLLpkpFKLYYIGPmfryerpqkgryrqfhqfGVEVIGSDSPLA-DAEIIALAADILKELGLKDFTLEI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 192 NDRRILDGMFAicgvsdsKFRTICSSVDK-LDKVSWEEVKNEMVGEKGLAPEVADRIGDYVQQhggvslveqllqDPKLS 270
Cdd:TIGR00442 160 NSLGILEGRLE-------YREALIRYLDKhKDKLGEDSVRRLEKNPLRILDSKNEKIQELLKN------------APKIL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 271 QNKQAlEGLGDLKLLFEYLTLFGIddKISFDLSLARGLDYYTGVIYEAVLLQTPAQageeplgvGSVAAGGRYDGLVGMF 350
Cdd:TIGR00442 221 DFLCE-ESRAHFEELKELLDALGI--PYKIDPSLVRGLDYYTGTVFEFVTDDLGAQ--------GSICGGGRYDGLVEEL 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 351 DpkGRKVPCVGLSIGVERIFSIVEQRLEALEEKirtTETQVLVASAQKKLLEERLKLVSELWDAGIKAElLYKKNPKLLN 430
Cdd:TIGR00442 290 G--GPPTPAVGFAIGIERLILLLEELGLIPPPS---KKPDVYVVPLGEEAELEALKLAQKLRKAGIRVE-VDLGGRKLKK 363
|
410 420 430
....*....|....*....|....*....|....*....
gi 384475554 431 QLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVDV 469
Cdd:TIGR00442 364 QLKYADKLGARFALIIGEDELENGTVTLKDLETGEQETV 402
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
69-374 |
1.81e-87 |
|
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: 268.70 E-value: 1.81e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 69 QMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGED-SKLIYDLKDQGGELLSLRYDLTVPFARYLAMNKL--- 144
Cdd:cd00773 1 EAALRRYIEDTLREVFERYGYEEIDTPVFEYTELFLRKSGDEvSKEMYRFKDKGGRDLALRPDLTAPVARAVAENLLslp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 145 TNIKRYHIAK------------------DFDIAGnFDPMIPDAECLKIMCEILSSLQIGDFLVKVNDRRILDGmfaICGV 206
Cdd:cd00773 81 LPLKLYYIGPvfryerpqkgryrefyqvGVEIIG-SDSPLADAEVIALAVEILEALGLKDFQIKINHRGILDG---IAGL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 207 SDSKFRTICSSVDKLDKvsweevknemvgekglapevadrigdyvqqhggvslveqllqdpklsqnkqalEGLGDLKLLF 286
Cdd:cd00773 157 LEDREEYIERLIDKLDK-----------------------------------------------------EALAHLEKLL 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 287 EYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLLQTPAQageeplgvGSVAAGGRYDGLVGMFDpkGRKVPCVGLSIGV 366
Cdd:cd00773 184 DYLEALGVDIKYSIDLSLVRGLDYYTGIVFEAVADGLGAQ--------GSIAGGGRYDGLLEEFG--GEDVPAVGFAIGL 253
|
....*...
gi 384475554 367 ERIFSIVE 374
Cdd:cd00773 254 ERLLLALE 261
|
|
| tRNA-synt_His |
pfam13393 |
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ... |
61-369 |
1.20e-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: 140.03 E-value: 1.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 61 GTRDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGEDSKLIYDLKDQGGELLSLRYDLTVPFARYLA 140
Cdd:pfam13393 1 GIRDLLPPEARRIEELRRRLLDLFRSWGYELVMPPLLEYLDSLLTGTGADLDQTFKLVDQSGRLLGLRADITPQVARIDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 141 mnKLTNIKR----------YHIAKDfdiaGNFDPMIP---------------DAECLKIMCEILSSLQIGDFLVKVNDRR 195
Cdd:pfam13393 81 --HRLNRPGplrlcyagsvLRTRPK----GLGRSREPlqvgaelighagieaDAEIISLLLEALAAAGVPGVTLDLGHVG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 196 ILDGMFAICGVSDSKFRTICSSVDKLDkvsWEEVKnEMVGEKGLAPEVADRIGDYVQQHGGVSLVEQLLQDpkLSQNKQA 275
Cdd:pfam13393 155 LVRALLEAAGLSEALEEALRAALQRKD---AAELA-ELAAEAGLPPALRRALLALPDLYGGPEVLDEARAA--LPGLPAL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 276 LEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLlqtpAQAGEEplgvgsVAAGGRYDGLVGMFdpkGR 355
Cdd:pfam13393 229 QEALDELEALAALLEALGDGVRLTFDLAELRGYEYYTGIVFAAYA----PGVGEP------LARGGRYDDLGAAF---GR 295
|
330
....*....|....
gi 384475554 356 KVPCVGLSIGVERI 369
Cdd:pfam13393 296 ARPATGFSLDLEAL 309
|
|
| HisRS_RNA |
cd00938 |
HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS ... |
5-49 |
7.06e-17 |
|
HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). This domain consists of a helix- turn- helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238474 [Multi-domain] Cd Length: 45 Bit Score: 74.04 E-value: 7.06e-17
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 384475554 5 AALEELVKLQGERVRGLKQQKASAELIEEEVAKLLKLKAQLGPDE 49
Cdd:cd00938 1 AKLEEAVKLQGELVRKLKAEKASKEQIAEEVAKLLELKAQLGGDE 45
|
|
| WHEP-TRS |
pfam00458 |
WHEP-TRS domain; |
7-45 |
4.33e-09 |
|
WHEP-TRS domain;
Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 52.11 E-value: 4.33e-09
10 20 30
....*....|....*....|....*....|....*....
gi 384475554 7 LEELVKLQGERVRGLKQQKASAELIEEEVAKLLKLKAQL 45
Cdd:pfam00458 1 LTEKIKAQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQY 39
|
|
| WHEP-TRS |
smart00991 |
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ... |
8-45 |
1.58e-08 |
|
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of higher eukaryote aminoacyl-transfer RNA synthetases; This domain is present one to six times in the several enzymes. There are three copies in mammalian multifunctional aminoacyl-tRNA synthetase in a region that separates the N-terminal glutamyl-tRNA synthetase domain from the C-terminal prolyl-tRNA synthetase domain, and six copies in the intercatalytic region of the Drosophila enzyme. The domain is found at the N-terminal extremity of the mammalian tryptophanyl- tRNA synthetase and histidyl-tRNA synthetase, and the mammalian, insect, nematode and plant glycyl- tRNA synthetases. This domain could contain a central alpha-helical region and may play a role in the association of tRNA-synthetases into multienzyme complexes.
Pssm-ID: 214960 [Multi-domain] Cd Length: 56 Bit Score: 50.80 E-value: 1.58e-08
10 20 30
....*....|....*....|....*....|....*...
gi 384475554 8 EELVKLQGERVRGLKQQKASAELIEEEVAKLLKLKAQL 45
Cdd:smart00991 1 EEAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQL 38
|
|
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
5-88 |
1.03e-03 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 41.65 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 5 AALEELVKLQGERVRGLKQQKASAELIEEEVAKLLKLKAQLgpdESKQKFVLKTPKGTRDYSPRQMAVREKVFDVIIR-- 82
Cdd:PLN02734 10 AEKQAAVTAQGNAVRALKASKADKAEIDAAIEKLKALKLEK---SALEKELQAAVGAGGDGAASKEAFRQAVVNTLERrl 86
|
90
....*....|
gi 384475554 83 ----CFKRHG 88
Cdd:PLN02734 87 fyipSFKIYG 96
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02972 |
PLN02972 |
Histidyl-tRNA synthetase |
57-481 |
0e+00 |
|
Histidyl-tRNA synthetase
Pssm-ID: 215525 [Multi-domain] Cd Length: 763 Bit Score: 528.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 57 KTPKGTRDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGEDSKLIYDLKDQGGELLSLRYDLTVPFA 136
Cdd:PLN02972 328 KIPKGTRDFAKEQMAIREKAFSIITSVFKRHGATALDTPVFELRETLMGKYGEDSKLIYDLADQGGELCSLRYDLTVPFA 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 137 RYLAMNKLTNIKRYHIAK------------------DFDIAGNFDPMIPDAECLKIMCEILSSLQIGDFLVKVNDRRILD 198
Cdd:PLN02972 408 RYVAMNGITSFKRYQIAKvyrrdnpskgryrefyqcDFDIAGVYEPMGPDFEIIKVLTELLDELDIGTYEVKLNHRKLLD 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 199 GMFAICGVSDSKFRTICSSVDKLDKVSWEEVKNEMVGEKGLAPEVADRIGDYVQQHGG-VSLVEQLLQ-DPKLSQNKQAL 276
Cdd:PLN02972 488 GMLEICGVPPEKFRTICSSIDKLDKQSFEQVKKEMVEEKGLSNETADKIGNFVKERGPpLELLSKLRQeGSEFLGNASSR 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 277 EGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLLQTPaqageeplgVGSVAAGGRYDGLVGMFDpkGRK 356
Cdd:PLN02972 568 AALDELEIMFKALEKSKAIGKIVFDLSLARGLDYYTGVIYEAVFKGAQ---------VGSIAAGGRYDNLVGMFS--GKQ 636
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 357 VPCVGLSIGVERIFSIVEQRLEALEEKIRTTETQVLVASAQKKLLEERLKLVSELWDAGIKAEllYKKNPKLLNQLQYCE 436
Cdd:PLN02972 637 VPAVGVSLGIERVFAIMEQQEEEKSQVIRPTETEVLVSIIGDDKLALAAELVSELWNAGIKAE--YKVSTRKAKHLKRAK 714
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 384475554 437 EAGIPLVAIIGEQELKDGVIKLRSVTSREEVDVRREDLVEEIKRR 481
Cdd:PLN02972 715 ESGIPWMVLVGEKELSKGFVKLKNLEAGVEEEVDRTCFVQELKAE 759
|
|
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
56-481 |
1.18e-101 |
|
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: 310.90 E-value: 1.18e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 56 LKTPKGTRDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGED--SKLIYDLKDQGGELLSLRYDLTV 133
Cdd:COG0124 4 IQAPRGTRDILPEESAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKIGEDivEKEMYTFEDRGGRSLTLRPEGTA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 134 PFARYLAMNKLTN---IKRYHIAK------------------DFDIAGNFDPMIpDAECLKIMCEILSSLQIGDFLVKVN 192
Cdd:COG0124 84 PVARAVAEHGNELpfpFKLYYIGPvfryerpqkgryrqfhqfGVEVIGSDSPLA-DAEVIALAADLLKALGLKDFTLEIN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 193 DRrildgmfaicGVSDSKFRTICSSVDKLDKVSWEEVknemvgekgLAPEVADRI------------GDYVQqhggvSLV 260
Cdd:COG0124 163 SR----------GLPEERAEALLRYLDKLDKIGHEDV---------LDEDSQRRLetnplraildskGPDCQ-----EVL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 261 EQLlqdPKLSQNKqALEGLGDLKLLFEYLTLFGIDdkISFDLSLARGLDYYTGVIYEAVLLQTPAQageeplgvGSVAAG 340
Cdd:COG0124 219 ADA---PKLLDYL-GEEGLAHFEEVLELLDALGIP--YVIDPRLVRGLDYYTGTVFEIVTDGLGAQ--------GSVCGG 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 341 GRYDGLVGMFDpkGRKVPCVGLSIGVERIFSIVEQRLEALEEKirtTETQVLVASAQKKLLEERLKLVSELWDAGIKAEL 420
Cdd:COG0124 285 GRYDGLVEQLG--GPPTPAVGFAIGLERLLLLLEELGLLPAAE---PPPDVYVVPLGEEARAEALKLAQELRAAGIRVEL 359
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 384475554 421 -LYKKNPKllNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVDVRREDLVEEIKRR 481
Cdd:COG0124 360 dLGGRKLK--KQLKYADKSGAPFVLILGEDELANGTVTLKDLATGEQETVPLDELVEYLKEL 419
|
|
| hisS |
TIGR00442 |
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ... |
57-469 |
5.86e-88 |
|
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: 275.13 E-value: 5.86e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 57 KTPKGTRDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGEDS----KLIYDLKDQGGELLSLRYDLT 132
Cdd:TIGR00442 1 QKPRGTRDFLPEEMIKWQYIEETIREVFERYGFKEIRTPIFEYTELFKRKVGEETdivsKEMYTFKDKGGRSLTLRPEGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 133 VPFARYLAMNKLTN---IKRYHIAK------------------DFDIAGNFDPMIpDAECLKIMCEILSSLQIGDFLVKV 191
Cdd:TIGR00442 81 APVARAVIENKLLLpkpFKLYYIGPmfryerpqkgryrqfhqfGVEVIGSDSPLA-DAEIIALAADILKELGLKDFTLEI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 192 NDRRILDGMFAicgvsdsKFRTICSSVDK-LDKVSWEEVKNEMVGEKGLAPEVADRIGDYVQQhggvslveqllqDPKLS 270
Cdd:TIGR00442 160 NSLGILEGRLE-------YREALIRYLDKhKDKLGEDSVRRLEKNPLRILDSKNEKIQELLKN------------APKIL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 271 QNKQAlEGLGDLKLLFEYLTLFGIddKISFDLSLARGLDYYTGVIYEAVLLQTPAQageeplgvGSVAAGGRYDGLVGMF 350
Cdd:TIGR00442 221 DFLCE-ESRAHFEELKELLDALGI--PYKIDPSLVRGLDYYTGTVFEFVTDDLGAQ--------GSICGGGRYDGLVEEL 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 351 DpkGRKVPCVGLSIGVERIFSIVEQRLEALEEKirtTETQVLVASAQKKLLEERLKLVSELWDAGIKAElLYKKNPKLLN 430
Cdd:TIGR00442 290 G--GPPTPAVGFAIGIERLILLLEELGLIPPPS---KKPDVYVVPLGEEAELEALKLAQKLRKAGIRVE-VDLGGRKLKK 363
|
410 420 430
....*....|....*....|....*....|....*....
gi 384475554 431 QLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVDV 469
Cdd:TIGR00442 364 QLKYADKLGARFALIIGEDELENGTVTLKDLETGEQETV 402
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
69-374 |
1.81e-87 |
|
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: 268.70 E-value: 1.81e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 69 QMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGED-SKLIYDLKDQGGELLSLRYDLTVPFARYLAMNKL--- 144
Cdd:cd00773 1 EAALRRYIEDTLREVFERYGYEEIDTPVFEYTELFLRKSGDEvSKEMYRFKDKGGRDLALRPDLTAPVARAVAENLLslp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 145 TNIKRYHIAK------------------DFDIAGnFDPMIPDAECLKIMCEILSSLQIGDFLVKVNDRRILDGmfaICGV 206
Cdd:cd00773 81 LPLKLYYIGPvfryerpqkgryrefyqvGVEIIG-SDSPLADAEVIALAVEILEALGLKDFQIKINHRGILDG---IAGL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 207 SDSKFRTICSSVDKLDKvsweevknemvgekglapevadrigdyvqqhggvslveqllqdpklsqnkqalEGLGDLKLLF 286
Cdd:cd00773 157 LEDREEYIERLIDKLDK-----------------------------------------------------EALAHLEKLL 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 287 EYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLLQTPAQageeplgvGSVAAGGRYDGLVGMFDpkGRKVPCVGLSIGV 366
Cdd:cd00773 184 DYLEALGVDIKYSIDLSLVRGLDYYTGIVFEAVADGLGAQ--------GSIAGGGRYDGLLEEFG--GEDVPAVGFAIGL 253
|
....*...
gi 384475554 367 ERIFSIVE 374
Cdd:cd00773 254 ERLLLALE 261
|
|
| PRK12420 |
PRK12420 |
histidyl-tRNA synthetase; Provisional |
53-469 |
4.33e-69 |
|
histidyl-tRNA synthetase; Provisional
Pssm-ID: 237097 [Multi-domain] Cd Length: 423 Bit Score: 226.92 E-value: 4.33e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 53 KFVLKTPKGTRDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYG---EDSKLIYDLKDQGGELLSLRY 129
Cdd:PRK12420 1 MMEMRNVKGTKDYLPEEQVLRNKIKRALEDVFERYGCKPLETPTLNMYELMSSKYGggdEILKEIYTLTDQGKRDLALRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 130 DLTVPFARYLAMNKltNI----KRYHIAK------------------DFDIAGNFDPMiPDAECLKIMCEILSSLQIgDF 187
Cdd:PRK12420 81 DLTIPFAKVVAMNP--NIrlpfKRYEIGKvfrdgpikqgrfrefiqcDVDIVGVESVM-AEAELMSMAFELFRRLNL-EV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 188 LVKVNDRRILDGMFAICGVSDSKFRTICSSVDKLDKVSWEEVKNEMVgEKGLAPEVADRIGDYVQQHGGVSLVEQllqdP 267
Cdd:PRK12420 157 TIQYNNRKLLNGILQAIGIPTELTSDVILSLDKIEKIGIDGVRKDLL-ERGISEEMADTICNTVLSCLQLSIADF----K 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 268 KLSQNKQALEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEaVLLQTPAQAgeeplgvGSVAAGGRYDGLV 347
Cdd:PRK12420 232 EAFNNPLVAEGVNELQQLQQYLIALGINENCIFNPFLARGLTMYTGTVYE-IFLKDGSIT-------SSIGSGGRYDNII 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 348 GMFDPKGRKVPCVGLSIGVERIfsiveqrLEALEEKIRTTET-QVLVASAQKKLleERLKLVSELW-DAGIKAELLYkKN 425
Cdd:PRK12420 304 GAFRGDDMNYPTVGISFGLDVI-------YTALSQKETISSTaDVFIIPLGTEL--QCLQIAQQLRsTTGLKVELEL-AG 373
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 384475554 426 PKLLNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVDV 469
Cdd:PRK12420 374 RKLKKALNYANKENIPYVLIIGEEEVSTGTVMLRNMKEGSEVKV 417
|
|
| HisZ |
COG3705 |
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism]; |
67-369 |
1.80e-42 |
|
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism];
Pssm-ID: 442919 [Multi-domain] Cd Length: 312 Bit Score: 153.02 E-value: 1.80e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 67 PRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGEDSKL-IYDLKDQGGELLSLRYDLTVPFARYLAmNKLT 145
Cdd:COG3705 2 PEEAARKEELRRRLLDVFRSWGYELVEPPLLEYLDSLLTGSGADLDLqTFKLVDQLGRTLGLRPDMTPQVARIAA-TRLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 146 NIKR----------YHIAKDF------------------DIAGnfdpmipDAECLKIMCEILSSLQIGDFLVKVNDRRIL 197
Cdd:COG3705 81 NRPGplrlcyagnvFRTRPSGlgrsreflqagaelighaGLEA-------DAEVIALALEALKAAGLEDFTLDLGHVGLF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 198 DGMFAICGVSDSKFRTICSSVDKLDKVsweEVKnEMVGEKGLAPEVADRIGDYVQQHGGVSLVEQLLqdpKLSQNKQALE 277
Cdd:COG3705 154 RALLEALGLSEEQREELRRALARKDAV---ELE-ELLAELGLSEELAEALLALPELYGGEEVLARAR---ALLLDAAIRA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 278 GLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLlqtpAQAGEEplgvgsVAAGGRYDGLVGMFdpkGRKV 357
Cdd:COG3705 227 ALDELEALAEALAARGPDVRLTFDLSELRGYDYYTGIVFEAYA----PGVGDP------LARGGRYDGLLAAF---GRAR 293
|
330
....*....|..
gi 384475554 358 PCVGLSIGVERI 369
Cdd:COG3705 294 PATGFSLDLDRL 305
|
|
| PLN02530 |
PLN02530 |
histidine-tRNA ligase |
47-474 |
5.52e-42 |
|
histidine-tRNA ligase
Pssm-ID: 178145 [Multi-domain] Cd Length: 487 Bit Score: 156.06 E-value: 5.52e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 47 PDESKQKFVLKTPKGTRDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGED-SKLIYDLKDQGGELL 125
Cdd:PLN02530 61 QEDGKPKIDVNPPKGTRDFPPEDMRLRNWLFDHFREVSRLFGFEEVDAPVLESEELYIRKAGEEiTDQLYNFEDKGGRRV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 126 SLRYDLTVPFARyLAMNKLTNI----------------------KRYHIAKDFDIAGnFDPMIPDAECLKIMCEILSSLQ 183
Cdd:PLN02530 141 ALRPELTPSLAR-LVLQKGKSLslplkwfaigqcwryermtrgrRREHYQWNMDIIG-VPGVEAEAELLAAIVTFFKRVG 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 184 I--GDFLVKVNDRRILDGMFAICGVSDSKFRTICSSVDKLDKVSWEEVKNEMvGEKGLAPEVADRIGDyVQQHGGVSLVE 261
Cdd:PLN02530 219 ItsSDVGIKVSSRKVLQAVLKSYGIPEESFAPVCVIVDKLEKLPREEIEKEL-DTLGVSEEAIEGILD-VLSLKSLDDLE 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 262 QLLqdpklsqnKQALEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVllqtpAQAGEeplgVGSVAAGG 341
Cdd:PLN02530 297 ALL--------GADSEAVADLKQLFSLAEAYGYQDWLVFDASVVRGLAYYTGIVFEGF-----DRAGK----LRAICGGG 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 342 RYDGLVGMFDpkGRKVPCVGLSIGVERIFSIVEQRlEALEEKIRTTETqvLVASAQKKLLEERLKLVSELWDAGIKAEL- 420
Cdd:PLN02530 360 RYDRLLSTFG--GEDTPACGFGFGDAVIVELLKEK-GLLPELPHQVDD--VVFALDEDLQGAAAGVASRLREKGRSVDLv 434
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 384475554 421 LYKKNPKLLnqLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVDVRREDL 474
Cdd:PLN02530 435 LEPKKLKWV--FKHAERIGAKRLVLVGASEWERGMVRVKDLSSGEQTEVKLDEL 486
|
|
| hisZ_biosyn_reg |
TIGR00443 |
ATP phosphoribosyltransferase, regulatory subunit; Apparant second copies of histidyl-tRNA ... |
63-369 |
5.58e-42 |
|
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: 152.00 E-value: 5.58e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 63 RDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGEDSKLIYDLKDQGGELLSLRYDLTVPFARyLAMN 142
Cdd:TIGR00443 1 RDLLPEEAARKEEIERQLQDVFRSWGYQEIITPTLEYLDTLSAGSGILNEDLFKLFDQLGRVLGLRPDMTAPIAR-LVST 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 143 KLTNIKR----------YHIAKDFDIAGN-----------FDPMIPDAECLKIMCEILSSLQIGDFLVKVNDRRILDGMF 201
Cdd:TIGR00443 80 RLRDRPLplrlcyagnvFRTNESGGGRSReftqagveligAGGPAADAEVIALLIEALKALGLKDFKIELGHVGLVRALL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 202 AICGVSDSKFRTICSSVDKLDKVSWEEVknemVGEKGLAPEVADRIGDYVQQHGGVSLVEQLLQdpKLSQNKQALEGLGD 281
Cdd:TIGR00443 160 EEAGLPEEAREALREALARKDLVALEEL----VAELGLSPEVRERLLALPRLRGDGEEVLEEAR--ALAGSETAEAALDE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 282 LKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLLQTPAQageeplgvgsVAAGGRYDGLVGMFdpkGRKVPCVG 361
Cdd:TIGR00443 234 LEAVLELLEARGVEEYISLDLGLVRGYHYYTGLIFEGYAPGLGAP----------LAGGGRYDELLGRF---GRPLPATG 300
|
....*...
gi 384475554 362 LSIGVERI 369
Cdd:TIGR00443 301 FALNLERL 308
|
|
| hisZ |
PRK12292 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
59-420 |
2.90e-40 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 237043 [Multi-domain] Cd Length: 391 Bit Score: 149.25 E-value: 2.90e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 59 PKGTRDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLM--GKYGEDSKLIYDLKDQGGELLSLRYDLTVPFA 136
Cdd:PRK12292 6 PEGIRDLLPEEARKIEEIRRRLLDLFRRWGYEEVITPTLEYLDTLLagGGAILDLRTFKLVDQLSGRTLGLRPDMTAQIA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 137 RyLAMNKLTNIKR----YHIAKDFDIAGNF-----------------DPMIPDAECLKIMCEILSSLQIGDFLVKVNDRR 195
Cdd:PRK12292 86 R-IAATRLANRPGplrlCYAGNVFRAQERGlgrsreflqsgveligdAGLEADAEVILLLLEALKALGLPNFTLDLGHVG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 196 ILDGMFAICGVSDSKFRTICSSVDKLDKVSWEEVknemvgEKGLAPEVADRIGDYVQQHGGVSLVEQLLQdpkLSQNKQA 275
Cdd:PRK12292 165 LFRALLEAAGLSEELEEVLRRALANKDYVALEEL------VLDLSEELRDALLALPRLRGGREVLEEARK---LLPSLPI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 276 LEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLLQTPAqageeplgvgSVAAGGRYDGLVGMFdpkGR 355
Cdd:PRK12292 236 KRALDELEALAEALEKYGYGIPLSLDLGLLRHLDYYTGIVFEGYVDGVGN----------PIASGGRYDDLLGRF---GR 302
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 384475554 356 KVPCVGLSIGVERIfsiveqrLEALEEKiRTTETQVLVASAQKKLLEERLKLVSELWDAGIKAEL 420
Cdd:PRK12292 303 ARPATGFSLDLDRL-------LELQLEL-PVEARKDLVIAPDSEALAAALAAAQELRKKGEIVVL 359
|
|
| tRNA-synt_His |
pfam13393 |
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ... |
61-369 |
1.20e-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: 140.03 E-value: 1.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 61 GTRDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGEDSKLIYDLKDQGGELLSLRYDLTVPFARYLA 140
Cdd:pfam13393 1 GIRDLLPPEARRIEELRRRLLDLFRSWGYELVMPPLLEYLDSLLTGTGADLDQTFKLVDQSGRLLGLRADITPQVARIDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 141 mnKLTNIKR----------YHIAKDfdiaGNFDPMIP---------------DAECLKIMCEILSSLQIGDFLVKVNDRR 195
Cdd:pfam13393 81 --HRLNRPGplrlcyagsvLRTRPK----GLGRSREPlqvgaelighagieaDAEIISLLLEALAAAGVPGVTLDLGHVG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 196 ILDGMFAICGVSDSKFRTICSSVDKLDkvsWEEVKnEMVGEKGLAPEVADRIGDYVQQHGGVSLVEQLLQDpkLSQNKQA 275
Cdd:pfam13393 155 LVRALLEAAGLSEALEEALRAALQRKD---AAELA-ELAAEAGLPPALRRALLALPDLYGGPEVLDEARAA--LPGLPAL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 276 LEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLlqtpAQAGEEplgvgsVAAGGRYDGLVGMFdpkGR 355
Cdd:pfam13393 229 QEALDELEALAALLEALGDGVRLTFDLAELRGYEYYTGIVFAAYA----PGVGEP------LARGGRYDDLGAAF---GR 295
|
330
....*....|....
gi 384475554 356 KVPCVGLSIGVERI 369
Cdd:pfam13393 296 ARPATGFSLDLEAL 309
|
|
| HisRS_anticodon |
cd00859 |
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases ... |
388-479 |
2.78e-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: 107.63 E-value: 2.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 388 ETQVLVASAQKKLLEERLKLVSELWDAGIKAELLYKkNPKLLNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEV 467
Cdd:cd00859 1 EVDVYVVPLGEGALSEALELAEQLRDAGIKAEIDYG-GRKLKKQFKYADRSGARFAVILGEDELAAGVVTVKDLETGEQE 79
|
90
....*....|..
gi 384475554 468 DVRREDLVEEIK 479
Cdd:cd00859 80 TVALDELVEELK 91
|
|
| syh |
CHL00201 |
histidine-tRNA synthetase; Provisional |
60-478 |
1.97e-20 |
|
histidine-tRNA synthetase; Provisional
Pssm-ID: 164576 [Multi-domain] Cd Length: 430 Bit Score: 93.43 E-value: 1.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 60 KGTRDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGEDSKLI----YDLKDQGGELLSLRYDLTVPF 135
Cdd:CHL00201 8 RGTKDILPDEINYWQFIHDKALTLLSLANYSEIRTPIFENSSLYDRGIGETTDIVnkemYRFTDRSNRDITLRPEGTAGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 136 ARYLAMNKLT---NIKR-YHIAKDF------------------DIAGNFDPMiPDAECLKIMCEILSSLQIGDFLVKVN- 192
Cdd:CHL00201 88 VRAFIENKMDyhsNLQRlWYSGPMFryerpqsgrqrqfhqlgiEFIGSIDAR-ADTEVIHLAMQIFNELQVKNLILDINs 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 193 -----DRRILDgmfaicgvsdSKFRTICSSV-DKLDKVSweevKNEMVGEkglaP-EVADRIGDYVQqhggvslvEQLLQ 265
Cdd:CHL00201 167 igkleDRQSYQ----------LKLVEYLSQYqDDLDTDS----QNRLYSN----PiRILDSKNLKTQ--------EILDG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 266 DPKLSQ--NKQALEGLGDLkllFEYLTLFGIDDKISFdlSLARGLDYYTGVIYEAVLLQTPAQageeplgvGSVAAGGRY 343
Cdd:CHL00201 221 APKISDflSLESTEHFYDV---CTYLNLLNIPYKINY--KLVRGLDYYNDTAFEIKTLSSNGQ--------DTICGGGRY 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 344 DGLVGMFDpkGRKVPCVGLSIGVERIFSIVEQRLEALEEKIrttetQVLVASAQKKLLEERLKLVSELWDAGIKAELLYk 423
Cdd:CHL00201 288 DSLIHQLG--GPKTPAVGCAIGLERLLLIAKDNIILPKQSI-----DVYIATQGLKAQKKGWEIIQFLEKQNIKFELDL- 359
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 384475554 424 KNPKLLNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVDVRREDLVEEI 478
Cdd:CHL00201 360 SSSNFHKQIKQAGKKRAKACIILGDNEIMDNCITIKWLDEQVQENAQYSNFKQEI 414
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
390-481 |
3.11e-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: 76.86 E-value: 3.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 390 QVLVASAQKK---LLEERLKLVSELWDAGIKAELLYKkNPKLLNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREE 466
Cdd:pfam03129 1 QVVVIPLGEKaeeLEEYAQKLAEELRAAGIRVELDDR-NESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQ 79
|
90
....*....|....*
gi 384475554 467 VDVRREDLVEEIKRR 481
Cdd:pfam03129 80 ETVSLDELVEKLKEL 94
|
|
| HisRS_RNA |
cd00938 |
HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS ... |
5-49 |
7.06e-17 |
|
HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). This domain consists of a helix- turn- helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238474 [Multi-domain] Cd Length: 45 Bit Score: 74.04 E-value: 7.06e-17
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 384475554 5 AALEELVKLQGERVRGLKQQKASAELIEEEVAKLLKLKAQLGPDE 49
Cdd:cd00938 1 AKLEEAVKLQGELVRKLKAEKASKEQIAEEVAKLLELKAQLGGDE 45
|
|
| hisZ |
PRK12295 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
70-369 |
4.97e-16 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 183413 [Multi-domain] Cd Length: 373 Bit Score: 79.59 E-value: 4.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 70 MAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGED-SKLIYDLKDQGGELLSLRYDLTVPFAR-YLAMNK---- 143
Cdd:PRK12295 4 LSASAAAAEALLASFEAAGAVRVDPPILQPAEPFLDLSGEDiRRRIFVTSDENGEELCLRPDFTIPVCRrHIATAGgepa 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 144 ----LTNIKRYHIAKD-------FDIAGNFDPMIPDAECLKIMCEILSSLQIGDFLVKVNDRRILDGMFAICGVSDS-KF 211
Cdd:PRK12295 84 ryayLGEVFRQRRDRAseflqagIESFGRADPAAADAEVLALALEALAALGPGDLEVRLGDVGLFAALVDALGLPPGwKR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 212 RTIcssVDKLDKVSWEEVKNEMVGEKGLAPEVADRIGDYVQQHGGVS-LVEQLLQDPKLSQN------------------ 272
Cdd:PRK12295 164 RLL---RHFGRPRSLDALLARLAGPRVDPLDEHAGVLAALADEAAARaLVEDLMSIAGISPVggrspaeiarrllekaal 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 273 ------------------------KQALEGL----GDLKL-------LFE----YLTLFGID-DKISFDLSLARGLDYYT 312
Cdd:PRK12295 241 aaaarlpaealavlerflaisgppDAALAALralaADAGLdldaaldRFEarlaALAARGIDlERLRFSASFGRPLDYYT 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 384475554 313 GVIYEAvllqTPAQAGEEPLgvgsvAAGGRYDGLVGMFDpKGRKVPCVGLSIGVERI 369
Cdd:PRK12295 321 GFVFEI----RAAGNGDPPL-----AGGGRYDGLLTRLG-AGEPIPAVGFSIWLDRL 367
|
|
| WHEPGMRS_RNA |
cd01200 |
EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher ... |
8-49 |
1.20e-09 |
|
EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in three copies in the mammalian bifunctional EPRS in a region that separates the N-terminal GluRS from the C-terminal ProRS. In the Drosophila EPRS, this domain is repeated six times. It is found at the N-terminus of TrpRS, HisRS and GlyR and at the C-terminus of MetRS. This domain consists of a helix- turn- helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238605 [Multi-domain] Cd Length: 42 Bit Score: 53.70 E-value: 1.20e-09
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 384475554 8 EELVKLQGERVRGLKQQKASAELIEEEVAKLLKLKAQLGPDE 49
Cdd:cd01200 1 YEKIAEQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKEAT 42
|
|
| PRK12421 |
PRK12421 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
59-415 |
1.29e-09 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 237098 Cd Length: 392 Bit Score: 59.98 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 59 PKGTRDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGEDSKL-IYDLKDQ-GGELLSLRYDLTVPFA 136
Cdd:PRK12421 10 PDGVADVLPEEAQKIERLRRRLLDLFASRGYQLVMPPLIEYLESLLTGAGQDLKLqTFKLIDQlSGRLMGVRADITPQVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 137 RYLA-MNKLTNIKRY-------HI---------------AKDFDIAGnfdpMIPDAECLKIMCEILSSLQIGDFLVKVND 193
Cdd:PRK12421 90 RIDAhLLNREGVARLcyagsvlHTlpqglfgsrtplqlgAELYGHAG----IEADLEIIRLMLGLLRNAGVPALHLDLGH 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 194 RRILDGMFAICGVSDSKFRTIcssVDKLDKVSWEEVKnEMVGEKGLAPEVADRIGDYVQQHGGVSLVEQLLQDpKLSQNK 273
Cdd:PRK12421 166 VGIFRRLAELAGLSPEEEEEL---FDLLQRKALPELA-EVCQNLGVGSDLRRMFYALARLNGGLEALDRALSV-LALQDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 274 QALEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYeAVLLQTPAQAgeeplgvgsVAAGGRYDGLVGMFdpk 353
Cdd:PRK12421 241 AIRQALDELKTLAAHLKNRWPELPVSIDLAELRGYHYHTGLVF-AAYIPGRGQA---------LARGGRYDGIGEAF--- 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 384475554 354 GRKVPCVGlsigveriFSIVEQRLEALEEKIRTTETQVLVASAQKKLLEErlklVSELWDAG 415
Cdd:PRK12421 308 GRARPATG--------FSMDLKELLALQFLEEEAGAILAPWGDDPDLLAA----IAELRQQG 357
|
|
| WHEP-TRS |
pfam00458 |
WHEP-TRS domain; |
7-45 |
4.33e-09 |
|
WHEP-TRS domain;
Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 52.11 E-value: 4.33e-09
10 20 30
....*....|....*....|....*....|....*....
gi 384475554 7 LEELVKLQGERVRGLKQQKASAELIEEEVAKLLKLKAQL 45
Cdd:pfam00458 1 LTEKIKAQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQY 39
|
|
| WHEP-TRS |
smart00991 |
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ... |
8-45 |
1.58e-08 |
|
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of higher eukaryote aminoacyl-transfer RNA synthetases; This domain is present one to six times in the several enzymes. There are three copies in mammalian multifunctional aminoacyl-tRNA synthetase in a region that separates the N-terminal glutamyl-tRNA synthetase domain from the C-terminal prolyl-tRNA synthetase domain, and six copies in the intercatalytic region of the Drosophila enzyme. The domain is found at the N-terminal extremity of the mammalian tryptophanyl- tRNA synthetase and histidyl-tRNA synthetase, and the mammalian, insect, nematode and plant glycyl- tRNA synthetases. This domain could contain a central alpha-helical region and may play a role in the association of tRNA-synthetases into multienzyme complexes.
Pssm-ID: 214960 [Multi-domain] Cd Length: 56 Bit Score: 50.80 E-value: 1.58e-08
10 20 30
....*....|....*....|....*....|....*...
gi 384475554 8 EELVKLQGERVRGLKQQKASAELIEEEVAKLLKLKAQL 45
Cdd:smart00991 1 EEAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQL 38
|
|
| HGTP_anticodon2 |
pfam12745 |
Anticodon binding domain of tRNAs; This is an HGTP_anticodon binding domain, found largely on ... |
391-481 |
3.90e-08 |
|
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: 54.53 E-value: 3.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 391 VLVASAQKKLL-EERLKLVSELWDAGIKAELLYKKNPKLLNQLQYCEEAGIPLVAIIGEQEL----KDGVIKLRSVTSRE 465
Cdd:pfam12745 8 VLVASFDASILrTTGVEILQELWAHGISADLAVDASYSPEDLVSRARDDGVSWIVIIKQQNKssdsKYKPLKVKNLLRKE 87
|
90 100
....*....|....*....|
gi 384475554 466 EVDVRREDLV----EEIKRR 481
Cdd:pfam12745 88 DVDLDSDELVswlrGEIRER 107
|
|
| MetRS_RNA |
cd00939 |
MetRS_RNA binding domain. This short RNA-binding domain is found at the C-terminus of MetRS in ... |
7-45 |
3.36e-06 |
|
MetRS_RNA binding domain. This short RNA-binding domain is found at the C-terminus of MetRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is repeated in Drosophila MetRS. This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238475 [Multi-domain] Cd Length: 45 Bit Score: 44.00 E-value: 3.36e-06
10 20 30
....*....|....*....|....*....|....*....
gi 384475554 7 LEELVKLQGERVRGLKQQKASAELIEEEVAKLLKLKAQL 45
Cdd:cd00939 1 LEKEVAEQGNKVRKLKASKADKSVWQPEVNKLLDLKKQL 39
|
|
| PRK03991 |
PRK03991 |
threonyl-tRNA synthetase; Validated |
365-485 |
1.21e-05 |
|
threonyl-tRNA synthetase; Validated
Pssm-ID: 235190 [Multi-domain] Cd Length: 613 Bit Score: 47.94 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 365 GVER-IFSIVE-QRLEALEEKIRT-----TETQVLVASAQKKLLEERLKLVSELWDAGIKAEL------LYKKnpkllnq 431
Cdd:PRK03991 469 SIERvIYALLEkAAKEEEEGKVPMlptwlSPTQVRVIPVSERHLDYAEEVADKLEAAGIRVDVddrdesLGKK------- 541
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 384475554 432 lqyCEEAG---IPLVAIIGEQELKDGVIklrSVTSREE---VDVRREDLVEEIKRRT-GQP 485
Cdd:PRK03991 542 ---IRDAGkewIPYVVVIGDKEMESGKL---TVTIREEsekVEMTLEELIERIKEETkGYP 596
|
|
| WEPRS_RNA |
cd00936 |
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ... |
14-44 |
8.41e-05 |
|
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in multiple copies in eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases (EPRS) in a region that separates the N-terminal glutamyl-tRNA synthetase (GluRS) from the C-terminal prolyl-tRNA synthetase (ProRS). It is also found at the N-terminus of vertebrate tryptophanyl-tRNA synthetases (TrpRS). This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238473 [Multi-domain] Cd Length: 50 Bit Score: 39.91 E-value: 8.41e-05
10 20 30
....*....|....*....|....*....|.
gi 384475554 14 QGERVRGLKQQKASAELIEEEVAKLLKLKAQ 44
Cdd:cd00936 8 QGDLVRELKAKKAPKEEIDAAVKKLLALKAD 38
|
|
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
5-88 |
1.03e-03 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 41.65 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 5 AALEELVKLQGERVRGLKQQKASAELIEEEVAKLLKLKAQLgpdESKQKFVLKTPKGTRDYSPRQMAVREKVFDVIIR-- 82
Cdd:PLN02734 10 AEKQAAVTAQGNAVRALKASKADKAEIDAAIEKLKALKLEK---SALEKELQAAVGAGGDGAASKEAFRQAVVNTLERrl 86
|
90
....*....|
gi 384475554 83 ----CFKRHG 88
Cdd:PLN02734 87 fyipSFKIYG 96
|
|
| ThrRS_anticodon |
cd00860 |
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases ... |
389-479 |
8.12e-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: 35.56 E-value: 8.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475554 389 TQVLVASAQKKLLEERLKLVSELWDAGIKAELLYKkNPKLLNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVD 468
Cdd:cd00860 2 VQVVVIPVTDEHLDYAKEVAKKLSDAGIRVEVDLR-NEKLGKKIREAQLQKIPYILVVGDKEVETGTVSVRTRDGGDLGS 80
|
90
....*....|.
gi 384475554 469 VRREDLVEEIK 479
Cdd:cd00860 81 MSLDEFIEKLK 91
|
|
| |
