|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02972 |
PLN02972 |
Histidyl-tRNA synthetase |
57-501 |
0e+00 |
|
Histidyl-tRNA synthetase
Pssm-ID: 215525 [Multi-domain] Cd Length: 763 Bit Score: 582.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 57 KTPKGTRDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGEDSKLIYDLKDQGGELLSLRYDLTVPFA 136
Cdd:PLN02972 328 KIPKGTRDFAKEQMAIREKAFSIITSVFKRHGATALDTPVFELRETLMGKYGEDSKLIYDLADQGGELCSLRYDLTVPFA 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 137 RYLAMNKLTNIKRYHIAKVYRRDNPamTRGRYREFYQCDFDIAGNFDPMIPDAECLKIMCEILSSLQIGDFLVKVNDRRI 216
Cdd:PLN02972 408 RYVAMNGITSFKRYQIAKVYRRDNP--SKGRYREFYQCDFDIAGVYEPMGPDFEIIKVLTELLDELDIGTYEVKLNHRKL 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 217 LDGMFAICGVSDSKFRTICSSVDKLDKVSWEEVKNEMVGEKGLAPEVADRIGDYVQQHGG-VSLVEQLLQ-DPKLSQNKQ 294
Cdd:PLN02972 486 LDGMLEICGVPPEKFRTICSSIDKLDKQSFEQVKKEMVEEKGLSNETADKIGNFVKERGPpLELLSKLRQeGSEFLGNAS 565
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 295 ALEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLLQTPaqageeplgVGSVAAGGRYDGLVGMFDpkG 374
Cdd:PLN02972 566 SRAALDELEIMFKALEKSKAIGKIVFDLSLARGLDYYTGVIYEAVFKGAQ---------VGSIAAGGRYDNLVGMFS--G 634
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 375 RKVPCVGLSIGVERIFSIVEQRLEALEEKIRTTETQVLVASAQKKLLEERLKLVSELWDAGIKAEllYKKNPKLLNQLQY 454
Cdd:PLN02972 635 KQVPAVGVSLGIERVFAIMEQQEEEKSQVIRPTETEVLVSIIGDDKLALAAELVSELWNAGIKAE--YKVSTRKAKHLKR 712
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 135123 455 CEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVDVRREDLVEEIKRR 501
Cdd:PLN02972 713 AKESGIPWMVLVGEKELSKGFVKLKNLEAGVEEEVDRTCFVQELKAE 759
|
|
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
56-501 |
6.96e-118 |
|
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: 353.27 E-value: 6.96e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 56 LKTPKGTRDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGED--SKLIYDLKDQGGELLSLRYDLTV 133
Cdd:COG0124 4 IQAPRGTRDILPEESAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKIGEDivEKEMYTFEDRGGRSLTLRPEGTA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 134 PFARYLAMNKLTN---IKRYHIAKVYRRDNPAmtRGRYREFYQCDFDIAGNFDPMIpDAECLKIMCEILSSLQIGDFLVK 210
Cdd:COG0124 84 PVARAVAEHGNELpfpFKLYYIGPVFRYERPQ--KGRYRQFHQFGVEVIGSDSPLA-DAEVIALAADLLKALGLKDFTLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 211 VNDRrildgmfaicGVSDSKFRTICSSVDKLDKVSWEEVknemvgekgLAPEVADRI------------GDYVQqhggvS 278
Cdd:COG0124 161 INSR----------GLPEERAEALLRYLDKLDKIGHEDV---------LDEDSQRRLetnplraildskGPDCQ-----E 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 279 LVEQLlqdPKLSQNKqALEGLGDLKLLFEYLTLFGIDdkISFDLSLARGLDYYTGVIYEAVLLQTPAQageeplgvGSVA 358
Cdd:COG0124 217 VLADA---PKLLDYL-GEEGLAHFEEVLELLDALGIP--YVIDPRLVRGLDYYTGTVFEIVTDGLGAQ--------GSVC 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 359 AGGRYDGLVGMFDpkGRKVPCVGLSIGVERIFSIVEQRLEALEEKirtTETQVLVASAQKKLLEERLKLVSELWDAGIKA 438
Cdd:COG0124 283 GGGRYDGLVEQLG--GPPTPAVGFAIGLERLLLLLEELGLLPAAE---PPPDVYVVPLGEEARAEALKLAQELRAAGIRV 357
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 135123 439 EL-LYKKNPKllNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVDVRREDLVEEIKRR 501
Cdd:COG0124 358 ELdLGGRKLK--KQLKYADKSGAPFVLILGEDELANGTVTLKDLATGEQETVPLDELVEYLKEL 419
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
69-394 |
5.41e-104 |
|
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: 311.84 E-value: 5.41e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 69 QMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGED-SKLIYDLKDQGGELLSLRYDLTVPFARYLAMNKL--- 144
Cdd:cd00773 1 EAALRRYIEDTLREVFERYGYEEIDTPVFEYTELFLRKSGDEvSKEMYRFKDKGGRDLALRPDLTAPVARAVAENLLslp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 145 TNIKRYHIAKVYRRDNPAmtRGRYREFYQCDFDIAGnFDPMIPDAECLKIMCEILSSLQIGDFLVKVNDRRILDGmfaIC 224
Cdd:cd00773 81 LPLKLYYIGPVFRYERPQ--KGRYREFYQVGVEIIG-SDSPLADAEVIALAVEILEALGLKDFQIKINHRGILDG---IA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 225 GVSDSKFRTICSSVDKLDKvsweevknemvgekglapevadrigdyvqqhggvslveqllqdpklsqnkqalEGLGDLKL 304
Cdd:cd00773 155 GLLEDREEYIERLIDKLDK-----------------------------------------------------EALAHLEK 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 305 LFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLLQTPAQageeplgvGSVAAGGRYDGLVGMFDpkGRKVPCVGLSI 384
Cdd:cd00773 182 LLDYLEALGVDIKYSIDLSLVRGLDYYTGIVFEAVADGLGAQ--------GSIAGGGRYDGLLEEFG--GEDVPAVGFAI 251
|
330
....*....|
gi 135123 385 GVERIFSIVE 394
Cdd:cd00773 252 GLERLLLALE 261
|
|
| hisS |
TIGR00442 |
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ... |
57-489 |
3.56e-103 |
|
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: 314.80 E-value: 3.56e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 57 KTPKGTRDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGEDS----KLIYDLKDQGGELLSLRYDLT 132
Cdd:TIGR00442 1 QKPRGTRDFLPEEMIKWQYIEETIREVFERYGFKEIRTPIFEYTELFKRKVGEETdivsKEMYTFKDKGGRSLTLRPEGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 133 VPFARYLAMNKLTN---IKRYHIAKVYRRDNPAmtRGRYREFYQCDFDIAGNFDPMIpDAECLKIMCEILSSLQIGDFLV 209
Cdd:TIGR00442 81 APVARAVIENKLLLpkpFKLYYIGPMFRYERPQ--KGRYRQFHQFGVEVIGSDSPLA-DAEIIALAADILKELGLKDFTL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 210 KVNDRRILDGMFAicgvsdsKFRTICSSVDK-LDKVSWEEVKNEMVGEKGLAPEVADRIGDYVQQhggvslveqllqDPK 288
Cdd:TIGR00442 158 EINSLGILEGRLE-------YREALIRYLDKhKDKLGEDSVRRLEKNPLRILDSKNEKIQELLKN------------APK 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 289 LSQNKQAlEGLGDLKLLFEYLTLFGIddKISFDLSLARGLDYYTGVIYEAVLLQTPAQageeplgvGSVAAGGRYDGLVG 368
Cdd:TIGR00442 219 ILDFLCE-ESRAHFEELKELLDALGI--PYKIDPSLVRGLDYYTGTVFEFVTDDLGAQ--------GSICGGGRYDGLVE 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 369 MFDpkGRKVPCVGLSIGVERIFSIVEQRLEALEEKirtTETQVLVASAQKKLLEERLKLVSELWDAGIKAElLYKKNPKL 448
Cdd:TIGR00442 288 ELG--GPPTPAVGFAIGIERLILLLEELGLIPPPS---KKPDVYVVPLGEEAELEALKLAQKLRKAGIRVE-VDLGGRKL 361
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 135123 449 LNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVDV 489
Cdd:TIGR00442 362 KKQLKYADKLGARFALIIGEDELENGTVTLKDLETGEQETV 402
|
|
| tRNA-synt_His |
pfam13393 |
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ... |
61-389 |
8.65e-44 |
|
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: 156.98 E-value: 8.65e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 61 GTRDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGEDSKLIYDLKDQGGELLSLRYDLTVPFARYLA 140
Cdd:pfam13393 1 GIRDLLPPEARRIEELRRRLLDLFRSWGYELVMPPLLEYLDSLLTGTGADLDQTFKLVDQSGRLLGLRADITPQVARIDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 141 mnKLTNIKR----YHIAKVYRRDNPAMtrGRYREFYQCDFDIAGNFDPMiPDAECLKIMCEILSSLQIGDFLVKVNDRRI 216
Cdd:pfam13393 81 --HRLNRPGplrlCYAGSVLRTRPKGL--GRSREPLQVGAELIGHAGIE-ADAEIISLLLEALAAAGVPGVTLDLGHVGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 217 LDGMFAICGVSDSKFRTICSSVDKLDkvsWEEVKnEMVGEKGLAPEVADRIGDYVQQHGGVSLVEQLLQDpkLSQNKQAL 296
Cdd:pfam13393 156 VRALLEAAGLSEALEEALRAALQRKD---AAELA-ELAAEAGLPPALRRALLALPDLYGGPEVLDEARAA--LPGLPALQ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 297 EGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLlqtpAQAGEEplgvgsVAAGGRYDGLVGMFdpkGRK 376
Cdd:pfam13393 230 EALDELEALAALLEALGDGVRLTFDLAELRGYEYYTGIVFAAYA----PGVGEP------LARGGRYDDLGAAF---GRA 296
|
330
....*....|...
gi 135123 377 VPCVGLSIGVERI 389
Cdd:pfam13393 297 RPATGFSLDLEAL 309
|
|
| HisRS_RNA |
cd00938 |
HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS ... |
5-49 |
2.81e-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: 75.20 E-value: 2.81e-17
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 135123 5 AALEELVKLQGERVRGLKQQKASAELIEEEVAKLLKLKAQLGPDE 49
Cdd:cd00938 1 AKLEEAVKLQGELVRKLKAEKASKEQIAEEVAKLLELKAQLGGDE 45
|
|
| WHEP-TRS |
pfam00458 |
WHEP-TRS domain; |
7-45 |
2.46e-09 |
|
WHEP-TRS domain;
Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 52.88 E-value: 2.46e-09
10 20 30
....*....|....*....|....*....|....*....
gi 135123 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 |
8.86e-09 |
|
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: 51.57 E-value: 8.86e-09
10 20 30
....*....|....*....|....*....|....*...
gi 135123 8 EELVKLQGERVRGLKQQKASAELIEEEVAKLLKLKAQL 45
Cdd:smart00991 1 EEAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQL 38
|
|
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
5-88 |
1.04e-03 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 41.65 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 5 AALEELVKLQGERVRGLKQQKASAELIEEEVAKLLKLKAQLgpdESKQKFVLKTPKGTRDYSPRQMAVREKVFDVIIR-- 82
Cdd:PLN02734 10 AEKQAAVTAQGNAVRALKASKADKAEIDAAIEKLKALKLEK---SALEKELQAAVGAGGDGAASKEAFRQAVVNTLERrl 86
|
90
....*....|
gi 135123 83 ----CFKRHG 88
Cdd:PLN02734 87 fyipSFKIYG 96
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02972 |
PLN02972 |
Histidyl-tRNA synthetase |
57-501 |
0e+00 |
|
Histidyl-tRNA synthetase
Pssm-ID: 215525 [Multi-domain] Cd Length: 763 Bit Score: 582.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 57 KTPKGTRDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGEDSKLIYDLKDQGGELLSLRYDLTVPFA 136
Cdd:PLN02972 328 KIPKGTRDFAKEQMAIREKAFSIITSVFKRHGATALDTPVFELRETLMGKYGEDSKLIYDLADQGGELCSLRYDLTVPFA 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 137 RYLAMNKLTNIKRYHIAKVYRRDNPamTRGRYREFYQCDFDIAGNFDPMIPDAECLKIMCEILSSLQIGDFLVKVNDRRI 216
Cdd:PLN02972 408 RYVAMNGITSFKRYQIAKVYRRDNP--SKGRYREFYQCDFDIAGVYEPMGPDFEIIKVLTELLDELDIGTYEVKLNHRKL 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 217 LDGMFAICGVSDSKFRTICSSVDKLDKVSWEEVKNEMVGEKGLAPEVADRIGDYVQQHGG-VSLVEQLLQ-DPKLSQNKQ 294
Cdd:PLN02972 486 LDGMLEICGVPPEKFRTICSSIDKLDKQSFEQVKKEMVEEKGLSNETADKIGNFVKERGPpLELLSKLRQeGSEFLGNAS 565
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 295 ALEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLLQTPaqageeplgVGSVAAGGRYDGLVGMFDpkG 374
Cdd:PLN02972 566 SRAALDELEIMFKALEKSKAIGKIVFDLSLARGLDYYTGVIYEAVFKGAQ---------VGSIAAGGRYDNLVGMFS--G 634
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 375 RKVPCVGLSIGVERIFSIVEQRLEALEEKIRTTETQVLVASAQKKLLEERLKLVSELWDAGIKAEllYKKNPKLLNQLQY 454
Cdd:PLN02972 635 KQVPAVGVSLGIERVFAIMEQQEEEKSQVIRPTETEVLVSIIGDDKLALAAELVSELWNAGIKAE--YKVSTRKAKHLKR 712
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 135123 455 CEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVDVRREDLVEEIKRR 501
Cdd:PLN02972 713 AKESGIPWMVLVGEKELSKGFVKLKNLEAGVEEEVDRTCFVQELKAE 759
|
|
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
56-501 |
6.96e-118 |
|
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: 353.27 E-value: 6.96e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 56 LKTPKGTRDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGED--SKLIYDLKDQGGELLSLRYDLTV 133
Cdd:COG0124 4 IQAPRGTRDILPEESAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKIGEDivEKEMYTFEDRGGRSLTLRPEGTA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 134 PFARYLAMNKLTN---IKRYHIAKVYRRDNPAmtRGRYREFYQCDFDIAGNFDPMIpDAECLKIMCEILSSLQIGDFLVK 210
Cdd:COG0124 84 PVARAVAEHGNELpfpFKLYYIGPVFRYERPQ--KGRYRQFHQFGVEVIGSDSPLA-DAEVIALAADLLKALGLKDFTLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 211 VNDRrildgmfaicGVSDSKFRTICSSVDKLDKVSWEEVknemvgekgLAPEVADRI------------GDYVQqhggvS 278
Cdd:COG0124 161 INSR----------GLPEERAEALLRYLDKLDKIGHEDV---------LDEDSQRRLetnplraildskGPDCQ-----E 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 279 LVEQLlqdPKLSQNKqALEGLGDLKLLFEYLTLFGIDdkISFDLSLARGLDYYTGVIYEAVLLQTPAQageeplgvGSVA 358
Cdd:COG0124 217 VLADA---PKLLDYL-GEEGLAHFEEVLELLDALGIP--YVIDPRLVRGLDYYTGTVFEIVTDGLGAQ--------GSVC 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 359 AGGRYDGLVGMFDpkGRKVPCVGLSIGVERIFSIVEQRLEALEEKirtTETQVLVASAQKKLLEERLKLVSELWDAGIKA 438
Cdd:COG0124 283 GGGRYDGLVEQLG--GPPTPAVGFAIGLERLLLLLEELGLLPAAE---PPPDVYVVPLGEEARAEALKLAQELRAAGIRV 357
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 135123 439 EL-LYKKNPKllNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVDVRREDLVEEIKRR 501
Cdd:COG0124 358 ELdLGGRKLK--KQLKYADKSGAPFVLILGEDELANGTVTLKDLATGEQETVPLDELVEYLKEL 419
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
69-394 |
5.41e-104 |
|
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: 311.84 E-value: 5.41e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 69 QMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGED-SKLIYDLKDQGGELLSLRYDLTVPFARYLAMNKL--- 144
Cdd:cd00773 1 EAALRRYIEDTLREVFERYGYEEIDTPVFEYTELFLRKSGDEvSKEMYRFKDKGGRDLALRPDLTAPVARAVAENLLslp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 145 TNIKRYHIAKVYRRDNPAmtRGRYREFYQCDFDIAGnFDPMIPDAECLKIMCEILSSLQIGDFLVKVNDRRILDGmfaIC 224
Cdd:cd00773 81 LPLKLYYIGPVFRYERPQ--KGRYREFYQVGVEIIG-SDSPLADAEVIALAVEILEALGLKDFQIKINHRGILDG---IA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 225 GVSDSKFRTICSSVDKLDKvsweevknemvgekglapevadrigdyvqqhggvslveqllqdpklsqnkqalEGLGDLKL 304
Cdd:cd00773 155 GLLEDREEYIERLIDKLDK-----------------------------------------------------EALAHLEK 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 305 LFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLLQTPAQageeplgvGSVAAGGRYDGLVGMFDpkGRKVPCVGLSI 384
Cdd:cd00773 182 LLDYLEALGVDIKYSIDLSLVRGLDYYTGIVFEAVADGLGAQ--------GSIAGGGRYDGLLEEFG--GEDVPAVGFAI 251
|
330
....*....|
gi 135123 385 GVERIFSIVE 394
Cdd:cd00773 252 GLERLLLALE 261
|
|
| hisS |
TIGR00442 |
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ... |
57-489 |
3.56e-103 |
|
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: 314.80 E-value: 3.56e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 57 KTPKGTRDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGEDS----KLIYDLKDQGGELLSLRYDLT 132
Cdd:TIGR00442 1 QKPRGTRDFLPEEMIKWQYIEETIREVFERYGFKEIRTPIFEYTELFKRKVGEETdivsKEMYTFKDKGGRSLTLRPEGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 133 VPFARYLAMNKLTN---IKRYHIAKVYRRDNPAmtRGRYREFYQCDFDIAGNFDPMIpDAECLKIMCEILSSLQIGDFLV 209
Cdd:TIGR00442 81 APVARAVIENKLLLpkpFKLYYIGPMFRYERPQ--KGRYRQFHQFGVEVIGSDSPLA-DAEIIALAADILKELGLKDFTL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 210 KVNDRRILDGMFAicgvsdsKFRTICSSVDK-LDKVSWEEVKNEMVGEKGLAPEVADRIGDYVQQhggvslveqllqDPK 288
Cdd:TIGR00442 158 EINSLGILEGRLE-------YREALIRYLDKhKDKLGEDSVRRLEKNPLRILDSKNEKIQELLKN------------APK 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 289 LSQNKQAlEGLGDLKLLFEYLTLFGIddKISFDLSLARGLDYYTGVIYEAVLLQTPAQageeplgvGSVAAGGRYDGLVG 368
Cdd:TIGR00442 219 ILDFLCE-ESRAHFEELKELLDALGI--PYKIDPSLVRGLDYYTGTVFEFVTDDLGAQ--------GSICGGGRYDGLVE 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 369 MFDpkGRKVPCVGLSIGVERIFSIVEQRLEALEEKirtTETQVLVASAQKKLLEERLKLVSELWDAGIKAElLYKKNPKL 448
Cdd:TIGR00442 288 ELG--GPPTPAVGFAIGIERLILLLEELGLIPPPS---KKPDVYVVPLGEEAELEALKLAQKLRKAGIRVE-VDLGGRKL 361
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 135123 449 LNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVDV 489
Cdd:TIGR00442 362 KKQLKYADKLGARFALIIGEDELENGTVTLKDLETGEQETV 402
|
|
| PRK12420 |
PRK12420 |
histidyl-tRNA synthetase; Provisional |
53-489 |
3.36e-82 |
|
histidyl-tRNA synthetase; Provisional
Pssm-ID: 237097 [Multi-domain] Cd Length: 423 Bit Score: 261.59 E-value: 3.36e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 53 KFVLKTPKGTRDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYG---EDSKLIYDLKDQGGELLSLRY 129
Cdd:PRK12420 1 MMEMRNVKGTKDYLPEEQVLRNKIKRALEDVFERYGCKPLETPTLNMYELMSSKYGggdEILKEIYTLTDQGKRDLALRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 130 DLTVPFARYLAMNKltNI----KRYHIAKVYrRDNPaMTRGRYREFYQCDFDIAGNFDPMiPDAECLKIMCEILSSLQIg 205
Cdd:PRK12420 81 DLTIPFAKVVAMNP--NIrlpfKRYEIGKVF-RDGP-IKQGRFREFIQCDVDIVGVESVM-AEAELMSMAFELFRRLNL- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 206 DFLVKVNDRRILDGMFAICGVSDSKFRTICSSVDKLDKVSWEEVKNEMVgEKGLAPEVADRIGDYVQQHGGVSLVEQllq 285
Cdd:PRK12420 155 EVTIQYNNRKLLNGILQAIGIPTELTSDVILSLDKIEKIGIDGVRKDLL-ERGISEEMADTICNTVLSCLQLSIADF--- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 286 dPKLSQNKQALEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEaVLLQTPAQAgeeplgvGSVAAGGRYDG 365
Cdd:PRK12420 231 -KEAFNNPLVAEGVNELQQLQQYLIALGINENCIFNPFLARGLTMYTGTVYE-IFLKDGSIT-------SSIGSGGRYDN 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 366 LVGMFDPKGRKVPCVGLSIGVERIfsiveqrLEALEEKIRTTET-QVLVASAQKKLleERLKLVSELW-DAGIKAELLYk 443
Cdd:PRK12420 302 IIGAFRGDDMNYPTVGISFGLDVI-------YTALSQKETISSTaDVFIIPLGTEL--QCLQIAQQLRsTTGLKVELEL- 371
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 135123 444 KNPKLLNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVDV 489
Cdd:PRK12420 372 AGRKLKKALNYANKENIPYVLIIGEEEVSTGTVMLRNMKEGSEVKV 417
|
|
| PLN02530 |
PLN02530 |
histidine-tRNA ligase |
47-494 |
2.84e-51 |
|
histidine-tRNA ligase
Pssm-ID: 178145 [Multi-domain] Cd Length: 487 Bit Score: 181.86 E-value: 2.84e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 47 PDESKQKFVLKTPKGTRDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGED-SKLIYDLKDQGGELL 125
Cdd:PLN02530 61 QEDGKPKIDVNPPKGTRDFPPEDMRLRNWLFDHFREVSRLFGFEEVDAPVLESEELYIRKAGEEiTDQLYNFEDKGGRRV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 126 SLRYDLTVPFARyLAMNKLTNI----KRYHIAKVYRRDNpaMTRGRYREFYQCDFDIAGnFDPMIPDAECLKIMCEILSS 201
Cdd:PLN02530 141 ALRPELTPSLAR-LVLQKGKSLslplKWFAIGQCWRYER--MTRGRRREHYQWNMDIIG-VPGVEAEAELLAAIVTFFKR 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 202 LQI--GDFLVKVNDRRILDGMFAICGVSDSKFRTICSSVDKLDKVSWEEVKNEMvGEKGLAPEVADRIGDyVQQHGGVSL 279
Cdd:PLN02530 217 VGItsSDVGIKVSSRKVLQAVLKSYGIPEESFAPVCVIVDKLEKLPREEIEKEL-DTLGVSEEAIEGILD-VLSLKSLDD 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 280 VEQLLqdpklsqnKQALEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVllqtpAQAGEeplgVGSVAA 359
Cdd:PLN02530 295 LEALL--------GADSEAVADLKQLFSLAEAYGYQDWLVFDASVVRGLAYYTGIVFEGF-----DRAGK----LRAICG 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 360 GGRYDGLVGMFDpkGRKVPCVGLSIGVERIFSIVEQRlEALEEKIRTTETqvLVASAQKKLLEERLKLVSELWDAGIKAE 439
Cdd:PLN02530 358 GGRYDRLLSTFG--GEDTPACGFGFGDAVIVELLKEK-GLLPELPHQVDD--VVFALDEDLQGAAAGVASRLREKGRSVD 432
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 135123 440 L-LYKKNPKLLnqLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVDVRREDL 494
Cdd:PLN02530 433 LvLEPKKLKWV--FKHAERIGAKRLVLVGASEWERGMVRVKDLSSGEQTEVKLDEL 486
|
|
| HisZ |
COG3705 |
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism]; |
67-389 |
1.09e-49 |
|
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism];
Pssm-ID: 442919 [Multi-domain] Cd Length: 312 Bit Score: 172.67 E-value: 1.09e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 67 PRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGEDSKL-IYDLKDQGGELLSLRYDLTVPFARYLAmNKLT 145
Cdd:COG3705 2 PEEAARKEELRRRLLDVFRSWGYELVEPPLLEYLDSLLTGSGADLDLqTFKLVDQLGRTLGLRPDMTPQVARIAA-TRLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 146 NIKR----YHIAKVYRrdNPAMTRGRYREFYQC------DFDIAGnfdpmipDAECLKIMCEILSSLQIGDFLVKVNDRR 215
Cdd:COG3705 81 NRPGplrlCYAGNVFR--TRPSGLGRSREFLQAgaeligHAGLEA-------DAEVIALALEALKAAGLEDFTLDLGHVG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 216 ILDGMFAICGVSDSKFRTICSSVDKLDKVsweEVKnEMVGEKGLAPEVADRIGDYVQQHGGVSLVEQLLqdpKLSQNKQA 295
Cdd:COG3705 152 LFRALLEALGLSEEQREELRRALARKDAV---ELE-ELLAELGLSEELAEALLALPELYGGEEVLARAR---ALLLDAAI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 296 LEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLlqtpAQAGEEplgvgsVAAGGRYDGLVGMFdpkGR 375
Cdd:COG3705 225 RAALDELEALAEALAARGPDVRLTFDLSELRGYDYYTGIVFEAYA----PGVGDP------LARGGRYDGLLAAF---GR 291
|
330
....*....|....
gi 135123 376 KVPCVGLSIGVERI 389
Cdd:COG3705 292 ARPATGFSLDLDRL 305
|
|
| hisZ_biosyn_reg |
TIGR00443 |
ATP phosphoribosyltransferase, regulatory subunit; Apparant second copies of histidyl-tRNA ... |
63-389 |
1.27e-49 |
|
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: 172.80 E-value: 1.27e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 63 RDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGEDSKLIYDLKDQGGELLSLRYDLTVPFARyLAMN 142
Cdd:TIGR00443 1 RDLLPEEAARKEEIERQLQDVFRSWGYQEIITPTLEYLDTLSAGSGILNEDLFKLFDQLGRVLGLRPDMTAPIAR-LVST 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 143 KLTNIKR----YHIAKVYRRDNPAmtRGRYREFYQCDFDIAGNfDPMIPDAECLKIMCEILSSLQIGDFLVKVNDRRILD 218
Cdd:TIGR00443 80 RLRDRPLplrlCYAGNVFRTNESG--GGRSREFTQAGVELIGA-GGPAADAEVIALLIEALKALGLKDFKIELGHVGLVR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 219 GMFAICGVSDSKFRTICSSVDKLDKVSWEEVknemVGEKGLAPEVADRIGDYVQQHGGVSLVEQLLQdpKLSQNKQALEG 298
Cdd:TIGR00443 157 ALLEEAGLPEEAREALREALARKDLVALEEL----VAELGLSPEVRERLLALPRLRGDGEEVLEEAR--ALAGSETAEAA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 299 LGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLLQTPAQageeplgvgsVAAGGRYDGLVGMFdpkGRKVP 378
Cdd:TIGR00443 231 LDELEAVLELLEARGVEEYISLDLGLVRGYHYYTGLIFEGYAPGLGAP----------LAGGGRYDELLGRF---GRPLP 297
|
330
....*....|.
gi 135123 379 CVGLSIGVERI 389
Cdd:TIGR00443 298 ATGFALNLERL 308
|
|
| hisZ |
PRK12292 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
59-440 |
2.53e-47 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 237043 [Multi-domain] Cd Length: 391 Bit Score: 168.89 E-value: 2.53e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 59 PKGTRDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLM--GKYGEDSKLIYDLKDQGGELLSLRYDLTVPFA 136
Cdd:PRK12292 6 PEGIRDLLPEEARKIEEIRRRLLDLFRRWGYEEVITPTLEYLDTLLagGGAILDLRTFKLVDQLSGRTLGLRPDMTAQIA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 137 RyLAMNKLTNIKR----YHIAKVYRrdNPAMTRGRYREFYQCDFDIAGnFDPMIPDAECLKIMCEILSSLQIGDFLVKVN 212
Cdd:PRK12292 86 R-IAATRLANRPGplrlCYAGNVFR--AQERGLGRSREFLQSGVELIG-DAGLEADAEVILLLLEALKALGLPNFTLDLG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 213 DRRILDGMFAICGVSDSKFRTICSSVDKLDKVSWEEVknemvgEKGLAPEVADRIGDYVQQHGGVSLVEQLLQdpkLSQN 292
Cdd:PRK12292 162 HVGLFRALLEAAGLSEELEEVLRRALANKDYVALEEL------VLDLSEELRDALLALPRLRGGREVLEEARK---LLPS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 293 KQALEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLLQTPAqageeplgvgSVAAGGRYDGLVGMFdp 372
Cdd:PRK12292 233 LPIKRALDELEALAEALEKYGYGIPLSLDLGLLRHLDYYTGIVFEGYVDGVGN----------PIASGGRYDDLLGRF-- 300
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 135123 373 kGRKVPCVGLSIGVERIfsiveqrLEALEEKiRTTETQVLVASAQKKLLEERLKLVSELWDAGIKAEL 440
Cdd:PRK12292 301 -GRARPATGFSLDLDRL-------LELQLEL-PVEARKDLVIAPDSEALAAALAAAQELRKKGEIVVL 359
|
|
| tRNA-synt_His |
pfam13393 |
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ... |
61-389 |
8.65e-44 |
|
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: 156.98 E-value: 8.65e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 61 GTRDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGEDSKLIYDLKDQGGELLSLRYDLTVPFARYLA 140
Cdd:pfam13393 1 GIRDLLPPEARRIEELRRRLLDLFRSWGYELVMPPLLEYLDSLLTGTGADLDQTFKLVDQSGRLLGLRADITPQVARIDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 141 mnKLTNIKR----YHIAKVYRRDNPAMtrGRYREFYQCDFDIAGNFDPMiPDAECLKIMCEILSSLQIGDFLVKVNDRRI 216
Cdd:pfam13393 81 --HRLNRPGplrlCYAGSVLRTRPKGL--GRSREPLQVGAELIGHAGIE-ADAEIISLLLEALAAAGVPGVTLDLGHVGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 217 LDGMFAICGVSDSKFRTICSSVDKLDkvsWEEVKnEMVGEKGLAPEVADRIGDYVQQHGGVSLVEQLLQDpkLSQNKQAL 296
Cdd:pfam13393 156 VRALLEAAGLSEALEEALRAALQRKD---AAELA-ELAAEAGLPPALRRALLALPDLYGGPEVLDEARAA--LPGLPALQ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 297 EGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLlqtpAQAGEEplgvgsVAAGGRYDGLVGMFdpkGRK 376
Cdd:pfam13393 230 EALDELEALAALLEALGDGVRLTFDLAELRGYEYYTGIVFAAYA----PGVGEP------LARGGRYDDLGAAF---GRA 296
|
330
....*....|...
gi 135123 377 VPCVGLSIGVERI 389
Cdd:pfam13393 297 RPATGFSLDLEAL 309
|
|
| HisRS_anticodon |
cd00859 |
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases ... |
408-499 |
1.74e-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: 108.40 E-value: 1.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 408 ETQVLVASAQKKLLEERLKLVSELWDAGIKAELLYKkNPKLLNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEV 487
Cdd:cd00859 1 EVDVYVVPLGEGALSEALELAEQLRDAGIKAEIDYG-GRKLKKQFKYADRSGARFAVILGEDELAAGVVTVKDLETGEQE 79
|
90
....*....|..
gi 135123 488 DVRREDLVEEIK 499
Cdd:cd00859 80 TVALDELVEELK 91
|
|
| syh |
CHL00201 |
histidine-tRNA synthetase; Provisional |
60-498 |
9.70e-28 |
|
histidine-tRNA synthetase; Provisional
Pssm-ID: 164576 [Multi-domain] Cd Length: 430 Bit Score: 115.38 E-value: 9.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 60 KGTRDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGEDSKLI----YDLKDQGGELLSLRYDLTVPF 135
Cdd:CHL00201 8 RGTKDILPDEINYWQFIHDKALTLLSLANYSEIRTPIFENSSLYDRGIGETTDIVnkemYRFTDRSNRDITLRPEGTAGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 136 ARYLAMNKLT---NIKR-YHIAKVYRRDNPamTRGRYREFYQCDFDIAGNFDPMiPDAECLKIMCEILSSLQIGDFLVKV 211
Cdd:CHL00201 88 VRAFIENKMDyhsNLQRlWYSGPMFRYERP--QSGRQRQFHQLGIEFIGSIDAR-ADTEVIHLAMQIFNELQVKNLILDI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 212 N------DRRILDgmfaicgvsdSKFRTICSSV-DKLDKVSweevKNEMVGEkglaP-EVADRIGDYVQqhggvslvEQL 283
Cdd:CHL00201 165 NsigkleDRQSYQ----------LKLVEYLSQYqDDLDTDS----QNRLYSN----PiRILDSKNLKTQ--------EIL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 284 LQDPKLSQ--NKQALEGLGDLkllFEYLTLFGIDDKISFdlSLARGLDYYTGVIYEAVLLQTPAQageeplgvGSVAAGG 361
Cdd:CHL00201 219 DGAPKISDflSLESTEHFYDV---CTYLNLLNIPYKINY--KLVRGLDYYNDTAFEIKTLSSNGQ--------DTICGGG 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 362 RYDGLVGMFDpkGRKVPCVGLSIGVERIFSIVEQRLEALEEKIrttetQVLVASAQKKLLEERLKLVSELWDAGIKAELL 441
Cdd:CHL00201 286 RYDSLIHQLG--GPKTPAVGCAIGLERLLLIAKDNIILPKQSI-----DVYIATQGLKAQKKGWEIIQFLEKQNIKFELD 358
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 135123 442 YkKNPKLLNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVDVRREDLVEEI 498
Cdd:CHL00201 359 L-SSSNFHKQIKQAGKKRAKACIILGDNEIMDNCITIKWLDEQVQENAQYSNFKQEI 414
|
|
| hisZ |
PRK12295 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
70-389 |
3.96e-22 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 183413 [Multi-domain] Cd Length: 373 Bit Score: 98.08 E-value: 3.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 70 MAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGED-SKLIYDLKDQGGELLSLRYDLTVPFAR-YLAMNKLTNI 147
Cdd:PRK12295 4 LSASAAAAEALLASFEAAGAVRVDPPILQPAEPFLDLSGEDiRRRIFVTSDENGEELCLRPDFTIPVCRrHIATAGGEPA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 148 KRYHIAKVYRRdnpamTRGRYREFYQCDFDIAGNFDPMIPDAECLKIMCEILSSLQIGDFLVKVNDRRILDGMFAICGVS 227
Cdd:PRK12295 84 RYAYLGEVFRQ-----RRDRASEFLQAGIESFGRADPAAADAEVLALALEALAALGPGDLEVRLGDVGLFAALVDALGLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 228 DS-KFRTIcssVDKLDKVSWEEVKNEMVGEKGLAPEVADRIGDYVQQHGGVS-LVEQLLQDPKLSQN------------- 292
Cdd:PRK12295 159 PGwKRRLL---RHFGRPRSLDALLARLAGPRVDPLDEHAGVLAALADEAAARaLVEDLMSIAGISPVggrspaeiarrll 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 293 -----------------------------KQALEGL----GDLKL-------LFE----YLTLFGID-DKISFDLSLARG 327
Cdd:PRK12295 236 ekaalaaaarlpaealavlerflaisgppDAALAALralaADAGLdldaaldRFEarlaALAARGIDlERLRFSASFGRP 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 135123 328 LDYYTGVIYEAvllqTPAQAGEEPLgvgsvAAGGRYDGLVGMFDpKGRKVPCVGLSIGVERI 389
Cdd:PRK12295 316 LDYYTGFVFEI----RAAGNGDPPL-----AGGGRYDGLLTRLG-AGEPIPAVGFSIWLDRL 367
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
410-501 |
2.52e-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: 2.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 410 QVLVASAQKK---LLEERLKLVSELWDAGIKAELLYKkNPKLLNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREE 486
Cdd:pfam03129 1 QVVVIPLGEKaeeLEEYAQKLAEELRAAGIRVELDDR-NESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQ 79
|
90
....*....|....*
gi 135123 487 VDVRREDLVEEIKRR 501
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 |
2.81e-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: 75.20 E-value: 2.81e-17
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 135123 5 AALEELVKLQGERVRGLKQQKASAELIEEEVAKLLKLKAQLGPDE 49
Cdd:cd00938 1 AKLEEAVKLQGELVRKLKAEKASKEQIAEEVAKLLELKAQLGGDE 45
|
|
| PRK12421 |
PRK12421 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
59-435 |
3.67e-11 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 237098 Cd Length: 392 Bit Score: 64.99 E-value: 3.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 59 PKGTRDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGEDSKL-IYDLKDQ-GGELLSLRYDLTVPFA 136
Cdd:PRK12421 10 PDGVADVLPEEAQKIERLRRRLLDLFASRGYQLVMPPLIEYLESLLTGAGQDLKLqTFKLIDQlSGRLMGVRADITPQVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 137 RYLA-MNKLTNIKRY-HIAKVY--RRDNPAMTRGRYR---EFYQCDfDIAGnfdpmipDAECLKIMCEILSSLQIGDFLV 209
Cdd:PRK12421 90 RIDAhLLNREGVARLcYAGSVLhtLPQGLFGSRTPLQlgaELYGHA-GIEA-------DLEIIRLMLGLLRNAGVPALHL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 210 KVNDRRILDGMFAICGVSDSKFRTIcssVDKLDKVSWEEVKnEMVGEKGLAPEVADRIGDYVQQHGGVSLVEQLLQDpKL 289
Cdd:PRK12421 162 DLGHVGIFRRLAELAGLSPEEEEEL---FDLLQRKALPELA-EVCQNLGVGSDLRRMFYALARLNGGLEALDRALSV-LA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 290 SQNKQALEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYeAVLLQTPAQAgeeplgvgsVAAGGRYDGLVGM 369
Cdd:PRK12421 237 LQDAAIRQALDELKTLAAHLKNRWPELPVSIDLAELRGYHYHTGLVF-AAYIPGRGQA---------LARGGRYDGIGEA 306
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 135123 370 FdpkGRKVPCVGlsigveriFSIVEQRLEALEEKIRTTETQVLVASAQKKLLEErlklVSELWDAG 435
Cdd:PRK12421 307 F---GRARPATG--------FSMDLKELLALQFLEEEAGAILAPWGDDPDLLAA----IAELRQQG 357
|
|
| WHEPGMRS_RNA |
cd01200 |
EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher ... |
8-49 |
6.87e-10 |
|
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: 54.47 E-value: 6.87e-10
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 135123 8 EELVKLQGERVRGLKQQKASAELIEEEVAKLLKLKAQLGPDE 49
Cdd:cd01200 1 YEKIAEQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKEAT 42
|
|
| WHEP-TRS |
pfam00458 |
WHEP-TRS domain; |
7-45 |
2.46e-09 |
|
WHEP-TRS domain;
Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 52.88 E-value: 2.46e-09
10 20 30
....*....|....*....|....*....|....*....
gi 135123 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 |
8.86e-09 |
|
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: 51.57 E-value: 8.86e-09
10 20 30
....*....|....*....|....*....|....*...
gi 135123 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 ... |
411-501 |
3.60e-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: 3.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 411 VLVASAQKKLL-EERLKLVSELWDAGIKAELLYKKNPKLLNQLQYCEEAGIPLVAIIGEQELKDG----VIKLRSVTSRE 485
Cdd:pfam12745 8 VLVASFDASILrTTGVEILQELWAHGISADLAVDASYSPEDLVSRARDDGVSWIVIIKQQNKSSDskykPLKVKNLLRKE 87
|
90 100
....*....|....*....|
gi 135123 486 EVDVRREDLV----EEIKRR 501
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 |
1.92e-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: 44.77 E-value: 1.92e-06
10 20 30
....*....|....*....|....*....|....*....
gi 135123 7 LEELVKLQGERVRGLKQQKASAELIEEEVAKLLKLKAQL 45
Cdd:cd00939 1 LEKEVAEQGNKVRKLKASKADKSVWQPEVNKLLDLKKQL 39
|
|
| PRK03991 |
PRK03991 |
threonyl-tRNA synthetase; Validated |
385-505 |
1.35e-05 |
|
threonyl-tRNA synthetase; Validated
Pssm-ID: 235190 [Multi-domain] Cd Length: 613 Bit Score: 47.56 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 385 GVER-IFSIVE-QRLEALEEKIRT-----TETQVLVASAQKKLLEERLKLVSELWDAGIKAEL------LYKKnpkllnq 451
Cdd:PRK03991 469 SIERvIYALLEkAAKEEEEGKVPMlptwlSPTQVRVIPVSERHLDYAEEVADKLEAAGIRVDVddrdesLGKK------- 541
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 135123 452 lqyCEEAG---IPLVAIIGEQELKDGVIklrSVTSREE---VDVRREDLVEEIKRRT-GQP 505
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 |
6.09e-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: 40.68 E-value: 6.09e-05
10 20 30
....*....|....*....|....*....|.
gi 135123 14 QGERVRGLKQQKASAELIEEEVAKLLKLKAQ 44
Cdd:cd00936 8 QGDLVRELKAKKAPKEEIDAAVKKLLALKAD 38
|
|
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
5-88 |
1.04e-03 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 41.65 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 5 AALEELVKLQGERVRGLKQQKASAELIEEEVAKLLKLKAQLgpdESKQKFVLKTPKGTRDYSPRQMAVREKVFDVIIR-- 82
Cdd:PLN02734 10 AEKQAAVTAQGNAVRALKASKADKAEIDAAIEKLKALKLEK---SALEKELQAAVGAGGDGAASKEAFRQAVVNTLERrl 86
|
90
....*....|
gi 135123 83 ----CFKRHG 88
Cdd:PLN02734 87 fyipSFKIYG 96
|
|
| ThrRS_anticodon |
cd00860 |
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases ... |
409-499 |
8.32e-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: 8.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135123 409 TQVLVASAQKKLLEERLKLVSELWDAGIKAELLYKkNPKLLNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVD 488
Cdd:cd00860 2 VQVVVIPVTDEHLDYAKEVAKKLSDAGIRVEVDLR-NEKLGKKIREAQLQKIPYILVVGDKEVETGTVSVRTRDGGDLGS 80
|
90
....*....|.
gi 135123 489 VRREDLVEEIK 499
Cdd:cd00860 81 MSLDEFIEKLK 91
|
|
| |
