|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02972 |
PLN02972 |
Histidyl-tRNA synthetase |
56-441 |
3.61e-155 |
|
Histidyl-tRNA synthetase
Pssm-ID: 215525 [Multi-domain] Cd Length: 763 Bit Score: 458.20 E-value: 3.61e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 56 LKTP----KETLMGKYGEDSKLIYDLKDQGGELLSLRYDLTVPFARYLAMNKLTNIKRYHIAK----------------- 114
Cdd:PLN02972 363 LDTPvfelRETLMGKYGEDSKLIYDLADQGGELCSLRYDLTVPFARYVAMNGITSFKRYQIAKvyrrdnpskgryrefyq 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 115 -DFDIAGNFDPMIPDAECLKIMCEILSSLQIGDFLVKVNDRRILDGMFAICGVSDSKFRTICSSVDKLDKVSWEEVKNEM 193
Cdd:PLN02972 443 cDFDIAGVYEPMGPDFEIIKVLTELLDELDIGTYEVKLNHRKLLDGMLEICGVPPEKFRTICSSIDKLDKQSFEQVKKEM 522
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 194 VGEKGLAPEVADRIGDYVQQHGG-VSLVEQLLQ-DPKLSQNKQALEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYY 271
Cdd:PLN02972 523 VEEKGLSNETADKIGNFVKERGPpLELLSKLRQeGSEFLGNASSRAALDELEIMFKALEKSKAIGKIVFDLSLARGLDYY 602
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 272 TGVIYEAVLLQTPaqageeplgVGSVAAGGRYDGLVGMFDpkGRKVPCVGLSIGVERIFSIVEQRLEALEEKIRTTETQV 351
Cdd:PLN02972 603 TGVIYEAVFKGAQ---------VGSIAAGGRYDNLVGMFS--GKQVPAVGVSLGIERVFAIMEQQEEEKSQVIRPTETEV 671
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 352 LVASAQKKLLEERLKLVSELWDAGIKAEllYKKNPKLLNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVDVRR 431
Cdd:PLN02972 672 LVSIIGDDKLALAAELVSELWNAGIKAE--YKVSTRKAKHLKRAKESGIPWMVLVGEKELSKGFVKLKNLEAGVEEEVDR 749
|
410
....*....|
gi 384475556 432 EDLVEEIKRR 441
Cdd:PLN02972 750 TCFVQELKAE 759
|
|
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
61-441 |
5.41e-83 |
|
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: 261.59 E-value: 5.41e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 61 ETLMGKYGED--SKLIYDLKDQGGELLSLRYDLTVPFARYLAMNKLTN---IKRYHIAK------------------DFD 117
Cdd:COG0124 49 ELFARKIGEDivEKEMYTFEDRGGRSLTLRPEGTAPVARAVAEHGNELpfpFKLYYIGPvfryerpqkgryrqfhqfGVE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 118 IAGNFDPMIpDAECLKIMCEILSSLQIGDFLVKVNDRrildgmfaicGVSDSKFRTICSSVDKLDKVSWEEVknemvgek 197
Cdd:COG0124 129 VIGSDSPLA-DAEVIALAADLLKALGLKDFTLEINSR----------GLPEERAEALLRYLDKLDKIGHEDV-------- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 198 gLAPEVADRI------------GDYVQqhggvSLVEQLlqdPKLSQNKqALEGLGDLKLLFEYLTLFGIDdkISFDLSLA 265
Cdd:COG0124 190 -LDEDSQRRLetnplraildskGPDCQ-----EVLADA---PKLLDYL-GEEGLAHFEEVLELLDALGIP--YVIDPRLV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 266 RGLDYYTGVIYEAVLLQTPAQageeplgvGSVAAGGRYDGLVGMFDpkGRKVPCVGLSIGVERIFSIVEQRLEALEEKir 345
Cdd:COG0124 258 RGLDYYTGTVFEIVTDGLGAQ--------GSVCGGGRYDGLVEQLG--GPPTPAVGFAIGLERLLLLLEELGLLPAAE-- 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 346 tTETQVLVASAQKKLLEERLKLVSELWDAGIKAEL-LYKKNPKllNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSR 424
Cdd:COG0124 326 -PPPDVYVVPLGEEARAEALKLAQELRAAGIRVELdLGGRKLK--KQLKYADKSGAPFVLILGEDELANGTVTLKDLATG 402
|
410
....*....|....*..
gi 384475556 425 EEVDVRREDLVEEIKRR 441
Cdd:COG0124 403 EQETVPLDELVEYLKEL 419
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
56-334 |
2.17e-72 |
|
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: 228.64 E-value: 2.17e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 56 LKTP----KETLMGKYGED-SKLIYDLKDQGGELLSLRYDLTVPFARYLAMNKL---TNIKRYHIAK------------- 114
Cdd:cd00773 24 IDTPvfeyTELFLRKSGDEvSKEMYRFKDKGGRDLALRPDLTAPVARAVAENLLslpLPLKLYYIGPvfryerpqkgryr 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 115 -----DFDIAGnFDPMIPDAECLKIMCEILSSLQIGDFLVKVNDRRILDGmfaICGVSDSKFRTICSSVDKLDKvsweev 189
Cdd:cd00773 104 efyqvGVEIIG-SDSPLADAEVIALAVEILEALGLKDFQIKINHRGILDG---IAGLLEDREEYIERLIDKLDK------ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 190 knemvgekglapevadrigdyvqqhggvslveqllqdpklsqnkqalEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLD 269
Cdd:cd00773 174 -----------------------------------------------EALAHLEKLLDYLEALGVDIKYSIDLSLVRGLD 206
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 384475556 270 YYTGVIYEAVLLQTPAQageeplgvGSVAAGGRYDGLVGMFDpkGRKVPCVGLSIGVERIFSIVE 334
Cdd:cd00773 207 YYTGIVFEAVADGLGAQ--------GSIAGGGRYDGLLEEFG--GEDVPAVGFAIGLERLLLALE 261
|
|
| hisS |
TIGR00442 |
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ... |
56-429 |
6.13e-70 |
|
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: 226.98 E-value: 6.13e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 56 LKTP----KETLMGKYGEDS----KLIYDLKDQGGELLSLRYDLTVPFARYLAMNKLTN---IKRYHIAK---------- 114
Cdd:TIGR00442 36 IRTPifeyTELFKRKVGEETdivsKEMYTFKDKGGRSLTLRPEGTAPVARAVIENKLLLpkpFKLYYIGPmfryerpqkg 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 115 --------DFDIAGNFDPMIpDAECLKIMCEILSSLQIGDFLVKVNDRRILDGMFAicgvsdsKFRTICSSVDK-LDKVS 185
Cdd:TIGR00442 116 ryrqfhqfGVEVIGSDSPLA-DAEIIALAADILKELGLKDFTLEINSLGILEGRLE-------YREALIRYLDKhKDKLG 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 186 WEEVKNEMVGEKGLAPEVADRIGDYVQQhggvslveqllqDPKLSQNKQAlEGLGDLKLLFEYLTLFGIddKISFDLSLA 265
Cdd:TIGR00442 188 EDSVRRLEKNPLRILDSKNEKIQELLKN------------APKILDFLCE-ESRAHFEELKELLDALGI--PYKIDPSLV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 266 RGLDYYTGVIYEAVLLQTPAQageeplgvGSVAAGGRYDGLVGMFDpkGRKVPCVGLSIGVERIFSIVEQRLEALEEKir 345
Cdd:TIGR00442 253 RGLDYYTGTVFEFVTDDLGAQ--------GSICGGGRYDGLVEELG--GPPTPAVGFAIGIERLILLLEELGLIPPPS-- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 346 tTETQVLVASAQKKLLEERLKLVSELWDAGIKAElLYKKNPKLLNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSRE 425
Cdd:TIGR00442 321 -KKPDVYVVPLGEEAELEALKLAQKLRKAGIRVE-VDLGGRKLKKQLKYADKLGARFALIIGEDELENGTVTLKDLETGE 398
|
....
gi 384475556 426 EVDV 429
Cdd:TIGR00442 399 QETV 402
|
|
| tRNA-synt_His |
pfam13393 |
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ... |
61-329 |
7.07e-29 |
|
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: 115.38 E-value: 7.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 61 ETLMGKYGEDSKLIYDLKDQGGELLSLRYDLTVPFARYLAmnKLTNIKR----------YHIAKDfdiaGNFDPMIP--- 127
Cdd:pfam13393 41 DSLLTGTGADLDQTFKLVDQSGRLLGLRADITPQVARIDA--HRLNRPGplrlcyagsvLRTRPK----GLGRSREPlqv 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 128 ------------DAECLKIMCEILSSLQIGDFLVKVNDRRILDGMFAICGVSDSKFRTICSSVDKLDkvsWEEVKnEMVG 195
Cdd:pfam13393 115 gaelighagieaDAEIISLLLEALAAAGVPGVTLDLGHVGLVRALLEAAGLSEALEEALRAALQRKD---AAELA-ELAA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 196 EKGLAPEVADRIGDYVQQHGGVSLVEQLLQDpkLSQNKQALEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVI 275
Cdd:pfam13393 191 EAGLPPALRRALLALPDLYGGPEVLDEARAA--LPGLPALQEALDELEALAALLEALGDGVRLTFDLAELRGYEYYTGIV 268
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 384475556 276 YEAVLlqtpAQAGEEplgvgsVAAGGRYDGLVGMFdpkGRKVPCVGLSIGVERI 329
Cdd:pfam13393 269 FAAYA----PGVGEP------LARGGRYDDLGAAF---GRARPATGFSLDLEAL 309
|
|
| HisRS_RNA |
cd00938 |
HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS ... |
5-49 |
1.59e-16 |
|
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: 72.89 E-value: 1.59e-16
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 384475556 5 AALEELVKLQGERVRGLKQQKASAELIEEEVAKLLKLKAQLGPDE 49
Cdd:cd00938 1 AKLEEAVKLQGELVRKLKAEKASKEQIAEEVAKLLELKAQLGGDE 45
|
|
| WHEP-TRS |
pfam00458 |
WHEP-TRS domain; |
7-45 |
6.60e-09 |
|
WHEP-TRS domain;
Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 51.73 E-value: 6.60e-09
10 20 30
....*....|....*....|....*....|....*....
gi 384475556 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 |
2.22e-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: 50.42 E-value: 2.22e-08
10 20 30
....*....|....*....|....*....|....*...
gi 384475556 8 EELVKLQGERVRGLKQQKASAELIEEEVAKLLKLKAQL 45
Cdd:smart00991 1 EEAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQL 38
|
|
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
5-66 |
4.16e-03 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 39.73 E-value: 4.16e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 384475556 5 AALEELVKLQGERVRGLKQQKASAELIEEEVAKLLKLKAQLGPDESKQKFVLKTPKETLMGK 66
Cdd:PLN02734 10 AEKQAAVTAQGNAVRALKASKADKAEIDAAIEKLKALKLEKSALEKELQAAVGAGGDGAASK 71
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02972 |
PLN02972 |
Histidyl-tRNA synthetase |
56-441 |
3.61e-155 |
|
Histidyl-tRNA synthetase
Pssm-ID: 215525 [Multi-domain] Cd Length: 763 Bit Score: 458.20 E-value: 3.61e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 56 LKTP----KETLMGKYGEDSKLIYDLKDQGGELLSLRYDLTVPFARYLAMNKLTNIKRYHIAK----------------- 114
Cdd:PLN02972 363 LDTPvfelRETLMGKYGEDSKLIYDLADQGGELCSLRYDLTVPFARYVAMNGITSFKRYQIAKvyrrdnpskgryrefyq 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 115 -DFDIAGNFDPMIPDAECLKIMCEILSSLQIGDFLVKVNDRRILDGMFAICGVSDSKFRTICSSVDKLDKVSWEEVKNEM 193
Cdd:PLN02972 443 cDFDIAGVYEPMGPDFEIIKVLTELLDELDIGTYEVKLNHRKLLDGMLEICGVPPEKFRTICSSIDKLDKQSFEQVKKEM 522
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 194 VGEKGLAPEVADRIGDYVQQHGG-VSLVEQLLQ-DPKLSQNKQALEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYY 271
Cdd:PLN02972 523 VEEKGLSNETADKIGNFVKERGPpLELLSKLRQeGSEFLGNASSRAALDELEIMFKALEKSKAIGKIVFDLSLARGLDYY 602
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 272 TGVIYEAVLLQTPaqageeplgVGSVAAGGRYDGLVGMFDpkGRKVPCVGLSIGVERIFSIVEQRLEALEEKIRTTETQV 351
Cdd:PLN02972 603 TGVIYEAVFKGAQ---------VGSIAAGGRYDNLVGMFS--GKQVPAVGVSLGIERVFAIMEQQEEEKSQVIRPTETEV 671
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 352 LVASAQKKLLEERLKLVSELWDAGIKAEllYKKNPKLLNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVDVRR 431
Cdd:PLN02972 672 LVSIIGDDKLALAAELVSELWNAGIKAE--YKVSTRKAKHLKRAKESGIPWMVLVGEKELSKGFVKLKNLEAGVEEEVDR 749
|
410
....*....|
gi 384475556 432 EDLVEEIKRR 441
Cdd:PLN02972 750 TCFVQELKAE 759
|
|
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
61-441 |
5.41e-83 |
|
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: 261.59 E-value: 5.41e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 61 ETLMGKYGED--SKLIYDLKDQGGELLSLRYDLTVPFARYLAMNKLTN---IKRYHIAK------------------DFD 117
Cdd:COG0124 49 ELFARKIGEDivEKEMYTFEDRGGRSLTLRPEGTAPVARAVAEHGNELpfpFKLYYIGPvfryerpqkgryrqfhqfGVE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 118 IAGNFDPMIpDAECLKIMCEILSSLQIGDFLVKVNDRrildgmfaicGVSDSKFRTICSSVDKLDKVSWEEVknemvgek 197
Cdd:COG0124 129 VIGSDSPLA-DAEVIALAADLLKALGLKDFTLEINSR----------GLPEERAEALLRYLDKLDKIGHEDV-------- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 198 gLAPEVADRI------------GDYVQqhggvSLVEQLlqdPKLSQNKqALEGLGDLKLLFEYLTLFGIDdkISFDLSLA 265
Cdd:COG0124 190 -LDEDSQRRLetnplraildskGPDCQ-----EVLADA---PKLLDYL-GEEGLAHFEEVLELLDALGIP--YVIDPRLV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 266 RGLDYYTGVIYEAVLLQTPAQageeplgvGSVAAGGRYDGLVGMFDpkGRKVPCVGLSIGVERIFSIVEQRLEALEEKir 345
Cdd:COG0124 258 RGLDYYTGTVFEIVTDGLGAQ--------GSVCGGGRYDGLVEQLG--GPPTPAVGFAIGLERLLLLLEELGLLPAAE-- 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 346 tTETQVLVASAQKKLLEERLKLVSELWDAGIKAEL-LYKKNPKllNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSR 424
Cdd:COG0124 326 -PPPDVYVVPLGEEARAEALKLAQELRAAGIRVELdLGGRKLK--KQLKYADKSGAPFVLILGEDELANGTVTLKDLATG 402
|
410
....*....|....*..
gi 384475556 425 EEVDVRREDLVEEIKRR 441
Cdd:COG0124 403 EQETVPLDELVEYLKEL 419
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
56-334 |
2.17e-72 |
|
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: 228.64 E-value: 2.17e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 56 LKTP----KETLMGKYGED-SKLIYDLKDQGGELLSLRYDLTVPFARYLAMNKL---TNIKRYHIAK------------- 114
Cdd:cd00773 24 IDTPvfeyTELFLRKSGDEvSKEMYRFKDKGGRDLALRPDLTAPVARAVAENLLslpLPLKLYYIGPvfryerpqkgryr 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 115 -----DFDIAGnFDPMIPDAECLKIMCEILSSLQIGDFLVKVNDRRILDGmfaICGVSDSKFRTICSSVDKLDKvsweev 189
Cdd:cd00773 104 efyqvGVEIIG-SDSPLADAEVIALAVEILEALGLKDFQIKINHRGILDG---IAGLLEDREEYIERLIDKLDK------ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 190 knemvgekglapevadrigdyvqqhggvslveqllqdpklsqnkqalEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLD 269
Cdd:cd00773 174 -----------------------------------------------EALAHLEKLLDYLEALGVDIKYSIDLSLVRGLD 206
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 384475556 270 YYTGVIYEAVLLQTPAQageeplgvGSVAAGGRYDGLVGMFDpkGRKVPCVGLSIGVERIFSIVE 334
Cdd:cd00773 207 YYTGIVFEAVADGLGAQ--------GSIAGGGRYDGLLEEFG--GEDVPAVGFAIGLERLLLALE 261
|
|
| hisS |
TIGR00442 |
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ... |
56-429 |
6.13e-70 |
|
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: 226.98 E-value: 6.13e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 56 LKTP----KETLMGKYGEDS----KLIYDLKDQGGELLSLRYDLTVPFARYLAMNKLTN---IKRYHIAK---------- 114
Cdd:TIGR00442 36 IRTPifeyTELFKRKVGEETdivsKEMYTFKDKGGRSLTLRPEGTAPVARAVIENKLLLpkpFKLYYIGPmfryerpqkg 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 115 --------DFDIAGNFDPMIpDAECLKIMCEILSSLQIGDFLVKVNDRRILDGMFAicgvsdsKFRTICSSVDK-LDKVS 185
Cdd:TIGR00442 116 ryrqfhqfGVEVIGSDSPLA-DAEIIALAADILKELGLKDFTLEINSLGILEGRLE-------YREALIRYLDKhKDKLG 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 186 WEEVKNEMVGEKGLAPEVADRIGDYVQQhggvslveqllqDPKLSQNKQAlEGLGDLKLLFEYLTLFGIddKISFDLSLA 265
Cdd:TIGR00442 188 EDSVRRLEKNPLRILDSKNEKIQELLKN------------APKILDFLCE-ESRAHFEELKELLDALGI--PYKIDPSLV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 266 RGLDYYTGVIYEAVLLQTPAQageeplgvGSVAAGGRYDGLVGMFDpkGRKVPCVGLSIGVERIFSIVEQRLEALEEKir 345
Cdd:TIGR00442 253 RGLDYYTGTVFEFVTDDLGAQ--------GSICGGGRYDGLVEELG--GPPTPAVGFAIGIERLILLLEELGLIPPPS-- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 346 tTETQVLVASAQKKLLEERLKLVSELWDAGIKAElLYKKNPKLLNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSRE 425
Cdd:TIGR00442 321 -KKPDVYVVPLGEEAELEALKLAQKLRKAGIRVE-VDLGGRKLKKQLKYADKLGARFALIIGEDELENGTVTLKDLETGE 398
|
....
gi 384475556 426 EVDV 429
Cdd:TIGR00442 399 QETV 402
|
|
| PRK12420 |
PRK12420 |
histidyl-tRNA synthetase; Provisional |
61-429 |
1.24e-57 |
|
histidyl-tRNA synthetase; Provisional
Pssm-ID: 237097 [Multi-domain] Cd Length: 423 Bit Score: 195.72 E-value: 1.24e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 61 ETLMGKYG---EDSKLIYDLKDQGGELLSLRYDLTVPFARYLAMNKltNI----KRYHIAK------------------D 115
Cdd:PRK12420 49 ELMSSKYGggdEILKEIYTLTDQGKRDLALRYDLTIPFAKVVAMNP--NIrlpfKRYEIGKvfrdgpikqgrfrefiqcD 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 116 FDIAGNFDPMiPDAECLKIMCEILSSLQIgDFLVKVNDRRILDGMFAICGVSDSKFRTICSSVDKLDKVSWEEVKNEMVg 195
Cdd:PRK12420 127 VDIVGVESVM-AEAELMSMAFELFRRLNL-EVTIQYNNRKLLNGILQAIGIPTELTSDVILSLDKIEKIGIDGVRKDLL- 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 196 EKGLAPEVADRIGDYVQQHGGVSLVEQllqdPKLSQNKQALEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVI 275
Cdd:PRK12420 204 ERGISEEMADTICNTVLSCLQLSIADF----KEAFNNPLVAEGVNELQQLQQYLIALGINENCIFNPFLARGLTMYTGTV 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 276 YEaVLLQTPAQAgeeplgvGSVAAGGRYDGLVGMFDPKGRKVPCVGLSIGVERIfsiveqrLEALEEKIRTTET-QVLVA 354
Cdd:PRK12420 280 YE-IFLKDGSIT-------SSIGSGGRYDNIIGAFRGDDMNYPTVGISFGLDVI-------YTALSQKETISSTaDVFII 344
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 384475556 355 SAQKKLleERLKLVSELW-DAGIKAELLYkKNPKLLNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVDV 429
Cdd:PRK12420 345 PLGTEL--QCLQIAQQLRsTTGLKVELEL-AGRKLKKALNYANKENIPYVLIIGEEEVSTGTVMLRNMKEGSEVKV 417
|
|
| HisZ |
COG3705 |
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism]; |
61-329 |
6.64e-33 |
|
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism];
Pssm-ID: 442919 [Multi-domain] Cd Length: 312 Bit Score: 126.44 E-value: 6.64e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 61 ETLMGKYGEDSKL-IYDLKDQGGELLSLRYDLTVPFARYLAmNKLTNIKR----------YHIAKDF------------- 116
Cdd:COG3705 36 DSLLTGSGADLDLqTFKLVDQLGRTLGLRPDMTPQVARIAA-TRLANRPGplrlcyagnvFRTRPSGlgrsreflqagae 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 117 -----DIAGnfdpmipDAECLKIMCEILSSLQIGDFLVKVNDRRILDGMFAICGVSDSKFRTICSSVDKLDKVsweEVKn 191
Cdd:COG3705 115 lighaGLEA-------DAEVIALALEALKAAGLEDFTLDLGHVGLFRALLEALGLSEEQREELRRALARKDAV---ELE- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 192 EMVGEKGLAPEVADRIGDYVQQHGGVSLVEQLLqdpKLSQNKQALEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYY 271
Cdd:COG3705 184 ELLAELGLSEELAEALLALPELYGGEEVLARAR---ALLLDAAIRAALDELEALAEALAARGPDVRLTFDLSELRGYDYY 260
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 384475556 272 TGVIYEAVLlqtpAQAGEEplgvgsVAAGGRYDGLVGMFdpkGRKVPCVGLSIGVERI 329
Cdd:COG3705 261 TGIVFEAYA----PGVGDP------LARGGRYDGLLAAF---GRARPATGFSLDLDRL 305
|
|
| PLN02530 |
PLN02530 |
histidine-tRNA ligase |
66-434 |
9.56e-31 |
|
histidine-tRNA ligase
Pssm-ID: 178145 [Multi-domain] Cd Length: 487 Bit Score: 123.70 E-value: 9.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 66 KYGED-SKLIYDLKDQGGELLSLRYDLTVPFARyLAMNKLTNI----------------------KRYHIAKDFDIAGnF 122
Cdd:PLN02530 120 KAGEEiTDQLYNFEDKGGRRVALRPELTPSLAR-LVLQKGKSLslplkwfaigqcwryermtrgrRREHYQWNMDIIG-V 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 123 DPMIPDAECLKIMCEILSSLQI--GDFLVKVNDRRILDGMFAICGVSDSKFRTICSSVDKLDKVSWEEVKNEMvGEKGLA 200
Cdd:PLN02530 198 PGVEAEAELLAAIVTFFKRVGItsSDVGIKVSSRKVLQAVLKSYGIPEESFAPVCVIVDKLEKLPREEIEKEL-DTLGVS 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 201 PEVADRIGDyVQQHGGVSLVEQLLqdpklsqnKQALEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVl 280
Cdd:PLN02530 277 EEAIEGILD-VLSLKSLDDLEALL--------GADSEAVADLKQLFSLAEAYGYQDWLVFDASVVRGLAYYTGIVFEGF- 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 281 lqtpAQAGEeplgVGSVAAGGRYDGLVGMFDpkGRKVPCVGLSIGVERIFSIVEQRlEALEEKIRTTETqvLVASAQKKL 360
Cdd:PLN02530 347 ----DRAGK----LRAICGGGRYDRLLSTFG--GEDTPACGFGFGDAVIVELLKEK-GLLPELPHQVDD--VVFALDEDL 413
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 384475556 361 LEERLKLVSELWDAGIKAEL-LYKKNPKLLnqLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVDVRREDL 434
Cdd:PLN02530 414 QGAAAGVASRLREKGRSVDLvLEPKKLKWV--FKHAERIGAKRLVLVGASEWERGMVRVKDLSSGEQTEVKLDEL 486
|
|
| hisZ_biosyn_reg |
TIGR00443 |
ATP phosphoribosyltransferase, regulatory subunit; Apparant second copies of histidyl-tRNA ... |
61-329 |
4.92e-30 |
|
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: 118.49 E-value: 4.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 61 ETLMGKYGEDSKLIYDLKDQGGELLSLRYDLTVPFARyLAMNKLTNIKR----------YHIAKDFDIAGN--------- 121
Cdd:TIGR00443 39 DTLSAGSGILNEDLFKLFDQLGRVLGLRPDMTAPIAR-LVSTRLRDRPLplrlcyagnvFRTNESGGGRSReftqagvel 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 122 --FDPMIPDAECLKIMCEILSSLQIGDFLVKVNDRRILDGMFAICGVSDSKFRTICSSVDKLDKVSWEEVknemVGEKGL 199
Cdd:TIGR00443 118 igAGGPAADAEVIALLIEALKALGLKDFKIELGHVGLVRALLEEAGLPEEAREALREALARKDLVALEEL----VAELGL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 200 APEVADRIGDYVQQHGGVSLVEQLLQdpKLSQNKQALEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAV 279
Cdd:TIGR00443 194 SPEVRERLLALPRLRGDGEEVLEEAR--ALAGSETAEAALDELEAVLELLEARGVEEYISLDLGLVRGYHYYTGLIFEGY 271
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 384475556 280 LLQTPAQageeplgvgsVAAGGRYDGLVGMFdpkGRKVPCVGLSIGVERI 329
Cdd:TIGR00443 272 APGLGAP----------LAGGGRYDELLGRF---GRPLPATGFALNLERL 308
|
|
| hisZ |
PRK12292 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
61-380 |
4.45e-29 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 237043 [Multi-domain] Cd Length: 391 Bit Score: 117.66 E-value: 4.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 61 ETLM--GKYGEDSKLIYDLKDQGGELLSLRYDLTVPFARyLAMNKLTNIKR----YHIAKDFDIAGNF------------ 122
Cdd:PRK12292 48 DTLLagGGAILDLRTFKLVDQLSGRTLGLRPDMTAQIAR-IAATRLANRPGplrlCYAGNVFRAQERGlgrsreflqsgv 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 123 -----DPMIPDAECLKIMCEILSSLQIGDFLVKVNDRRILDGMFAICGVSDSKFRTICSSVDKLDKVSWEEVknemvgEK 197
Cdd:PRK12292 127 eligdAGLEADAEVILLLLEALKALGLPNFTLDLGHVGLFRALLEAAGLSEELEEVLRRALANKDYVALEEL------VL 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 198 GLAPEVADRIGDYVQQHGGVSLVEQLLQdpkLSQNKQALEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYE 277
Cdd:PRK12292 201 DLSEELRDALLALPRLRGGREVLEEARK---LLPSLPIKRALDELEALAEALEKYGYGIPLSLDLGLLRHLDYYTGIVFE 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 278 AVLLQTPAqageeplgvgSVAAGGRYDGLVGMFdpkGRKVPCVGLSIGVERIfsiveqrLEALEEKiRTTETQVLVASAQ 357
Cdd:PRK12292 278 GYVDGVGN----------PIASGGRYDDLLGRF---GRARPATGFSLDLDRL-------LELQLEL-PVEARKDLVIAPD 336
|
330 340
....*....|....*....|...
gi 384475556 358 KKLLEERLKLVSELWDAGIKAEL 380
Cdd:PRK12292 337 SEALAAALAAAQELRKKGEIVVL 359
|
|
| tRNA-synt_His |
pfam13393 |
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ... |
61-329 |
7.07e-29 |
|
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: 115.38 E-value: 7.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 61 ETLMGKYGEDSKLIYDLKDQGGELLSLRYDLTVPFARYLAmnKLTNIKR----------YHIAKDfdiaGNFDPMIP--- 127
Cdd:pfam13393 41 DSLLTGTGADLDQTFKLVDQSGRLLGLRADITPQVARIDA--HRLNRPGplrlcyagsvLRTRPK----GLGRSREPlqv 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 128 ------------DAECLKIMCEILSSLQIGDFLVKVNDRRILDGMFAICGVSDSKFRTICSSVDKLDkvsWEEVKnEMVG 195
Cdd:pfam13393 115 gaelighagieaDAEIISLLLEALAAAGVPGVTLDLGHVGLVRALLEAAGLSEALEEALRAALQRKD---AAELA-ELAA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 196 EKGLAPEVADRIGDYVQQHGGVSLVEQLLQDpkLSQNKQALEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVI 275
Cdd:pfam13393 191 EAGLPPALRRALLALPDLYGGPEVLDEARAA--LPGLPALQEALDELEALAALLEALGDGVRLTFDLAELRGYEYYTGIV 268
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 384475556 276 YEAVLlqtpAQAGEEplgvgsVAAGGRYDGLVGMFdpkGRKVPCVGLSIGVERI 329
Cdd:pfam13393 269 FAAYA----PGVGEP------LARGGRYDDLGAAF---GRARPATGFSLDLEAL 309
|
|
| HisRS_anticodon |
cd00859 |
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases ... |
348-439 |
3.08e-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: 106.86 E-value: 3.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 348 ETQVLVASAQKKLLEERLKLVSELWDAGIKAELLYKkNPKLLNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEV 427
Cdd:cd00859 1 EVDVYVVPLGEGALSEALELAEQLRDAGIKAEIDYG-GRKLKKQFKYADRSGARFAVILGEDELAAGVVTVKDLETGEQE 79
|
90
....*....|..
gi 384475556 428 DVRREDLVEEIK 439
Cdd:cd00859 80 TVALDELVEELK 91
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
350-441 |
2.31e-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: 2.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 350 QVLVASAQKK---LLEERLKLVSELWDAGIKAELLYKkNPKLLNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREE 426
Cdd:pfam03129 1 QVVVIPLGEKaeeLEEYAQKLAEELRAAGIRVELDDR-NESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQ 79
|
90
....*....|....*
gi 384475556 427 VDVRREDLVEEIKRR 441
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 |
1.59e-16 |
|
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: 72.89 E-value: 1.59e-16
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 384475556 5 AALEELVKLQGERVRGLKQQKASAELIEEEVAKLLKLKAQLGPDE 49
Cdd:cd00938 1 AKLEEAVKLQGELVRKLKAEKASKEQIAEEVAKLLELKAQLGGDE 45
|
|
| syh |
CHL00201 |
histidine-tRNA synthetase; Provisional |
68-438 |
3.10e-15 |
|
histidine-tRNA synthetase; Provisional
Pssm-ID: 164576 [Multi-domain] Cd Length: 430 Bit Score: 77.25 E-value: 3.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 68 GEDSKLI----YDLKDQGGELLSLRYDLTVPFARYLAMNKLT---NIKR-YHIAKDF------------------DIAGN 121
Cdd:CHL00201 56 GETTDIVnkemYRFTDRSNRDITLRPEGTAGIVRAFIENKMDyhsNLQRlWYSGPMFryerpqsgrqrqfhqlgiEFIGS 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 122 FDPMiPDAECLKIMCEILSSLQIGDFLVKVN------DRRILDgmfaicgvsdSKFRTICSSV-DKLDKVSweevKNEMV 194
Cdd:CHL00201 136 IDAR-ADTEVIHLAMQIFNELQVKNLILDINsigkleDRQSYQ----------LKLVEYLSQYqDDLDTDS----QNRLY 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 195 GEkglaP-EVADRIGDYVQqhggvslvEQLLQDPKLSQ--NKQALEGLGDLkllFEYLTLFGIDDKISFdlSLARGLDYY 271
Cdd:CHL00201 201 SN----PiRILDSKNLKTQ--------EILDGAPKISDflSLESTEHFYDV---CTYLNLLNIPYKINY--KLVRGLDYY 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 272 TGVIYEAVLLQTPAQageeplgvGSVAAGGRYDGLVGMFDpkGRKVPCVGLSIGVERIFSIVEQRLEALEEKIrttetQV 351
Cdd:CHL00201 264 NDTAFEIKTLSSNGQ--------DTICGGGRYDSLIHQLG--GPKTPAVGCAIGLERLLLIAKDNIILPKQSI-----DV 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 352 LVASAQKKLLEERLKLVSELWDAGIKAELLYkKNPKLLNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVDVRR 431
Cdd:CHL00201 329 YIATQGLKAQKKGWEIIQFLEKQNIKFELDL-SSSNFHKQIKQAGKKRAKACIILGDNEIMDNCITIKWLDEQVQENAQY 407
|
....*..
gi 384475556 432 EDLVEEI 438
Cdd:CHL00201 408 SNFKQEI 414
|
|
| hisZ |
PRK12295 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
59-329 |
1.48e-12 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 183413 [Multi-domain] Cd Length: 373 Bit Score: 68.81 E-value: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 59 PKETLMGKYGED-SKLIYDLKDQGGELLSLRYDLTVPFAR-YLAMNK--------LTNIKRYHIAKD-------FDIAGN 121
Cdd:PRK12295 33 PAEPFLDLSGEDiRRRIFVTSDENGEELCLRPDFTIPVCRrHIATAGgeparyayLGEVFRQRRDRAseflqagIESFGR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 122 FDPMIPDAECLKIMCEILSSLQIGDFLVKVNDRRILDGMFAICGVSDS-KFRTIcssVDKLDKVSWEEVKNEMVGEKGLA 200
Cdd:PRK12295 113 ADPAAADAEVLALALEALAALGPGDLEVRLGDVGLFAALVDALGLPPGwKRRLL---RHFGRPRSLDALLARLAGPRVDP 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 201 PEVADRIGDYVQQHGGVS-LVEQLLQDPKLSQN------------------------------------------KQALE 237
Cdd:PRK12295 190 LDEHAGVLAALADEAAARaLVEDLMSIAGISPVggrspaeiarrllekaalaaaarlpaealavlerflaisgppDAALA 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 238 GL----GDLKL-------LFE----YLTLFGID-DKISFDLSLARGLDYYTGVIYEAvllqTPAQAGEEPLgvgsvAAGG 301
Cdd:PRK12295 270 ALralaADAGLdldaaldRFEarlaALAARGIDlERLRFSASFGRPLDYYTGFVFEI----RAAGNGDPPL-----AGGG 340
|
330 340
....*....|....*....|....*...
gi 384475556 302 RYDGLVGMFDpKGRKVPCVGLSIGVERI 329
Cdd:PRK12295 341 RYDGLLTRLG-AGEPIPAVGFSIWLDRL 367
|
|
| WHEPGMRS_RNA |
cd01200 |
EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher ... |
8-49 |
1.92e-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: 52.93 E-value: 1.92e-09
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 384475556 8 EELVKLQGERVRGLKQQKASAELIEEEVAKLLKLKAQLGPDE 49
Cdd:cd01200 1 YEKIAEQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKEAT 42
|
|
| WHEP-TRS |
pfam00458 |
WHEP-TRS domain; |
7-45 |
6.60e-09 |
|
WHEP-TRS domain;
Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 51.73 E-value: 6.60e-09
10 20 30
....*....|....*....|....*....|....*....
gi 384475556 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 |
2.22e-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: 50.42 E-value: 2.22e-08
10 20 30
....*....|....*....|....*....|....*...
gi 384475556 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 ... |
351-441 |
3.43e-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: 3.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 351 VLVASAQKKLL-EERLKLVSELWDAGIKAELLYKKNPKLLNQLQYCEEAGIPLVAIIGEQEL----KDGVIKLRSVTSRE 425
Cdd:pfam12745 8 VLVASFDASILrTTGVEILQELWAHGISADLAVDASYSPEDLVSRARDDGVSWIVIIKQQNKssdsKYKPLKVKNLLRKE 87
|
90 100
....*....|....*....|
gi 384475556 426 EVDVRREDLV----EEIKRR 441
Cdd:pfam12745 88 DVDLDSDELVswlrGEIRER 107
|
|
| PRK12421 |
PRK12421 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
192-375 |
2.37e-07 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 237098 Cd Length: 392 Bit Score: 52.66 E-value: 2.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 192 EMVGEKGLAPEVADRIGDYVQQHGGVSLVEQLLQDpKLSQNKQALEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYY 271
Cdd:PRK12421 200 EVCQNLGVGSDLRRMFYALARLNGGLEALDRALSV-LALQDAAIRQALDELKTLAAHLKNRWPELPVSIDLAELRGYHYH 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 272 TGVIYeAVLLQTPAQAgeeplgvgsVAAGGRYDGLVGMFdpkGRKVPCVGlsigveriFSIVEQRLEALEEKIRTTETQV 351
Cdd:PRK12421 279 TGLVF-AAYIPGRGQA---------LARGGRYDGIGEAF---GRARPATG--------FSMDLKELLALQFLEEEAGAIL 337
|
170 180
....*....|....*....|....
gi 384475556 352 LVASAQKKLLEErlklVSELWDAG 375
Cdd:PRK12421 338 APWGDDPDLLAA----IAELRQQG 357
|
|
| MetRS_RNA |
cd00939 |
MetRS_RNA binding domain. This short RNA-binding domain is found at the C-terminus of MetRS in ... |
7-45 |
5.30e-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: 43.23 E-value: 5.30e-06
10 20 30
....*....|....*....|....*....|....*....
gi 384475556 7 LEELVKLQGERVRGLKQQKASAELIEEEVAKLLKLKAQL 45
Cdd:cd00939 1 LEKEVAEQGNKVRKLKASKADKSVWQPEVNKLLDLKKQL 39
|
|
| PRK03991 |
PRK03991 |
threonyl-tRNA synthetase; Validated |
325-445 |
8.60e-06 |
|
threonyl-tRNA synthetase; Validated
Pssm-ID: 235190 [Multi-domain] Cd Length: 613 Bit Score: 47.94 E-value: 8.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 325 GVER-IFSIVE-QRLEALEEKIRT-----TETQVLVASAQKKLLEERLKLVSELWDAGIKAEL------LYKKnpkllnq 391
Cdd:PRK03991 469 SIERvIYALLEkAAKEEEEGKVPMlptwlSPTQVRVIPVSERHLDYAEEVADKLEAAGIRVDVddrdesLGKK------- 541
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 384475556 392 lqyCEEAG---IPLVAIIGEQELKDGVIklrSVTSREE---VDVRREDLVEEIKRRT-GQP 445
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 |
1.05e-04 |
|
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: 39.53 E-value: 1.05e-04
10 20 30
....*....|....*....|....*....|.
gi 384475556 14 QGERVRGLKQQKASAELIEEEVAKLLKLKAQ 44
Cdd:cd00936 8 QGDLVRELKAKKAPKEEIDAAVKKLLALKAD 38
|
|
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
5-66 |
4.16e-03 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 39.73 E-value: 4.16e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 384475556 5 AALEELVKLQGERVRGLKQQKASAELIEEEVAKLLKLKAQLGPDESKQKFVLKTPKETLMGK 66
Cdd:PLN02734 10 AEKQAAVTAQGNAVRALKASKADKAEIDAAIEKLKALKLEKSALEKELQAAVGAGGDGAASK 71
|
|
| ThrRS_anticodon |
cd00860 |
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases ... |
349-439 |
7.12e-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: 7.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 349 TQVLVASAQKKLLEERLKLVSELWDAGIKAELLYKkNPKLLNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVD 428
Cdd:cd00860 2 VQVVVIPVTDEHLDYAKEVAKKLSDAGIRVEVDLR-NEKLGKKIREAQLQKIPYILVVGDKEVETGTVSVRTRDGGDLGS 80
|
90
....*....|.
gi 384475556 429 VRREDLVEEIK 439
Cdd:cd00860 81 MSLDEFIEKLK 91
|
|
| PRK09194 |
PRK09194 |
prolyl-tRNA synthetase; Provisional |
311-440 |
9.16e-03 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 236405 [Multi-domain] Cd Length: 565 Bit Score: 38.53 E-value: 9.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 311 DPKGRKVP----CVGlsIGVERIFS-IVEQRLEaleEK--IRTTET---QV-LVAS-----AQKKLLEerlKLVSELWDA 374
Cdd:PRK09194 426 DENGKAQPlimgCYG--IGVSRLVAaAIEQNHD---EKgiIWPKAIapfDVhIVPVnmkdeEVKELAE---KLYAELQAA 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475556 375 GIK----------------AELLykknpkllnqlqyceeaGIPLVAIIGEQELKDGVIKLRSVTSREEVDVRREDLVEEI 438
Cdd:PRK09194 498 GIEvllddrkerpgvkfadADLI-----------------GIPHRIVVGDRGLAEGIVEYKDRRTGEKEEVPVDELVEFL 560
|
..
gi 384475556 439 KR 440
Cdd:PRK09194 561 KA 562
|
|
| |
