|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02972 |
PLN02972 |
Histidyl-tRNA synthetase |
61-387 |
4.43e-116 |
|
Histidyl-tRNA synthetase
Pssm-ID: 215525 [Multi-domain] Cd Length: 763 Bit Score: 355.35 E-value: 4.43e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278942 61 DFDIAGNFDPMIPDAECLKIMCEILSSLQIGDFLVKVNDRRILDGMFAICGVSDSKFRTICSSVDKLDKVSWEEVKNEMV 140
Cdd:PLN02972 444 DFDIAGVYEPMGPDFEIIKVLTELLDELDIGTYEVKLNHRKLLDGMLEICGVPPEKFRTICSSIDKLDKQSFEQVKKEMV 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278942 141 GEKGLAPEVADRIGDYVQQHGG-VSLVEQLLQ-DPKLSQNKQALEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYT 218
Cdd:PLN02972 524 EEKGLSNETADKIGNFVKERGPpLELLSKLRQeGSEFLGNASSRAALDELEIMFKALEKSKAIGKIVFDLSLARGLDYYT 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278942 219 GVIYEAVLLQTPaqageeplgVGSVAAGGRYDGLVGMFDpkGRKVPCVGLSIGVERIFSIVEQRLEALEEKIRTTETQVL 298
Cdd:PLN02972 604 GVIYEAVFKGAQ---------VGSIAAGGRYDNLVGMFS--GKQVPAVGVSLGIERVFAIMEQQEEEKSQVIRPTETEVL 672
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278942 299 VASAQKKLLEERLKLVSELWDAGIKAEllYKKNPKLLNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVDVRRE 378
Cdd:PLN02972 673 VSIIGDDKLALAAELVSELWNAGIKAE--YKVSTRKAKHLKRAKESGIPWMVLVGEKELSKGFVKLKNLEAGVEEEVDRT 750
|
....*....
gi 574278942 379 DLVEEIKRR 387
Cdd:PLN02972 751 CFVQELKAE 759
|
|
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
61-387 |
5.74e-62 |
|
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: 204.97 E-value: 5.74e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278942 61 DFDIAGNFDPMIpDAECLKIMCEILSSLQIGDFLVKVNDRrildgmfaicGVSDSKFRTICSSVDKLDKVSWEEVknemv 140
Cdd:COG0124 126 GVEVIGSDSPLA-DAEVIALAADLLKALGLKDFTLEINSR----------GLPEERAEALLRYLDKLDKIGHEDV----- 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278942 141 gekgLAPEVADRI------------GDYVQqhggvSLVEQLlqdPKLSQNKqALEGLGDLKLLFEYLTLFGIDdkISFDL 208
Cdd:COG0124 190 ----LDEDSQRRLetnplraildskGPDCQ-----EVLADA---PKLLDYL-GEEGLAHFEEVLELLDALGIP--YVIDP 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278942 209 SLARGLDYYTGVIYEAVLLQTPAQageeplgvGSVAAGGRYDGLVGMFDpkGRKVPCVGLSIGVERIFSIVEQRLEALEE 288
Cdd:COG0124 255 RLVRGLDYYTGTVFEIVTDGLGAQ--------GSVCGGGRYDGLVEQLG--GPPTPAVGFAIGLERLLLLLEELGLLPAA 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278942 289 KirtTETQVLVASAQKKLLEERLKLVSELWDAGIKAEL-LYKKNPKllNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSV 367
Cdd:COG0124 325 E---PPPDVYVVPLGEEARAEALKLAQELRAAGIRVELdLGGRKLK--KQLKYADKSGAPFVLILGEDELANGTVTLKDL 399
|
330 340
....*....|....*....|
gi 574278942 368 TSREEVDVRREDLVEEIKRR 387
Cdd:COG0124 400 ATGEQETVPLDELVEYLKEL 419
|
|
| hisS |
TIGR00442 |
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ... |
61-375 |
5.66e-52 |
|
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: 178.44 E-value: 5.66e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278942 61 DFDIAGNFDPMIpDAECLKIMCEILSSLQIGDFLVKVNDRRILDGMFAicgvsdsKFRTICSSVDK-LDKVSWEEVKNEM 139
Cdd:TIGR00442 124 GVEVIGSDSPLA-DAEIIALAADILKELGLKDFTLEINSLGILEGRLE-------YREALIRYLDKhKDKLGEDSVRRLE 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278942 140 VGEKGLAPEVADRIGDYVQQhggvslveqllqDPKLSQNKQAlEGLGDLKLLFEYLTLFGIddKISFDLSLARGLDYYTG 219
Cdd:TIGR00442 196 KNPLRILDSKNEKIQELLKN------------APKILDFLCE-ESRAHFEELKELLDALGI--PYKIDPSLVRGLDYYTG 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278942 220 VIYEAVLLQTPAQageeplgvGSVAAGGRYDGLVGMFDpkGRKVPCVGLSIGVERIFSIVEQRLEALEEKirtTETQVLV 299
Cdd:TIGR00442 261 TVFEFVTDDLGAQ--------GSICGGGRYDGLVEELG--GPPTPAVGFAIGIERLILLLEELGLIPPPS---KKPDVYV 327
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 574278942 300 ASAQKKLLEERLKLVSELWDAGIKAElLYKKNPKLLNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVDV 375
Cdd:TIGR00442 328 VPLGEEAELEALKLAQKLRKAGIRVE-VDLGGRKLKKQLKYADKLGARFALIIGEDELENGTVTLKDLETGEQETV 402
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
61-280 |
3.63e-49 |
|
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: 167.01 E-value: 3.63e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278942 61 DFDIAGnFDPMIPDAECLKIMCEILSSLQIGDFLVKVNDRRILDGmfaICGVSDSKFRTICSSVDKLDKvsweevknemv 140
Cdd:cd00773 109 GVEIIG-SDSPLADAEVIALAVEILEALGLKDFQIKINHRGILDG---IAGLLEDREEYIERLIDKLDK----------- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278942 141 gekglapevadrigdyvqqhggvslveqllqdpklsqnkqalEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGV 220
Cdd:cd00773 174 ------------------------------------------EALAHLEKLLDYLEALGVDIKYSIDLSLVRGLDYYTGI 211
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278942 221 IYEAVLLQTPAQageeplgvGSVAAGGRYDGLVGMFDpkGRKVPCVGLSIGVERIFSIVE 280
Cdd:cd00773 212 VFEAVADGLGAQ--------GSIAGGGRYDGLLEEFG--GEDVPAVGFAIGLERLLLALE 261
|
|
| tRNA-synt_His |
pfam13393 |
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ... |
74-275 |
4.37e-25 |
|
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: 103.82 E-value: 4.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278942 74 DAECLKIMCEILSSLQIGDFLVKVNDRRILDGMFAICGVSDSKFRTICSSVDKLDkvsWEEVKnEMVGEKGLAPEVADRI 153
Cdd:pfam13393 127 DAEIISLLLEALAAAGVPGVTLDLGHVGLVRALLEAAGLSEALEEALRAALQRKD---AAELA-ELAAEAGLPPALRRAL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278942 154 GDYVQQHGGVSLVEQLLQDpkLSQNKQALEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLlqtpAQA 233
Cdd:pfam13393 203 LALPDLYGGPEVLDEARAA--LPGLPALQEALDELEALAALLEALGDGVRLTFDLAELRGYEYYTGIVFAAYA----PGV 276
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 574278942 234 GEEplgvgsVAAGGRYDGLVGMFdpkGRKVPCVGLSIGVERI 275
Cdd:pfam13393 277 GEP------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 |
3.10e-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: 72.12 E-value: 3.10e-16
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 574278942 5 AALEELVKLQGERVRGLKQQKASAELIEEEVAKLLKLKAQLGPDE 49
Cdd:cd00938 1 AKLEEAVKLQGELVRKLKAEKASKEQIAEEVAKLLELKAQLGGDE 45
|
|
| WHEP-TRS |
pfam00458 |
WHEP-TRS domain; |
7-45 |
7.25e-09 |
|
WHEP-TRS domain;
Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 51.34 E-value: 7.25e-09
10 20 30
....*....|....*....|....*....|....*....
gi 574278942 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 ... |
8-61 |
2.61e-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: 50.03 E-value: 2.61e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 574278942 8 EELVKLQGERVRGLKQQKASAELIEEEVAKLLKLKAQLGPDESKQKFVLKTPKD 61
Cdd:smart00991 1 EEAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLKEATGQDYKPGAPPGD 54
|
|
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
5-53 |
9.69e-03 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 38.19 E-value: 9.69e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 574278942 5 AALEELVKLQGERVRGLKQQKASAELIEEEVAKLLKLKAQLGPDESKQK 53
Cdd:PLN02734 10 AEKQAAVTAQGNAVRALKASKADKAEIDAAIEKLKALKLEKSALEKELQ 58
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02972 |
PLN02972 |
Histidyl-tRNA synthetase |
61-387 |
4.43e-116 |
|
Histidyl-tRNA synthetase
Pssm-ID: 215525 [Multi-domain] Cd Length: 763 Bit Score: 355.35 E-value: 4.43e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278942 61 DFDIAGNFDPMIPDAECLKIMCEILSSLQIGDFLVKVNDRRILDGMFAICGVSDSKFRTICSSVDKLDKVSWEEVKNEMV 140
Cdd:PLN02972 444 DFDIAGVYEPMGPDFEIIKVLTELLDELDIGTYEVKLNHRKLLDGMLEICGVPPEKFRTICSSIDKLDKQSFEQVKKEMV 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278942 141 GEKGLAPEVADRIGDYVQQHGG-VSLVEQLLQ-DPKLSQNKQALEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYT 218
Cdd:PLN02972 524 EEKGLSNETADKIGNFVKERGPpLELLSKLRQeGSEFLGNASSRAALDELEIMFKALEKSKAIGKIVFDLSLARGLDYYT 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278942 219 GVIYEAVLLQTPaqageeplgVGSVAAGGRYDGLVGMFDpkGRKVPCVGLSIGVERIFSIVEQRLEALEEKIRTTETQVL 298
Cdd:PLN02972 604 GVIYEAVFKGAQ---------VGSIAAGGRYDNLVGMFS--GKQVPAVGVSLGIERVFAIMEQQEEEKSQVIRPTETEVL 672
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278942 299 VASAQKKLLEERLKLVSELWDAGIKAEllYKKNPKLLNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVDVRRE 378
Cdd:PLN02972 673 VSIIGDDKLALAAELVSELWNAGIKAE--YKVSTRKAKHLKRAKESGIPWMVLVGEKELSKGFVKLKNLEAGVEEEVDRT 750
|
....*....
gi 574278942 379 DLVEEIKRR 387
Cdd:PLN02972 751 CFVQELKAE 759
|
|
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
61-387 |
5.74e-62 |
|
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: 204.97 E-value: 5.74e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278942 61 DFDIAGNFDPMIpDAECLKIMCEILSSLQIGDFLVKVNDRrildgmfaicGVSDSKFRTICSSVDKLDKVSWEEVknemv 140
Cdd:COG0124 126 GVEVIGSDSPLA-DAEVIALAADLLKALGLKDFTLEINSR----------GLPEERAEALLRYLDKLDKIGHEDV----- 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278942 141 gekgLAPEVADRI------------GDYVQqhggvSLVEQLlqdPKLSQNKqALEGLGDLKLLFEYLTLFGIDdkISFDL 208
Cdd:COG0124 190 ----LDEDSQRRLetnplraildskGPDCQ-----EVLADA---PKLLDYL-GEEGLAHFEEVLELLDALGIP--YVIDP 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278942 209 SLARGLDYYTGVIYEAVLLQTPAQageeplgvGSVAAGGRYDGLVGMFDpkGRKVPCVGLSIGVERIFSIVEQRLEALEE 288
Cdd:COG0124 255 RLVRGLDYYTGTVFEIVTDGLGAQ--------GSVCGGGRYDGLVEQLG--GPPTPAVGFAIGLERLLLLLEELGLLPAA 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278942 289 KirtTETQVLVASAQKKLLEERLKLVSELWDAGIKAEL-LYKKNPKllNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSV 367
Cdd:COG0124 325 E---PPPDVYVVPLGEEARAEALKLAQELRAAGIRVELdLGGRKLK--KQLKYADKSGAPFVLILGEDELANGTVTLKDL 399
|
330 340
....*....|....*....|
gi 574278942 368 TSREEVDVRREDLVEEIKRR 387
Cdd:COG0124 400 ATGEQETVPLDELVEYLKEL 419
|
|
| hisS |
TIGR00442 |
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ... |
61-375 |
5.66e-52 |
|
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: 178.44 E-value: 5.66e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278942 61 DFDIAGNFDPMIpDAECLKIMCEILSSLQIGDFLVKVNDRRILDGMFAicgvsdsKFRTICSSVDK-LDKVSWEEVKNEM 139
Cdd:TIGR00442 124 GVEVIGSDSPLA-DAEIIALAADILKELGLKDFTLEINSLGILEGRLE-------YREALIRYLDKhKDKLGEDSVRRLE 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278942 140 VGEKGLAPEVADRIGDYVQQhggvslveqllqDPKLSQNKQAlEGLGDLKLLFEYLTLFGIddKISFDLSLARGLDYYTG 219
Cdd:TIGR00442 196 KNPLRILDSKNEKIQELLKN------------APKILDFLCE-ESRAHFEELKELLDALGI--PYKIDPSLVRGLDYYTG 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278942 220 VIYEAVLLQTPAQageeplgvGSVAAGGRYDGLVGMFDpkGRKVPCVGLSIGVERIFSIVEQRLEALEEKirtTETQVLV 299
Cdd:TIGR00442 261 TVFEFVTDDLGAQ--------GSICGGGRYDGLVEELG--GPPTPAVGFAIGIERLILLLEELGLIPPPS---KKPDVYV 327
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 574278942 300 ASAQKKLLEERLKLVSELWDAGIKAElLYKKNPKLLNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVDV 375
Cdd:TIGR00442 328 VPLGEEAELEALKLAQKLRKAGIRVE-VDLGGRKLKKQLKYADKLGARFALIIGEDELENGTVTLKDLETGEQETV 402
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
61-280 |
3.63e-49 |
|
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: 167.01 E-value: 3.63e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278942 61 DFDIAGnFDPMIPDAECLKIMCEILSSLQIGDFLVKVNDRRILDGmfaICGVSDSKFRTICSSVDKLDKvsweevknemv 140
Cdd:cd00773 109 GVEIIG-SDSPLADAEVIALAVEILEALGLKDFQIKINHRGILDG---IAGLLEDREEYIERLIDKLDK----------- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278942 141 gekglapevadrigdyvqqhggvslveqllqdpklsqnkqalEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGV 220
Cdd:cd00773 174 ------------------------------------------EALAHLEKLLDYLEALGVDIKYSIDLSLVRGLDYYTGI 211
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278942 221 IYEAVLLQTPAQageeplgvGSVAAGGRYDGLVGMFDpkGRKVPCVGLSIGVERIFSIVE 280
Cdd:cd00773 212 VFEAVADGLGAQ--------GSIAGGGRYDGLLEEFG--GEDVPAVGFAIGLERLLLALE 261
|
|
| PRK12420 |
PRK12420 |
histidyl-tRNA synthetase; Provisional |
61-375 |
4.40e-42 |
|
histidyl-tRNA synthetase; Provisional
Pssm-ID: 237097 [Multi-domain] Cd Length: 423 Bit Score: 152.58 E-value: 4.40e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278942 61 DFDIAGNFDPMiPDAECLKIMCEILSSLQIgDFLVKVNDRRILDGMFAICGVSDSKFRTICSSVDKLDKVSWEEVKNEMV 140
Cdd:PRK12420 126 DVDIVGVESVM-AEAELMSMAFELFRRLNL-EVTIQYNNRKLLNGILQAIGIPTELTSDVILSLDKIEKIGIDGVRKDLL 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278942 141 gEKGLAPEVADRIGDYVQQHGGVSLVEQllqdPKLSQNKQALEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGV 220
Cdd:PRK12420 204 -ERGISEEMADTICNTVLSCLQLSIADF----KEAFNNPLVAEGVNELQQLQQYLIALGINENCIFNPFLARGLTMYTGT 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278942 221 IYEaVLLQTPAQAgeeplgvGSVAAGGRYDGLVGMFDPKGRKVPCVGLSIGVERIfsiveqrLEALEEKIRTTET-QVLV 299
Cdd:PRK12420 279 VYE-IFLKDGSIT-------SSIGSGGRYDNIIGAFRGDDMNYPTVGISFGLDVI-------YTALSQKETISSTaDVFI 343
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 574278942 300 ASAQKKLleERLKLVSELW-DAGIKAELLYkKNPKLLNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVDV 375
Cdd:PRK12420 344 IPLGTEL--QCLQIAQQLRsTTGLKVELEL-AGRKLKKALNYANKENIPYVLIIGEEEVSTGTVMLRNMKEGSEVKV 417
|
|
| HisZ |
COG3705 |
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism]; |
74-275 |
1.58e-28 |
|
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism];
Pssm-ID: 442919 [Multi-domain] Cd Length: 312 Bit Score: 113.35 E-value: 1.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278942 74 DAECLKIMCEILSSLQIGDFLVKVNDRRILDGMFAICGVSDSKFRTICSSVDKLDKVsweEVKnEMVGEKGLAPEVADRI 153
Cdd:COG3705 124 DAEVIALALEALKAAGLEDFTLDLGHVGLFRALLEALGLSEEQREELRRALARKDAV---ELE-ELLAELGLSEELAEAL 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278942 154 GDYVQQHGGVSLVEQLLqdpKLSQNKQALEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLlqtpAQA 233
Cdd:COG3705 200 LALPELYGGEEVLARAR---ALLLDAAIRAALDELEALAEALAARGPDVRLTFDLSELRGYDYYTGIVFEAYA----PGV 272
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 574278942 234 GEEplgvgsVAAGGRYDGLVGMFdpkGRKVPCVGLSIGVERI 275
Cdd:COG3705 273 GDP------LARGGRYDGLLAAF---GRARPATGFSLDLDRL 305
|
|
| HisRS_anticodon |
cd00859 |
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases ... |
294-385 |
2.89e-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: 106.08 E-value: 2.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278942 294 ETQVLVASAQKKLLEERLKLVSELWDAGIKAELLYKkNPKLLNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEV 373
Cdd:cd00859 1 EVDVYVVPLGEGALSEALELAEQLRDAGIKAEIDYG-GRKLKKQFKYADRSGARFAVILGEDELAAGVVTVKDLETGEQE 79
|
90
....*....|..
gi 574278942 374 DVRREDLVEEIK 385
Cdd:cd00859 80 TVALDELVEELK 91
|
|
| PLN02530 |
PLN02530 |
histidine-tRNA ligase |
74-380 |
2.92e-28 |
|
histidine-tRNA ligase
Pssm-ID: 178145 [Multi-domain] Cd Length: 487 Bit Score: 115.61 E-value: 2.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278942 74 DAECLKIMCEILSSLQI--GDFLVKVNDRRILDGMFAICGVSDSKFRTICSSVDKLDKVSWEEVKNEMvGEKGLAPEVAD 151
Cdd:PLN02530 203 EAELLAAIVTFFKRVGItsSDVGIKVSSRKVLQAVLKSYGIPEESFAPVCVIVDKLEKLPREEIEKEL-DTLGVSEEAIE 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278942 152 RIGDyVQQHGGVSLVEQLLqdpklsqnKQALEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVllqtpA 231
Cdd:PLN02530 282 GILD-VLSLKSLDDLEALL--------GADSEAVADLKQLFSLAEAYGYQDWLVFDASVVRGLAYYTGIVFEGF-----D 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278942 232 QAGEeplgVGSVAAGGRYDGLVGMFDpkGRKVPCVGLSIGVERIFSIVEQRlEALEEKIRTTETqvLVASAQKKLLEERL 311
Cdd:PLN02530 348 RAGK----LRAICGGGRYDRLLSTFG--GEDTPACGFGFGDAVIVELLKEK-GLLPELPHQVDD--VVFALDEDLQGAAA 418
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278942 312 KLVSELWDAGIKAEL-LYKKNPKLLnqLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVDVRREDL 380
Cdd:PLN02530 419 GVASRLREKGRSVDLvLEPKKLKWV--FKHAERIGAKRLVLVGASEWERGMVRVKDLSSGEQTEVKLDEL 486
|
|
| hisZ |
PRK12292 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
73-326 |
1.15e-27 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 237043 [Multi-domain] Cd Length: 391 Bit Score: 112.65 E-value: 1.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278942 73 PDAECLKIMCEILSSLQIGDFLVKVNDRRILDGMFAICGVSDSKFRTICSSVDKLDKVSWEEVknemvgEKGLAPEVADR 152
Cdd:PRK12292 136 ADAEVILLLLEALKALGLPNFTLDLGHVGLFRALLEAAGLSEELEEVLRRALANKDYVALEEL------VLDLSEELRDA 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278942 153 IGDYVQQHGGVSLVEQLLQdpkLSQNKQALEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLLQTPAq 232
Cdd:PRK12292 210 LLALPRLRGGREVLEEARK---LLPSLPIKRALDELEALAEALEKYGYGIPLSLDLGLLRHLDYYTGIVFEGYVDGVGN- 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278942 233 ageeplgvgSVAAGGRYDGLVGMFdpkGRKVPCVGLSIGVERIfsiveqrLEALEEKiRTTETQVLVASAQKKLLEERLK 312
Cdd:PRK12292 286 ---------PIASGGRYDDLLGRF---GRARPATGFSLDLDRL-------LELQLEL-PVEARKDLVIAPDSEALAAALA 345
|
250
....*....|....
gi 574278942 313 LVSELWDAGIKAEL 326
Cdd:PRK12292 346 AAQELRKKGEIVVL 359
|
|
| hisZ_biosyn_reg |
TIGR00443 |
ATP phosphoribosyltransferase, regulatory subunit; Apparant second copies of histidyl-tRNA ... |
74-275 |
2.87e-27 |
|
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: 110.01 E-value: 2.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278942 74 DAECLKIMCEILSSLQIGDFLVKVNDRRILDGMFAICGVSDSKFRTICSSVDKLDKVSWEEVknemVGEKGLAPEVADRI 153
Cdd:TIGR00443 126 DAEVIALLIEALKALGLKDFKIELGHVGLVRALLEEAGLPEEAREALREALARKDLVALEEL----VAELGLSPEVRERL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278942 154 GDYVQQHGGVSLVEQLLQdpKLSQNKQALEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLLQTPAQa 233
Cdd:TIGR00443 202 LALPRLRGDGEEVLEEAR--ALAGSETAEAALDELEAVLELLEARGVEEYISLDLGLVRGYHYYTGLIFEGYAPGLGAP- 278
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 574278942 234 geeplgvgsVAAGGRYDGLVGMFdpkGRKVPCVGLSIGVERI 275
Cdd:TIGR00443 279 ---------LAGGGRYDELLGRF---GRPLPATGFALNLERL 308
|
|
| tRNA-synt_His |
pfam13393 |
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ... |
74-275 |
4.37e-25 |
|
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: 103.82 E-value: 4.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278942 74 DAECLKIMCEILSSLQIGDFLVKVNDRRILDGMFAICGVSDSKFRTICSSVDKLDkvsWEEVKnEMVGEKGLAPEVADRI 153
Cdd:pfam13393 127 DAEIISLLLEALAAAGVPGVTLDLGHVGLVRALLEAAGLSEALEEALRAALQRKD---AAELA-ELAAEAGLPPALRRAL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278942 154 GDYVQQHGGVSLVEQLLQDpkLSQNKQALEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLlqtpAQA 233
Cdd:pfam13393 203 LALPDLYGGPEVLDEARAA--LPGLPALQEALDELEALAALLEALGDGVRLTFDLAELRGYEYYTGIVFAAYA----PGV 276
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 574278942 234 GEEplgvgsVAAGGRYDGLVGMFdpkGRKVPCVGLSIGVERI 275
Cdd:pfam13393 277 GEP------LARGGRYDDLGAAF---GRARPATGFSLDLEAL 309
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
296-387 |
3.36e-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: 76.09 E-value: 3.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278942 296 QVLVASAQKK---LLEERLKLVSELWDAGIKAELLYKkNPKLLNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREE 372
Cdd:pfam03129 1 QVVVIPLGEKaeeLEEYAQKLAEELRAAGIRVELDDR-NESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQ 79
|
90
....*....|....*
gi 574278942 373 VDVRREDLVEEIKRR 387
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 |
3.10e-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: 72.12 E-value: 3.10e-16
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 574278942 5 AALEELVKLQGERVRGLKQQKASAELIEEEVAKLLKLKAQLGPDE 49
Cdd:cd00938 1 AKLEEAVKLQGELVRKLKAEKASKEQIAEEVAKLLELKAQLGGDE 45
|
|
| syh |
CHL00201 |
histidine-tRNA synthetase; Provisional |
66-384 |
4.73e-14 |
|
histidine-tRNA synthetase; Provisional
Pssm-ID: 164576 [Multi-domain] Cd Length: 430 Bit Score: 73.40 E-value: 4.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278942 66 GNFDPMiPDAECLKIMCEILSSLQIGDFLVKVN------DRRILDgmfaicgvsdSKFRTICSSV-DKLDKVSweevKNE 138
Cdd:CHL00201 134 GSIDAR-ADTEVIHLAMQIFNELQVKNLILDINsigkleDRQSYQ----------LKLVEYLSQYqDDLDTDS----QNR 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278942 139 MVGEkglaP-EVADRIGDYVQqhggvslvEQLLQDPKLSQ--NKQALEGLGDLkllFEYLTLFGIDDKISFdlSLARGLD 215
Cdd:CHL00201 199 LYSN----PiRILDSKNLKTQ--------EILDGAPKISDflSLESTEHFYDV---CTYLNLLNIPYKINY--KLVRGLD 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278942 216 YYTGVIYEAVLLQTPAQageeplgvGSVAAGGRYDGLVGMFDpkGRKVPCVGLSIGVERIFSIVEQRLEALEEKIrttet 295
Cdd:CHL00201 262 YYNDTAFEIKTLSSNGQ--------DTICGGGRYDSLIHQLG--GPKTPAVGCAIGLERLLLIAKDNIILPKQSI----- 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278942 296 QVLVASAQKKLLEERLKLVSELWDAGIKAELLYkKNPKLLNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVDV 375
Cdd:CHL00201 327 DVYIATQGLKAQKKGWEIIQFLEKQNIKFELDL-SSSNFHKQIKQAGKKRAKACIILGDNEIMDNCITIKWLDEQVQENA 405
|
....*....
gi 574278942 376 RREDLVEEI 384
Cdd:CHL00201 406 QYSNFKQEI 414
|
|
| hisZ |
PRK12295 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
199-275 |
3.85e-11 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 183413 [Multi-domain] Cd Length: 373 Bit Score: 63.80 E-value: 3.85e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 574278942 199 GID-DKISFDLSLARGLDYYTGVIYEAvllqTPAQAGEEPLgvgsvAAGGRYDGLVGMFDpKGRKVPCVGLSIGVERI 275
Cdd:PRK12295 300 GIDlERLRFSASFGRPLDYYTGFVFEI----RAAGNGDPPL-----AGGGRYDGLLTRLG-AGEPIPAVGFSIWLDRL 367
|
|
| WHEPGMRS_RNA |
cd01200 |
EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher ... |
8-49 |
2.24e-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: 52.54 E-value: 2.24e-09
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 574278942 8 EELVKLQGERVRGLKQQKASAELIEEEVAKLLKLKAQLGPDE 49
Cdd:cd01200 1 YEKIAEQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKEAT 42
|
|
| WHEP-TRS |
pfam00458 |
WHEP-TRS domain; |
7-45 |
7.25e-09 |
|
WHEP-TRS domain;
Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 51.34 E-value: 7.25e-09
10 20 30
....*....|....*....|....*....|....*....
gi 574278942 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 ... |
8-61 |
2.61e-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: 50.03 E-value: 2.61e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 574278942 8 EELVKLQGERVRGLKQQKASAELIEEEVAKLLKLKAQLGPDESKQKFVLKTPKD 61
Cdd:smart00991 1 EEAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLKEATGQDYKPGAPPGD 54
|
|
| HGTP_anticodon2 |
pfam12745 |
Anticodon binding domain of tRNAs; This is an HGTP_anticodon binding domain, found largely on ... |
297-387 |
3.16e-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: 54.15 E-value: 3.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278942 297 VLVASAQKKLL-EERLKLVSELWDAGIKAELLYKKNPKLLNQLQYCEEAGIPLVAIIGEQEL----KDGVIKLRSVTSRE 371
Cdd:pfam12745 8 VLVASFDASILrTTGVEILQELWAHGISADLAVDASYSPEDLVSRARDDGVSWIVIIKQQNKssdsKYKPLKVKNLLRKE 87
|
90 100
....*....|....*....|
gi 574278942 372 EVDVRREDLV----EEIKRR 387
Cdd:pfam12745 88 DVDLDSDELVswlrGEIRER 107
|
|
| PRK12421 |
PRK12421 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
138-321 |
2.11e-07 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 237098 Cd Length: 392 Bit Score: 52.66 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278942 138 EMVGEKGLAPEVADRIGDYVQQHGGVSLVEQLLQDpKLSQNKQALEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYY 217
Cdd:PRK12421 200 EVCQNLGVGSDLRRMFYALARLNGGLEALDRALSV-LALQDAAIRQALDELKTLAAHLKNRWPELPVSIDLAELRGYHYH 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278942 218 TGVIYeAVLLQTPAQAgeeplgvgsVAAGGRYDGLVGMFdpkGRKVPCVGlsigveriFSIVEQRLEALEEKIRTTETQV 297
Cdd:PRK12421 279 TGLVF-AAYIPGRGQA---------LARGGRYDGIGEAF---GRARPATG--------FSMDLKELLALQFLEEEAGAIL 337
|
170 180
....*....|....*....|....
gi 574278942 298 LVASAQKKLLEErlklVSELWDAG 321
Cdd:PRK12421 338 APWGDDPDLLAA----IAELRQQG 357
|
|
| PRK03991 |
PRK03991 |
threonyl-tRNA synthetase; Validated |
271-391 |
6.56e-06 |
|
threonyl-tRNA synthetase; Validated
Pssm-ID: 235190 [Multi-domain] Cd Length: 613 Bit Score: 48.33 E-value: 6.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278942 271 GVER-IFSIVE-QRLEALEEKIRT-----TETQVLVASAQKKLLEERLKLVSELWDAGIKAEL------LYKKnpkllnq 337
Cdd:PRK03991 469 SIERvIYALLEkAAKEEEEGKVPMlptwlSPTQVRVIPVSERHLDYAEEVADKLEAAGIRVDVddrdesLGKK------- 541
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 574278942 338 lqyCEEAG---IPLVAIIGEQELKDGVIklrSVTSREE---VDVRREDLVEEIKRRT-GQP 391
Cdd:PRK03991 542 ---IRDAGkewIPYVVVIGDKEMESGKL---TVTIREEsekVEMTLEELIERIKEETkGYP 596
|
|
| MetRS_RNA |
cd00939 |
MetRS_RNA binding domain. This short RNA-binding domain is found at the C-terminus of MetRS in ... |
7-45 |
7.24e-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: 42.84 E-value: 7.24e-06
10 20 30
....*....|....*....|....*....|....*....
gi 574278942 7 LEELVKLQGERVRGLKQQKASAELIEEEVAKLLKLKAQL 45
Cdd:cd00939 1 LEKEVAEQGNKVRKLKASKADKSVWQPEVNKLLDLKKQL 39
|
|
| WEPRS_RNA |
cd00936 |
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ... |
14-44 |
9.36e-05 |
|
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in multiple copies in eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases (EPRS) in a region that separates the N-terminal glutamyl-tRNA synthetase (GluRS) from the C-terminal prolyl-tRNA synthetase (ProRS). It is also found at the N-terminus of vertebrate tryptophanyl-tRNA synthetases (TrpRS). This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238473 [Multi-domain] Cd Length: 50 Bit Score: 39.53 E-value: 9.36e-05
10 20 30
....*....|....*....|....*....|.
gi 574278942 14 QGERVRGLKQQKASAELIEEEVAKLLKLKAQ 44
Cdd:cd00936 8 QGDLVRELKAKKAPKEEIDAAVKKLLALKAD 38
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|
| ThrRS_anticodon |
cd00860 |
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases ... |
295-385 |
7.08e-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: 7.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278942 295 TQVLVASAQKKLLEERLKLVSELWDAGIKAELLYKkNPKLLNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVD 374
Cdd:cd00860 2 VQVVVIPVTDEHLDYAKEVAKKLSDAGIRVEVDLR-NEKLGKKIREAQLQKIPYILVVGDKEVETGTVSVRTRDGGDLGS 80
|
90
....*....|.
gi 574278942 375 VRREDLVEEIK 385
Cdd:cd00860 81 MSLDEFIEKLK 91
|
|
| PRK09194 |
PRK09194 |
prolyl-tRNA synthetase; Provisional |
257-386 |
7.97e-03 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 236405 [Multi-domain] Cd Length: 565 Bit Score: 38.14 E-value: 7.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278942 257 DPKGRKVP----CVGlsIGVERIFS-IVEQRLEaleEK--IRTTET---QV-LVAS-----AQKKLLEerlKLVSELWDA 320
Cdd:PRK09194 426 DENGKAQPlimgCYG--IGVSRLVAaAIEQNHD---EKgiIWPKAIapfDVhIVPVnmkdeEVKELAE---KLYAELQAA 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278942 321 GIK----------------AELLykknpkllnqlqyceeaGIPLVAIIGEQELKDGVIKLRSVTSREEVDVRREDLVEEI 384
Cdd:PRK09194 498 GIEvllddrkerpgvkfadADLI-----------------GIPHRIVVGDRGLAEGIVEYKDRRTGEKEEVPVDELVEFL 560
|
..
gi 574278942 385 KR 386
Cdd:PRK09194 561 KA 562
|
|
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
5-53 |
9.69e-03 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 38.19 E-value: 9.69e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 574278942 5 AALEELVKLQGERVRGLKQQKASAELIEEEVAKLLKLKAQLGPDESKQK 53
Cdd:PLN02734 10 AEKQAAVTAQGNAVRALKASKADKAEIDAAIEKLKALKLEKSALEKELQ 58
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