|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02972 |
PLN02972 |
Histidyl-tRNA synthetase |
56-461 |
7.72e-176 |
|
Histidyl-tRNA synthetase
Pssm-ID: 215525 [Multi-domain] Cd Length: 763 Bit Score: 511.74 E-value: 7.72e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 56 LKTP----KETLMGKYGEDSKLIYDLKDQGGELLSLRYDLTVPFARYLAMNKLTNIKRYHIAKVYRRDNPamTRGRYREF 131
Cdd:PLN02972 363 LDTPvfelRETLMGKYGEDSKLIYDLADQGGELCSLRYDLTVPFARYVAMNGITSFKRYQIAKVYRRDNP--SKGRYREF 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 132 YQCDFDIAGNFDPMIPDAECLKIMCEILSSLQIGDFLVKVNDRRILDGMFAICGVSDSKFRTICSSVDKLDKVSWEEVKN 211
Cdd:PLN02972 441 YQCDFDIAGVYEPMGPDFEIIKVLTELLDELDIGTYEVKLNHRKLLDGMLEICGVPPEKFRTICSSIDKLDKQSFEQVKK 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 212 EMVGEKGLAPEVADRIGDYVQQHGG-VSLVEQLLQ-DPKLSQNKQALEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLD 289
Cdd:PLN02972 521 EMVEEKGLSNETADKIGNFVKERGPpLELLSKLRQeGSEFLGNASSRAALDELEIMFKALEKSKAIGKIVFDLSLARGLD 600
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 290 YYTGVIYEAVLLQTPaqageeplgVGSVAAGGRYDGLVGMFDpkGRKVPCVGLSIGVERIFSIVEQRLEALEEKIRTTET 369
Cdd:PLN02972 601 YYTGVIYEAVFKGAQ---------VGSIAAGGRYDNLVGMFS--GKQVPAVGVSLGIERVFAIMEQQEEEKSQVIRPTET 669
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 370 QVLVASAQKKLLEERLKLVSELWDAGIKAEllYKKNPKLLNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVDV 449
Cdd:PLN02972 670 EVLVSIIGDDKLALAAELVSELWNAGIKAE--YKVSTRKAKHLKRAKESGIPWMVLVGEKELSKGFVKLKNLEAGVEEEV 747
|
410
....*....|..
gi 194379338 450 RREDLVEEIKRR 461
Cdd:PLN02972 748 DRTCFVQELKAE 759
|
|
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
61-461 |
3.66e-99 |
|
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: 303.97 E-value: 3.66e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 61 ETLMGKYGED--SKLIYDLKDQGGELLSLRYDLTVPFARYLAMNKLTN---IKRYHIAKVYRRDNPAmtRGRYREFYQCD 135
Cdd:COG0124 49 ELFARKIGEDivEKEMYTFEDRGGRSLTLRPEGTAPVARAVAEHGNELpfpFKLYYIGPVFRYERPQ--KGRYRQFHQFG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 136 FDIAGNFDPMIpDAECLKIMCEILSSLQIGDFLVKVNDRrildgmfaicGVSDSKFRTICSSVDKLDKVSWEEVknemvg 215
Cdd:COG0124 127 VEVIGSDSPLA-DAEVIALAADLLKALGLKDFTLEINSR----------GLPEERAEALLRYLDKLDKIGHEDV------ 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 216 ekgLAPEVADRI------------GDYVQqhggvSLVEQLlqdPKLSQNKqALEGLGDLKLLFEYLTLFGIDdkISFDLS 283
Cdd:COG0124 190 ---LDEDSQRRLetnplraildskGPDCQ-----EVLADA---PKLLDYL-GEEGLAHFEEVLELLDALGIP--YVIDPR 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 284 LARGLDYYTGVIYEAVLLQTPAQageeplgvGSVAAGGRYDGLVGMFDpkGRKVPCVGLSIGVERIFSIVEQRLEALEEK 363
Cdd:COG0124 256 LVRGLDYYTGTVFEIVTDGLGAQ--------GSVCGGGRYDGLVEQLG--GPPTPAVGFAIGLERLLLLLEELGLLPAAE 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 364 irtTETQVLVASAQKKLLEERLKLVSELWDAGIKAEL-LYKKNPKllNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVT 442
Cdd:COG0124 326 ---PPPDVYVVPLGEEARAEALKLAQELRAAGIRVELdLGGRKLK--KQLKYADKSGAPFVLILGEDELANGTVTLKDLA 400
|
410
....*....|....*....
gi 194379338 443 SREEVDVRREDLVEEIKRR 461
Cdd:COG0124 401 TGEQETVPLDELVEYLKEL 419
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
56-354 |
6.12e-89 |
|
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: 271.78 E-value: 6.12e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 56 LKTP----KETLMGKYGED-SKLIYDLKDQGGELLSLRYDLTVPFARYLAMNKL---TNIKRYHIAKVYRRDNPAmtRGR 127
Cdd:cd00773 24 IDTPvfeyTELFLRKSGDEvSKEMYRFKDKGGRDLALRPDLTAPVARAVAENLLslpLPLKLYYIGPVFRYERPQ--KGR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 128 YREFYQCDFDIAGnFDPMIPDAECLKIMCEILSSLQIGDFLVKVNDRRILDGmfaICGVSDSKFRTICSSVDKLDKvswe 207
Cdd:cd00773 102 YREFYQVGVEIIG-SDSPLADAEVIALAVEILEALGLKDFQIKINHRGILDG---IAGLLEDREEYIERLIDKLDK---- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 208 evknemvgekglapevadrigdyvqqhggvslveqllqdpklsqnkqalEGLGDLKLLFEYLTLFGIDDKISFDLSLARG 287
Cdd:cd00773 174 -------------------------------------------------EALAHLEKLLDYLEALGVDIKYSIDLSLVRG 204
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 194379338 288 LDYYTGVIYEAVLLQTPAQageeplgvGSVAAGGRYDGLVGMFDpkGRKVPCVGLSIGVERIFSIVE 354
Cdd:cd00773 205 LDYYTGIVFEAVADGLGAQ--------GSIAGGGRYDGLLEEFG--GEDVPAVGFAIGLERLLLALE 261
|
|
| hisS |
TIGR00442 |
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ... |
56-449 |
4.51e-85 |
|
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: 267.04 E-value: 4.51e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 56 LKTP----KETLMGKYGEDS----KLIYDLKDQGGELLSLRYDLTVPFARYLAMNKLTN---IKRYHIAKVYRRDNPAmt 124
Cdd:TIGR00442 36 IRTPifeyTELFKRKVGEETdivsKEMYTFKDKGGRSLTLRPEGTAPVARAVIENKLLLpkpFKLYYIGPMFRYERPQ-- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 125 RGRYREFYQCDFDIAGNFDPMIpDAECLKIMCEILSSLQIGDFLVKVNDRRILDGMFAicgvsdsKFRTICSSVDK-LDK 203
Cdd:TIGR00442 114 KGRYRQFHQFGVEVIGSDSPLA-DAEIIALAADILKELGLKDFTLEINSLGILEGRLE-------YREALIRYLDKhKDK 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 204 VSWEEVKNEMVGEKGLAPEVADRIGDYVQQhggvslveqllqDPKLSQNKQAlEGLGDLKLLFEYLTLFGIddKISFDLS 283
Cdd:TIGR00442 186 LGEDSVRRLEKNPLRILDSKNEKIQELLKN------------APKILDFLCE-ESRAHFEELKELLDALGI--PYKIDPS 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 284 LARGLDYYTGVIYEAVLLQTPAQageeplgvGSVAAGGRYDGLVGMFDpkGRKVPCVGLSIGVERIFSIVEQRLEALEEK 363
Cdd:TIGR00442 251 LVRGLDYYTGTVFEFVTDDLGAQ--------GSICGGGRYDGLVEELG--GPPTPAVGFAIGIERLILLLEELGLIPPPS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 364 irtTETQVLVASAQKKLLEERLKLVSELWDAGIKAElLYKKNPKLLNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTS 443
Cdd:TIGR00442 321 ---KKPDVYVVPLGEEAELEALKLAQKLRKAGIRVE-VDLGGRKLKKQLKYADKLGARFALIIGEDELENGTVTLKDLET 396
|
....*.
gi 194379338 444 REEVDV 449
Cdd:TIGR00442 397 GEQETV 402
|
|
| tRNA-synt_His |
pfam13393 |
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ... |
61-349 |
6.25e-35 |
|
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: 132.32 E-value: 6.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 61 ETLMGKYGEDSKLIYDLKDQGGELLSLRYDLTVPFARYLAmnKLTNIKR----YHIAKVYRRDNPAMtrGRYREFYQCDF 136
Cdd:pfam13393 41 DSLLTGTGADLDQTFKLVDQSGRLLGLRADITPQVARIDA--HRLNRPGplrlCYAGSVLRTRPKGL--GRSREPLQVGA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 137 DIAGNFDPMiPDAECLKIMCEILSSLQIGDFLVKVNDRRILDGMFAICGVSDSKFRTICSSVDKLDkvsWEEVKnEMVGE 216
Cdd:pfam13393 117 ELIGHAGIE-ADAEIISLLLEALAAAGVPGVTLDLGHVGLVRALLEAAGLSEALEEALRAALQRKD---AAELA-ELAAE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 217 KGLAPEVADRIGDYVQQHGGVSLVEQLLQDpkLSQNKQALEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIY 296
Cdd:pfam13393 192 AGLPPALRRALLALPDLYGGPEVLDEARAA--LPGLPALQEALDELEALAALLEALGDGVRLTFDLAELRGYEYYTGIVF 269
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 194379338 297 EAVLlqtpAQAGEEplgvgsVAAGGRYDGLVGMFdpkGRKVPCVGLSIGVERI 349
Cdd:pfam13393 270 AAYA----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 |
5.51e-17 |
|
HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). This domain consists of a helix- turn- helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238474 [Multi-domain] Cd Length: 45 Bit Score: 74.43 E-value: 5.51e-17
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 194379338 5 AALEELVKLQGERVRGLKQQKASAELIEEEVAKLLKLKAQLGPDE 49
Cdd:cd00938 1 AKLEEAVKLQGELVRKLKAEKASKEQIAEEVAKLLELKAQLGGDE 45
|
|
| WHEP-TRS |
pfam00458 |
WHEP-TRS domain; |
7-45 |
3.58e-09 |
|
WHEP-TRS domain;
Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 52.50 E-value: 3.58e-09
10 20 30
....*....|....*....|....*....|....*....
gi 194379338 7 LEELVKLQGERVRGLKQQKASAELIEEEVAKLLKLKAQL 45
Cdd:pfam00458 1 LTEKIKAQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQY 39
|
|
| WHEP-TRS |
smart00991 |
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ... |
8-45 |
1.24e-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: 51.19 E-value: 1.24e-08
10 20 30
....*....|....*....|....*....|....*...
gi 194379338 8 EELVKLQGERVRGLKQQKASAELIEEEVAKLLKLKAQL 45
Cdd:smart00991 1 EEAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQL 38
|
|
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
5-66 |
4.17e-03 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 39.73 E-value: 4.17e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 194379338 5 AALEELVKLQGERVRGLKQQKASAELIEEEVAKLLKLKAQLGPDESKQKFVLKTPKETLMGK 66
Cdd:PLN02734 10 AEKQAAVTAQGNAVRALKASKADKAEIDAAIEKLKALKLEKSALEKELQAAVGAGGDGAASK 71
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02972 |
PLN02972 |
Histidyl-tRNA synthetase |
56-461 |
7.72e-176 |
|
Histidyl-tRNA synthetase
Pssm-ID: 215525 [Multi-domain] Cd Length: 763 Bit Score: 511.74 E-value: 7.72e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 56 LKTP----KETLMGKYGEDSKLIYDLKDQGGELLSLRYDLTVPFARYLAMNKLTNIKRYHIAKVYRRDNPamTRGRYREF 131
Cdd:PLN02972 363 LDTPvfelRETLMGKYGEDSKLIYDLADQGGELCSLRYDLTVPFARYVAMNGITSFKRYQIAKVYRRDNP--SKGRYREF 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 132 YQCDFDIAGNFDPMIPDAECLKIMCEILSSLQIGDFLVKVNDRRILDGMFAICGVSDSKFRTICSSVDKLDKVSWEEVKN 211
Cdd:PLN02972 441 YQCDFDIAGVYEPMGPDFEIIKVLTELLDELDIGTYEVKLNHRKLLDGMLEICGVPPEKFRTICSSIDKLDKQSFEQVKK 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 212 EMVGEKGLAPEVADRIGDYVQQHGG-VSLVEQLLQ-DPKLSQNKQALEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLD 289
Cdd:PLN02972 521 EMVEEKGLSNETADKIGNFVKERGPpLELLSKLRQeGSEFLGNASSRAALDELEIMFKALEKSKAIGKIVFDLSLARGLD 600
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 290 YYTGVIYEAVLLQTPaqageeplgVGSVAAGGRYDGLVGMFDpkGRKVPCVGLSIGVERIFSIVEQRLEALEEKIRTTET 369
Cdd:PLN02972 601 YYTGVIYEAVFKGAQ---------VGSIAAGGRYDNLVGMFS--GKQVPAVGVSLGIERVFAIMEQQEEEKSQVIRPTET 669
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 370 QVLVASAQKKLLEERLKLVSELWDAGIKAEllYKKNPKLLNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVDV 449
Cdd:PLN02972 670 EVLVSIIGDDKLALAAELVSELWNAGIKAE--YKVSTRKAKHLKRAKESGIPWMVLVGEKELSKGFVKLKNLEAGVEEEV 747
|
410
....*....|..
gi 194379338 450 RREDLVEEIKRR 461
Cdd:PLN02972 748 DRTCFVQELKAE 759
|
|
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
61-461 |
3.66e-99 |
|
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: 303.97 E-value: 3.66e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 61 ETLMGKYGED--SKLIYDLKDQGGELLSLRYDLTVPFARYLAMNKLTN---IKRYHIAKVYRRDNPAmtRGRYREFYQCD 135
Cdd:COG0124 49 ELFARKIGEDivEKEMYTFEDRGGRSLTLRPEGTAPVARAVAEHGNELpfpFKLYYIGPVFRYERPQ--KGRYRQFHQFG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 136 FDIAGNFDPMIpDAECLKIMCEILSSLQIGDFLVKVNDRrildgmfaicGVSDSKFRTICSSVDKLDKVSWEEVknemvg 215
Cdd:COG0124 127 VEVIGSDSPLA-DAEVIALAADLLKALGLKDFTLEINSR----------GLPEERAEALLRYLDKLDKIGHEDV------ 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 216 ekgLAPEVADRI------------GDYVQqhggvSLVEQLlqdPKLSQNKqALEGLGDLKLLFEYLTLFGIDdkISFDLS 283
Cdd:COG0124 190 ---LDEDSQRRLetnplraildskGPDCQ-----EVLADA---PKLLDYL-GEEGLAHFEEVLELLDALGIP--YVIDPR 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 284 LARGLDYYTGVIYEAVLLQTPAQageeplgvGSVAAGGRYDGLVGMFDpkGRKVPCVGLSIGVERIFSIVEQRLEALEEK 363
Cdd:COG0124 256 LVRGLDYYTGTVFEIVTDGLGAQ--------GSVCGGGRYDGLVEQLG--GPPTPAVGFAIGLERLLLLLEELGLLPAAE 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 364 irtTETQVLVASAQKKLLEERLKLVSELWDAGIKAEL-LYKKNPKllNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVT 442
Cdd:COG0124 326 ---PPPDVYVVPLGEEARAEALKLAQELRAAGIRVELdLGGRKLK--KQLKYADKSGAPFVLILGEDELANGTVTLKDLA 400
|
410
....*....|....*....
gi 194379338 443 SREEVDVRREDLVEEIKRR 461
Cdd:COG0124 401 TGEQETVPLDELVEYLKEL 419
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
56-354 |
6.12e-89 |
|
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: 271.78 E-value: 6.12e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 56 LKTP----KETLMGKYGED-SKLIYDLKDQGGELLSLRYDLTVPFARYLAMNKL---TNIKRYHIAKVYRRDNPAmtRGR 127
Cdd:cd00773 24 IDTPvfeyTELFLRKSGDEvSKEMYRFKDKGGRDLALRPDLTAPVARAVAENLLslpLPLKLYYIGPVFRYERPQ--KGR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 128 YREFYQCDFDIAGnFDPMIPDAECLKIMCEILSSLQIGDFLVKVNDRRILDGmfaICGVSDSKFRTICSSVDKLDKvswe 207
Cdd:cd00773 102 YREFYQVGVEIIG-SDSPLADAEVIALAVEILEALGLKDFQIKINHRGILDG---IAGLLEDREEYIERLIDKLDK---- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 208 evknemvgekglapevadrigdyvqqhggvslveqllqdpklsqnkqalEGLGDLKLLFEYLTLFGIDDKISFDLSLARG 287
Cdd:cd00773 174 -------------------------------------------------EALAHLEKLLDYLEALGVDIKYSIDLSLVRG 204
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 194379338 288 LDYYTGVIYEAVLLQTPAQageeplgvGSVAAGGRYDGLVGMFDpkGRKVPCVGLSIGVERIFSIVE 354
Cdd:cd00773 205 LDYYTGIVFEAVADGLGAQ--------GSIAGGGRYDGLLEEFG--GEDVPAVGFAIGLERLLLALE 261
|
|
| hisS |
TIGR00442 |
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ... |
56-449 |
4.51e-85 |
|
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: 267.04 E-value: 4.51e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 56 LKTP----KETLMGKYGEDS----KLIYDLKDQGGELLSLRYDLTVPFARYLAMNKLTN---IKRYHIAKVYRRDNPAmt 124
Cdd:TIGR00442 36 IRTPifeyTELFKRKVGEETdivsKEMYTFKDKGGRSLTLRPEGTAPVARAVIENKLLLpkpFKLYYIGPMFRYERPQ-- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 125 RGRYREFYQCDFDIAGNFDPMIpDAECLKIMCEILSSLQIGDFLVKVNDRRILDGMFAicgvsdsKFRTICSSVDK-LDK 203
Cdd:TIGR00442 114 KGRYRQFHQFGVEVIGSDSPLA-DAEIIALAADILKELGLKDFTLEINSLGILEGRLE-------YREALIRYLDKhKDK 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 204 VSWEEVKNEMVGEKGLAPEVADRIGDYVQQhggvslveqllqDPKLSQNKQAlEGLGDLKLLFEYLTLFGIddKISFDLS 283
Cdd:TIGR00442 186 LGEDSVRRLEKNPLRILDSKNEKIQELLKN------------APKILDFLCE-ESRAHFEELKELLDALGI--PYKIDPS 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 284 LARGLDYYTGVIYEAVLLQTPAQageeplgvGSVAAGGRYDGLVGMFDpkGRKVPCVGLSIGVERIFSIVEQRLEALEEK 363
Cdd:TIGR00442 251 LVRGLDYYTGTVFEFVTDDLGAQ--------GSICGGGRYDGLVEELG--GPPTPAVGFAIGIERLILLLEELGLIPPPS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 364 irtTETQVLVASAQKKLLEERLKLVSELWDAGIKAElLYKKNPKLLNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTS 443
Cdd:TIGR00442 321 ---KKPDVYVVPLGEEAELEALKLAQKLRKAGIRVE-VDLGGRKLKKQLKYADKLGARFALIIGEDELENGTVTLKDLET 396
|
....*.
gi 194379338 444 REEVDV 449
Cdd:TIGR00442 397 GEQETV 402
|
|
| PRK12420 |
PRK12420 |
histidyl-tRNA synthetase; Provisional |
61-449 |
9.55e-71 |
|
histidyl-tRNA synthetase; Provisional
Pssm-ID: 237097 [Multi-domain] Cd Length: 423 Bit Score: 230.39 E-value: 9.55e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 61 ETLMGKYG---EDSKLIYDLKDQGGELLSLRYDLTVPFARYLAMNKltNI----KRYHIAKVYrRDNPaMTRGRYREFYQ 133
Cdd:PRK12420 49 ELMSSKYGggdEILKEIYTLTDQGKRDLALRYDLTIPFAKVVAMNP--NIrlpfKRYEIGKVF-RDGP-IKQGRFREFIQ 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 134 CDFDIAGNFDPMiPDAECLKIMCEILSSLQIgDFLVKVNDRRILDGMFAICGVSDSKFRTICSSVDKLDKVSWEEVKNEM 213
Cdd:PRK12420 125 CDVDIVGVESVM-AEAELMSMAFELFRRLNL-EVTIQYNNRKLLNGILQAIGIPTELTSDVILSLDKIEKIGIDGVRKDL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 214 VgEKGLAPEVADRIGDYVQQHGGVSLVEqlLQDPKLSQNKQalEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTG 293
Cdd:PRK12420 203 L-ERGISEEMADTICNTVLSCLQLSIAD--FKEAFNNPLVA--EGVNELQQLQQYLIALGINENCIFNPFLARGLTMYTG 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 294 VIYEaVLLQTPAQAgeeplgvGSVAAGGRYDGLVGMFDPKGRKVPCVGLSIGVERIfsiveqrLEALEEKIRTTET-QVL 372
Cdd:PRK12420 278 TVYE-IFLKDGSIT-------SSIGSGGRYDNIIGAFRGDDMNYPTVGISFGLDVI-------YTALSQKETISSTaDVF 342
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 194379338 373 VASAQKKLleERLKLVSELW-DAGIKAELLYkKNPKLLNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVDV 449
Cdd:PRK12420 343 IIPLGTEL--QCLQIAQQLRsTTGLKVELEL-AGRKLKKALNYANKENIPYVLIIGEEEVSTGTVMLRNMKEGSEVKV 417
|
|
| HisZ |
COG3705 |
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism]; |
61-349 |
4.96e-40 |
|
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism];
Pssm-ID: 442919 [Multi-domain] Cd Length: 312 Bit Score: 146.09 E-value: 4.96e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 61 ETLMGKYGEDSKL-IYDLKDQGGELLSLRYDLTVPFARYLAmNKLTNIKR----YHIAKVYRrdNPAMTRGRYREFYQC- 134
Cdd:COG3705 36 DSLLTGSGADLDLqTFKLVDQLGRTLGLRPDMTPQVARIAA-TRLANRPGplrlCYAGNVFR--TRPSGLGRSREFLQAg 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 135 -----DFDIAGnfdpmipDAECLKIMCEILSSLQIGDFLVKVNDRRILDGMFAICGVSDSKFRTICSSVDKLDKVsweEV 209
Cdd:COG3705 113 aeligHAGLEA-------DAEVIALALEALKAAGLEDFTLDLGHVGLFRALLEALGLSEEQREELRRALARKDAV---EL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 210 KnEMVGEKGLAPEVADRIGDYVQQHGGVSLVEQLLqdpKLSQNKQALEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLD 289
Cdd:COG3705 183 E-ELLAELGLSEELAEALLALPELYGGEEVLARAR---ALLLDAAIRAALDELEALAEALAARGPDVRLTFDLSELRGYD 258
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 290 YYTGVIYEAVLlqtpAQAGEEplgvgsVAAGGRYDGLVGMFdpkGRKVPCVGLSIGVERI 349
Cdd:COG3705 259 YYTGIVFEAYA----PGVGDP------LARGGRYDGLLAAF---GRARPATGFSLDLDRL 305
|
|
| PLN02530 |
PLN02530 |
histidine-tRNA ligase |
66-454 |
9.25e-40 |
|
histidine-tRNA ligase
Pssm-ID: 178145 [Multi-domain] Cd Length: 487 Bit Score: 149.51 E-value: 9.25e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 66 KYGED-SKLIYDLKDQGGELLSLRYDLTVPFARyLAMNKLTNI----KRYHIAKVYRRDNpaMTRGRYREFYQCDFDIAG 140
Cdd:PLN02530 120 KAGEEiTDQLYNFEDKGGRRVALRPELTPSLAR-LVLQKGKSLslplKWFAIGQCWRYER--MTRGRRREHYQWNMDIIG 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 141 nFDPMIPDAECLKIMCEILSSLQI--GDFLVKVNDRRILDGMFAICGVSDSKFRTICSSVDKLDKVSWEEVKNEMvGEKG 218
Cdd:PLN02530 197 -VPGVEAEAELLAAIVTFFKRVGItsSDVGIKVSSRKVLQAVLKSYGIPEESFAPVCVIVDKLEKLPREEIEKEL-DTLG 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 219 LAPEVADRIGDyVQQHGGVSLVEQLLqdpklsqnKQALEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEA 298
Cdd:PLN02530 275 VSEEAIEGILD-VLSLKSLDDLEALL--------GADSEAVADLKQLFSLAEAYGYQDWLVFDASVVRGLAYYTGIVFEG 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 299 VllqtpAQAGEeplgVGSVAAGGRYDGLVGMFDpkGRKVPCVGLSIGVERIFSIVEQRlEALEEKIRTTETqvLVASAQK 378
Cdd:PLN02530 346 F-----DRAGK----LRAICGGGRYDRLLSTFG--GEDTPACGFGFGDAVIVELLKEK-GLLPELPHQVDD--VVFALDE 411
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 194379338 379 KLLEERLKLVSELWDAGIKAEL-LYKKNPKLLnqLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVDVRREDL 454
Cdd:PLN02530 412 DLQGAAAGVASRLREKGRSVDLvLEPKKLKWV--FKHAERIGAKRLVLVGASEWERGMVRVKDLSSGEQTEVKLDEL 486
|
|
| hisZ_biosyn_reg |
TIGR00443 |
ATP phosphoribosyltransferase, regulatory subunit; Apparant second copies of histidyl-tRNA ... |
61-349 |
1.65e-37 |
|
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: 139.29 E-value: 1.65e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 61 ETLMGKYGEDSKLIYDLKDQGGELLSLRYDLTVPFARyLAMNKLTNIKR----YHIAKVYRRDNPAmtRGRYREFYQCDF 136
Cdd:TIGR00443 39 DTLSAGSGILNEDLFKLFDQLGRVLGLRPDMTAPIAR-LVSTRLRDRPLplrlCYAGNVFRTNESG--GGRSREFTQAGV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 137 DIAGNfDPMIPDAECLKIMCEILSSLQIGDFLVKVNDRRILDGMFAICGVSDSKFRTICSSVDKLDKVSWEEVknemVGE 216
Cdd:TIGR00443 116 ELIGA-GGPAADAEVIALLIEALKALGLKDFKIELGHVGLVRALLEEAGLPEEAREALREALARKDLVALEEL----VAE 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 217 KGLAPEVADRIGDYVQQHGGVSLVEQLLQdpKLSQNKQALEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIY 296
Cdd:TIGR00443 191 LGLSPEVRERLLALPRLRGDGEEVLEEAR--ALAGSETAEAALDELEAVLELLEARGVEEYISLDLGLVRGYHYYTGLIF 268
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 194379338 297 EAVLLQTPAQageeplgvgsVAAGGRYDGLVGMFdpkGRKVPCVGLSIGVERI 349
Cdd:TIGR00443 269 EGYAPGLGAP----------LAGGGRYDELLGRF---GRPLPATGFALNLERL 308
|
|
| hisZ |
PRK12292 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
61-400 |
6.02e-36 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 237043 [Multi-domain] Cd Length: 391 Bit Score: 136.92 E-value: 6.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 61 ETLM--GKYGEDSKLIYDLKDQGGELLSLRYDLTVPFARyLAMNKLTNIKR----YHIAKVYRrdNPAMTRGRYREFYQC 134
Cdd:PRK12292 48 DTLLagGGAILDLRTFKLVDQLSGRTLGLRPDMTAQIAR-IAATRLANRPGplrlCYAGNVFR--AQERGLGRSREFLQS 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 135 DFDIAGnFDPMIPDAECLKIMCEILSSLQIGDFLVKVNDRRILDGMFAICGVSDSKFRTICSSVDKLDKVSWEEVknemv 214
Cdd:PRK12292 125 GVELIG-DAGLEADAEVILLLLEALKALGLPNFTLDLGHVGLFRALLEAAGLSEELEEVLRRALANKDYVALEEL----- 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 215 gEKGLAPEVADRIGDYVQQHGGVSLVEQLLQdpkLSQNKQALEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGV 294
Cdd:PRK12292 199 -VLDLSEELRDALLALPRLRGGREVLEEARK---LLPSLPIKRALDELEALAEALEKYGYGIPLSLDLGLLRHLDYYTGI 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 295 IYEAVLLQTPAqageeplgvgSVAAGGRYDGLVGMFdpkGRKVPCVGLSIGVERIfsiveqrLEALEEKiRTTETQVLVA 374
Cdd:PRK12292 275 VFEGYVDGVGN----------PIASGGRYDDLLGRF---GRARPATGFSLDLDRL-------LELQLEL-PVEARKDLVI 333
|
330 340
....*....|....*....|....*.
gi 194379338 375 SAQKKLLEERLKLVSELWDAGIKAEL 400
Cdd:PRK12292 334 APDSEALAAALAAAQELRKKGEIVVL 359
|
|
| tRNA-synt_His |
pfam13393 |
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ... |
61-349 |
6.25e-35 |
|
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: 132.32 E-value: 6.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 61 ETLMGKYGEDSKLIYDLKDQGGELLSLRYDLTVPFARYLAmnKLTNIKR----YHIAKVYRRDNPAMtrGRYREFYQCDF 136
Cdd:pfam13393 41 DSLLTGTGADLDQTFKLVDQSGRLLGLRADITPQVARIDA--HRLNRPGplrlCYAGSVLRTRPKGL--GRSREPLQVGA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 137 DIAGNFDPMiPDAECLKIMCEILSSLQIGDFLVKVNDRRILDGMFAICGVSDSKFRTICSSVDKLDkvsWEEVKnEMVGE 216
Cdd:pfam13393 117 ELIGHAGIE-ADAEIISLLLEALAAAGVPGVTLDLGHVGLVRALLEAAGLSEALEEALRAALQRKD---AAELA-ELAAE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 217 KGLAPEVADRIGDYVQQHGGVSLVEQLLQDpkLSQNKQALEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIY 296
Cdd:pfam13393 192 AGLPPALRRALLALPDLYGGPEVLDEARAA--LPGLPALQEALDELEALAALLEALGDGVRLTFDLAELRGYEYYTGIVF 269
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 194379338 297 EAVLlqtpAQAGEEplgvgsVAAGGRYDGLVGMFdpkGRKVPCVGLSIGVERI 349
Cdd:pfam13393 270 AAYA----PGVGEP------LARGGRYDDLGAAF---GRARPATGFSLDLEAL 309
|
|
| HisRS_anticodon |
cd00859 |
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases ... |
368-459 |
1.72e-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: 108.01 E-value: 1.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 368 ETQVLVASAQKKLLEERLKLVSELWDAGIKAELLYKkNPKLLNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEV 447
Cdd:cd00859 1 EVDVYVVPLGEGALSEALELAEQLRDAGIKAEIDYG-GRKLKKQFKYADRSGARFAVILGEDELAAGVVTVKDLETGEQE 79
|
90
....*....|..
gi 194379338 448 DVRREDLVEEIK 459
Cdd:cd00859 80 TVALDELVEELK 91
|
|
| syh |
CHL00201 |
histidine-tRNA synthetase; Provisional |
68-458 |
2.26e-22 |
|
histidine-tRNA synthetase; Provisional
Pssm-ID: 164576 [Multi-domain] Cd Length: 430 Bit Score: 99.20 E-value: 2.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 68 GEDSKLI----YDLKDQGGELLSLRYDLTVPFARYLAMNKLT---NIKR-YHIAKVYRRDNPamTRGRYREFYQCDFDIA 139
Cdd:CHL00201 56 GETTDIVnkemYRFTDRSNRDITLRPEGTAGIVRAFIENKMDyhsNLQRlWYSGPMFRYERP--QSGRQRQFHQLGIEFI 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 140 GNFDPMiPDAECLKIMCEILSSLQIGDFLVKVN------DRRILDgmfaicgvsdSKFRTICSSV-DKLDKVSweevKNE 212
Cdd:CHL00201 134 GSIDAR-ADTEVIHLAMQIFNELQVKNLILDINsigkleDRQSYQ----------LKLVEYLSQYqDDLDTDS----QNR 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 213 MVGEkglaP-EVADRIGDYVQqhggvslvEQLLQDPKLSQ--NKQALEGLGDLkllFEYLTLFGIDDKISFdlSLARGLD 289
Cdd:CHL00201 199 LYSN----PiRILDSKNLKTQ--------EILDGAPKISDflSLESTEHFYDV---CTYLNLLNIPYKINY--KLVRGLD 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 290 YYTGVIYEAVLLQTPAQageeplgvGSVAAGGRYDGLVGMFDpkGRKVPCVGLSIGVERIFSIVEQRLEALEEKIrttet 369
Cdd:CHL00201 262 YYNDTAFEIKTLSSNGQ--------DTICGGGRYDSLIHQLG--GPKTPAVGCAIGLERLLLIAKDNIILPKQSI----- 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 370 QVLVASAQKKLLEERLKLVSELWDAGIKAELLYkKNPKLLNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVDV 449
Cdd:CHL00201 327 DVYIATQGLKAQKKGWEIIQFLEKQNIKFELDL-SSSNFHKQIKQAGKKRAKACIILGDNEIMDNCITIKWLDEQVQENA 405
|
....*....
gi 194379338 450 RREDLVEEI 458
Cdd:CHL00201 406 QYSNFKQEI 414
|
|
| hisZ |
PRK12295 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
59-349 |
1.37e-18 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 183413 [Multi-domain] Cd Length: 373 Bit Score: 87.30 E-value: 1.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 59 PKETLMGKYGED-SKLIYDLKDQGGELLSLRYDLTVPFAR-YLAMNKLTNIKRYHIAKVYRRdnpamTRGRYREFYQCDF 136
Cdd:PRK12295 33 PAEPFLDLSGEDiRRRIFVTSDENGEELCLRPDFTIPVCRrHIATAGGEPARYAYLGEVFRQ-----RRDRASEFLQAGI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 137 DIAGNFDPMIPDAECLKIMCEILSSLQIGDFLVKVNDRRILDGMFAICGVSDS-KFRTIcssVDKLDKVSWEEVKNEMVG 215
Cdd:PRK12295 108 ESFGRADPAAADAEVLALALEALAALGPGDLEVRLGDVGLFAALVDALGLPPGwKRRLL---RHFGRPRSLDALLARLAG 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 216 EKGLAPEVADRIGDYVQQHGGVS-LVEQLLQDPKLSQN------------------------------------------ 252
Cdd:PRK12295 185 PRVDPLDEHAGVLAALADEAAARaLVEDLMSIAGISPVggrspaeiarrllekaalaaaarlpaealavlerflaisgpp 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 253 KQALEGL----GDLKL-------LFE----YLTLFGID-DKISFDLSLARGLDYYTGVIYEAvllqTPAQAGEEPLgvgs 316
Cdd:PRK12295 265 DAALAALralaADAGLdldaaldRFEarlaALAARGIDlERLRFSASFGRPLDYYTGFVFEI----RAAGNGDPPL---- 336
|
330 340 350
....*....|....*....|....*....|...
gi 194379338 317 vAAGGRYDGLVGMFDpKGRKVPCVGLSIGVERI 349
Cdd:PRK12295 337 -AGGGRYDGLLTRLG-AGEPIPAVGFSIWLDRL 367
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
370-461 |
1.85e-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: 77.24 E-value: 1.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 370 QVLVASAQKK---LLEERLKLVSELWDAGIKAELLYKkNPKLLNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREE 446
Cdd:pfam03129 1 QVVVIPLGEKaeeLEEYAQKLAEELRAAGIRVELDDR-NESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQ 79
|
90
....*....|....*
gi 194379338 447 VDVRREDLVEEIKRR 461
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 |
5.51e-17 |
|
HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). This domain consists of a helix- turn- helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238474 [Multi-domain] Cd Length: 45 Bit Score: 74.43 E-value: 5.51e-17
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 194379338 5 AALEELVKLQGERVRGLKQQKASAELIEEEVAKLLKLKAQLGPDE 49
Cdd:cd00938 1 AKLEEAVKLQGELVRKLKAEKASKEQIAEEVAKLLELKAQLGGDE 45
|
|
| WHEPGMRS_RNA |
cd01200 |
EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher ... |
8-49 |
9.73e-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: 53.70 E-value: 9.73e-10
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 194379338 8 EELVKLQGERVRGLKQQKASAELIEEEVAKLLKLKAQLGPDE 49
Cdd:cd01200 1 YEKIAEQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKEAT 42
|
|
| WHEP-TRS |
pfam00458 |
WHEP-TRS domain; |
7-45 |
3.58e-09 |
|
WHEP-TRS domain;
Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 52.50 E-value: 3.58e-09
10 20 30
....*....|....*....|....*....|....*....
gi 194379338 7 LEELVKLQGERVRGLKQQKASAELIEEEVAKLLKLKAQL 45
Cdd:pfam00458 1 LTEKIKAQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQY 39
|
|
| WHEP-TRS |
smart00991 |
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ... |
8-45 |
1.24e-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: 51.19 E-value: 1.24e-08
10 20 30
....*....|....*....|....*....|....*...
gi 194379338 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 ... |
371-461 |
3.19e-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: 3.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 371 VLVASAQKKLL-EERLKLVSELWDAGIKAELLYKKNPKLLNQLQYCEEAGIPLVAIIGEQELKDG----VIKLRSVTSRE 445
Cdd:pfam12745 8 VLVASFDASILrTTGVEILQELWAHGISADLAVDASYSPEDLVSRARDDGVSWIVIIKQQNKSSDskykPLKVKNLLRKE 87
|
90 100
....*....|....*....|
gi 194379338 446 EVDVRREDLV----EEIKRR 461
Cdd:pfam12745 88 DVDLDSDELVswlrGEIRER 107
|
|
| PRK12421 |
PRK12421 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
212-395 |
2.42e-07 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 237098 Cd Length: 392 Bit Score: 52.66 E-value: 2.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 212 EMVGEKGLAPEVADRIGDYVQQHGGVSLVEQLLQDpKLSQNKQALEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYY 291
Cdd:PRK12421 200 EVCQNLGVGSDLRRMFYALARLNGGLEALDRALSV-LALQDAAIRQALDELKTLAAHLKNRWPELPVSIDLAELRGYHYH 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 292 TGVIYeAVLLQTPAQAgeeplgvgsVAAGGRYDGLVGMFdpkGRKVPCVGlsigveriFSIVEQRLEALEEKIRTTETQV 371
Cdd:PRK12421 279 TGLVF-AAYIPGRGQA---------LARGGRYDGIGEAF---GRARPATG--------FSMDLKELLALQFLEEEAGAIL 337
|
170 180
....*....|....*....|....
gi 194379338 372 LVASAQKKLLEErlklVSELWDAG 395
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 |
2.89e-06 |
|
MetRS_RNA binding domain. This short RNA-binding domain is found at the C-terminus of MetRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is repeated in Drosophila MetRS. This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238475 [Multi-domain] Cd Length: 45 Bit Score: 44.00 E-value: 2.89e-06
10 20 30
....*....|....*....|....*....|....*....
gi 194379338 7 LEELVKLQGERVRGLKQQKASAELIEEEVAKLLKLKAQL 45
Cdd:cd00939 1 LEKEVAEQGNKVRKLKASKADKSVWQPEVNKLLDLKKQL 39
|
|
| PRK03991 |
PRK03991 |
threonyl-tRNA synthetase; Validated |
345-465 |
9.33e-06 |
|
threonyl-tRNA synthetase; Validated
Pssm-ID: 235190 [Multi-domain] Cd Length: 613 Bit Score: 47.94 E-value: 9.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 345 GVER-IFSIVE-QRLEALEEKIRT-----TETQVLVASAQKKLLEERLKLVSELWDAGIKAEL------LYKKnpkllnq 411
Cdd:PRK03991 469 SIERvIYALLEkAAKEEEEGKVPMlptwlSPTQVRVIPVSERHLDYAEEVADKLEAAGIRVDVddrdesLGKK------- 541
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 194379338 412 lqyCEEAG---IPLVAIIGEQELKDGVIklrSVTSREE---VDVRREDLVEEIKRRT-GQP 465
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 |
7.75e-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: 40.30 E-value: 7.75e-05
10 20 30
....*....|....*....|....*....|.
gi 194379338 14 QGERVRGLKQQKASAELIEEEVAKLLKLKAQ 44
Cdd:cd00936 8 QGDLVRELKAKKAPKEEIDAAVKKLLALKAD 38
|
|
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
5-66 |
4.17e-03 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 39.73 E-value: 4.17e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 194379338 5 AALEELVKLQGERVRGLKQQKASAELIEEEVAKLLKLKAQLGPDESKQKFVLKTPKETLMGK 66
Cdd:PLN02734 10 AEKQAAVTAQGNAVRALKASKADKAEIDAAIEKLKALKLEKSALEKELQAAVGAGGDGAASK 71
|
|
| ThrRS_anticodon |
cd00860 |
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases ... |
369-459 |
6.64e-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: 35.94 E-value: 6.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 369 TQVLVASAQKKLLEERLKLVSELWDAGIKAELLYKkNPKLLNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVD 448
Cdd:cd00860 2 VQVVVIPVTDEHLDYAKEVAKKLSDAGIRVEVDLR-NEKLGKKIREAQLQKIPYILVVGDKEVETGTVSVRTRDGGDLGS 80
|
90
....*....|.
gi 194379338 449 VRREDLVEEIK 459
Cdd:cd00860 81 MSLDEFIEKLK 91
|
|
| PRK09194 |
PRK09194 |
prolyl-tRNA synthetase; Provisional |
331-460 |
8.86e-03 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 236405 [Multi-domain] Cd Length: 565 Bit Score: 38.53 E-value: 8.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 331 DPKGRKVP----CVGlsIGVERIFS-IVEQRLEaleEK--IRTTET---QV-LVAS-----AQKKLLEerlKLVSELWDA 394
Cdd:PRK09194 426 DENGKAQPlimgCYG--IGVSRLVAaAIEQNHD---EKgiIWPKAIapfDVhIVPVnmkdeEVKELAE---KLYAELQAA 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379338 395 GIK----------------AELLykknpkllnqlqyceeaGIPLVAIIGEQELKDGVIKLRSVTSREEVDVRREDLVEEI 458
Cdd:PRK09194 498 GIEvllddrkerpgvkfadADLI-----------------GIPHRIVVGDRGLAEGIVEYKDRRTGEKEEVPVDELVEFL 560
|
..
gi 194379338 459 KR 460
Cdd:PRK09194 561 KA 562
|
|
| |
