|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02972 |
PLN02972 |
Histidyl-tRNA synthetase |
57-427 |
9.74e-131 |
|
Histidyl-tRNA synthetase
Pssm-ID: 215525 [Multi-domain] Cd Length: 763 Bit Score: 394.64 E-value: 9.74e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 57 KTPKGTRDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELK------------------------------------ 100
Cdd:PLN02972 328 KIPKGTRDFAKEQMAIREKAFSIITSVFKRHGATALDTPVFELRetlmgkygedskliydladqggelcslrydltvpfa 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 101 ------------------------------------DFDIAGNFDPMIPDAECLKIMCEILSSLQIGDFLVKVNDRRILD 144
Cdd:PLN02972 408 ryvamngitsfkryqiakvyrrdnpskgryrefyqcDFDIAGVYEPMGPDFEIIKVLTELLDELDIGTYEVKLNHRKLLD 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 145 GMFAICGVSDSKFRTICSSVDKLDKVSWEEVKNEMVGEKGLAPEVADRIGDYVQQHGG-VSLVEQLLQ-DPKLSQNKQAL 222
Cdd:PLN02972 488 GMLEICGVPPEKFRTICSSIDKLDKQSFEQVKKEMVEEKGLSNETADKIGNFVKERGPpLELLSKLRQeGSEFLGNASSR 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 223 EGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLLQTPaqageeplgVGSVAAGGRYDGLVGMFDpkGRK 302
Cdd:PLN02972 568 AALDELEIMFKALEKSKAIGKIVFDLSLARGLDYYTGVIYEAVFKGAQ---------VGSIAAGGRYDNLVGMFS--GKQ 636
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 303 VPCVGLSIGVERIFSIVEQRLEALEEKIRTTETQVLVASAQKKLLEERLKLVSELWDAGIKAEllYKKNPKLLNQLQYCE 382
Cdd:PLN02972 637 VPAVGVSLGIERVFAIMEQQEEEKSQVIRPTETEVLVSIIGDDKLALAAELVSELWNAGIKAE--YKVSTRKAKHLKRAK 714
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 574278766 383 EAGIPLVAIIGEQELKDGVIKLRSVTSREEVDVRREDLVEEIKRR 427
Cdd:PLN02972 715 ESGIPWMVLVGEKELSKGFVKLKNLEAGVEEEVDRTCFVQELKAE 759
|
|
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
56-427 |
3.80e-68 |
|
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: 222.69 E-value: 3.80e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 56 LKTPKGTRDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFE------------------------------------- 98
Cdd:COG0124 4 IQAPRGTRDILPEESAKWQYVEDTIREVFERYGFQEIRTPIFEytelfarkigedivekemytfedrggrsltlrpegta 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 99 ----------------LK------------------------DFDIAGNFDPMIpDAECLKIMCEILSSLQIGDFLVKVN 138
Cdd:COG0124 84 pvaravaehgnelpfpFKlyyigpvfryerpqkgryrqfhqfGVEVIGSDSPLA-DAEVIALAADLLKALGLKDFTLEIN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 139 DRrildgmfaicGVSDSKFRTICSSVDKLDKVSWEEVknemvgekgLAPEVADRI------------GDYVQqhggvSLV 206
Cdd:COG0124 163 SR----------GLPEERAEALLRYLDKLDKIGHEDV---------LDEDSQRRLetnplraildskGPDCQ-----EVL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 207 EQLlqdPKLSQNKqALEGLGDLKLLFEYLTLFGIDdkISFDLSLARGLDYYTGVIYEAVLLQTPAQageeplgvGSVAAG 286
Cdd:COG0124 219 ADA---PKLLDYL-GEEGLAHFEEVLELLDALGIP--YVIDPRLVRGLDYYTGTVFEIVTDGLGAQ--------GSVCGG 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 287 GRYDGLVGMFDpkGRKVPCVGLSIGVERIFSIVEQRLEALEEKirtTETQVLVASAQKKLLEERLKLVSELWDAGIKAEL 366
Cdd:COG0124 285 GRYDGLVEQLG--GPPTPAVGFAIGLERLLLLLEELGLLPAAE---PPPDVYVVPLGEEARAEALKLAQELRAAGIRVEL 359
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 574278766 367 -LYKKNPKllNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVDVRREDLVEEIKRR 427
Cdd:COG0124 360 dLGGRKLK--KQLKYADKSGAPFVLILGEDELANGTVTLKDLATGEQETVPLDELVEYLKEL 419
|
|
| hisS |
TIGR00442 |
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ... |
57-415 |
5.21e-57 |
|
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: 193.08 E-value: 5.21e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 57 KTPKGTRDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFE-------------------------------------- 98
Cdd:TIGR00442 1 QKPRGTRDFLPEEMIKWQYIEETIREVFERYGFKEIRTPIFEytelfkrkvgeetdivskemytfkdkggrsltlrpegt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 99 -----------------LK------------------------DFDIAGNFDPMIpDAECLKIMCEILSSLQIGDFLVKV 137
Cdd:TIGR00442 81 apvaravienklllpkpFKlyyigpmfryerpqkgryrqfhqfGVEVIGSDSPLA-DAEIIALAADILKELGLKDFTLEI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 138 NDRRILDGMFAicgvsdsKFRTICSSVDK-LDKVSWEEVKNEMVGEKGLAPEVADRIGDYVQQhggvslveqllqDPKLS 216
Cdd:TIGR00442 160 NSLGILEGRLE-------YREALIRYLDKhKDKLGEDSVRRLEKNPLRILDSKNEKIQELLKN------------APKIL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 217 QNKQAlEGLGDLKLLFEYLTLFGIddKISFDLSLARGLDYYTGVIYEAVLLQTPAQageeplgvGSVAAGGRYDGLVGMF 296
Cdd:TIGR00442 221 DFLCE-ESRAHFEELKELLDALGI--PYKIDPSLVRGLDYYTGTVFEFVTDDLGAQ--------GSICGGGRYDGLVEEL 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 297 DpkGRKVPCVGLSIGVERIFSIVEQRLEALEEKirtTETQVLVASAQKKLLEERLKLVSELWDAGIKAElLYKKNPKLLN 376
Cdd:TIGR00442 290 G--GPPTPAVGFAIGIERLILLLEELGLIPPPS---KKPDVYVVPLGEEAELEALKLAQKLRKAGIRVE-VDLGGRKLKK 363
|
410 420 430
....*....|....*....|....*....|....*....
gi 574278766 377 QLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVDV 415
Cdd:TIGR00442 364 QLKYADKLGARFALIIGEDELENGTVTLKDLETGEQETV 402
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
69-320 |
2.27e-51 |
|
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: 173.94 E-value: 2.27e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 69 QMAVREKVFDVIIRCFKRHGAEVIDTPVFELKD----------------------------------------------- 101
Cdd:cd00773 1 EAALRRYIEDTLREVFERYGYEEIDTPVFEYTElflrksgdevskemyrfkdkggrdlalrpdltapvaravaenllslp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 102 -----------------------------FDIAGnFDPMIPDAECLKIMCEILSSLQIGDFLVKVNDRRILDGmfaICGV 152
Cdd:cd00773 81 lplklyyigpvfryerpqkgryrefyqvgVEIIG-SDSPLADAEVIALAVEILEALGLKDFQIKINHRGILDG---IAGL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 153 SDSKFRTICSSVDKLDKvsweevknemvgekglapevadrigdyvqqhggvslveqllqdpklsqnkqalEGLGDLKLLF 232
Cdd:cd00773 157 LEDREEYIERLIDKLDK-----------------------------------------------------EALAHLEKLL 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 233 EYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLLQTPAQageeplgvGSVAAGGRYDGLVGMFDpkGRKVPCVGLSIGV 312
Cdd:cd00773 184 DYLEALGVDIKYSIDLSLVRGLDYYTGIVFEAVADGLGAQ--------GSIAGGGRYDGLLEEFG--GEDVPAVGFAIGL 253
|
....*...
gi 574278766 313 ERIFSIVE 320
Cdd:cd00773 254 ERLLLALE 261
|
|
| tRNA-synt_His |
pfam13393 |
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ... |
114-315 |
4.83e-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: 104.20 E-value: 4.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 114 DAECLKIMCEILSSLQIGDFLVKVNDRRILDGMFAICGVSDSKFRTICSSVDKLDkvsWEEVKnEMVGEKGLAPEVADRI 193
Cdd:pfam13393 127 DAEIISLLLEALAAAGVPGVTLDLGHVGLVRALLEAAGLSEALEEALRAALQRKD---AAELA-ELAAEAGLPPALRRAL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 194 GDYVQQHGGVSLVEQLLQDpkLSQNKQALEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLlqtpAQA 273
Cdd:pfam13393 203 LALPDLYGGPEVLDEARAA--LPGLPALQEALDELEALAALLEALGDGVRLTFDLAELRGYEYYTGIVFAAYA----PGV 276
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 574278766 274 GEEplgvgsVAAGGRYDGLVGMFdpkGRKVPCVGLSIGVERI 315
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 |
1.27e-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: 73.27 E-value: 1.27e-16
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 574278766 5 AALEELVKLQGERVRGLKQQKASAELIEEEVAKLLKLKAQLGPDE 49
Cdd:cd00938 1 AKLEEAVKLQGELVRKLKAEKASKEQIAEEVAKLLELKAQLGGDE 45
|
|
| WHEP-TRS |
pfam00458 |
WHEP-TRS domain; |
7-45 |
4.32e-09 |
|
WHEP-TRS domain;
Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 52.11 E-value: 4.32e-09
10 20 30
....*....|....*....|....*....|....*....
gi 574278766 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 |
1.84e-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: 1.84e-08
10 20 30
....*....|....*....|....*....|....*...
gi 574278766 8 EELVKLQGERVRGLKQQKASAELIEEEVAKLLKLKAQL 45
Cdd:smart00991 1 EEAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQL 38
|
|
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
5-88 |
9.52e-04 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 41.65 E-value: 9.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 5 AALEELVKLQGERVRGLKQQKASAELIEEEVAKLLKLKAQLgpdESKQKFVLKTPKGTRDYSPRQMAVREKVFDVIIR-- 82
Cdd:PLN02734 10 AEKQAAVTAQGNAVRALKASKADKAEIDAAIEKLKALKLEK---SALEKELQAAVGAGGDGAASKEAFRQAVVNTLERrl 86
|
90
....*....|
gi 574278766 83 ----CFKRHG 88
Cdd:PLN02734 87 fyipSFKIYG 96
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02972 |
PLN02972 |
Histidyl-tRNA synthetase |
57-427 |
9.74e-131 |
|
Histidyl-tRNA synthetase
Pssm-ID: 215525 [Multi-domain] Cd Length: 763 Bit Score: 394.64 E-value: 9.74e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 57 KTPKGTRDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELK------------------------------------ 100
Cdd:PLN02972 328 KIPKGTRDFAKEQMAIREKAFSIITSVFKRHGATALDTPVFELRetlmgkygedskliydladqggelcslrydltvpfa 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 101 ------------------------------------DFDIAGNFDPMIPDAECLKIMCEILSSLQIGDFLVKVNDRRILD 144
Cdd:PLN02972 408 ryvamngitsfkryqiakvyrrdnpskgryrefyqcDFDIAGVYEPMGPDFEIIKVLTELLDELDIGTYEVKLNHRKLLD 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 145 GMFAICGVSDSKFRTICSSVDKLDKVSWEEVKNEMVGEKGLAPEVADRIGDYVQQHGG-VSLVEQLLQ-DPKLSQNKQAL 222
Cdd:PLN02972 488 GMLEICGVPPEKFRTICSSIDKLDKQSFEQVKKEMVEEKGLSNETADKIGNFVKERGPpLELLSKLRQeGSEFLGNASSR 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 223 EGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLLQTPaqageeplgVGSVAAGGRYDGLVGMFDpkGRK 302
Cdd:PLN02972 568 AALDELEIMFKALEKSKAIGKIVFDLSLARGLDYYTGVIYEAVFKGAQ---------VGSIAAGGRYDNLVGMFS--GKQ 636
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 303 VPCVGLSIGVERIFSIVEQRLEALEEKIRTTETQVLVASAQKKLLEERLKLVSELWDAGIKAEllYKKNPKLLNQLQYCE 382
Cdd:PLN02972 637 VPAVGVSLGIERVFAIMEQQEEEKSQVIRPTETEVLVSIIGDDKLALAAELVSELWNAGIKAE--YKVSTRKAKHLKRAK 714
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 574278766 383 EAGIPLVAIIGEQELKDGVIKLRSVTSREEVDVRREDLVEEIKRR 427
Cdd:PLN02972 715 ESGIPWMVLVGEKELSKGFVKLKNLEAGVEEEVDRTCFVQELKAE 759
|
|
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
56-427 |
3.80e-68 |
|
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: 222.69 E-value: 3.80e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 56 LKTPKGTRDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFE------------------------------------- 98
Cdd:COG0124 4 IQAPRGTRDILPEESAKWQYVEDTIREVFERYGFQEIRTPIFEytelfarkigedivekemytfedrggrsltlrpegta 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 99 ----------------LK------------------------DFDIAGNFDPMIpDAECLKIMCEILSSLQIGDFLVKVN 138
Cdd:COG0124 84 pvaravaehgnelpfpFKlyyigpvfryerpqkgryrqfhqfGVEVIGSDSPLA-DAEVIALAADLLKALGLKDFTLEIN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 139 DRrildgmfaicGVSDSKFRTICSSVDKLDKVSWEEVknemvgekgLAPEVADRI------------GDYVQqhggvSLV 206
Cdd:COG0124 163 SR----------GLPEERAEALLRYLDKLDKIGHEDV---------LDEDSQRRLetnplraildskGPDCQ-----EVL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 207 EQLlqdPKLSQNKqALEGLGDLKLLFEYLTLFGIDdkISFDLSLARGLDYYTGVIYEAVLLQTPAQageeplgvGSVAAG 286
Cdd:COG0124 219 ADA---PKLLDYL-GEEGLAHFEEVLELLDALGIP--YVIDPRLVRGLDYYTGTVFEIVTDGLGAQ--------GSVCGG 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 287 GRYDGLVGMFDpkGRKVPCVGLSIGVERIFSIVEQRLEALEEKirtTETQVLVASAQKKLLEERLKLVSELWDAGIKAEL 366
Cdd:COG0124 285 GRYDGLVEQLG--GPPTPAVGFAIGLERLLLLLEELGLLPAAE---PPPDVYVVPLGEEARAEALKLAQELRAAGIRVEL 359
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 574278766 367 -LYKKNPKllNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVDVRREDLVEEIKRR 427
Cdd:COG0124 360 dLGGRKLK--KQLKYADKSGAPFVLILGEDELANGTVTLKDLATGEQETVPLDELVEYLKEL 419
|
|
| hisS |
TIGR00442 |
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ... |
57-415 |
5.21e-57 |
|
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: 193.08 E-value: 5.21e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 57 KTPKGTRDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFE-------------------------------------- 98
Cdd:TIGR00442 1 QKPRGTRDFLPEEMIKWQYIEETIREVFERYGFKEIRTPIFEytelfkrkvgeetdivskemytfkdkggrsltlrpegt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 99 -----------------LK------------------------DFDIAGNFDPMIpDAECLKIMCEILSSLQIGDFLVKV 137
Cdd:TIGR00442 81 apvaravienklllpkpFKlyyigpmfryerpqkgryrqfhqfGVEVIGSDSPLA-DAEIIALAADILKELGLKDFTLEI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 138 NDRRILDGMFAicgvsdsKFRTICSSVDK-LDKVSWEEVKNEMVGEKGLAPEVADRIGDYVQQhggvslveqllqDPKLS 216
Cdd:TIGR00442 160 NSLGILEGRLE-------YREALIRYLDKhKDKLGEDSVRRLEKNPLRILDSKNEKIQELLKN------------APKIL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 217 QNKQAlEGLGDLKLLFEYLTLFGIddKISFDLSLARGLDYYTGVIYEAVLLQTPAQageeplgvGSVAAGGRYDGLVGMF 296
Cdd:TIGR00442 221 DFLCE-ESRAHFEELKELLDALGI--PYKIDPSLVRGLDYYTGTVFEFVTDDLGAQ--------GSICGGGRYDGLVEEL 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 297 DpkGRKVPCVGLSIGVERIFSIVEQRLEALEEKirtTETQVLVASAQKKLLEERLKLVSELWDAGIKAElLYKKNPKLLN 376
Cdd:TIGR00442 290 G--GPPTPAVGFAIGIERLILLLEELGLIPPPS---KKPDVYVVPLGEEAELEALKLAQKLRKAGIRVE-VDLGGRKLKK 363
|
410 420 430
....*....|....*....|....*....|....*....
gi 574278766 377 QLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVDV 415
Cdd:TIGR00442 364 QLKYADKLGARFALIIGEDELENGTVTLKDLETGEQETV 402
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
69-320 |
2.27e-51 |
|
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: 173.94 E-value: 2.27e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 69 QMAVREKVFDVIIRCFKRHGAEVIDTPVFELKD----------------------------------------------- 101
Cdd:cd00773 1 EAALRRYIEDTLREVFERYGYEEIDTPVFEYTElflrksgdevskemyrfkdkggrdlalrpdltapvaravaenllslp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 102 -----------------------------FDIAGnFDPMIPDAECLKIMCEILSSLQIGDFLVKVNDRRILDGmfaICGV 152
Cdd:cd00773 81 lplklyyigpvfryerpqkgryrefyqvgVEIIG-SDSPLADAEVIALAVEILEALGLKDFQIKINHRGILDG---IAGL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 153 SDSKFRTICSSVDKLDKvsweevknemvgekglapevadrigdyvqqhggvslveqllqdpklsqnkqalEGLGDLKLLF 232
Cdd:cd00773 157 LEDREEYIERLIDKLDK-----------------------------------------------------EALAHLEKLL 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 233 EYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLLQTPAQageeplgvGSVAAGGRYDGLVGMFDpkGRKVPCVGLSIGV 312
Cdd:cd00773 184 DYLEALGVDIKYSIDLSLVRGLDYYTGIVFEAVADGLGAQ--------GSIAGGGRYDGLLEEFG--GEDVPAVGFAIGL 253
|
....*...
gi 574278766 313 ERIFSIVE 320
Cdd:cd00773 254 ERLLLALE 261
|
|
| PRK12420 |
PRK12420 |
histidyl-tRNA synthetase; Provisional |
84-415 |
4.91e-42 |
|
histidyl-tRNA synthetase; Provisional
Pssm-ID: 237097 [Multi-domain] Cd Length: 423 Bit Score: 153.73 E-value: 4.91e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 84 FKRH--GAEVIDTPV-------FELKDFDIAGNFDPMiPDAECLKIMCEILSSLQIgDFLVKVNDRRILDGMFAICGVSD 154
Cdd:PRK12420 100 FKRYeiGKVFRDGPIkqgrfreFIQCDVDIVGVESVM-AEAELMSMAFELFRRLNL-EVTIQYNNRKLLNGILQAIGIPT 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 155 SKFRTICSSVDKLDKVSWEEVKNEMVgEKGLAPEVADRIGDYVQQHGGVSLVEQllqdPKLSQNKQALEGLGDLKLLFEY 234
Cdd:PRK12420 178 ELTSDVILSLDKIEKIGIDGVRKDLL-ERGISEEMADTICNTVLSCLQLSIADF----KEAFNNPLVAEGVNELQQLQQY 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 235 LTLFGIDDKISFDLSLARGLDYYTGVIYEaVLLQTPAQAgeeplgvGSVAAGGRYDGLVGMFDPKGRKVPCVGLSIGVER 314
Cdd:PRK12420 253 LIALGINENCIFNPFLARGLTMYTGTVYE-IFLKDGSIT-------SSIGSGGRYDNIIGAFRGDDMNYPTVGISFGLDV 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 315 IfsiveqrLEALEEKIRTTET-QVLVASAQKKLleERLKLVSELW-DAGIKAELLYkKNPKLLNQLQYCEEAGIPLVAII 392
Cdd:PRK12420 325 I-------YTALSQKETISSTaDVFIIPLGTEL--QCLQIAQQLRsTTGLKVELEL-AGRKLKKALNYANKENIPYVLII 394
|
330 340
....*....|....*....|...
gi 574278766 393 GEQELKDGVIKLRSVTSREEVDV 415
Cdd:PRK12420 395 GEEEVSTGTVMLRNMKEGSEVKV 417
|
|
| PLN02530 |
PLN02530 |
histidine-tRNA ligase |
47-420 |
1.59e-28 |
|
histidine-tRNA ligase
Pssm-ID: 178145 [Multi-domain] Cd Length: 487 Bit Score: 117.15 E-value: 1.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 47 PDESKQKFVLKTPKGTRDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKDFDI--AG--------NFD------- 109
Cdd:PLN02530 61 QEDGKPKIDVNPPKGTRDFPPEDMRLRNWLFDHFREVSRLFGFEEVDAPVLESEELYIrkAGeeitdqlyNFEdkggrrv 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 110 ----PMIP------------------------------------------------------DAECLKIMCEILSSLQI- 130
Cdd:PLN02530 141 alrpELTPslarlvlqkgkslslplkwfaigqcwryermtrgrrrehyqwnmdiigvpgveaEAELLAAIVTFFKRVGIt 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 131 -GDFLVKVNDRRILDGMFAICGVSDSKFRTICSSVDKLDKVSWEEVKNEMvGEKGLAPEVADRIGDyVQQHGGVSLVEQL 209
Cdd:PLN02530 221 sSDVGIKVSSRKVLQAVLKSYGIPEESFAPVCVIVDKLEKLPREEIEKEL-DTLGVSEEAIEGILD-VLSLKSLDDLEAL 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 210 LqdpklsqnKQALEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVllqtpAQAGEeplgVGSVAAGGRY 289
Cdd:PLN02530 299 L--------GADSEAVADLKQLFSLAEAYGYQDWLVFDASVVRGLAYYTGIVFEGF-----DRAGK----LRAICGGGRY 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 290 DGLVGMFDpkGRKVPCVGLSIGVERIFSIVEQRlEALEEKIRTTETqvLVASAQKKLLEERLKLVSELWDAGIKAEL-LY 368
Cdd:PLN02530 362 DRLLSTFG--GEDTPACGFGFGDAVIVELLKEK-GLLPELPHQVDD--VVFALDEDLQGAAAGVASRLREKGRSVDLvLE 436
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 574278766 369 KKNPKLLnqLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVDVRREDL 420
Cdd:PLN02530 437 PKKLKWV--FKHAERIGAKRLVLVGASEWERGMVRVKDLSSGEQTEVKLDEL 486
|
|
| HisZ |
COG3705 |
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism]; |
114-315 |
1.77e-28 |
|
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism];
Pssm-ID: 442919 [Multi-domain] Cd Length: 312 Bit Score: 114.12 E-value: 1.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 114 DAECLKIMCEILSSLQIGDFLVKVNDRRILDGMFAICGVSDSKFRTICSSVDKLDKVsweEVKnEMVGEKGLAPEVADRI 193
Cdd:COG3705 124 DAEVIALALEALKAAGLEDFTLDLGHVGLFRALLEALGLSEEQREELRRALARKDAV---ELE-ELLAELGLSEELAEAL 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 194 GDYVQQHGGVSLVEQLLqdpKLSQNKQALEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLlqtpAQA 273
Cdd:COG3705 200 LALPELYGGEEVLARAR---ALLLDAAIRAALDELEALAEALAARGPDVRLTFDLSELRGYDYYTGIVFEAYA----PGV 272
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 574278766 274 GEEplgvgsVAAGGRYDGLVGMFdpkGRKVPCVGLSIGVERI 315
Cdd:COG3705 273 GDP------LARGGRYDGLLAAF---GRARPATGFSLDLDRL 305
|
|
| hisZ_biosyn_reg |
TIGR00443 |
ATP phosphoribosyltransferase, regulatory subunit; Apparant second copies of histidyl-tRNA ... |
63-315 |
2.53e-28 |
|
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: 113.48 E-value: 2.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 63 RDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKDFDIAGN----------FDP----------MIP--------- 113
Cdd:TIGR00443 1 RDLLPEEAARKEEIERQLQDVFRSWGYQEIITPTLEYLDTLSAGSgilnedlfklFDQlgrvlglrpdMTApiarlvstr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 114 ---------------------------------------------DAECLKIMCEILSSLQIGDFLVKVNDRRILDGMFA 148
Cdd:TIGR00443 81 lrdrplplrlcyagnvfrtnesgggrsreftqagveligaggpaaDAEVIALLIEALKALGLKDFKIELGHVGLVRALLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 149 ICGVSDSKFRTICSSVDKLDKVSWEEVknemVGEKGLAPEVADRIGDYVQQHGGVSLVEQLLQdpKLSQNKQALEGLGDL 228
Cdd:TIGR00443 161 EAGLPEEAREALREALARKDLVALEEL----VAELGLSPEVRERLLALPRLRGDGEEVLEEAR--ALAGSETAEAALDEL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 229 KLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLLQTPAQageeplgvgsVAAGGRYDGLVGMFdpkGRKVPCVGL 308
Cdd:TIGR00443 235 EAVLELLEARGVEEYISLDLGLVRGYHYYTGLIFEGYAPGLGAP----------LAGGGRYDELLGRF---GRPLPATGF 301
|
....*..
gi 574278766 309 SIGVERI 315
Cdd:TIGR00443 302 ALNLERL 308
|
|
| HisRS_anticodon |
cd00859 |
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases ... |
334-425 |
3.11e-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: 3.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 334 ETQVLVASAQKKLLEERLKLVSELWDAGIKAELLYKkNPKLLNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEV 413
Cdd:cd00859 1 EVDVYVVPLGEGALSEALELAEQLRDAGIKAEIDYG-GRKLKKQFKYADRSGARFAVILGEDELAAGVVTVKDLETGEQE 79
|
90
....*....|..
gi 574278766 414 DVRREDLVEEIK 425
Cdd:cd00859 80 TVALDELVEELK 91
|
|
| hisZ |
PRK12292 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
113-366 |
1.07e-27 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 237043 [Multi-domain] Cd Length: 391 Bit Score: 113.42 E-value: 1.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 113 PDAECLKIMCEILSSLQIGDFLVKVNDRRILDGMFAICGVSDSKFRTICSSVDKLDKVSWEEVknemvgEKGLAPEVADR 192
Cdd:PRK12292 136 ADAEVILLLLEALKALGLPNFTLDLGHVGLFRALLEAAGLSEELEEVLRRALANKDYVALEEL------VLDLSEELRDA 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 193 IGDYVQQHGGVSLVEQLLQdpkLSQNKQALEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLLQTPAq 272
Cdd:PRK12292 210 LLALPRLRGGREVLEEARK---LLPSLPIKRALDELEALAEALEKYGYGIPLSLDLGLLRHLDYYTGIVFEGYVDGVGN- 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 273 ageeplgvgSVAAGGRYDGLVGMFdpkGRKVPCVGLSIGVERIfsiveqrLEALEEKiRTTETQVLVASAQKKLLEERLK 352
Cdd:PRK12292 286 ---------PIASGGRYDDLLGRF---GRARPATGFSLDLDRL-------LELQLEL-PVEARKDLVIAPDSEALAAALA 345
|
250
....*....|....
gi 574278766 353 LVSELWDAGIKAEL 366
Cdd:PRK12292 346 AAQELRKKGEIVVL 359
|
|
| tRNA-synt_His |
pfam13393 |
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ... |
114-315 |
4.83e-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: 104.20 E-value: 4.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 114 DAECLKIMCEILSSLQIGDFLVKVNDRRILDGMFAICGVSDSKFRTICSSVDKLDkvsWEEVKnEMVGEKGLAPEVADRI 193
Cdd:pfam13393 127 DAEIISLLLEALAAAGVPGVTLDLGHVGLVRALLEAAGLSEALEEALRAALQRKD---AAELA-ELAAEAGLPPALRRAL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 194 GDYVQQHGGVSLVEQLLQDpkLSQNKQALEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLlqtpAQA 273
Cdd:pfam13393 203 LALPDLYGGPEVLDEARAA--LPGLPALQEALDELEALAALLEALGDGVRLTFDLAELRGYEYYTGIVFAAYA----PGV 276
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 574278766 274 GEEplgvgsVAAGGRYDGLVGMFdpkGRKVPCVGLSIGVERI 315
Cdd:pfam13393 277 GEP------LARGGRYDDLGAAF---GRARPATGFSLDLEAL 309
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
336-427 |
4.44e-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: 4.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 336 QVLVASAQKK---LLEERLKLVSELWDAGIKAELLYKkNPKLLNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREE 412
Cdd:pfam03129 1 QVVVIPLGEKaeeLEEYAQKLAEELRAAGIRVELDDR-NESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQ 79
|
90
....*....|....*
gi 574278766 413 VDVRREDLVEEIKRR 427
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 |
1.27e-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: 73.27 E-value: 1.27e-16
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 574278766 5 AALEELVKLQGERVRGLKQQKASAELIEEEVAKLLKLKAQLGPDE 49
Cdd:cd00938 1 AKLEEAVKLQGELVRKLKAEKASKEQIAEEVAKLLELKAQLGGDE 45
|
|
| syh |
CHL00201 |
histidine-tRNA synthetase; Provisional |
106-424 |
4.20e-14 |
|
histidine-tRNA synthetase; Provisional
Pssm-ID: 164576 [Multi-domain] Cd Length: 430 Bit Score: 73.78 E-value: 4.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 106 GNFDPMiPDAECLKIMCEILSSLQIGDFLVKVN------DRRILDgmfaicgvsdSKFRTICSSV-DKLDKVSweevKNE 178
Cdd:CHL00201 134 GSIDAR-ADTEVIHLAMQIFNELQVKNLILDINsigkleDRQSYQ----------LKLVEYLSQYqDDLDTDS----QNR 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 179 MVGEkglaP-EVADRIGDYVQqhggvslvEQLLQDPKLSQ--NKQALEGLGDLkllFEYLTLFGIDDKISFdlSLARGLD 255
Cdd:CHL00201 199 LYSN----PiRILDSKNLKTQ--------EILDGAPKISDflSLESTEHFYDV---CTYLNLLNIPYKINY--KLVRGLD 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 256 YYTGVIYEAVLLQTPAQageeplgvGSVAAGGRYDGLVGMFDpkGRKVPCVGLSIGVERIFSIVEQRLEALEEKIrttet 335
Cdd:CHL00201 262 YYNDTAFEIKTLSSNGQ--------DTICGGGRYDSLIHQLG--GPKTPAVGCAIGLERLLLIAKDNIILPKQSI----- 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 336 QVLVASAQKKLLEERLKLVSELWDAGIKAELLYkKNPKLLNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVDV 415
Cdd:CHL00201 327 DVYIATQGLKAQKKGWEIIQFLEKQNIKFELDL-SSSNFHKQIKQAGKKRAKACIILGDNEIMDNCITIKWLDEQVQENA 405
|
....*....
gi 574278766 416 RREDLVEEI 424
Cdd:CHL00201 406 QYSNFKQEI 414
|
|
| hisZ |
PRK12295 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
239-315 |
4.63e-11 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 183413 [Multi-domain] Cd Length: 373 Bit Score: 64.18 E-value: 4.63e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 574278766 239 GID-DKISFDLSLARGLDYYTGVIYEAvllqTPAQAGEEPLgvgsvAAGGRYDGLVGMFDpKGRKVPCVGLSIGVERI 315
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 |
1.31e-09 |
|
EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in three copies in the mammalian bifunctional EPRS in a region that separates the N-terminal GluRS from the C-terminal ProRS. In the Drosophila EPRS, this domain is repeated six times. It is found at the N-terminus of TrpRS, HisRS and GlyR and at the C-terminus of MetRS. This domain consists of a helix- turn- helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238605 [Multi-domain] Cd Length: 42 Bit Score: 53.31 E-value: 1.31e-09
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 574278766 8 EELVKLQGERVRGLKQQKASAELIEEEVAKLLKLKAQLGPDE 49
Cdd:cd01200 1 YEKIAEQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKEAT 42
|
|
| WHEP-TRS |
pfam00458 |
WHEP-TRS domain; |
7-45 |
4.32e-09 |
|
WHEP-TRS domain;
Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 52.11 E-value: 4.32e-09
10 20 30
....*....|....*....|....*....|....*....
gi 574278766 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 |
1.84e-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: 1.84e-08
10 20 30
....*....|....*....|....*....|....*...
gi 574278766 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 ... |
337-427 |
3.58e-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: 3.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 337 VLVASAQKKLL-EERLKLVSELWDAGIKAELLYKKNPKLLNQLQYCEEAGIPLVAIIGEQEL----KDGVIKLRSVTSRE 411
Cdd:pfam12745 8 VLVASFDASILrTTGVEILQELWAHGISADLAVDASYSPEDLVSRARDDGVSWIVIIKQQNKssdsKYKPLKVKNLLRKE 87
|
90 100
....*....|....*....|
gi 574278766 412 EVDVRREDLV----EEIKRR 427
Cdd:pfam12745 88 DVDLDSDELVswlrGEIRER 107
|
|
| PRK12421 |
PRK12421 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
178-361 |
1.98e-07 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 237098 Cd Length: 392 Bit Score: 52.66 E-value: 1.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 178 EMVGEKGLAPEVADRIGDYVQQHGGVSLVEQLLQDpKLSQNKQALEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYY 257
Cdd:PRK12421 200 EVCQNLGVGSDLRRMFYALARLNGGLEALDRALSV-LALQDAAIRQALDELKTLAAHLKNRWPELPVSIDLAELRGYHYH 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 258 TGVIYeAVLLQTPAQAgeeplgvgsVAAGGRYDGLVGMFdpkGRKVPCVGlsigveriFSIVEQRLEALEEKIRTTETQV 337
Cdd:PRK12421 279 TGLVF-AAYIPGRGQA---------LARGGRYDGIGEAF---GRARPATG--------FSMDLKELLALQFLEEEAGAIL 337
|
170 180
....*....|....*....|....
gi 574278766 338 LVASAQKKLLEErlklVSELWDAG 361
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 |
4.01e-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: 43.62 E-value: 4.01e-06
10 20 30
....*....|....*....|....*....|....*....
gi 574278766 7 LEELVKLQGERVRGLKQQKASAELIEEEVAKLLKLKAQL 45
Cdd:cd00939 1 LEKEVAEQGNKVRKLKASKADKSVWQPEVNKLLDLKKQL 39
|
|
| PRK03991 |
PRK03991 |
threonyl-tRNA synthetase; Validated |
311-431 |
9.13e-06 |
|
threonyl-tRNA synthetase; Validated
Pssm-ID: 235190 [Multi-domain] Cd Length: 613 Bit Score: 47.94 E-value: 9.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 311 GVER-IFSIVE-QRLEALEEKIRT-----TETQVLVASAQKKLLEERLKLVSELWDAGIKAEL------LYKKnpkllnq 377
Cdd:PRK03991 469 SIERvIYALLEkAAKEEEEGKVPMlptwlSPTQVRVIPVSERHLDYAEEVADKLEAAGIRVDVddrdesLGKK------- 541
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 574278766 378 lqyCEEAG---IPLVAIIGEQELKDGVIklrSVTSREE---VDVRREDLVEEIKRRT-GQP 431
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 |
7.32e-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: 7.32e-05
10 20 30
....*....|....*....|....*....|.
gi 574278766 14 QGERVRGLKQQKASAELIEEEVAKLLKLKAQ 44
Cdd:cd00936 8 QGDLVRELKAKKAPKEEIDAAVKKLLALKAD 38
|
|
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
5-88 |
9.52e-04 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 41.65 E-value: 9.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 5 AALEELVKLQGERVRGLKQQKASAELIEEEVAKLLKLKAQLgpdESKQKFVLKTPKGTRDYSPRQMAVREKVFDVIIR-- 82
Cdd:PLN02734 10 AEKQAAVTAQGNAVRALKASKADKAEIDAAIEKLKALKLEK---SALEKELQAAVGAGGDGAASKEAFRQAVVNTLERrl 86
|
90
....*....|
gi 574278766 83 ----CFKRHG 88
Cdd:PLN02734 87 fyipSFKIYG 96
|
|
| ThrRS_anticodon |
cd00860 |
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases ... |
335-425 |
9.21e-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: 35.17 E-value: 9.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 335 TQVLVASAQKKLLEERLKLVSELWDAGIKAELLYKkNPKLLNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVD 414
Cdd:cd00860 2 VQVVVIPVTDEHLDYAKEVAKKLSDAGIRVEVDLR-NEKLGKKIREAQLQKIPYILVVGDKEVETGTVSVRTRDGGDLGS 80
|
90
....*....|.
gi 574278766 415 VRREDLVEEIK 425
Cdd:cd00860 81 MSLDEFIEKLK 91
|
|
| PRK09194 |
PRK09194 |
prolyl-tRNA synthetase; Provisional |
297-426 |
9.70e-03 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 236405 [Multi-domain] Cd Length: 565 Bit Score: 38.14 E-value: 9.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 297 DPKGRKVP----CVGlsIGVERIFS-IVEQRLEaleEK--IRTTET---QV-LVAS-----AQKKLLEerlKLVSELWDA 360
Cdd:PRK09194 426 DENGKAQPlimgCYG--IGVSRLVAaAIEQNHD---EKgiIWPKAIapfDVhIVPVnmkdeEVKELAE---KLYAELQAA 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574278766 361 GIK----------------AELLykknpkllnqlqyceeaGIPLVAIIGEQELKDGVIKLRSVTSREEVDVRREDLVEEI 424
Cdd:PRK09194 498 GIEvllddrkerpgvkfadADLI-----------------GIPHRIVVGDRGLAEGIVEYKDRRTGEKEEVPVDELVEFL 560
|
..
gi 574278766 425 KR 426
Cdd:PRK09194 561 KA 562
|
|
| |
