|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02972 |
PLN02972 |
Histidyl-tRNA synthetase |
89-559 |
1.63e-174 |
|
Histidyl-tRNA synthetase
Pssm-ID: 215525 [Multi-domain] Cd Length: 763 Bit Score: 512.12 E-value: 1.63e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 89 KTPKGTKDWCDKDVVLREHIFSTVTEIFKRHGGVTLDTPVFELKEILSGKYGEDSKLIYDLKDQGGELCSLRYDLTVPFA 168
Cdd:PLN02972 328 KIPKGTRDFAKEQMAIREKAFSIITSVFKRHGATALDTPVFELRETLMGKYGEDSKLIYDLADQGGELCSLRYDLTVPFA 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 169 RWLAMNpKVTSIKRFHIAKVYRRDQPamTKGRMREFYQCDFDIAGNYDPMIPDSEALKVLVEALDALEVGNYTIKLNHRK 248
Cdd:PLN02972 408 RYVAMN-GITSFKRYQIAKVYRRDNP--SKGRYREFYQCDFDIAGVYEPMGPDFEIIKVLTELLDELDIGTYEVKLNHRK 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 249 ILDGIFTVCGVPDDKIRTISSAVDKLDKLPWEDVRREMVVEKGLKEEVADKIKEYVLLKGD-RSLLDKLEA-DSLLSSNS 326
Cdd:PLN02972 485 LLDGMLEICGVPPEKFRTICSSIDKLDKQSFEQVKKEMVEEKGLSNETADKIGNFVKERGPpLELLSKLRQeGSEFLGNA 564
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 327 SAVAAFNDMRLLFDYLEAFGVLDRFSFDMSLARGLDYYTGIIYEAVTEASApkikssaekkksadpeadrsnddsigVGS 406
Cdd:PLN02972 565 SSRAALDELEIMFKALEKSKAIGKIVFDLSLARGLDYYTGVIYEAVFKGAQ--------------------------VGS 618
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 407 IAAGGRYDNLVGMFAAKknaKIPCVGISLGLERIFSIL--RSKIPDEDIRANDVDVFVMAFGGGKewtgfLKERMSVCKD 484
Cdd:PLN02972 619 IAAGGRYDNLVGMFSGK---QVPAVGVSLGIERVFAIMeqQEEEKSQVIRPTETEVLVSIIGDDK-----LALAAELVSE 690
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 429240963 485 LWANGIKAEflYKVKPKPRQQFDAADKFDVPFAVILGQDEFAKGSVRIKQMGLKENSDEGQLVPREEMVSVLKKL 559
Cdd:PLN02972 691 LWNAGIKAE--YKVSTRKAKHLKRAKESGIPWMVLVGEKELSKGFVKLKNLEAGVEEEVDRTCFVQELKAELLKL 763
|
|
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
87-561 |
1.70e-105 |
|
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: 323.23 E-value: 1.70e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 87 TLKTPKGTKDWCDKDVVLREHIFSTVTEIFKRHGGVTLDTPVFELKEILSGKYGED--SKLIYDLKDQGGELCSLRYDLT 164
Cdd:COG0124 3 KIQAPRGTRDILPEESAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKIGEDivEKEMYTFEDRGGRSLTLRPEGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 165 VPFARWLAMN----PKVtsIKRFHIAKVYRRDQPAmtKGRMREFYQCDFDIAGNYDPMIpDSEALKVLVEALDALEVGNY 240
Cdd:COG0124 83 APVARAVAEHgnelPFP--FKLYYIGPVFRYERPQ--KGRYRQFHQFGVEVIGSDSPLA-DAEVIALAADLLKALGLKDF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 241 TIKLNHRkildgiftvcGVPDDKIRTISSAVDKLDKLPWEDVrremvvekgLKEEVADKIKEYVLL-----KGD------ 309
Cdd:COG0124 158 TLEINSR----------GLPEERAEALLRYLDKLDKIGHEDV---------LDEDSQRRLETNPLRaildsKGPdcqevl 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 310 ---RSLLDKLEADSLlssnssavaafNDMRLLFDYLEAFGVldRFSFDMSLARGLDYYTGIIYEAVTEasapkikssaek 386
Cdd:COG0124 219 adaPKLLDYLGEEGL-----------AHFEEVLELLDALGI--PYVIDPRLVRGLDYYTGTVFEIVTD------------ 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 387 kksaDPEADrsnddsigvGSIAAGGRYDNLVGMFAAKknaKIPCVGISLGLERIFSILRSKiPDEDIRANDVDVFVMAFG 466
Cdd:COG0124 274 ----GLGAQ---------GSVCGGGRYDGLVEQLGGP---PTPAVGFAIGLERLLLLLEEL-GLLPAAEPPPDVYVVPLG 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 467 GgkewtGFLKERMSVCKDLWANGIKAEFLYKVKpKPRQQFDAADKFDVPFAVILGQDEFAKGSVRIKQMglkeNSDEGQL 546
Cdd:COG0124 337 E-----EARAEALKLAQELRAAGIRVELDLGGR-KLKKQLKYADKSGAPFVLILGEDELANGTVTLKDL----ATGEQET 406
|
490
....*....|....*
gi 429240963 547 VPREEMVSVLKKLLK 561
Cdd:COG0124 407 VPLDELVEYLKELLA 421
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
101-444 |
1.13e-99 |
|
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: 302.60 E-value: 1.13e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 101 DVVLREHIFSTVTEIFKRHGGVTLDTPVFELKEILSGKYGED-SKLIYDLKDQGGELCSLRYDLTVPFARWLAMNPK--V 177
Cdd:cd00773 1 EAALRRYIEDTLREVFERYGYEEIDTPVFEYTELFLRKSGDEvSKEMYRFKDKGGRDLALRPDLTAPVARAVAENLLslP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 178 TSIKRFHIAKVYRRDQPAmtKGRMREFYQCDFDIAGnYDPMIPDSEALKVLVEALDALEVGNYTIKLNHRKILDGIftvC 257
Cdd:cd00773 81 LPLKLYYIGPVFRYERPQ--KGRYREFYQVGVEIIG-SDSPLADAEVIALAVEILEALGLKDFQIKINHRGILDGI---A 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 258 GVPDDKIRTISSAVDKLDKlpwedvrremvvekglkeevadkikeyvllkgdrslldkleadsllssnssavAAFNDMRL 337
Cdd:cd00773 155 GLLEDREEYIERLIDKLDK-----------------------------------------------------EALAHLEK 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 338 LFDYLEAFGVLDRFSFDMSLARGLDYYTGIIYEAVTeasapkikssaekkksadpeadrsnDDSIGVGSIAAGGRYDNLV 417
Cdd:cd00773 182 LLDYLEALGVDIKYSIDLSLVRGLDYYTGIVFEAVA-------------------------DGLGAQGSIAGGGRYDGLL 236
|
330 340
....*....|....*....|....*..
gi 429240963 418 GMFAAKknaKIPCVGISLGLERIFSIL 444
Cdd:cd00773 237 EEFGGE---DVPAVGFAIGLERLLLAL 260
|
|
| hisS |
TIGR00442 |
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ... |
89-535 |
1.94e-98 |
|
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: 304.40 E-value: 1.94e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 89 KTPKGTKDWCDKDVVLREHIFSTVTEIFKRHGGVTLDTPVFELKEILSGKYGEDS----KLIYDLKDQGGELCSLRYDLT 164
Cdd:TIGR00442 1 QKPRGTRDFLPEEMIKWQYIEETIREVFERYGFKEIRTPIFEYTELFKRKVGEETdivsKEMYTFKDKGGRSLTLRPEGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 165 VPFARWLAMNPKVTS--IKRFHIAKVYRRDQPAmtKGRMREFYQCDFDIAGNYDPMIpDSEALKVLVEALDALEVGNYTI 242
Cdd:TIGR00442 81 APVARAVIENKLLLPkpFKLYYIGPMFRYERPQ--KGRYRQFHQFGVEVIGSDSPLA-DAEIIALAADILKELGLKDFTL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 243 KLNHRKILDGIFtvcgvpdDKIRTISSAVDK-LDKLPWEDVRREMVVEKGLKEEVADKIKEyvLLKGDRSLLDKLEADSL 321
Cdd:TIGR00442 158 EINSLGILEGRL-------EYREALIRYLDKhKDKLGEDSVRRLEKNPLRILDSKNEKIQE--LLKNAPKILDFLCEESR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 322 lssnssavaafNDMRLLFDYLEAFGVldRFSFDMSLARGLDYYTGIIYEAVTeasapkikssaekkksadpeadrsndDS 401
Cdd:TIGR00442 229 -----------AHFEELKELLDALGI--PYKIDPSLVRGLDYYTGTVFEFVT--------------------------DD 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 402 IGV-GSIAAGGRYDNLVGMFaakKNAKIPCVGISLGLERIFSILRSKiPDEDIRANDVDVFVMAFGggkewTGFLKERMS 480
Cdd:TIGR00442 270 LGAqGSICGGGRYDGLVEEL---GGPPTPAVGFAIGIERLILLLEEL-GLIPPPSKKPDVYVVPLG-----EEAELEALK 340
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 429240963 481 VCKDLWANGIKAEFLYKVKpKPRQQFDAADKFDVPFAVILGQDEFAKGSVRIKQM 535
Cdd:TIGR00442 341 LAQKLRKAGIRVEVDLGGR-KLKKQLKYADKLGARFALIIGEDELENGTVTLKDL 394
|
|
| tRNA-synt_His |
pfam13393 |
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ... |
105-440 |
1.18e-41 |
|
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: 151.97 E-value: 1.18e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 105 REHIFSTVTEIFKRHG--GVTLdtPVFELKEILSGKYGEDSKLIYDLKDQGGELCSLRYDLTVPFARWLAMNPKVTSIKR 182
Cdd:pfam13393 13 IEELRRRLLDLFRSWGyeLVMP--PLLEYLDSLLTGTGADLDQTFKLVDQSGRLLGLRADITPQVARIDAHRLNRPGPLR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 183 FH-IAKVYRRDQPAMtkGRMREFYQCDFDIAGNYDPMiPDSEALKVLVEALDALEVGNYTIKLNHRKILDGIFTVCGVPD 261
Cdd:pfam13393 91 LCyAGSVLRTRPKGL--GRSREPLQVGAELIGHAGIE-ADAEIISLLLEALAAAGVPGVTLDLGHVGLVRALLEAAGLSE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 262 DKIRTISSAVDKLDklpWEDVRrEMVVEKGLKEEVADKIKEYVLLKGDRSLLDKLEAdsLLSSNSSAVAAFNDMRLLFDY 341
Cdd:pfam13393 168 ALEEALRAALQRKD---AAELA-ELAAEAGLPPALRRALLALPDLYGGPEVLDEARA--ALPGLPALQEALDELEALAAL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 342 LEAFGVLDRFSFDMSLARGLDYYTGIIYEAVTEasapkikssaekkksadpeadrsnddsiGVGS-IAAGGRYDNLVGMF 420
Cdd:pfam13393 242 LEALGDGVRLTFDLAELRGYEYYTGIVFAAYAP----------------------------GVGEpLARGGRYDDLGAAF 293
|
330 340
....*....|....*....|
gi 429240963 421 aakkNAKIPCVGISLGLERI 440
Cdd:pfam13393 294 ----GRARPATGFSLDLEAL 309
|
|
| WHEP-TRS |
pfam00458 |
WHEP-TRS domain; |
33-62 |
2.46e-08 |
|
WHEP-TRS domain;
Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 50.19 E-value: 2.46e-08
10 20 30
....*....|....*....|....*....|
gi 429240963 33 INERITSQGNLVRSLKSQGASKEDIDKEVA 62
Cdd:pfam00458 1 LTEKIKAQGDLVRKLKAEKAPKEEIDAAVK 30
|
|
| WHEP-TRS |
smart00991 |
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ... |
34-62 |
9.64e-07 |
|
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: 45.80 E-value: 9.64e-07
10 20
....*....|....*....|....*....
gi 429240963 34 NERITSQGNLVRSLKSQGASKEDIDKEVA 62
Cdd:smart00991 1 EEAVAAQGELVRKLKAEKASKDEIDAAVA 29
|
|
| WHEPGMRS_RNA |
cd01200 |
EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher ... |
34-63 |
1.28e-06 |
|
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: 45.22 E-value: 1.28e-06
10 20 30
....*....|....*....|....*....|
gi 429240963 34 NERITSQGNLVRSLKSQGASKEDIDKEVAK 63
Cdd:cd01200 1 YEKIAEQGDLVRKLKAEKAPKEEIDAAVKK 30
|
|
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
25-62 |
1.46e-03 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 41.65 E-value: 1.46e-03
10 20 30
....*....|....*....|....*....|....*...
gi 429240963 25 TMADSLVDINERITSQGNLVRSLKSQGASKEDIDKEVA 62
Cdd:PLN02734 4 SLRDALAEKQAAVTAQGNAVRALKASKADKAEIDAAIE 41
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02972 |
PLN02972 |
Histidyl-tRNA synthetase |
89-559 |
1.63e-174 |
|
Histidyl-tRNA synthetase
Pssm-ID: 215525 [Multi-domain] Cd Length: 763 Bit Score: 512.12 E-value: 1.63e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 89 KTPKGTKDWCDKDVVLREHIFSTVTEIFKRHGGVTLDTPVFELKEILSGKYGEDSKLIYDLKDQGGELCSLRYDLTVPFA 168
Cdd:PLN02972 328 KIPKGTRDFAKEQMAIREKAFSIITSVFKRHGATALDTPVFELRETLMGKYGEDSKLIYDLADQGGELCSLRYDLTVPFA 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 169 RWLAMNpKVTSIKRFHIAKVYRRDQPamTKGRMREFYQCDFDIAGNYDPMIPDSEALKVLVEALDALEVGNYTIKLNHRK 248
Cdd:PLN02972 408 RYVAMN-GITSFKRYQIAKVYRRDNP--SKGRYREFYQCDFDIAGVYEPMGPDFEIIKVLTELLDELDIGTYEVKLNHRK 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 249 ILDGIFTVCGVPDDKIRTISSAVDKLDKLPWEDVRREMVVEKGLKEEVADKIKEYVLLKGD-RSLLDKLEA-DSLLSSNS 326
Cdd:PLN02972 485 LLDGMLEICGVPPEKFRTICSSIDKLDKQSFEQVKKEMVEEKGLSNETADKIGNFVKERGPpLELLSKLRQeGSEFLGNA 564
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 327 SAVAAFNDMRLLFDYLEAFGVLDRFSFDMSLARGLDYYTGIIYEAVTEASApkikssaekkksadpeadrsnddsigVGS 406
Cdd:PLN02972 565 SSRAALDELEIMFKALEKSKAIGKIVFDLSLARGLDYYTGVIYEAVFKGAQ--------------------------VGS 618
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 407 IAAGGRYDNLVGMFAAKknaKIPCVGISLGLERIFSIL--RSKIPDEDIRANDVDVFVMAFGGGKewtgfLKERMSVCKD 484
Cdd:PLN02972 619 IAAGGRYDNLVGMFSGK---QVPAVGVSLGIERVFAIMeqQEEEKSQVIRPTETEVLVSIIGDDK-----LALAAELVSE 690
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 429240963 485 LWANGIKAEflYKVKPKPRQQFDAADKFDVPFAVILGQDEFAKGSVRIKQMGLKENSDEGQLVPREEMVSVLKKL 559
Cdd:PLN02972 691 LWNAGIKAE--YKVSTRKAKHLKRAKESGIPWMVLVGEKELSKGFVKLKNLEAGVEEEVDRTCFVQELKAELLKL 763
|
|
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
87-561 |
1.70e-105 |
|
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: 323.23 E-value: 1.70e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 87 TLKTPKGTKDWCDKDVVLREHIFSTVTEIFKRHGGVTLDTPVFELKEILSGKYGED--SKLIYDLKDQGGELCSLRYDLT 164
Cdd:COG0124 3 KIQAPRGTRDILPEESAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKIGEDivEKEMYTFEDRGGRSLTLRPEGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 165 VPFARWLAMN----PKVtsIKRFHIAKVYRRDQPAmtKGRMREFYQCDFDIAGNYDPMIpDSEALKVLVEALDALEVGNY 240
Cdd:COG0124 83 APVARAVAEHgnelPFP--FKLYYIGPVFRYERPQ--KGRYRQFHQFGVEVIGSDSPLA-DAEVIALAADLLKALGLKDF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 241 TIKLNHRkildgiftvcGVPDDKIRTISSAVDKLDKLPWEDVrremvvekgLKEEVADKIKEYVLL-----KGD------ 309
Cdd:COG0124 158 TLEINSR----------GLPEERAEALLRYLDKLDKIGHEDV---------LDEDSQRRLETNPLRaildsKGPdcqevl 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 310 ---RSLLDKLEADSLlssnssavaafNDMRLLFDYLEAFGVldRFSFDMSLARGLDYYTGIIYEAVTEasapkikssaek 386
Cdd:COG0124 219 adaPKLLDYLGEEGL-----------AHFEEVLELLDALGI--PYVIDPRLVRGLDYYTGTVFEIVTD------------ 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 387 kksaDPEADrsnddsigvGSIAAGGRYDNLVGMFAAKknaKIPCVGISLGLERIFSILRSKiPDEDIRANDVDVFVMAFG 466
Cdd:COG0124 274 ----GLGAQ---------GSVCGGGRYDGLVEQLGGP---PTPAVGFAIGLERLLLLLEEL-GLLPAAEPPPDVYVVPLG 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 467 GgkewtGFLKERMSVCKDLWANGIKAEFLYKVKpKPRQQFDAADKFDVPFAVILGQDEFAKGSVRIKQMglkeNSDEGQL 546
Cdd:COG0124 337 E-----EARAEALKLAQELRAAGIRVELDLGGR-KLKKQLKYADKSGAPFVLILGEDELANGTVTLKDL----ATGEQET 406
|
490
....*....|....*
gi 429240963 547 VPREEMVSVLKKLLK 561
Cdd:COG0124 407 VPLDELVEYLKELLA 421
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
101-444 |
1.13e-99 |
|
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: 302.60 E-value: 1.13e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 101 DVVLREHIFSTVTEIFKRHGGVTLDTPVFELKEILSGKYGED-SKLIYDLKDQGGELCSLRYDLTVPFARWLAMNPK--V 177
Cdd:cd00773 1 EAALRRYIEDTLREVFERYGYEEIDTPVFEYTELFLRKSGDEvSKEMYRFKDKGGRDLALRPDLTAPVARAVAENLLslP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 178 TSIKRFHIAKVYRRDQPAmtKGRMREFYQCDFDIAGnYDPMIPDSEALKVLVEALDALEVGNYTIKLNHRKILDGIftvC 257
Cdd:cd00773 81 LPLKLYYIGPVFRYERPQ--KGRYREFYQVGVEIIG-SDSPLADAEVIALAVEILEALGLKDFQIKINHRGILDGI---A 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 258 GVPDDKIRTISSAVDKLDKlpwedvrremvvekglkeevadkikeyvllkgdrslldkleadsllssnssavAAFNDMRL 337
Cdd:cd00773 155 GLLEDREEYIERLIDKLDK-----------------------------------------------------EALAHLEK 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 338 LFDYLEAFGVLDRFSFDMSLARGLDYYTGIIYEAVTeasapkikssaekkksadpeadrsnDDSIGVGSIAAGGRYDNLV 417
Cdd:cd00773 182 LLDYLEALGVDIKYSIDLSLVRGLDYYTGIVFEAVA-------------------------DGLGAQGSIAGGGRYDGLL 236
|
330 340
....*....|....*....|....*..
gi 429240963 418 GMFAAKknaKIPCVGISLGLERIFSIL 444
Cdd:cd00773 237 EEFGGE---DVPAVGFAIGLERLLLAL 260
|
|
| hisS |
TIGR00442 |
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ... |
89-535 |
1.94e-98 |
|
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: 304.40 E-value: 1.94e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 89 KTPKGTKDWCDKDVVLREHIFSTVTEIFKRHGGVTLDTPVFELKEILSGKYGEDS----KLIYDLKDQGGELCSLRYDLT 164
Cdd:TIGR00442 1 QKPRGTRDFLPEEMIKWQYIEETIREVFERYGFKEIRTPIFEYTELFKRKVGEETdivsKEMYTFKDKGGRSLTLRPEGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 165 VPFARWLAMNPKVTS--IKRFHIAKVYRRDQPAmtKGRMREFYQCDFDIAGNYDPMIpDSEALKVLVEALDALEVGNYTI 242
Cdd:TIGR00442 81 APVARAVIENKLLLPkpFKLYYIGPMFRYERPQ--KGRYRQFHQFGVEVIGSDSPLA-DAEIIALAADILKELGLKDFTL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 243 KLNHRKILDGIFtvcgvpdDKIRTISSAVDK-LDKLPWEDVRREMVVEKGLKEEVADKIKEyvLLKGDRSLLDKLEADSL 321
Cdd:TIGR00442 158 EINSLGILEGRL-------EYREALIRYLDKhKDKLGEDSVRRLEKNPLRILDSKNEKIQE--LLKNAPKILDFLCEESR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 322 lssnssavaafNDMRLLFDYLEAFGVldRFSFDMSLARGLDYYTGIIYEAVTeasapkikssaekkksadpeadrsndDS 401
Cdd:TIGR00442 229 -----------AHFEELKELLDALGI--PYKIDPSLVRGLDYYTGTVFEFVT--------------------------DD 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 402 IGV-GSIAAGGRYDNLVGMFaakKNAKIPCVGISLGLERIFSILRSKiPDEDIRANDVDVFVMAFGggkewTGFLKERMS 480
Cdd:TIGR00442 270 LGAqGSICGGGRYDGLVEEL---GGPPTPAVGFAIGIERLILLLEEL-GLIPPPSKKPDVYVVPLG-----EEAELEALK 340
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 429240963 481 VCKDLWANGIKAEFLYKVKpKPRQQFDAADKFDVPFAVILGQDEFAKGSVRIKQM 535
Cdd:TIGR00442 341 LAQKLRKAGIRVEVDLGGR-KLKKQLKYADKLGARFALIIGEDELENGTVTLKDL 394
|
|
| PRK12420 |
PRK12420 |
histidyl-tRNA synthetase; Provisional |
88-535 |
2.29e-82 |
|
histidyl-tRNA synthetase; Provisional
Pssm-ID: 237097 [Multi-domain] Cd Length: 423 Bit Score: 263.52 E-value: 2.29e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 88 LKTPKGTKDWCDKDVVLREHIFSTVTEIFKRHGGVTLDTPVFELKEILSGKYG---EDSKLIYDLKDQGGELCSLRYDLT 164
Cdd:PRK12420 4 MRNVKGTKDYLPEEQVLRNKIKRALEDVFERYGCKPLETPTLNMYELMSSKYGggdEILKEIYTLTDQGKRDLALRYDLT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 165 VPFARWLAMNPKVT-SIKRFHIAKVYrRDQPaMTKGRMREFYQCDFDIAGNYDPMiPDSEALKVLVEALDALEVgNYTIK 243
Cdd:PRK12420 84 IPFAKVVAMNPNIRlPFKRYEIGKVF-RDGP-IKQGRFREFIQCDVDIVGVESVM-AEAELMSMAFELFRRLNL-EVTIQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 244 LNHRKILDGIFTVCGVPDDKIRTISSAVDKLDKLPWEDVRREmVVEKGLKEEVADKIKEYVLLKGDRSLLDKLEAdsllS 323
Cdd:PRK12420 160 YNNRKLLNGILQAIGIPTELTSDVILSLDKIEKIGIDGVRKD-LLERGISEEMADTICNTVLSCLQLSIADFKEA----F 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 324 SNSSAVAAFNDMRLLFDYLEAFGVLDRFSFDMSLARGLDYYTGIIYEAVteasapkikssaekkksadpEADRSNDDSIG 403
Cdd:PRK12420 235 NNPLVAEGVNELQQLQQYLIALGINENCIFNPFLARGLTMYTGTVYEIF--------------------LKDGSITSSIG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 404 vgsiaAGGRYDNLVGMFAAkKNAKIPCVGISLGLERIFSILRskipDEDIRANDVDVFVMAFGGGKEwtgflkERMSVCK 483
Cdd:PRK12420 295 -----SGGRYDNIIGAFRG-DDMNYPTVGISFGLDVIYTALS----QKETISSTADVFIIPLGTELQ------CLQIAQQ 358
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 429240963 484 DLWANGIKAEFLYKVKpKPRQQFDAADKFDVPFAVILGQDEFAKGSVRIKQM 535
Cdd:PRK12420 359 LRSTTGLKVELELAGR-KLKKALNYANKENIPYVLIIGEEEVSTGTVMLRNM 409
|
|
| PLN02530 |
PLN02530 |
histidine-tRNA ligase |
91-542 |
1.17e-53 |
|
histidine-tRNA ligase
Pssm-ID: 178145 [Multi-domain] Cd Length: 487 Bit Score: 189.57 E-value: 1.17e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 91 PKGTKDWCDKDVVLREHIFSTVTEIFKRHGGVTLDTPVFELKEILSGKYGED-SKLIYDLKDQGGELCSLRYDLTVPFAR 169
Cdd:PLN02530 73 PKGTRDFPPEDMRLRNWLFDHFREVSRLFGFEEVDAPVLESEELYIRKAGEEiTDQLYNFEDKGGRRVALRPELTPSLAR 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 170 WLAMNPKVTSI--KRFHIAKVYRRDQpaMTKGRMREFYQCDFDIAGnydpmIPDSEALKVLVEA---------LDALEVG 238
Cdd:PLN02530 153 LVLQKGKSLSLplKWFAIGQCWRYER--MTRGRRREHYQWNMDIIG-----VPGVEAEAELLAAivtffkrvgITSSDVG 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 239 nytIKLNHRKILDGIFTVCGVPDDKIRTISSAVDKLDKLPWEDVRREMVvEKGLKEEVADKIKEYVLLKGdrslLDKLEA 318
Cdd:PLN02530 226 ---IKVSSRKVLQAVLKSYGIPEESFAPVCVIVDKLEKLPREEIEKELD-TLGVSEEAIEGILDVLSLKS----LDDLEA 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 319 dsLLSSNSSAVAafnDMRLLFDYLEAFGVLDRFSFDMSLARGLDYYTGIIYEAVteasapkikssaekkksadpeaDRSN 398
Cdd:PLN02530 298 --LLGADSEAVA---DLKQLFSLAEAYGYQDWLVFDASVVRGLAYYTGIVFEGF----------------------DRAG 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 399 DdsigVGSIAAGGRYDNLVGMFAAKknaKIPCVGISLGLERIFSILRSK--IPDEdirANDVDVFVMAFGGGKEWTGflk 476
Cdd:PLN02530 351 K----LRAICGGGRYDRLLSTFGGE---DTPACGFGFGDAVIVELLKEKglLPEL---PHQVDDVVFALDEDLQGAA--- 417
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 429240963 477 erMSVCKDLWANGIKAEFLYKVKpKPRQQFDAADKFDVPFAVILGQDEFAKGSVRIKQMGLKENSD 542
Cdd:PLN02530 418 --AGVASRLREKGRSVDLVLEPK-KLKWVFKHAERIGAKRLVLVGASEWERGMVRVKDLSSGEQTE 480
|
|
| hisZ_biosyn_reg |
TIGR00443 |
ATP phosphoribosyltransferase, regulatory subunit; Apparant second copies of histidyl-tRNA ... |
101-444 |
9.40e-46 |
|
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: 163.55 E-value: 9.40e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 101 DVVLREHIFSTVTEIFKRHGGVTLDTPVFELKEILSGKYGEDSKLIYDLKDQGGELCSLRYDLTVPFARwlAMNPKVTSI 180
Cdd:TIGR00443 7 EAARKEEIERQLQDVFRSWGYQEIITPTLEYLDTLSAGSGILNEDLFKLFDQLGRVLGLRPDMTAPIAR--LVSTRLRDR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 181 KR----FHIAKVYRRDQPAMtkGRMREFYQCDFDIAGnYDPMIPDSEALKVLVEALDALEVGNYTIKLNHRKILDGIFTV 256
Cdd:TIGR00443 85 PLplrlCYAGNVFRTNESGG--GRSREFTQAGVELIG-AGGPAADAEVIALLIEALKALGLKDFKIELGHVGLVRALLEE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 257 CGVPDDKIRTISSAVDKLDKLPWEdvrrEMVVEKGLKEEVADKIKEYVLLKGD-RSLLDKLEAdslLSSNSSAVAAFNDM 335
Cdd:TIGR00443 162 AGLPEEAREALREALARKDLVALE----ELVAELGLSPEVRERLLALPRLRGDgEEVLEEARA---LAGSETAEAALDEL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 336 RLLFDYLEAFGVLDRFSFDMSLARGLDYYTGIIYEAVTEasapkikssaekkksadpeadrsnddsiGVG-SIAAGGRYD 414
Cdd:TIGR00443 235 EAVLELLEARGVEEYISLDLGLVRGYHYYTGLIFEGYAP----------------------------GLGaPLAGGGRYD 286
|
330 340 350
....*....|....*....|....*....|
gi 429240963 415 NLVGMFAakknAKIPCVGISLGLERIFSIL 444
Cdd:TIGR00443 287 ELLGRFG----RPLPATGFALNLERLLEAL 312
|
|
| HisZ |
COG3705 |
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism]; |
105-446 |
9.08e-45 |
|
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism];
Pssm-ID: 442919 [Multi-domain] Cd Length: 312 Bit Score: 160.73 E-value: 9.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 105 REHIFSTVTEIFKRHGGVTLDTPVFELKEILSGKYGEDSKL-IYDLKDQGGELCSLRYDLTVPFARWLAMN-PKVTSIKR 182
Cdd:COG3705 8 KEELRRRLLDVFRSWGYELVEPPLLEYLDSLLTGSGADLDLqTFKLVDQLGRTLGLRPDMTPQVARIAATRlANRPGPLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 183 F-HIAKVYRRdQPAMTkGRMREFYQcdfdiAG----NYDPMIPDSEALKVLVEALDALEVGNYTIKLNHRKILDGIFTVC 257
Cdd:COG3705 88 LcYAGNVFRT-RPSGL-GRSREFLQ-----AGaeliGHAGLEADAEVIALALEALKAAGLEDFTLDLGHVGLFRALLEAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 258 GVPDDKIRTISSAVDKLDKLpweDVRrEMVVEKGLKEEVADKIKEYVLLKGDRSLLDKLEAdslLSSNSSAVAAFNDMRL 337
Cdd:COG3705 161 GLSEEQREELRRALARKDAV---ELE-ELLAELGLSEELAEALLALPELYGGEEVLARARA---LLLDAAIRAALDELEA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 338 LFDYLEAFGVLDRFSFDMSLARGLDYYTGIIYEAVTEasapkikssaekkksadpeadrsnddsiGVGS-IAAGGRYDNL 416
Cdd:COG3705 234 LAEALAARGPDVRLTFDLSELRGYDYYTGIVFEAYAP----------------------------GVGDpLARGGRYDGL 285
|
330 340 350
....*....|....*....|....*....|
gi 429240963 417 VGMFaakkNAKIPCVGISLGLERIFSILRS 446
Cdd:COG3705 286 LAAF----GRARPATGFSLDLDRLLRALPA 311
|
|
| tRNA-synt_His |
pfam13393 |
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ... |
105-440 |
1.18e-41 |
|
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: 151.97 E-value: 1.18e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 105 REHIFSTVTEIFKRHG--GVTLdtPVFELKEILSGKYGEDSKLIYDLKDQGGELCSLRYDLTVPFARWLAMNPKVTSIKR 182
Cdd:pfam13393 13 IEELRRRLLDLFRSWGyeLVMP--PLLEYLDSLLTGTGADLDQTFKLVDQSGRLLGLRADITPQVARIDAHRLNRPGPLR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 183 FH-IAKVYRRDQPAMtkGRMREFYQCDFDIAGNYDPMiPDSEALKVLVEALDALEVGNYTIKLNHRKILDGIFTVCGVPD 261
Cdd:pfam13393 91 LCyAGSVLRTRPKGL--GRSREPLQVGAELIGHAGIE-ADAEIISLLLEALAAAGVPGVTLDLGHVGLVRALLEAAGLSE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 262 DKIRTISSAVDKLDklpWEDVRrEMVVEKGLKEEVADKIKEYVLLKGDRSLLDKLEAdsLLSSNSSAVAAFNDMRLLFDY 341
Cdd:pfam13393 168 ALEEALRAALQRKD---AAELA-ELAAEAGLPPALRRALLALPDLYGGPEVLDEARA--ALPGLPALQEALDELEALAAL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 342 LEAFGVLDRFSFDMSLARGLDYYTGIIYEAVTEasapkikssaekkksadpeadrsnddsiGVGS-IAAGGRYDNLVGMF 420
Cdd:pfam13393 242 LEALGDGVRLTFDLAELRGYEYYTGIVFAAYAP----------------------------GVGEpLARGGRYDDLGAAF 293
|
330 340
....*....|....*....|
gi 429240963 421 aakkNAKIPCVGISLGLERI 440
Cdd:pfam13393 294 ----GRARPATGFSLDLEAL 309
|
|
| hisZ |
PRK12292 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
91-440 |
3.08e-40 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 237043 [Multi-domain] Cd Length: 391 Bit Score: 150.40 E-value: 3.08e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 91 PKGTKDWCDKDVVLREHIFSTVTEIFKRHGGVTLDTPVFELKEIL--SGKYGEDSKLIYDLKDQGGELCSLRYDLTVPFA 168
Cdd:PRK12292 6 PEGIRDLLPEEARKIEEIRRRLLDLFRRWGYEEVITPTLEYLDTLlaGGGAILDLRTFKLVDQLSGRTLGLRPDMTAQIA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 169 RWLA--MNPKVTSIKRFHIAKVYRRdqPAMTKGRMREFYQCDFDIAGnYDPMIPDSEALKVLVEALDALEVGNYTIKLNH 246
Cdd:PRK12292 86 RIAAtrLANRPGPLRLCYAGNVFRA--QERGLGRSREFLQSGVELIG-DAGLEADAEVILLLLEALKALGLPNFTLDLGH 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 247 RKILDGIFTVCGVPDDKIRTISSAVDKLD--KLpwedvrREMVveKGLKEEVADKIKEYVLLKGDRSLLDKLEAdslLSS 324
Cdd:PRK12292 163 VGLFRALLEAAGLSEELEEVLRRALANKDyvAL------EELV--LDLSEELRDALLALPRLRGGREVLEEARK---LLP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 325 NSSAVAAFNDMRLLFDYLEAFGVLDRFSFDMSLARGLDYYTGIIYEAVTEasapkikssaekkksadpeadrsnddsiGV 404
Cdd:PRK12292 232 SLPIKRALDELEALAEALEKYGYGIPLSLDLGLLRHLDYYTGIVFEGYVD----------------------------GV 283
|
330 340 350
....*....|....*....|....*....|....*..
gi 429240963 405 G-SIAAGGRYDNLVGMFAAKKNAkipcVGISLGLERI 440
Cdd:PRK12292 284 GnPIASGGRYDDLLGRFGRARPA----TGFSLDLDRL 316
|
|
| HisRS_anticodon |
cd00859 |
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases ... |
458-557 |
5.40e-24 |
|
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: 96.07 E-value: 5.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 458 VDVFVMAFGGGkewtgFLKERMSVCKDLWANGIKAEFLYKvKPKPRQQFDAADKFDVPFAVILGQDEFAKGSVRIKQMgl 537
Cdd:cd00859 2 VDVYVVPLGEG-----ALSEALELAEQLRDAGIKAEIDYG-GRKLKKQFKYADRSGARFAVILGEDELAAGVVTVKDL-- 73
|
90 100
....*....|....*....|
gi 429240963 538 keNSDEGQLVPREEMVSVLK 557
Cdd:cd00859 74 --ETGEQETVALDELVEELK 91
|
|
| hisZ |
PRK12295 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
116-440 |
7.65e-21 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 183413 [Multi-domain] Cd Length: 373 Bit Score: 94.62 E-value: 7.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 116 FKRHGGVTLDTPVFELKEILSGKYGED-SKLIYDLKDQ-GGELCsLRYDLTVPFAR-WLAMNPKvTSIKRFHIAKVYRRd 192
Cdd:PRK12295 18 FEAAGAVRVDPPILQPAEPFLDLSGEDiRRRIFVTSDEnGEELC-LRPDFTIPVCRrHIATAGG-EPARYAYLGEVFRQ- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 193 qpamTKGRMREFYQCDFDIAGNYDPMIPDSEALKVLVEALDALEVGNYTIKLNHRKILDGIFTVCGVPDD-KIRTI---- 267
Cdd:PRK12295 95 ----RRDRASEFLQAGIESFGRADPAAADAEVLALALEALAALGPGDLEVRLGDVGLFAALVDALGLPPGwKRRLLrhfg 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 268 --------------------SSAVDKLDKLPWEDVRREMVVEK---------GLK--EEVADKIKEYVLLKG----DRSL 312
Cdd:PRK12295 171 rprsldallarlagprvdplDEHAGVLAALADEAAARALVEDLmsiagispvGGRspAEIARRLLEKAALAAaarlPAEA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 313 LDKLEAdsLLSSNSSAVAAFNDMRLLF-----------DYLE-------AFGV-LDRFSFDMSLARGLDYYTGIIYEAVT 373
Cdd:PRK12295 251 LAVLER--FLAISGPPDAALAALRALAadagldldaalDRFEarlaalaARGIdLERLRFSASFGRPLDYYTGFVFEIRA 328
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 429240963 374 EASapkikssaekkksadpeadrsnddsiGVGSIAAGGRYDNLVGMFAAKknAKIPCVGISLGLERI 440
Cdd:PRK12295 329 AGN--------------------------GDPPLAGGGRYDGLLTRLGAG--EPIPAVGFSIWLDRL 367
|
|
| syh |
CHL00201 |
histidine-tRNA synthetase; Provisional |
92-558 |
2.49e-20 |
|
histidine-tRNA synthetase; Provisional
Pssm-ID: 164576 [Multi-domain] Cd Length: 430 Bit Score: 93.81 E-value: 2.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 92 KGTKDWCDKDVVLREHIFSTVTEIFKRHGGVTLDTPVFELKEILSGKYGEDSKLI----YDLKDQGGELCSLRYDLTVPF 167
Cdd:CHL00201 8 RGTKDILPDEINYWQFIHDKALTLLSLANYSEIRTPIFENSSLYDRGIGETTDIVnkemYRFTDRSNRDITLRPEGTAGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 168 ARWLAMNPKV--TSIKR-FHIAKVYRRDQPamTKGRMREFYQCDFDIAGNYDPMiPDSEALKVLVEALDALEVGNYTIKL 244
Cdd:CHL00201 88 VRAFIENKMDyhSNLQRlWYSGPMFRYERP--QSGRQRQFHQLGIEFIGSIDAR-ADTEVIHLAMQIFNELQVKNLILDI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 245 NH------------------RKILDGIFTvcgvpDDKIRTISSAVDKLDKlpwedvrREMVVEKGLKEevADKIKEYVLL 306
Cdd:CHL00201 165 NSigkledrqsyqlklveylSQYQDDLDT-----DSQNRLYSNPIRILDS-------KNLKTQEILDG--APKISDFLSL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 307 KGDRSLLDkleadsllssnssavaafndmrlLFDYLEAFGVldRFSFDMSLARGLDYYTGIIYEavteasapkIKSSaeK 386
Cdd:CHL00201 231 ESTEHFYD-----------------------VCTYLNLLNI--PYKINYKLVRGLDYYNDTAFE---------IKTL--S 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 387 KKSADpeadrsnddsigvgSIAAGGRYDNLVGMFAAKKNakiPCVGISLGLERIFSILRSKIpdeDIRANDVDVFVMAFG 466
Cdd:CHL00201 275 SNGQD--------------TICGGGRYDSLIHQLGGPKT---PAVGCAIGLERLLLIAKDNI---ILPKQSIDVYIATQG 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 467 GGKEWTGflkerMSVCKDLWANGIKAEfLYKVKPKPRQQFDAADKFDVPFAVILGQDEFAKGSVRIKQMGLKENsDEGQL 546
Cdd:CHL00201 335 LKAQKKG-----WEIIQFLEKQNIKFE-LDLSSSNFHKQIKQAGKKRAKACIILGDNEIMDNCITIKWLDEQVQ-ENAQY 407
|
490
....*....|..
gi 429240963 547 VPREEMVSVLKK 558
Cdd:CHL00201 408 SNFKQEISYLKK 419
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
459-559 |
4.06e-12 |
|
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: 62.22 E-value: 4.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 459 DVFVMAFGGGKEwtGFLKERMSVCKDLWANGIKAEFLYkVKPKPRQQFDAADKFDVPFAVILGQDEFAKGSVRIKQMglk 538
Cdd:pfam03129 1 QVVVIPLGEKAE--ELEEYAQKLAEELRAAGIRVELDD-RNESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRR--- 74
|
90 100
....*....|....*....|.
gi 429240963 539 eNSDEGQLVPREEMVSVLKKL 559
Cdd:pfam03129 75 -DTGEQETVSLDELVEKLKEL 94
|
|
| WHEP-TRS |
pfam00458 |
WHEP-TRS domain; |
33-62 |
2.46e-08 |
|
WHEP-TRS domain;
Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 50.19 E-value: 2.46e-08
10 20 30
....*....|....*....|....*....|
gi 429240963 33 INERITSQGNLVRSLKSQGASKEDIDKEVA 62
Cdd:pfam00458 1 LTEKIKAQGDLVRKLKAEKAPKEEIDAAVK 30
|
|
| WHEP-TRS |
smart00991 |
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ... |
34-62 |
9.64e-07 |
|
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: 45.80 E-value: 9.64e-07
10 20
....*....|....*....|....*....
gi 429240963 34 NERITSQGNLVRSLKSQGASKEDIDKEVA 62
Cdd:smart00991 1 EEAVAAQGELVRKLKAEKASKDEIDAAVA 29
|
|
| WHEPGMRS_RNA |
cd01200 |
EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher ... |
34-63 |
1.28e-06 |
|
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: 45.22 E-value: 1.28e-06
10 20 30
....*....|....*....|....*....|
gi 429240963 34 NERITSQGNLVRSLKSQGASKEDIDKEVAK 63
Cdd:cd01200 1 YEKIAEQGDLVRKLKAEKAPKEEIDAAVKK 30
|
|
| HisRS_RNA |
cd00938 |
HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS ... |
33-63 |
2.06e-05 |
|
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: 41.69 E-value: 2.06e-05
10 20 30
....*....|....*....|....*....|.
gi 429240963 33 INERITSQGNLVRSLKSQGASKEDIDKEVAK 63
Cdd:cd00938 3 LEEAVKLQGELVRKLKAEKASKEQIAEEVAK 33
|
|
| WEPRS_RNA |
cd00936 |
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ... |
33-62 |
3.74e-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: 41.07 E-value: 3.74e-05
10 20 30
....*....|....*....|....*....|
gi 429240963 33 INERITSQGNLVRSLKSQGASKEDIDKEVA 62
Cdd:cd00936 1 LYKKIAAQGDLVRELKAKKAPKEEIDAAVK 30
|
|
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
25-62 |
1.46e-03 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 41.65 E-value: 1.46e-03
10 20 30
....*....|....*....|....*....|....*...
gi 429240963 25 TMADSLVDINERITSQGNLVRSLKSQGASKEDIDKEVA 62
Cdd:PLN02734 4 SLRDALAEKQAAVTAQGNAVRALKASKADKAEIDAAIE 41
|
|
| HGTP_anticodon2 |
pfam12745 |
Anticodon binding domain of tRNAs; This is an HGTP_anticodon binding domain, found largely on ... |
458-557 |
1.89e-03 |
|
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: 40.28 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429240963 458 VDVFVMAFGGGkewtgFLK-ERMSVCKDLWANGIKAEFLYKVKPKPRQQFDAADKFDVPFAVILGQDEFAKGS----VRI 532
Cdd:pfam12745 6 CDVLVASFDAS-----ILRtTGVEILQELWAHGISADLAVDASYSPEDLVSRARDDGVSWIVIIKQQNKSSDSkykpLKV 80
|
90 100
....*....|....*....|....*
gi 429240963 533 KQMGLKENSDegqlVPREEMVSVLK 557
Cdd:pfam12745 81 KNLLRKEDVD----LDSDELVSWLR 101
|
|
| GlyRS_RNA |
cd00935 |
GlyRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of GlyRS ... |
30-62 |
9.26e-03 |
|
GlyRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of GlyRS 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: 238472 [Multi-domain] Cd Length: 51 Bit Score: 34.77 E-value: 9.26e-03
10 20 30
....*....|....*....|....*....|...
gi 429240963 30 LVDINERITSQGNLVRSLKSQGASKEDIDKEVA 62
Cdd:cd00935 1 LAPLRAAVKEQGDLVRKLKEEGAPDVDIKKAVA 33
|
|
| |
