|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02972 |
PLN02972 |
Histidyl-tRNA synthetase |
40-505 |
0e+00 |
|
Histidyl-tRNA synthetase
Pssm-ID: 215525 [Multi-domain] Cd Length: 763 Bit Score: 586.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 40 KLKAQLGHDEGKQKfvLKTPKGTRDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLTGKYGEDSKLIYDLKD 119
Cdd:PLN02972 313 KVKEIVESNEVRRL--PKIPKGTRDFAKEQMAIREKAFSIITSVFKRHGATALDTPVFELRETLMGKYGEDSKLIYDLAD 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 120 QGGELLSLRYDLTVPFARYLAMNKLTNIKRYHIAKVYRRDNPamTRGRYREFYQCDFDIAGQFDPMIPDAECLKIMCEIL 199
Cdd:PLN02972 391 QGGELCSLRYDLTVPFARYVAMNGITSFKRYQIAKVYRRDNP--SKGRYREFYQCDFDIAGVYEPMGPDFEIIKVLTELL 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 200 SSLQIGNFQVKVNDRRILDGMFAVCGVPDSKFRTICSSVDKLDKVSWEEVKNEMVGEKGLAPEVADRIGDYVQQHGG-VS 278
Cdd:PLN02972 469 DELDIGTYEVKLNHRKLLDGMLEICGVPPEKFRTICSSIDKLDKQSFEQVKKEMVEEKGLSNETADKIGNFVKERGPpLE 548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 279 LVEQLLQ-DPKLSQNKQAVEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLLqmptqaGEEplgVGSI 357
Cdd:PLN02972 549 LLSKLRQeGSEFLGNASSRAALDELEIMFKALEKSKAIGKIVFDLSLARGLDYYTGVIYEAVFK------GAQ---VGSI 619
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 358 AAGGRYDGLVGMFDpkGRKVPCVGLSIGVERIFSIVEQKLEASEEKVRTTETQVLVASAQKKLLEERLKLISELWDAGIK 437
Cdd:PLN02972 620 AAGGRYDNLVGMFS--GKQVPAVGVSLGIERVFAIMEQQEEEKSQVIRPTETEVLVSIIGDDKLALAAELVSELWNAGIK 697
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 70794762 438 AEllYKKNPKLLNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVDVRREDLVEEIRRRTSQP 505
Cdd:PLN02972 698 AE--YKVSTRKAKHLKRAKESGIPWMVLVGEKELSKGFVKLKNLEAGVEEEVDRTCFVQELKAELLKL 763
|
|
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
56-504 |
1.15e-117 |
|
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: 352.89 E-value: 1.15e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 56 LKTPKGTRDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLTGKYGED--SKLIYDLKDQGGELLSLRYDLTV 133
Cdd:COG0124 4 IQAPRGTRDILPEESAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKIGEDivEKEMYTFEDRGGRSLTLRPEGTA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 134 PFARYLAMNKLTN---IKRYHIAKVYRRDNPAmtRGRYREFYQCDFDIAGQFDPMIpDAECLKIMCEILSSLQIGNFQVK 210
Cdd:COG0124 84 PVARAVAEHGNELpfpFKLYYIGPVFRYERPQ--KGRYRQFHQFGVEVIGSDSPLA-DAEVIALAADLLKALGLKDFTLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 211 VNDRrildgmfavcGVPDSKFRTICSSVDKLDKVSWEEVknemvgekgLAPEVADRI------------GDYVQqhggvS 278
Cdd:COG0124 161 INSR----------GLPEERAEALLRYLDKLDKIGHEDV---------LDEDSQRRLetnplraildskGPDCQ-----E 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 279 LVEQLlqdPKLSQNKqAVEGLGDLKLLFEYLTLFGIDdkISFDLSLARGLDYYTGVIYEAVLLQMPTQageeplgvGSIA 358
Cdd:COG0124 217 VLADA---PKLLDYL-GEEGLAHFEEVLELLDALGIP--YVIDPRLVRGLDYYTGTVFEIVTDGLGAQ--------GSVC 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 359 AGGRYDGLVGMFDpkGRKVPCVGLSIGVERIFSIVEqklEASEEKVRTTETQVLVASAQKKLLEERLKLISELWDAGIKA 438
Cdd:COG0124 283 GGGRYDGLVEQLG--GPPTPAVGFAIGLERLLLLLE---ELGLLPAAEPPPDVYVVPLGEEARAEALKLAQELRAAGIRV 357
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 70794762 439 EL-LYKKNPKllNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVDVRREDLVEEIRRRTSQ 504
Cdd:COG0124 358 ELdLGGRKLK--KQLKYADKSGAPFVLILGEDELANGTVTLKDLATGEQETVPLDELVEYLKELLAE 422
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
69-394 |
1.59e-105 |
|
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: 315.70 E-value: 1.59e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 69 QMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLTGKYGED-SKLIYDLKDQGGELLSLRYDLTVPFARYLAMNKL--- 144
Cdd:cd00773 1 EAALRRYIEDTLREVFERYGYEEIDTPVFEYTELFLRKSGDEvSKEMYRFKDKGGRDLALRPDLTAPVARAVAENLLslp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 145 TNIKRYHIAKVYRRDNPAmtRGRYREFYQCDFDIAGqFDPMIPDAECLKIMCEILSSLQIGNFQVKVNDRRILDGmfaVC 224
Cdd:cd00773 81 LPLKLYYIGPVFRYERPQ--KGRYREFYQVGVEIIG-SDSPLADAEVIALAVEILEALGLKDFQIKINHRGILDG---IA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 225 GVPDSKFRTICSSVDKLDKvsweevknemvgekglapevadrigdyvqqhggvslveqllqdpklsqnkqavEGLGDLKL 304
Cdd:cd00773 155 GLLEDREEYIERLIDKLDK-----------------------------------------------------EALAHLEK 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 305 LFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLLQMPTQageeplgvGSIAAGGRYDGLVGMFDpkGRKVPCVGLSI 384
Cdd:cd00773 182 LLDYLEALGVDIKYSIDLSLVRGLDYYTGIVFEAVADGLGAQ--------GSIAGGGRYDGLLEEFG--GEDVPAVGFAI 251
|
330
....*....|
gi 70794762 385 GVERIFSIVE 394
Cdd:cd00773 252 GLERLLLALE 261
|
|
| hisS |
TIGR00442 |
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ... |
57-489 |
8.89e-105 |
|
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: 319.04 E-value: 8.89e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 57 KTPKGTRDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLTGKYGEDS----KLIYDLKDQGGELLSLRYDLT 132
Cdd:TIGR00442 1 QKPRGTRDFLPEEMIKWQYIEETIREVFERYGFKEIRTPIFEYTELFKRKVGEETdivsKEMYTFKDKGGRSLTLRPEGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 133 VPFARYLAMNKLTN---IKRYHIAKVYRRDNPAmtRGRYREFYQCDFDIAGQFDPMIpDAECLKIMCEILSSLQIGNFQV 209
Cdd:TIGR00442 81 APVARAVIENKLLLpkpFKLYYIGPMFRYERPQ--KGRYRQFHQFGVEVIGSDSPLA-DAEIIALAADILKELGLKDFTL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 210 KVNDRRILDGMFAvcgvpdsKFRTICSSVDK-LDKVSWEEVKNEMVGEKGLAPEVADRIGDYVQQhggvslveqllqDPK 288
Cdd:TIGR00442 158 EINSLGILEGRLE-------YREALIRYLDKhKDKLGEDSVRRLEKNPLRILDSKNEKIQELLKN------------APK 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 289 LSQNKQAvEGLGDLKLLFEYLTLFGIddKISFDLSLARGLDYYTGVIYEAVLLQMPTQageeplgvGSIAAGGRYDGLVG 368
Cdd:TIGR00442 219 ILDFLCE-ESRAHFEELKELLDALGI--PYKIDPSLVRGLDYYTGTVFEFVTDDLGAQ--------GSICGGGRYDGLVE 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 369 MFDpkGRKVPCVGLSIGVERIFSIVEqklEASEEKVRTTETQVLVASAQKKLLEERLKLISELWDAGIKAElLYKKNPKL 448
Cdd:TIGR00442 288 ELG--GPPTPAVGFAIGIERLILLLE---ELGLIPPPSKKPDVYVVPLGEEAELEALKLAQKLRKAGIRVE-VDLGGRKL 361
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 70794762 449 LNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVDV 489
Cdd:TIGR00442 362 KKQLKYADKLGARFALIIGEDELENGTVTLKDLETGEQETV 402
|
|
| tRNA-synt_His |
pfam13393 |
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ... |
61-389 |
1.50e-43 |
|
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: 156.21 E-value: 1.50e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 61 GTRDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLTGKYGEDSKLIYDLKDQGGELLSLRYDLTVPFARYLA 140
Cdd:pfam13393 1 GIRDLLPPEARRIEELRRRLLDLFRSWGYELVMPPLLEYLDSLLTGTGADLDQTFKLVDQSGRLLGLRADITPQVARIDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 141 mnKLTNIKR----YHIAKVYRRDNPAMtrGRYREFYQCDFDIAGQFDPMiPDAECLKIMCEILSSLQIGNFQVKVNDRRI 216
Cdd:pfam13393 81 --HRLNRPGplrlCYAGSVLRTRPKGL--GRSREPLQVGAELIGHAGIE-ADAEIISLLLEALAAAGVPGVTLDLGHVGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 217 LDGMFAVCGVPDSKFRTICSSVDKLDkvsWEEVKnEMVGEKGLAPEVADRIGDYVQQHGGVSLVEQLLQDpkLSQNKQAV 296
Cdd:pfam13393 156 VRALLEAAGLSEALEEALRAALQRKD---AAELA-ELAAEAGLPPALRRALLALPDLYGGPEVLDEARAA--LPGLPALQ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 297 EGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLLqmptQAGEEplgvgsIAAGGRYDGLVGMFdpkGRK 376
Cdd:pfam13393 230 EALDELEALAALLEALGDGVRLTFDLAELRGYEYYTGIVFAAYAP----GVGEP------LARGGRYDDLGAAF---GRA 296
|
330
....*....|...
gi 70794762 377 VPCVGLSIGVERI 389
Cdd:pfam13393 297 RPATGFSLDLEAL 309
|
|
| HisRS_RNA |
cd00938 |
HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS ... |
5-49 |
6.12e-17 |
|
HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). This domain consists of a helix- turn- helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238474 [Multi-domain] Cd Length: 45 Bit Score: 74.43 E-value: 6.12e-17
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 70794762 5 AALEELVRLQGAHVRGLKEQKASAEQIEEEVTKLLKLKAQLGHDE 49
Cdd:cd00938 1 AKLEEAVKLQGELVRKLKAEKASKEQIAEEVAKLLELKAQLGGDE 45
|
|
| WHEP-TRS |
smart00991 |
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ... |
8-63 |
1.05e-10 |
|
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: 56.97 E-value: 1.05e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 70794762 8 EELVRLQGAHVRGLKEQKASAEQIEEEVTKLLKLKAQLGHDEGKQKFVLKTPKGTR 63
Cdd:smart00991 1 EEAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLKEATGQDYKPGAPPGDTP 56
|
|
| WHEP-TRS |
pfam00458 |
WHEP-TRS domain; |
7-51 |
3.29e-09 |
|
WHEP-TRS domain;
Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 52.50 E-value: 3.29e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 70794762 7 LEELVRLQGAHVRGLKEQKASAEQIEEEVTKLLKLKAQLGHDEGK 51
Cdd:pfam00458 1 LTEKIKAQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKALTGK 45
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02972 |
PLN02972 |
Histidyl-tRNA synthetase |
40-505 |
0e+00 |
|
Histidyl-tRNA synthetase
Pssm-ID: 215525 [Multi-domain] Cd Length: 763 Bit Score: 586.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 40 KLKAQLGHDEGKQKfvLKTPKGTRDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLTGKYGEDSKLIYDLKD 119
Cdd:PLN02972 313 KVKEIVESNEVRRL--PKIPKGTRDFAKEQMAIREKAFSIITSVFKRHGATALDTPVFELRETLMGKYGEDSKLIYDLAD 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 120 QGGELLSLRYDLTVPFARYLAMNKLTNIKRYHIAKVYRRDNPamTRGRYREFYQCDFDIAGQFDPMIPDAECLKIMCEIL 199
Cdd:PLN02972 391 QGGELCSLRYDLTVPFARYVAMNGITSFKRYQIAKVYRRDNP--SKGRYREFYQCDFDIAGVYEPMGPDFEIIKVLTELL 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 200 SSLQIGNFQVKVNDRRILDGMFAVCGVPDSKFRTICSSVDKLDKVSWEEVKNEMVGEKGLAPEVADRIGDYVQQHGG-VS 278
Cdd:PLN02972 469 DELDIGTYEVKLNHRKLLDGMLEICGVPPEKFRTICSSIDKLDKQSFEQVKKEMVEEKGLSNETADKIGNFVKERGPpLE 548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 279 LVEQLLQ-DPKLSQNKQAVEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLLqmptqaGEEplgVGSI 357
Cdd:PLN02972 549 LLSKLRQeGSEFLGNASSRAALDELEIMFKALEKSKAIGKIVFDLSLARGLDYYTGVIYEAVFK------GAQ---VGSI 619
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 358 AAGGRYDGLVGMFDpkGRKVPCVGLSIGVERIFSIVEQKLEASEEKVRTTETQVLVASAQKKLLEERLKLISELWDAGIK 437
Cdd:PLN02972 620 AAGGRYDNLVGMFS--GKQVPAVGVSLGIERVFAIMEQQEEEKSQVIRPTETEVLVSIIGDDKLALAAELVSELWNAGIK 697
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 70794762 438 AEllYKKNPKLLNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVDVRREDLVEEIRRRTSQP 505
Cdd:PLN02972 698 AE--YKVSTRKAKHLKRAKESGIPWMVLVGEKELSKGFVKLKNLEAGVEEEVDRTCFVQELKAELLKL 763
|
|
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
56-504 |
1.15e-117 |
|
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: 352.89 E-value: 1.15e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 56 LKTPKGTRDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLTGKYGED--SKLIYDLKDQGGELLSLRYDLTV 133
Cdd:COG0124 4 IQAPRGTRDILPEESAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKIGEDivEKEMYTFEDRGGRSLTLRPEGTA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 134 PFARYLAMNKLTN---IKRYHIAKVYRRDNPAmtRGRYREFYQCDFDIAGQFDPMIpDAECLKIMCEILSSLQIGNFQVK 210
Cdd:COG0124 84 PVARAVAEHGNELpfpFKLYYIGPVFRYERPQ--KGRYRQFHQFGVEVIGSDSPLA-DAEVIALAADLLKALGLKDFTLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 211 VNDRrildgmfavcGVPDSKFRTICSSVDKLDKVSWEEVknemvgekgLAPEVADRI------------GDYVQqhggvS 278
Cdd:COG0124 161 INSR----------GLPEERAEALLRYLDKLDKIGHEDV---------LDEDSQRRLetnplraildskGPDCQ-----E 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 279 LVEQLlqdPKLSQNKqAVEGLGDLKLLFEYLTLFGIDdkISFDLSLARGLDYYTGVIYEAVLLQMPTQageeplgvGSIA 358
Cdd:COG0124 217 VLADA---PKLLDYL-GEEGLAHFEEVLELLDALGIP--YVIDPRLVRGLDYYTGTVFEIVTDGLGAQ--------GSVC 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 359 AGGRYDGLVGMFDpkGRKVPCVGLSIGVERIFSIVEqklEASEEKVRTTETQVLVASAQKKLLEERLKLISELWDAGIKA 438
Cdd:COG0124 283 GGGRYDGLVEQLG--GPPTPAVGFAIGLERLLLLLE---ELGLLPAAEPPPDVYVVPLGEEARAEALKLAQELRAAGIRV 357
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 70794762 439 EL-LYKKNPKllNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVDVRREDLVEEIRRRTSQ 504
Cdd:COG0124 358 ELdLGGRKLK--KQLKYADKSGAPFVLILGEDELANGTVTLKDLATGEQETVPLDELVEYLKELLAE 422
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
69-394 |
1.59e-105 |
|
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: 315.70 E-value: 1.59e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 69 QMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLTGKYGED-SKLIYDLKDQGGELLSLRYDLTVPFARYLAMNKL--- 144
Cdd:cd00773 1 EAALRRYIEDTLREVFERYGYEEIDTPVFEYTELFLRKSGDEvSKEMYRFKDKGGRDLALRPDLTAPVARAVAENLLslp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 145 TNIKRYHIAKVYRRDNPAmtRGRYREFYQCDFDIAGqFDPMIPDAECLKIMCEILSSLQIGNFQVKVNDRRILDGmfaVC 224
Cdd:cd00773 81 LPLKLYYIGPVFRYERPQ--KGRYREFYQVGVEIIG-SDSPLADAEVIALAVEILEALGLKDFQIKINHRGILDG---IA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 225 GVPDSKFRTICSSVDKLDKvsweevknemvgekglapevadrigdyvqqhggvslveqllqdpklsqnkqavEGLGDLKL 304
Cdd:cd00773 155 GLLEDREEYIERLIDKLDK-----------------------------------------------------EALAHLEK 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 305 LFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLLQMPTQageeplgvGSIAAGGRYDGLVGMFDpkGRKVPCVGLSI 384
Cdd:cd00773 182 LLDYLEALGVDIKYSIDLSLVRGLDYYTGIVFEAVADGLGAQ--------GSIAGGGRYDGLLEEFG--GEDVPAVGFAI 251
|
330
....*....|
gi 70794762 385 GVERIFSIVE 394
Cdd:cd00773 252 GLERLLLALE 261
|
|
| hisS |
TIGR00442 |
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ... |
57-489 |
8.89e-105 |
|
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: 319.04 E-value: 8.89e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 57 KTPKGTRDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLTGKYGEDS----KLIYDLKDQGGELLSLRYDLT 132
Cdd:TIGR00442 1 QKPRGTRDFLPEEMIKWQYIEETIREVFERYGFKEIRTPIFEYTELFKRKVGEETdivsKEMYTFKDKGGRSLTLRPEGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 133 VPFARYLAMNKLTN---IKRYHIAKVYRRDNPAmtRGRYREFYQCDFDIAGQFDPMIpDAECLKIMCEILSSLQIGNFQV 209
Cdd:TIGR00442 81 APVARAVIENKLLLpkpFKLYYIGPMFRYERPQ--KGRYRQFHQFGVEVIGSDSPLA-DAEIIALAADILKELGLKDFTL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 210 KVNDRRILDGMFAvcgvpdsKFRTICSSVDK-LDKVSWEEVKNEMVGEKGLAPEVADRIGDYVQQhggvslveqllqDPK 288
Cdd:TIGR00442 158 EINSLGILEGRLE-------YREALIRYLDKhKDKLGEDSVRRLEKNPLRILDSKNEKIQELLKN------------APK 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 289 LSQNKQAvEGLGDLKLLFEYLTLFGIddKISFDLSLARGLDYYTGVIYEAVLLQMPTQageeplgvGSIAAGGRYDGLVG 368
Cdd:TIGR00442 219 ILDFLCE-ESRAHFEELKELLDALGI--PYKIDPSLVRGLDYYTGTVFEFVTDDLGAQ--------GSICGGGRYDGLVE 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 369 MFDpkGRKVPCVGLSIGVERIFSIVEqklEASEEKVRTTETQVLVASAQKKLLEERLKLISELWDAGIKAElLYKKNPKL 448
Cdd:TIGR00442 288 ELG--GPPTPAVGFAIGIERLILLLE---ELGLIPPPSKKPDVYVVPLGEEAELEALKLAQKLRKAGIRVE-VDLGGRKL 361
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 70794762 449 LNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVDV 489
Cdd:TIGR00442 362 KKQLKYADKLGARFALIIGEDELENGTVTLKDLETGEQETV 402
|
|
| PRK12420 |
PRK12420 |
histidyl-tRNA synthetase; Provisional |
53-489 |
1.40e-83 |
|
histidyl-tRNA synthetase; Provisional
Pssm-ID: 237097 [Multi-domain] Cd Length: 423 Bit Score: 265.06 E-value: 1.40e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 53 KFVLKTPKGTRDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLTGKYG---EDSKLIYDLKDQGGELLSLRY 129
Cdd:PRK12420 1 MMEMRNVKGTKDYLPEEQVLRNKIKRALEDVFERYGCKPLETPTLNMYELMSSKYGggdEILKEIYTLTDQGKRDLALRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 130 DLTVPFARYLAMNKltNI----KRYHIAKVYrRDNPaMTRGRYREFYQCDFDIAGQFDPMiPDAECLKIMCEILSSLQIg 205
Cdd:PRK12420 81 DLTIPFAKVVAMNP--NIrlpfKRYEIGKVF-RDGP-IKQGRFREFIQCDVDIVGVESVM-AEAELMSMAFELFRRLNL- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 206 NFQVKVNDRRILDGMFAVCGVPDSKFRTICSSVDKLDKVSWEEVKNEMVgEKGLAPEVADRIGDYVQQHGGVSLVEQllq 285
Cdd:PRK12420 155 EVTIQYNNRKLLNGILQAIGIPTELTSDVILSLDKIEKIGIDGVRKDLL-ERGISEEMADTICNTVLSCLQLSIADF--- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 286 dPKLSQNKQAVEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLlqmptqagEEPLGVGSIAAGGRYDG 365
Cdd:PRK12420 231 -KEAFNNPLVAEGVNELQQLQQYLIALGINENCIFNPFLARGLTMYTGTVYEIFL--------KDGSITSSIGSGGRYDN 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 366 LVGMFDPKGRKVPCVGLSIGVERIFSIVEQKLEASEekvrttETQVLVASAQKKLleERLKLISELW-DAGIKAELLYkK 444
Cdd:PRK12420 302 IIGAFRGDDMNYPTVGISFGLDVIYTALSQKETISS------TADVFIIPLGTEL--QCLQIAQQLRsTTGLKVELEL-A 372
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 70794762 445 NPKLLNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVDV 489
Cdd:PRK12420 373 GRKLKKALNYANKENIPYVLIIGEEEVSTGTVMLRNMKEGSEVKV 417
|
|
| PLN02530 |
PLN02530 |
histidine-tRNA ligase |
49-494 |
2.16e-53 |
|
histidine-tRNA ligase
Pssm-ID: 178145 [Multi-domain] Cd Length: 487 Bit Score: 187.64 E-value: 2.16e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 49 EGKQKFVLKTPKGTRDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLTGKYGED-SKLIYDLKDQGGELLSL 127
Cdd:PLN02530 63 DGKPKIDVNPPKGTRDFPPEDMRLRNWLFDHFREVSRLFGFEEVDAPVLESEELYIRKAGEEiTDQLYNFEDKGGRRVAL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 128 RYDLTVPFARyLAMNKLTNI----KRYHIAKVYRRDNpaMTRGRYREFYQCDFDIAGqFDPMIPDAECLKIMCEILSSLQ 203
Cdd:PLN02530 143 RPELTPSLAR-LVLQKGKSLslplKWFAIGQCWRYER--MTRGRRREHYQWNMDIIG-VPGVEAEAELLAAIVTFFKRVG 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 204 IGNFQV--KVNDRRILDGMFAVCGVPDSKFRTICSSVDKLDKVSWEEVKNEMvGEKGLAPEVADRIGDyVQQHGGVSLVE 281
Cdd:PLN02530 219 ITSSDVgiKVSSRKVLQAVLKSYGIPEESFAPVCVIVDKLEKLPREEIEKEL-DTLGVSEEAIEGILD-VLSLKSLDDLE 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 282 QLLqdpklsqnKQAVEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVllqmpTQAGEeplgVGSIAAGG 361
Cdd:PLN02530 297 ALL--------GADSEAVADLKQLFSLAEAYGYQDWLVFDASVVRGLAYYTGIVFEGF-----DRAGK----LRAICGGG 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 362 RYDGLVGMFDpkGRKVPCVGLSIGVERIFSIVEQKLEASEEkvrTTETQVLVASAQKKLLEERLKLISELWDAGIKAEL- 440
Cdd:PLN02530 360 RYDRLLSTFG--GEDTPACGFGFGDAVIVELLKEKGLLPEL---PHQVDDVVFALDEDLQGAAAGVASRLREKGRSVDLv 434
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 70794762 441 LYKKNPKLLnqLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVDVRREDL 494
Cdd:PLN02530 435 LEPKKLKWV--FKHAERIGAKRLVLVGASEWERGMVRVKDLSSGEQTEVKLDEL 486
|
|
| hisZ_biosyn_reg |
TIGR00443 |
ATP phosphoribosyltransferase, regulatory subunit; Apparant second copies of histidyl-tRNA ... |
63-389 |
1.83e-51 |
|
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: 177.42 E-value: 1.83e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 63 RDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLTGKYGEDSKLIYDLKDQGGELLSLRYDLTVPFARyLAMN 142
Cdd:TIGR00443 1 RDLLPEEAARKEEIERQLQDVFRSWGYQEIITPTLEYLDTLSAGSGILNEDLFKLFDQLGRVLGLRPDMTAPIAR-LVST 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 143 KLTNIKR----YHIAKVYRRDNPAmtRGRYREFYQCDFDIAGQfDPMIPDAECLKIMCEILSSLQIGNFQVKVNDRRILD 218
Cdd:TIGR00443 80 RLRDRPLplrlCYAGNVFRTNESG--GGRSREFTQAGVELIGA-GGPAADAEVIALLIEALKALGLKDFKIELGHVGLVR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 219 GMFAVCGVPDSKFRTICSSVDKLDKVSWEEVknemVGEKGLAPEVADRIGDYVQQHGGVSLVEQLLQdpKLSQNKQAVEG 298
Cdd:TIGR00443 157 ALLEEAGLPEEAREALREALARKDLVALEEL----VAELGLSPEVRERLLALPRLRGDGEEVLEEAR--ALAGSETAEAA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 299 LGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLLQMPTQageeplgvgsIAAGGRYDGLVGMFdpkGRKVP 378
Cdd:TIGR00443 231 LDELEAVLELLEARGVEEYISLDLGLVRGYHYYTGLIFEGYAPGLGAP----------LAGGGRYDELLGRF---GRPLP 297
|
330
....*....|.
gi 70794762 379 CVGLSIGVERI 389
Cdd:TIGR00443 298 ATGFALNLERL 308
|
|
| HisZ |
COG3705 |
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism]; |
67-389 |
2.18e-50 |
|
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism];
Pssm-ID: 442919 [Multi-domain] Cd Length: 312 Bit Score: 174.59 E-value: 2.18e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 67 PRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLTGKYGEDSKL-IYDLKDQGGELLSLRYDLTVPFARYLAmNKLT 145
Cdd:COG3705 2 PEEAARKEELRRRLLDVFRSWGYELVEPPLLEYLDSLLTGSGADLDLqTFKLVDQLGRTLGLRPDMTPQVARIAA-TRLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 146 NIKR----YHIAKVYRrdNPAMTRGRYREFYQC------DFDIAGqfdpmipDAECLKIMCEILSSLQIGNFQVKVNDRR 215
Cdd:COG3705 81 NRPGplrlCYAGNVFR--TRPSGLGRSREFLQAgaeligHAGLEA-------DAEVIALALEALKAAGLEDFTLDLGHVG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 216 ILDGMFAVCGVPDSKFRTICSSVDKLDKVsweEVKnEMVGEKGLAPEVADRIGDYVQQHGGVSLVEQLLqdpKLSQNKQA 295
Cdd:COG3705 152 LFRALLEALGLSEEQREELRRALARKDAV---ELE-ELLAELGLSEELAEALLALPELYGGEEVLARAR---ALLLDAAI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 296 VEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLlqmpTQAGEEplgvgsIAAGGRYDGLVGMFdpkGR 375
Cdd:COG3705 225 RAALDELEALAEALAARGPDVRLTFDLSELRGYDYYTGIVFEAYA----PGVGDP------LARGGRYDGLLAAF---GR 291
|
330
....*....|....
gi 70794762 376 KVPCVGLSIGVERI 389
Cdd:COG3705 292 ARPATGFSLDLDRL 305
|
|
| hisZ |
PRK12292 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
59-440 |
1.45e-47 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 237043 [Multi-domain] Cd Length: 391 Bit Score: 169.28 E-value: 1.45e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 59 PKGTRDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLT--GKYGEDSKLIYDLKDQGGELLSLRYDLTVPFA 136
Cdd:PRK12292 6 PEGIRDLLPEEARKIEEIRRRLLDLFRRWGYEEVITPTLEYLDTLLagGGAILDLRTFKLVDQLSGRTLGLRPDMTAQIA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 137 RyLAMNKLTNIKR----YHIAKVYRrdNPAMTRGRYREFYQCDFDIAGqFDPMIPDAECLKIMCEILSSLQIGNFQVKVN 212
Cdd:PRK12292 86 R-IAATRLANRPGplrlCYAGNVFR--AQERGLGRSREFLQSGVELIG-DAGLEADAEVILLLLEALKALGLPNFTLDLG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 213 DRRILDGMFAVCGVPDSKFRTICSSVDKLDKVSWEEVknemvgEKGLAPEVADRIGDYVQQHGGVSLVEQLLQdpkLSQN 292
Cdd:PRK12292 162 HVGLFRALLEAAGLSEELEEVLRRALANKDYVALEEL------VLDLSEELRDALLALPRLRGGREVLEEARK---LLPS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 293 KQAVEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLLQMPTqageeplgvgSIAAGGRYDGLVGMFdp 372
Cdd:PRK12292 233 LPIKRALDELEALAEALEKYGYGIPLSLDLGLLRHLDYYTGIVFEGYVDGVGN----------PIASGGRYDDLLGRF-- 300
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 70794762 373 kGRKVPCVGLSIGVERIfsiveqkLEASEEKvRTTETQVLVASAQKKLLEERLKLISELWDAGIKAEL 440
Cdd:PRK12292 301 -GRARPATGFSLDLDRL-------LELQLEL-PVEARKDLVIAPDSEALAAALAAAQELRKKGEIVVL 359
|
|
| tRNA-synt_His |
pfam13393 |
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ... |
61-389 |
1.50e-43 |
|
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: 156.21 E-value: 1.50e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 61 GTRDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLTGKYGEDSKLIYDLKDQGGELLSLRYDLTVPFARYLA 140
Cdd:pfam13393 1 GIRDLLPPEARRIEELRRRLLDLFRSWGYELVMPPLLEYLDSLLTGTGADLDQTFKLVDQSGRLLGLRADITPQVARIDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 141 mnKLTNIKR----YHIAKVYRRDNPAMtrGRYREFYQCDFDIAGQFDPMiPDAECLKIMCEILSSLQIGNFQVKVNDRRI 216
Cdd:pfam13393 81 --HRLNRPGplrlCYAGSVLRTRPKGL--GRSREPLQVGAELIGHAGIE-ADAEIISLLLEALAAAGVPGVTLDLGHVGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 217 LDGMFAVCGVPDSKFRTICSSVDKLDkvsWEEVKnEMVGEKGLAPEVADRIGDYVQQHGGVSLVEQLLQDpkLSQNKQAV 296
Cdd:pfam13393 156 VRALLEAAGLSEALEEALRAALQRKD---AAELA-ELAAEAGLPPALRRALLALPDLYGGPEVLDEARAA--LPGLPALQ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 297 EGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLLqmptQAGEEplgvgsIAAGGRYDGLVGMFdpkGRK 376
Cdd:pfam13393 230 EALDELEALAALLEALGDGVRLTFDLAELRGYEYYTGIVFAAYAP----GVGEP------LARGGRYDDLGAAF---GRA 296
|
330
....*....|...
gi 70794762 377 VPCVGLSIGVERI 389
Cdd:pfam13393 297 RPATGFSLDLEAL 309
|
|
| syh |
CHL00201 |
histidine-tRNA synthetase; Provisional |
60-498 |
4.42e-29 |
|
histidine-tRNA synthetase; Provisional
Pssm-ID: 164576 [Multi-domain] Cd Length: 430 Bit Score: 119.24 E-value: 4.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 60 KGTRDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLTGKYGEDSKLI----YDLKDQGGELLSLRYDLTVPF 135
Cdd:CHL00201 8 RGTKDILPDEINYWQFIHDKALTLLSLANYSEIRTPIFENSSLYDRGIGETTDIVnkemYRFTDRSNRDITLRPEGTAGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 136 ARYLAMNKLT---NIKR-YHIAKVYRRDNPamTRGRYREFYQCDFDIAGQFDPMiPDAECLKIMCEILSSLQIGNFQVKV 211
Cdd:CHL00201 88 VRAFIENKMDyhsNLQRlWYSGPMFRYERP--QSGRQRQFHQLGIEFIGSIDAR-ADTEVIHLAMQIFNELQVKNLILDI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 212 N------DRRILDgmfavcgvpdSKFRTICSSV-DKLDKVSweevKNEMVGEkglaP-EVADRIGDYVQqhggvslvEQL 283
Cdd:CHL00201 165 NsigkleDRQSYQ----------LKLVEYLSQYqDDLDTDS----QNRLYSN----PiRILDSKNLKTQ--------EIL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 284 LQDPKLSQ--NKQAVEGLGDLkllFEYLTLFGIDDKISFdlSLARGLDYYTGVIYEAVLLQMPTQageeplgvGSIAAGG 361
Cdd:CHL00201 219 DGAPKISDflSLESTEHFYDV---CTYLNLLNIPYKINY--KLVRGLDYYNDTAFEIKTLSSNGQ--------DTICGGG 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 362 RYDGLVGMFDpkGRKVPCVGLSIGVERIFSIVEQKLEASEEKVrttetQVLVASAQKKLLEERLKLISELWDAGIKAELL 441
Cdd:CHL00201 286 RYDSLIHQLG--GPKTPAVGCAIGLERLLLIAKDNIILPKQSI-----DVYIATQGLKAQKKGWEIIQFLEKQNIKFELD 358
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 70794762 442 YkKNPKLLNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVDVRREDLVEEI 498
Cdd:CHL00201 359 L-SSSNFHKQIKQAGKKRAKACIILGDNEIMDNCITIKWLDEQVQENAQYSNFKQEI 414
|
|
| HisRS_anticodon |
cd00859 |
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases ... |
408-499 |
8.53e-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: 106.47 E-value: 8.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 408 ETQVLVASAQKKLLEERLKLISELWDAGIKAELLYKkNPKLLNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEV 487
Cdd:cd00859 1 EVDVYVVPLGEGALSEALELAEQLRDAGIKAEIDYG-GRKLKKQFKYADRSGARFAVILGEDELAAGVVTVKDLETGEQE 79
|
90
....*....|..
gi 70794762 488 DVRREDLVEEIR 499
Cdd:cd00859 80 TVALDELVEELK 91
|
|
| hisZ |
PRK12295 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
70-389 |
9.59e-23 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 183413 [Multi-domain] Cd Length: 373 Bit Score: 99.62 E-value: 9.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 70 MAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLTGKYGED-SKLIYDLKDQGGELLSLRYDLTVPFAR-YLAMNKLTNI 147
Cdd:PRK12295 4 LSASAAAAEALLASFEAAGAVRVDPPILQPAEPFLDLSGEDiRRRIFVTSDENGEELCLRPDFTIPVCRrHIATAGGEPA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 148 KRYHIAKVYRRdnpamTRGRYREFYQCDFDIAGQFDPMIPDAECLKIMCEILSSLQIGNFQVKVNDRRILDGMFAVCGVP 227
Cdd:PRK12295 84 RYAYLGEVFRQ-----RRDRASEFLQAGIESFGRADPAAADAEVLALALEALAALGPGDLEVRLGDVGLFAALVDALGLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 228 DS-KFRTIcssVDKLDKVSWEEVKNEMVGEKGLAPEVADRIGDYVQQHGGVS-LVEQLLQDPKLSQNK------------ 293
Cdd:PRK12295 159 PGwKRRLL---RHFGRPRSLDALLARLAGPRVDPLDEHAGVLAALADEAAARaLVEDLMSIAGISPVGgrspaeiarrll 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 294 -----QAVEGLGD--LKLLFEYLTL--------------------------------------FGID-DKISFDLSLARG 327
Cdd:PRK12295 236 ekaalAAAARLPAeaLAVLERFLAIsgppdaalaalralaadagldldaaldrfearlaalaaRGIDlERLRFSASFGRP 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 70794762 328 LDYYTGVIYEAVLlqmpTQAGEEPLgvgsiAAGGRYDGLVGMFDpKGRKVPCVGLSIGVERI 389
Cdd:PRK12295 316 LDYYTGFVFEIRA----AGNGDPPL-----AGGGRYDGLLTRLG-AGEPIPAVGFSIWLDRL 367
|
|
| HisRS_RNA |
cd00938 |
HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS ... |
5-49 |
6.12e-17 |
|
HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). This domain consists of a helix- turn- helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238474 [Multi-domain] Cd Length: 45 Bit Score: 74.43 E-value: 6.12e-17
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 70794762 5 AALEELVRLQGAHVRGLKEQKASAEQIEEEVTKLLKLKAQLGHDE 49
Cdd:cd00938 1 AKLEEAVKLQGELVRKLKAEKASKEQIAEEVAKLLELKAQLGGDE 45
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
410-501 |
6.60e-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: 75.70 E-value: 6.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 410 QVLVASAQKK---LLEERLKLISELWDAGIKAELLYKkNPKLLNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREE 486
Cdd:pfam03129 1 QVVVIPLGEKaeeLEEYAQKLAEELRAAGIRVELDDR-NESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQ 79
|
90
....*....|....*
gi 70794762 487 VDVRREDLVEEIRRR 501
Cdd:pfam03129 80 ETVSLDELVEKLKEL 94
|
|
| PRK12421 |
PRK12421 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
59-435 |
2.80e-11 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 237098 Cd Length: 392 Bit Score: 65.38 E-value: 2.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 59 PKGTRDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLTGKYGEDSKL-IYDLKDQ-GGELLSLRYDLTVPFA 136
Cdd:PRK12421 10 PDGVADVLPEEAQKIERLRRRLLDLFASRGYQLVMPPLIEYLESLLTGAGQDLKLqTFKLIDQlSGRLMGVRADITPQVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 137 RYLA-MNKLTNIKRY-HIAKVY--RRDNPAMTRGRYR---EFYQCDfDIAGqfdpmipDAECLKIMCEILSSLQIGNFQV 209
Cdd:PRK12421 90 RIDAhLLNREGVARLcYAGSVLhtLPQGLFGSRTPLQlgaELYGHA-GIEA-------DLEIIRLMLGLLRNAGVPALHL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 210 KVNDRRILDGMFAVCGVPDSKFRTIcssVDKLDKVSWEEVKnEMVGEKGLAPEVADRIGDYVQQHGGVSLVEQLLQDpKL 289
Cdd:PRK12421 162 DLGHVGIFRRLAELAGLSPEEEEEL---FDLLQRKALPELA-EVCQNLGVGSDLRRMFYALARLNGGLEALDRALSV-LA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 290 SQNKQAVEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYeAVLLQMPTQAgeeplgvgsIAAGGRYDGLVGM 369
Cdd:PRK12421 237 LQDAAIRQALDELKTLAAHLKNRWPELPVSIDLAELRGYHYHTGLVF-AAYIPGRGQA---------LARGGRYDGIGEA 306
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 70794762 370 FdpkGRKVPCVGLSIGVERIfsIVEQKLEASEEKVrttetqVLVASAQKKLLEErlklISELWDAG 435
Cdd:PRK12421 307 F---GRARPATGFSMDLKEL--LALQFLEEEAGAI------LAPWGDDPDLLAA----IAELRQQG 357
|
|
| WHEP-TRS |
smart00991 |
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ... |
8-63 |
1.05e-10 |
|
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: 56.97 E-value: 1.05e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 70794762 8 EELVRLQGAHVRGLKEQKASAEQIEEEVTKLLKLKAQLGHDEGKQKFVLKTPKGTR 63
Cdd:smart00991 1 EEAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLKEATGQDYKPGAPPGDTP 56
|
|
| WHEPGMRS_RNA |
cd01200 |
EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher ... |
8-49 |
1.16e-10 |
|
EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in three copies in the mammalian bifunctional EPRS in a region that separates the N-terminal GluRS from the C-terminal ProRS. In the Drosophila EPRS, this domain is repeated six times. It is found at the N-terminus of TrpRS, HisRS and GlyR and at the C-terminus of MetRS. This domain consists of a helix- turn- helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238605 [Multi-domain] Cd Length: 42 Bit Score: 56.39 E-value: 1.16e-10
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 70794762 8 EELVRLQGAHVRGLKEQKASAEQIEEEVTKLLKLKAQLGHDE 49
Cdd:cd01200 1 YEKIAEQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKEAT 42
|
|
| WHEP-TRS |
pfam00458 |
WHEP-TRS domain; |
7-51 |
3.29e-09 |
|
WHEP-TRS domain;
Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 52.50 E-value: 3.29e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 70794762 7 LEELVRLQGAHVRGLKEQKASAEQIEEEVTKLLKLKAQLGHDEGK 51
Cdd:pfam00458 1 LTEKIKAQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKALTGK 45
|
|
| HGTP_anticodon2 |
pfam12745 |
Anticodon binding domain of tRNAs; This is an HGTP_anticodon binding domain, found largely on ... |
411-501 |
2.11e-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: 55.30 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 411 VLVASAQKKLL-EERLKLISELWDAGIKAELLYKKNPKLLNQLQYCEEAGIPLVAIIGEQELKDG----VIKLRSVTSRE 485
Cdd:pfam12745 8 VLVASFDASILrTTGVEILQELWAHGISADLAVDASYSPEDLVSRARDDGVSWIVIIKQQNKSSDskykPLKVKNLLRKE 87
|
90 100
....*....|....*....|
gi 70794762 486 EVDVRREDLV----EEIRRR 501
Cdd:pfam12745 88 DVDLDSDELVswlrGEIRER 107
|
|
| MetRS_RNA |
cd00939 |
MetRS_RNA binding domain. This short RNA-binding domain is found at the C-terminus of MetRS in ... |
7-51 |
2.38e-07 |
|
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: 47.08 E-value: 2.38e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 70794762 7 LEELVRLQGAHVRGLKEQKASAEQIEEEVTKLLKLKAQLGHDEGK 51
Cdd:cd00939 1 LEKEVAEQGNKVRKLKASKADKSVWQPEVNKLLDLKKQLALAEGK 45
|
|
| PRK03991 |
PRK03991 |
threonyl-tRNA synthetase; Validated |
385-503 |
9.31e-06 |
|
threonyl-tRNA synthetase; Validated
Pssm-ID: 235190 [Multi-domain] Cd Length: 613 Bit Score: 48.33 E-value: 9.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 385 GVER-IFSIVE-QKLEASEEKVRT-----TETQVLVASAQKKLLEERLKLISELWDAGIKAEL------LYKKnpkllnq 451
Cdd:PRK03991 469 SIERvIYALLEkAAKEEEEGKVPMlptwlSPTQVRVIPVSERHLDYAEEVADKLEAAGIRVDVddrdesLGKK------- 541
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 70794762 452 lqyCEEAG---IPLVAIIGEQELKDGVIklrSVTSREE---VDVRREDLVEEIRRRTS 503
Cdd:PRK03991 542 ---IRDAGkewIPYVVVIGDKEMESGKL---TVTIREEsekVEMTLEELIERIKEETK 593
|
|
| WEPRS_RNA |
cd00936 |
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ... |
14-44 |
8.57e-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: 8.57e-05
10 20 30
....*....|....*....|....*....|.
gi 70794762 14 QGAHVRGLKEQKASAEQIEEEVTKLLKLKAQ 44
Cdd:cd00936 8 QGDLVRELKAKKAPKEEIDAAVKKLLALKAD 38
|
|
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
5-88 |
4.03e-03 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 39.73 E-value: 4.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 5 AALEELVRLQGAHVRGLKEQKASAEQIEEEVTKLLKLKAQLghdEGKQKFVLKTPKGTRDYSPRQMAVREKVFDVIIR-- 82
Cdd:PLN02734 10 AEKQAAVTAQGNAVRALKASKADKAEIDAAIEKLKALKLEK---SALEKELQAAVGAGGDGAASKEAFRQAVVNTLERrl 86
|
90
....*....|
gi 70794762 83 ----CFKRHG 88
Cdd:PLN02734 87 fyipSFKIYG 96
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
72-202 |
6.82e-03 |
|
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA synthetases (aaRS) share a common fold and generally attach an amino acid to the 3' OH of ribose of the appropriate tRNA. PheRS is an exception in that it attaches the amino acid at the 2'-OH group, like class I aaRSs. These enzymes are usually homodimers. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. The substrate specificity of this reaction is further determined by additional domains. Intererestingly, this domain is also found is asparagine synthase A (AsnA), in the accessory subunit of mitochondrial polymerase gamma and in the bacterial ATP phosphoribosyltransferase regulatory subunit HisZ.
Pssm-ID: 238391 [Multi-domain] Cd Length: 211 Bit Score: 37.87 E-value: 6.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70794762 72 VREKVFDVIIRCFKRHGAEVIDTPVFElKETLTGKYGEDSKLIYDLKDQGGELLSLRYDLTvPFARYLAMNKLTNI--KR 149
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVE-REPLLEKAGHEPKDLLPVGAENEEDLYLRPTLE-PGLVRLFVSHIRKLplRL 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 70794762 150 YHIAKVYRRDNPAMTRGRYREFYQCDFDIAG-QFDPMIPDAECLKIMCEILSSL 202
Cdd:cd00768 79 AEIGPAFRNEGGRRGLRRVREFTQLEGEVFGeDGEEASEFEELIELTEELLRAL 132
|
|
| |
