|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02972 |
PLN02972 |
Histidyl-tRNA synthetase |
57-511 |
0e+00 |
|
Histidyl-tRNA synthetase
Pssm-ID: 215525 [Multi-domain] Cd Length: 763 Bit Score: 568.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 57 KTAKGTRDYNPKQMAIREKVFNTIVSCFKRHGAETIDTPVFELKETLTGKYGEDSKLIYDLKDQGGELLSLRYDLTVPFA 136
Cdd:PLN02972 328 KIPKGTRDFAKEQMAIREKAFSIITSVFKRHGATALDTPVFELRETLMGKYGEDSKLIYDLADQGGELCSLRYDLTVPFA 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 137 RYLAMNKITNIKRYHIAKVYRRDNPamTRGRYREFYQCDFDIAGQYDAMIPDAECLKIVHEILSELDLGDFRIKVNDRRI 216
Cdd:PLN02972 408 RYVAMNGITSFKRYQIAKVYRRDNP--SKGRYREFYQCDFDIAGVYEPMGPDFEIIKVLTELLDELDIGTYEVKLNHRKL 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 217 LDGMFAVCGVPDNMFRTICSTVDKLDKLPWEAVKNEMVNEKGLSEEAADQIGVYVGMQGG-MDLAERLLQ-DQKMCQSTQ 294
Cdd:PLN02972 486 LDGMLEICGVPPEKFRTICSSIDKLDKQSFEQVKKEMVEEKGLSNETADKIGNFVKERGPpLELLSKLRQeGSEFLGNAS 565
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 295 ACAGLTDIKLLFSYLQLFQVTDKVVFDLSLARGLDYYTGIIYEAILTQAgvapvapetsneapteecvTVGSVAGGGRYD 374
Cdd:PLN02972 566 SRAALDELEIMFKALEKSKAIGKIVFDLSLARGLDYYTGVIYEAVFKGA-------------------QVGSIAAGGRYD 626
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 375 GLVGMFDpkGRKVPCVGVSIGIERIFSIMEQKAEASTEKIRTTEVQVMVAAAQKNLLEERLRLITELWNAGIKAElmYKK 454
Cdd:PLN02972 627 NLVGMFS--GKQVPAVGVSLGIERVFAIMEQQEEEKSQVIRPTETEVLVSIIGDDKLALAAELVSELWNAGIKAE--YKV 702
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 410927344 455 SPKLLSQLQHCEESGIPLVAILGEQELKNGVVKLRNVATRDEVDISRADLIAEIKKR 511
Cdd:PLN02972 703 STRKAKHLKRAKESGIPWMVLVGEKELSKGFVKLKNLEAGVEEEVDRTCFVQELKAE 759
|
|
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
56-511 |
5.54e-118 |
|
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: 353.66 E-value: 5.54e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 56 LKTAKGTRDYNPKQMAIREKVFNTIVSCFKRHGAETIDTPVFELKETLTGKYGED--SKLIYDLKDQGGELLSLRYDLTV 133
Cdd:COG0124 4 IQAPRGTRDILPEESAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKIGEDivEKEMYTFEDRGGRSLTLRPEGTA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 134 PFARYLAMNKITN---IKRYHIAKVYRRDNPAmtRGRYREFYQCDFDIAGQYDAMIpDAECLKIVHEILSELDLGDFRIK 210
Cdd:COG0124 84 PVARAVAEHGNELpfpFKLYYIGPVFRYERPQ--KGRYRQFHQFGVEVIGSDSPLA-DAEVIALAADLLKALGLKDFTLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 211 VNDRrildgmfavcGVPDNMFRTICSTVDKLDKLPWEAVknemvnekgLSEEAADQIGVYV----------GMQGGMDLA 280
Cdd:COG0124 161 INSR----------GLPEERAEALLRYLDKLDKIGHEDV---------LDEDSQRRLETNPlraildskgpDCQEVLADA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 281 ERLLqdQKMCQstqacAGLTDIKLLFSYLQLFQVtdKVVFDLSLARGLDYYTGIIYEAILTQAGVapvapetsneaptee 360
Cdd:COG0124 222 PKLL--DYLGE-----EGLAHFEEVLELLDALGI--PYVIDPRLVRGLDYYTGTVFEIVTDGLGA--------------- 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 361 cvtVGSVAGGGRYDGLVGMFDpkGRKVPCVGVSIGIERIFSIMEQKAEASTEKirtTEVQVMVAAAQKNLLEERLRLITE 440
Cdd:COG0124 278 ---QGSVCGGGRYDGLVEQLG--GPPTPAVGFAIGLERLLLLLEELGLLPAAE---PPPDVYVVPLGEEARAEALKLAQE 349
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 410927344 441 LWNAGIKAELMYK-KSPKllSQLQHCEESGIPLVAILGEQELKNGVVKLRNVATRDEVDISRADLIAEIKKR 511
Cdd:COG0124 350 LRAAGIRVELDLGgRKLK--KQLKYADKSGAPFVLILGEDELANGTVTLKDLATGEQETVPLDELVEYLKEL 419
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
69-404 |
1.24e-107 |
|
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: 321.47 E-value: 1.24e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 69 QMAIREKVFNTIVSCFKRHGAETIDTPVFELKETLTGKYGED-SKLIYDLKDQGGELLSLRYDLTVPFARYLAMNKI--- 144
Cdd:cd00773 1 EAALRRYIEDTLREVFERYGYEEIDTPVFEYTELFLRKSGDEvSKEMYRFKDKGGRDLALRPDLTAPVARAVAENLLslp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 145 TNIKRYHIAKVYRRDNPAmtRGRYREFYQCDFDIAGqYDAMIPDAECLKIVHEILSELDLGDFRIKVNDRRILDGmfaVC 224
Cdd:cd00773 81 LPLKLYYIGPVFRYERPQ--KGRYREFYQVGVEIIG-SDSPLADAEVIALAVEILEALGLKDFQIKINHRGILDG---IA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 225 GVPDNMFRTICSTVDKLDKlpweavknemvnekglseeaadqigvyvgmqggmdlaerllqdqkmcqstqacAGLTDIKL 304
Cdd:cd00773 155 GLLEDREEYIERLIDKLDK-----------------------------------------------------EALAHLEK 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 305 LFSYLQLFQVTDKVVFDLSLARGLDYYTGIIYEAILTQAGVapvapetsneapteecvtVGSVAGGGRYDGLVGMFDpkG 384
Cdd:cd00773 182 LLDYLEALGVDIKYSIDLSLVRGLDYYTGIVFEAVADGLGA------------------QGSIAGGGRYDGLLEEFG--G 241
|
330 340
....*....|....*....|
gi 410927344 385 RKVPCVGVSIGIERIFSIME 404
Cdd:cd00773 242 EDVPAVGFAIGLERLLLALE 261
|
|
| hisS |
TIGR00442 |
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ... |
60-501 |
1.18e-104 |
|
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: 1.18e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 60 KGTRDYNPKQMAIREKVFNTIVSCFKRHGAETIDTPVFELKETLTGKYGEDS----KLIYDLKDQGGELLSLRYDLTVPF 135
Cdd:TIGR00442 4 RGTRDFLPEEMIKWQYIEETIREVFERYGFKEIRTPIFEYTELFKRKVGEETdivsKEMYTFKDKGGRSLTLRPEGTAPV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 136 ARYLAMNKITN---IKRYHIAKVYRRDNPAmtRGRYREFYQCDFDIAGQYDAMIpDAECLKIVHEILSELDLGDFRIKVN 212
Cdd:TIGR00442 84 ARAVIENKLLLpkpFKLYYIGPMFRYERPQ--KGRYRQFHQFGVEVIGSDSPLA-DAEIIALAADILKELGLKDFTLEIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 213 DRRILDGMFAvcgvpdnmFR-TICSTVDK-LDKLPWEAVKNEMVNEKGLSEEAADQIgvyvgmQGGMDLAERLLQDQKMc 290
Cdd:TIGR00442 161 SLGILEGRLE--------YReALIRYLDKhKDKLGEDSVRRLEKNPLRILDSKNEKI------QELLKNAPKILDFLCE- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 291 qstqacAGLTDIKLLFSYLQLFQVtdKVVFDLSLARGLDYYTGIIYEAILTQAGVApvapetsneapteecvtvGSVAGG 370
Cdd:TIGR00442 226 ------ESRAHFEELKELLDALGI--PYKIDPSLVRGLDYYTGTVFEFVTDDLGAQ------------------GSICGG 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 371 GRYDGLVGMFDpkGRKVPCVGVSIGIERIFSIMEqkaEASTEKIRTTEVQVMVAAAQKNLLEERLRLITELWNAGIKAEL 450
Cdd:TIGR00442 280 GRYDGLVEELG--GPPTPAVGFAIGIERLILLLE---ELGLIPPPSKKPDVYVVPLGEEAELEALKLAQKLRKAGIRVEV 354
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 410927344 451 MYKKSpKLLSQLQHCEESGIPLVAILGEQELKNGVVKLRNVATRDEVDISR 501
Cdd:TIGR00442 355 DLGGR-KLKKQLKYADKLGARFALIIGEDELENGTVTLKDLETGEQETVPL 404
|
|
| tRNA-synt_His |
pfam13393 |
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ... |
61-399 |
1.33e-44 |
|
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: 159.29 E-value: 1.33e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 61 GTRDYNPKQMAIREKVFNTIVSCFKRHGAETIDTPVFELKETLTGKYGEDSKLIYDLKDQGGELLSLRYDLTVPFARYLA 140
Cdd:pfam13393 1 GIRDLLPPEARRIEELRRRLLDLFRSWGYELVMPPLLEYLDSLLTGTGADLDQTFKLVDQSGRLLGLRADITPQVARIDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 141 --MNKITNIKRYHIAKVYRRDNPAMtrGRYREFYQCDFDIAGqYDAMIPDAECLKIVHEILSELDLGDFRIKVNDRRILD 218
Cdd:pfam13393 81 hrLNRPGPLRLCYAGSVLRTRPKGL--GRSREPLQVGAELIG-HAGIEADAEIISLLLEALAAAGVPGVTLDLGHVGLVR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 219 GMFAVCGVPDNMFRTICSTVDKLDklpWEAVKnEMVNEKGLSEEAADQIGVYVGMQGGMDLAERLLQDqkMCQSTQACAG 298
Cdd:pfam13393 158 ALLEAAGLSEALEEALRAALQRKD---AAELA-ELAAEAGLPPALRRALLALPDLYGGPEVLDEARAA--LPGLPALQEA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 299 LTDIKLLFSYLQLFQVTDKVVFDLSLARGLDYYTGIIYEAiltqagvapVAPETSNEapteecvtvgsVAGGGRYDGLVG 378
Cdd:pfam13393 232 LDELEALAALLEALGDGVRLTFDLAELRGYEYYTGIVFAA---------YAPGVGEP-----------LARGGRYDDLGA 291
|
330 340
....*....|....*....|.
gi 410927344 379 MFdpkGRKVPCVGVSIGIERI 399
Cdd:pfam13393 292 AF---GRARPATGFSLDLEAL 309
|
|
| HisRS_RNA |
cd00938 |
HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS ... |
5-49 |
2.61e-19 |
|
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: 80.98 E-value: 2.61e-19
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 410927344 5 AQIQEAIKCQGEVVRKLKAEKASKEQIDEEVAKLLELKAHLGGDD 49
Cdd:cd00938 1 AKLEEAVKLQGELVRKLKAEKASKEQIAEEVAKLLELKAQLGGDE 45
|
|
| WHEP-TRS |
pfam00458 |
WHEP-TRS domain; |
7-69 |
1.17e-14 |
|
WHEP-TRS domain;
Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 68.29 E-value: 1.17e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 410927344 7 IQEAIKCQGEVVRKLKAEKASKEQIDEEVAKLLELKAHlggddgkhqfvLKTAKGTrDYNPKQ 69
Cdd:pfam00458 1 LTEKIKAQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQ-----------YKALTGK-DYKPGA 51
|
|
| WHEP-TRS |
smart00991 |
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ... |
8-51 |
8.19e-13 |
|
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: 63.13 E-value: 8.19e-13
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 410927344 8 QEAIKCQGEVVRKLKAEKASKEQIDEEVAKLLELKAHLGGDDGK 51
Cdd:smart00991 1 EEAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLKEATGQ 44
|
|
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
1-88 |
3.46e-06 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 49.74 E-value: 3.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 1 MDDKAQIQEAIKCQGEVVRKLKAEKASKEQIDEEVAKLLELKAHLGGDDGKHQfvlKTAKGTRDYNPKQMAIREKVFNTI 80
Cdd:PLN02734 6 RDALAEKQAAVTAQGNAVRALKASKADKAEIDAAIEKLKALKLEKSALEKELQ---AAVGAGGDGAASKEAFRQAVVNTL 82
|
90
....*....|....
gi 410927344 81 ------VSCFKRHG 88
Cdd:PLN02734 83 errlfyIPSFKIYG 96
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02972 |
PLN02972 |
Histidyl-tRNA synthetase |
57-511 |
0e+00 |
|
Histidyl-tRNA synthetase
Pssm-ID: 215525 [Multi-domain] Cd Length: 763 Bit Score: 568.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 57 KTAKGTRDYNPKQMAIREKVFNTIVSCFKRHGAETIDTPVFELKETLTGKYGEDSKLIYDLKDQGGELLSLRYDLTVPFA 136
Cdd:PLN02972 328 KIPKGTRDFAKEQMAIREKAFSIITSVFKRHGATALDTPVFELRETLMGKYGEDSKLIYDLADQGGELCSLRYDLTVPFA 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 137 RYLAMNKITNIKRYHIAKVYRRDNPamTRGRYREFYQCDFDIAGQYDAMIPDAECLKIVHEILSELDLGDFRIKVNDRRI 216
Cdd:PLN02972 408 RYVAMNGITSFKRYQIAKVYRRDNP--SKGRYREFYQCDFDIAGVYEPMGPDFEIIKVLTELLDELDIGTYEVKLNHRKL 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 217 LDGMFAVCGVPDNMFRTICSTVDKLDKLPWEAVKNEMVNEKGLSEEAADQIGVYVGMQGG-MDLAERLLQ-DQKMCQSTQ 294
Cdd:PLN02972 486 LDGMLEICGVPPEKFRTICSSIDKLDKQSFEQVKKEMVEEKGLSNETADKIGNFVKERGPpLELLSKLRQeGSEFLGNAS 565
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 295 ACAGLTDIKLLFSYLQLFQVTDKVVFDLSLARGLDYYTGIIYEAILTQAgvapvapetsneapteecvTVGSVAGGGRYD 374
Cdd:PLN02972 566 SRAALDELEIMFKALEKSKAIGKIVFDLSLARGLDYYTGVIYEAVFKGA-------------------QVGSIAAGGRYD 626
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 375 GLVGMFDpkGRKVPCVGVSIGIERIFSIMEQKAEASTEKIRTTEVQVMVAAAQKNLLEERLRLITELWNAGIKAElmYKK 454
Cdd:PLN02972 627 NLVGMFS--GKQVPAVGVSLGIERVFAIMEQQEEEKSQVIRPTETEVLVSIIGDDKLALAAELVSELWNAGIKAE--YKV 702
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 410927344 455 SPKLLSQLQHCEESGIPLVAILGEQELKNGVVKLRNVATRDEVDISRADLIAEIKKR 511
Cdd:PLN02972 703 STRKAKHLKRAKESGIPWMVLVGEKELSKGFVKLKNLEAGVEEEVDRTCFVQELKAE 759
|
|
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
56-511 |
5.54e-118 |
|
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: 353.66 E-value: 5.54e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 56 LKTAKGTRDYNPKQMAIREKVFNTIVSCFKRHGAETIDTPVFELKETLTGKYGED--SKLIYDLKDQGGELLSLRYDLTV 133
Cdd:COG0124 4 IQAPRGTRDILPEESAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKIGEDivEKEMYTFEDRGGRSLTLRPEGTA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 134 PFARYLAMNKITN---IKRYHIAKVYRRDNPAmtRGRYREFYQCDFDIAGQYDAMIpDAECLKIVHEILSELDLGDFRIK 210
Cdd:COG0124 84 PVARAVAEHGNELpfpFKLYYIGPVFRYERPQ--KGRYRQFHQFGVEVIGSDSPLA-DAEVIALAADLLKALGLKDFTLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 211 VNDRrildgmfavcGVPDNMFRTICSTVDKLDKLPWEAVknemvnekgLSEEAADQIGVYV----------GMQGGMDLA 280
Cdd:COG0124 161 INSR----------GLPEERAEALLRYLDKLDKIGHEDV---------LDEDSQRRLETNPlraildskgpDCQEVLADA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 281 ERLLqdQKMCQstqacAGLTDIKLLFSYLQLFQVtdKVVFDLSLARGLDYYTGIIYEAILTQAGVapvapetsneaptee 360
Cdd:COG0124 222 PKLL--DYLGE-----EGLAHFEEVLELLDALGI--PYVIDPRLVRGLDYYTGTVFEIVTDGLGA--------------- 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 361 cvtVGSVAGGGRYDGLVGMFDpkGRKVPCVGVSIGIERIFSIMEQKAEASTEKirtTEVQVMVAAAQKNLLEERLRLITE 440
Cdd:COG0124 278 ---QGSVCGGGRYDGLVEQLG--GPPTPAVGFAIGLERLLLLLEELGLLPAAE---PPPDVYVVPLGEEARAEALKLAQE 349
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 410927344 441 LWNAGIKAELMYK-KSPKllSQLQHCEESGIPLVAILGEQELKNGVVKLRNVATRDEVDISRADLIAEIKKR 511
Cdd:COG0124 350 LRAAGIRVELDLGgRKLK--KQLKYADKSGAPFVLILGEDELANGTVTLKDLATGEQETVPLDELVEYLKEL 419
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
69-404 |
1.24e-107 |
|
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: 321.47 E-value: 1.24e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 69 QMAIREKVFNTIVSCFKRHGAETIDTPVFELKETLTGKYGED-SKLIYDLKDQGGELLSLRYDLTVPFARYLAMNKI--- 144
Cdd:cd00773 1 EAALRRYIEDTLREVFERYGYEEIDTPVFEYTELFLRKSGDEvSKEMYRFKDKGGRDLALRPDLTAPVARAVAENLLslp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 145 TNIKRYHIAKVYRRDNPAmtRGRYREFYQCDFDIAGqYDAMIPDAECLKIVHEILSELDLGDFRIKVNDRRILDGmfaVC 224
Cdd:cd00773 81 LPLKLYYIGPVFRYERPQ--KGRYREFYQVGVEIIG-SDSPLADAEVIALAVEILEALGLKDFQIKINHRGILDG---IA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 225 GVPDNMFRTICSTVDKLDKlpweavknemvnekglseeaadqigvyvgmqggmdlaerllqdqkmcqstqacAGLTDIKL 304
Cdd:cd00773 155 GLLEDREEYIERLIDKLDK-----------------------------------------------------EALAHLEK 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 305 LFSYLQLFQVTDKVVFDLSLARGLDYYTGIIYEAILTQAGVapvapetsneapteecvtVGSVAGGGRYDGLVGMFDpkG 384
Cdd:cd00773 182 LLDYLEALGVDIKYSIDLSLVRGLDYYTGIVFEAVADGLGA------------------QGSIAGGGRYDGLLEEFG--G 241
|
330 340
....*....|....*....|
gi 410927344 385 RKVPCVGVSIGIERIFSIME 404
Cdd:cd00773 242 EDVPAVGFAIGLERLLLALE 261
|
|
| hisS |
TIGR00442 |
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ... |
60-501 |
1.18e-104 |
|
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: 1.18e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 60 KGTRDYNPKQMAIREKVFNTIVSCFKRHGAETIDTPVFELKETLTGKYGEDS----KLIYDLKDQGGELLSLRYDLTVPF 135
Cdd:TIGR00442 4 RGTRDFLPEEMIKWQYIEETIREVFERYGFKEIRTPIFEYTELFKRKVGEETdivsKEMYTFKDKGGRSLTLRPEGTAPV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 136 ARYLAMNKITN---IKRYHIAKVYRRDNPAmtRGRYREFYQCDFDIAGQYDAMIpDAECLKIVHEILSELDLGDFRIKVN 212
Cdd:TIGR00442 84 ARAVIENKLLLpkpFKLYYIGPMFRYERPQ--KGRYRQFHQFGVEVIGSDSPLA-DAEIIALAADILKELGLKDFTLEIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 213 DRRILDGMFAvcgvpdnmFR-TICSTVDK-LDKLPWEAVKNEMVNEKGLSEEAADQIgvyvgmQGGMDLAERLLQDQKMc 290
Cdd:TIGR00442 161 SLGILEGRLE--------YReALIRYLDKhKDKLGEDSVRRLEKNPLRILDSKNEKI------QELLKNAPKILDFLCE- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 291 qstqacAGLTDIKLLFSYLQLFQVtdKVVFDLSLARGLDYYTGIIYEAILTQAGVApvapetsneapteecvtvGSVAGG 370
Cdd:TIGR00442 226 ------ESRAHFEELKELLDALGI--PYKIDPSLVRGLDYYTGTVFEFVTDDLGAQ------------------GSICGG 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 371 GRYDGLVGMFDpkGRKVPCVGVSIGIERIFSIMEqkaEASTEKIRTTEVQVMVAAAQKNLLEERLRLITELWNAGIKAEL 450
Cdd:TIGR00442 280 GRYDGLVEELG--GPPTPAVGFAIGIERLILLLE---ELGLIPPPSKKPDVYVVPLGEEAELEALKLAQKLRKAGIRVEV 354
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 410927344 451 MYKKSpKLLSQLQHCEESGIPLVAILGEQELKNGVVKLRNVATRDEVDISR 501
Cdd:TIGR00442 355 DLGGR-KLKKQLKYADKLGARFALIIGEDELENGTVTLKDLETGEQETVPL 404
|
|
| PRK12420 |
PRK12420 |
histidyl-tRNA synthetase; Provisional |
55-500 |
5.08e-83 |
|
histidyl-tRNA synthetase; Provisional
Pssm-ID: 237097 [Multi-domain] Cd Length: 423 Bit Score: 263.90 E-value: 5.08e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 55 VLKTAKGTRDYNPKQMAIREKVFNTIVSCFKRHGAETIDTPVFELKETLTGKYG---EDSKLIYDLKDQGGELLSLRYDL 131
Cdd:PRK12420 3 EMRNVKGTKDYLPEEQVLRNKIKRALEDVFERYGCKPLETPTLNMYELMSSKYGggdEILKEIYTLTDQGKRDLALRYDL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 132 TVPFARYLAMNKitNI----KRYHIAKVYrRDNPaMTRGRYREFYQCDFDIAGqYDAMIPDAECLKIVHEILSELDLgDF 207
Cdd:PRK12420 83 TIPFAKVVAMNP--NIrlpfKRYEIGKVF-RDGP-IKQGRFREFIQCDVDIVG-VESVMAEAELMSMAFELFRRLNL-EV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 208 RIKVNDRRILDGMFAVCGVPDNMFRTICSTVDKLDKLPWEAVKNEmVNEKGLSEEAADQIGVYVGMQGGMDLAERllqdQ 287
Cdd:PRK12420 157 TIQYNNRKLLNGILQAIGIPTELTSDVILSLDKIEKIGIDGVRKD-LLERGISEEMADTICNTVLSCLQLSIADF----K 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 288 KMCQSTQACAGLTDIKLLFSYLQLFQVTDKVVFDLSLARGLDYYTGIIYEAILTQAGVApvapetsneapteecvtvGSV 367
Cdd:PRK12420 232 EAFNNPLVAEGVNELQQLQQYLIALGINENCIFNPFLARGLTMYTGTVYEIFLKDGSIT------------------SSI 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 368 AGGGRYDGLVGMFDPKGRKVPCVGVSIGIERIFSIMEQKAE-ASTEKIRTTEVQVMVAAAQknlLEERLRLITelwnaGI 446
Cdd:PRK12420 294 GSGGRYDNIIGAFRGDDMNYPTVGISFGLDVIYTALSQKETiSSTADVFIIPLGTELQCLQ---IAQQLRSTT-----GL 365
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 410927344 447 KAELMYKKSpKLLSQLQHCEESGIPLVAILGEQELKNGVVKLRNVATRDEVDIS 500
Cdd:PRK12420 366 KVELELAGR-KLKKALNYANKENIPYVLIIGEEEVSTGTVMLRNMKEGSEVKVP 418
|
|
| PLN02530 |
PLN02530 |
histidine-tRNA ligase |
49-505 |
7.68e-55 |
|
histidine-tRNA ligase
Pssm-ID: 178145 [Multi-domain] Cd Length: 487 Bit Score: 191.49 E-value: 7.68e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 49 DGKHQFVLKTAKGTRDYNPKQMAIREKVFNTIVSCFKRHGAETIDTPVFELKETLTGKYGED-SKLIYDLKDQGGELLSL 127
Cdd:PLN02530 63 DGKPKIDVNPPKGTRDFPPEDMRLRNWLFDHFREVSRLFGFEEVDAPVLESEELYIRKAGEEiTDQLYNFEDKGGRRVAL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 128 RYDLTVPFARyLAMNKITNI----KRYHIAKVYRRDNpaMTRGRYREFYQCDFDIAGqYDAMIPDAECLKIVHEILSELD 203
Cdd:PLN02530 143 RPELTPSLAR-LVLQKGKSLslplKWFAIGQCWRYER--MTRGRRREHYQWNMDIIG-VPGVEAEAELLAAIVTFFKRVG 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 204 L--GDFRIKVNDRRILDGMFAVCGVPDNMFRTICSTVDKLDKLPWEAVKNEMvNEKGLSEEAADQIGVYVGMQGGMDLAE 281
Cdd:PLN02530 219 ItsSDVGIKVSSRKVLQAVLKSYGIPEESFAPVCVIVDKLEKLPREEIEKEL-DTLGVSEEAIEGILDVLSLKSLDDLEA 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 282 RLLQDQKmcqstqacaGLTDIKLLFSYLQLFQVTDKVVFDLSLARGLDYYTGIIYEAiLTQAGVapvapetsneapteec 361
Cdd:PLN02530 298 LLGADSE---------AVADLKQLFSLAEAYGYQDWLVFDASVVRGLAYYTGIVFEG-FDRAGK---------------- 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 362 vtVGSVAGGGRYDGLVGMFDpkGRKVPCVGVSIGIERIFSIMEQKAEASTEkirTTEVQVMVAAAQKNLLEERLRLITEL 441
Cdd:PLN02530 352 --LRAICGGGRYDRLLSTFG--GEDTPACGFGFGDAVIVELLKEKGLLPEL---PHQVDDVVFALDEDLQGAAAGVASRL 424
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 410927344 442 WNAGIKAELMYKKSpKLLSQLQHCEESGIPLVAILGEQELKNGVVKLRNVATRDEVDISRADLI 505
Cdd:PLN02530 425 REKGRSVDLVLEPK-KLKWVFKHAERIGAKRLVLVGASEWERGMVRVKDLSSGEQTEVKLDELE 487
|
|
| hisZ_biosyn_reg |
TIGR00443 |
ATP phosphoribosyltransferase, regulatory subunit; Apparant second copies of histidyl-tRNA ... |
63-404 |
1.77e-48 |
|
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: 169.72 E-value: 1.77e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 63 RDYNPKQMAIREKVFNTIVSCFKRHGAETIDTPVFELKETLTGKYGEDSKLIYDLKDQGGELLSLRYDLTVPFARyLAMN 142
Cdd:TIGR00443 1 RDLLPEEAARKEEIERQLQDVFRSWGYQEIITPTLEYLDTLSAGSGILNEDLFKLFDQLGRVLGLRPDMTAPIAR-LVST 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 143 KITNIKR----YHIAKVYRRDNPAmtRGRYREFYQCDFDIAGqYDAMIPDAECLKIVHEILSELDLGDFRIKVNDRRILD 218
Cdd:TIGR00443 80 RLRDRPLplrlCYAGNVFRTNESG--GGRSREFTQAGVELIG-AGGPAADAEVIALLIEALKALGLKDFKIELGHVGLVR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 219 GMFAVCGVPDNMFRTIcstVDKLDKLPWEAVKnEMVNEKGLSEEAAD---QIGVYVGmqGGMDLAERLlqdQKMCQSTQA 295
Cdd:TIGR00443 157 ALLEEAGLPEEAREAL---REALARKDLVALE-ELVAELGLSPEVRErllALPRLRG--DGEEVLEEA---RALAGSETA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 296 CAGLTDIKLLFSYLQLFQVTDKVVFDLSLARGLDYYTGIIYEAILTQAGVApvapetsneapteecvtvgsVAGGGRYDG 375
Cdd:TIGR00443 228 EAALDELEAVLELLEARGVEEYISLDLGLVRGYHYYTGLIFEGYAPGLGAP--------------------LAGGGRYDE 287
|
330 340
....*....|....*....|....*....
gi 410927344 376 LVGMFdpkGRKVPCVGVSIGIERIFSIME 404
Cdd:TIGR00443 288 LLGRF---GRPLPATGFALNLERLLEALT 313
|
|
| hisZ |
PRK12292 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
59-450 |
1.78e-45 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 237043 [Multi-domain] Cd Length: 391 Bit Score: 163.88 E-value: 1.78e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 59 AKGTRDYNPKQMAIREKVFNTIVSCFKRHGAETIDTPVFELKETLT--GKYGEDSKLIYDLKDQGGELLSLRYDLTVPFA 136
Cdd:PRK12292 6 PEGIRDLLPEEARKIEEIRRRLLDLFRRWGYEEVITPTLEYLDTLLagGGAILDLRTFKLVDQLSGRTLGLRPDMTAQIA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 137 RYLA--MNKITNIKR-YHIAKVYRrdNPAMTRGRYREFYQCDFDIAGqYDAMIPDAECLKIVHEILSELDLGDFRIKVND 213
Cdd:PRK12292 86 RIAAtrLANRPGPLRlCYAGNVFR--AQERGLGRSREFLQSGVELIG-DAGLEADAEVILLLLEALKALGLPNFTLDLGH 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 214 RRILDGMFAVCGVPDNMFRTICSTVDKLDKLpweAVKnEMVneKGLSEEAADQIGVYVGMQGGMD---LAERLLQDQKmc 290
Cdd:PRK12292 163 VGLFRALLEAAGLSEELEEVLRRALANKDYV---ALE-ELV--LDLSEELRDALLALPRLRGGREvleEARKLLPSLP-- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 291 qstqACAGLTDIKLLFSYLQLFQVTDKVVFDLSLARGLDYYTGIIYEAILTQAGVApvapetsneapteecvtvgsVAGG 370
Cdd:PRK12292 235 ----IKRALDELEALAEALEKYGYGIPLSLDLGLLRHLDYYTGIVFEGYVDGVGNP--------------------IASG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 371 GRYDGLVGMFdpkGRKVPCVGVSIGIERifsIMEQKAEASTEKIRttevqVMVAAAQKNLLEERLRLITELWNAGIKAEL 450
Cdd:PRK12292 291 GRYDDLLGRF---GRARPATGFSLDLDR---LLELQLELPVEARK-----DLVIAPDSEALAAALAAAQELRKKGEIVVL 359
|
|
| HisZ |
COG3705 |
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism]; |
67-405 |
9.17e-45 |
|
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism];
Pssm-ID: 442919 [Multi-domain] Cd Length: 312 Bit Score: 159.57 E-value: 9.17e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 67 PKQMAIREKVFNTIVSCFKRHGAETIDTPVFELKETLTGKYGEDSKL-IYDLKDQGGELLSLRYDLTVPFARYLAmNKIT 145
Cdd:COG3705 2 PEEAARKEELRRRLLDVFRSWGYELVEPPLLEYLDSLLTGSGADLDLqTFKLVDQLGRTLGLRPDMTPQVARIAA-TRLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 146 NIKR----YHIAKVYRrdNPAMTRGRYREFYQCDFDIAGqYDAMIPDAECLKIVHEILSELDLGDFRIKVNDRRILDGMF 221
Cdd:COG3705 81 NRPGplrlCYAGNVFR--TRPSGLGRSREFLQAGAELIG-HAGLEADAEVIALALEALKAAGLEDFTLDLGHVGLFRALL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 222 AVCGVPDNMFRTICSTVDKLDKLpweAVKnEMVNEKGLSEEAADQIGVYVGMQGGMDLAERLlqdQKMCQSTQACAGLTD 301
Cdd:COG3705 158 EALGLSEEQREELRRALARKDAV---ELE-ELLAELGLSEELAEALLALPELYGGEEVLARA---RALLLDAAIRAALDE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 302 IKLLFSYLQLFQVTDKVVFDLSLARGLDYYTGIIYEAILTQAGVApvapetsneapteecvtvgsVAGGGRYDGLVGMFd 381
Cdd:COG3705 231 LEALAEALAARGPDVRLTFDLSELRGYDYYTGIVFEAYAPGVGDP--------------------LARGGRYDGLLAAF- 289
|
330 340
....*....|....*....|....
gi 410927344 382 pkGRKVPCVGVSIGIERIFSIMEQ 405
Cdd:COG3705 290 --GRARPATGFSLDLDRLLRALPA 311
|
|
| tRNA-synt_His |
pfam13393 |
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ... |
61-399 |
1.33e-44 |
|
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: 159.29 E-value: 1.33e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 61 GTRDYNPKQMAIREKVFNTIVSCFKRHGAETIDTPVFELKETLTGKYGEDSKLIYDLKDQGGELLSLRYDLTVPFARYLA 140
Cdd:pfam13393 1 GIRDLLPPEARRIEELRRRLLDLFRSWGYELVMPPLLEYLDSLLTGTGADLDQTFKLVDQSGRLLGLRADITPQVARIDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 141 --MNKITNIKRYHIAKVYRRDNPAMtrGRYREFYQCDFDIAGqYDAMIPDAECLKIVHEILSELDLGDFRIKVNDRRILD 218
Cdd:pfam13393 81 hrLNRPGPLRLCYAGSVLRTRPKGL--GRSREPLQVGAELIG-HAGIEADAEIISLLLEALAAAGVPGVTLDLGHVGLVR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 219 GMFAVCGVPDNMFRTICSTVDKLDklpWEAVKnEMVNEKGLSEEAADQIGVYVGMQGGMDLAERLLQDqkMCQSTQACAG 298
Cdd:pfam13393 158 ALLEAAGLSEALEEALRAALQRKD---AAELA-ELAAEAGLPPALRRALLALPDLYGGPEVLDEARAA--LPGLPALQEA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 299 LTDIKLLFSYLQLFQVTDKVVFDLSLARGLDYYTGIIYEAiltqagvapVAPETSNEapteecvtvgsVAGGGRYDGLVG 378
Cdd:pfam13393 232 LDELEALAALLEALGDGVRLTFDLAELRGYEYYTGIVFAA---------YAPGVGEP-----------LARGGRYDDLGA 291
|
330 340
....*....|....*....|.
gi 410927344 379 MFdpkGRKVPCVGVSIGIERI 399
Cdd:pfam13393 292 AF---GRARPATGFSLDLEAL 309
|
|
| HisRS_anticodon |
cd00859 |
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases ... |
418-509 |
2.82e-29 |
|
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: 110.32 E-value: 2.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 418 EVQVMVAAAQKNLLEERLRLITELWNAGIKAELMYKKsPKLLSQLQHCEESGIPLVAILGEQELKNGVVKLRNVATRDEV 497
Cdd:cd00859 1 EVDVYVVPLGEGALSEALELAEQLRDAGIKAEIDYGG-RKLKKQFKYADRSGARFAVILGEDELAAGVVTVKDLETGEQE 79
|
90
....*....|..
gi 410927344 498 DISRADLIAEIK 509
Cdd:cd00859 80 TVALDELVEELK 91
|
|
| syh |
CHL00201 |
histidine-tRNA synthetase; Provisional |
60-510 |
6.24e-23 |
|
histidine-tRNA synthetase; Provisional
Pssm-ID: 164576 [Multi-domain] Cd Length: 430 Bit Score: 101.13 E-value: 6.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 60 KGTRDYNPKQMAIREKVFNTIVSCFKRHGAETIDTPVFELKETLTGKYGEDSKLI----YDLKDQGGELLSLRYDLTVPF 135
Cdd:CHL00201 8 RGTKDILPDEINYWQFIHDKALTLLSLANYSEIRTPIFENSSLYDRGIGETTDIVnkemYRFTDRSNRDITLRPEGTAGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 136 ARYLAMNKIT---NIKR-YHIAKVYRRDNPamTRGRYREFYQCDFDIAGQYDAMiPDAECLKIVHEILSELDLGDFRIKV 211
Cdd:CHL00201 88 VRAFIENKMDyhsNLQRlWYSGPMFRYERP--QSGRQRQFHQLGIEFIGSIDAR-ADTEVIHLAMQIFNELQVKNLILDI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 212 N------DRRILDGmfavcgvpdNMFRTICSTVDKLDklpwEAVKNEMVNEKGLSEEAADQigvyvGMQGGMDLAERlLQ 285
Cdd:CHL00201 165 NsigkleDRQSYQL---------KLVEYLSQYQDDLD----TDSQNRLYSNPIRILDSKNL-----KTQEILDGAPK-IS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 286 DQKMCQSTQacagltDIKLLFSYLQLFQVTDKVvfDLSLARGLDYYTGIIYEailtqagvapVAPETSNEAPTeecvtvg 365
Cdd:CHL00201 226 DFLSLESTE------HFYDVCTYLNLLNIPYKI--NYKLVRGLDYYNDTAFE----------IKTLSSNGQDT------- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 366 sVAGGGRYDGLVGMFDpkGRKVPCVGVSIGIERIFSIMEQKAEASTEKIrTTEVQVMVAAAQKNLLEerlrLITELWNAG 445
Cdd:CHL00201 281 -ICGGGRYDSLIHQLG--GPKTPAVGCAIGLERLLLIAKDNIILPKQSI-DVYIATQGLKAQKKGWE----IIQFLEKQN 352
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 410927344 446 IKAELMYKKSpKLLSQLQHCEESGIPLVAILGEQELKNGVVKLRNVATRDEVDISRADLIAEIKK 510
Cdd:CHL00201 353 IKFELDLSSS-NFHKQIKQAGKKRAKACIILGDNEIMDNCITIKWLDEQVQENAQYSNFKQEISY 416
|
|
| hisZ |
PRK12295 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
70-399 |
7.77e-21 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 183413 [Multi-domain] Cd Length: 373 Bit Score: 94.23 E-value: 7.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 70 MAIREKVFNTIVSCFKRHGAETIDTPVFELKETLTGKYGED-SKLIYDLKDQGGELLSLRYDLTVPFAR-YLAMNKITNI 147
Cdd:PRK12295 4 LSASAAAAEALLASFEAAGAVRVDPPILQPAEPFLDLSGEDiRRRIFVTSDENGEELCLRPDFTIPVCRrHIATAGGEPA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 148 KRYHIAKVYRRdnpamTRGRYREFYQCDFDIAGQYDAMIPDAECLKIVHEILSELDLGDFRIKVNDRRILDGMFAVCGVP 227
Cdd:PRK12295 84 RYAYLGEVFRQ-----RRDRASEFLQAGIESFGRADPAAADAEVLALALEALAALGPGDLEVRLGDVGLFAALVDALGLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 228 D-------------NMFRTIcstvdkLDKLPWEAVKNEMVNEKGLSEEaADQIGVYVGMQGGM--------------DLA 280
Cdd:PRK12295 159 PgwkrrllrhfgrpRSLDAL------LARLAGPRVDPLDEHAGVLAAL-ADEAAARALVEDLMsiagispvggrspaEIA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 281 ERLLQDQK------------------------MCQSTQACAGLT-DIKL-LFSYLQLFQV-----------TDKVVFDLS 323
Cdd:PRK12295 232 RRLLEKAAlaaaarlpaealavlerflaisgpPDAALAALRALAaDAGLdLDAALDRFEArlaalaargidLERLRFSAS 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 410927344 324 LARGLDYYTGIIYEailtqagvapVAPETSNEAPteecvtvgsVAGGGRYDGLVGMFDpKGRKVPCVGVSIGIERI 399
Cdd:PRK12295 312 FGRPLDYYTGFVFE----------IRAAGNGDPP---------LAGGGRYDGLLTRLG-AGEPIPAVGFSIWLDRL 367
|
|
| HisRS_RNA |
cd00938 |
HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS ... |
5-49 |
2.61e-19 |
|
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: 80.98 E-value: 2.61e-19
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 410927344 5 AQIQEAIKCQGEVVRKLKAEKASKEQIDEEVAKLLELKAHLGGDD 49
Cdd:cd00938 1 AKLEEAVKLQGELVRKLKAEKASKEQIAEEVAKLLELKAQLGGDE 45
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
420-511 |
1.23e-16 |
|
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: 74.93 E-value: 1.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 420 QVMVAAAQKN---LLEERLRLITELWNAGIKAELMYKkSPKLLSQLQHCEESGIPLVAILGEQELKNGVVKLRNVATRDE 496
Cdd:pfam03129 1 QVVVIPLGEKaeeLEEYAQKLAEELRAAGIRVELDDR-NESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQ 79
|
90
....*....|....*
gi 410927344 497 VDISRADLIAEIKKR 511
Cdd:pfam03129 80 ETVSLDELVEKLKEL 94
|
|
| WHEP-TRS |
pfam00458 |
WHEP-TRS domain; |
7-69 |
1.17e-14 |
|
WHEP-TRS domain;
Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 68.29 E-value: 1.17e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 410927344 7 IQEAIKCQGEVVRKLKAEKASKEQIDEEVAKLLELKAHlggddgkhqfvLKTAKGTrDYNPKQ 69
Cdd:pfam00458 1 LTEKIKAQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQ-----------YKALTGK-DYKPGA 51
|
|
| WHEPGMRS_RNA |
cd01200 |
EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher ... |
8-48 |
2.56e-13 |
|
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: 64.10 E-value: 2.56e-13
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 410927344 8 QEAIKCQGEVVRKLKAEKASKEQIDEEVAKLLELKAHLGGD 48
Cdd:cd01200 1 YEKIAEQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKEA 41
|
|
| WHEP-TRS |
smart00991 |
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ... |
8-51 |
8.19e-13 |
|
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: 63.13 E-value: 8.19e-13
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 410927344 8 QEAIKCQGEVVRKLKAEKASKEQIDEEVAKLLELKAHLGGDDGK 51
Cdd:smart00991 1 EEAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLKEATGQ 44
|
|
| WEPRS_RNA |
cd00936 |
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ... |
11-43 |
4.37e-10 |
|
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: 54.93 E-value: 4.37e-10
10 20 30
....*....|....*....|....*....|...
gi 410927344 11 IKCQGEVVRKLKAEKASKEQIDEEVAKLLELKA 43
Cdd:cd00936 5 IAAQGDLVRELKAKKAPKEEIDAAVKKLLALKA 37
|
|
| HGTP_anticodon2 |
pfam12745 |
Anticodon binding domain of tRNAs; This is an HGTP_anticodon binding domain, found largely on ... |
415-511 |
1.51e-07 |
|
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: 52.61 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 415 RTTEVQVMVAAAQKNLL-EERLRLITELWNAGIKAELMYKKSPKLLSQLQHCEESGIPLVAILGEQELKNG----VVKLR 489
Cdd:pfam12745 2 KPRRCDVLVASFDASILrTTGVEILQELWAHGISADLAVDASYSPEDLVSRARDDGVSWIVIIKQQNKSSDskykPLKVK 81
|
90 100
....*....|....*....|....*.
gi 410927344 490 NVATRDEVDISRADLIA----EIKKR 511
Cdd:pfam12745 82 NLLRKEDVDLDSDELVSwlrgEIRER 107
|
|
| MetRS_RNA |
cd00939 |
MetRS_RNA binding domain. This short RNA-binding domain is found at the C-terminus of MetRS in ... |
7-51 |
3.52e-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: 46.70 E-value: 3.52e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 410927344 7 IQEAIKCQGEVVRKLKAEKASKEQIDEEVAKLLELKAHLGGDDGK 51
Cdd:cd00939 1 LEKEVAEQGNKVRKLKASKADKSVWQPEVNKLLDLKKQLALAEGK 45
|
|
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
1-88 |
3.46e-06 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 49.74 E-value: 3.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 1 MDDKAQIQEAIKCQGEVVRKLKAEKASKEQIDEEVAKLLELKAHLGGDDGKHQfvlKTAKGTRDYNPKQMAIREKVFNTI 80
Cdd:PLN02734 6 RDALAEKQAAVTAQGNAVRALKASKADKAEIDAAIEKLKALKLEKSALEKELQ---AAVGAGGDGAASKEAFRQAVVNTL 82
|
90
....*....|....
gi 410927344 81 ------VSCFKRHG 88
Cdd:PLN02734 83 errlfyIPSFKIYG 96
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
72-214 |
2.57e-05 |
|
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: 45.57 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 72 IREKVFNTIVSCFKRHGAETIDTPVFElKETLTGKYGEDSKLIYDLKDQGGELLSLRYDLTvPFARYLAMNKITNI--KR 149
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVE-REPLLEKAGHEPKDLLPVGAENEEDLYLRPTLE-PGLVRLFVSHIRKLplRL 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 410927344 150 YHIAKVYRRDNPAMTRGRYREFYQCDFDIAGQYDAMIP-DAECLKIVHEILSELDL-GDFRIKVNDR 214
Cdd:cd00768 79 AEIGPAFRNEGGRRGLRRVREFTQLEGEVFGEDGEEASeFEELIELTEELLRALGIkLDIVFVEKTP 145
|
|
| PRK12421 |
PRK12421 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
67-436 |
2.80e-05 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 237098 Cd Length: 392 Bit Score: 46.50 E-value: 2.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 67 PKQMAIREKVFNTIVSCFKRHGAETIDTPVFELKETLTGKYGEDSKL-IYDLKDQ-GGELLSLRYDLTVPFAR----YLA 140
Cdd:PRK12421 18 PEEAQKIERLRRRLLDLFASRGYQLVMPPLIEYLESLLTGAGQDLKLqTFKLIDQlSGRLMGVRADITPQVARidahLLN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 141 MNKITnikRY-HIAKVY--RRDNPAMTRGRYR---EFYQCDfDIAGqydamipDAECLKIVHEILSELDLGDFRIKVNDR 214
Cdd:PRK12421 98 REGVA---RLcYAGSVLhtLPQGLFGSRTPLQlgaELYGHA-GIEA-------DLEIIRLMLGLLRNAGVPALHLDLGHV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 215 RILDGMFAVCGVPDNmfrticSTVDKLDKLPWEAVK--NEMVNEKGLSEEAADQIGVYVGMQGGMDLAERLLQdQKMCQS 292
Cdd:PRK12421 167 GIFRRLAELAGLSPE------EEEELFDLLQRKALPelAEVCQNLGVGSDLRRMFYALARLNGGLEALDRALS-VLALQD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 293 TQACAGLTDIKLLFSYLQLFQVTDKVVFDLSLARGLDYYTGIIYEAILTQAGVApvapetsneapteecvtvgsVAGGGR 372
Cdd:PRK12421 240 AAIRQALDELKTLAAHLKNRWPELPVSIDLAELRGYHYHTGLVFAAYIPGRGQA--------------------LARGGR 299
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 410927344 373 YDGLVGMFdpkGRKVPCVGVSIGIERIFSImeQKAEASTEKIrttevqVMVAAAQKNLLE--ERLR 436
Cdd:PRK12421 300 YDGIGEAF---GRARPATGFSMDLKELLAL--QFLEEEAGAI------LAPWGDDPDLLAaiAELR 354
|
|
| HGTP_anticodon |
cd00738 |
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ... |
430-509 |
1.32e-04 |
|
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and prolyl tRNA synthetases, which are classified as a group of class II aminoacyl-tRNA synthetases (aaRS). In aaRSs, the anticodon binding domain 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. This domain is also found in the accessory subunit of mitochondrial polymerase gamma (Pol gamma b).
Pssm-ID: 238379 [Multi-domain] Cd Length: 94 Bit Score: 40.84 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 430 LLEERLRLITELWNAGIKAELMYKKSpKLLSQLQHCEESGIPLVAILGEQELKNGVVKLRNVATRDEVDISRADLIAEIK 509
Cdd:cd00738 16 AREYAQKLLNALLANGIRVLYDDRER-KIGKKFREADLRGVPFAVVVGEDELENGKVTVKSRDTGESETLHVDELPEFLV 94
|
|
| GlyRS_RNA |
cd00935 |
GlyRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of GlyRS ... |
5-43 |
7.47e-04 |
|
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: 37.47 E-value: 7.47e-04
10 20 30
....*....|....*....|....*....|....*....
gi 410927344 5 AQIQEAIKCQGEVVRKLKAEKASKEQIDEEVAkllELKA 43
Cdd:cd00935 2 APLRAAVKEQGDLVRKLKEEGAPDVDIKKAVA---ELKA 37
|
|
| PRK09194 |
PRK09194 |
prolyl-tRNA synthetase; Provisional |
381-510 |
2.28e-03 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 236405 [Multi-domain] Cd Length: 565 Bit Score: 40.45 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 381 DPKGRKVP----CVGvsIGIERIFS-IMEQKAEastEK--IRTTEV---QVMVAA------AQKNLLEErlrLITELWNA 444
Cdd:PRK09194 426 DENGKAQPlimgCYG--IGVSRLVAaAIEQNHD---EKgiIWPKAIapfDVHIVPvnmkdeEVKELAEK---LYAELQAA 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 445 GIK----------------AELMykkspkllsqlqhceesGIPLVAILGEQELKNGVVKLRNVATRDEVDISRADLIAEI 508
Cdd:PRK09194 498 GIEvllddrkerpgvkfadADLI-----------------GIPHRIVVGDRGLAEGIVEYKDRRTGEKEEVPVDELVEFL 560
|
..
gi 410927344 509 KK 510
Cdd:PRK09194 561 KA 562
|
|
| PRK03991 |
PRK03991 |
threonyl-tRNA synthetase; Validated |
395-513 |
6.27e-03 |
|
threonyl-tRNA synthetase; Validated
Pssm-ID: 235190 [Multi-domain] Cd Length: 613 Bit Score: 39.08 E-value: 6.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410927344 395 GIER-IFSIMEqKAEASTEKIRT-------TEVQVMVAAAQKNLLEERLRLITELWNAGIKAEL------MYKKspklls 460
Cdd:PRK03991 469 SIERvIYALLE-KAAKEEEEGKVpmlptwlSPTQVRVIPVSERHLDYAEEVADKLEAAGIRVDVddrdesLGKK------ 541
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 410927344 461 qLQHCEESGIPLVAILGEQELKNGVVKLRNVATRDEVDISRADLIAEIKKRTS 513
Cdd:PRK03991 542 -IRDAGKEWIPYVVVIGDKEMESGKLTVTIREESEKVEMTLEELIERIKEETK 593
|
|
| |
