|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02972 |
PLN02972 |
Histidyl-tRNA synthetase |
108-564 |
1.99e-167 |
|
Histidyl-tRNA synthetase
Pssm-ID: 215525 [Multi-domain] Cd Length: 763 Bit Score: 496.33 E-value: 1.99e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 108 EVKFTLKTPKGTRDWEPLAMSLRKRIFSTIEDVFSAHGAVTIDTPVFELKEILSGKYGEDSKLIYDLQDQGGELCSLRYD 187
Cdd:PLN02972 322 EVRRLPKIPKGTRDFAKEQMAIREKAFSIITSVFKRHGATALDTPVFELRETLMGKYGEDSKLIYDLADQGGELCSLRYD 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 188 LTVPFARFVAMNPSehGNIKRYHIAKVYRRDQPamSKGRFREFYQCDIDIAGVYDPMVPDSEVLCILVEALDALGIEGFT 267
Cdd:PLN02972 402 LTVPFARYVAMNGI--TSFKRYQIAKVYRRDNP--SKGRYREFYQCDFDIAGVYEPMGPDFEIIKVLTELLDELDIGTYE 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 268 IKINHRKILDGIFDICGVPADKIRTISSAVDKLDKSPWSEVKREMTVDKGLAEDVADRIGEYVKLKGG-RDLLEKLKA-D 345
Cdd:PLN02972 478 VKLNHRKLLDGMLEICGVPPEKFRTICSSIDKLDKQSFEQVKKEMVEEKGLSNETADKIGNFVKERGPpLELLSKLRQeG 557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 346 ATMSGHAIASQGVKDMELLFDYLDVYGISDRMSFDLSLARGLDYYTGLIYEAVtaasappgFSGeaaAQdkapekkskkk 425
Cdd:PLN02972 558 SEFLGNASSRAALDELEIMFKALEKSKAIGKIVFDLSLARGLDYYTGVIYEAV--------FKG---AQ----------- 615
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 426 ksadgeeevdestvgVGSIAAGGRYDNLVGMFSGSKkpdaVPCVGVSIGVERVFAIMMQrlREKEARGErtsVRSKEVDV 505
Cdd:PLN02972 616 ---------------VGSIAAGGRYDNLVGMFSGKQ----VPAVGVSLGIERVFAIMEQ--QEEEKSQV---IRPTETEV 671
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 955482957 506 YVMSVGEGLLKERMQVAKMLWDAGIKAEFmhKAKPKLPQQFGVVDKEGIPFAVILAPNE 564
Cdd:PLN02972 672 LVSIIGDDKLALAAELVSELWNAGIKAEY--KVSTRKAKHLKRAKESGIPWMVLVGEKE 728
|
|
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
112-607 |
1.30e-111 |
|
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: 340.95 E-value: 1.30e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 112 TLKTPKGTRDWEPLAMSLRKRIFSTIEDVFSAHGAVTIDTPVFELKEILSGKYGED--SKLIYDLQDQGGELCSLRYDLT 189
Cdd:COG0124 3 KIQAPRGTRDILPEESAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKIGEDivEKEMYTFEDRGGRSLTLRPEGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 190 VPFARFVAMNPSEHGN-IKRYHIAKVYRRDQPAmsKGRFREFYQCDIDIAGVYDPMVpDSEVLCILVEALDALGIEGFTI 268
Cdd:COG0124 83 APVARAVAEHGNELPFpFKLYYIGPVFRYERPQ--KGRYRQFHQFGVEVIGSDSPLA-DAEVIALAADLLKALGLKDFTL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 269 KINHRkildgifdicGVPADKIRTISSAVDKLDKSPWSEVkremtvdkgLAEDVADRIG-----EYVKLKGGRD--LLEK 341
Cdd:COG0124 160 EINSR----------GLPEERAEALLRYLDKLDKIGHEDV---------LDEDSQRRLEtnplrAILDSKGPDCqeVLAD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 342 LKAdatmSGHAIASQGVKDMELLFDYLDVYGISdrMSFDLSLARGLDYYTGLIYEAVTaasappgfsGEAAAQdkapekk 421
Cdd:COG0124 221 APK----LLDYLGEEGLAHFEEVLELLDALGIP--YVIDPRLVRGLDYYTGTVFEIVT---------DGLGAQ------- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 422 skkkksadgeeevdestvgvGSIAAGGRYDNLVGMFSGSKkpdaVPCVGVSIGVERVFAIMMQRLREKEARgertsvrsK 501
Cdd:COG0124 279 --------------------GSVCGGGRYDGLVEQLGGPP----TPAVGFAIGLERLLLLLEELGLLPAAE--------P 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 502 EVDVYVMSVGEGLLKERMQVAKMLWDAGIKAEFMHKAKpKLPQQFGVVDKEGIPFAVILAPNEWNADarQVRVKqqkgkd 581
Cdd:COG0124 327 PPDVYVVPLGEEARAEALKLAQELRAAGIRVELDLGGR-KLKKQLKYADKSGAPFVLILGEDELANG--TVTLK------ 397
|
490 500
....*....|....*....|....*.
gi 955482957 582 sDEGQGQGEIVNLDQLIKHLKSLGAG 607
Cdd:COG0124 398 -DLATGEQETVPLDELVEYLKELLAE 422
|
|
| hisS |
TIGR00442 |
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ... |
114-575 |
6.04e-102 |
|
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: 315.57 E-value: 6.04e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 114 KTPKGTRDWEPLAMSLRKRIFSTIEDVFSAHGAVTIDTPVFELKEILSGKYGEDS----KLIYDLQDQGGELCSLRYDLT 189
Cdd:TIGR00442 1 QKPRGTRDFLPEEMIKWQYIEETIREVFERYGFKEIRTPIFEYTELFKRKVGEETdivsKEMYTFKDKGGRSLTLRPEGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 190 VPFARFVAMNPSEHGN-IKRYHIAKVYRRDQPAmsKGRFREFYQCDIDIAGVYDPMVpDSEVLCILVEALDALGIEGFTI 268
Cdd:TIGR00442 81 APVARAVIENKLLLPKpFKLYYIGPMFRYERPQ--KGRYRQFHQFGVEVIGSDSPLA-DAEIIALAADILKELGLKDFTL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 269 KINHRKILDGIFDIcgvPADKIRTISSAVDKLDKSpwsEVKREMTVDKGLAEDVADRIGEYVKlkGGRDLLEKLKADatm 348
Cdd:TIGR00442 158 EINSLGILEGRLEY---REALIRYLDKHKDKLGED---SVRRLEKNPLRILDSKNEKIQELLK--NAPKILDFLCEE--- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 349 sghaiasqGVKDMELLFDYLDVYGIsdRMSFDLSLARGLDYYTGLIYEAVTaasappgfsGEAAAQdkapekkskkkksa 428
Cdd:TIGR00442 227 --------SRAHFEELKELLDALGI--PYKIDPSLVRGLDYYTGTVFEFVT---------DDLGAQ-------------- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 429 dgeeevdestvgvGSIAAGGRYDNLVGMFSGSKkpdaVPCVGVSIGVERVFAIMMQRlrekeargERTSVRSKEVDVYVM 508
Cdd:TIGR00442 274 -------------GSICGGGRYDGLVEELGGPP----TPAVGFAIGIERLILLLEEL--------GLIPPPSKKPDVYVV 328
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 955482957 509 SVGEGLLKERMQVAKMLWDAGIKAEFMHKAKpKLPQQFGVVDKEGIPFAVILAPNEWNADarQVRVK 575
Cdd:TIGR00442 329 PLGEEAELEALKLAQKLRKAGIRVEVDLGGR-KLKKQLKYADKLGARFALIIGEDELENG--TVTLK 392
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
127-482 |
3.89e-99 |
|
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. It is responsible for the attachment of histidine to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs. This domain is also found at the C-terminus of eukaryotic GCN2 protein kinase and at the N-terminus of the ATP phosphoribosyltransferase accessory subunit, HisZ. HisZ along with HisG catalyze the first reaction in histidine biosynthesis. HisZ is found only in a subset of bacteria and differs from HisRS in lacking a C-terminal anti-codon binding domain.
Pssm-ID: 238396 [Multi-domain] Cd Length: 261 Bit Score: 302.98 E-value: 3.89e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 127 MSLRKRIFSTIEDVFSAHGAVTIDTPVFELKEILSGKYGED-SKLIYDLQDQGGELCSLRYDLTVPFARFVAMNPSEHG- 204
Cdd:cd00773 2 AALRRYIEDTLREVFERYGYEEIDTPVFEYTELFLRKSGDEvSKEMYRFKDKGGRDLALRPDLTAPVARAVAENLLSLPl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 205 NIKRYHIAKVYRRDQPAmsKGRFREFYQCDIDIAGvYDPMVPDSEVLCILVEALDALGIEGFTIKINHRKILDGifdICG 284
Cdd:cd00773 82 PLKLYYIGPVFRYERPQ--KGRYREFYQVGVEIIG-SDSPLADAEVIALAVEILEALGLKDFQIKINHRGILDG---IAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 285 VPADKIRTISSAVDKLDKSpwsevkremtvdkglaedvadrigeyvklkggrdlleklkadatmsghaiasqGVKDMELL 364
Cdd:cd00773 156 LLEDREEYIERLIDKLDKE-----------------------------------------------------ALAHLEKL 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 365 FDYLDVYGISDRMSFDLSLARGLDYYTGLIYEAVTaasappgfsgeaaaqDKAPekkskkkksadgeeevdestvGVGSI 444
Cdd:cd00773 183 LDYLEALGVDIKYSIDLSLVRGLDYYTGIVFEAVA---------------DGLG---------------------AQGSI 226
|
330 340 350
....*....|....*....|....*....|....*...
gi 955482957 445 AAGGRYDNLVGMFSGSKkpdaVPCVGVSIGVERVFAIM 482
Cdd:cd00773 227 AGGGRYDGLLEEFGGED----VPAVGFAIGLERLLLAL 260
|
|
| tRNA-synt_His |
pfam13393 |
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ... |
118-478 |
3.66e-41 |
|
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP phosphoribosyltransferase regulatory subunits.
Pssm-ID: 433170 [Multi-domain] Cd Length: 309 Bit Score: 151.58 E-value: 3.66e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 118 GTRDWEPLAMSLRKRIFSTIEDVFSAHGAVTIDTPVFELKEILSGKYGEDSKLIYDLQDQGGELCSLRYDLTVPFARFVA 197
Cdd:pfam13393 1 GIRDLLPPEARRIEELRRRLLDLFRSWGYELVMPPLLEYLDSLLTGTGADLDQTFKLVDQSGRLLGLRADITPQVARIDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 198 MNPSEHGNIKRYHIAKVYRRDQPAMskGRFREFYQCDIDIAGVYDPMVpDSEVLCILVEALDALGIEGFTIKINHRKILD 277
Cdd:pfam13393 81 HRLNRPGPLRLCYAGSVLRTRPKGL--GRSREPLQVGAELIGHAGIEA-DAEIISLLLEALAAAGVPGVTLDLGHVGLVR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 278 GIFDICGVPADKIRTISSAVDKLDkspWSEVkREMTVDKGLAEDVADRIGEYVKLKGGRDLLEKLKADAtmsGHAIASQG 357
Cdd:pfam13393 158 ALLEAAGLSEALEEALRAALQRKD---AAEL-AELAAEAGLPPALRRALLALPDLYGGPEVLDEARAAL---PGLPALQE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 358 VKD-MELLFDYLDVYGISDRMSFDLSLARGLDYYTGLIYEAVTaasapPGFSGEaaaqdkapekkskkkksadgeeevde 436
Cdd:pfam13393 231 ALDeLEALAALLEALGDGVRLTFDLAELRGYEYYTGIVFAAYA-----PGVGEP-------------------------- 279
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 955482957 437 stvgvgsIAAGGRYDNLVGMFSgskkpDAVPCVGVSIGVERV 478
Cdd:pfam13393 280 -------LARGGRYDDLGAAFG-----RARPATGFSLDLEAL 309
|
|
| MetRS_RNA |
cd00939 |
MetRS_RNA binding domain. This short RNA-binding domain is found at the C-terminus of MetRS in ... |
55-96 |
1.34e-03 |
|
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: 37.07 E-value: 1.34e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 955482957 55 LQAARAEQDDKVQQLRAANTEPATLKAEIGKLKKLEAQLAQL 96
Cdd:cd00939 1 LEKEVAEQGNKVRKLKASKADKSVWQPEVNKLLDLKKQLALA 42
|
|
| WHEP-TRS |
pfam00458 |
WHEP-TRS domain; |
55-106 |
1.79e-03 |
|
WHEP-TRS domain;
Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 36.70 E-value: 1.79e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 955482957 55 LQAARAEQDDKVQQLRAANTEPATLKAEIGKLKKLEAQLAQL-GIGAKAGSSK 106
Cdd:pfam00458 1 LTEKIKAQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKALtGKDYKPGAAP 53
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02972 |
PLN02972 |
Histidyl-tRNA synthetase |
108-564 |
1.99e-167 |
|
Histidyl-tRNA synthetase
Pssm-ID: 215525 [Multi-domain] Cd Length: 763 Bit Score: 496.33 E-value: 1.99e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 108 EVKFTLKTPKGTRDWEPLAMSLRKRIFSTIEDVFSAHGAVTIDTPVFELKEILSGKYGEDSKLIYDLQDQGGELCSLRYD 187
Cdd:PLN02972 322 EVRRLPKIPKGTRDFAKEQMAIREKAFSIITSVFKRHGATALDTPVFELRETLMGKYGEDSKLIYDLADQGGELCSLRYD 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 188 LTVPFARFVAMNPSehGNIKRYHIAKVYRRDQPamSKGRFREFYQCDIDIAGVYDPMVPDSEVLCILVEALDALGIEGFT 267
Cdd:PLN02972 402 LTVPFARYVAMNGI--TSFKRYQIAKVYRRDNP--SKGRYREFYQCDFDIAGVYEPMGPDFEIIKVLTELLDELDIGTYE 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 268 IKINHRKILDGIFDICGVPADKIRTISSAVDKLDKSPWSEVKREMTVDKGLAEDVADRIGEYVKLKGG-RDLLEKLKA-D 345
Cdd:PLN02972 478 VKLNHRKLLDGMLEICGVPPEKFRTICSSIDKLDKQSFEQVKKEMVEEKGLSNETADKIGNFVKERGPpLELLSKLRQeG 557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 346 ATMSGHAIASQGVKDMELLFDYLDVYGISDRMSFDLSLARGLDYYTGLIYEAVtaasappgFSGeaaAQdkapekkskkk 425
Cdd:PLN02972 558 SEFLGNASSRAALDELEIMFKALEKSKAIGKIVFDLSLARGLDYYTGVIYEAV--------FKG---AQ----------- 615
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 426 ksadgeeevdestvgVGSIAAGGRYDNLVGMFSGSKkpdaVPCVGVSIGVERVFAIMMQrlREKEARGErtsVRSKEVDV 505
Cdd:PLN02972 616 ---------------VGSIAAGGRYDNLVGMFSGKQ----VPAVGVSLGIERVFAIMEQ--QEEEKSQV---IRPTETEV 671
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 955482957 506 YVMSVGEGLLKERMQVAKMLWDAGIKAEFmhKAKPKLPQQFGVVDKEGIPFAVILAPNE 564
Cdd:PLN02972 672 LVSIIGDDKLALAAELVSELWNAGIKAEY--KVSTRKAKHLKRAKESGIPWMVLVGEKE 728
|
|
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
112-607 |
1.30e-111 |
|
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: 340.95 E-value: 1.30e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 112 TLKTPKGTRDWEPLAMSLRKRIFSTIEDVFSAHGAVTIDTPVFELKEILSGKYGED--SKLIYDLQDQGGELCSLRYDLT 189
Cdd:COG0124 3 KIQAPRGTRDILPEESAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKIGEDivEKEMYTFEDRGGRSLTLRPEGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 190 VPFARFVAMNPSEHGN-IKRYHIAKVYRRDQPAmsKGRFREFYQCDIDIAGVYDPMVpDSEVLCILVEALDALGIEGFTI 268
Cdd:COG0124 83 APVARAVAEHGNELPFpFKLYYIGPVFRYERPQ--KGRYRQFHQFGVEVIGSDSPLA-DAEVIALAADLLKALGLKDFTL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 269 KINHRkildgifdicGVPADKIRTISSAVDKLDKSPWSEVkremtvdkgLAEDVADRIG-----EYVKLKGGRD--LLEK 341
Cdd:COG0124 160 EINSR----------GLPEERAEALLRYLDKLDKIGHEDV---------LDEDSQRRLEtnplrAILDSKGPDCqeVLAD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 342 LKAdatmSGHAIASQGVKDMELLFDYLDVYGISdrMSFDLSLARGLDYYTGLIYEAVTaasappgfsGEAAAQdkapekk 421
Cdd:COG0124 221 APK----LLDYLGEEGLAHFEEVLELLDALGIP--YVIDPRLVRGLDYYTGTVFEIVT---------DGLGAQ------- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 422 skkkksadgeeevdestvgvGSIAAGGRYDNLVGMFSGSKkpdaVPCVGVSIGVERVFAIMMQRLREKEARgertsvrsK 501
Cdd:COG0124 279 --------------------GSVCGGGRYDGLVEQLGGPP----TPAVGFAIGLERLLLLLEELGLLPAAE--------P 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 502 EVDVYVMSVGEGLLKERMQVAKMLWDAGIKAEFMHKAKpKLPQQFGVVDKEGIPFAVILAPNEWNADarQVRVKqqkgkd 581
Cdd:COG0124 327 PPDVYVVPLGEEARAEALKLAQELRAAGIRVELDLGGR-KLKKQLKYADKSGAPFVLILGEDELANG--TVTLK------ 397
|
490 500
....*....|....*....|....*.
gi 955482957 582 sDEGQGQGEIVNLDQLIKHLKSLGAG 607
Cdd:COG0124 398 -DLATGEQETVPLDELVEYLKELLAE 422
|
|
| hisS |
TIGR00442 |
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ... |
114-575 |
6.04e-102 |
|
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: 315.57 E-value: 6.04e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 114 KTPKGTRDWEPLAMSLRKRIFSTIEDVFSAHGAVTIDTPVFELKEILSGKYGEDS----KLIYDLQDQGGELCSLRYDLT 189
Cdd:TIGR00442 1 QKPRGTRDFLPEEMIKWQYIEETIREVFERYGFKEIRTPIFEYTELFKRKVGEETdivsKEMYTFKDKGGRSLTLRPEGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 190 VPFARFVAMNPSEHGN-IKRYHIAKVYRRDQPAmsKGRFREFYQCDIDIAGVYDPMVpDSEVLCILVEALDALGIEGFTI 268
Cdd:TIGR00442 81 APVARAVIENKLLLPKpFKLYYIGPMFRYERPQ--KGRYRQFHQFGVEVIGSDSPLA-DAEIIALAADILKELGLKDFTL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 269 KINHRKILDGIFDIcgvPADKIRTISSAVDKLDKSpwsEVKREMTVDKGLAEDVADRIGEYVKlkGGRDLLEKLKADatm 348
Cdd:TIGR00442 158 EINSLGILEGRLEY---REALIRYLDKHKDKLGED---SVRRLEKNPLRILDSKNEKIQELLK--NAPKILDFLCEE--- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 349 sghaiasqGVKDMELLFDYLDVYGIsdRMSFDLSLARGLDYYTGLIYEAVTaasappgfsGEAAAQdkapekkskkkksa 428
Cdd:TIGR00442 227 --------SRAHFEELKELLDALGI--PYKIDPSLVRGLDYYTGTVFEFVT---------DDLGAQ-------------- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 429 dgeeevdestvgvGSIAAGGRYDNLVGMFSGSKkpdaVPCVGVSIGVERVFAIMMQRlrekeargERTSVRSKEVDVYVM 508
Cdd:TIGR00442 274 -------------GSICGGGRYDGLVEELGGPP----TPAVGFAIGIERLILLLEEL--------GLIPPPSKKPDVYVV 328
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 955482957 509 SVGEGLLKERMQVAKMLWDAGIKAEFMHKAKpKLPQQFGVVDKEGIPFAVILAPNEWNADarQVRVK 575
Cdd:TIGR00442 329 PLGEEAELEALKLAQKLRKAGIRVEVDLGGR-KLKKQLKYADKLGARFALIIGEDELENG--TVTLK 392
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
127-482 |
3.89e-99 |
|
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. It is responsible for the attachment of histidine to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs. This domain is also found at the C-terminus of eukaryotic GCN2 protein kinase and at the N-terminus of the ATP phosphoribosyltransferase accessory subunit, HisZ. HisZ along with HisG catalyze the first reaction in histidine biosynthesis. HisZ is found only in a subset of bacteria and differs from HisRS in lacking a C-terminal anti-codon binding domain.
Pssm-ID: 238396 [Multi-domain] Cd Length: 261 Bit Score: 302.98 E-value: 3.89e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 127 MSLRKRIFSTIEDVFSAHGAVTIDTPVFELKEILSGKYGED-SKLIYDLQDQGGELCSLRYDLTVPFARFVAMNPSEHG- 204
Cdd:cd00773 2 AALRRYIEDTLREVFERYGYEEIDTPVFEYTELFLRKSGDEvSKEMYRFKDKGGRDLALRPDLTAPVARAVAENLLSLPl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 205 NIKRYHIAKVYRRDQPAmsKGRFREFYQCDIDIAGvYDPMVPDSEVLCILVEALDALGIEGFTIKINHRKILDGifdICG 284
Cdd:cd00773 82 PLKLYYIGPVFRYERPQ--KGRYREFYQVGVEIIG-SDSPLADAEVIALAVEILEALGLKDFQIKINHRGILDG---IAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 285 VPADKIRTISSAVDKLDKSpwsevkremtvdkglaedvadrigeyvklkggrdlleklkadatmsghaiasqGVKDMELL 364
Cdd:cd00773 156 LLEDREEYIERLIDKLDKE-----------------------------------------------------ALAHLEKL 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 365 FDYLDVYGISDRMSFDLSLARGLDYYTGLIYEAVTaasappgfsgeaaaqDKAPekkskkkksadgeeevdestvGVGSI 444
Cdd:cd00773 183 LDYLEALGVDIKYSIDLSLVRGLDYYTGIVFEAVA---------------DGLG---------------------AQGSI 226
|
330 340 350
....*....|....*....|....*....|....*...
gi 955482957 445 AAGGRYDNLVGMFSGSKkpdaVPCVGVSIGVERVFAIM 482
Cdd:cd00773 227 AGGGRYDGLLEEFGGED----VPAVGFAIGLERLLLAL 260
|
|
| PRK12420 |
PRK12420 |
histidyl-tRNA synthetase; Provisional |
110-578 |
1.27e-85 |
|
histidyl-tRNA synthetase; Provisional
Pssm-ID: 237097 [Multi-domain] Cd Length: 423 Bit Score: 273.92 E-value: 1.27e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 110 KFTLKTPKGTRDWEPLAMSLRKRIFSTIEDVFSAHGAVTIDTPVFELKEILSGKYG---EDSKLIYDLQDQGGELCSLRY 186
Cdd:PRK12420 1 MMEMRNVKGTKDYLPEEQVLRNKIKRALEDVFERYGCKPLETPTLNMYELMSSKYGggdEILKEIYTLTDQGKRDLALRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 187 DLTVPFARFVAMNPSEHGNIKRYHIAKVYrRDQPaMSKGRFREFYQCDIDIAGVYDPMVpDSEVLCILVEALDALGIEgF 266
Cdd:PRK12420 81 DLTIPFAKVVAMNPNIRLPFKRYEIGKVF-RDGP-IKQGRFREFIQCDVDIVGVESVMA-EAELMSMAFELFRRLNLE-V 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 267 TIKINHRKILDGIFDICGVPADKIRTISSAVDKLDKSPWSEVKREMtVDKGLAEDVADRIGEYVKLKGGRDlLEKLKADA 346
Cdd:PRK12420 157 TIQYNNRKLLNGILQAIGIPTELTSDVILSLDKIEKIGIDGVRKDL-LERGISEEMADTICNTVLSCLQLS-IADFKEAF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 347 TMSghaIASQGVKDMELLFDYLDVYGISDRMSFDLSLARGLDYYTGLIYEAvtaasappgFSGEAAAQDkapekkskkkk 426
Cdd:PRK12420 235 NNP---LVAEGVNELQQLQQYLIALGINENCIFNPFLARGLTMYTGTVYEI---------FLKDGSITS----------- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 427 sadgeeevdestvgvgSIAAGGRYDNLVGMFSGSKKPdaVPCVGVSIGVERVFAIMMQRLREKEArgertsvrskeVDVY 506
Cdd:PRK12420 292 ----------------SIGSGGRYDNIIGAFRGDDMN--YPTVGISFGLDVIYTALSQKETISST-----------ADVF 342
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 955482957 507 VMSVGEGLlkERMQVA-KMLWDAGIKAEfMHKAKPKLPQQFGVVDKEGIPFAVILAPNEwnADARQVRVKQQK 578
Cdd:PRK12420 343 IIPLGTEL--QCLQIAqQLRSTTGLKVE-LELAGRKLKKALNYANKENIPYVLIIGEEE--VSTGTVMLRNMK 410
|
|
| PLN02530 |
PLN02530 |
histidine-tRNA ligase |
104-575 |
1.50e-52 |
|
histidine-tRNA ligase
Pssm-ID: 178145 [Multi-domain] Cd Length: 487 Bit Score: 187.64 E-value: 1.50e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 104 SSKQEVKFTLKTPKGTRDWEPLAMSLRKRIFSTIEDVFSAHGAVTIDTPVFELKEILSGKYGED-SKLIYDLQDQGGELC 182
Cdd:PLN02530 61 QEDGKPKIDVNPPKGTRDFPPEDMRLRNWLFDHFREVSRLFGFEEVDAPVLESEELYIRKAGEEiTDQLYNFEDKGGRRV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 183 SLRYDLTVPFARFV-AMNPSEHGNIKRYHIAKVYRRDQpaMSKGRFREFYQCDIDIAGVYDPMVpDSEVLCILVEALDAL 261
Cdd:PLN02530 141 ALRPELTPSLARLVlQKGKSLSLPLKWFAIGQCWRYER--MTRGRRREHYQWNMDIIGVPGVEA-EAELLAAIVTFFKRV 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 262 GI--EGFTIKINHRKILDGIFDICGVPADKIRTISSAVDKLDKSPWSEVKREMtVDKGLAEDVADRIGEYVKLKGGRDLL 339
Cdd:PLN02530 218 GItsSDVGIKVSSRKVLQAVLKSYGIPEESFAPVCVIVDKLEKLPREEIEKEL-DTLGVSEEAIEGILDVLSLKSLDDLE 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 340 EKLKADatmsghaiaSQGVKDMELLFDYLDVYGISDRMSFDLSLARGLDYYTGLIYEavtaasappGFsgeaaaqDKAPE 419
Cdd:PLN02530 297 ALLGAD---------SEAVADLKQLFSLAEAYGYQDWLVFDASVVRGLAYYTGIVFE---------GF-------DRAGK 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 420 kkskkkksadgeeevdestvgVGSIAAGGRYDNLVGMFSGskkpDAVPCVGVSIGVervfAIMMQRLREKEARGErtsvR 499
Cdd:PLN02530 352 ---------------------LRAICGGGRYDRLLSTFGG----EDTPACGFGFGD----AVIVELLKEKGLLPE----L 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 955482957 500 SKEVDVYVMSVGEGLLKERMQVAKMLWDAGIKAEFMHKAKpKLPQQFGVVDKEGIPFAVILAPNEWNADArqVRVK 575
Cdd:PLN02530 399 PHQVDDVVFALDEDLQGAAAGVASRLREKGRSVDLVLEPK-KLKWVFKHAERIGAKRLVLVGASEWERGM--VRVK 471
|
|
| HisZ |
COG3705 |
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism]; |
124-482 |
3.58e-50 |
|
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism];
Pssm-ID: 442919 [Multi-domain] Cd Length: 312 Bit Score: 176.14 E-value: 3.58e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 124 PLAMSLRKRIFSTIEDVFSAHGAVTIDTPVFELKEILSGKYGEDSKL-IYDLQDQGGELCSLRYDLTVPFARFVAMN-PS 201
Cdd:COG3705 2 PEEAARKEELRRRLLDVFRSWGYELVEPPLLEYLDSLLTGSGADLDLqTFKLVDQLGRTLGLRPDMTPQVARIAATRlAN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 202 EHGNIKRYHIAKVYRRdQPAMSkGRFREFYQcdidiAGV----YDPMVPDSEVLCILVEALDALGIEGFTIKINHRKILD 277
Cdd:COG3705 82 RPGPLRLCYAGNVFRT-RPSGL-GRSREFLQ-----AGAeligHAGLEADAEVIALALEALKAAGLEDFTLDLGHVGLFR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 278 GIFDICGVPADKIRTISSAVDKLDkspWSEVkREMTVDKGLAEDVADRIGEYVKLKGGRDLLEKLKAdatMSGHAIASQG 357
Cdd:COG3705 155 ALLEALGLSEEQREELRRALARKD---AVEL-EELLAELGLSEELAEALLALPELYGGEEVLARARA---LLLDAAIRAA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 358 VKDMELLFDYLDVYGISDRMSFDLSLARGLDYYTGLIYEAVTAASAPPgfsgeaaaqdkapekkskkkksadgeeevdes 437
Cdd:COG3705 228 LDELEALAEALAARGPDVRLTFDLSELRGYDYYTGIVFEAYAPGVGDP-------------------------------- 275
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 955482957 438 tvgvgsIAAGGRYDNLVGMFsGSkkpdAVPCVGVSIGVERVFAIM 482
Cdd:COG3705 276 ------LARGGRYDGLLAAF-GR----ARPATGFSLDLDRLLRAL 309
|
|
| hisZ_biosyn_reg |
TIGR00443 |
ATP phosphoribosyltransferase, regulatory subunit; Apparant second copies of histidyl-tRNA ... |
120-478 |
3.84e-46 |
|
ATP phosphoribosyltransferase, regulatory subunit; Apparant second copies of histidyl-tRNA synthetase, found in Bacillus subtilis, Synechocystis sp., Aquifex aeolicus, and others, are in fact a regulatory subunit of ATP phosphoribosyltransferase, and usually encoded by a gene adjacent to that encoding the catalytic subunit. [Amino acid biosynthesis, Histidine family]
Pssm-ID: 273081 [Multi-domain] Cd Length: 313 Bit Score: 165.48 E-value: 3.84e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 120 RDWEPLAMSLRKRIFSTIEDVFSAHGAVTIDTPVFELKEILSGKYGEDSKLIYDLQDQGGELCSLRYDLTVPFARFVAMN 199
Cdd:TIGR00443 1 RDLLPEEAARKEEIERQLQDVFRSWGYQEIITPTLEYLDTLSAGSGILNEDLFKLFDQLGRVLGLRPDMTAPIARLVSTR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 200 -PSEHGNIKRYHIAKVYRRDQPAMskGRFREFYQCDIDIAGvYDPMVPDSEVLCILVEALDALGIEGFTIKINHRKILDG 278
Cdd:TIGR00443 81 lRDRPLPLRLCYAGNVFRTNESGG--GRSREFTQAGVELIG-AGGPAADAEVIALLIEALKALGLKDFKIELGHVGLVRA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 279 IFDICGVPADKIRTISSAVDKLDkspWSEVKrEMTVDKGLAEDVADRIGEYVKLKG-GRDLLEKLKAdatMSGHAIASQG 357
Cdd:TIGR00443 158 LLEEAGLPEEAREALREALARKD---LVALE-ELVAELGLSPEVRERLLALPRLRGdGEEVLEEARA---LAGSETAEAA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 358 VKDMELLFDYLDVYGISDRMSFDLSLARGLDYYTGLIYEAVTAasappgfsGEAAAqdkapekkskkkksadgeeevdes 437
Cdd:TIGR00443 231 LDELEAVLELLEARGVEEYISLDLGLVRGYHYYTGLIFEGYAP--------GLGAP------------------------ 278
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 955482957 438 tvgvgsIAAGGRYDNLVGMFSgskkpDAVPCVGVSIGVERV 478
Cdd:TIGR00443 279 ------LAGGGRYDELLGRFG-----RPLPATGFALNLERL 308
|
|
| hisZ |
PRK12292 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
116-499 |
4.92e-43 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 237043 [Multi-domain] Cd Length: 391 Bit Score: 159.26 E-value: 4.92e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 116 PKGTRDWEPLAMSLRKRIFSTIEDVFSAHGAVTIDTPVFELKEIL--SGKYGEDSKLIYDLQDQGGELCSLRYDLTVPFA 193
Cdd:PRK12292 6 PEGIRDLLPEEARKIEEIRRRLLDLFRRWGYEEVITPTLEYLDTLlaGGGAILDLRTFKLVDQLSGRTLGLRPDMTAQIA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 194 RFVAMNPSEH-GNIKRYHIAKVYRRdQPAMSkGRFREFYQCDIDIAGVYDPMvPDSEVLCILVEALDALGIEGFTIKINH 272
Cdd:PRK12292 86 RIAATRLANRpGPLRLCYAGNVFRA-QERGL-GRSREFLQSGVELIGDAGLE-ADAEVILLLLEALKALGLPNFTLDLGH 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 273 RKILDGIFDICGVPADKIRTISSAVDKLDKSpwsEVkREMTvdKGLAEDVADRIGEYVKLKGGRDLLEKLKAdatMSGHA 352
Cdd:PRK12292 163 VGLFRALLEAAGLSEELEEVLRRALANKDYV---AL-EELV--LDLSEELRDALLALPRLRGGREVLEEARK---LLPSL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 353 IASQGVKDMELLFDYLDVYGISDRMSFDLSLARGLDYYTGLIYEAVTAasappgfsgeaaaqdkapekkskkkksadgee 432
Cdd:PRK12292 234 PIKRALDELEALAEALEKYGYGIPLSLDLGLLRHLDYYTGIVFEGYVD-------------------------------- 281
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 955482957 433 evdestvGVG-SIAAGGRYDNLVGMFSGskkpdAVPCVGVSIGVERVfaimMQRLREKEARGERTSVR 499
Cdd:PRK12292 282 -------GVGnPIASGGRYDDLLGRFGR-----ARPATGFSLDLDRL----LELQLELPVEARKDLVI 333
|
|
| tRNA-synt_His |
pfam13393 |
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ... |
118-478 |
3.66e-41 |
|
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP phosphoribosyltransferase regulatory subunits.
Pssm-ID: 433170 [Multi-domain] Cd Length: 309 Bit Score: 151.58 E-value: 3.66e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 118 GTRDWEPLAMSLRKRIFSTIEDVFSAHGAVTIDTPVFELKEILSGKYGEDSKLIYDLQDQGGELCSLRYDLTVPFARFVA 197
Cdd:pfam13393 1 GIRDLLPPEARRIEELRRRLLDLFRSWGYELVMPPLLEYLDSLLTGTGADLDQTFKLVDQSGRLLGLRADITPQVARIDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 198 MNPSEHGNIKRYHIAKVYRRDQPAMskGRFREFYQCDIDIAGVYDPMVpDSEVLCILVEALDALGIEGFTIKINHRKILD 277
Cdd:pfam13393 81 HRLNRPGPLRLCYAGSVLRTRPKGL--GRSREPLQVGAELIGHAGIEA-DAEIISLLLEALAAAGVPGVTLDLGHVGLVR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 278 GIFDICGVPADKIRTISSAVDKLDkspWSEVkREMTVDKGLAEDVADRIGEYVKLKGGRDLLEKLKADAtmsGHAIASQG 357
Cdd:pfam13393 158 ALLEAAGLSEALEEALRAALQRKD---AAEL-AELAAEAGLPPALRRALLALPDLYGGPEVLDEARAAL---PGLPALQE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 358 VKD-MELLFDYLDVYGISDRMSFDLSLARGLDYYTGLIYEAVTaasapPGFSGEaaaqdkapekkskkkksadgeeevde 436
Cdd:pfam13393 231 ALDeLEALAALLEALGDGVRLTFDLAELRGYEYYTGIVFAAYA-----PGVGEP-------------------------- 279
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 955482957 437 stvgvgsIAAGGRYDNLVGMFSgskkpDAVPCVGVSIGVERV 478
Cdd:pfam13393 280 -------LARGGRYDDLGAAFG-----RARPATGFSLDLEAL 309
|
|
| syh |
CHL00201 |
histidine-tRNA synthetase; Provisional |
117-564 |
9.53e-20 |
|
histidine-tRNA synthetase; Provisional
Pssm-ID: 164576 [Multi-domain] Cd Length: 430 Bit Score: 92.27 E-value: 9.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 117 KGTRDWEPLAMSLRKRIFSTIEDVFSAHGAVTIDTPVFELKEILSGKYGEDSKLI----YDLQDQGGELCSLRYDLTVPF 192
Cdd:CHL00201 8 RGTKDILPDEINYWQFIHDKALTLLSLANYSEIRTPIFENSSLYDRGIGETTDIVnkemYRFTDRSNRDITLRPEGTAGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 193 AR-FVAMNPSEHGNIKR-YHIAKVYRRDQPamSKGRFREFYQCDIDIAGVYDPMVpDSEVLCILVEALDALGIEGFTIKI 270
Cdd:CHL00201 88 VRaFIENKMDYHSNLQRlWYSGPMFRYERP--QSGRQRQFHQLGIEFIGSIDARA-DTEVIHLAMQIFNELQVKNLILDI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 271 NHRKILDgifDICGVPADKIRTISSAVDKLDkspwSEVKREMTVDKGLAEDVADRIGEYVkLKGGRDLLEKLKADATmsg 350
Cdd:CHL00201 165 NSIGKLE---DRQSYQLKLVEYLSQYQDDLD----TDSQNRLYSNPIRILDSKNLKTQEI-LDGAPKISDFLSLEST--- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 351 haiasqgvKDMELLFDYLDVYGISDRMSFdlSLARGLDYYTGLIYEAVTAASappgfsgeaAAQDkapekkskkkksadg 430
Cdd:CHL00201 234 --------EHFYDVCTYLNLLNIPYKINY--KLVRGLDYYNDTAFEIKTLSS---------NGQD--------------- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 431 eeevdestvgvgSIAAGGRYDNLVGMFSGSKkpdaVPCVGVSIGVERVFAIMMQRLrekeargertSVRSKEVDVYVMSV 510
Cdd:CHL00201 280 ------------TICGGGRYDSLIHQLGGPK----TPAVGCAIGLERLLLIAKDNI----------ILPKQSIDVYIATQ 333
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 955482957 511 GEGLLKERMQVAKMLWDAGIKAEfMHKAKPKLPQQFGVVDKEGIPFAVILAPNE 564
Cdd:CHL00201 334 GLKAQKKGWEIIQFLEKQNIKFE-LDLSSSNFHKQIKQAGKKRAKACIILGDNE 386
|
|
| hisZ |
PRK12295 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
141-480 |
3.66e-17 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 183413 [Multi-domain] Cd Length: 373 Bit Score: 83.44 E-value: 3.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 141 FSAHGAVTIDTPVFELKEILSGKYGED-SKLIYDLQDQ-GGELCsLRYDLTVPFAR-FVAMNPSEHgniKRY-HIAKVYR 216
Cdd:PRK12295 18 FEAAGAVRVDPPILQPAEPFLDLSGEDiRRRIFVTSDEnGEELC-LRPDFTIPVCRrHIATAGGEP---ARYaYLGEVFR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 217 RdqpamSKGRFREFYQCDIDIAGVYDPMVPDSEVLCILVEALDALGIEGFTIKINHRKILDGIFDICGVP---------- 286
Cdd:PRK12295 94 Q-----RRDRASEFLQAGIESFGRADPAAADAEVLALALEALAALGPGDLEVRLGDVGLFAALVDALGLPpgwkrrllrh 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 287 --------ADKIRTISSAVDKLD------------KSPWSEVKREM------TVDKGLAEDVADRIGEYVKLKGG----R 336
Cdd:PRK12295 169 fgrprsldALLARLAGPRVDPLDehagvlaaladeAAARALVEDLMsiagisPVGGRSPAEIARRLLEKAALAAAarlpA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 337 DLLEKLKA---------DATMSGHAIASQGVKDMELLFDYLDV-------YGI-SDRMSFDLSLARGLDYYTGLIYEAVT 399
Cdd:PRK12295 249 EALAVLERflaisgppdAALAALRALAADAGLDLDAALDRFEArlaalaaRGIdLERLRFSASFGRPLDYYTGFVFEIRA 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 400 AASAPPgfsgeaaaqdkapekkskkkksadgeeevdestvgvgSIAAGGRYDNLVGMFsGSKKPdaVPCVGVSIGVERVF 479
Cdd:PRK12295 329 AGNGDP-------------------------------------PLAGGGRYDGLLTRL-GAGEP--IPAVGFSIWLDRLA 368
|
.
gi 955482957 480 A 480
Cdd:PRK12295 369 A 369
|
|
| HisRS_anticodon |
cd00859 |
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases ... |
502-602 |
1.81e-16 |
|
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: 74.88 E-value: 1.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 502 EVDVYVMSVGEGLLKERMQVAKMLWDAGIKAEFMHKAkPKLPQQFGVVDKEGIPFAVILAPNEwnADARQVRVKqqkgkd 581
Cdd:cd00859 1 EVDVYVVPLGEGALSEALELAEQLRDAGIKAEIDYGG-RKLKKQFKYADRSGARFAVILGEDE--LAAGVVTVK------ 71
|
90 100
....*....|....*....|.
gi 955482957 582 sDEGQGQGEIVNLDQLIKHLK 602
Cdd:cd00859 72 -DLETGEQETVALDELVEELK 91
|
|
| PRK12421 |
PRK12421 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
128-451 |
2.35e-08 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 237098 Cd Length: 392 Bit Score: 56.52 E-value: 2.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 128 SLRKRIFstieDVFSAHGAVTIDTPVFELKEILSGKYGEDSKL-IYDLQDQ-GGELCSLRYDLTVPFARFVAMNPSEHGn 205
Cdd:PRK12421 26 RLRRRLL----DLFASRGYQLVMPPLIEYLESLLTGAGQDLKLqTFKLIDQlSGRLMGVRADITPQVARIDAHLLNREG- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 206 IKRYHIAKVYRRDQPAmSKGRFREFYQCDIDIAGvYDPMVPDSEVLCILVEALDALGIEGFTIKINHRKILDGIFDICGV 285
Cdd:PRK12421 101 VARLCYAGSVLHTLPQ-GLFGSRTPLQLGAELYG-HAGIEADLEIIRLMLGLLRNAGVPALHLDLGHVGIFRRLAELAGL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 286 PADKIRTISS-----AVDKLDkspwsevkrEMTVDKGLAEDVADRIGEYVKLKGGRDLLEKLKADATMSGHAIAsQGVKD 360
Cdd:PRK12421 179 SPEEEEELFDllqrkALPELA---------EVCQNLGVGSDLRRMFYALARLNGGLEALDRALSVLALQDAAIR-QALDE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 361 MELLFDYLDVYGISDRMSFDLSLARGLDYYTGLIYeavtAASAPpgfsGEAAAqdkapekkskkkksadgeeevdestvg 440
Cdd:PRK12421 249 LKTLAAHLKNRWPELPVSIDLAELRGYHYHTGLVF----AAYIP----GRGQA--------------------------- 293
|
330
....*....|.
gi 955482957 441 vgsIAAGGRYD 451
Cdd:PRK12421 294 ---LARGGRYD 301
|
|
| HGTP_anticodon2 |
pfam12745 |
Anticodon binding domain of tRNAs; This is an HGTP_anticodon binding domain, found largely on ... |
499-603 |
2.04e-05 |
|
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: 46.45 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 499 RSKEVDVYVMSVGEGLLK-ERMQVAKMLWDAGIKAEFMHKAKPKLPQqfgVVDK---EGIPFAVILAPNEWNADARQ--V 572
Cdd:pfam12745 2 KPRRCDVLVASFDASILRtTGVEILQELWAHGISADLAVDASYSPED---LVSRardDGVSWIVIIKQQNKSSDSKYkpL 78
|
90 100 110
....*....|....*....|....*....|..
gi 955482957 573 RVK-QQKGKDSDegqgqgeiVNLDQLIKHLKS 603
Cdd:pfam12745 79 KVKnLLRKEDVD--------LDSDELVSWLRG 102
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
504-604 |
1.74e-04 |
|
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: 40.65 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955482957 504 DVYVMSVGEG---LLKERMQVAKMLWDAGIKAEFmHKAKPKLPQQFGVVDKEGIPFAVILAPNEwnADARQVRVKQQKGk 580
Cdd:pfam03129 1 QVVVIPLGEKaeeLEEYAQKLAEELRAAGIRVEL-DDRNESIGKKFRRADLIGIPFALVVGEKE--LEEGTVTVRRRDT- 76
|
90 100
....*....|....*....|....
gi 955482957 581 dsdegqGQGEIVNLDQLIKHLKSL 604
Cdd:pfam03129 77 ------GEQETVSLDELVEKLKEL 94
|
|
| MetRS_RNA |
cd00939 |
MetRS_RNA binding domain. This short RNA-binding domain is found at the C-terminus of MetRS in ... |
55-96 |
1.34e-03 |
|
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: 37.07 E-value: 1.34e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 955482957 55 LQAARAEQDDKVQQLRAANTEPATLKAEIGKLKKLEAQLAQL 96
Cdd:cd00939 1 LEKEVAEQGNKVRKLKASKADKSVWQPEVNKLLDLKKQLALA 42
|
|
| WHEP-TRS |
pfam00458 |
WHEP-TRS domain; |
55-106 |
1.79e-03 |
|
WHEP-TRS domain;
Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 36.70 E-value: 1.79e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 955482957 55 LQAARAEQDDKVQQLRAANTEPATLKAEIGKLKKLEAQLAQL-GIGAKAGSSK 106
Cdd:pfam00458 1 LTEKIKAQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKALtGKDYKPGAAP 53
|
|
| |
