|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
1-556 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 1100.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 1 MSAESKKAHNFIQSLIEDAVAKGEHTgKVVTRFPPEPNGYLHVGHAKSICLNFGIAETFEGECNLRFDDTNPEKESLEYI 80
Cdd:PRK05347 3 MSEAEARPSNFIRQIIDEDLASGKHT-RVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 81 NAIKRDVEWLGFKWADELRYASDYFDQLYAFAEELIEKGKAYVCALTADEMAEYRGSLKEPGRNSPYRDRPAEESLQLFR 160
Cdd:PRK05347 82 DSIKEDVRWLGFDWSGELRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREYRGTLTEPGKNSPYRDRSVEENLDLFE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 161 DMRDGKFQNGELVLRAKIDMASPNINLRDPILYRIRYADHHQTGDKWCIYPMYDFTHPISDALEGVTHSLCTLEFEDHRP 240
Cdd:PRK05347 162 RMRAGEFPEGSAVLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHRP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 241 LYDWVLDNITIPCHPRQIEFARLNLNYTVTSKRKLKRLVDDNVVDGWDDPRMPTISGMRRRGFTPESIRTFCDMIGVNKA 320
Cdd:PRK05347 242 LYDWVLDNLPIPPHPRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 321 GGTVDVGMLEHAIREDLNARAPRAMCVMRPIKVTLTNYPEGQTETLTLPVHPQNPDMGEREVTWSQVLYIDREDFALEPP 400
Cdd:PRK05347 322 DSVIDMSMLESCIREDLNENAPRAMAVLDPLKLVITNYPEGQVEELEAPNHPEDPEMGTREVPFSRELYIEREDFMEEPP 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 401 RKWKRLAPDQAVRLRGGYVMTCKEVICDDSGDIVELKCEFDPKTLGVNP-EGYKPNGVIHWVSAADSVEVCINQYDRLFN 479
Cdd:PRK05347 402 KKYFRLVPGKEVRLRNAYVIKCEEVVKDADGNITEIHCTYDPDTLSGNPaDGRKVKGTIHWVSAAHAVPAEVRLYDRLFT 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1591635903 480 HEAPDSDKdgDMMDHINSDSLVVLEGaRVEKSLASPGTDLPYQFEREGYFLYDQKlaANAGKPVFNRTVTLRDSWGK 556
Cdd:PRK05347 482 VPNPAAGK--DFLDFLNPDSLVIKQG-FVEPSLADAKPEDRFQFEREGYFCADKD--STPGKLVFNRTVGLRDSWAK 553
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
29-554 |
0e+00 |
|
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found in the cytosolic compartment of eukaryotes, in E. coli and a number of other Gram-negative Bacteria, and in Deinococcus radiodurans. In contrast, the pathway to Gln-tRNA in mitochondria, Archaea, Gram-positive Bacteria, and a number of other lineages is by misacylation with Glu followed by transamidation to correct the aminoacylation to Gln. This enzyme is a class I tRNA synthetase (hit by the pfam model tRNA-synt_1c) and is quite closely related to glutamyl-tRNA synthetases. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273079 [Multi-domain] Cd Length: 522 Bit Score: 718.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 29 VVTRFPPEPNGYLHVGHAKSICLNFGIAETFEGECNLRFDDTNPEKESLEYINAIKRDVEWLGFKWADELRYASDYFDQL 108
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEGKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 109 YAFAEELIEKGKAYVCALTADEMAEYRGSLKEPGRNSPYRDRPAEESLQLFRDMRDGKFQNGELVLRAKIDMASPNINLR 188
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIREYRGTLTDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 189 DPILYRIRYADHHQTGDKWCIYPMYDFTHPISDALEGVTHSLCTLEFEDHRPLYDWVLDNITIPCHPRQIEFARLNLNYT 268
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFPRPAQYEFSRLNLEGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 269 VTSKRKLKRLVDDNVVDGWDDPRMPTISGMRRRGFTPESIRTFCDMIGVNKAGGTVDVGMLEHAIREDLNARAPRAMCVM 348
Cdd:TIGR00440 241 VLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAVI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 349 RPIKVTLTNYpEGQTETLTLPVHPQNPDMGEREVTWSQVLYIDREDFALEPPRKWKRLAPDQAVRLRGGYVMTCKEVICD 428
Cdd:TIGR00440 321 DPVEVVIENL-SDEYELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAERVEKD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 429 DSGDIVELKCEFDPKTLGVNP-EGYKPNGVIHWVSAADSVEVCINQYDRLFNHEAPDSDKdgDMMDHINSDSLVVLEGAr 507
Cdd:TIGR00440 400 AAGKITTIFCTYDNKTLGKEPaDGRKVKGVIHWVSASSKYPTETRLYDRLFKVPNPGAPD--DFLSVINPESLVIKQGF- 476
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1591635903 508 VEKSLASPGTDLPYQFEREGYFLYDQKlAANAGKPVFNRTVTLRDSW 554
Cdd:TIGR00440 477 MEHSLGDAVANKRFQFEREGYFCLDSK-ESTTEKVVFNRTVSLKDAT 522
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
28-343 |
7.78e-151 |
|
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) cataytic core domain. These enzymes attach Gln to the appropriate tRNA. Like other class I tRNA synthetases, they aminoacylate the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. GlnRS contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. These enzymes function as monomers. Archaea and most bacteria lack GlnRS. In these organisms, the "non-discriminating" form of GluRS aminoacylates both tRNA(Glu) and tRNA(Gln) with Glu, which is converted to Gln when appropriate by a transamidation enzyme.
Pssm-ID: 185676 [Multi-domain] Cd Length: 238 Bit Score: 432.06 E-value: 7.78e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 28 KVVTRFPPEPNGYLHVGHAKSICLNFGIAETFEGECNLRFDDTNPEKESLEYINAIKRDVEWLGFKWaDELRYASDYFDQ 107
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKP-YKVTYASDYFDQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 108 LYAFAEELIEKGKAYVcaltademaeyrgslkepgrnspyrdrpaeeslqlfrdmrdgkfqngelvlrakidmaspninl 187
Cdd:cd00807 80 LYEYAEQLIKKGKAYV---------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 188 rdpilyriryadHHQTGDKWCIYPMYDFTHPISDALEGVTHSLCTLEFEDHRPLYDWVLDNITIPChPRQIEFARLNLNY 267
Cdd:cd00807 96 ------------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYR-PHQWEFSRLNLTY 162
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1591635903 268 TVTSKRKLKRLVDDNVVDGWDDPRMPTISGMRRRGFTPESIRTFCDMIGVNKAGGTVDVGMLEHAIREDLNARAPR 343
Cdd:cd00807 163 TVMSKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
28-338 |
6.85e-146 |
|
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are too dissimilar to be included. This family includes only glutamyl and glutaminyl tRNA synthetases. In some organizms, a single glutamyl-tRNA synthetase aminoacylates both tRNA(Glu) and tRNA(Gln).
Pssm-ID: 395606 [Multi-domain] Cd Length: 314 Bit Score: 422.50 E-value: 6.85e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 28 KVVTRFPPEPNGYLHVGHAKSICLNFGIAETFEGECNLRFDDTNPEKESLEYINAIKRDVEWLGFKWADELRYASDYFDQ 107
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 108 LYAFAEELIEKGKAYVCALTADEMAEYRGSLkePGRNSPYRDRPAEESLQLF-RDMRDGKFQNGELVLRAKIDMASPnIN 186
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEREEQ--EALGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMESP-YV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 187 LRDPILYRIRYA---DHHQTGDKWCIYPMYDFTHPISDALEGVTHSLCTLEFEDHRPLYDWVLDNITIPCHPRQIEFARL 263
Cdd:pfam00749 158 FRDPVRGRIKFTpqeIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHEYLRL 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1591635903 264 NLNYTVTSKRKLKRLVDDNVVDGWDDPRMPTISGMRRRGFTPESIRTFCDMIGVNKAggtVDVGMLEHAI----REDLN 338
Cdd:pfam00749 238 NLDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKS---FDVNRLSKSLeafdRKKLD 313
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
25-464 |
2.45e-134 |
|
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Glutamyl- or glutaminyl-tRNA synthetase is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 439779 [Multi-domain] Cd Length: 467 Bit Score: 398.78 E-value: 2.45e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 25 HTGKVVTRFPPEPNGYLHVGHAKSICLNFGIAETFEGECNLRFDDTNPEKESLEYINAIKRDVEWLGFKWADELRYASDY 104
Cdd:COG0008 1 HGMKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGPYYQSDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 105 FDQLYAFAEELIEKGKAYVCALTADEMAEYRGSLKEPGRNSPY----RDRPAEEslqlfrdmRDGKFQNGEL-VLRAKI- 178
Cdd:COG0008 81 FDIYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYdgrcRDLSPEE--------LERMLAAGEPpVLRFKIp 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 179 -------DMAS-----PNINLRDPILYRiryADhhqtGdkwciYPMYDFTHPISDALEGVTHSLCTLEFEDHRPLYDWVL 246
Cdd:COG0008 153 eegvvfdDLVRgeitfPNPNLRDPVLYR---AD----G-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLY 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 247 DNITIPcHPrqiEFARLNLNY----TVTSKRKlkrlvddNVVdgwddprmpTISGMRRRGFTPESIRTFCDMIGVNKAGG 322
Cdd:COG0008 221 EALGWE-PP---EFAHLPLILgpdgTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALLGWSKSDD 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 323 TV--DVGMLEHAIreDLNaRAPRAMCVMRPIKVTLTNYPEGQT---ETLTLPVHPQNPDMGERE---------------- 381
Cdd:COG0008 281 QEifSLEELIEAF--DLD-RVSRSPAVFDPVKLVWLNGPYIRAlddEELAELLAPELPEAGIREdlerlvplvreraktl 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 382 ---VTWSQVLYIDREDfalEPPRKwKRLAPDQAVRlrggyVMTCkevicddSGDIVELKCEFDPKTLgvnpegykpNGVI 458
Cdd:COG0008 358 selAELARFFFIERED---EKAAK-KRLAPEEVRK-----VLKA-------ALEVLEAVETWDPETV---------KGTI 412
|
....*.
gi 1591635903 459 HWVSAA 464
Cdd:COG0008 413 HWVSAE 418
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
1-556 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 1100.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 1 MSAESKKAHNFIQSLIEDAVAKGEHTgKVVTRFPPEPNGYLHVGHAKSICLNFGIAETFEGECNLRFDDTNPEKESLEYI 80
Cdd:PRK05347 3 MSEAEARPSNFIRQIIDEDLASGKHT-RVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 81 NAIKRDVEWLGFKWADELRYASDYFDQLYAFAEELIEKGKAYVCALTADEMAEYRGSLKEPGRNSPYRDRPAEESLQLFR 160
Cdd:PRK05347 82 DSIKEDVRWLGFDWSGELRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREYRGTLTEPGKNSPYRDRSVEENLDLFE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 161 DMRDGKFQNGELVLRAKIDMASPNINLRDPILYRIRYADHHQTGDKWCIYPMYDFTHPISDALEGVTHSLCTLEFEDHRP 240
Cdd:PRK05347 162 RMRAGEFPEGSAVLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHRP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 241 LYDWVLDNITIPCHPRQIEFARLNLNYTVTSKRKLKRLVDDNVVDGWDDPRMPTISGMRRRGFTPESIRTFCDMIGVNKA 320
Cdd:PRK05347 242 LYDWVLDNLPIPPHPRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 321 GGTVDVGMLEHAIREDLNARAPRAMCVMRPIKVTLTNYPEGQTETLTLPVHPQNPDMGEREVTWSQVLYIDREDFALEPP 400
Cdd:PRK05347 322 DSVIDMSMLESCIREDLNENAPRAMAVLDPLKLVITNYPEGQVEELEAPNHPEDPEMGTREVPFSRELYIEREDFMEEPP 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 401 RKWKRLAPDQAVRLRGGYVMTCKEVICDDSGDIVELKCEFDPKTLGVNP-EGYKPNGVIHWVSAADSVEVCINQYDRLFN 479
Cdd:PRK05347 402 KKYFRLVPGKEVRLRNAYVIKCEEVVKDADGNITEIHCTYDPDTLSGNPaDGRKVKGTIHWVSAAHAVPAEVRLYDRLFT 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1591635903 480 HEAPDSDKdgDMMDHINSDSLVVLEGaRVEKSLASPGTDLPYQFEREGYFLYDQKlaANAGKPVFNRTVTLRDSWGK 556
Cdd:PRK05347 482 VPNPAAGK--DFLDFLNPDSLVIKQG-FVEPSLADAKPEDRFQFEREGYFCADKD--STPGKLVFNRTVGLRDSWAK 553
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
8-558 |
0e+00 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 830.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 8 AHNFIQSLIEDAVAKGEHtGKVVTRFPPEPNGYLHVGHAKSICLNFGIAETFEGECNLRFDDTNPEKESLEYINAIKRDV 87
Cdd:PRK14703 12 SPNFITEIIEEDLEAGRY-PRVVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETEDTEYVEAIKDDV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 88 EWLGFKWADELRYASDYFDQLYAFAEELIEKGKAYVCALTADEMAEYRGSLKEPGRNSPYRDRPAEESLQLFRDMRDGKF 167
Cdd:PRK14703 91 RWLGFDWGEHLYYASDYFERMYAYAEQLIKMGLAYVDSVSEEEIRELRGTVTEPGTPSPYRDRSVEENLDLFRRMRAGEF 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 168 QNGELVLRAKIDMASPNINLRDPILYRIRYADHHQTGDKWCIYPMYDFTHPISDALEGVTHSLCTLEFEDHRPLYDWVLD 247
Cdd:PRK14703 171 PDGAHVLRAKIDMSSPNMKLRDPLLYRIRHAHHYRTGDEWCIYPMYDFAHPLEDAIEGVTHSICTLEFENNRAIYDWVLD 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 248 NIT-IPCHPRQIEFARLNLNYTVTSKRKLKRLVDDNVVDGWDDPRMPTISGMRRRGFTPESIRTFCDMIGVNKAGGTVDV 326
Cdd:PRK14703 251 HLGpWPPRPRQYEFARLALGYTVMSKRKLRELVEEGYVSGWDDPRMPTIAGQRRRGVTPEAIRDFADQIGVAKTNSTVDI 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 327 GMLEHAIREDLNARAPRAMCVMRPIKVTLTNYPEGQTETLTLPVHPQN-PDMGEREVTWSQVLYIDREDFALEPPRKWKR 405
Cdd:PRK14703 331 GVLEFAIRDDLNRRAPRVMAVLDPLKVVIENLPAGKVEELDLPYWPHDvPKEGSRKVPFTRELYIERDDFSEDPPKGFKR 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 406 LAPDQAVRLRGGYVMTCKEVICDDSGDIVELKCEFDPKTLGVNPEGYKPNGVIHWVSAADSVEVCINQYDRLFNHEAPDS 485
Cdd:PRK14703 411 LTPGREVRLRGAYIIRCDEVVRDADGAVTELRCTYDPESAKGEDTGRKAAGVIHWVSAKHALPAEVRLYDRLFKVPQPEA 490
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1591635903 486 dKDGDMMDHINSDSLVVLEGaRVEKSLASPGTDLPYQFEREGYFLYDqKLAANAGKPVFNRTVTLRDSWGKGG 558
Cdd:PRK14703 491 -ADEDFLEFLNPDSLRVAQG-RVEPAVRDDPADTRYQFERQGYFWAD-PVDSRPDALVFNRIITLKDTWGARA 560
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
29-554 |
0e+00 |
|
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found in the cytosolic compartment of eukaryotes, in E. coli and a number of other Gram-negative Bacteria, and in Deinococcus radiodurans. In contrast, the pathway to Gln-tRNA in mitochondria, Archaea, Gram-positive Bacteria, and a number of other lineages is by misacylation with Glu followed by transamidation to correct the aminoacylation to Gln. This enzyme is a class I tRNA synthetase (hit by the pfam model tRNA-synt_1c) and is quite closely related to glutamyl-tRNA synthetases. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273079 [Multi-domain] Cd Length: 522 Bit Score: 718.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 29 VVTRFPPEPNGYLHVGHAKSICLNFGIAETFEGECNLRFDDTNPEKESLEYINAIKRDVEWLGFKWADELRYASDYFDQL 108
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEGKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 109 YAFAEELIEKGKAYVCALTADEMAEYRGSLKEPGRNSPYRDRPAEESLQLFRDMRDGKFQNGELVLRAKIDMASPNINLR 188
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIREYRGTLTDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 189 DPILYRIRYADHHQTGDKWCIYPMYDFTHPISDALEGVTHSLCTLEFEDHRPLYDWVLDNITIPCHPRQIEFARLNLNYT 268
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFPRPAQYEFSRLNLEGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 269 VTSKRKLKRLVDDNVVDGWDDPRMPTISGMRRRGFTPESIRTFCDMIGVNKAGGTVDVGMLEHAIREDLNARAPRAMCVM 348
Cdd:TIGR00440 241 VLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAVI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 349 RPIKVTLTNYpEGQTETLTLPVHPQNPDMGEREVTWSQVLYIDREDFALEPPRKWKRLAPDQAVRLRGGYVMTCKEVICD 428
Cdd:TIGR00440 321 DPVEVVIENL-SDEYELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAERVEKD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 429 DSGDIVELKCEFDPKTLGVNP-EGYKPNGVIHWVSAADSVEVCINQYDRLFNHEAPDSDKdgDMMDHINSDSLVVLEGAr 507
Cdd:TIGR00440 400 AAGKITTIFCTYDNKTLGKEPaDGRKVKGVIHWVSASSKYPTETRLYDRLFKVPNPGAPD--DFLSVINPESLVIKQGF- 476
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1591635903 508 VEKSLASPGTDLPYQFEREGYFLYDQKlAANAGKPVFNRTVTLRDSW 554
Cdd:TIGR00440 477 MEHSLGDAVANKRFQFEREGYFCLDSK-ESTTEKVVFNRTVSLKDAT 522
|
|
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
27-559 |
0e+00 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 567.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 27 GKVVTRFPPEPNGYLHVGHAKSICLNFGIAETFEGECNLRFDDTNPEKESLEYINAIKRDVEWLGFKwADELRYASDYFD 106
Cdd:PLN02859 263 GKVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIEEIVEWMGWE-PFKITYTSDYFQ 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 107 QLYAFAEELIEKGKAYVCALTADEMAEYRgslkEPGRNSPYRDRPAEESLQLFRDMRDGKFQNGELVLRAKIDMASPNIN 186
Cdd:PLN02859 342 ELYELAVELIRRGHAYVDHQTPEEIKEYR----EKKMNSPWRDRPIEESLKLFEDMRRGLIEEGKATLRMKQDMQNDNFN 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 187 LRDPILYRIRYADHHQTGDKWCIYPMYDFTHPISDALEGVTHSLCTLEFEDHRPLYDWVLDNITIpCHPRQIEFARLNLN 266
Cdd:PLN02859 418 MYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLDSLGL-YQPYVWEYSRLNVT 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 267 YTVTSKRKLKRLVDDNVVDGWDDPRMPTISGMRRRGFTPESIRTFCDMIGVNKA-GGTVDVGMLEHAIREDLNARAPRAM 345
Cdd:PLN02859 497 NTVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITRSdNSLIRMDRLEHHIREELNKTAPRTM 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 346 CVMRPIKVTLTNYPEGQTETL---TLPVHPQNPDMGEREVTWSQVLYIDREDFALEPPRKWKRLAPDQAVRLRGGYVMTC 422
Cdd:PLN02859 577 VVLHPLKVVITNLESGEVIELdakRWPDAQNDDPSAFYKVPFSRVVYIERSDFRLKDSKDYYGLAPGKSVLLRYAFPIKC 656
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 423 KEVIC-DDSGDIVELKCEFDPKtlgvnpEGYKPNGVIHWVSAA----DSVEVCINQYDRLFNHEAPDSDKdgDMMDHINS 497
Cdd:PLN02859 657 TDVVLaDDNETVVEIRAEYDPE------KKTKPKGVLHWVAEPspgvEPLKVEVRLFDKLFLSENPAELE--DWLEDLNP 728
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1591635903 498 DSLVVLEGARVEKSLASPGTDLPYQFEREGYFLYDQKlaANAGKPVFNRTVTLRDSWGKGGK 559
Cdd:PLN02859 729 QSKEVISGAYAVPSLKDAKVGDRFQFERLGYFAVDKD--STPEKLVFNRTVTLKDSYGKGGK 788
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
27-557 |
9.97e-158 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 462.53 E-value: 9.97e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 27 GKVVTRFPPEPNGYLHVGHAKSICLNFGIAETFEGECNLRFDDTNPEKESLEYINAIKRDVEWLGFKwADELRYASDYFD 106
Cdd:PTZ00437 50 GKPYFRFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTNPETEEQVYIDAIMEMVKWMGWK-PDWVTFSSDYFD 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 107 QLYAFAEELIEKGKAYVCALTADEMAEYRGSLKEpgrnSPYRDRPAEESLQLFRDMRDGKFQNGELVLRAKIDMASPNIN 186
Cdd:PTZ00437 129 QLHEFAVQLIKDGKAYVDHSTPDELKQQREQRED----SPWRNRSVEENLLLFEHMRQGRYAEGEATLRVKADMKSDNPN 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 187 LRDPILYRIRYADHHQTGDKWCIYPMYDFTHPISDALEGVTHSLCTLEFEDHRPLYDWVLDNITIpCHPRQIEFARLNLN 266
Cdd:PTZ00437 205 MRDFIAYRVKYVEHPHAKDKWCIYPSYDFTHCLIDSLEDIDYSLCTLEFETRRESYFWLLEELNL-WRPHVWEFSRLNVT 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 267 YTVTSKRKLKRLVDDNVVDGWDDPRMPTISGMRRRGFTPESIRTFCDMIGVNKAGGTVDVGMLEHAIREDLNARAPRAMC 346
Cdd:PTZ00437 284 GSLLSKRKINVLVRKGIVRGFDDPRLLTLAGMRRRGYTPAAINRFCELVGITRSMNVIQISMLENTLREDLDERCERRLM 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 347 VMRPIKVTLTNYpEGQTEtLTLPVHPQNPDMGEREVTWSQVLYIDREDFALEP-PRKWKRLAPD-QAVRLRGGYVMTCKE 424
Cdd:PTZ00437 364 VIDPIKVVVDNW-KGERE-FECPNHPRKPELGSRKVMFTDTFYVDRSDFRTEDnNSKFYGLAPGpRVVGLKYSGNVVCKG 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 425 VICDDSGD--IVELKCEFDPKTlgvnpegyKPNGVIHWVSAADSVEVCINQYDRLFNHEApdSDKDGDMMDHINSDSLVV 502
Cdd:PTZ00437 442 FEVDAAGQpsVIHVDIDFERKD--------KPKTNISWVSATACTPVEVRLYNALLKDDR--AAIDPEFLKFIDEDSEVV 511
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1591635903 503 LEGaRVEKSLASPGTDLPYQFEREGYFLYDQKlaANAGKPVFNRTVTLRDSWGKG 557
Cdd:PTZ00437 512 SHG-YAEKGIENAKHFESVQAERFGYFVVDPD--TRPDHLVMNRVLGLREDKEKA 563
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
28-343 |
7.78e-151 |
|
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) cataytic core domain. These enzymes attach Gln to the appropriate tRNA. Like other class I tRNA synthetases, they aminoacylate the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. GlnRS contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. These enzymes function as monomers. Archaea and most bacteria lack GlnRS. In these organisms, the "non-discriminating" form of GluRS aminoacylates both tRNA(Glu) and tRNA(Gln) with Glu, which is converted to Gln when appropriate by a transamidation enzyme.
Pssm-ID: 185676 [Multi-domain] Cd Length: 238 Bit Score: 432.06 E-value: 7.78e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 28 KVVTRFPPEPNGYLHVGHAKSICLNFGIAETFEGECNLRFDDTNPEKESLEYINAIKRDVEWLGFKWaDELRYASDYFDQ 107
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKP-YKVTYASDYFDQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 108 LYAFAEELIEKGKAYVcaltademaeyrgslkepgrnspyrdrpaeeslqlfrdmrdgkfqngelvlrakidmaspninl 187
Cdd:cd00807 80 LYEYAEQLIKKGKAYV---------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 188 rdpilyriryadHHQTGDKWCIYPMYDFTHPISDALEGVTHSLCTLEFEDHRPLYDWVLDNITIPChPRQIEFARLNLNY 267
Cdd:cd00807 96 ------------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYR-PHQWEFSRLNLTY 162
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1591635903 268 TVTSKRKLKRLVDDNVVDGWDDPRMPTISGMRRRGFTPESIRTFCDMIGVNKAGGTVDVGMLEHAIREDLNARAPR 343
Cdd:cd00807 163 TVMSKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
28-338 |
6.85e-146 |
|
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are too dissimilar to be included. This family includes only glutamyl and glutaminyl tRNA synthetases. In some organizms, a single glutamyl-tRNA synthetase aminoacylates both tRNA(Glu) and tRNA(Gln).
Pssm-ID: 395606 [Multi-domain] Cd Length: 314 Bit Score: 422.50 E-value: 6.85e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 28 KVVTRFPPEPNGYLHVGHAKSICLNFGIAETFEGECNLRFDDTNPEKESLEYINAIKRDVEWLGFKWADELRYASDYFDQ 107
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 108 LYAFAEELIEKGKAYVCALTADEMAEYRGSLkePGRNSPYRDRPAEESLQLF-RDMRDGKFQNGELVLRAKIDMASPnIN 186
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEREEQ--EALGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMESP-YV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 187 LRDPILYRIRYA---DHHQTGDKWCIYPMYDFTHPISDALEGVTHSLCTLEFEDHRPLYDWVLDNITIPCHPRQIEFARL 263
Cdd:pfam00749 158 FRDPVRGRIKFTpqeIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHEYLRL 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1591635903 264 NLNYTVTSKRKLKRLVDDNVVDGWDDPRMPTISGMRRRGFTPESIRTFCDMIGVNKAggtVDVGMLEHAI----REDLN 338
Cdd:pfam00749 238 NLDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKS---FDVNRLSKSLeafdRKKLD 313
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
25-464 |
2.45e-134 |
|
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Glutamyl- or glutaminyl-tRNA synthetase is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 439779 [Multi-domain] Cd Length: 467 Bit Score: 398.78 E-value: 2.45e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 25 HTGKVVTRFPPEPNGYLHVGHAKSICLNFGIAETFEGECNLRFDDTNPEKESLEYINAIKRDVEWLGFKWADELRYASDY 104
Cdd:COG0008 1 HGMKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGPYYQSDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 105 FDQLYAFAEELIEKGKAYVCALTADEMAEYRGSLKEPGRNSPY----RDRPAEEslqlfrdmRDGKFQNGEL-VLRAKI- 178
Cdd:COG0008 81 FDIYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYdgrcRDLSPEE--------LERMLAAGEPpVLRFKIp 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 179 -------DMAS-----PNINLRDPILYRiryADhhqtGdkwciYPMYDFTHPISDALEGVTHSLCTLEFEDHRPLYDWVL 246
Cdd:COG0008 153 eegvvfdDLVRgeitfPNPNLRDPVLYR---AD----G-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLY 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 247 DNITIPcHPrqiEFARLNLNY----TVTSKRKlkrlvddNVVdgwddprmpTISGMRRRGFTPESIRTFCDMIGVNKAGG 322
Cdd:COG0008 221 EALGWE-PP---EFAHLPLILgpdgTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALLGWSKSDD 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 323 TV--DVGMLEHAIreDLNaRAPRAMCVMRPIKVTLTNYPEGQT---ETLTLPVHPQNPDMGERE---------------- 381
Cdd:COG0008 281 QEifSLEELIEAF--DLD-RVSRSPAVFDPVKLVWLNGPYIRAlddEELAELLAPELPEAGIREdlerlvplvreraktl 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 382 ---VTWSQVLYIDREDfalEPPRKwKRLAPDQAVRlrggyVMTCkevicddSGDIVELKCEFDPKTLgvnpegykpNGVI 458
Cdd:COG0008 358 selAELARFFFIERED---EKAAK-KRLAPEEVRK-----VLKA-------ALEVLEAVETWDPETV---------KGTI 412
|
....*.
gi 1591635903 459 HWVSAA 464
Cdd:COG0008 413 HWVSAE 418
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
1-542 |
1.99e-107 |
|
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the eukaryotic cytosol and of the Archaea are more similar to glutaminyl-tRNA synthetases than to bacterial glutamyl-tRNA synthetases. This model models just the eukaryotic cytosolic and archaeal forms of the enzyme. In some eukaryotes, the glutamyl-tRNA synthetase is part of a longer, multifunctional aminoacyl-tRNA ligase. In many species, the charging of tRNA(gln) proceeds first through misacylation with Glu and then transamidation. For this reason, glutamyl-tRNA synthetases, including all known archaeal enzymes (as of 2010) may act on both tRNA(gln) and tRNA(glu). [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273091 [Multi-domain] Cd Length: 556 Bit Score: 332.94 E-value: 1.99e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 1 MSAESKKAHNFIQSLIEDAVAKgehTGKVVTRFPPEPNGYLHVGHAKSICLNFGIAETFEGECNLRFDDTNPEKESLEYI 80
Cdd:TIGR00463 69 LGLDIKKKEKKRKGLRELPGAK---MGEVVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAY 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 81 NAIKRDVEWLGFKWaDELRYASDYFDQLYAFAEELIEKGKAYVCALTADEMAEYRGSlkepGRNSPYRDRPAEESLQLFR 160
Cdd:TIGR00463 146 DMILEDLEWLGVKW-DEVVYQSDRIETYYDYTRKLIEMGKAYVCDCRPEEFRELRNR----GEACHCRDRSVEENLERWE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 161 DMRDGKFQNGELVLRAKIDMASPNINLRDPILYRIRYADHHQTGDKWCIYPMYDFTHPISDALEGVTHSLCTLEFEDH-- 238
Cdd:TIGR00463 221 EMLEGKEEGGSVVVRVKTDLKHKNPAIRDWVIFRIVKTPHPRTGDKYRVYPTMDFSVAIDDHLLGVTHVLRGKDHIDNrr 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 239 RPLYDWVLDNITIPcHPRQIEFARLNLNYTVTSKRKLKRLVDDNVVdGWDDPRMPTISGMRRRGFTPESIRTFCDMIGVN 318
Cdd:TIGR00463 301 KQEYIYRYFGWEPP-EFIHWGRLKIDDVRALSTSSARKGILRGEYS-GWDDPRLPTLRAIRRRGIRPEAIRKFMLSIGVK 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 319 KAGGTVDVGMLEHAIREDLNARAPRAMCVMRPIKVTLTNYPEGQTEtlTLPVHPQNPDMGEREVTWSQVLYIDREDFALE 398
Cdd:TIGR00463 379 INDVTMSWKNIYALNRKIIDEEARRYFFIWNPVKIEIVGLPEPKRV--ERPLHPDHPEIGERVLILRGEIYVPKDDLEEG 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 399 PprkwkrlapdQAVRLrggyvMTCKEVICDdsgdivelkcEFDPKTLGVNPEGYKPNG--VIHWVSAADSVEVcinqydr 476
Cdd:TIGR00463 457 V----------EPVRL-----MDAVNVIYS----------KKELRYHSEGLEGARKLGksIIHWLPAKDAVKV------- 504
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1591635903 477 lfnheapdsdkdgdmmDHINSDSLVVlEGaRVEKSLASPGTDLPYQFEREGYFLYDQklAANAGKP 542
Cdd:TIGR00463 505 ----------------KVIMPDASIV-EG-VIEADASELEVGDVVQFERFGFARLDS--ADKDGMV 550
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
6-532 |
6.32e-107 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 333.08 E-value: 6.32e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 6 KKAHNFIQSLIEDAVAKGEHT----------GKVVTRFPPEPNGYLHVGHAKSICLNFGIAETFEGECNLRFDDTNPEKE 75
Cdd:PTZ00402 20 KALTSFLSNTYFTAANANEENdklqltnaeeGKVVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 76 SLEYINAIKRDVEWLGFKWADELRYASDYFDQLYAFAEELIEKGKAYVCALTADEMAEYRGSlkepGRNSPYRDRPAEES 155
Cdd:PTZ00402 100 KEHFEQAILDDLATLGVSWDVGPTYSSDYMDLMYEKAEELIKKGLAYCDKTPREEMQKCRFD----GVPTKYRDISVEET 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 156 LQLFRDMRDGKFQNGELVLRAKIDMASPNINLRDPILYRIRYADHHQTGDKWCIYPMYDFTHPISDALEGVTHSLCTLEF 235
Cdd:PTZ00402 176 KRLWNEMKKGSAEGQETCLRAKISVDNENKAMRDPVIYRVNLTPHARQGTKYKAYPTYDFCCPIIDSVEGVTHALRTNEY 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 236 EDHRPLYDWVLDNITIPcHPRQIEFARLNLNYTVTSKRKLKRLVDDNVVDGWDDPRMPTISGMRRRGFTPESIRTFCDMI 315
Cdd:PTZ00402 256 HDRNDQYYWFCDALGIR-KPIVEDFSRLNMEYSVMSKRKLTQLVDTHVVDGWDDPRFPTVRALVRRGLKMEALRQFVQEQ 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 316 GVNKAGGTVDVGMLEHAIREDLNARAPRAMCVMRPIKVTLTNYPEGQTETLTLPVHPQNPDMGEREVTWSQVLYIDREDF 395
Cdd:PTZ00402 335 GMSKTVNFMEWSKLWYFNTQILDPSVPRYTVVSNTLKVRCTVEGQIHLEACEKLLHKKVPDMGEKTYYKSDVIFLDAEDV 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 396 ALepprkwkrLAPDQAVRLR---GGYVMTCKEviCDDSGDIVElkcefdpKTLGVNPEG--YKPNGVIHWVSAADSVEVC 470
Cdd:PTZ00402 415 AL--------LKEGDEVTLMdwgNAYIKNIRR--SGEDALITD-------ADIVLHLEGdvKKTKFKLTWVPESPKAEVM 477
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1591635903 471 -INQYDRLFNHEAPDSDKDgdmMDHINSDSLVVLEGARVEKSLASPGTDLPYQFEREGYFLYD 532
Cdd:PTZ00402 478 eLNEYDHLLTKKKPDPEES---IDDIIAPVTKYTQEVYGEEALSVLKKGDIIQLERRGYYIVD 537
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
23-543 |
2.17e-106 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 335.16 E-value: 2.17e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 23 GEHTGKVVTRFPPEPNGYLHVGHAKSICLNFGIAETFEGECNLRFDDTNPEKESLEYINAIKRDVEWLGFKWaDELRYAS 102
Cdd:PLN02907 208 GAEEGKVCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIKY-DAVTYTS 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 103 DYFDQLYAFAEELIEKGKAYVCALTADEMAEYRGSLKEpgrnSPYRDRPAEESLQLFRDMRDGKFQNGELVLRAKIDMAS 182
Cdd:PLN02907 287 DYFPQLMEMAEKLIKEGKAYVDDTPREQMRKERMDGIE----SKCRNNSVEENLRLWKEMIAGSERGLQCCVRGKLDMQD 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 183 PNINLRDPILYRIRYADHHQTGDKWCIYPMYDFTHPISDALEGVTHSLCTLEFEDHRPLYDWVLDNITIPcHPRQIEFAR 262
Cdd:PLN02907 363 PNKSLRDPVYYRCNPTPHHRIGSKYKVYPTYDFACPFVDALEGVTHALRSSEYHDRNAQYYRILEDMGLR-KVHIWEFSR 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 263 LNLNYTVTSKRKLKRLVDDNVVDGWDDPRMPTISGMRRRGFTPESIRTFCDMIGVNKaggtvDVGMLEHAIREDLNAR-- 340
Cdd:PLN02907 442 LNFVYTLLSKRKLQWFVDNGKVEGWDDPRFPTVQGIVRRGLKIEALKQFILSQGASK-----NLNLMEWDKLWTINKKii 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 341 ---APRAMCVMRPIKV--TLTNYPEgQTETLTLPVHPQNPDMGEREVTWSQVLYIDREDFALepprkwkrLAPDQAVRLR 415
Cdd:PLN02907 517 dpvCPRHTAVLKEGRVllTLTDGPE-TPFVRIIPRHKKYEGAGKKATTFTNRIWLDYADAEA--------ISEGEEVTLM 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 416 GGYVMTCKEVICDDSGDIVELKCEfdpktlgVNPEG-YKPNGV-IHWVSA-ADSVEVCINQYDRLFNHEAPDSDKdgDMM 492
Cdd:PLN02907 588 DWGNAIIKEITKDEGGAVTALSGE-------LHLEGsVKTTKLkLTWLPDtNELVPLSLVEFDYLITKKKLEEDD--NFL 658
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1591635903 493 DHINSDSlvvlegaRVEKS-LASP-------GTDLpyQFEREGYFLYDQKLaANAGKPV 543
Cdd:PLN02907 659 DVLNPCT-------KKETAaLGDSnmrnlkrGEII--QLERKGYYRCDAPF-VRSSKPI 707
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
27-469 |
1.48e-97 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 307.55 E-value: 1.48e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 27 GKVVTRFPPEPNGYLHVGHAKSICLNFGIAETFEGECNLRFDDTNPEKES--LEYINAIKRDVEWLGFKWaDELRYASDY 104
Cdd:PRK04156 100 GKVVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDPRTKRpdPEAYDMILEDLKWLGVKW-DEVVIQSDR 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 105 FDQLYAFAEELIEKGKAYVCALTADEMAEYRGSlkepGRNSPYRDRPAEESLQLFRDMRDGKFQNGELVLRAKIDMASPN 184
Cdd:PRK04156 179 LEIYYEYARKLIEMGGAYVCTCDPEEFKELRDA----GKPCPHRDKSPEENLELWEKMLDGEYKEGEAVVRVKTDLEHPN 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 185 INLRDPILYRIRYADHHQTGDKWCIYPMYDFTHPISDALEGVTHslcTLEFEDH-------RPLYD---WVLdnitipch 254
Cdd:PRK04156 255 PSVRDWVAFRIVKTPHPRVGDKYRVWPTYNFAVAVDDHLLGVTH---VLRGKDHidntekqRYIYDyfgWEY-------- 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 255 PRQIEFARLNLNYTVTSKRKLKRLVDDNVVDGWDDPRMPTISGMRRRGFTPESIRTFCDMIGVNKAGGTVDVGMLeHAI- 333
Cdd:PRK04156 324 PETIHYGRLKIEGFVLSTSKIRKGIEEGEYSGWDDPRLPTLRALRRRGILPEAIRELIIEVGVKETDATISWENL-YAIn 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 334 REDLNARAPRAMCVMRPIKVTLTNYPEgqtETLTLPVHPQNPDMGEREVTWSQVLYIDREDFALEPPRkwkrlapdqaVR 413
Cdd:PRK04156 403 RKLIDPIANRYFFVRDPVELEIEGAEP---LEAKIPLHPDRPERGEREIPVGGKVYVSSDDLEAEGKM----------VR 469
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1591635903 414 LrggyvmtcKEVICDDSGDIVELKCEFDPKTLGVNPEGYKPngVIHWVSAADSVEV 469
Cdd:PRK04156 470 L--------MDLFNVEITGVSVDKARYHSDDLEEARKNKAP--IIQWVPEDESVPV 515
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
22-543 |
6.20e-92 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 291.53 E-value: 6.20e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 22 KGEHTGKVVTRFPPEPNGYLHVGHAKSICLNFGIAETFEGECNLRFDDTNPEKESLEYINAIKRDVEWLGFKwADELRYA 101
Cdd:PLN03233 5 EGAIAGQIVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIK-PDSVSFT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 102 SDYFDQLYAFAEELIEKGKAYVCALTADEMAEYRGSLKEpgrnSPYRDRPAEESLQLFRDMRDGKFQNGELVLRAKIDMA 181
Cdd:PLN03233 84 SDYFEPIRCYAIILIEEGLAYMDDTPQEEMKKERADRAE----SKHRNQSPEEALEMFKEMCSGKEEGGAWCLRAKIDMQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 182 SPNINLRDPILYRIRYADHHQTGDKWCIYPMYDFTHPISDALEGVTHSLCTLEFEDHRPLYDWVLDNITIPcHPRQIEFA 261
Cdd:PLN03233 160 SDNGTLRDPVLFRQNTTPHHRSGTAYKAYPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQKALGLR-RPRIHAFA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 262 RLNLNYTVTSKRKLKRLVDDNVVDGWDDPRMPTISGMRRRGFTPESIRTFCDMIGVNKAGGTVDVGMLEHAIREDLNARA 341
Cdd:PLN03233 239 RMNFMNTVLSKRKLTWFVDNGHVTGWDDARFPTIRGISRRGIDIDALKMFMCSQGASRRVVNLDWAKFWAENKKEIDKRA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 342 PRAMCVMRP--IKVTLTNYPEGQ----TETltlPVHPQNPDMGEREVTWSQVLYIDREDFalepprKWKRLAPDqAVRLR 415
Cdd:PLN03233 319 KRFMAIDKAdhTALTVTNADEEAdfafSET---DCHPKDPGFGKRAMRICDEVLLEKADT------EDIQLGED-IVLLR 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 416 GGYVMTCKevicddsgdivelkcefdpktLGVNPEG-YKPNG-------VIHWVS-AADSVEVCINQYDRLFNHEapDSD 486
Cdd:PLN03233 389 WGVIEISK---------------------IDGDLEGhFIPDGdfkaakkKISWIAdVSDNIPVVLSEFDNLIIKE--KLE 445
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1591635903 487 KDGDMMDHINSDSLVVLE--GARVEKSLASPGTdlpYQFEREGYFLYDQKLaANAGKPV 543
Cdd:PLN03233 446 EDDKFEDFINPDTLAETDviGDAGLKTLKEHDI---IQLERRGFYRVDRPY-MGEEKPL 500
|
|
| tRNA-synt_1c_C |
pfam03950 |
tRNA synthetases class I (E and Q), anti-codon binding domain; Other tRNA synthetase ... |
341-529 |
1.06e-68 |
|
tRNA synthetases class I (E and Q), anti-codon binding domain; Other tRNA synthetase sub-families are too dissimilar to be included. This family includes only glutamyl and glutaminyl tRNA synthetases. In some organizms, a single glutamyl-tRNA synthetase aminoacylates both tRNA(Glu) and tRNA(Gln).
Pssm-ID: 427609 [Multi-domain] Cd Length: 175 Bit Score: 219.06 E-value: 1.06e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 341 APRAMCVMRPIKVTLTNYPEGQTETLTLPVHPQNPDMGEREVTWSQVLYIDREDFalepprkwKRLAPDQAVRLRGGYVM 420
Cdd:pfam03950 1 APRYMAVLDPVKVVIENYPEGQEETAEVPNHPKNPELGTRKVPFSREIYIEREDF--------KRLAPGEEVRLMDAYNI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 421 TCKEVICDDSGDIVELKCEFDPKTLGVNpegYKPNG-VIHWVSAADSVEVCINQYDRLFNHEAPDSDKdgdmmdhINSDS 499
Cdd:pfam03950 73 KVTEVVKDEDGNVTELHCTYDGDDLGGA---RKVKGkIIHWVSASDAVPAEVRLYDRLFKDEDDADFL-------LNPDS 142
|
170 180 190
....*....|....*....|....*....|
gi 1591635903 500 LVVLEGARVEKSLASPGTDLPYQFEREGYF 529
Cdd:pfam03950 143 LKVLTEGLAEPALANLKPGDIVQFERIGYF 172
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
28-338 |
1.09e-66 |
|
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA synthetase(GluRS)/Glutaminyl-tRNA synthetase (GlnRS) cataytic core domain. These enzymes attach Glu or Gln, respectively, to the appropriate tRNA. Like other class I tRNA synthetases, they aminoacylate the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. These enzymes function as monomers. Archaea, cellular organelles, and some bacteria lack GlnRS. In these cases, the "non-discriminating" form of GluRS aminoacylates both tRNA(Glu) and tRNA(Gln) with Glu, which is converted to Gln when appropriate by a transamidation enzyme. The discriminating form of GluRS differs from GlnRS and the non-discriminating form of GluRS in their C-terminal anti-codon binding domains.
Pssm-ID: 185672 [Multi-domain] Cd Length: 230 Bit Score: 216.18 E-value: 1.09e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 28 KVVTRFPPEPNGYLHVGHAKSICLNFGIAETFEGECNLRFDDTNPEKESLEYINAIKRDVEWLGFKWADELRYASDYFDQ 107
Cdd:cd00418 1 TVVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDWDEGPYRQSDRFDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 108 LYAFAEELIEKGkayvcaltademaeyrgslkepgrnspyrdrpaeeslqlfrdmrdgkfqngelvlrakidmaspninl 187
Cdd:cd00418 81 YRAYAEELIKKG-------------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 188 rdpilyriryadhhqtgdkwcIYPMYDFTHPISDALEGVTHSLCTLEFEDHRPLYDWVLDNITIPcHPRQIEFARLNLNY 267
Cdd:cd00418 93 ---------------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWE-PPRFYHFPRLLLED 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 268 -TVTSKRKLKrlvddnvvdgwddprmPTISGMRRRGFTPESIRTFCDMIG-----------------------VNKAGGT 323
Cdd:cd00418 151 gTKLSKRKLN----------------TTLRALRRRGYLPEALRNYLALIGwskpdghelftleemiaafsverVNSADAT 214
|
330
....*....|....*
gi 1591635903 324 VDVGMLEHAIREDLN 338
Cdd:cd00418 215 FDWAKLEWLNREYIR 229
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
28-343 |
5.02e-48 |
|
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating Glutamyl-tRNA synthetase (GluRS) cataytic core domain. These enzymes attach Glu to the appropriate tRNA. Like other class I tRNA synthetases, they aminoacylate the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. These enzymes function as monomers. Archaea and most bacteria lack GlnRS. In these organisms, the "non-discriminating" form of GluRS aminoacylates both tRNA(Glu) and tRNA(Gln) with Glu, which is converted to Gln when appropriate by a transamidation enzyme.
Pssm-ID: 185682 [Multi-domain] Cd Length: 240 Bit Score: 167.14 E-value: 5.02e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 28 KVVTRFPPEPNGYLHVGHAKSICLNFGIAETFEGECNLRFDDTNPE--KESLEYINAIKRDVEWLGFKWaDELRYASDYF 105
Cdd:cd09287 1 KVVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPRtkRPDPEAYDMIPEDLEWLGVKW-DEVVIASDRI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 106 DQLYAFAEELIEKGKAYVcaltademaeyrgslkepgrnspyrdrpaeeslqlfrdmrdgkfqngelvlrakidmaspni 185
Cdd:cd09287 80 ELYYEYARKLIEMGGAYV-------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 186 nlrdpilyriryadHHQTGDKWCIYPMYDFTHPISDALEGVTHSLCTLEFED----HRPLYD---WVldnitipcHPRQI 258
Cdd:cd09287 98 --------------HPRTGSKYRVWPTLNFAVAVDDHLLGVTHVLRGKDHIDntekQRYIYEyfgWE--------YPETI 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 259 EFARLNLNYTVTSKRKLKRLVDDNVVDGWDDPRMPTISGMRRRGFTPESIRTFCDMIGVNKAGGTVDVGMLEHAIREDLN 338
Cdd:cd09287 156 HWGRLKIEGGKLSTSKIRKGIESGEYEGWDDPRLPTLRALRRRGIRPEAIRDFIIEVGVKQTDATISWENLYAINRKLID 235
|
....*
gi 1591635903 339 ARAPR 343
Cdd:cd09287 236 PRANR 240
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
25-205 |
1.78e-15 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 77.20 E-value: 1.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 25 HTGKVVTRFPPEPNGYLHVGHAKSICLNFGIAETFEGECNLRFDDTNPEKESLEYINAIKRDVEWLGFKWADELRYASDY 104
Cdd:PRK05710 2 TMTPYIGRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWDGPVLYQSQR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 105 FDqLYAFA-EELIEKGKAYVCALTADEMAEYRGSLKEPGRNSPYRDRPAEESLQLFRDMRdgkfqngelvlrakIDMASP 183
Cdd:PRK05710 82 HD-AYRAAlDRLRAQGLVYPCFCSRKEIAAAAPAPPDGGGIYPGTCRDLLHGPRNPPAWR--------------LRVPDA 146
|
170 180
....*....|....*....|..
gi 1591635903 184 NINLRDPILYRIRYADHHQTGD 205
Cdd:PRK05710 147 VIAFDDRLQGRQHQDLALAVGD 168
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
28-119 |
5.88e-15 |
|
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA synthetase (GluRS) catalytic core domain . The discriminating form of GluRS is only found in bacteria and cellular organelles. GluRS is a monomer that attaches Glu to the appropriate tRNA. Like other class I tRNA synthetases, GluRS aminoacylates the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173905 [Multi-domain] Cd Length: 239 Bit Score: 74.55 E-value: 5.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 28 KVVTRFPPEPNGYLHVGHAKSICLNFGIAETFEGECNLRFDDTNPEKESLEYINAIKRDVEWLGFKWaDELR-------- 99
Cdd:cd00808 1 KVRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDW-DEGPdvggpygp 79
|
90 100
....*....|....*....|.
gi 1591635903 100 -YASDYFDQLYAFAEELIEKG 119
Cdd:cd00808 80 yRQSERLEIYRKYAEKLLEKG 100
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
19-240 |
3.24e-14 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 75.16 E-value: 3.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 19 AVAKGEHTGKVVTRFPPEPNGYLHVGHAKSICLNFGIAETFEGECNLRFDDTNPEKESLEYINAIKRDVEWLGFKWADEL 98
Cdd:PLN02627 36 AAAGESKGGPVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDEGP 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 99 RYASDY--FDQ-----LY-AFAEELIEKGKAYVCALTADEMAEYRGSLKEPGRNSPYRDRPAEESLQ-LFRDMRDG---- 165
Cdd:PLN02627 116 DVGGEYgpYRQsernaIYkQYAEKLLESGHVYPCFCTDEELEAMKEEAELKKLPPRYTGKWATASDEeVQAELAKGtpyt 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 166 -KF---QNGELVLRAKI-DMASPNIN-LRDPILYRiryadhhQTGdkwciYPMYDFTHPISDALEGVTHslcTLEFEDHR 239
Cdd:PLN02627 196 yRFrvpKEGSVKIDDLIrGEVSWNTDtLGDFVLLR-------SNG-----QPVYNFCVAVDDATMGITH---VIRAEEHL 260
|
.
gi 1591635903 240 P 240
Cdd:PLN02627 261 P 261
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
30-274 |
5.50e-12 |
|
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA synthetase (aaRS) catalytic core domain. These enzymes are mostly monomers which aminoacylate the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173901 [Multi-domain] Cd Length: 143 Bit Score: 63.65 E-value: 5.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 30 VTRFPPEPNGYLHVGHAKSICLNFGIA-----ETFEGECNLRFDDTNPEKESLeyinaikRDVEWLGFKwadelryasdy 104
Cdd:cd00802 1 TTFSGITPNGYLHIGHLRTIVTFDFLAqayrkLGYKVRCIALIDDAGGLIGDP-------ANKKGENAK----------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 105 fdqlyAFAEELIEKGKAYVcaltademaeyrgslkepgrnspyrdrpaeeslqlfrdmrdgkfqngelvlrakidmaspn 184
Cdd:cd00802 63 -----AFVERWIERIKEDV------------------------------------------------------------- 76
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 185 inlrdpilyriryadhhqtgdkwciypMYDFTHPISDALEGVTH---SLCTLEFEDHRPLYDWVLDNITIPCHPRQIEFA 261
Cdd:cd00802 77 ---------------------------EYMFLQAADFLLLYETEcdiHLGGSDQLGHIELGLELLKKAGGPARPFGLTFG 129
|
250
....*....|....
gi 1591635903 262 RLNLNY-TVTSKRK 274
Cdd:cd00802 130 RVMGADgTKMSKSK 143
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
30-106 |
6.51e-10 |
|
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily includes the class I amino-acyl tRNA synthetases, pantothenate synthetase (PanC), ATP sulfurylase, and the cytidylyltransferases, all of which have a conserved dinucleotide-binding domain.
Pssm-ID: 173912 [Multi-domain] Cd Length: 105 Bit Score: 56.39 E-value: 6.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591635903 30 VTRFPPEPnGYLHVGHAKSICLNFGIAetfeGECNLRFDDTNPEK------ESLEYINAIKRDVEWLGFKWADELRYASD 103
Cdd:cd02156 1 KARFPGEP-GYLHIGHAKLICRAKGIA----DQCVVRIDDNPPVKvwqdphELEERKESIEEDISVCGEDFQQNRELYRW 75
|
...
gi 1591635903 104 YFD 106
Cdd:cd02156 76 VKD 78
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
228-274 |
9.79e-10 |
|
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily includes the class I amino-acyl tRNA synthetases, pantothenate synthetase (PanC), ATP sulfurylase, and the cytidylyltransferases, all of which have a conserved dinucleotide-binding domain.
Pssm-ID: 173912 [Multi-domain] Cd Length: 105 Bit Score: 56.01 E-value: 9.79e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1591635903 228 HSLCTLEFEDHRPLYDWVLDNITIPCHPRQIEFARLNLNYTVTSKRK 274
Cdd:cd02156 59 ISVCGEDFQQNRELYRWVKDNITLPVDPEQVELPRLNLETTVMSKRK 105
|
|
| |
