|
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: 1109.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 1 MSAESKKAHNFIQSLIEDAIASGEHTgKVVTRFPPEPNGYLHIGHAKSICLNFGIAETFSGDCNLRFDDTNPEKENQEYI 80
Cdd:PRK05347 3 MSEAEARPSNFIRQIIDEDLASGKHT-RVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 81 DAIKQDVEWLGYEWAGDVLYASDYFDALYEFAEELITRDKAYVCALTADEMAEYRGSLKEPGRNSPYRDRPVEESLQMFR 160
Cdd:PRK05347 82 DSIKEDVRWLGFDWSGELRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREYRGTLTEPGKNSPYRDRSVEENLDLFE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 161 DMRDGKYQNGELVLRAKIDMSSPNINMRDPILYRIRYAEHHQTGNKWCIYPMYDFTHPISDALEGITHSLCTLEFEDHRP 240
Cdd:PRK05347 162 RMRAGEFPEGSAVLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHRP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 241 LYDWVLDNISGPCHPRQIEFARLNLNYTITSKRKLKRLVDENVVDGWNDPRMPTISGMRRRGYTPESIRTFCDMIGVNKA 320
Cdd:PRK05347 242 LYDWVLDNLPIPPHPRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 321 GGTVDVGMLEHAIREDLNIRAPRAMCVMRPLKVTLTNYPADQSETLTLPVHPQNPDMGEREVPWTQTLYIDREDFEMEPP 400
Cdd:PRK05347 322 DSVIDMSMLESCIREDLNENAPRAMAVLDPLKLVITNYPEGQVEELEAPNHPEDPEMGTREVPFSRELYIEREDFMEEPP 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 401 RKWKRLAPDQAVRLRGGYVMTCREVIRDDSGQIVELKCEYDPNTLGVNP-EGYKPNGVIHWVSASDSVEADINLYDRLFN 479
Cdd:PRK05347 402 KKYFRLVPGKEVRLRNAYVIKCEEVVKDADGNITEIHCTYDPDTLSGNPaDGRKVKGTIHWVSAAHAVPAEVRLYDRLFT 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 914748874 480 HESPdsDKEGDLMDHLNPESLVVlKGARVEKSLVAPRMDLPYQFEREGYFFCDQAHTeaAGRPVFNRTVTLRDSWGK 556
Cdd:PRK05347 482 VPNP--AAGKDFLDFLNPDSLVI-KQGFVEPSLADAKPEDRFQFEREGYFCADKDST--PGKLVFNRTVGLRDSWAK 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: 715.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 29 VVTRFPPEPNGYLHIGHAKSICLNFGIAETFSGDCNLRFDDTNPEKENQEYIDAIKQDVEWLGYEWAGDVLYASDYFDAL 108
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEGKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 109 YEFAEELITRDKAYVCALTADEMAEYRGSLKEPGRNSPYRDRPVEESLQMFRDMRDGKYQNGELVLRAKIDMSSPNINMR 188
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIREYRGTLTDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 189 DPILYRIRYAEHHQTGNKWCIYPMYDFTHPISDALEGITHSLCTLEFEDHRPLYDWVLDNISGPCHPRQIEFARLNLNYT 268
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFPRPAQYEFSRLNLEGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 269 ITSKRKLKRLVDENVVDGWNDPRMPTISGMRRRGYTPESIRTFCDMIGVNKAGGTVDVGMLEHAIREDLNIRAPRAMCVM 348
Cdd:TIGR00440 241 VLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAVI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 349 RPLKVTLTNYpADQSETLTLPVHPQNPDMGEREVPWTQTLYIDREDFEMEPPRKWKRLAPDQAVRLRGGYVMTCREVIRD 428
Cdd:TIGR00440 321 DPVEVVIENL-SDEYELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAERVEKD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 429 DSGQIVELKCEYDPNTLGVNP-EGYKPNGVIHWVSASDSVEADINLYDRLFNHESPDSdkEGDLMDHLNPESLVVLKGAr 507
Cdd:TIGR00440 400 AAGKITTIFCTYDNKTLGKEPaDGRKVKGVIHWVSASSKYPTETRLYDRLFKVPNPGA--PDDFLSVINPESLVIKQGF- 476
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 914748874 508 VEKSLVAPRMDLPYQFEREGYFFCDQAHTEAAgRPVFNRTVTLRDSW 554
Cdd:TIGR00440 477 MEHSLGDAVANKRFQFEREGYFCLDSKESTTE-KVVFNRTVSLKDAT 522
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
28-343 |
2.28e-146 |
|
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: 420.89 E-value: 2.28e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 28 KVVTRFPPEPNGYLHIGHAKSICLNFGIAETFSGDCNLRFDDTNPEKENQEYIDAIKQDVEWLGYEWaGDVLYASDYFDA 107
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKP-YKVTYASDYFDQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 108 LYEFAEELITRDKAYVcaltademaeyrgslkepgrnspyrdrpveeslqmfrdmrdgkyqngelvlrakidmsspninm 187
Cdd:cd00807 80 LYEYAEQLIKKGKAYV---------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 188 rdpilyriryaeHHQTGNKWCIYPMYDFTHPISDALEGITHSLCTLEFEDHRPLYDWVLDNISGPChPRQIEFARLNLNY 267
Cdd:cd00807 96 ------------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYR-PHQWEFSRLNLTY 162
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 914748874 268 TITSKRKLKRLVDENVVDGWNDPRMPTISGMRRRGYTPESIRTFCDMIGVNKAGGTVDVGMLEHAIREDLNIRAPR 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 |
2.38e-140 |
|
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: 408.63 E-value: 2.38e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 28 KVVTRFPPEPNGYLHIGHAKSICLNFGIAETFSGDCNLRFDDTNPEKENQEYIDAIKQDVEWLGYEWAGDVLYASDYFDA 107
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 108 LYEFAEELITRDKAYVCALTADEMAEYRGSLkePGRNSPYRDRPVEESLQMF-RDMRDGKYQNGELVLRAKIDMSSPnIN 186
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEREEQ--EALGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMESP-YV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 187 MRDPILYRIRYAE---HHQTGNKWCIYPMYDFTHPISDALEGITHSLCTLEFEDHRPLYDWVLDNISGPCHPRQIEFARL 263
Cdd:pfam00749 158 FRDPVRGRIKFTPqeiHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHEYLRL 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 914748874 264 NLNYTITSKRKLKRLVDENVVDGWNDPRMPTISGMRRRGYTPESIRTFCDMIGVNKAggtVDVGMLEHAI----REDLN 338
Cdd:pfam00749 238 NLDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKS---FDVNRLSKSLeafdRKKLD 313
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
25-529 |
1.32e-133 |
|
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: 396.86 E-value: 1.32e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 25 HTGKVVTRFPPEPNGYLHIGHAKSICLNFGIAETFSGDCNLRFDDTNPEKENQEYIDAIKQDVEWLGYEWAGDVLYASDY 104
Cdd:COG0008 1 HGMKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGPYYQSDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 105 FDALYEFAEELITRDKAYVCALTADEMAEYRGSLKEPGRNSPY----RDRPVEESLQMFrdmrdgkyQNGEL-VLRAKI- 178
Cdd:COG0008 81 FDIYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYdgrcRDLSPEELERML--------AAGEPpVLRFKIp 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 179 -------DMSS-----PNINMRDPILYRiryaehhQTGnkwciYPMYDFTHPISDALEGITHSLCTLEFEDHRPLYDWVL 246
Cdd:COG0008 153 eegvvfdDLVRgeitfPNPNLRDPVLYR-------ADG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLY 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 247 DNISGPcHPrqiEFARLNLNY----TITSKRKlkrlvdeNVVdgwndprmpTISGMRRRGYTPESIRTFCDMIGVNKAGG 322
Cdd:COG0008 221 EALGWE-PP---EFAHLPLILgpdgTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALLGWSKSDD 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 323 TV--DVGMLEHAIreDLNiRAPRAMCVMRPLKVTLTNYPADQS---ETLTLPVHPQNPDMGERE---------------- 381
Cdd:COG0008 281 QEifSLEELIEAF--DLD-RVSRSPAVFDPVKLVWLNGPYIRAlddEELAELLAPELPEAGIREdlerlvplvreraktl 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 382 ---VPWTQTLYIDREDfemEPPRKwKRLAPDQAvrlrggyvmtcREVIRDDSGQIVELKcEYDPNTLgvnpegykpNGVI 458
Cdd:COG0008 358 selAELARFFFIERED---EKAAK-KRLAPEEV-----------RKVLKAALEVLEAVE-TWDPETV---------KGTI 412
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 914748874 459 HWVSAsdsvEADInlydrlfnhespdsdKEGDLMDHLNpeslVVLKGARVEKSLVAPrMDLPYQ---FEREGYF 529
Cdd:COG0008 413 HWVSA----EAGV---------------KDGLLFMPLR----VALTGRTVEPSLFDV-LELLGKervFERLGYA 462
|
|
| |
|
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: 1109.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 1 MSAESKKAHNFIQSLIEDAIASGEHTgKVVTRFPPEPNGYLHIGHAKSICLNFGIAETFSGDCNLRFDDTNPEKENQEYI 80
Cdd:PRK05347 3 MSEAEARPSNFIRQIIDEDLASGKHT-RVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 81 DAIKQDVEWLGYEWAGDVLYASDYFDALYEFAEELITRDKAYVCALTADEMAEYRGSLKEPGRNSPYRDRPVEESLQMFR 160
Cdd:PRK05347 82 DSIKEDVRWLGFDWSGELRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREYRGTLTEPGKNSPYRDRSVEENLDLFE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 161 DMRDGKYQNGELVLRAKIDMSSPNINMRDPILYRIRYAEHHQTGNKWCIYPMYDFTHPISDALEGITHSLCTLEFEDHRP 240
Cdd:PRK05347 162 RMRAGEFPEGSAVLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHRP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 241 LYDWVLDNISGPCHPRQIEFARLNLNYTITSKRKLKRLVDENVVDGWNDPRMPTISGMRRRGYTPESIRTFCDMIGVNKA 320
Cdd:PRK05347 242 LYDWVLDNLPIPPHPRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 321 GGTVDVGMLEHAIREDLNIRAPRAMCVMRPLKVTLTNYPADQSETLTLPVHPQNPDMGEREVPWTQTLYIDREDFEMEPP 400
Cdd:PRK05347 322 DSVIDMSMLESCIREDLNENAPRAMAVLDPLKLVITNYPEGQVEELEAPNHPEDPEMGTREVPFSRELYIEREDFMEEPP 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 401 RKWKRLAPDQAVRLRGGYVMTCREVIRDDSGQIVELKCEYDPNTLGVNP-EGYKPNGVIHWVSASDSVEADINLYDRLFN 479
Cdd:PRK05347 402 KKYFRLVPGKEVRLRNAYVIKCEEVVKDADGNITEIHCTYDPDTLSGNPaDGRKVKGTIHWVSAAHAVPAEVRLYDRLFT 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 914748874 480 HESPdsDKEGDLMDHLNPESLVVlKGARVEKSLVAPRMDLPYQFEREGYFFCDQAHTeaAGRPVFNRTVTLRDSWGK 556
Cdd:PRK05347 482 VPNP--AAGKDFLDFLNPDSLVI-KQGFVEPSLADAKPEDRFQFEREGYFCADKDST--PGKLVFNRTVGLRDSWAK 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: 835.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 8 AHNFIQSLIEDAIASGEHtGKVVTRFPPEPNGYLHIGHAKSICLNFGIAETFSGDCNLRFDDTNPEKENQEYIDAIKQDV 87
Cdd:PRK14703 12 SPNFITEIIEEDLEAGRY-PRVVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETEDTEYVEAIKDDV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 88 EWLGYEWAGDVLYASDYFDALYEFAEELITRDKAYVCALTADEMAEYRGSLKEPGRNSPYRDRPVEESLQMFRDMRDGKY 167
Cdd:PRK14703 91 RWLGFDWGEHLYYASDYFERMYAYAEQLIKMGLAYVDSVSEEEIRELRGTVTEPGTPSPYRDRSVEENLDLFRRMRAGEF 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 168 QNGELVLRAKIDMSSPNINMRDPILYRIRYAEHHQTGNKWCIYPMYDFTHPISDALEGITHSLCTLEFEDHRPLYDWVLD 247
Cdd:PRK14703 171 PDGAHVLRAKIDMSSPNMKLRDPLLYRIRHAHHYRTGDEWCIYPMYDFAHPLEDAIEGVTHSICTLEFENNRAIYDWVLD 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 248 NISG-PCHPRQIEFARLNLNYTITSKRKLKRLVDENVVDGWNDPRMPTISGMRRRGYTPESIRTFCDMIGVNKAGGTVDV 326
Cdd:PRK14703 251 HLGPwPPRPRQYEFARLALGYTVMSKRKLRELVEEGYVSGWDDPRMPTIAGQRRRGVTPEAIRDFADQIGVAKTNSTVDI 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 327 GMLEHAIREDLNIRAPRAMCVMRPLKVTLTNYPADQSETLTLPVHPQN-PDMGEREVPWTQTLYIDREDFEMEPPRKWKR 405
Cdd:PRK14703 331 GVLEFAIRDDLNRRAPRVMAVLDPLKVVIENLPAGKVEELDLPYWPHDvPKEGSRKVPFTRELYIERDDFSEDPPKGFKR 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 406 LAPDQAVRLRGGYVMTCREVIRDDSGQIVELKCEYDPNTLGVNPEGYKPNGVIHWVSASDSVEADINLYDRLFNHESPDS 485
Cdd:PRK14703 411 LTPGREVRLRGAYIIRCDEVVRDADGAVTELRCTYDPESAKGEDTGRKAAGVIHWVSAKHALPAEVRLYDRLFKVPQPEA 490
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 914748874 486 dKEGDLMDHLNPESLVVLKGaRVEKSLVAPRMDLPYQFEREGYFFCDQAHTEaAGRPVFNRTVTLRDSWGKGG 558
Cdd:PRK14703 491 -ADEDFLEFLNPDSLRVAQG-RVEPAVRDDPADTRYQFERQGYFWADPVDSR-PDALVFNRIITLKDTWGARA 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: 715.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 29 VVTRFPPEPNGYLHIGHAKSICLNFGIAETFSGDCNLRFDDTNPEKENQEYIDAIKQDVEWLGYEWAGDVLYASDYFDAL 108
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEGKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 109 YEFAEELITRDKAYVCALTADEMAEYRGSLKEPGRNSPYRDRPVEESLQMFRDMRDGKYQNGELVLRAKIDMSSPNINMR 188
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIREYRGTLTDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 189 DPILYRIRYAEHHQTGNKWCIYPMYDFTHPISDALEGITHSLCTLEFEDHRPLYDWVLDNISGPCHPRQIEFARLNLNYT 268
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFPRPAQYEFSRLNLEGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 269 ITSKRKLKRLVDENVVDGWNDPRMPTISGMRRRGYTPESIRTFCDMIGVNKAGGTVDVGMLEHAIREDLNIRAPRAMCVM 348
Cdd:TIGR00440 241 VLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAVI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 349 RPLKVTLTNYpADQSETLTLPVHPQNPDMGEREVPWTQTLYIDREDFEMEPPRKWKRLAPDQAVRLRGGYVMTCREVIRD 428
Cdd:TIGR00440 321 DPVEVVIENL-SDEYELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAERVEKD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 429 DSGQIVELKCEYDPNTLGVNP-EGYKPNGVIHWVSASDSVEADINLYDRLFNHESPDSdkEGDLMDHLNPESLVVLKGAr 507
Cdd:TIGR00440 400 AAGKITTIFCTYDNKTLGKEPaDGRKVKGVIHWVSASSKYPTETRLYDRLFKVPNPGA--PDDFLSVINPESLVIKQGF- 476
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 914748874 508 VEKSLVAPRMDLPYQFEREGYFFCDQAHTEAAgRPVFNRTVTLRDSW 554
Cdd:TIGR00440 477 MEHSLGDAVANKRFQFEREGYFCLDSKESTTE-KVVFNRTVSLKDAT 522
|
|
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
27-559 |
0e+00 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 577.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 27 GKVVTRFPPEPNGYLHIGHAKSICLNFGIAETFSGDCNLRFDDTNPEKENQEYIDAIKQDVEWLGYEwAGDVLYASDYFD 106
Cdd:PLN02859 263 GKVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIEEIVEWMGWE-PFKITYTSDYFQ 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 107 ALYEFAEELITRDKAYVCALTADEMAEYRgslkEPGRNSPYRDRPVEESLQMFRDMRDGKYQNGELVLRAKIDMSSPNIN 186
Cdd:PLN02859 342 ELYELAVELIRRGHAYVDHQTPEEIKEYR----EKKMNSPWRDRPIEESLKLFEDMRRGLIEEGKATLRMKQDMQNDNFN 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 187 MRDPILYRIRYAEHHQTGNKWCIYPMYDFTHPISDALEGITHSLCTLEFEDHRPLYDWVLDNIsGPCHPRQIEFARLNLN 266
Cdd:PLN02859 418 MYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLDSL-GLYQPYVWEYSRLNVT 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 267 YTITSKRKLKRLVDENVVDGWNDPRMPTISGMRRRGYTPESIRTFCDMIGVNKA-GGTVDVGMLEHAIREDLNIRAPRAM 345
Cdd:PLN02859 497 NTVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITRSdNSLIRMDRLEHHIREELNKTAPRTM 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 346 CVMRPLKVTLTNYPADQSETL---TLPVHPQNPDMGEREVPWTQTLYIDREDFEMEPPRKWKRLAPDQAVRLRGGYVMTC 422
Cdd:PLN02859 577 VVLHPLKVVITNLESGEVIELdakRWPDAQNDDPSAFYKVPFSRVVYIERSDFRLKDSKDYYGLAPGKSVLLRYAFPIKC 656
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 423 REVIR-DDSGQIVELKCEYDPNtlgvnpEGYKPNGVIHWVSAS----DSVEADINLYDRLFNHESPDSDKegDLMDHLNP 497
Cdd:PLN02859 657 TDVVLaDDNETVVEIRAEYDPE------KKTKPKGVLHWVAEPspgvEPLKVEVRLFDKLFLSENPAELE--DWLEDLNP 728
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 914748874 498 ESLVVLKGARVEKSLVAPRMDLPYQFEREGYFFCDQAHTeaAGRPVFNRTVTLRDSWGKGGK 559
Cdd:PLN02859 729 QSKEVISGAYAVPSLKDAKVGDRFQFERLGYFAVDKDST--PEKLVFNRTVTLKDSYGKGGK 788
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
27-557 |
6.87e-157 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 460.60 E-value: 6.87e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 27 GKVVTRFPPEPNGYLHIGHAKSICLNFGIAETFSGDCNLRFDDTNPEKENQEYIDAIKQDVEWLGYE--WagdVLYASDY 104
Cdd:PTZ00437 50 GKPYFRFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTNPETEEQVYIDAIMEMVKWMGWKpdW---VTFSSDY 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 105 FDALYEFAEELITRDKAYVCALTADEMAEYRGSLKEpgrnSPYRDRPVEESLQMFRDMRDGKYQNGELVLRAKIDMSSPN 184
Cdd:PTZ00437 127 FDQLHEFAVQLIKDGKAYVDHSTPDELKQQREQRED----SPWRNRSVEENLLLFEHMRQGRYAEGEATLRVKADMKSDN 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 185 INMRDPILYRIRYAEHHQTGNKWCIYPMYDFTHPISDALEGITHSLCTLEFEDHRPLYDWVLDNISgPCHPRQIEFARLN 264
Cdd:PTZ00437 203 PNMRDFIAYRVKYVEHPHAKDKWCIYPSYDFTHCLIDSLEDIDYSLCTLEFETRRESYFWLLEELN-LWRPHVWEFSRLN 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 265 LNYTITSKRKLKRLVDENVVDGWNDPRMPTISGMRRRGYTPESIRTFCDMIGVNKAGGTVDVGMLEHAIREDLNIRAPRA 344
Cdd:PTZ00437 282 VTGSLLSKRKINVLVRKGIVRGFDDPRLLTLAGMRRRGYTPAAINRFCELVGITRSMNVIQISMLENTLREDLDERCERR 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 345 MCVMRPLKVTLTNYpaDQSETLTLPVHPQNPDMGEREVPWTQTLYIDREDFEMEP-PRKWKRLAPD-QAVRLRGGYVMTC 422
Cdd:PTZ00437 362 LMVIDPIKVVVDNW--KGEREFECPNHPRKPELGSRKVMFTDTFYVDRSDFRTEDnNSKFYGLAPGpRVVGLKYSGNVVC 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 423 REVIRDDSGQ--IVELKCEYDPNTlgvnpegyKPNGVIHWVSASDSVEADINLYDRLFNHESPDSDKegDLMDHLNPESL 500
Cdd:PTZ00437 440 KGFEVDAAGQpsVIHVDIDFERKD--------KPKTNISWVSATACTPVEVRLYNALLKDDRAAIDP--EFLKFIDEDSE 509
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 914748874 501 VVLKGaRVEKSLVAPRMDLPYQFEREGYFFCDQAHTeaAGRPVFNRTVTLRDSWGKG 557
Cdd:PTZ00437 510 VVSHG-YAEKGIENAKHFESVQAERFGYFVVDPDTR--PDHLVMNRVLGLREDKEKA 563
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
28-343 |
2.28e-146 |
|
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: 420.89 E-value: 2.28e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 28 KVVTRFPPEPNGYLHIGHAKSICLNFGIAETFSGDCNLRFDDTNPEKENQEYIDAIKQDVEWLGYEWaGDVLYASDYFDA 107
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKP-YKVTYASDYFDQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 108 LYEFAEELITRDKAYVcaltademaeyrgslkepgrnspyrdrpveeslqmfrdmrdgkyqngelvlrakidmsspninm 187
Cdd:cd00807 80 LYEYAEQLIKKGKAYV---------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 188 rdpilyriryaeHHQTGNKWCIYPMYDFTHPISDALEGITHSLCTLEFEDHRPLYDWVLDNISGPChPRQIEFARLNLNY 267
Cdd:cd00807 96 ------------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYR-PHQWEFSRLNLTY 162
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 914748874 268 TITSKRKLKRLVDENVVDGWNDPRMPTISGMRRRGYTPESIRTFCDMIGVNKAGGTVDVGMLEHAIREDLNIRAPR 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 |
2.38e-140 |
|
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: 408.63 E-value: 2.38e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 28 KVVTRFPPEPNGYLHIGHAKSICLNFGIAETFSGDCNLRFDDTNPEKENQEYIDAIKQDVEWLGYEWAGDVLYASDYFDA 107
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 108 LYEFAEELITRDKAYVCALTADEMAEYRGSLkePGRNSPYRDRPVEESLQMF-RDMRDGKYQNGELVLRAKIDMSSPnIN 186
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEREEQ--EALGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMESP-YV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 187 MRDPILYRIRYAE---HHQTGNKWCIYPMYDFTHPISDALEGITHSLCTLEFEDHRPLYDWVLDNISGPCHPRQIEFARL 263
Cdd:pfam00749 158 FRDPVRGRIKFTPqeiHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHEYLRL 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 914748874 264 NLNYTITSKRKLKRLVDENVVDGWNDPRMPTISGMRRRGYTPESIRTFCDMIGVNKAggtVDVGMLEHAI----REDLN 338
Cdd:pfam00749 238 NLDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKS---FDVNRLSKSLeafdRKKLD 313
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
25-529 |
1.32e-133 |
|
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: 396.86 E-value: 1.32e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 25 HTGKVVTRFPPEPNGYLHIGHAKSICLNFGIAETFSGDCNLRFDDTNPEKENQEYIDAIKQDVEWLGYEWAGDVLYASDY 104
Cdd:COG0008 1 HGMKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGPYYQSDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 105 FDALYEFAEELITRDKAYVCALTADEMAEYRGSLKEPGRNSPY----RDRPVEESLQMFrdmrdgkyQNGEL-VLRAKI- 178
Cdd:COG0008 81 FDIYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYdgrcRDLSPEELERML--------AAGEPpVLRFKIp 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 179 -------DMSS-----PNINMRDPILYRiryaehhQTGnkwciYPMYDFTHPISDALEGITHSLCTLEFEDHRPLYDWVL 246
Cdd:COG0008 153 eegvvfdDLVRgeitfPNPNLRDPVLYR-------ADG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLY 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 247 DNISGPcHPrqiEFARLNLNY----TITSKRKlkrlvdeNVVdgwndprmpTISGMRRRGYTPESIRTFCDMIGVNKAGG 322
Cdd:COG0008 221 EALGWE-PP---EFAHLPLILgpdgTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALLGWSKSDD 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 323 TV--DVGMLEHAIreDLNiRAPRAMCVMRPLKVTLTNYPADQS---ETLTLPVHPQNPDMGERE---------------- 381
Cdd:COG0008 281 QEifSLEELIEAF--DLD-RVSRSPAVFDPVKLVWLNGPYIRAlddEELAELLAPELPEAGIREdlerlvplvreraktl 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 382 ---VPWTQTLYIDREDfemEPPRKwKRLAPDQAvrlrggyvmtcREVIRDDSGQIVELKcEYDPNTLgvnpegykpNGVI 458
Cdd:COG0008 358 selAELARFFFIERED---EKAAK-KRLAPEEV-----------RKVLKAALEVLEAVE-TWDPETV---------KGTI 412
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 914748874 459 HWVSAsdsvEADInlydrlfnhespdsdKEGDLMDHLNpeslVVLKGARVEKSLVAPrMDLPYQ---FEREGYF 529
Cdd:COG0008 413 HWVSA----EAGV---------------KDGLLFMPLR----VALTGRTVEPSLFDV-LELLGKervFERLGYA 462
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
23-543 |
6.04e-108 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 339.01 E-value: 6.04e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 23 GEHTGKVVTRFPPEPNGYLHIGHAKSICLNFGIAETFSGDCNLRFDDTNPEKENQEYIDAIKQDVEWLGYEwaGDVL-YA 101
Cdd:PLN02907 208 GAEEGKVCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIK--YDAVtYT 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 102 SDYFDALYEFAEELITRDKAYVCALTADEMAEYRGSlkepGRNSPYRDRPVEESLQMFRDMRDGKYQNGELVLRAKIDMS 181
Cdd:PLN02907 286 SDYFPQLMEMAEKLIKEGKAYVDDTPREQMRKERMD----GIESKCRNNSVEENLRLWKEMIAGSERGLQCCVRGKLDMQ 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 182 SPNINMRDPILYRIRYAEHHQTGNKWCIYPMYDFTHPISDALEGITHSLCTLEFEDHRPLYDWVLDNIsGPCHPRQIEFA 261
Cdd:PLN02907 362 DPNKSLRDPVYYRCNPTPHHRIGSKYKVYPTYDFACPFVDALEGVTHALRSSEYHDRNAQYYRILEDM-GLRKVHIWEFS 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 262 RLNLNYTITSKRKLKRLVDENVVDGWNDPRMPTISGMRRRGYTPESIRTFCDMIGVNKaggtvDVGMLEHAIREDLNIR- 340
Cdd:PLN02907 441 RLNFVYTLLSKRKLQWFVDNGKVEGWDDPRFPTVQGIVRRGLKIEALKQFILSQGASK-----NLNLMEWDKLWTINKKi 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 341 ----APRAMCVMRPLKV--TLTNYPaDQSETLTLPVHPQNPDMGEREVPWTQTLYIDREDFEMepprkwkrLAPDQAVRL 414
Cdd:PLN02907 516 idpvCPRHTAVLKEGRVllTLTDGP-ETPFVRIIPRHKKYEGAGKKATTFTNRIWLDYADAEA--------ISEGEEVTL 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 415 RGGYVMTCREVIRDDSGQIVELKCEydpntlgVNPEG-YKPNGV-IHWVSA-SDSVEADINLYDRLFNHESPDSDKegDL 491
Cdd:PLN02907 587 MDWGNAIIKEITKDEGGAVTALSGE-------LHLEGsVKTTKLkLTWLPDtNELVPLSLVEFDYLITKKKLEEDD--NF 657
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 914748874 492 MDHLNPESlvvlkgaRVEKSLVA-------PRMDLpYQFEREGYFFCDQAHtEAAGRPV 543
Cdd:PLN02907 658 LDVLNPCT-------KKETAALGdsnmrnlKRGEI-IQLERKGYYRCDAPF-VRSSKPI 707
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
23-534 |
1.64e-106 |
|
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: 330.25 E-value: 1.64e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 23 GEHTGKVVTRFPPEPNGYLHIGHAKSICLNFGIAETFSGDCNLRFDDTNPEKENQEYIDAIKQDVEWLGYEWaGDVLYAS 102
Cdd:TIGR00463 88 GAKMGEVVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVKW-DEVVYQS 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 103 DYFDALYEFAEELITRDKAYVCALTADEMAEYRGSlkepGRNSPYRDRPVEESLQMFRDMRDGKYQNGELVLRAKIDMSS 182
Cdd:TIGR00463 167 DRIETYYDYTRKLIEMGKAYVCDCRPEEFRELRNR----GEACHCRDRSVEENLERWEEMLEGKEEGGSVVVRVKTDLKH 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 183 PNINMRDPILYRIRYAEHHQTGNKWCIYPMYDFTHPISDALEGITHSLCTLEFEDH--RPLYDWVLdniSGPCHPRQIEF 260
Cdd:TIGR00463 243 KNPAIRDWVIFRIVKTPHPRTGDKYRVYPTMDFSVAIDDHLLGVTHVLRGKDHIDNrrKQEYIYRY---FGWEPPEFIHW 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 261 ARLNLNY--TITSKRKLKRLVDENVVdGWNDPRMPTISGMRRRGYTPESIRTFCDMIGVNKAGGTVDVGMLEHAIREDLN 338
Cdd:TIGR00463 320 GRLKIDDvrALSTSSARKGILRGEYS-GWDDPRLPTLRAIRRRGIRPEAIRKFMLSIGVKINDVTMSWKNIYALNRKIID 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 339 IRAPRAMCVMRPLKVTLTNYPADQSEtlTLPVHPQNPDMGEREVPWTQTLYIDREDFEMEPprkwkrlapdQAVRLrggy 418
Cdd:TIGR00463 399 EEARRYFFIWNPVKIEIVGLPEPKRV--ERPLHPDHPEIGERVLILRGEIYVPKDDLEEGV----------EPVRL---- 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 419 vMTCREVIRDdsgqivelkcEYDPNTLGVNPEGYKPNG--VIHWVSASDSVEADINLYDRlfnhespdSDKEGdlmdhln 496
Cdd:TIGR00463 463 -MDAVNVIYS----------KKELRYHSEGLEGARKLGksIIHWLPAKDAVKVKVIMPDA--------SIVEG------- 516
|
490 500 510
....*....|....*....|....*....|....*...
gi 914748874 497 peslvvlkgaRVEKSLVAPRMDLPYQFEREGYFFCDQA 534
Cdd:TIGR00463 517 ----------VIEADASELEVGDVVQFERFGFARLDSA 544
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
17-532 |
8.41e-103 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 322.30 E-value: 8.41e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 17 EDAIASGEHTGKVVTRFPPEPNGYLHIGHAKSICLNFGIAETFSGDCNLRFDDTNPEKENQEYIDAIKQDVEWLGYEWAG 96
Cdd:PTZ00402 41 DKLQLTNAEEGKVVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDLATLGVSWDV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 97 DVLYASDYFDALYEFAEELITRDKAYVCALTADEMAEYRGSlkepGRNSPYRDRPVEESLQMFRDMRDGKYQNGELVLRA 176
Cdd:PTZ00402 121 GPTYSSDYMDLMYEKAEELIKKGLAYCDKTPREEMQKCRFD----GVPTKYRDISVEETKRLWNEMKKGSAEGQETCLRA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 177 KIDMSSPNINMRDPILYRIRYAEHHQTGNKWCIYPMYDFTHPISDALEGITHSLCTLEFEDHRPLYDWVLDNIsGPCHPR 256
Cdd:PTZ00402 197 KISVDNENKAMRDPVIYRVNLTPHARQGTKYKAYPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQYYWFCDAL-GIRKPI 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 257 QIEFARLNLNYTITSKRKLKRLVDENVVDGWNDPRMPTISGMRRRGYTPESIRTFCDMIGVNKAGGTVDVGMLEHAIRED 336
Cdd:PTZ00402 276 VEDFSRLNMEYSVMSKRKLTQLVDTHVVDGWDDPRFPTVRALVRRGLKMEALRQFVQEQGMSKTVNFMEWSKLWYFNTQI 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 337 LNIRAPRAMCVMRPLKVTLTNYPADQSETLTLPVHPQNPDMGEREVPWTQTLYIDREDFEMepprkwkrLAPDQAVRLR- 415
Cdd:PTZ00402 356 LDPSVPRYTVVSNTLKVRCTVEGQIHLEACEKLLHKKVPDMGEKTYYKSDVIFLDAEDVAL--------LKEGDEVTLMd 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 416 --GGYVMTCREviRDDSGQIVELkceydpnTLGVNPEG--YKPNGVIHWVSASDSVEA-DINLYDRLFNHESPDSdkEGD 490
Cdd:PTZ00402 428 wgNAYIKNIRR--SGEDALITDA-------DIVLHLEGdvKKTKFKLTWVPESPKAEVmELNEYDHLLTKKKPDP--EES 496
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 914748874 491 LMDHLNPESLVVLKGARVEKSLVAPRMDLpYQFEREGYFFCD 532
Cdd:PTZ00402 497 IDDIIAPVTKYTQEVYGEEALSVLKKGDI-IQLERRGYYIVD 537
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
27-528 |
6.76e-94 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 297.92 E-value: 6.76e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 27 GKVVTRFPPEPNGYLHIGHAKSICLNFGIAETFSGDCNLRFDDTNPEKEN--QEYIDAIKQDVEWLGYEWAgDVLYASDY 104
Cdd:PRK04156 100 GKVVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDPRTKRpdPEAYDMILEDLKWLGVKWD-EVVIQSDR 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 105 FDALYEFAEELITRDKAYVCALTADEMAEYRGSlkepGRNSPYRDRPVEESLQMFRDMRDGKYQNGELVLRAKIDMSSPN 184
Cdd:PRK04156 179 LEIYYEYARKLIEMGGAYVCTCDPEEFKELRDA----GKPCPHRDKSPEENLELWEKMLDGEYKEGEAVVRVKTDLEHPN 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 185 INMRDPILYRIRYAEHHQTGNKWCIYPMYDFTHPISDALEGITHslcTLEFEDH-------RPLYD---WVLdnisgpch 254
Cdd:PRK04156 255 PSVRDWVAFRIVKTPHPRVGDKYRVWPTYNFAVAVDDHLLGVTH---VLRGKDHidntekqRYIYDyfgWEY-------- 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 255 PRQIEFARLNLNYTITSKRKLKRLVDENVVDGWNDPRMPTISGMRRRGYTPESIRTFCDMIGVNKAGGTVDVGMLeHAI- 333
Cdd:PRK04156 324 PETIHYGRLKIEGFVLSTSKIRKGIEEGEYSGWDDPRLPTLRALRRRGILPEAIRELIIEVGVKETDATISWENL-YAIn 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 334 REDLNIRAPRAMCVMRPLKVTLTNYPadqSETLTLPVHPQNPDMGEREVPWTQTLYIDREDFEMEPPRkwkrlapdqaVR 413
Cdd:PRK04156 403 RKLIDPIANRYFFVRDPVELEIEGAE---PLEAKIPLHPDRPERGEREIPVGGKVYVSSDDLEAEGKM----------VR 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 414 LRG-GYVmtcrEVIRDDsgqivELKCEYDPNTLGVNPEGYKPngVIHWVSASDSVEADInlydrlfnhESPD-SDKEGdl 491
Cdd:PRK04156 470 LMDlFNV----EITGVS-----VDKARYHSDDLEEARKNKAP--IIQWVPEDESVPVRV---------LKPDgGDIEG-- 527
|
490 500 510
....*....|....*....|....*....|....*..
gi 914748874 492 mdHLNPESLVVLKGARVekslvaprmdlpyQFEREGY 528
Cdd:PRK04156 528 --LAEPDVADLEVDDIV-------------QFERFGF 549
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
16-535 |
9.76e-87 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 278.05 E-value: 9.76e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 16 IEDAIAsgehtGKVVTRFPPEPNGYLHIGHAKSICLNFGIAETFSGDCNLRFDDTNPEKENQEYIDAIKQDVEWLGYEwA 95
Cdd:PLN03233 4 LEGAIA-----GQIVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIK-P 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 96 GDVLYASDYFDALYEFAEELITRDKAYVCALTADEMAEYRGSLKEpgrnSPYRDRPVEESLQMFRDMRDGKYQNGELVLR 175
Cdd:PLN03233 78 DSVSFTSDYFEPIRCYAIILIEEGLAYMDDTPQEEMKKERADRAE----SKHRNQSPEEALEMFKEMCSGKEEGGAWCLR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 176 AKIDMSSPNINMRDPILYRIRYAEHHQTGNKWCIYPMYDFTHPISDALEGITHSLCTLEFEDHRPLYDWVLDNIsGPCHP 255
Cdd:PLN03233 154 AKIDMQSDNGTLRDPVLFRQNTTPHHRSGTAYKAYPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQKAL-GLRRP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 256 RQIEFARLNLNYTITSKRKLKRLVDENVVDGWNDPRMPTISGMRRRGYTPESIRTFCDMIGVNKAGGTVDVGMLEHAIRE 335
Cdd:PLN03233 233 RIHAFARMNFMNTVLSKRKLTWFVDNGHVTGWDDARFPTIRGISRRGIDIDALKMFMCSQGASRRVVNLDWAKFWAENKK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 336 DLNIRAPRAMCVMRPLKVTLTNYPADQSETLTLP---VHPQNPDMGEREVPWTQTLYIDREDFEmepprkwKRLAPDQAV 412
Cdd:PLN03233 313 EIDKRAKRFMAIDKADHTALTVTNADEEADFAFSetdCHPKDPGFGKRAMRICDEVLLEKADTE-------DIQLGEDIV 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 413 RLRGGYVmtcrEVIRDDSGqiveLKCEYDPNTlGVNPEGYKpngvIHWVS-ASDSVEADINLYDRLFNHESPDSDKegDL 491
Cdd:PLN03233 386 LLRWGVI----EISKIDGD----LEGHFIPDG-DFKAAKKK----ISWIAdVSDNIPVVLSEFDNLIIKEKLEEDD--KF 450
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 914748874 492 MDHLNPESLVVLK--GARVEKSLvaPRMDLpYQFEREGYFFCDQAH 535
Cdd:PLN03233 451 EDFINPDTLAETDviGDAGLKTL--KEHDI-IQLERRGFYRVDRPY 493
|
|
| tRNA-synt_1c_C |
pfam03950 |
tRNA synthetases class I (E and Q), anti-codon binding domain; Other tRNA synthetase ... |
341-532 |
1.73e-74 |
|
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: 234.09 E-value: 1.73e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 341 APRAMCVMRPLKVTLTNYPADQSETLTLPVHPQNPDMGEREVPWTQTLYIDREDFemepprkwKRLAPDQAVRLRGGYVM 420
Cdd:pfam03950 1 APRYMAVLDPVKVVIENYPEGQEETAEVPNHPKNPELGTRKVPFSREIYIEREDF--------KRLAPGEEVRLMDAYNI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 421 TCREVIRDDSGQIVELKCEYDPNTLGVNpegYKPNG-VIHWVSASDSVEADINLYDRLFNHEspdsDKEGDLmdhLNPES 499
Cdd:pfam03950 73 KVTEVVKDEDGNVTELHCTYDGDDLGGA---RKVKGkIIHWVSASDAVPAEVRLYDRLFKDE----DDADFL---LNPDS 142
|
170 180 190
....*....|....*....|....*....|...
gi 914748874 500 LVVLKGARVEKSLVAPRMDLPYQFEREGYFFCD 532
Cdd:pfam03950 143 LKVLTEGLAEPALANLKPGDIVQFERIGYFRVD 175
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
28-338 |
2.48e-63 |
|
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: 207.32 E-value: 2.48e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 28 KVVTRFPPEPNGYLHIGHAKSICLNFGIAETFSGDCNLRFDDTNPEKENQEYIDAIKQDVEWLGYEWAGDVLYASDYFDA 107
Cdd:cd00418 1 TVVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDWDEGPYRQSDRFDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 108 LYEFAEELITRDkayvcaltademaeyrgslkepgrnspyrdrpveeslqmfrdmrdgkyqngelvlrakidmsspninm 187
Cdd:cd00418 81 YRAYAEELIKKG-------------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 188 rdpilyriryaehhqtgnkwcIYPMYDFTHPISDALEGITHSLCTLEFEDHRPLYDWVLDNISGPcHPRQIEFARLNLNY 267
Cdd:cd00418 93 ---------------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWE-PPRFYHFPRLLLED 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 268 -TITSKRKLKrlvdenvvdgwndprmPTISGMRRRGYTPESIRTFCDMIG-----------------------VNKAGGT 323
Cdd:cd00418 151 gTKLSKRKLN----------------TTLRALRRRGYLPEALRNYLALIGwskpdghelftleemiaafsverVNSADAT 214
|
330
....*....|....*
gi 914748874 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 |
6.21e-45 |
|
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: 158.67 E-value: 6.21e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 28 KVVTRFPPEPNGYLHIGHAKSICLNFGIAETFSGDCNLRFDDTNPE--KENQEYIDAIKQDVEWLGYEWAgDVLYASDYF 105
Cdd:cd09287 1 KVVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPRtkRPDPEAYDMIPEDLEWLGVKWD-EVVIASDRI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 106 DALYEFAEELITRDKAYVcaltademaeyrgslkepgrnspyrdrpveeslqmfrdmrdgkyqngelvlrakidmsspni 185
Cdd:cd09287 80 ELYYEYARKLIEMGGAYV-------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 186 nmrdpilyriryaeHHQTGNKWCIYPMYDFTHPISDALEGITHSLCTLEFED----HRPLYDWVldnisGPCHPRQIEFA 261
Cdd:cd09287 98 --------------HPRTGSKYRVWPTLNFAVAVDDHLLGVTHVLRGKDHIDntekQRYIYEYF-----GWEYPETIHWG 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 262 RLNLNYTITSKRKLKRLVDENVVDGWNDPRMPTISGMRRRGYTPESIRTFCDMIGVNKAGGTVDVGMLEHAIREDLNIRA 341
Cdd:cd09287 159 RLKIEGGKLSTSKIRKGIESGEYEGWDDPRLPTLRALRRRGIRPEAIRDFIIEVGVKQTDATISWENLYAINRKLIDPRA 238
|
..
gi 914748874 342 PR 343
Cdd:cd09287 239 NR 240
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
25-142 |
3.17e-16 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 79.51 E-value: 3.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 25 HTGKVVTRFPPEPNGYLHIGHAKSICLNFGIAETFSGDCNLRFDDTNPEKENQEYIDAIKQDVEWLGYEWAGDVLYASDY 104
Cdd:PRK05710 2 TMTPYIGRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWDGPVLYQSQR 81
|
90 100 110
....*....|....*....|....*....|....*....
gi 914748874 105 FDAlYEFA-EELITRDKAYVCALTADEMAEYRGSLKEPG 142
Cdd:PRK05710 82 HDA-YRAAlDRLRAQGLVYPCFCSRKEIAAAAPAPPDGG 119
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
28-116 |
8.72e-14 |
|
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: 71.08 E-value: 8.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 28 KVVTRFPPEPNGYLHIGHAKSICLNFGIAETFSGDCNLRFDDTNPEKENQEYIDAIKQDVEWLGYEWAGDVL-------- 99
Cdd:cd00808 1 KVRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEGPDvggpygpy 80
|
90
....*....|....*..
gi 914748874 100 YASDYFDALYEFAEELI 116
Cdd:cd00808 81 RQSERLEIYRKYAEKLL 97
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
19-240 |
2.92e-12 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 69.00 E-value: 2.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 19 AIASGEHT-GKVVTRFPPEPNGYLHIGHAKSICLNFGIAETFSGDCNLRFDDTNPEKENQEYIDAIKQDVEWLGYEW--- 94
Cdd:PLN02627 35 AAAAGESKgGPVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWdeg 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 95 ---AGDV-LYASDYFDALY-EFAEELITRDKAYVCALTADEMAEYRGSLKEPGRNSPYR-------DRPVEESLQ----- 157
Cdd:PLN02627 115 pdvGGEYgPYRQSERNAIYkQYAEKLLESGHVYPCFCTDEELEAMKEEAELKKLPPRYTgkwatasDEEVQAELAkgtpy 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 158 --MFRDMRDGKYQNGELVlRAKIdmsSPNIN-MRDPILYRiryaehhQTGNkwciyPMYDFTHPISDALEGITHslcTLE 234
Cdd:PLN02627 195 tyRFRVPKEGSVKIDDLI-RGEV---SWNTDtLGDFVLLR-------SNGQ-----PVYNFCVAVDDATMGITH---VIR 255
|
....*.
gi 914748874 235 FEDHRP 240
Cdd:PLN02627 256 AEEHLP 261
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
30-115 |
1.18e-10 |
|
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: 59.80 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914748874 30 VTRFPPEPNGYLHIGHAKSICLNFGIAETFSGD-----CNLRFDDTNPEKENQ-------------EYIDAIKQDVEWLg 91
Cdd:cd00802 1 TTFSGITPNGYLHIGHLRTIVTFDFLAQAYRKLgykvrCIALIDDAGGLIGDPankkgenakafveRWIERIKEDVEYM- 79
|
90 100
....*....|....*....|....
gi 914748874 92 YEWAGDVLYASDYFDALYEFAEEL 115
Cdd:cd00802 80 FLQAADFLLLYETECDIHLGGSDQ 103
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
30-97 |
7.98e-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: 7.98e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 914748874 30 VTRFPPEPnGYLHIGHAKSICLNFGIAetfsGDCNLRFDDTNPEKENQ------EYIDAIKQDVEWLGYEWAGD 97
Cdd:cd02156 1 KARFPGEP-GYLHIGHAKLICRAKGIA----DQCVVRIDDNPPVKVWQdpheleERKESIEEDISVCGEDFQQN 69
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
228-274 |
8.04e-08 |
|
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: 50.62 E-value: 8.04e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 914748874 228 HSLCTLEFEDHRPLYDWVLDNISGPCHPRQIEFARLNLNYTITSKRK 274
Cdd:cd02156 59 ISVCGEDFQQNRELYRWVKDNITLPVDPEQVELPRLNLETTVMSKRK 105
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