|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09194 |
PRK09194 |
prolyl-tRNA synthetase; Provisional |
1-570 |
0e+00 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 236405 [Multi-domain] Cd Length: 565 Bit Score: 1129.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193038 1 MRTSQYLLSTLKETPADAVVISHQLLLRAGMIRRLASGLYTWLPMGLRVLRKVETIVREEMNAAGALEVLMPAVQPAELW 80
Cdd:PRK09194 1 MRTSQLFLPTLKETPADAEVISHQLLLRAGYIRKLASGIYTYLPLGLRVLRKIENIVREEMNKIGAQEVLMPALQPAELW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193038 81 QESGRWEQYGPELLRLKDRHEREFCVGPTHEEVITDLARNELNSYKQLPINFYQIQTKFRDEIRPRFGLMRGREFIMKDA 160
Cdd:PRK09194 81 QESGRWEEYGPELLRLKDRHGRDFVLGPTHEEVITDLVRNEIKSYKQLPLNLYQIQTKFRDEIRPRFGLMRGREFIMKDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193038 161 YSFHLSQDSLQQTYDGMYQAYSKIFSRLGLDFRPVQADNGSIGGSGSHEFHVLANSGEDDIVFSDSSDYAANIEKAEAVP 240
Cdd:PRK09194 161 YSFHADEESLDETYDAMYQAYSRIFDRLGLDFRAVEADSGAIGGSASHEFMVLADSGEDTIVYSDESDYAANIEKAEALP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193038 241 RESArgSATEDMRLVDTPNTKTIAALVDGFQLPIEKTIKTLVVHGAEEgtLVALIVRGDHELNEIKAANQPLVAsPLVFA 320
Cdd:PRK09194 241 PPRA--AAEEALEKVDTPNAKTIEELAEFLNVPAEKTVKTLLVKADGE--LVAVLVRGDHELNEVKLENLLGAA-PLELA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193038 321 SEAEIRAAIGAGPGSLGPVNLP--IACIVDRSVALMSDFAAGANIEDKHYFGVNWERDLPLPEVADLRNVVEGDPSPDGK 398
Cdd:PRK09194 316 TEEEIRAALGAVPGFLGPVGLPkdVPIIADRSVADMSNFVVGANEDDYHYVGVNWGRDFPVPEVADLRNVVEGDPSPDGG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193038 399 GTLVIKRGIEVGHIFQLGTKYSEAMKLSVLSEQGKPVNLIMGCYGIGVSRVVAAAIEQNHDERGILWPSALAPFQIALVP 478
Cdd:PRK09194 396 GTLKIARGIEVGHIFQLGTKYSEAMNATVLDENGKAQPLIMGCYGIGVSRLVAAAIEQNHDEKGIIWPKAIAPFDVHIVP 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193038 479 LKYETESVKQATDKLYAELTAAGFEVLLDDRDKktSPGVKFADMELIGIPHRIVISDRGLSEGVLEYKGRRDSESQNLPI 558
Cdd:PRK09194 476 VNMKDEEVKELAEKLYAELQAAGIEVLLDDRKE--RPGVKFADADLIGIPHRIVVGDRGLAEGIVEYKDRRTGEKEEVPV 553
|
570
....*....|..
gi 489193038 559 GELMSFITEKLS 570
Cdd:PRK09194 554 DELVEFLKALKK 565
|
|
| ProS |
COG0442 |
Prolyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Prolyl-tRNA ... |
1-569 |
0e+00 |
|
Prolyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Prolyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440211 [Multi-domain] Cd Length: 564 Bit Score: 1056.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193038 1 MRTSQYLLSTLKETPADAVVISHQLLLRAGMIRRLASGLYTWLPMGLRVLRKVETIVREEMNAAGALEVLMPAVQPAELW 80
Cdd:COG0442 1 MRASKLFIPTLKERPADAEVWSHQLMLRAGLIRKLASGIYTYLPLGYRVLEKIEAIVREEMKRTGAQEVLMPLLQPAELW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193038 81 QESGRWEQYGPELLRLKDRHEREFCVGPTHEEVITDLARNELNSYKQLPINFYQIQTKFRDEIRPRFGLMRGREFIMKDA 160
Cdd:COG0442 81 EESGRWEGFGPELARVTDRLEREFCLGPTHEEVITDLVRNEIKSYRDLPLLLYQIQTKFRDEIRPRFGLLRTREFLMKDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193038 161 YSFHLSQDSLQQTYDGMYQAYSKIFSRLGLDFRPVQADNGSIGGSGSHEFHVLANSGEDDIVFSDSSDYAANIEKAEAVP 240
Cdd:COG0442 161 YSFHATEEELDEEYQKMLDAYERIFERLGLPVRAVEADSGAIGGSESHEFMVLADSGEDTIVYCDACDYAANIEKAEALA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193038 241 RESARGSATEDMRLVDTPNTKTIAALVDGFQLPIEKTIKTLVVHGaeEGTLVALIVRGDHELNEIKAANQpLVASPLVFA 320
Cdd:COG0442 241 PPAERAEPTKELEAVATPGAKTIEEVAEFLGVPAEKTVKTLVYKA--DGELVAVLVRGDHELNEIKLENL-LGASELELA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193038 321 SEAEIRAAIGAGPGSLGPVNLPIACIVDRSVALMSDFAAGANIEDKHYFGVNWERDLPLPEVADLRNVVEGDPSPDGKGT 400
Cdd:COG0442 318 TEEEIEAALGAVPGFLGPVGLGVPYIADRSVAGMSNFVCGANEDDYHYTNVNWGRDFPVDEVADLRNVVEGDPCPDCGGL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193038 401 LVIKRGIEVGHIFQLGTKYSEAMKLSVLSEQGKPVNLIMGCYGIGVSRVVAAAIEQNHDERGILWPSALAPFQIALVPLK 480
Cdd:COG0442 398 LQDGRGIEVGHIFKLGTKYSKAMDATFLDENGKEQPVWMGCYGIGVTRLIAAAIEQHHDDKGIIWPPAIAPFQVVIVPIN 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193038 481 YETESVKQATDKLYAELTAAGFEVLLDDRDKktSPGVKFADMELIGIPHRIVISDRGLSEGVLEYKGRRDSESQNLPIGE 560
Cdd:COG0442 478 MKDEAVLEAAEELYAELKAAGIDVLLDDRDE--RPGVKFADAELIGIPLRIVIGPRDLEEGQVEVKRRDTGEKEEVPLDE 555
|
....*....
gi 489193038 561 LMSFITEKL 569
Cdd:COG0442 556 LVETVKELL 564
|
|
| proS_fam_II |
TIGR00409 |
prolyl-tRNA synthetase, family II; Prolyl-tRNA synthetase is a class II tRNA synthetase and is ... |
1-568 |
0e+00 |
|
prolyl-tRNA synthetase, family II; Prolyl-tRNA synthetase is a class II tRNA synthetase and is recognized by pfam model tRNA-synt_2b, which recognizes tRNA synthetases for Gly, His, Ser, and Pro. The prolyl-tRNA synthetases are divided into two widely divergent groups. This group includes enzymes from Escherichia coli, Bacillus subtilis, Aquifex aeolicus, the spirochete Treponema pallidum, Synechocystis PCC6803, and one of the two prolyL-tRNA synthetases of Saccharomyces cerevisiae. The other group includes the Pro-specific domain of a human multifunctional tRNA ligase and the prolyl-tRNA synthetases from the Archaea, the Mycoplasmas, and the spirochete Borrelia burgdorferi. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273063 [Multi-domain] Cd Length: 568 Bit Score: 895.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193038 1 MRTSQYLLSTLKETPADAVVISHQLLLRAGMIRRLASGLYTWLPMGLRVLRKVETIVREEMNAAGALEVLMPAVQPAELW 80
Cdd:TIGR00409 1 MRTSQYLFPTLKETPADAEVKSHQLLLRAGFIRRLGSGLYNWLPLGLRVLKKVENIVREEMNKDGAIEVLLPALQPAELW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193038 81 QESGRWEQYGPELLRLKDRHEREFCVGPTHEEVITDLARNELNSYKQLPINFYQIQTKFRDEIRPRFGLMRGREFIMKDA 160
Cdd:TIGR00409 81 QESGRWDTYGPELLRLKDRKGREFVLGPTHEEVITDLARNEIKSYKQLPLNLYQIQTKFRDEIRPRFGLMRGREFIMKDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193038 161 YSFHLSQDSLQQTYDGMYQAYSKIFSRLGLDFRPVQADNGSIGGSGSHEFHVLANSGEDDIVFSDSSDYAANIEKAEAVP 240
Cdd:TIGR00409 161 YSFHSDEESLDATYQKMYQAYSNIFSRLGLDFRPVQADSGAIGGSASHEFMVLAESGEDTIVYSDESDYAANIELAEALA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193038 241 REsARGSATEDMRLVDTPNTKTIAALVDGFQLPIEKTIKTLVVHGAEEG-TLVALIVRGDHELNEIKAANQPLVASPLVF 319
Cdd:TIGR00409 241 PG-ERNAPTAELDKVDTPNTKTIAELVECFNLPAEKVVKTLLVKAVDKSePLVALLVRGDHELNEVKAPNLLLVAQVLEL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193038 320 ASEAEIRAAIGAGPGSLGPVNLP--IACIVDRSVALMSDFAAGANIEDKHYFGVNWERDLPLPEVADLRNVVEGDPSPDG 397
Cdd:TIGR00409 320 ATEEEIFQKIASGPGSLGPVNINggIPVLIDQTVALMSDFAAGANADDKHYFNVNWDRDVAIPEVADIRKVKEGDPSPDG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193038 398 KGTLVIKRGIEVGHIFQLGTKYSEAMKLSVLSEQGKPVNLIMGCYGIGVSRVVAAAIEQNHDERGILWPSALAPFQIALV 477
Cdd:TIGR00409 400 QGTLKIARGIEVGHIFQLGTKYSEALKATFLDENGKNQFMTMGCYGIGVSRLVSAIAEQHHDERGIIWPKAIAPYDVVIV 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193038 478 PLKYETESVKQATDKLYAELTAAGFEVLLDDRDKKtsPGVKFADMELIGIPHRIVISDRGLSEGVLEYKGRRDSESQNLP 557
Cdd:TIGR00409 480 VMNMKDEEQQQLAEELYSELLAQGVDVLLDDRNER--AGVKFADSELIGIPLRVVVGKKNLDNGEIEVKKRRNGEKQLIK 557
|
570
....*....|.
gi 489193038 558 IGELMSFITEK 568
Cdd:TIGR00409 558 KDELVECLEEQ 568
|
|
| PRK12325 |
PRK12325 |
prolyl-tRNA synthetase; Provisional |
1-567 |
0e+00 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 237059 [Multi-domain] Cd Length: 439 Bit Score: 612.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193038 1 MRTSQYLLSTLKETPADAVVISHQLLLRAGMIRRLASGLYTWLPMGLRVLRKVETIVREEMNAAGALEVLMPAVQPAELW 80
Cdd:PRK12325 1 MRLSRYFLPTLKENPKEAEIVSHRLMLRAGMIRQQAAGIYSWLPLGLKVLKKIENIVREEQNRAGAIEILMPTIQPADLW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193038 81 QESGRWEQYGPELLRLKDRHEREFCVGPTHEEVITDLARNELNSYKQLPINFYQIQTKFRDEIRPRFGLMRGREFIMKDA 160
Cdd:PRK12325 81 RESGRYDAYGKEMLRIKDRHDREMLYGPTNEEMITDIFRSYVKSYKDLPLNLYHIQWKFRDEIRPRFGVMRGREFLMKDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193038 161 YSFHLSQDSLQQTYDGMYQAYSKIFSRLGLDFRPVQADNGSIGGSGSHEFHVLANSGEDDIVFsdssdyaaniekaeavp 240
Cdd:PRK12325 161 YSFDLDEEGARHSYNRMFVAYLRTFARLGLKAIPMRADTGPIGGDLSHEFIILAETGESTVFY----------------- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193038 241 resargsateDMRLVDTPntktiaalVDGFQLPIEktiktlvvhgaeegtlvalivrgDHELNEIKAanqplvasplvfa 320
Cdd:PRK12325 224 ----------DKDFLDLL--------VPGEDIDFD-----------------------VADLQPIVD------------- 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193038 321 seaeiraaigagpgslgpvnlpiacivdrsvALMSDFAAganIEDKHyfgvNWERDLPLPEvadlrnvvegdpspdgkGT 400
Cdd:PRK12325 250 -------------------------------EWTSLYAA---TEEMH----DEAAFAAVPE-----------------ER 274
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193038 401 LVIKRGIEVGHIFQLGTKYSEAMKLSVLSEQGKPVNLIMGCYGIGVSRVVAAAIEQNHDERGILWPSALAPFQIALVPLK 480
Cdd:PRK12325 275 RLSARGIEVGHIFYFGTKYSEPMNAKVQGPDGKEVPVHMGSYGIGVSRLVAAIIEASHDDKGIIWPESVAPFKVGIINLK 354
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193038 481 YETESVKQATDKLYAELTAAGFEVLLDDRDKktSPGVKFADMELIGIPHRIVISDRGLSEGVLEYKGRRDSESQNLPIGE 560
Cdd:PRK12325 355 QGDEACDAACEKLYAALSAAGIDVLYDDTDE--RPGAKFATMDLIGLPWQIIVGPKGLAEGKVELKDRKTGEREELSVEA 432
|
....*..
gi 489193038 561 LMSFITE 567
Cdd:PRK12325 433 AINRLTA 439
|
|
| ProRS_core_prok |
cd00779 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
17-456 |
1.30e-157 |
|
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain. This subfamily contains the core domain of ProRS from prokaryotes and from the mitochondria of eukaryotes.
Pssm-ID: 238402 [Multi-domain] Cd Length: 255 Bit Score: 450.49 E-value: 1.30e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193038 17 DAVVISHQLLLRAGMIRRLASGLYTWLPMGLRVLRKVETIVREEMNAAGALEVLMPAVQPAELWQESGRWEQYGPELLRL 96
Cdd:cd00779 1 DAEIISHKLLLRAGFIRQTSSGLYSWLPLGLRVLKKIENIIREEMNKIGAQEILMPILQPAELWKESGRWDAYGPELLRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193038 97 KDRHEREFCVGPTHEEVITDLARNELNSYKQLPINFYQIQTKFRDEIRPRFGLMRGREFIMKDAYSFHLSQDSLQQTYDG 176
Cdd:cd00779 81 KDRHGKEFLLGPTHEEVITDLVANEIKSYKQLPLNLYQIQTKFRDEIRPRFGLMRGREFLMKDAYSFDIDEESLEETYEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193038 177 MYQAYSKIFSRLGLDFRPVQADNGSIGGSGSHEFHVLANsgeddivfsdssdyaaniekaeavpresargsatedmrlvd 256
Cdd:cd00779 161 MYQAYSRIFKRLGLPFVKVEADSGAIGGSLSHEFHVLSP----------------------------------------- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193038 257 tpntktiaalvdgfqlpiektiktlvvhgaeegtlvalivrgdhelneikaanqplvasplvfaseaeiraaigagpgsl 336
Cdd:cd00779 --------------------------------------------------------------------------------
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193038 337 gpvnlpiacivdrsvalmsdfaaganiedkhyfgvnwerdlplpevadlrnvvegdpspdgkgtLVIKRGIEVGHIFQLG 416
Cdd:cd00779 200 ----------------------------------------------------------------LKITKGIEVGHIFQLG 215
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 489193038 417 TKYSEAMKLSVLSEQGKPVNLIMGCYGIGVSRVVAAAIEQ 456
Cdd:cd00779 216 TKYSKALGATFLDENGKPKPLEMGCYGIGVSRLLAAIIEQ 255
|
|
| ProRS-INS |
cd04334 |
INS is an amino acid-editing domain inserted (INS) into the bacterial class II prolyl-tRNA ... |
226-385 |
8.18e-77 |
|
INS is an amino acid-editing domain inserted (INS) into the bacterial class II prolyl-tRNA synthetase (ProRS) however, this CD is not exclusively bacterial. It is also found at the N-terminus of the eukaryotic/archaea-like ProRS's of yeasts and single-celled parasites. ProRS catalyzes the attachment of proline to tRNA(Pro); proline is first activated by ATP, and then transferred to the acceptor end of tRNA(Pro). ProRS can inadvertently process noncognate amino acids such as alanine and cysteine, and to avoid such errors, in post-transfer editing, the INS domain deacylates mischarged Ala-tRNA(Pro), thus ensuring the fidelity of translation. Misacylated Cys-tRNA(Pro) is not edited by ProRS. In addition to the INS editing domain, the prokaryote-like ProRS protein contains catalytic and anticodon-binding domains which form a dimeric interface.
Pssm-ID: 239826 [Multi-domain] Cd Length: 160 Bit Score: 240.11 E-value: 8.18e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193038 226 SSDYAANIEKAEAVPRESARGSATEDMRLVDTPNTKTIAALVDGFQLPIEKTIKTLVVHGAEEGTLVALIVRGDHELNEI 305
Cdd:cd04334 1 DCDYAANIEKAESLPPAAERPAPPKELEKVATPGQKTIEELAEFLGVPPSQTVKTLLVKADGEEELVAVLLRGDHELNEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193038 306 KAANQPLVAsPLVFASEAEIRAAIGAGPGSLGPVNLP-IACIVDRSVALMSDFAAGANIEDKHYFGVNWERDLPLPEVAD 384
Cdd:cd04334 81 KLENLLGAA-PLELASEEEIEAATGAPPGFIGPVGLKkIPIIADRSVADLKNFVCGANEDDYHYVNVNWGRDFPLPEVAD 159
|
.
gi 489193038 385 L 385
Cdd:cd04334 160 L 160
|
|
| ProRS_core |
cd00772 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
17-217 |
3.92e-46 |
|
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain.
Pssm-ID: 238395 [Multi-domain] Cd Length: 264 Bit Score: 163.31 E-value: 3.92e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193038 17 DAVVISHQLLLRAGMIRRL-ASGLYTWLPMGLRVLRKVETIVREEMNAAGALEVLMPAVQPAELWQESGRWEQYG-PELL 94
Cdd:cd00772 1 DASEKSLEHIGKAELADQGpGRGIINFLPLAKAILDKIENVLDKMFKEHGAQNALFPFFILASFLEKEAEHDEGFsKELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193038 95 RLKDR----HEREFCVGPTHEEVITDLARNELNSYKQLPINFYQIQTKFRDEIRPRFGLMRGREFIMKDAYSFHLSQDSL 170
Cdd:cd00772 81 VFKDAgdeeLEEDFALRPTLEENIGEIAAKFIKSWKDLPQHLNQIGNKFRDEIRPRFGFLRAREFIMKDGHSAHADAEEA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489193038 171 QQTYDGMYQAYSKIFSRLG-LDFRPVQADNGS--IGGSGSHEFHVLANSG 217
Cdd:cd00772 161 DEEFLNMLSAYAEIARDLAaIDFIEGEADEGAkfAGASKSREFEALMEDG 210
|
|
| ProRS_anticodon_short |
cd00861 |
ProRS Prolyl-anticodon binding domain, short version found predominantly in bacteria. ProRS ... |
471-566 |
1.17e-34 |
|
ProRS Prolyl-anticodon binding domain, short version found predominantly in bacteria. ProRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only.
Pssm-ID: 238438 [Multi-domain] Cd Length: 94 Bit Score: 125.78 E-value: 1.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193038 471 PFQIALVPLKYETESVKQATDKLYAELTAAGFEVLLDDRDKktSPGVKFADMELIGIPHRIVISDRGLSEGVLEYKGRRD 550
Cdd:cd00861 1 PFDVVIIPMNMKDEVQQELAEKLYAELQAAGVDVLLDDRNE--RPGVKFADADLIGIPYRIVVGKKSAAEGIVEIKVRKT 78
|
90
....*....|....*.
gi 489193038 551 SESQNLPIGELMSFIT 566
Cdd:cd00861 79 GEKEEISIDELLEFLQ 94
|
|
| YbaK_like |
cd04332 |
YbaK-like. The YbaK family of deacylase domains includes the INS amino acid-editing domain of ... |
250-383 |
6.36e-33 |
|
YbaK-like. The YbaK family of deacylase domains includes the INS amino acid-editing domain of the bacterial class II prolyl tRNA synthetase (ProRS), and it's trans-acting homologs, YbaK, ProX, and PrdX. The primary function of INS is to hydrolyze mischarged cysteinyl-tRNA(Pro)'s, thus helping ensure the fidelity of translation. Organisms whose ProRS lacks the INS domain express an INS homolog in trans (e.g. YbaK, ProX, or PrdX).
Pssm-ID: 239824 [Multi-domain] Cd Length: 136 Bit Score: 122.65 E-value: 6.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193038 250 EDMRLVDTPNTKTIAALVDGFQLPIEKTIKTLVVHGAEEGtLVALIVRGDHELNEIKAANQPLVAsPLVFASEAEIRAAI 329
Cdd:cd04332 1 EYLEYEHTPGAKTIEEAAEALGVPPGQIAKTLVLKDDKGG-LVLVVVPGDHELDLKKLAKALGAK-KLRLASEEELEELT 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 489193038 330 GAGPGSLGPVNLP--IACIVDRSVALMSDFAAGANI--EDKHYFGVNWERDLPLPEVA 383
Cdd:cd04332 79 GCEPGGVGPFGLKkgVPVVVDESLLELEDVYVGAGErgADLHLSPADLLRLLGEAEVA 136
|
|
| Gly_His_Pro_Ser_Thr_tRS_core |
cd00670 |
Gly_His_Pro_Ser_Thr_tRNA synthetase class II core domain. This domain is the core catalytic ... |
49-206 |
2.11e-29 |
|
Gly_His_Pro_Ser_Thr_tRNA synthetase class II core domain. This domain is the core catalytic domain of tRNA synthetases of the subgroup containing glycyl, histidyl, prolyl, seryl and threonyl tRNA synthetases. It is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. These enzymes belong to class II aminoacyl-tRNA synthetases (aaRS) based upon their structure and the presence of three characteristic sequence motifs in the core domain. This domain is also found at the C-terminus of eukaryotic GCN2 protein kinase and at the N-terminus of the ATP phosphoribosyltransferase accessory subunit, HisZ and the accessory subunit of mitochondrial polymerase gamma (Pol gamma b) . Most class II tRNA synthetases are dimers, with this subgroup consisting of mostly homodimers. These enzymes attach a specific amino acid to the 3' OH group of ribose of the appropriate tRNA.
Pssm-ID: 238359 [Multi-domain] Cd Length: 235 Bit Score: 116.34 E-value: 2.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193038 49 VLRKVETIVREEMNAAGALEVLMPAVQPAELWQESGRWEQYGPELLRLKDR----HEREFCVGPTHEEVITDLARNELNS 124
Cdd:cd00670 4 LWRALERFLDDRMAEYGYQEILFPFLAPTVLFFKGGHLDGYRKEMYTFEDKgrelRDTDLVLRPAACEPIYQIFSGEILS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193038 125 YKQLPINFYQIQTKFRDEIRPRFGLMRGREFIMKDAYSFHlSQDSLQQTYDGMYQAYSKIFSRLGLDFRPVQADNGSIGG 204
Cdd:cd00670 84 YRALPLRLDQIGPCFRHEPSGRRGLMRVREFRQVEYVVFG-EPEEAEEERREWLELAEEIARELGLPVRVVVADDPFFGR 162
|
..
gi 489193038 205 SG 206
Cdd:cd00670 163 GG 164
|
|
| tRNA_edit |
pfam04073 |
Aminoacyl-tRNA editing domain; This domain is found either on its own or in association with ... |
257-374 |
9.79e-25 |
|
Aminoacyl-tRNA editing domain; This domain is found either on its own or in association with the tRNA synthetase class II core domain (pfam00587). It is involved in the tRNA editing of mis-charged tRNAs including Cys-tRNA(Pro), Cys-tRNA(Cys), Ala-tRNA(Pro). The structure of this domain shows a novel fold.
Pssm-ID: 427693 [Multi-domain] Cd Length: 123 Bit Score: 99.21 E-value: 9.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193038 257 TPNTKTIAALVDGFQLPIEKTIKTLVVHGAeEGTLVALIVRGDHELNEIKAANQpLVASPLVFASEAEIRAAIGAGPGSL 336
Cdd:pfam04073 1 HPPAATIEELAAALGVPPGRIAKTLVLKDK-KGKYVLVVVPGDREVDLKKLAKL-LGVKRLRLASEEELLELTGVEPGGV 78
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 489193038 337 GPVNLPIA---CIVDRSVALMSDFAAGANIEDKHYFGVNWE 374
Cdd:pfam04073 79 TPFGLKAKgvpVLVDESLKDLPDVVVGAGENGATLRLSNAD 119
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
95-207 |
6.85e-22 |
|
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely threonyl-tRNA members.
Pssm-ID: 395469 [Multi-domain] Cd Length: 181 Bit Score: 93.25 E-value: 6.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193038 95 RLKDRHEREFCVGPTHEEVITDLARNELNSYKQLPINFYQIQTKFRDEIRPRF-GLMRGREFIMKDAYSFHLSQDSLQQT 173
Cdd:pfam00587 2 KVEDENGDELALKPTNEPGHTLLFREEGLRSKDLPLKLAQFGTCFRHEASGDTrGLIRVRQFHQDDAHIFHAPGQSPDEL 81
|
90 100 110
....*....|....*....|....*....|....
gi 489193038 174 YDgMYQAYSKIFSRLGLDFRPVQADNGSIGGSGS 207
Cdd:pfam00587 82 ED-YIKLIDRVYSRLGLEVRVVRLSNSDGSAFYG 114
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
49-203 |
2.02e-19 |
|
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA synthetases (aaRS) share a common fold and generally attach an amino acid to the 3' OH of ribose of the appropriate tRNA. PheRS is an exception in that it attaches the amino acid at the 2'-OH group, like class I aaRSs. These enzymes are usually homodimers. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. The substrate specificity of this reaction is further determined by additional domains. Intererestingly, this domain is also found is asparagine synthase A (AsnA), in the accessory subunit of mitochondrial polymerase gamma and in the bacterial ATP phosphoribosyltransferase regulatory subunit HisZ.
Pssm-ID: 238391 [Multi-domain] Cd Length: 211 Bit Score: 86.79 E-value: 2.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193038 49 VLRKVETIVREEMNAAGALEVLMPAVQPAELWQESGRWEQYgpeLLRLKDRHEREFCVGPTHEEVITDLARNELnsyKQL 128
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGHEPKD---LLPVGAENEEDLYLRPTLEPGLVRLFVSHI---RKL 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489193038 129 PINFYQIQTKFRDEIRPRfGLMRGREFIMKDAYSFHlSQDSLQQTYDGMYQAYSKIFSRLG--LDFRPVQADNGSIG 203
Cdd:cd00768 75 PLRLAEIGPAFRNEGGRR-GLRRVREFTQLEGEVFG-EDGEEASEFEELIELTEELLRALGikLDIVFVEKTPGEFS 149
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
473-568 |
3.50e-19 |
|
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA synthetases it is probably the anticodon binding domain.
Pssm-ID: 460819 [Multi-domain] Cd Length: 94 Bit Score: 82.63 E-value: 3.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193038 473 QIALVPLKYETESVKQATDKLYAELTAAGFEVLLDDRDKktSPGVKFADMELIGIPHRIVISDRGLSEGVLEYKGRRDSE 552
Cdd:pfam03129 1 QVVVIPLGEKAEELEEYAQKLAEELRAAGIRVELDDRNE--SIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGE 78
|
90
....*....|....*.
gi 489193038 553 SQNLPIGELMSFITEK 568
Cdd:pfam03129 79 QETVSLDELVEKLKEL 94
|
|
| ProRS_core_arch_euk |
cd00778 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
23-188 |
2.30e-16 |
|
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain. This subfamily contains the core domain of ProRS from archaea, the cytoplasm of eukaryotes and some bacteria.
Pssm-ID: 238401 [Multi-domain] Cd Length: 261 Bit Score: 79.18 E-value: 2.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193038 23 HQLLLRAGMI-RRLASGLYTWLPMGLRVLRKVETIVREEMNAAGALEVLMPAVQP-AELWQESGRWEQYGPEL-----LR 95
Cdd:cd00778 7 TEVITKAELIdYGPVKGCMVFRPYGYAIWENIQKILDKEIKETGHENVYFPLLIPeSELEKEKEHIEGFAPEVawvthGG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193038 96 LKDRHEReFCVGPTHEEVITDLARNELNSYKQLPINFYQIQTKFRDEIRPRFGLMRGREFIMKDAYSFHLSQ-DSLQQTY 174
Cdd:cd00778 87 LEELEEP-LALRPTSETAIYPMFSKWIRSYRDLPLKINQWVNVFRWETKTTRPFLRTREFLWQEGHTAHATEeEAEEEVL 165
|
170
....*....|....
gi 489193038 175 DgMYQAYSKIFSRL 188
Cdd:cd00778 166 Q-ILDLYKEFYEDL 178
|
|
| ProRS_anticodon_zinc |
cd00862 |
ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and ... |
462-569 |
2.33e-16 |
|
ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and archaea. ProRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only, and an additional C-terminal zinc-binding domain specific to this subfamily of aaRSs.
Pssm-ID: 238439 [Multi-domain] Cd Length: 202 Bit Score: 77.72 E-value: 2.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193038 462 GILWPSALAPFQIALVPLKY---ETESVKQATDKLYAELTAAGFEVLLDDRDKKTsPGVKFADMELIGIPHRIVISDRGL 538
Cdd:cd00862 1 GLVLPPRVAPIQVVIVPIGIkdeKREEVLEAADELAERLKAAGIRVHVDDRDNYT-PGWKFNDWELKGVPLRIEIGPRDL 79
|
90 100 110
....*....|....*....|....*....|.
gi 489193038 539 SEGVLEYKGRRDSESQNLPIGELMSFITEKL 569
Cdd:cd00862 80 EKNTVVIVRRDTGEKKTVPLAELVEKVPELL 110
|
|
| HGTP_anticodon |
cd00738 |
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ... |
471-565 |
9.13e-16 |
|
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and prolyl tRNA synthetases, which are classified as a group of class II aminoacyl-tRNA synthetases (aaRS). In aaRSs, the anticodon binding domain is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only. This domain is also found in the accessory subunit of mitochondrial polymerase gamma (Pol gamma b).
Pssm-ID: 238379 [Multi-domain] Cd Length: 94 Bit Score: 72.82 E-value: 9.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193038 471 PFQIALVPLKYETESVKQATDKLYAELTAAGFEVLLDDRDKKtsPGVKFADMELIGIPHRIVISDRGLSEGVLEYKGRRD 550
Cdd:cd00738 1 PIDVAIVPLTDPRVEAREYAQKLLNALLANGIRVLYDDRERK--IGKKFREADLRGVPFAVVVGEDELENGKVTVKSRDT 78
|
90
....*....|....*
gi 489193038 551 SESQNLPIGELMSFI 565
Cdd:cd00738 79 GESETLHVDELPEFL 93
|
|
| ThrRS_core |
cd00771 |
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ... |
35-163 |
7.89e-11 |
|
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is responsible for the attachment of threonine to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain.
Pssm-ID: 238394 [Multi-domain] Cd Length: 298 Bit Score: 63.34 E-value: 7.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193038 35 LASGLYTWLPMGLRVLRKVETIVREEMNAAGALEVLMPAVQPAELWQESGRWEQYGPELLRLkDRHEREFCVGPT----H 110
Cdd:cd00771 18 AGPGLPFWLPKGAIIRNELEDFLRELQRKRGYQEVETPIIYNKELWETSGHWDHYRENMFPF-EEEDEEYGLKPMncpgH 96
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 489193038 111 EEVItdlaRNELNSYKQLPINFYQIQTKFRDEIRPRF-GLMRGREFIMKDAYSF 163
Cdd:cd00771 97 CLIF----KSKPRSYRDLPLRLAEFGTVHRYEQSGALhGLTRVRGFTQDDAHIF 146
|
|
| PRK12444 |
PRK12444 |
threonyl-tRNA synthetase; Reviewed |
31-192 |
1.38e-08 |
|
threonyl-tRNA synthetase; Reviewed
Pssm-ID: 183530 [Multi-domain] Cd Length: 639 Bit Score: 57.45 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193038 31 MIRRLASGLYTWLPMGLRVLRKVETIVREEMNAAGALEVLMPAVQPAELWQESGRWEQYgPELLRLKDRHEREFCVGPTH 110
Cdd:PRK12444 258 MFSEEAPGMPFYLPKGQIIRNELEAFLREIQKEYNYQEVRTPFMMNQELWERSGHWDHY-KDNMYFSEVDNKSFALKPMN 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193038 111 EEVITDLARNELNSYKQLPINFYQIQTKFRDEIRPRF-GLMRGREFIMKDAYSFhLSQDSLQQTYDGMYQAYSKIFSRLG 189
Cdd:PRK12444 337 CPGHMLMFKNKLHSYRELPIRMCEFGQVHRHEFSGALnGLLRVRTFCQDDAHLF-VTPDQIEDEIKSVMAQIDYVYKTFG 415
|
...
gi 489193038 190 LDF 192
Cdd:PRK12444 416 FEY 418
|
|
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
36-163 |
1.70e-06 |
|
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440210 [Multi-domain] Cd Length: 639 Bit Score: 50.80 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193038 36 ASGLYTWLPMGLRVLRKVETIVREEMNAAGALEVLMPAVQPAELWQESGRWEQYGPELLRLKDrHEREFCVG----PTHE 111
Cdd:COG0441 260 GPGLPFWHPKGAIIRRELEDYIREKHRKAGYQEVKTPHILDRELWETSGHWDHYRENMFPTES-DGEEYALKpmncPGHI 338
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 489193038 112 EVItdlaRNELNSYKQLPINFYQIQTKFRDEirPR---FGLMRGREFIMKDAYSF 163
Cdd:COG0441 339 LIY----KSGLRSYRDLPLRLAEFGTVHRYE--PSgalHGLMRVRGFTQDDAHIF 387
|
|
| PRK03991 |
PRK03991 |
threonyl-tRNA synthetase; Validated |
430-570 |
1.40e-05 |
|
threonyl-tRNA synthetase; Validated
Pssm-ID: 235190 [Multi-domain] Cd Length: 613 Bit Score: 47.94 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193038 430 EQGKPVN-LIMGCYGIG-VSRVVAA-----AIEQNHDERGILwPSALAPFQIALVPLkyeTESVKQATDKLYAELTAAGF 502
Cdd:PRK03991 452 ENGEEKYpIILHCSPTGsIERVIYAllekaAKEEEEGKVPML-PTWLSPTQVRVIPV---SERHLDYAEEVADKLEAAGI 527
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489193038 503 EVLLDDRDKktSPGVKFADMELIGIPHRIVISDRGLSEGVLEYKGRRDSESQNLPIGELMSFITEKLS 570
Cdd:PRK03991 528 RVDVDDRDE--SLGKKIRDAGKEWIPYVVVIGDKEMESGKLTVTIREESEKVEMTLEELIERIKEETK 593
|
|
| GlyRS_anticodon |
cd00858 |
GlyRS Glycyl-anticodon binding domain. GlyRS belongs to class II aminoacyl-tRNA synthetases ... |
454-569 |
2.02e-05 |
|
GlyRS Glycyl-anticodon binding domain. GlyRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only.
Pssm-ID: 238435 [Multi-domain] Cd Length: 121 Bit Score: 44.09 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193038 454 IEQNHDERGIL-WPSALAPFQIALVPLKYETESVKQAtDKLYAELTAAGFEVLLDDRdkkTSPGVKFADMELIGIPHRIV 532
Cdd:cd00858 8 VREGDEGRIVLrLPPALAPIKVAVLPLVKRDELVEIA-KEISEELRELGFSVKYDDS---GSIGRRYARQDEIGTPFCVT 83
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 489193038 533 ISDRGLSEG---VLEykgrRDSESQ-NLPIGELMSFITEKL 569
Cdd:cd00858 84 VDFDTLEDGtvtIRE----RDSMRQvRVKIEELPSYLRELI 120
|
|
| EbsC |
COG2606 |
Cys-tRNA(Pro) deacylase, prolyl-tRNA editing enzyme YbaK/EbsC [Translation, ribosomal ... |
260-360 |
2.72e-05 |
|
Cys-tRNA(Pro) deacylase, prolyl-tRNA editing enzyme YbaK/EbsC [Translation, ribosomal structure and biogenesis];
Pssm-ID: 442018 [Multi-domain] Cd Length: 152 Bit Score: 44.31 E-value: 2.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193038 260 TKTIAALVDGFQLPIEKTIKTLVVHGaeEGTLVALIVRGDHELNEIKAANQpLVASPLVFASEAEIRAAIGAGPGSLGPV 339
Cdd:COG2606 23 AATAEEAAEALGVPPEQIAKTLVFRG--DGGPVLAVVPGDRRLDLKKLAAA-LGAKKVEMADPEEVERLTGYEVGGVSPF 99
|
90 100
....*....|....*....|....*
gi 489193038 340 NLP--IACIVDRSVALMSD--FAAG 360
Cdd:COG2606 100 GLKkgLPVYVDESLLEFDEvyVSAG 124
|
|
| PLN02908 |
PLN02908 |
threonyl-tRNA synthetase |
35-163 |
2.72e-05 |
|
threonyl-tRNA synthetase
Pssm-ID: 178496 [Multi-domain] Cd Length: 686 Bit Score: 47.07 E-value: 2.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193038 35 LASGLYTWLPMGLRVLRKVETIVREEMNAAGALEVLMPAVQPAELWQESGRWEQYgPELLRLKDRHEREFCVGPTHEEVI 114
Cdd:PLN02908 309 LSPGSCFFLPHGARIYNKLMDFIREQYWERGYDEVITPNIYNMDLWETSGHAAHY-KENMFVFEIEKQEFGLKPMNCPGH 387
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 489193038 115 TDLARNELNSYKQLPINFYQIQTKFRDEIRPRF-GLMRGREFIMKDAYSF 163
Cdd:PLN02908 388 CLMFAHRVRSYRELPLRLADFGVLHRNELSGALtGLTRVRRFQQDDAHIF 437
|
|
| PLN02837 |
PLN02837 |
threonine-tRNA ligase |
38-209 |
3.41e-05 |
|
threonine-tRNA ligase
Pssm-ID: 215450 [Multi-domain] Cd Length: 614 Bit Score: 46.81 E-value: 3.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193038 38 GLYTWLPMGlRVLRKVETIVREEMNAAGALEVL-MPAVQPAELWQESGRWEQYGPELLRLKDRHEREFCVGPTHEEVITD 116
Cdd:PLN02837 238 GLVFWHPKG-AIVRHIIEDSWKKMHFEHGYDLLyTPHVAKADLWKTSGHLDFYKENMYDQMDIEDELYQLRPMNCPYHIL 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193038 117 LARNELNSYKQLPINFYQIQTKFRDEIRPRF-GLMRGREFIMKDAYSFHLsQDSLQQTYDGMYQAYSKIFSRLGLDFRPV 195
Cdd:PLN02837 317 VYKRKLHSYRDLPIRVAELGTVYRYELSGSLhGLFRVRGFTQDDAHIFCL-EDQIKDEIRGVLDLTEEILKQFGFSKYEI 395
|
170
....*....|....
gi 489193038 196 QADNGSIGGSGSHE 209
Cdd:PLN02837 396 NLSTRPEKSVGSDD 409
|
|
| Pol_gamma_b_Cterm |
cd02426 |
C-terminal domain of mitochondrial DNA polymerase gamma B subunit, which is required for ... |
452-566 |
3.84e-04 |
|
C-terminal domain of mitochondrial DNA polymerase gamma B subunit, which is required for processivity. Polymerase gamma replicates and repairs mitochondrial DNA. The c-terminal domain of its B subunit is strikingly similar to the anticodon-binding domain of glycyl tRNA synthetase.
Pssm-ID: 239106 [Multi-domain] Cd Length: 128 Bit Score: 40.48 E-value: 3.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193038 452 AAIEQNHDERGILWPSALAPFQIALVPLKYETESVKQATDKLYAELTAAGFEVllddrdkktSPGVKFA----------- 520
Cdd:cd02426 8 DGRKKGRQRQVLKLHPCLAPYKVAIDCGKGDTAELRDLCQGLKNELREAGLSV---------WPGYLETqhssleqlldk 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 489193038 521 -DMelIGIPHRIVISDRGLSEGVLEYKGRRDSESQNLPIGELMSFIT 566
Cdd:cd02426 79 yDE--MGVLFTLLISEQTLENGLLQLRSRDTTLKETIHISDLPDYLL 123
|
|
| PRK12444 |
PRK12444 |
threonyl-tRNA synthetase; Reviewed |
403-569 |
5.22e-04 |
|
threonyl-tRNA synthetase; Reviewed
Pssm-ID: 183530 [Multi-domain] Cd Length: 639 Bit Score: 42.81 E-value: 5.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193038 403 IKRGIEVGHIfQLGTKYSEAMKLSVLSEQG---KPVNLIMGCYGiGVSRVVAAAIEQnhdeRGILWPSALAPFQIALVPL 479
Cdd:PRK12444 476 LNRSHQCGTI-QLDFQMPEKFDLNYIDEKNekrRPVVIHRAVLG-SLDRFLAILIEH----FGGAFPAWLAPVQVKVIPV 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193038 480 KYETEsvKQATDKLYAELTAAGFEVLLDDRDKKTspGVKFADMELIGIPHRIVISDRGLSEGVLEYKGRRDSESQNLPIG 559
Cdd:PRK12444 550 SNAVH--VQYADEVADKLAQAGIRVERDERDEKL--GYKIREAQMQKIPYVLVIGDKEMENGAVNVRKYGEEKSEVIELD 625
|
170
....*....|
gi 489193038 560 ELMSFITEKL 569
Cdd:PRK12444 626 MFVESIKEEI 635
|
|
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
42-155 |
3.06e-03 |
|
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439894 [Multi-domain] Cd Length: 422 Bit Score: 40.11 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193038 42 WLPMGLRVLRKVETIVREEMNAAGALEVLMPAVQPAELWQESgrweqYGP-----ELLRLKDRHEREFC------VGpth 110
Cdd:COG0124 13 ILPEESAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARK-----IGEdivekEMYTFEDRGGRSLTlrpegtAP--- 84
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 489193038 111 eevitdLAR--NELNSYKQLPINFYQIQTKFRDEiRPRFGlmRGREF 155
Cdd:COG0124 85 ------VARavAEHGNELPFPFKLYYIGPVFRYE-RPQKG--RYRQF 122
|
|
| ProX_deacylase |
cd04333 |
This CD, composed mainly of bacterial single-domain proteins, includes the Thermus ... |
279-350 |
3.24e-03 |
|
This CD, composed mainly of bacterial single-domain proteins, includes the Thermus thermophilus (Tt) YbaK-like protein, a homolog of the trans-acting Escherichia coli YbaK Cys-tRNA(Pro) deacylase and the Agrobacterium tumefaciens ProX Ala-tRNA(Pro) deacylase and also the cis-acting prolyl-tRNA synthetase-editing domain (ProRS-INS). While ProX and ProRS-INS hydrolyze misacylated Ala-tRNA(Pro), the E. coli YbaK hydrolyzes misacylated Cys-tRNA(Pro). A few CD members are N-terminal, YbaK-ProX-like domains of an uncharacterized protein with a C-terminal, predicted Fe-S protein domain.
Pssm-ID: 239825 [Multi-domain] Cd Length: 148 Bit Score: 38.25 E-value: 3.24e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489193038 279 KTLVVHGAEEgtLVALIVRGDHELNEIKAANqpLVASPLVFASEAEIRAAIGAGPGSLGPVNL--PIACIVDRS 350
Cdd:cd04333 43 KSLVFRVDDE--PVLVVTSGDARVDNKKFKA--LFGEKLKMADAEEVRELTGFAIGGVCPFGHpePLPVYLDES 112
|
|
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
126-157 |
3.99e-03 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 40.11 E-value: 3.99e-03
10 20 30
....*....|....*....|....*....|..
gi 489193038 126 KQLPINFYQIQTKFRDEIRPRFGLMRGREFIM 157
Cdd:PLN02734 272 GKLPFAAAQIGQAFRNEISPRQGLLRVREFTL 303
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