|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09194 |
PRK09194 |
prolyl-tRNA synthetase; Provisional |
1-573 |
0e+00 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 236405 [Multi-domain] Cd Length: 565 Bit Score: 1104.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754627186 1 MRTSQYLLSTLKETPSDAEVVSHQLMLRAGMIRKLASGMYAWLPTGLRVLKKIENIVREEMNNAGAVEVSMPVVQPAELW 80
Cdd:PRK09194 1 MRTSQLFLPTLKETPADAEVISHQLLLRAGYIRKLASGIYTYLPLGLRVLRKIENIVREEMNKIGAQEVLMPALQPAELW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754627186 81 QESGRWDDYGPELCRLTDRHNRPFVLGPTHEEVITALVRYEVNSYKQLPLNLYQIQTKFRDEVRPRFGVMRGREFLMKDA 160
Cdd:PRK09194 81 QESGRWEEYGPELLRLKDRHGRDFVLGPTHEEVITDLVRNEIKSYKQLPLNLYQIQTKFRDEIRPRFGLMRGREFIMKDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754627186 161 YSFHIDKASLVDTYEKMHAAYCTAFTRMGLNFRPVQADTGSIGGTGSHEFQVLAESGEDLIAFSDTSDYAANIEMAEALA 240
Cdd:PRK09194 161 YSFHADEESLDETYDAMYQAYSRIFDRLGLDFRAVEADSGAIGGSASHEFMVLADSGEDTIVYSDESDYAANIEKAEALP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754627186 241 PagERAAATKALTKVATPAVHTIDEVAAFLNVAPTAIAKTLLVLAEEdehgkqAVIALVLRGDHELNEIKAEKLSGVAnP 320
Cdd:PRK09194 241 P--PRAAAEEALEKVDTPNAKTIEELAEFLNVPAEKTVKTLLVKADG------ELVAVLVRGDHELNEVKLENLLGAA-P 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754627186 321 LTFANDEQIKAAAGCDAGSIGPVGFAG--RIIVDRSAAHLSDFVCGANETGFHLTGANWDRDITSFEVADLRNVVEGDPS 398
Cdd:PRK09194 312 LELATEEEIRAALGAVPGFLGPVGLPKdvPIIADRSVADMSNFVVGANEDDYHYVGVNWGRDFPVPEVADLRNVVEGDPS 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754627186 399 PCGQGKLLLKRGIEVGHIFQLGTKYSEAMKASVLNEGGKSVTMEMGCYGIGVSRLVAAAIEQNNDQYGIIWPDAIAPFEV 478
Cdd:PRK09194 392 PDGGGTLKIARGIEVGHIFQLGTKYSEAMNATVLDENGKAQPLIMGCYGIGVSRLVAAAIEQNHDEKGIIWPKAIAPFDV 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754627186 479 AIVPMNMhKSERVALQAQQFYAELKAAGVDVLFDDRKERPGVMFADMELIGVPHAIVIGDRGLDNGVVEYKCRRSGEKQE 558
Cdd:PRK09194 472 HIVPVNM-KDEEVKELAEKLYAELQAAGIEVLLDDRKERPGVKFADADLIGIPHRIVVGDRGLAEGIVEYKDRRTGEKEE 550
|
570
....*....|....*
gi 754627186 559 VAIGEIVAMLKAKLG 573
Cdd:PRK09194 551 VPVDELVEFLKALKK 565
|
|
| ProS |
COG0442 |
Prolyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Prolyl-tRNA ... |
1-572 |
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: 1042.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754627186 1 MRTSQYLLSTLKETPSDAEVVSHQLMLRAGMIRKLASGMYAWLPTGLRVLKKIENIVREEMNNAGAVEVSMPVVQPAELW 80
Cdd:COG0442 1 MRASKLFIPTLKERPADAEVWSHQLMLRAGLIRKLASGIYTYLPLGYRVLEKIEAIVREEMKRTGAQEVLMPLLQPAELW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754627186 81 QESGRWDDYGPELCRLTDRHNRPFVLGPTHEEVITALVRYEVNSYKQLPLNLYQIQTKFRDEVRPRFGVMRGREFLMKDA 160
Cdd:COG0442 81 EESGRWEGFGPELARVTDRLEREFCLGPTHEEVITDLVRNEIKSYRDLPLLLYQIQTKFRDEIRPRFGLLRTREFLMKDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754627186 161 YSFHIDKASLVDTYEKMHAAYCTAFTRMGLNFRPVQADTGSIGGTGSHEFQVLAESGEDLIAFSDTSDYAANIEMAEALA 240
Cdd:COG0442 161 YSFHATEEELDEEYQKMLDAYERIFERLGLPVRAVEADSGAIGGSESHEFMVLADSGEDTIVYCDACDYAANIEKAEALA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754627186 241 PAGERAAATKALTKVATPAVHTIDEVAAFLNVAPTAIAKTLLVLAEEDehgkqaVIALVLRGDHELNEIKAEKLSGvANP 320
Cdd:COG0442 241 PPAERAEPTKELEAVATPGAKTIEEVAEFLGVPAEKTVKTLVYKADGE------LVAVLVRGDHELNEIKLENLLG-ASE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754627186 321 LTFANDEQIKAAAGCDAGSIGPVGFAGRIIVDRSAAHLSDFVCGANETGFHLTGANWDRDITSFEVADLRNVVEGDPSPC 400
Cdd:COG0442 314 LELATEEEIEAALGAVPGFLGPVGLGVPYIADRSVAGMSNFVCGANEDDYHYTNVNWGRDFPVDEVADLRNVVEGDPCPD 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754627186 401 GQGKLLLKRGIEVGHIFQLGTKYSEAMKASVLNEGGKSVTMEMGCYGIGVSRLVAAAIEQNNDQYGIIWPDAIAPFEVAI 480
Cdd:COG0442 394 CGGLLQDGRGIEVGHIFKLGTKYSKAMDATFLDENGKEQPVWMGCYGIGVTRLIAAAIEQHHDDKGIIWPPAIAPFQVVI 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754627186 481 VPMNMhKSERVALQAQQFYAELKAAGVDVLFDDRKERPGVMFADMELIGVPHAIVIGDRGLDNGVVEYKCRRSGEKQEVA 560
Cdd:COG0442 474 VPINM-KDEAVLEAAEELYAELKAAGIDVLLDDRDERPGVKFADAELIGIPLRIVIGPRDLEEGQVEVKRRDTGEKEEVP 552
|
570
....*....|..
gi 754627186 561 IGEIVAMLKAKL 572
Cdd:COG0442 553 LDELVETVKELL 564
|
|
| proS_fam_II |
TIGR00409 |
prolyl-tRNA synthetase, family II; Prolyl-tRNA synthetase is a class II tRNA synthetase and is ... |
1-571 |
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: 862.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754627186 1 MRTSQYLLSTLKETPSDAEVVSHQLMLRAGMIRKLASGMYAWLPTGLRVLKKIENIVREEMNNAGAVEVSMPVVQPAELW 80
Cdd:TIGR00409 1 MRTSQYLFPTLKETPADAEVKSHQLLLRAGFIRRLGSGLYNWLPLGLRVLKKVENIVREEMNKDGAIEVLLPALQPAELW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754627186 81 QESGRWDDYGPELCRLTDRHNRPFVLGPTHEEVITALVRYEVNSYKQLPLNLYQIQTKFRDEVRPRFGVMRGREFLMKDA 160
Cdd:TIGR00409 81 QESGRWDTYGPELLRLKDRKGREFVLGPTHEEVITDLARNEIKSYKQLPLNLYQIQTKFRDEIRPRFGLMRGREFIMKDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754627186 161 YSFHIDKASLVDTYEKMHAAYCTAFTRMGLNFRPVQADTGSIGGTGSHEFQVLAESGEDLIAFSDTSDYAANIEMAEALA 240
Cdd:TIGR00409 161 YSFHSDEESLDATYQKMYQAYSNIFSRLGLDFRPVQADSGAIGGSASHEFMVLAESGEDTIVYSDESDYAANIELAEALA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754627186 241 PaGERAAATKALTKVATPAVHTIDEVAAFLNVAPTAIAKTLLVLAeedEHGKQAVIALVLRGDHELNEIKAEKLSGVANP 320
Cdd:TIGR00409 241 P-GERNAPTAELDKVDTPNTKTIAELVECFNLPAEKVVKTLLVKA---VDKSEPLVALLVRGDHELNEVKAPNLLLVAQV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754627186 321 LTFANDEQIKAAAGCDAGSIGPVGFAGRI--IVDRSAAHLSDFVCGANETGFHLTGANWDRDITSFEVADLRNVVEGDPS 398
Cdd:TIGR00409 317 LELATEEEIFQKIASGPGSLGPVNINGGIpvLIDQTVALMSDFAAGANADDKHYFNVNWDRDVAIPEVADIRKVKEGDPS 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754627186 399 PCGQGKLLLKRGIEVGHIFQLGTKYSEAMKASVLNEGGKSVTMEMGCYGIGVSRLVAAAIEQNNDQYGIIWPDAIAPFEV 478
Cdd:TIGR00409 397 PDGQGTLKIARGIEVGHIFQLGTKYSEALKATFLDENGKNQFMTMGCYGIGVSRLVSAIAEQHHDERGIIWPKAIAPYDV 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754627186 479 AIVPMNMHKsERVALQAQQFYAELKAAGVDVLFDDRKERPGVMFADMELIGVPHAIVIGDRGLDNGVVEYKCRRSGEKQE 558
Cdd:TIGR00409 477 VIVVMNMKD-EEQQQLAEELYSELLAQGVDVLLDDRNERAGVKFADSELIGIPLRVVVGKKNLDNGEIEVKKRRNGEKQL 555
|
570
....*....|...
gi 754627186 559 VAIGEIVAMLKAK 571
Cdd:TIGR00409 556 IKKDELVECLEEQ 568
|
|
| PRK12325 |
PRK12325 |
prolyl-tRNA synthetase; Provisional |
1-570 |
0e+00 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 237059 [Multi-domain] Cd Length: 439 Bit Score: 639.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754627186 1 MRTSQYLLSTLKETPSDAEVVSHQLMLRAGMIRKLASGMYAWLPTGLRVLKKIENIVREEMNNAGAVEVSMPVVQPAELW 80
Cdd:PRK12325 1 MRLSRYFLPTLKENPKEAEIVSHRLMLRAGMIRQQAAGIYSWLPLGLKVLKKIENIVREEQNRAGAIEILMPTIQPADLW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754627186 81 QESGRWDDYGPELCRLTDRHNRPFVLGPTHEEVITALVRYEVNSYKQLPLNLYQIQTKFRDEVRPRFGVMRGREFLMKDA 160
Cdd:PRK12325 81 RESGRYDAYGKEMLRIKDRHDREMLYGPTNEEMITDIFRSYVKSYKDLPLNLYHIQWKFRDEIRPRFGVMRGREFLMKDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754627186 161 YSFHIDKASLVDTYEKMHAAYCTAFTRMGLNFRPVQADTGSIGGTGSHEFQVLAESGEDLIaFSDtsdyaaniemaeala 240
Cdd:PRK12325 161 YSFDLDEEGARHSYNRMFVAYLRTFARLGLKAIPMRADTGPIGGDLSHEFIILAETGESTV-FYD--------------- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754627186 241 pageraaatkaltkvatpavhtidevaaflnvaptaiaKTLLVLAEEDEHgkqavialvlrgdhelneikaeklsgvanp 320
Cdd:PRK12325 225 --------------------------------------KDFLDLLVPGED------------------------------ 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754627186 321 ltfandeqikaaagcdagsigpvgfagriiVDRSAAHLSDFVcganetgfhltganwdRDITSFEVA--DLRNVVEGDPS 398
Cdd:PRK12325 237 ------------------------------IDFDVADLQPIV----------------DEWTSLYAAteEMHDEAAFAAV 270
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754627186 399 PcgQGKLLLKRGIEVGHIFQLGTKYSEAMKASVLNEGGKSVTMEMGCYGIGVSRLVAAAIEQNNDQYGIIWPDAIAPFEV 478
Cdd:PRK12325 271 P--EERRLSARGIEVGHIFYFGTKYSEPMNAKVQGPDGKEVPVHMGSYGIGVSRLVAAIIEASHDDKGIIWPESVAPFKV 348
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754627186 479 AIVPMNMHKSERVALqAQQFYAELKAAGVDVLFDDRKERPGVMFADMELIGVPHAIVIGDRGLDNGVVEYKCRRSGEKQE 558
Cdd:PRK12325 349 GIINLKQGDEACDAA-CEKLYAALSAAGIDVLYDDTDERPGAKFATMDLIGLPWQIIVGPKGLAEGKVELKDRKTGEREE 427
|
570
....*....|..
gi 754627186 559 VAIGEIVAMLKA 570
Cdd:PRK12325 428 LSVEAAINRLTA 439
|
|
| ProRS_core_prok |
cd00779 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
17-460 |
9.74e-150 |
|
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: 430.46 E-value: 9.74e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754627186 17 DAEVVSHQLMLRAGMIRKLASGMYAWLPTGLRVLKKIENIVREEMNNAGAVEVSMPVVQPAELWQESGRWDDYGPELCRL 96
Cdd:cd00779 1 DAEIISHKLLLRAGFIRQTSSGLYSWLPLGLRVLKKIENIIREEMNKIGAQEILMPILQPAELWKESGRWDAYGPELLRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754627186 97 TDRHNRPFVLGPTHEEVITALVRYEVNSYKQLPLNLYQIQTKFRDEVRPRFGVMRGREFLMKDAYSFHIDKASLVDTYEK 176
Cdd:cd00779 81 KDRHGKEFLLGPTHEEVITDLVANEIKSYKQLPLNLYQIQTKFRDEIRPRFGLMRGREFLMKDAYSFDIDEESLEETYEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754627186 177 MHAAYCTAFTRMGLNFRPVQADTGSIGGTGSHEFQVLAesgedliafsdtsdyaaniemaealapageraaatkaltkva 256
Cdd:cd00779 161 MYQAYSRIFKRLGLPFVKVEADSGAIGGSLSHEFHVLS------------------------------------------ 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754627186 257 tpavhtidevaaflnvaptaiaktllvlaeedehgkqavialvlrgdhelneikaeklsgvanPLTFandeqikaaagcd 336
Cdd:cd00779 199 ---------------------------------------------------------------PLKI------------- 202
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754627186 337 agsigpvgfagriivdrsaahlsdfvcganetgfhltganwdrditsfevadlrnvvegdpspcgqgklllKRGIEVGHI 416
Cdd:cd00779 203 -----------------------------------------------------------------------TKGIEVGHI 211
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 754627186 417 FQLGTKYSEAMKASVLNEGGKSVTMEMGCYGIGVSRLVAAAIEQ 460
Cdd:cd00779 212 FQLGTKYSKALGATFLDENGKPKPLEMGCYGIGVSRLLAAIIEQ 255
|
|
| ProRS-INS |
cd04334 |
INS is an amino acid-editing domain inserted (INS) into the bacterial class II prolyl-tRNA ... |
226-389 |
1.81e-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: 241.65 E-value: 1.81e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754627186 226 TSDYAANIEMAEALAPAGERAAATKALTKVATPAVHTIDEVAAFLNVAPTAIAKTLLVLAEEDEHgkqaVIALVLRGDHE 305
Cdd:cd04334 1 DCDYAANIEKAESLPPAAERPAPPKELEKVATPGQKTIEELAEFLGVPPSQTVKTLLVKADGEEE----LVAVLLRGDHE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754627186 306 LNEIKAEKLSGVAnPLTFANDEQIKAAAGCDAGSIGPVGFAG-RIIVDRSAAHLSDFVCGANETGFHLTGANWDRDITSF 384
Cdd:cd04334 77 LNEVKLENLLGAA-PLELASEEEIEAATGAPPGFIGPVGLKKiPIIADRSVADLKNFVCGANEDDYHYVNVNWGRDFPLP 155
|
....*
gi 754627186 385 EVADL 389
Cdd:cd04334 156 EVADL 160
|
|
| ProRS_core |
cd00772 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
17-220 |
1.45e-43 |
|
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: 156.37 E-value: 1.45e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754627186 17 DAEVVSHQLMLRAGMIRKL-ASGMYAWLPTGLRVLKKIENIVREEMNNAGAVEVSMPVVQPAELWQESGRWDDYG-PELC 94
Cdd:cd00772 1 DASEKSLEHIGKAELADQGpGRGIINFLPLAKAILDKIENVLDKMFKEHGAQNALFPFFILASFLEKEAEHDEGFsKELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754627186 95 RLTDRHNR----PFVLGPTHEEVITALVRYEVNSYKQLPLNLYQIQTKFRDEVRPRFGVMRGREFLMKDAYSFHIDKASL 170
Cdd:cd00772 81 VFKDAGDEeleeDFALRPTLEENIGEIAAKFIKSWKDLPQHLNQIGNKFRDEIRPRFGFLRAREFIMKDGHSAHADAEEA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 754627186 171 VDTYEKMHAAYCTAFTRMG-LNFRPVQADTGS--IGGTGSHEFQVLAESGEDL 220
Cdd:cd00772 161 DEEFLNMLSAYAEIARDLAaIDFIEGEADEGAkfAGASKSREFEALMEDGKAK 213
|
|
| ProRS_anticodon_short |
cd00861 |
ProRS Prolyl-anticodon binding domain, short version found predominantly in bacteria. ProRS ... |
475-569 |
4.13e-42 |
|
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: 146.20 E-value: 4.13e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754627186 475 PFEVAIVPMNMHKSERVALqAQQFYAELKAAGVDVLFDDRKERPGVMFADMELIGVPHAIVIGDRGLDNGVVEYKCRRSG 554
Cdd:cd00861 1 PFDVVIIPMNMKDEVQQEL-AEKLYAELQAAGVDVLLDDRNERPGVKFADADLIGIPYRIVVGKKSAAEGIVEIKVRKTG 79
|
90
....*....|....*
gi 754627186 555 EKQEVAIGEIVAMLK 569
Cdd:cd00861 80 EKEEISIDELLEFLQ 94
|
|
| YbaK_like |
cd04332 |
YbaK-like. The YbaK family of deacylase domains includes the INS amino acid-editing domain of ... |
250-387 |
1.58e-38 |
|
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: 138.06 E-value: 1.58e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754627186 250 KALTKVATPAVHTIDEVAAFLNVAPTAIAKTLLVLAEEDEHgkqavIALVLRGDHELNEIKAEKLSGvANPLTFANDEQI 329
Cdd:cd04332 1 EYLEYEHTPGAKTIEEAAEALGVPPGQIAKTLVLKDDKGGL-----VLVVVPGDHELDLKKLAKALG-AKKLRLASEEEL 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 754627186 330 KAAAGCDAGSIGPVGFAG--RIIVDRSAAHLSDFVCGANETG--FHLTGANWDRDITSFEVA 387
Cdd:cd04332 75 EELTGCEPGGVGPFGLKKgvPVVVDESLLELEDVYVGAGERGadLHLSPADLLRLLGEAEVA 136
|
|
| tRNA_edit |
pfam04073 |
Aminoacyl-tRNA editing domain; This domain is found either on its own or in association with ... |
257-378 |
2.55e-28 |
|
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: 109.23 E-value: 2.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754627186 257 TPAVHTIDEVAAFLNVAPTAIAKTLLVLAEEDEHgkqavIALVLRGDHELNEIKAEKLSGVANpLTFANDEQIKAAAGCD 336
Cdd:pfam04073 1 HPPAATIEELAAALGVPPGRIAKTLVLKDKKGKY-----VLVVVPGDREVDLKKLAKLLGVKR-LRLASEEELLELTGVE 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 754627186 337 AGSIGPVGFAG---RIIVDRSAAHLSDFVCGANETGFHLTGANWD 378
Cdd:pfam04073 75 PGGVTPFGLKAkgvPVLVDESLKDLPDVVVGAGENGATLRLSNAD 119
|
|
| 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 ... |
49-203 |
1.61e-27 |
|
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: 110.94 E-value: 1.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754627186 49 VLKKIENIVREEMNNAGAVEVSMPVVQPAELWQESGRWDDYGPELCRLTDR----HNRPFVLGPTHEEVITALVRYEVNS 124
Cdd:cd00670 4 LWRALERFLDDRMAEYGYQEILFPFLAPTVLFFKGGHLDGYRKEMYTFEDKgrelRDTDLVLRPAACEPIYQIFSGEILS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754627186 125 YKQLPLNLYQIQTKFRDEVRPRFGVMRGREFLMKDAYSFHIDKAS------LVDTYEKMHAAyctaftrMGLNFRPVQAD 198
Cdd:cd00670 84 YRALPLRLDQIGPCFRHEPSGRRGLMRVREFRQVEYVVFGEPEEAeeerreWLELAEEIARE-------LGLPVRVVVAD 156
|
....*
gi 754627186 199 TGSIG 203
Cdd:cd00670 157 DPFFG 161
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
477-571 |
3.77e-23 |
|
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: 93.80 E-value: 3.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754627186 477 EVAIVPMNMHKSERVALqAQQFYAELKAAGVDVLFDDRKERPGVMFADMELIGVPHAIVIGDRGLDNGVVEYKCRRSGEK 556
Cdd:pfam03129 1 QVVVIPLGEKAEELEEY-AQKLAEELRAAGIRVELDDRNESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQ 79
|
90
....*....|....*
gi 754627186 557 QEVAIGEIVAMLKAK 571
Cdd:pfam03129 80 ETVSLDELVEKLKEL 94
|
|
| HGTP_anticodon |
cd00738 |
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ... |
475-569 |
6.76e-19 |
|
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: 81.68 E-value: 6.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754627186 475 PFEVAIVPMNMHKSERVALqAQQFYAELKAAGVDVLFDDRKERPGVMFADMELIGVPHAIVIGDRGLDNGVVEYKCRRSG 554
Cdd:cd00738 1 PIDVAIVPLTDPRVEAREY-AQKLLNALLANGIRVLYDDRERKIGKKFREADLRGVPFAVVVGEDELENGKVTVKSRDTG 79
|
90
....*....|....*
gi 754627186 555 EKQEVAIGEIVAMLK 569
Cdd:cd00738 80 ESETLHVDELPEFLV 94
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
49-203 |
1.68e-17 |
|
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: 81.40 E-value: 1.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754627186 49 VLKKIENIVREEMNNAGAVEVSMPVVQPAELWQESGRWddyGPELCRLTDRHNRPFVLGPTHEEVItalVRYEVNSYKQL 128
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGHE---PKDLLPVGAENEEDLYLRPTLEPGL---VRLFVSHIRKL 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 754627186 129 PLNLYQIQTKFRDEvRPRFGVMRGREFLMKDAYSFHIDkASLVDTYEKMHAAYCTAFTRMG--LNFRPVQADTGSIG 203
Cdd:cd00768 75 PLRLAEIGPAFRNE-GGRRGLRRVREFTQLEGEVFGED-GEEASEFEELIELTEELLRALGikLDIVFVEKTPGEFS 149
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
95-216 |
1.15e-16 |
|
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: 78.22 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754627186 95 RLTDRHNRPFVLGPTHEEVITALVRYEVNSYKQLPLNLYQIQTKFRDEVRPRF-GVMRGREFLMKDAYSFHIdKASLVDT 173
Cdd:pfam00587 2 KVEDENGDELALKPTNEPGHTLLFREEGLRSKDLPLKLAQFGTCFRHEASGDTrGLIRVRQFHQDDAHIFHA-PGQSPDE 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 754627186 174 YEKMHAAYCTAFTRMGLNFRPVQADTGSIGGTG--SHEFQVLAES 216
Cdd:pfam00587 81 LEDYIKLIDRVYSRLGLEVRVVRLSNSDGSAFYgpKLDFEVVFPS 125
|
|
| ProRS_core_arch_euk |
cd00778 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
23-188 |
1.94e-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: 79.56 E-value: 1.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754627186 23 HQLMLRAGMI-RKLASGMYAWLPTGLRVLKKIENIVREEMNNAGAVEVSMPVVQP-AELWQESGRWDDYGPELCRLTdrH 100
Cdd:cd00778 7 TEVITKAELIdYGPVKGCMVFRPYGYAIWENIQKILDKEIKETGHENVYFPLLIPeSELEKEKEHIEGFAPEVAWVT--H 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754627186 101 ------NRPFVLGPTHEEVITALVRYEVNSYKQLPLNLYQIQTKFRDEVRPRFGVMRGREFLMKDAYSFHIDKASLVDTY 174
Cdd:cd00778 85 ggleelEEPLALRPTSETAIYPMFSKWIRSYRDLPLKINQWVNVFRWETKTTRPFLRTREFLWQEGHTAHATEEEAEEEV 164
|
170
....*....|....
gi 754627186 175 EKMHAAYCTAFTRM 188
Cdd:cd00778 165 LQILDLYKEFYEDL 178
|
|
| EbsC |
COG2606 |
Cys-tRNA(Pro) deacylase, prolyl-tRNA editing enzyme YbaK/EbsC [Translation, ribosomal ... |
258-389 |
5.82e-14 |
|
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: 69.35 E-value: 5.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754627186 258 PAVHTIDEVAAFLNVAPTAIAKTLLVlaeedeHGKQAVIALVLRGDHELNEIKAEKLSGvANPLTFANDEQIKAAAGCDA 337
Cdd:COG2606 21 EPAATAEEAAEALGVPPEQIAKTLVF------RGDGGPVLAVVPGDRRLDLKKLAAALG-AKKVEMADPEEVERLTGYEV 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 754627186 338 GSIGPVGFAG--RIIVDRSAAHLSDFVCGANETG--FHLTGANWDRdITSFEVADL 389
Cdd:COG2606 94 GGVSPFGLKKglPVYVDESLLEFDEVYVSAGDRGllVELAPADLAR-LTGATVADI 148
|
|
| ProRS_anticodon_zinc |
cd00862 |
ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and ... |
466-572 |
1.22e-13 |
|
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: 70.02 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754627186 466 GIIWPDAIAPFEVAIVPM--NMHKSERVALQAQQFYAELKAAGVDVLFDDRKE-RPGVMFADMELIGVPHAIVIGDRGLD 542
Cdd:cd00862 1 GLVLPPRVAPIQVVIVPIgiKDEKREEVLEAADELAERLKAAGIRVHVDDRDNyTPGWKFNDWELKGVPLRIEIGPRDLE 80
|
90 100 110
....*....|....*....|....*....|
gi 754627186 543 NGVVEYKCRRSGEKQEVAIGEIVAMLKAKL 572
Cdd:cd00862 81 KNTVVIVRRDTGEKKTVPLAELVEKVPELL 110
|
|
| ThrRS_core |
cd00771 |
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ... |
34-165 |
6.77e-12 |
|
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: 66.42 E-value: 6.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754627186 34 KLASGMYAWLPTGLRVLKKIENIVREEMNNAGAVEVSMPVVQPAELWQESGRWDDYGPELCRlTDRHNRPFVLGPT---- 109
Cdd:cd00771 17 EAGPGLPFWLPKGAIIRNELEDFLRELQRKRGYQEVETPIIYNKELWETSGHWDHYRENMFP-FEEEDEEYGLKPMncpg 95
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 754627186 110 HEEVITALVRyevnSYKQLPLNLYQIQTKFRDEVRPRF-GVMRGREFLMKDAysfHI 165
Cdd:cd00771 96 HCLIFKSKPR----SYRDLPLRLAEFGTVHRYEQSGALhGLTRVRGFTQDDA---HI 145
|
|
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
447-574 |
3.71e-11 |
|
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: 65.14 E-value: 3.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754627186 447 GIGVSRLVAAAIEQNndqygiIWPDAIAPFEVAIVPMnmhkSERVALQAQQFYAELKAAG--VDVLFDDRKERPGVMFAD 524
Cdd:COG0124 305 AIGLERLLLLLEELG------LLPAAEPPPDVYVVPL----GEEARAEALKLAQELRAAGirVELDLGGRKLKKQLKYAD 374
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 754627186 525 MelIGVPHAIVIGDRGLDNGVVEYKCRRSGEKQEVAIGEIVAMLKAKLGR 574
Cdd:COG0124 375 K--SGAPFVLILGEDELANGTVTLKDLATGEQETVPLDELVEYLKELLAE 422
|
|
| PRK12444 |
PRK12444 |
threonyl-tRNA synthetase; Reviewed |
31-163 |
2.81e-09 |
|
threonyl-tRNA synthetase; Reviewed
Pssm-ID: 183530 [Multi-domain] Cd Length: 639 Bit Score: 59.76 E-value: 2.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754627186 31 MIRKLASGMYAWLPTGLRVLKKIENIVREEMNNAGAVEVSMPVVQPAELWQESGRWDDYGPELcRLTDRHNRPFVLGPTH 110
Cdd:PRK12444 258 MFSEEAPGMPFYLPKGQIIRNELEAFLREIQKEYNYQEVRTPFMMNQELWERSGHWDHYKDNM-YFSEVDNKSFALKPMN 336
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 754627186 111 EEVITALVRYEVNSYKQLPLNLYQIQTKFRDEVRPRF-GVMRGREFLMKDAYSF 163
Cdd:PRK12444 337 CPGHMLMFKNKLHSYRELPIRMCEFGQVHRHEFSGALnGLLRVRTFCQDDAHLF 390
|
|
| PRK12444 |
PRK12444 |
threonyl-tRNA synthetase; Reviewed |
407-572 |
3.51e-08 |
|
threonyl-tRNA synthetase; Reviewed
Pssm-ID: 183530 [Multi-domain] Cd Length: 639 Bit Score: 56.29 E-value: 3.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754627186 407 LKRGIEVGHI---FQLGTKYsEAMKASVLNEGGKSVTMEMGCYGiGVSRLVAAAIEQnndqYGIIWPDAIAPFEVAIVPM 483
Cdd:PRK12444 476 LNRSHQCGTIqldFQMPEKF-DLNYIDEKNEKRRPVVIHRAVLG-SLDRFLAILIEH----FGGAFPAWLAPVQVKVIPV 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754627186 484 nmhkSERVALQ-AQQFYAELKAAGVDVLFDDRKERPGVMFADMELIGVPHAIVIGDRGLDNGVVEYKCRRSGEKQEVAIG 562
Cdd:PRK12444 550 ----SNAVHVQyADEVADKLAQAGIRVERDERDEKLGYKIREAQMQKIPYVLVIGDKEMENGAVNVRKYGEEKSEVIELD 625
|
170
....*....|
gi 754627186 563 EIVAMLKAKL 572
Cdd:PRK12444 626 MFVESIKEEI 635
|
|
| PRK03991 |
PRK03991 |
threonyl-tRNA synthetase; Validated |
473-571 |
5.48e-08 |
|
threonyl-tRNA synthetase; Validated
Pssm-ID: 235190 [Multi-domain] Cd Length: 613 Bit Score: 55.65 E-value: 5.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754627186 473 IAPFEVAIVPMnmhkSERVALQAQQFYAELKAAGVDVLFDDRKERPGVMFADMELIGVPHAIVIGDRGLDNGVVEYKCRR 552
Cdd:PRK03991 497 LSPTQVRVIPV----SERHLDYAEEVADKLEAAGIRVDVDDRDESLGKKIRDAGKEWIPYVVVIGDKEMESGKLTVTIRE 572
|
90
....*....|....*....
gi 754627186 553 SGEKQEVAIGEIVAMLKAK 571
Cdd:PRK03991 573 ESEKVEMTLEELIERIKEE 591
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
407-461 |
1.50e-07 |
|
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: 51.64 E-value: 1.50e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 754627186 407 LKRGIEVGHIFQLGTKYSEAMKASVLNEGGKSVTMEMGCYG-IGVSRLVAAAIEQN 461
Cdd:pfam00587 126 LGKQRQTGTIQNDGFRLPRRLGIRYKDEDNESKFPYMIHRAgLGVERFLAAILENN 181
|
|
| ThrRS_anticodon |
cd00860 |
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases ... |
475-569 |
2.82e-07 |
|
ThrRS Threonyl-anticodon binding domain. ThrRS 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: 238437 [Multi-domain] Cd Length: 91 Bit Score: 48.65 E-value: 2.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754627186 475 PFEVAIVPMNmhksERVALQAQQFYAELKAAGVDVLFDDRKERPGVMFADMELIGVPHAIVIGDRGLDNGVVEYKCRRSG 554
Cdd:cd00860 1 PVQVVVIPVT----DEHLDYAKEVAKKLSDAGIRVEVDLRNEKLGKKIREAQLQKIPYILVVGDKEVETGTVSVRTRDGG 76
|
90
....*....|....*
gi 754627186 555 EKQEVAIGEIVAMLK 569
Cdd:cd00860 77 DLGSMSLDEFIEKLK 91
|
|
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
34-165 |
3.75e-07 |
|
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: 53.11 E-value: 3.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754627186 34 KLASGMYAWLPTGLRVLKKIENIVREEMNNAGAVEVSMPVVQPAELWQESGRWDDYGpELCRLTDRHNRPFVLG----PT 109
Cdd:COG0441 258 EVGPGLPFWHPKGAIIRRELEDYIREKHRKAGYQEVKTPHILDRELWETSGHWDHYR-ENMFPTESDGEEYALKpmncPG 336
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 754627186 110 HeevitALV-RYEVNSYKQLPLNLYQIQTKFRDEvrpRFGV----MRGREFLMKDAysfHI 165
Cdd:COG0441 337 H-----ILIyKSGLRSYRDLPLRLAEFGTVHRYE---PSGAlhglMRVRGFTQDDA---HI 386
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
47-155 |
2.74e-06 |
|
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. It is responsible for the attachment of histidine to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs. This domain is also found at the C-terminus of eukaryotic GCN2 protein kinase and at the N-terminus of the ATP phosphoribosyltransferase accessory subunit, HisZ. HisZ along with HisG catalyze the first reaction in histidine biosynthesis. HisZ is found only in a subset of bacteria and differs from HisRS in lacking a C-terminal anti-codon binding domain.
Pssm-ID: 238396 [Multi-domain] Cd Length: 261 Bit Score: 49.14 E-value: 2.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754627186 47 LRVLKKIENIVREEMNNAGAVEVSMPVVQPAELWQeSGRWDDYGPELCRLTDRHNRPFVLGPtheEVITALVRY--EVNS 124
Cdd:cd00773 2 AALRRYIEDTLREVFERYGYEEIDTPVFEYTELFL-RKSGDEVSKEMYRFKDKGGRDLALRP---DLTAPVARAvaENLL 77
|
90 100 110
....*....|....*....|....*....|.
gi 754627186 125 YKQLPLNLYQIQTKFRDEvRPRFGvmRGREF 155
Cdd:cd00773 78 SLPLPLKLYYIGPVFRYE-RPQKG--RYREF 105
|
|
| ProX_deacylase |
cd04333 |
This CD, composed mainly of bacterial single-domain proteins, includes the Thermus ... |
259-354 |
4.41e-06 |
|
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: 46.73 E-value: 4.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754627186 259 AVHTIDEVAAFLNVAPTAIAKTLLVLAEEDehgkqaVIALVLRGDHELNEIKAEKLSGVanPLTFANDEQIKAAAGCDAG 338
Cdd:cd04333 23 STRTAALAAEALGCEPGQIAKSLVFRVDDE------PVLVVTSGDARVDNKKFKALFGE--KLKMADAEEVRELTGFAIG 94
|
90
....*....|....*...
gi 754627186 339 SIGPVGFAG--RIIVDRS 354
Cdd:cd04333 95 GVCPFGHPEplPVYLDES 112
|
|
| PLN02908 |
PLN02908 |
threonyl-tRNA synthetase |
31-163 |
4.97e-05 |
|
threonyl-tRNA synthetase
Pssm-ID: 178496 [Multi-domain] Cd Length: 686 Bit Score: 46.30 E-value: 4.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754627186 31 MIRKLASGMYAWLPTGLRVLKKIENIVREEMNNAGAVEVSMPVVQPAELWQESGRWDDYgPELCRLTDRHNRPFVLGPTH 110
Cdd:PLN02908 305 FFHELSPGSCFFLPHGARIYNKLMDFIREQYWERGYDEVITPNIYNMDLWETSGHAAHY-KENMFVFEIEKQEFGLKPMN 383
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 754627186 111 EEVITALVRYEVNSYKQLPLNLYQIQTKFRDEVRPRF-GVMRGREFLMKDAYSF 163
Cdd:PLN02908 384 CPGHCLMFAHRVRSYRELPLRLADFGVLHRNELSGALtGLTRVRRFQQDDAHIF 437
|
|
| HisRS_anticodon |
cd00859 |
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases ... |
501-569 |
1.30e-04 |
|
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only.
Pssm-ID: 238436 [Multi-domain] Cd Length: 91 Bit Score: 40.99 E-value: 1.30e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 754627186 501 ELKAAGVDVLFDDRKERPGVMFADMELIGVPHAIVIGDRGLDNGVVEYKCRRSGEKQEVAIGEIVAMLK 569
Cdd:cd00859 23 QLRDAGIKAEIDYGGRKLKKQFKYADRSGARFAVILGEDELAAGVVTVKDLETGEQETVALDELVEELK 91
|
|
| YeaK |
cd04336 |
YeaK is an uncharacterized Echerichia coli protein with a YbaK-like domain of unknown function. ... |
258-354 |
1.36e-03 |
|
YeaK is an uncharacterized Echerichia coli protein with a YbaK-like domain of unknown function. The YbaK-like domain family includes the INS amino acid-editing domain of the bacterial class II prolyl tRNA synthetase (ProRS), and it's trans-acting homologs, YbaK, and ProX. 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 a single-domain INS homolog such as YbaK, ProX, or PrdX which supplies the function of INS in trans.
Pssm-ID: 239828 [Multi-domain] Cd Length: 153 Bit Score: 39.64 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754627186 258 PAVHTIDEVAAFLNVAPTAIAKTLLVlaeEDEHGKQAVIALVLRGDHELNEIKAEKLSGvANPLTFANDEQIKAAAGCDA 337
Cdd:cd04336 21 PPEGTSEEVAAIRGTELGQGAKALLC---KVKDGSRRFVLAVLPADKKLDLKAVAAAVG-GKKADLASPEEAEELTGCVI 96
|
90
....*....|....*....
gi 754627186 338 GSIGPVGFAGRI--IVDRS 354
Cdd:cd04336 97 GAVPPFSFDPKLklIADPS 115
|
|
| PRK14938 |
PRK14938 |
Ser-tRNA(Thr) hydrolase; Provisional |
470-569 |
1.70e-03 |
|
Ser-tRNA(Thr) hydrolase; Provisional
Pssm-ID: 184902 [Multi-domain] Cd Length: 387 Bit Score: 40.98 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754627186 470 PDAIAPFEVAIVPMnmhKSERVAlQAQQFYAELKAAGVDVLFDDRKERPG--VMFADMELIgvPHAIVIGDRGLDNGVVE 547
Cdd:PRK14938 269 PDWLNPIQVRILPV---KKDFLD-FSIQVAERLRKEGIRVNVDDLDDSLGnkIRRAGTEWI--PFVIIIGEREVKTSTLT 342
|
90 100
....*....|....*....|..
gi 754627186 548 YKCRRSGEKQEVAIGEIVAMLK 569
Cdd:PRK14938 343 VKIRANNEQKSMTVEELVKEIK 364
|
|
| GlyRS_anticodon |
cd00858 |
GlyRS Glycyl-anticodon binding domain. GlyRS belongs to class II aminoacyl-tRNA synthetases ... |
470-572 |
5.70e-03 |
|
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: 37.15 E-value: 5.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754627186 470 PDAIAPFEVAIVPMnMHKSERVALqAQQFYAELKAAGVDVLFDD------RKERpgvmfADmElIGVPHAIVIGDRGLDN 543
Cdd:cd00858 21 PPALAPIKVAVLPL-VKRDELVEI-AKEISEELRELGFSVKYDDsgsigrRYAR-----QD-E-IGTPFCVTVDFDTLED 91
|
90 100
....*....|....*....|....*....
gi 754627186 544 GVVEYKCRRSGEKQEVAIGEIVAMLKAKL 572
Cdd:cd00858 92 GTVTIRERDSMRQVRVKIEELPSYLRELI 120
|
|
| PLN02837 |
PLN02837 |
threonine-tRNA ligase |
38-163 |
9.25e-03 |
|
threonine-tRNA ligase
Pssm-ID: 215450 [Multi-domain] Cd Length: 614 Bit Score: 38.73 E-value: 9.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754627186 38 GMYAWLPTGLRVLKKIENIVREEMNNAGAVEVSMPVVQPAELWQESGRWDDYGPELCRLTDRHNRPFVLGPTHEEVITAL 117
Cdd:PLN02837 238 GLVFWHPKGAIVRHIIEDSWKKMHFEHGYDLLYTPHVAKADLWKTSGHLDFYKENMYDQMDIEDELYQLRPMNCPYHILV 317
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 754627186 118 VRYEVNSYKQLPLNLYQIQTKFRDEVRPRF-GVMRGREFLMKDAYSF 163
Cdd:PLN02837 318 YKRKLHSYRDLPIRVAELGTVYRYELSGSLhGLFRVRGFTQDDAHIF 364
|
|
| |
