|
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: 1102.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020351452 1 MRVSKYLLSTQKETPANAEVISHQLMLRAGMIRRNASGLYSYLPTGLRVLRKVEAIVREEMNKAGAIEILMPMVQPADLW 80
Cdd:PRK09194 1 MRTSQLFLPTLKETPADAEVISHQLLLRAGYIRKLASGIYTYLPLGLRVLRKIENIVREEMNKIGAQEVLMPALQPAELW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020351452 81 VETGRWDKFGPELLRFKDRHNRDFVLGPTHEEVITDLIRKEVSSYKQLPLNLYQIQTKFRDEVRPRFGVMRSREFLMKDA 160
Cdd:PRK09194 81 QESGRWEEYGPELLRLKDRHGRDFVLGPTHEEVITDLVRNEIKSYKQLPLNLYQIQTKFRDEIRPRFGLMRGREFIMKDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020351452 161 YSFHLDVDTMNETYEAMYQAYSNILSRMGLAFRPVLADTGSIGGSMSHEFHVLAQSGEDLIAYSTGSDYAANIEKAESPM 240
Cdd:PRK09194 161 YSFHADEESLDETYDAMYQAYSRIFDRLGLDFRAVEADSGAIGGSASHEFMVLADSGEDTIVYSDESDYAANIEKAEALP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020351452 241 PTEArgAATEALRLVDTPNAKTIAELVEQFGLDITKTVKTLIVKGATEeapLVALIVRGDHELNEIKADKLdLVASPLEF 320
Cdd:PRK09194 241 PPRA--AAEEALEKVDTPNAKTIEELAEFLNVPAEKTVKTLLVKADGE---LVAVLVRGDHELNEVKLENL-LGAAPLEL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020351452 321 APEALIRDAIGAGPGSLGPVGL--NMPIIIDHSVSVMSDFAAGANLDDKHYFGINWERDLPLAQAADIRNVVEGEPTPDG 398
Cdd:PRK09194 315 ATEEEIRAALGAVPGFLGPVGLpkDVPIIADRSVADMSNFVVGANEDDYHYVGVNWGRDFPVPEVADLRNVVEGDPSPDG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020351452 399 LGTYAMARGIEVGHIFQLGTNYSKSMNATVLDENGKSQVLLMGCYGVGVSRIVAAAIEQNFDDRGIVWPEAIAPFSVGIL 478
Cdd:PRK09194 395 GGTLKIARGIEVGHIFQLGTKYSEAMNATVLDENGKAQPLIMGCYGIGVSRLVAAAIEQNHDEKGIIWPKAIAPFDVHIV 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020351452 479 PMNMhKSHRVTDIAEQLYKDLSAAGIDVLLDDRKERPGVMFADMELIGIPHTVVIGDRNIDAGVFEYKNRRTGEKQDVPF 558
Cdd:PRK09194 475 PVNM-KDEEVKELAEKLYAELQAAGIEVLLDDRKERPGVKFADADLIGIPHRIVVGDRGLAEGIVEYKDRRTGEKEEVPV 553
|
570
....*....|..
gi 2020351452 559 DQIVDFLKNLQA 570
Cdd:PRK09194 554 DELVEFLKALKK 565
|
|
| ProS |
COG0442 |
Prolyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Prolyl-tRNA ... |
1-568 |
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: 1028.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020351452 1 MRVSKYLLSTQKETPANAEVISHQLMLRAGMIRRNASGLYSYLPTGLRVLRKVEAIVREEMNKAGAIEILMPMVQPADLW 80
Cdd:COG0442 1 MRASKLFIPTLKERPADAEVWSHQLMLRAGLIRKLASGIYTYLPLGYRVLEKIEAIVREEMKRTGAQEVLMPLLQPAELW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020351452 81 VETGRWDKFGPELLRFKDRHNRDFVLGPTHEEVITDLIRKEVSSYKQLPLNLYQIQTKFRDEVRPRFGVMRSREFLMKDA 160
Cdd:COG0442 81 EESGRWEGFGPELARVTDRLEREFCLGPTHEEVITDLVRNEIKSYRDLPLLLYQIQTKFRDEIRPRFGLLRTREFLMKDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020351452 161 YSFHLDVDTMNETYEAMYQAYSNILSRMGLAFRPVLADTGSIGGSMSHEFHVLAQSGEDLIAYSTGSDYAANIEKAESPM 240
Cdd:COG0442 161 YSFHATEEELDEEYQKMLDAYERIFERLGLPVRAVEADSGAIGGSESHEFMVLADSGEDTIVYCDACDYAANIEKAEALA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020351452 241 PTEARGAATEALRLVDTPNAKTIAELVEQFGLDITKTVKTLIVKGateEAPLVALIVRGDHELNEIKADKLdLVASPLEF 320
Cdd:COG0442 241 PPAERAEPTKELEAVATPGAKTIEEVAEFLGVPAEKTVKTLVYKA---DGELVAVLVRGDHELNEIKLENL-LGASELEL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020351452 321 APEALIRDAIGAGPGSLGPVGLNMPIIIDHSVSVMSDFAAGANLDDKHYFGINWERDLPLAQAADIRNVVEGEPTPDGLG 400
Cdd:COG0442 317 ATEEEIEAALGAVPGFLGPVGLGVPYIADRSVAGMSNFVCGANEDDYHYTNVNWGRDFPVDEVADLRNVVEGDPCPDCGG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020351452 401 TYAMARGIEVGHIFQLGTNYSKSMNATVLDENGKSQVLLMGCYGVGVSRIVAAAIEQNFDDRGIVWPEAIAPFSVGILPM 480
Cdd:COG0442 397 LLQDGRGIEVGHIFKLGTKYSKAMDATFLDENGKEQPVWMGCYGIGVTRLIAAAIEQHHDDKGIIWPPAIAPFQVVIVPI 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020351452 481 NMhKSHRVTDIAEQLYKDLSAAGIDVLLDDRKERPGVMFADMELIGIPHTVVIGDRNIDAGVFEYKNRRTGEKQDVPFDQ 560
Cdd:COG0442 477 NM-KDEAVLEAAEELYAELKAAGIDVLLDDRDERPGVKFADAELIGIPLRIVIGPRDLEEGQVEVKRRDTGEKEEVPLDE 555
|
....*...
gi 2020351452 561 IVDFLKNL 568
Cdd:COG0442 556 LVETVKEL 563
|
|
| proS_fam_II |
TIGR00409 |
prolyl-tRNA synthetase, family II; Prolyl-tRNA synthetase is a class II tRNA synthetase and is ... |
1-565 |
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: 871.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020351452 1 MRVSKYLLSTQKETPANAEVISHQLMLRAGMIRRNASGLYSYLPTGLRVLRKVEAIVREEMNKAGAIEILMPMVQPADLW 80
Cdd:TIGR00409 1 MRTSQYLFPTLKETPADAEVKSHQLLLRAGFIRRLGSGLYNWLPLGLRVLKKVENIVREEMNKDGAIEVLLPALQPAELW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020351452 81 VETGRWDKFGPELLRFKDRHNRDFVLGPTHEEVITDLIRKEVSSYKQLPLNLYQIQTKFRDEVRPRFGVMRSREFLMKDA 160
Cdd:TIGR00409 81 QESGRWDTYGPELLRLKDRKGREFVLGPTHEEVITDLARNEIKSYKQLPLNLYQIQTKFRDEIRPRFGLMRGREFIMKDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020351452 161 YSFHLDVDTMNETYEAMYQAYSNILSRMGLAFRPVLADTGSIGGSMSHEFHVLAQSGEDLIAYSTGSDYAANIEKAESPM 240
Cdd:TIGR00409 161 YSFHSDEESLDATYQKMYQAYSNIFSRLGLDFRPVQADSGAIGGSASHEFMVLAESGEDTIVYSDESDYAANIELAEALA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020351452 241 PtEARGAATEALRLVDTPNAKTIAELVEQFGLDITKTVKTLIVKGATEEAPLVALIVRGDHELNEIKADKLDLVASPLEF 320
Cdd:TIGR00409 241 P-GERNAPTAELDKVDTPNTKTIAELVECFNLPAEKVVKTLLVKAVDKSEPLVALLVRGDHELNEVKAPNLLLVAQVLEL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020351452 321 APEALIRDAIGAGPGSLGPVGLN--MPIIIDHSVSVMSDFAAGANLDDKHYFGINWERDLPLAQAADIRNVVEGEPTPDG 398
Cdd:TIGR00409 320 ATEEEIFQKIASGPGSLGPVNINggIPVLIDQTVALMSDFAAGANADDKHYFNVNWDRDVAIPEVADIRKVKEGDPSPDG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020351452 399 LGTYAMARGIEVGHIFQLGTNYSKSMNATVLDENGKSQVLLMGCYGVGVSRIVAAAIEQNFDDRGIVWPEAIAPFSVGIL 478
Cdd:TIGR00409 400 QGTLKIARGIEVGHIFQLGTKYSEALKATFLDENGKNQFMTMGCYGIGVSRLVSAIAEQHHDERGIIWPKAIAPYDVVIV 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020351452 479 PMNMHKShRVTDIAEQLYKDLSAAGIDVLLDDRKERPGVMFADMELIGIPHTVVIGDRNIDAGVFEYKNRRTGEKQDVPF 558
Cdd:TIGR00409 480 VMNMKDE-EQQQLAEELYSELLAQGVDVLLDDRNERAGVKFADSELIGIPLRVVVGKKNLDNGEIEVKKRRNGEKQLIKK 558
|
....*..
gi 2020351452 559 DQIVDFL 565
Cdd:TIGR00409 559 DELVECL 565
|
|
| PRK12325 |
PRK12325 |
prolyl-tRNA synthetase; Provisional |
1-567 |
0e+00 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 237059 [Multi-domain] Cd Length: 439 Bit Score: 616.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020351452 1 MRVSKYLLSTQKETPANAEVISHQLMLRAGMIRRNASGLYSYLPTGLRVLRKVEAIVREEMNKAGAIEILMPMVQPADLW 80
Cdd:PRK12325 1 MRLSRYFLPTLKENPKEAEIVSHRLMLRAGMIRQQAAGIYSWLPLGLKVLKKIENIVREEQNRAGAIEILMPTIQPADLW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020351452 81 VETGRWDKFGPELLRFKDRHNRDFVLGPTHEEVITDLIRKEVSSYKQLPLNLYQIQTKFRDEVRPRFGVMRSREFLMKDA 160
Cdd:PRK12325 81 RESGRYDAYGKEMLRIKDRHDREMLYGPTNEEMITDIFRSYVKSYKDLPLNLYHIQWKFRDEIRPRFGVMRGREFLMKDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020351452 161 YSFHLDVDTMNETYEAMYQAYSNILSRMGLAFRPVLADTGSIGGSMSHEFHVLAQSGEDLIAYstgsdyaaniEKAESPM 240
Cdd:PRK12325 161 YSFDLDEEGARHSYNRMFVAYLRTFARLGLKAIPMRADTGPIGGDLSHEFIILAETGESTVFY----------DKDFLDL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020351452 241 PTEARGAATEalrlvdtpnaktiaelveqfglditktvktlivkgateeaplvalivrgDHELNEIKADkldlvasplef 320
Cdd:PRK12325 231 LVPGEDIDFD-------------------------------------------------VADLQPIVDE----------- 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020351452 321 apealirdaigagpgslgpvglnmpiiidhsvsVMSDFAAganLDDKHYfginwERDLPLAQAADIRNvvegeptpdglg 400
Cdd:PRK12325 251 ---------------------------------WTSLYAA---TEEMHD-----EAAFAAVPEERRLS------------ 277
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020351452 401 tyamARGIEVGHIFQLGTNYSKSMNATVLDENGKSQVLLMGCYGVGVSRIVAAAIEQNFDDRGIVWPEAIAPFSVGILPM 480
Cdd:PRK12325 278 ----ARGIEVGHIFYFGTKYSEPMNAKVQGPDGKEVPVHMGSYGIGVSRLVAAIIEASHDDKGIIWPESVAPFKVGIINL 353
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020351452 481 NMHKShRVTDIAEQLYKDLSAAGIDVLLDDRKERPGVMFADMELIGIPHTVVIGDRNIDAGVFEYKNRRTGEKQDVPFDQ 560
Cdd:PRK12325 354 KQGDE-ACDAACEKLYAALSAAGIDVLYDDTDERPGAKFATMDLIGLPWQIIVGPKGLAEGKVELKDRKTGEREELSVEA 432
|
....*..
gi 2020351452 561 IVDFLKN 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 ... |
17-457 |
3.02e-149 |
|
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: 429.30 E-value: 3.02e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020351452 17 NAEVISHQLMLRAGMIRRNASGLYSYLPTGLRVLRKVEAIVREEMNKAGAIEILMPMVQPADLWVETGRWDKFGPELLRF 96
Cdd:cd00779 1 DAEIISHKLLLRAGFIRQTSSGLYSWLPLGLRVLKKIENIIREEMNKIGAQEILMPILQPAELWKESGRWDAYGPELLRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020351452 97 KDRHNRDFVLGPTHEEVITDLIRKEVSSYKQLPLNLYQIQTKFRDEVRPRFGVMRSREFLMKDAYSFHLDVDTMNETYEA 176
Cdd:cd00779 81 KDRHGKEFLLGPTHEEVITDLVANEIKSYKQLPLNLYQIQTKFRDEIRPRFGLMRGREFLMKDAYSFDIDEESLEETYEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020351452 177 MYQAYSNILSRMGLAFRPVLADTGSIGGSMSHEFHVLaqsgedliaystgsdyaaniekaespmpteargaatealrlvd 256
Cdd:cd00779 161 MYQAYSRIFKRLGLPFVKVEADSGAIGGSLSHEFHVL------------------------------------------- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020351452 257 tpnaktiaelveqfglditktvktlivkgateeaplvalivrgdhelneikadkldlvaSPLEfapealirdaigagpgs 336
Cdd:cd00779 198 -----------------------------------------------------------SPLK----------------- 201
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020351452 337 lgpvglnmpiiidhsvsvmsdfaaganlddkhyfginwerdlplaqaadirnvvegeptpdglgtyaMARGIEVGHIFQL 416
Cdd:cd00779 202 -------------------------------------------------------------------ITKGIEVGHIFQL 214
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2020351452 417 GTNYSKSMNATVLDENGKSQVLLMGCYGVGVSRIVAAAIEQ 457
Cdd:cd00779 215 GTKYSKALGATFLDENGKPKPLEMGCYGIGVSRLLAAIIEQ 255
|
|
| ProRS-INS |
cd04334 |
INS is an amino acid-editing domain inserted (INS) into the bacterial class II prolyl-tRNA ... |
226-386 |
3.66e-73 |
|
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: 230.48 E-value: 3.66e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020351452 226 GSDYAANIEKAESPMPTEARGAATEALRLVDTPNAKTIAELVEQFGLDITKTVKTLIVKgATEEAPLVALIVRGDHELNE 305
Cdd:cd04334 1 DCDYAANIEKAESLPPAAERPAPPKELEKVATPGQKTIEELAEFLGVPPSQTVKTLLVK-ADGEEELVAVLLRGDHELNE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020351452 306 IKADKLDLVAsPLEFAPEALIRDAIGAGPGSLGPVGL-NMPIIIDHSVSVMSDFAAGANLDDKHYFGINWERDLPLAQAA 384
Cdd:cd04334 80 VKLENLLGAA-PLELASEEEIEAATGAPPGFIGPVGLkKIPIIADRSVADLKNFVCGANEDDYHYVNVNWGRDFPLPEVA 158
|
..
gi 2020351452 385 DI 386
Cdd:cd04334 159 DL 160
|
|
| ProRS_core |
cd00772 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
37-238 |
1.70e-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: 164.08 E-value: 1.70e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020351452 37 SGLYSYLPTGLRVLRKVEAIVREEMNKAGAIEILMPMVQPADLWVETGRWDKFG-PELLRFKDRHNR----DFVLGPTHE 111
Cdd:cd00772 22 RGIINFLPLAKAILDKIENVLDKMFKEHGAQNALFPFFILASFLEKEAEHDEGFsKELAVFKDAGDEeleeDFALRPTLE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020351452 112 EVITDLIRKEVSSYKQLPLNLYQIQTKFRDEVRPRFGVMRSREFLMKDAYSFHLDVDTMNETYEAMYQAYSNILSRMG-L 190
Cdd:cd00772 102 ENIGEIAAKFIKSWKDLPQHLNQIGNKFRDEIRPRFGFLRAREFIMKDGHSAHADAEEADEEFLNMLSAYAEIARDLAaI 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2020351452 191 AFRPVLADTGS--IGGSMSHEFHVLAQSGEDLIAySTGSDYAANIEKAES 238
Cdd:cd00772 182 DFIEGEADEGAkfAGASKSREFEALMEDGKAKQA-ETGHIFGEGFARAFD 230
|
|
| ProRS_anticodon_short |
cd00861 |
ProRS Prolyl-anticodon binding domain, short version found predominantly in bacteria. ProRS ... |
472-566 |
2.48e-43 |
|
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: 149.66 E-value: 2.48e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020351452 472 PFSVGILPMNMHkSHRVTDIAEQLYKDLSAAGIDVLLDDRKERPGVMFADMELIGIPHTVVIGDRNIDAGVFEYKNRRTG 551
Cdd:cd00861 1 PFDVVIIPMNMK-DEVQQELAEKLYAELQAAGVDVLLDDRNERPGVKFADADLIGIPYRIVVGKKSAAEGIVEIKVRKTG 79
|
90
....*....|....*
gi 2020351452 552 EKQDVPFDQIVDFLK 566
Cdd:cd00861 80 EKEEISIDELLEFLQ 94
|
|
| YbaK_like |
cd04332 |
YbaK-like. The YbaK family of deacylase domains includes the INS amino acid-editing domain of ... |
250-384 |
2.19e-32 |
|
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: 121.11 E-value: 2.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020351452 250 EALRLVDTPNAKTIAELVEQFGLDITKTVKTLIVKGATEEapLVALIVRGDHELNEIKADKLdLVASPLEFAPEALIRDA 329
Cdd:cd04332 1 EYLEYEHTPGAKTIEEAAEALGVPPGQIAKTLVLKDDKGG--LVLVVVPGDHELDLKKLAKA-LGAKKLRLASEEELEEL 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2020351452 330 IGAGPGSLGPVGL--NMPIIIDHSVSVMSDFAAGANLD--DKHYFGINWERDLPLAQAA 384
Cdd:cd04332 78 TGCEPGGVGPFGLkkGVPVVVDESLLELEDVYVGAGERgaDLHLSPADLLRLLGEAEVA 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 ... |
49-203 |
1.77e-30 |
|
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: 119.03 E-value: 1.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020351452 49 VLRKVEAIVREEMNKAGAIEILMPMVQPADLWVETGRWDKFGPELLRFKDR----HNRDFVLGPTHEEVITDLIRKEVSS 124
Cdd:cd00670 4 LWRALERFLDDRMAEYGYQEILFPFLAPTVLFFKGGHLDGYRKEMYTFEDKgrelRDTDLVLRPAACEPIYQIFSGEILS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020351452 125 YKQLPLNLYQIQTKFRDEVRPRFGVMRSREFLMKDAYSFHLD------VDTMNETYEAMYQAysnilsrMGLAFRPVLAD 198
Cdd:cd00670 84 YRALPLRLDQIGPCFRHEPSGRRGLMRVREFRQVEYVVFGEPeeaeeeRREWLELAEEIARE-------LGLPVRVVVAD 156
|
....*
gi 2020351452 199 TGSIG 203
Cdd:cd00670 157 DPFFG 161
|
|
| tRNA_edit |
pfam04073 |
Aminoacyl-tRNA editing domain; This domain is found either on its own or in association with ... |
257-375 |
1.87e-26 |
|
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: 104.22 E-value: 1.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020351452 257 TPNAKTIAELVEQFGLDITKTVKTLIVKGATEEapLVALIVRGDHELNEIKADKLdLVASPLEFAPEALIRDAIGAGPGS 336
Cdd:pfam04073 1 HPPAATIEELAAALGVPPGRIAKTLVLKDKKGK--YVLVVVPGDREVDLKKLAKL-LGVKRLRLASEEELLELTGVEPGG 77
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2020351452 337 LGPVGL---NMPIIIDHSVSVMSDFAAGANLDDKHYFGINWE 375
Cdd:pfam04073 78 VTPFGLkakGVPVLVDESLKDLPDVVVGAGENGATLRLSNAD 119
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
475-568 |
4.92e-24 |
|
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: 96.12 E-value: 4.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020351452 475 VGILPMNMHKShRVTDIAEQLYKDLSAAGIDVLLDDRKERPGVMFADMELIGIPHTVVIGDRNIDAGVFEYKNRRTGEKQ 554
Cdd:pfam03129 2 VVVIPLGEKAE-ELEEYAQKLAEELRAAGIRVELDDRNESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQE 80
|
90
....*....|....
gi 2020351452 555 DVPFDQIVDFLKNL 568
Cdd:pfam03129 81 TVSLDELVEKLKEL 94
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
95-203 |
1.80e-19 |
|
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: 86.31 E-value: 1.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020351452 95 RFKDRHNRDFVLGPTHEEVITDLIRKEVSSYKQLPLNLYQIQTKFRDEVRPRF-GVMRSREFLMKDAYSFHLDvDTMNET 173
Cdd:pfam00587 2 KVEDENGDELALKPTNEPGHTLLFREEGLRSKDLPLKLAQFGTCFRHEASGDTrGLIRVRQFHQDDAHIFHAP-GQSPDE 80
|
90 100 110
....*....|....*....|....*....|
gi 2020351452 174 YEAMYQAYSNILSRMGLAFRPVLADTGSIG 203
Cdd:pfam00587 81 LEDYIKLIDRVYSRLGLEVRVVRLSNSDGS 110
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
49-203 |
4.34e-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: 86.02 E-value: 4.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020351452 49 VLRKVEAIVREEMNKAGAIEILMPMVQPADLWVETGRWdkfGPELLRFKDRHNRDFVLGPTHEEVITdliRKEVSSYKQL 128
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGHE---PKDLLPVGAENEEDLYLRPTLEPGLV---RLFVSHIRKL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020351452 129 PLNLYQIQTKFRDEvRPRFGVMRSREFLMKDAYSFHLDV---DTMNETYEAMYQaysnILSRMGLA--FRPVLADTGSIG 203
Cdd:cd00768 75 PLRLAEIGPAFRNE-GGRRGLRRVREFTQLEGEVFGEDGeeaSEFEELIELTEE----LLRALGIKldIVFVEKTPGEFS 149
|
|
| HGTP_anticodon |
cd00738 |
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ... |
472-566 |
1.24e-18 |
|
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: 80.91 E-value: 1.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020351452 472 PFSVGILPMNMhKSHRVTDIAEQLYKDLSAAGIDVLLDDRKERPGVMFADMELIGIPHTVVIGDRNIDAGVFEYKNRRTG 551
Cdd:cd00738 1 PIDVAIVPLTD-PRVEAREYAQKLLNALLANGIRVLYDDRERKIGKKFREADLRGVPFAVVVGEDELENGKVTVKSRDTG 79
|
90
....*....|....*
gi 2020351452 552 EKQDVPFDQIVDFLK 566
Cdd:cd00738 80 ESETLHVDELPEFLV 94
|
|
| ProRS_core_arch_euk |
cd00778 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
23-181 |
1.73e-15 |
|
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: 76.48 E-value: 1.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020351452 23 HQLMLRAGMI-RRNASGLYSYLPTGLRVLRKVEAIVREEMNKAGAIEILMPMVQP-ADLWVETGRWDKFGPELlrFKDRH 100
Cdd:cd00778 7 TEVITKAELIdYGPVKGCMVFRPYGYAIWENIQKILDKEIKETGHENVYFPLLIPeSELEKEKEHIEGFAPEV--AWVTH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020351452 101 NRD------FVLGPTHEEVITDLIRKEVSSYKQLPLNLYQIQTKFRDEVRPRFGVMRSREFLMKDAYSFHLD-------V 167
Cdd:cd00778 85 GGLeeleepLALRPTSETAIYPMFSKWIRSYRDLPLKINQWVNVFRWETKTTRPFLRTREFLWQEGHTAHATeeeaeeeV 164
|
170
....*....|....
gi 2020351452 168 DTMNETYEAMYQAY 181
Cdd:cd00778 165 LQILDLYKEFYEDL 178
|
|
| ProRS_anticodon_zinc |
cd00862 |
ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and ... |
463-568 |
1.90e-12 |
|
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: 66.55 E-value: 1.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020351452 463 GIVWPEAIAPFSVGILPM--NMHKSHRVTDIAEQLYKDLSAAGIDVLLDDRKE-RPGVMFADMELIGIPHTVVIGDRNID 539
Cdd:cd00862 1 GLVLPPRVAPIQVVIVPIgiKDEKREEVLEAADELAERLKAAGIRVHVDDRDNyTPGWKFNDWELKGVPLRIEIGPRDLE 80
|
90 100
....*....|....*....|....*....
gi 2020351452 540 AGVFEYKNRRTGEKQDVPFDQIVDFLKNL 568
Cdd:cd00862 81 KNTVVIVRRDTGEKKTVPLAELVEKVPEL 109
|
|
| ThrRS_core |
cd00771 |
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ... |
36-163 |
1.91e-10 |
|
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: 62.18 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020351452 36 ASGLYSYLPTGLRVLRKVEAIVREEMNKAGAIEILMPMVQPADLWVETGRWDKFGPELLRFkDRHNRDFVLGPT----HE 111
Cdd:cd00771 19 GPGLPFWLPKGAIIRNELEDFLRELQRKRGYQEVETPIIYNKELWETSGHWDHYRENMFPF-EEEDEEYGLKPMncpgHC 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2020351452 112 EVITDLIRkevsSYKQLPLNLYQIQTKFRDEVRPRF-GVMRSREFLMKDAYSF 163
Cdd:cd00771 98 LIFKSKPR----SYRDLPLRLAEFGTVHRYEQSGALhGLTRVRGFTQDDAHIF 146
|
|
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
444-570 |
6.06e-09 |
|
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: 58.21 E-value: 6.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020351452 444 GVGVSRIVAAAIEQNfddrgiVWPEAIAPFSVGILPMNMHKSHRVTDIAEQLykdlSAAGIDVLLD--DRKERPGVMFAD 521
Cdd:COG0124 305 AIGLERLLLLLEELG------LLPAAEPPPDVYVVPLGEEARAEALKLAQEL----RAAGIRVELDlgGRKLKKQLKYAD 374
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2020351452 522 MelIGIPHTVVIGDRNIDAGVFEYKNRRTGEKQDVPFDQIVDFLKNLQA 570
Cdd:COG0124 375 K--SGAPFVLILGEDELANGTVTLKDLATGEQETVPLDELVEYLKELLA 421
|
|
| PRK03991 |
PRK03991 |
threonyl-tRNA synthetase; Validated |
367-567 |
3.22e-08 |
|
threonyl-tRNA synthetase; Validated
Pssm-ID: 235190 [Multi-domain] Cd Length: 613 Bit Score: 56.42 E-value: 3.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020351452 367 KHYFGINWERdlplaqaadirNVVegeptpDGLGtyamaRGIEVGhIFQLGTNYSKSMNATVLDENGKSQ-VLLMGCYGV 445
Cdd:PRK03991 411 KHYWVLKVEF-----------AFI------DSLG-----RPIENP-TVQIDVENAERFGIKYVDENGEEKyPIILHCSPT 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020351452 446 G-VSRIVAAAIEQNFDD--RGIV--WPEAIAPFSVGILPMnmhkSHRVTDIAEQLYKDLSAAGIDVLLDDRKERPGVMFA 520
Cdd:PRK03991 468 GsIERVIYALLEKAAKEeeEGKVpmLPTWLSPTQVRVIPV----SERHLDYAEEVADKLEAAGIRVDVDDRDESLGKKIR 543
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2020351452 521 DMELIGIPHTVVIGDRNIDAGVFEYKNRRTGEKQDVPFDQIVDFLKN 567
Cdd:PRK03991 544 DAGKEWIPYVVVIGDKEMESGKLTVTIREESEKVEMTLEELIERIKE 590
|
|
| ThrRS_anticodon |
cd00860 |
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases ... |
472-566 |
1.31e-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: 49.42 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020351452 472 PFSVGILPMNmhksHRVTDIAEQLYKDLSAAGIDVLLDDRKERPGVMFADMELIGIPHTVVIGDRNIDAGVFEYKNRRTG 551
Cdd:cd00860 1 PVQVVVIPVT----DEHLDYAKEVAKKLSDAGIRVEVDLRNEKLGKKIREAQLQKIPYILVVGDKEVETGTVSVRTRDGG 76
|
90
....*....|....*
gi 2020351452 552 EKQDVPFDQIVDFLK 566
Cdd:cd00860 77 DLGSMSLDEFIEKLK 91
|
|
| HisRS_anticodon |
cd00859 |
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases ... |
490-566 |
2.68e-07 |
|
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: 48.69 E-value: 2.68e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2020351452 490 DIAEQLYKDLSAAGIDVLLDDRKERPGVMFADMELIGIPHTVVIGDRNIDAGVFEYKNRRTGEKQDVPFDQIVDFLK 566
Cdd:cd00859 15 SEALELAEQLRDAGIKAEIDYGGRKLKKQFKYADRSGARFAVILGEDELAAGVVTVKDLETGEQETVALDELVEELK 91
|
|
| PRK12444 |
PRK12444 |
threonyl-tRNA synthetase; Reviewed |
31-163 |
4.40e-07 |
|
threonyl-tRNA synthetase; Reviewed
Pssm-ID: 183530 [Multi-domain] Cd Length: 639 Bit Score: 52.83 E-value: 4.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020351452 31 MIRRNASGLYSYLPTGLRVLRKVEAIVREEMNKAGAIEILMPMVQPADLWVETGRWDKFgPELLRFKDRHNRDFVLGPTH 110
Cdd:PRK12444 258 MFSEEAPGMPFYLPKGQIIRNELEAFLREIQKEYNYQEVRTPFMMNQELWERSGHWDHY-KDNMYFSEVDNKSFALKPMN 336
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2020351452 111 EEVITDLIRKEVSSYKQLPLNLYQIQTKFRDEVRPRF-GVMRSREFLMKDAYSF 163
Cdd:PRK12444 337 CPGHMLMFKNKLHSYRELPIRMCEFGQVHRHEFSGALnGLLRVRTFCQDDAHLF 390
|
|
| PRK12444 |
PRK12444 |
threonyl-tRNA synthetase; Reviewed |
463-567 |
4.40e-07 |
|
threonyl-tRNA synthetase; Reviewed
Pssm-ID: 183530 [Multi-domain] Cd Length: 639 Bit Score: 52.83 E-value: 4.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020351452 463 GIVWPEAIAPFSVGILPMnmhkSHRV-TDIAEQLYKDLSAAGIDVLLDDRKERPGVMFADMELIGIPHTVVIGDRNIDAG 541
Cdd:PRK12444 532 GGAFPAWLAPVQVKVIPV----SNAVhVQYADEVADKLAQAGIRVERDERDEKLGYKIREAQMQKIPYVLVIGDKEMENG 607
|
90 100
....*....|....*....|....*.
gi 2020351452 542 VFEYKNRRTGEKQDVPFDQIVDFLKN 567
Cdd:PRK12444 608 AVNVRKYGEEKSEVIELDMFVESIKE 633
|
|
| EbsC |
COG2606 |
Cys-tRNA(Pro) deacylase, prolyl-tRNA editing enzyme YbaK/EbsC [Translation, ribosomal ... |
243-361 |
1.65e-06 |
|
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: 47.78 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020351452 243 EARGAATEALRLVDTpnAKTIAELVEQFGLDITKTVKTLIVKGatEEAPLVAlIVRGDHELNEIKADKLdLVASPLEFAP 322
Cdd:COG2606 8 DAAGIPYEVVEHPEP--AATAEEAAEALGVPPEQIAKTLVFRG--DGGPVLA-VVPGDRRLDLKKLAAA-LGAKKVEMAD 81
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2020351452 323 EALIRDAIGAGPGSLGPVGL--NMPIIIDHSVSVMSD--FAAG 361
Cdd:COG2606 82 PEEVERLTGYEVGGVSPFGLkkGLPVYVDESLLEFDEvyVSAG 124
|
|
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
465-567 |
3.52e-05 |
|
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: 46.56 E-value: 3.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020351452 465 VWpeaIAPFSVGILPMnmhkSHRVTDIAEQLYKDLSAAGIDVLLDDRKERPGVMFADMELIGIPHTVVIGDRNIDAGVFE 544
Cdd:COG0441 535 LW---LAPVQVVVLPI----SDKHADYAKEVAKKLRAAGIRVEVDLRNEKIGYKIREAQLQKVPYMLVVGDKEVENGTVS 607
|
90 100
....*....|....*....|...
gi 2020351452 545 YKNRRTGEKQDVPFDQIVDFLKN 567
Cdd:COG0441 608 VRRRGGGDLGTMSLDEFIARLKE 630
|
|
| ProX_deacylase |
cd04333 |
This CD, composed mainly of bacterial single-domain proteins, includes the Thermus ... |
243-346 |
1.80e-04 |
|
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: 42.10 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020351452 243 EARGAATEALRLVDTpnAKTIAELVEQFGLDITKTVKTLIVKGATEeapLVALIVRGDHELNEIKADKLdlVASPLEFAP 322
Cdd:cd04333 9 AARGLDLEVIELPES--TRTAALAAEALGCEPGQIAKSLVFRVDDE---PVLVVTSGDARVDNKKFKAL--FGEKLKMAD 81
|
90 100
....*....|....*....|....
gi 2020351452 323 EALIRDAIGAGPGSLGPVGLNMPI 346
Cdd:cd04333 82 AEEVRELTGFAIGGVCPFGHPEPL 105
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
47-155 |
4.16e-04 |
|
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: 42.20 E-value: 4.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020351452 47 LRVLRKVEAIVREEMNKAGAIEILMPMVQPADLwVETGRWDKFGPELLRFKDRHNRDFVLGPtheEVITDLIRKEVS--S 124
Cdd:cd00773 2 AALRRYIEDTLREVFERYGYEEIDTPVFEYTEL-FLRKSGDEVSKEMYRFKDKGGRDLALRP---DLTAPVARAVAEnlL 77
|
90 100 110
....*....|....*....|....*....|.
gi 2020351452 125 YKQLPLNLYQIQTKFRDEvRPRFGvmRSREF 155
Cdd:cd00773 78 SLPLPLKLYYIGPVFRYE-RPQKG--RYREF 105
|
|
| PLN02908 |
PLN02908 |
threonyl-tRNA synthetase |
38-194 |
9.23e-04 |
|
threonyl-tRNA synthetase
Pssm-ID: 178496 [Multi-domain] Cd Length: 686 Bit Score: 42.07 E-value: 9.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020351452 38 GLYSYLPTGLRVLRKVEAIVREEMNKAGAIEILMPMVQPADLWVETGRWDKFGPELLRFkDRHNRDFVLGPTHEEVITDL 117
Cdd:PLN02908 312 GSCFFLPHGARIYNKLMDFIREQYWERGYDEVITPNIYNMDLWETSGHAAHYKENMFVF-EIEKQEFGLKPMNCPGHCLM 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020351452 118 IRKEVSSYKQLPLNLYQIQTKFRDEVRPRF-GVMRSREFLMKDAYSFHLD----------VDTMNETYEAMYQAYSnils 186
Cdd:PLN02908 391 FAHRVRSYRELPLRLADFGVLHRNELSGALtGLTRVRRFQQDDAHIFCREdqikdevkgvLDFLDYVYEVFGFTYE---- 466
|
....*...
gi 2020351452 187 rMGLAFRP 194
Cdd:PLN02908 467 -LKLSTRP 473
|
|
| PRK14938 |
PRK14938 |
Ser-tRNA(Thr) hydrolase; Provisional |
467-566 |
1.28e-03 |
|
Ser-tRNA(Thr) hydrolase; Provisional
Pssm-ID: 184902 [Multi-domain] Cd Length: 387 Bit Score: 41.37 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020351452 467 PEAIAPFSVGILPMnmhKSHRVtDIAEQLYKDLSAAGIDVLLDDRKERPGVMFADMELIGIPHTVVIGDRNIDAGVFEYK 546
Cdd:PRK14938 269 PDWLNPIQVRILPV---KKDFL-DFSIQVAERLRKEGIRVNVDDLDDSLGNKIRRAGTEWIPFVIIIGEREVKTSTLTVK 344
|
90 100
....*....|....*....|
gi 2020351452 547 NRRTGEKQDVPFDQIVDFLK 566
Cdd:PRK14938 345 IRANNEQKSMTVEELVKEIK 364
|
|
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
36-163 |
1.55e-03 |
|
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: 41.56 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020351452 36 ASGLYSYLPTGLRVLRKVEAIVREEMNKAGAIEILMPMVQPADLWVETGRWDKFGpELLRFKDRHNRDFVLG----PTHE 111
Cdd:COG0441 260 GPGLPFWHPKGAIIRRELEDYIREKHRKAGYQEVKTPHILDRELWETSGHWDHYR-ENMFPTESDGEEYALKpmncPGHI 338
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2020351452 112 EVITDLIRkevsSYKQLPLNLYQIQTKFRDEvrpRFGV----MRSREFLMKDAYSF 163
Cdd:COG0441 339 LIYKSGLR----SYRDLPLRLAEFGTVHRYE---PSGAlhglMRVRGFTQDDAHIF 387
|
|
| SerRS_core |
cd00770 |
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the ... |
61-203 |
7.87e-03 |
|
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the attachment of serine to the 3' OH group of ribose of the appropriate tRNA. This domain It 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. SerRS synthetase is a homodimer.
Pssm-ID: 238393 [Multi-domain] Cd Length: 297 Bit Score: 38.69 E-value: 7.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020351452 61 MNKAGAIEILMPMVQPADLWVETGRWDKFGPELlrFKDRHNrDFVLGPTHEEVITDLIRKEVSSYKQLPLNLYQIQTKFR 140
Cdd:cd00770 66 LTKRGFTPVIPPFLVRKEVMEGTGQLPKFDEQL--YKVEGE-DLYLIATAEVPLAALHRDEILEEEELPLKYAGYSPCFR 142
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2020351452 141 DEV----RPRFGVMRSREFLMKDAYSFHLDVDTMNEtYEAMYQAYSNILSRMGLAFRPVLADTGSIG 203
Cdd:cd00770 143 KEAgsagRDTRGLFRVHQFEKVEQFVFTKPEESWEE-LEELISNAEEILQELGLPYRVVNICTGDLG 208
|
|
|