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Conserved domains on  [gi|2020351452|ref|WP_208662166|]
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MULTISPECIES: proline--tRNA ligase [Shewanella]

Protein Classification

proline--tRNA ligase( domain architecture ID 11483602)

proline--tRNA ligase catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro)

Graphical summary

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List of domain hits

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
 
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
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
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
 
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
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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