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Conserved domains on  [gi|2002300084|ref|NP_001014086|]
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probable proline--tRNA ligase, mitochondrial precursor [Rattus norvegicus]

Protein Classification

proline--tRNA ligase( domain architecture ID 10092266)

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
ProRS_core_prok cd00779
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ...
70-359 1.28e-150

Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain. This subfamily contains the core domain of ProRS from prokaryotes and from the mitochondria of eukaryotes.


:

Pssm-ID: 238402 [Multi-domain]  Cd Length: 255  Bit Score: 429.30  E-value: 1.28e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084  70 DLTCKSQRLMLQVGLILPASPGCYHLMPYTVRAVEKLVRVIDQEMQAIGGQKINMPSLSPAELWRATGRWDLMGRELLRL 149
Cdd:cd00779     1 DAEIISHKLLLRAGFIRQTSSGLYSWLPLGLRVLKKIENIIREEMNKIGAQEILMPILQPAELWKESGRWDAYGPELLRL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084 150 KDRHGKEYCLGPTHEEAVTALVASQKKlSYKQLPLLLYQVTRKFRDEPRPRFGLLRGREFYMKDMYTFDSSSEAAQETYS 229
Cdd:cd00779    81 KDRHGKEFLLGPTHEEVITDLVANEIK-SYKQLPLNLYQIQTKFRDEIRPRFGLMRGREFLMKDAYSFDIDEESLEETYE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084 230 LVCDAYCRLFDRLGLRWMKARADVGSIGGTMSHEFQLPVdigedrlvvcpschfsanteivdlsqkicpdcqgPLTETKG 309
Cdd:cd00779   160 KMYQAYSRIFKRLGLPFVKVEADSGAIGGSLSHEFHVLS----------------------------------PLKITKG 205
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 2002300084 310 IEVGHTFYLGTKYSSIFNAHFTNAHGESLLAEMGCYGLGVTRILAAAIEV 359
Cdd:cd00779   206 IEVGHIFQLGTKYSKALGATFLDENGKPKPLEMGCYGIGVSRLLAAIIEQ 255
ProRS_anticodon_short cd00861
ProRS Prolyl-anticodon binding domain, short version found predominantly in bacteria. ProRS ...
374-475 9.66e-20

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: 83.79  E-value: 9.66e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084 374 PYQVCIIPPKKGSkeAAATEIVERLYDDVTEALpqlrGEVLLDDRThLTIGNRLKDANKLGYPFVIIASKRALEDPaHFE 453
Cdd:cd00861     1 PFDVVIIPMNMKD--EVQQELAEKLYAELQAAG----VDVLLDDRN-ERPGVKFADADLIGIPYRIVVGKKSAAEG-IVE 72
                          90       100
                  ....*....|....*....|..
gi 2002300084 454 VWSQNTGEVVFLTKEGVMELLT 475
Cdd:cd00861    73 IKVRKTGEKEEISIDELLEFLQ 94
 
Name Accession Description Interval E-value
ProRS_core_prok cd00779
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ...
70-359 1.28e-150

Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain. This subfamily contains the core domain of ProRS from prokaryotes and from the mitochondria of eukaryotes.


Pssm-ID: 238402 [Multi-domain]  Cd Length: 255  Bit Score: 429.30  E-value: 1.28e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084  70 DLTCKSQRLMLQVGLILPASPGCYHLMPYTVRAVEKLVRVIDQEMQAIGGQKINMPSLSPAELWRATGRWDLMGRELLRL 149
Cdd:cd00779     1 DAEIISHKLLLRAGFIRQTSSGLYSWLPLGLRVLKKIENIIREEMNKIGAQEILMPILQPAELWKESGRWDAYGPELLRL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084 150 KDRHGKEYCLGPTHEEAVTALVASQKKlSYKQLPLLLYQVTRKFRDEPRPRFGLLRGREFYMKDMYTFDSSSEAAQETYS 229
Cdd:cd00779    81 KDRHGKEFLLGPTHEEVITDLVANEIK-SYKQLPLNLYQIQTKFRDEIRPRFGLMRGREFLMKDAYSFDIDEESLEETYE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084 230 LVCDAYCRLFDRLGLRWMKARADVGSIGGTMSHEFQLPVdigedrlvvcpschfsanteivdlsqkicpdcqgPLTETKG 309
Cdd:cd00779   160 KMYQAYSRIFKRLGLPFVKVEADSGAIGGSLSHEFHVLS----------------------------------PLKITKG 205
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 2002300084 310 IEVGHTFYLGTKYSSIFNAHFTNAHGESLLAEMGCYGLGVTRILAAAIEV 359
Cdd:cd00779   206 IEVGHIFQLGTKYSKALGATFLDENGKPKPLEMGCYGIGVSRLLAAIIEQ 255
PRK09194 PRK09194
prolyl-tRNA synthetase; Provisional
47-475 1.40e-150

prolyl-tRNA synthetase; Provisional


Pssm-ID: 236405 [Multi-domain]  Cd Length: 565  Bit Score: 441.06  E-value: 1.40e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084  47 VSRMFQPqNLREDqvlslegrASDLTCKSQRLMLQVGLILPASPGCYHLMPYTVRAVEKLVRVIDQEMQAIGGQKINMPS 126
Cdd:PRK09194    3 TSQLFLP-TLKET--------PADAEVISHQLLLRAGYIRKLASGIYTYLPLGLRVLRKIENIVREEMNKIGAQEVLMPA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084 127 LSPAELWRATGRWDLMGRELLRLKDRHGKEYCLGPTHEEAVTALVASQKKlSYKQLPLLLYQVTRKFRDEPRPRFGLLRG 206
Cdd:PRK09194   74 LQPAELWQESGRWEEYGPELLRLKDRHGRDFVLGPTHEEVITDLVRNEIK-SYKQLPLNLYQIQTKFRDEIRPRFGLMRG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084 207 REFYMKDMYTFDSSSEAAQETYSLVCDAYCRLFDRLGLRWMKARADVGSIGGTMSHEFQLPVDIGEDRLVVCPSCHFSAN 286
Cdd:PRK09194  153 REFIMKDAYSFHADEESLDETYDAMYQAYSRIFDRLGLDFRAVEADSGAIGGSASHEFMVLADSGEDTIVYSDESDYAAN 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084 287 TE------------------------------------------------------------------------------ 288
Cdd:PRK09194  233 IEkaealpppraaaeealekvdtpnaktieelaeflnvpaektvktllvkadgelvavlvrgdhelnevklenllgaapl 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084 289 ------------------------------IVDLSQK----------------------------------------ICP 298
Cdd:PRK09194  313 elateeeiraalgavpgflgpvglpkdvpiIADRSVAdmsnfvvganeddyhyvgvnwgrdfpvpevadlrnvvegdPSP 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084 299 DCQGPLTETKGIEVGHTFYLGTKYSSIFNAHFTNAHGESLLAEMGCYGLGVTRILAAAIEVLSTEDCIRWPSLLAPYQVC 378
Cdd:PRK09194  393 DGGGTLKIARGIEVGHIFQLGTKYSEAMNATVLDENGKAQPLIMGCYGIGVSRLVAAAIEQNHDEKGIIWPKAIAPFDVH 472
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084 379 IIPPkkGSKEAAATEIVERLYDDVTEAlpqlrG-EVLLDDRtHLTIGNRLKDANKLGYPFVIIASKRALEDpAHFEVWSQ 457
Cdd:PRK09194  473 IVPV--NMKDEEVKELAEKLYAELQAA-----GiEVLLDDR-KERPGVKFADADLIGIPHRIVVGDRGLAE-GIVEYKDR 543
                         570
                  ....*....|....*...
gi 2002300084 458 NTGEVVFLTKEGVMELLT 475
Cdd:PRK09194  544 RTGEKEEVPVDELVEFLK 561
ProS COG0442
Prolyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Prolyl-tRNA ...
75-474 6.02e-150

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: 439.21  E-value: 6.02e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084  75 SQRLMLQVGLILPASPGCYHLMPYTVRAVEKLVRVIDQEMQAIGGQKINMPSLSPAELWRATGRWDLMGRELLRLKDRHG 154
Cdd:COG0442    22 SHQLMLRAGLIRKLASGIYTYLPLGYRVLEKIEAIVREEMKRTGAQEVLMPLLQPAELWEESGRWEGFGPELARVTDRLE 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084 155 KEYCLGPTHEEAVTALVASQKKlSYKQLPLLLYQVTRKFRDEPRPRFGLLRGREFYMKDMYTFDSSSEAAQETYSLVCDA 234
Cdd:COG0442   102 REFCLGPTHEEVITDLVRNEIK-SYRDLPLLLYQIQTKFRDEIRPRFGLLRTREFLMKDAYSFHATEEELDEEYQKMLDA 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084 235 YCRLFDRLGLRWMKARADVGSIGGTMSHEFQLPVDIGEDRLVVCPSCHFSANTE-------------------------- 288
Cdd:COG0442   181 YERIFERLGLPVRAVEADSGAIGGSESHEFMVLADSGEDTIVYCDACDYAANIEkaealappaeraeptkeleavatpga 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084     --------------------------------------------------------------------------------
Cdd:COG0442   261 ktieevaeflgvpaektvktlvykadgelvavlvrgdhelneiklenllgaselelateeeieaalgavpgflgpvglgv 340
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084 289 --IVDLSQK----------------------------------------ICPDCQGPLTETKGIEVGHTFYLGTKYSSIF 326
Cdd:COG0442   341 pyIADRSVAgmsnfvcganeddyhytnvnwgrdfpvdevadlrnvvegdPCPDCGGLLQDGRGIEVGHIFKLGTKYSKAM 420
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084 327 NAHFTNAHGESLLAEMGCYGLGVTRILAAAIEVLSTEDCIRWPSLLAPYQVCIIPPkkGSKEAAATEIVERLYDDVTEAl 406
Cdd:COG0442   421 DATFLDENGKEQPVWMGCYGIGVTRLIAAAIEQHHDDKGIIWPPAIAPFQVVIVPI--NMKDEAVLEAAEELYAELKAA- 497
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2002300084 407 pqlrG-EVLLDDRTHlTIGNRLKDANKLGYPFVIIASKRALEDPAhFEVWSQNTGEVVFLTKEGVMELL 474
Cdd:COG0442   498 ----GiDVLLDDRDE-RPGVKFADAELIGIPLRIVIGPRDLEEGQ-VEVKRRDTGEKEEVPLDELVETV 560
proS_fam_II TIGR00409
prolyl-tRNA synthetase, family II; Prolyl-tRNA synthetase is a class II tRNA synthetase and is ...
70-475 1.10e-116

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: 354.12  E-value: 1.10e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084  70 DLTCKSQRLMLQVGLILPASPGCYHLMPYTVRAVEKLVRVIDQEMQAIGGQKINMPSLSPAELWRATGRWDLMGRELLRL 149
Cdd:TIGR00409  17 DAEVKSHQLLLRAGFIRRLGSGLYNWLPLGLRVLKKVENIVREEMNKDGAIEVLLPALQPAELWQESGRWDTYGPELLRL 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084 150 KDRHGKEYCLGPTHEEAVTALVASQKKlSYKQLPLLLYQVTRKFRDEPRPRFGLLRGREFYMKDMYTFDSSSEAAQETYS 229
Cdd:TIGR00409  97 KDRKGREFVLGPTHEEVITDLARNEIK-SYKQLPLNLYQIQTKFRDEIRPRFGLMRGREFIMKDAYSFHSDEESLDATYQ 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084 230 LVCDAYCRLFDRLGLRWMKARADVGSIGGTMSHEFQLPVDIGEDRLVVCPSCHFSANTEI-------------------- 289
Cdd:TIGR00409 176 KMYQAYSNIFSRLGLDFRPVQADSGAIGGSASHEFMVLAESGEDTIVYSDESDYAANIELaealapgernaptaeldkvd 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084     --------------------------------------------------------------------------------
Cdd:TIGR00409 256 tpntktiaelvecfnlpaekvvktllvkavdkseplvallvrgdhelnevkapnlllvaqvlelateeeifqkiasgpgs 335
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084 290 ---VDLSQKI--------------------------------------------------CPDCQGPLTETKGIEVGHTF 316
Cdd:TIGR00409 336 lgpVNINGGIpvlidqtvalmsdfaaganaddkhyfnvnwdrdvaipevadirkvkegdpSPDGQGTLKIARGIEVGHIF 415
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084 317 YLGTKYSSIFNAHFTNAHGESLLAEMGCYGLGVTRILAAAIEVLSTEDCIRWPSLLAPYQVCIIPPKKGSKEaaateiVE 396
Cdd:TIGR00409 416 QLGTKYSEALKATFLDENGKNQFMTMGCYGIGVSRLVSAIAEQHHDERGIIWPKAIAPYDVVIVVMNMKDEE------QQ 489
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2002300084 397 RLYDDVTEALPQLRGEVLLDDRTHlTIGNRLKDANKLGYPFVIIASKRALEDpAHFEVWSQNTGEVVFLTKEGVMELLT 475
Cdd:TIGR00409 490 QLAEELYSELLAQGVDVLLDDRNE-RAGVKFADSELIGIPLRVVVGKKNLDN-GEIEVKKRRNGEKQLIKKDELVECLE 566
tRNA-synt_2b pfam00587
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ...
148-359 3.88e-20

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: 87.85  E-value: 3.88e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084 148 RLKDRHGKEYCLGPTHEEAVTALVaSQKKLSYKQLPLLLYQVTRKFRDEPRPRF-GLLRGREFYMKDMYTFDSSSEAAQE 226
Cdd:pfam00587   2 KVEDENGDELALKPTNEPGHTLLF-REEGLRSKDLPLKLAQFGTCFRHEASGDTrGLIRVRQFHQDDAHIFHAPGQSPDE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084 227 TYSLVCDAYcRLFDRLGLRWMKARADvgsiggtmSHEFQLPVDIGEDRLVVCPSChfsanteivdlsqkicpdcqgplte 306
Cdd:pfam00587  81 LEDYIKLID-RVYSRLGLEVRVVRLS--------NSDGSAFYGPKLDFEVVFPSL------------------------- 126
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2002300084 307 TKGIEVGHTFYLGTKYSSIFNAHFTNAHGESLLAEMGCYG-LGVTRILAAAIEV 359
Cdd:pfam00587 127 GKQRQTGTIQNDGFRLPRRLGIRYKDEDNESKFPYMIHRAgLGVERFLAAILEN 180
ProRS_anticodon_short cd00861
ProRS Prolyl-anticodon binding domain, short version found predominantly in bacteria. ProRS ...
374-475 9.66e-20

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: 83.79  E-value: 9.66e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084 374 PYQVCIIPPKKGSkeAAATEIVERLYDDVTEALpqlrGEVLLDDRThLTIGNRLKDANKLGYPFVIIASKRALEDPaHFE 453
Cdd:cd00861     1 PFDVVIIPMNMKD--EVQQELAEKLYAELQAAG----VDVLLDDRN-ERPGVKFADADLIGIPYRIVVGKKSAAEG-IVE 72
                          90       100
                  ....*....|....*....|..
gi 2002300084 454 VWSQNTGEVVFLTKEGVMELLT 475
Cdd:cd00861    73 IKVRKTGEKEEISIDELLEFLQ 94
HGTP_anticodon pfam03129
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ...
376-448 2.10e-06

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: 46.04  E-value: 2.10e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2002300084 376 QVCIIPPKKGskeaaaTEIVERLYDDVTEALPQLRGEVLLDDRtHLTIGNRLKDANKLGYPFVIIASKRALED 448
Cdd:pfam03129   1 QVVVIPLGEK------AEELEEYAQKLAEELRAAGIRVELDDR-NESIGKKFRRADLIGIPFALVVGEKELEE 66
 
Name Accession Description Interval E-value
ProRS_core_prok cd00779
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ...
70-359 1.28e-150

Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain. This subfamily contains the core domain of ProRS from prokaryotes and from the mitochondria of eukaryotes.


Pssm-ID: 238402 [Multi-domain]  Cd Length: 255  Bit Score: 429.30  E-value: 1.28e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084  70 DLTCKSQRLMLQVGLILPASPGCYHLMPYTVRAVEKLVRVIDQEMQAIGGQKINMPSLSPAELWRATGRWDLMGRELLRL 149
Cdd:cd00779     1 DAEIISHKLLLRAGFIRQTSSGLYSWLPLGLRVLKKIENIIREEMNKIGAQEILMPILQPAELWKESGRWDAYGPELLRL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084 150 KDRHGKEYCLGPTHEEAVTALVASQKKlSYKQLPLLLYQVTRKFRDEPRPRFGLLRGREFYMKDMYTFDSSSEAAQETYS 229
Cdd:cd00779    81 KDRHGKEFLLGPTHEEVITDLVANEIK-SYKQLPLNLYQIQTKFRDEIRPRFGLMRGREFLMKDAYSFDIDEESLEETYE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084 230 LVCDAYCRLFDRLGLRWMKARADVGSIGGTMSHEFQLPVdigedrlvvcpschfsanteivdlsqkicpdcqgPLTETKG 309
Cdd:cd00779   160 KMYQAYSRIFKRLGLPFVKVEADSGAIGGSLSHEFHVLS----------------------------------PLKITKG 205
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 2002300084 310 IEVGHTFYLGTKYSSIFNAHFTNAHGESLLAEMGCYGLGVTRILAAAIEV 359
Cdd:cd00779   206 IEVGHIFQLGTKYSKALGATFLDENGKPKPLEMGCYGIGVSRLLAAIIEQ 255
PRK09194 PRK09194
prolyl-tRNA synthetase; Provisional
47-475 1.40e-150

prolyl-tRNA synthetase; Provisional


Pssm-ID: 236405 [Multi-domain]  Cd Length: 565  Bit Score: 441.06  E-value: 1.40e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084  47 VSRMFQPqNLREDqvlslegrASDLTCKSQRLMLQVGLILPASPGCYHLMPYTVRAVEKLVRVIDQEMQAIGGQKINMPS 126
Cdd:PRK09194    3 TSQLFLP-TLKET--------PADAEVISHQLLLRAGYIRKLASGIYTYLPLGLRVLRKIENIVREEMNKIGAQEVLMPA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084 127 LSPAELWRATGRWDLMGRELLRLKDRHGKEYCLGPTHEEAVTALVASQKKlSYKQLPLLLYQVTRKFRDEPRPRFGLLRG 206
Cdd:PRK09194   74 LQPAELWQESGRWEEYGPELLRLKDRHGRDFVLGPTHEEVITDLVRNEIK-SYKQLPLNLYQIQTKFRDEIRPRFGLMRG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084 207 REFYMKDMYTFDSSSEAAQETYSLVCDAYCRLFDRLGLRWMKARADVGSIGGTMSHEFQLPVDIGEDRLVVCPSCHFSAN 286
Cdd:PRK09194  153 REFIMKDAYSFHADEESLDETYDAMYQAYSRIFDRLGLDFRAVEADSGAIGGSASHEFMVLADSGEDTIVYSDESDYAAN 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084 287 TE------------------------------------------------------------------------------ 288
Cdd:PRK09194  233 IEkaealpppraaaeealekvdtpnaktieelaeflnvpaektvktllvkadgelvavlvrgdhelnevklenllgaapl 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084 289 ------------------------------IVDLSQK----------------------------------------ICP 298
Cdd:PRK09194  313 elateeeiraalgavpgflgpvglpkdvpiIADRSVAdmsnfvvganeddyhyvgvnwgrdfpvpevadlrnvvegdPSP 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084 299 DCQGPLTETKGIEVGHTFYLGTKYSSIFNAHFTNAHGESLLAEMGCYGLGVTRILAAAIEVLSTEDCIRWPSLLAPYQVC 378
Cdd:PRK09194  393 DGGGTLKIARGIEVGHIFQLGTKYSEAMNATVLDENGKAQPLIMGCYGIGVSRLVAAAIEQNHDEKGIIWPKAIAPFDVH 472
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084 379 IIPPkkGSKEAAATEIVERLYDDVTEAlpqlrG-EVLLDDRtHLTIGNRLKDANKLGYPFVIIASKRALEDpAHFEVWSQ 457
Cdd:PRK09194  473 IVPV--NMKDEEVKELAEKLYAELQAA-----GiEVLLDDR-KERPGVKFADADLIGIPHRIVVGDRGLAE-GIVEYKDR 543
                         570
                  ....*....|....*...
gi 2002300084 458 NTGEVVFLTKEGVMELLT 475
Cdd:PRK09194  544 RTGEKEEVPVDELVEFLK 561
ProS COG0442
Prolyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Prolyl-tRNA ...
75-474 6.02e-150

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: 439.21  E-value: 6.02e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084  75 SQRLMLQVGLILPASPGCYHLMPYTVRAVEKLVRVIDQEMQAIGGQKINMPSLSPAELWRATGRWDLMGRELLRLKDRHG 154
Cdd:COG0442    22 SHQLMLRAGLIRKLASGIYTYLPLGYRVLEKIEAIVREEMKRTGAQEVLMPLLQPAELWEESGRWEGFGPELARVTDRLE 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084 155 KEYCLGPTHEEAVTALVASQKKlSYKQLPLLLYQVTRKFRDEPRPRFGLLRGREFYMKDMYTFDSSSEAAQETYSLVCDA 234
Cdd:COG0442   102 REFCLGPTHEEVITDLVRNEIK-SYRDLPLLLYQIQTKFRDEIRPRFGLLRTREFLMKDAYSFHATEEELDEEYQKMLDA 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084 235 YCRLFDRLGLRWMKARADVGSIGGTMSHEFQLPVDIGEDRLVVCPSCHFSANTE-------------------------- 288
Cdd:COG0442   181 YERIFERLGLPVRAVEADSGAIGGSESHEFMVLADSGEDTIVYCDACDYAANIEkaealappaeraeptkeleavatpga 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084     --------------------------------------------------------------------------------
Cdd:COG0442   261 ktieevaeflgvpaektvktlvykadgelvavlvrgdhelneiklenllgaselelateeeieaalgavpgflgpvglgv 340
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084 289 --IVDLSQK----------------------------------------ICPDCQGPLTETKGIEVGHTFYLGTKYSSIF 326
Cdd:COG0442   341 pyIADRSVAgmsnfvcganeddyhytnvnwgrdfpvdevadlrnvvegdPCPDCGGLLQDGRGIEVGHIFKLGTKYSKAM 420
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084 327 NAHFTNAHGESLLAEMGCYGLGVTRILAAAIEVLSTEDCIRWPSLLAPYQVCIIPPkkGSKEAAATEIVERLYDDVTEAl 406
Cdd:COG0442   421 DATFLDENGKEQPVWMGCYGIGVTRLIAAAIEQHHDDKGIIWPPAIAPFQVVIVPI--NMKDEAVLEAAEELYAELKAA- 497
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2002300084 407 pqlrG-EVLLDDRTHlTIGNRLKDANKLGYPFVIIASKRALEDPAhFEVWSQNTGEVVFLTKEGVMELL 474
Cdd:COG0442   498 ----GiDVLLDDRDE-RPGVKFADAELIGIPLRIVIGPRDLEEGQ-VEVKRRDTGEKEEVPLDELVETV 560
PRK12325 PRK12325
prolyl-tRNA synthetase; Provisional
47-476 5.63e-126

prolyl-tRNA synthetase; Provisional


Pssm-ID: 237059 [Multi-domain]  Cd Length: 439  Bit Score: 373.43  E-value: 5.63e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084  47 VSRMFQPqNLREDqvlslegrASDLTCKSQRLMLQVGLILPASPGCYHLMPYTVRAVEKLVRVIDQEMQAIGGQKINMPS 126
Cdd:PRK12325    3 LSRYFLP-TLKEN--------PKEAEIVSHRLMLRAGMIRQQAAGIYSWLPLGLKVLKKIENIVREEQNRAGAIEILMPT 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084 127 LSPAELWRATGRWDLMGRELLRLKDRHGKEYCLGPTHEEAVTALVASQKKlSYKQLPLLLYQVTRKFRDEPRPRFGLLRG 206
Cdd:PRK12325   74 IQPADLWRESGRYDAYGKEMLRIKDRHDREMLYGPTNEEMITDIFRSYVK-SYKDLPLNLYHIQWKFRDEIRPRFGVMRG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084 207 REFYMKDMYTFDSSSEAAQETYSLVCDAYCRLFDRLGLRWMKARADVGSIGGTMSHEFQLPVDIGED------RLVVCPS 280
Cdd:PRK12325  153 REFLMKDAYSFDLDEEGARHSYNRMFVAYLRTFARLGLKAIPMRADTGPIGGDLSHEFIILAETGEStvfydkDFLDLLV 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084 281 CHFSANTEIVDLS------------------QKICPD-CQGPLTETKGIEVGHTFYLGTKYSSIFNAHFTNAHGESLLAE 341
Cdd:PRK12325  233 PGEDIDFDVADLQpivdewtslyaateemhdEAAFAAvPEERRLSARGIEVGHIFYFGTKYSEPMNAKVQGPDGKEVPVH 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084 342 MGCYGLGVTRILAAAIEVLSTEDCIRWPSLLAPYQVCIIPPKKGskEAAATEIVERLYddvtEALPQLRGEVLLDDRTHl 421
Cdd:PRK12325  313 MGSYGIGVSRLVAAIIEASHDDKGIIWPESVAPFKVGIINLKQG--DEACDAACEKLY----AALSAAGIDVLYDDTDE- 385
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2002300084 422 TIGNRLKDANKLGYPFVIIASKRALEDpAHFEVWSQNTGEVVFLTKEGVMELLTG 476
Cdd:PRK12325  386 RPGAKFATMDLIGLPWQIIVGPKGLAE-GKVELKDRKTGEREELSVEAAINRLTA 439
proS_fam_II TIGR00409
prolyl-tRNA synthetase, family II; Prolyl-tRNA synthetase is a class II tRNA synthetase and is ...
70-475 1.10e-116

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: 354.12  E-value: 1.10e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084  70 DLTCKSQRLMLQVGLILPASPGCYHLMPYTVRAVEKLVRVIDQEMQAIGGQKINMPSLSPAELWRATGRWDLMGRELLRL 149
Cdd:TIGR00409  17 DAEVKSHQLLLRAGFIRRLGSGLYNWLPLGLRVLKKVENIVREEMNKDGAIEVLLPALQPAELWQESGRWDTYGPELLRL 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084 150 KDRHGKEYCLGPTHEEAVTALVASQKKlSYKQLPLLLYQVTRKFRDEPRPRFGLLRGREFYMKDMYTFDSSSEAAQETYS 229
Cdd:TIGR00409  97 KDRKGREFVLGPTHEEVITDLARNEIK-SYKQLPLNLYQIQTKFRDEIRPRFGLMRGREFIMKDAYSFHSDEESLDATYQ 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084 230 LVCDAYCRLFDRLGLRWMKARADVGSIGGTMSHEFQLPVDIGEDRLVVCPSCHFSANTEI-------------------- 289
Cdd:TIGR00409 176 KMYQAYSNIFSRLGLDFRPVQADSGAIGGSASHEFMVLAESGEDTIVYSDESDYAANIELaealapgernaptaeldkvd 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084     --------------------------------------------------------------------------------
Cdd:TIGR00409 256 tpntktiaelvecfnlpaekvvktllvkavdkseplvallvrgdhelnevkapnlllvaqvlelateeeifqkiasgpgs 335
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084 290 ---VDLSQKI--------------------------------------------------CPDCQGPLTETKGIEVGHTF 316
Cdd:TIGR00409 336 lgpVNINGGIpvlidqtvalmsdfaaganaddkhyfnvnwdrdvaipevadirkvkegdpSPDGQGTLKIARGIEVGHIF 415
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084 317 YLGTKYSSIFNAHFTNAHGESLLAEMGCYGLGVTRILAAAIEVLSTEDCIRWPSLLAPYQVCIIPPKKGSKEaaateiVE 396
Cdd:TIGR00409 416 QLGTKYSEALKATFLDENGKNQFMTMGCYGIGVSRLVSAIAEQHHDERGIIWPKAIAPYDVVIVVMNMKDEE------QQ 489
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2002300084 397 RLYDDVTEALPQLRGEVLLDDRTHlTIGNRLKDANKLGYPFVIIASKRALEDpAHFEVWSQNTGEVVFLTKEGVMELLT 475
Cdd:TIGR00409 490 QLAEELYSELLAQGVDVLLDDRNE-RAGVKFADSELIGIPLRVVVGKKNLDN-GEIEVKKRRNGEKQLIKKDELVECLE 566
ProRS_core cd00772
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ...
70-358 6.76e-40

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: 144.82  E-value: 6.76e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084  70 DLTCKSQRLMLQVGLI--LPASpGCYHLMPYTVRAVEKLVRVIDQEMQAIGGQKINMPSLSPAELWRATGRWDLMG-REL 146
Cdd:cd00772     1 DASEKSLEHIGKAELAdqGPGR-GIINFLPLAKAILDKIENVLDKMFKEHGAQNALFPFFILASFLEKEAEHDEGFsKEL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084 147 LRLKDRHGKE----YCLGPTHEEAVTALVASQKKlSYKQLPLLLYQVTRKFRDEPRPRFGLLRGREFYMKDMYTFDSSSE 222
Cdd:cd00772    80 AVFKDAGDEEleedFALRPTLEENIGEIAAKFIK-SWKDLPQHLNQIGNKFRDEIRPRFGFLRAREFIMKDGHSAHADAE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084 223 AAQETYSLVCDAYCRLFDRLG-LRWMKARADVGS--IGGTMSHEFQLPVDIGedrlvvcpschfsanteivdlsqkicpd 299
Cdd:cd00772   159 EADEEFLNMLSAYAEIARDLAaIDFIEGEADEGAkfAGASKSREFEALMEDG---------------------------- 210
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2002300084 300 cqgpltETKGIEVGHTFYLGTKYSSIFNAHFTNAHGESLLAEMGCYGLGVTRILAAAIE 358
Cdd:cd00772   211 ------KAKQAETGHIFGEGFARAFDLKAKFLDKDGKEKFFEMGCWGIGISRFIGAIIE 263
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 ...
104-355 2.16e-23

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: 98.62  E-value: 2.16e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084 104 EKLVRVIDQEMQAIGGQKINMPSLSPAELWRATGRWDLMGRELLRLKDR----HGKEYCLGPTHEEAVTAlVASQKKLSY 179
Cdd:cd00670     6 RALERFLDDRMAEYGYQEILFPFLAPTVLFFKGGHLDGYRKEMYTFEDKgrelRDTDLVLRPAACEPIYQ-IFSGEILSY 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084 180 KQLPLLLYQVTRKFRDEPRPRFGLLRGREFYMKDMYTFDSSSEAAQETYSLVcDAYCRLFDRLGLRWmkaRADVGSIGgt 259
Cdd:cd00670    85 RALPLRLDQIGPCFRHEPSGRRGLMRVREFRQVEYVVFGEPEEAEEERREWL-ELAEEIARELGLPV---RVVVADDP-- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084 260 mshEFQLPVDIGEDRlvvcpscHFSANTEIVDLSqkicPDCQGplteTKGIEVGHTFYLGTKYSSIFNahfTNAHGESLL 339
Cdd:cd00670   159 ---FFGRGGKRGLDA-------GRETVVEFELLL----PLPGR----AKETAVGSANVHLDHFGASFK---IDEDGGGRA 217
                         250
                  ....*....|....*.
gi 2002300084 340 AEMGCYGLGVTRILAA 355
Cdd:cd00670   218 HTGCGGAGGEERLVLA 233
tRNA-synt_2b pfam00587
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ...
148-359 3.88e-20

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: 87.85  E-value: 3.88e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084 148 RLKDRHGKEYCLGPTHEEAVTALVaSQKKLSYKQLPLLLYQVTRKFRDEPRPRF-GLLRGREFYMKDMYTFDSSSEAAQE 226
Cdd:pfam00587   2 KVEDENGDELALKPTNEPGHTLLF-REEGLRSKDLPLKLAQFGTCFRHEASGDTrGLIRVRQFHQDDAHIFHAPGQSPDE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084 227 TYSLVCDAYcRLFDRLGLRWMKARADvgsiggtmSHEFQLPVDIGEDRLVVCPSChfsanteivdlsqkicpdcqgplte 306
Cdd:pfam00587  81 LEDYIKLID-RVYSRLGLEVRVVRLS--------NSDGSAFYGPKLDFEVVFPSL------------------------- 126
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2002300084 307 TKGIEVGHTFYLGTKYSSIFNAHFTNAHGESLLAEMGCYG-LGVTRILAAAIEV 359
Cdd:pfam00587 127 GKQRQTGTIQNDGFRLPRRLGIRYKDEDNESKFPYMIHRAgLGVERFLAAILEN 180
ProRS_anticodon_short cd00861
ProRS Prolyl-anticodon binding domain, short version found predominantly in bacteria. ProRS ...
374-475 9.66e-20

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: 83.79  E-value: 9.66e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084 374 PYQVCIIPPKKGSkeAAATEIVERLYDDVTEALpqlrGEVLLDDRThLTIGNRLKDANKLGYPFVIIASKRALEDPaHFE 453
Cdd:cd00861     1 PFDVVIIPMNMKD--EVQQELAEKLYAELQAAG----VDVLLDDRN-ERPGVKFADADLIGIPYRIVVGKKSAAEG-IVE 72
                          90       100
                  ....*....|....*....|..
gi 2002300084 454 VWSQNTGEVVFLTKEGVMELLT 475
Cdd:cd00861    73 IKVRKTGEKEEISIDELLEFLQ 94
class_II_aaRS-like_core cd00768
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ...
104-352 2.48e-16

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: 77.54  E-value: 2.48e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084 104 EKLVRVIDQEMQAIGGQKINMPSLSPAELWRATGRWdlmGRELLRLKDRHGKEYCLGPTHEEAVTALVASQKKlsykQLP 183
Cdd:cd00768     3 SKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGHE---PKDLLPVGAENEEDLYLRPTLEPGLVRLFVSHIR----KLP 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084 184 LLLYQVTRKFRDEPRPRfGLLRGREFYMKDMYTFDSSSEAAQETYSLVcDAYCRLFDRLGLRWmKARADVGSIGgtmshE 263
Cdd:cd00768    76 LRLAEIGPAFRNEGGRR-GLRRVREFTQLEGEVFGEDGEEASEFEELI-ELTEELLRALGIKL-DIVFVEKTPG-----E 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084 264 FQLPvdigedrlvvcpscHFSANTEIVDLSQkicpdcqgpltETKGIEVGHTFYLGTKYSSIFNAHFTNAHGESLLAEMG 343
Cdd:cd00768   148 FSPG--------------GAGPGFEIEVDHP-----------EGRGLEIGSGGYRQDEQARAADLYFLDEALEYRYPPTI 202

                  ....*....
gi 2002300084 344 CYGLGVTRI 352
Cdd:cd00768   203 GFGLGLERL 211
ProRS_core_arch_euk cd00778
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ...
91-357 6.09e-14

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: 71.86  E-value: 6.09e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084  91 GCYHLMPYTVRAVEKLVRVIDQEMQAIGGQKINMPSLSPAelwratgrwDLMGRELLRLKD---------RHGKE----- 156
Cdd:cd00778    23 GCMVFRPYGYAIWENIQKILDKEIKETGHENVYFPLLIPE---------SELEKEKEHIEGfapevawvtHGGLEeleep 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084 157 YCLGPTHEEAVTALVASQKKlSYKQLPLLLYQVTRKFRDE---PRPrfgLLRGREFYMKDMYT-FDSSSEAAQETYSLVc 232
Cdd:cd00778    94 LALRPTSETAIYPMFSKWIR-SYRDLPLKINQWVNVFRWEtktTRP---FLRTREFLWQEGHTaHATEEEAEEEVLQIL- 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084 233 DAYCRLFDRLglrwmkaradvgsiggtmsheFQLPVDIGE----DRlvvcpschF--SANTEIVDlsqKICPDcqGplte 306
Cdd:cd00778   169 DLYKEFYEDL---------------------LAIPVVKGRktewEK--------FagADYTYTIE---AMMPD--G---- 210
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2002300084 307 tKGIEVGHTFYLGTKYSSIFNAHFTNAHGESLLAEMGCYGLGvTRILAAAI 357
Cdd:cd00778   211 -RALQSGTSHNLGQNFSKAFDIKYQDKDGQKEYVHQTSWGIS-TRLIGAII 259
HGTP_anticodon pfam03129
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ...
376-448 2.10e-06

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: 46.04  E-value: 2.10e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2002300084 376 QVCIIPPKKGskeaaaTEIVERLYDDVTEALPQLRGEVLLDDRtHLTIGNRLKDANKLGYPFVIIASKRALED 448
Cdd:pfam03129   1 QVVVIPLGEK------AEELEEYAQKLAEELRAAGIRVELDDR-NESIGKKFRRADLIGIPFALVVGEKELEE 66
HGTP_anticodon cd00738
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ...
374-474 7.32e-06

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: 44.31  E-value: 7.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084 374 PYQVCIIPPKKGSKEAaaTEIVERLYddvtEALPQLRGEVLLDDRTHlTIGNRLKDANKLGYPFVIIASKRALEDpAHFE 453
Cdd:cd00738     1 PIDVAIVPLTDPRVEA--REYAQKLL----NALLANGIRVLYDDRER-KIGKKFREADLRGVPFAVVVGEDELEN-GKVT 72
                          90       100
                  ....*....|....*....|.
gi 2002300084 454 VWSQNTGEVVFLTKEGVMELL 474
Cdd:cd00738    73 VKSRDTGESETLHVDELPEFL 93
ThrRS_core cd00771
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ...
105-226 8.48e-06

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: 47.54  E-value: 8.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084 105 KLVRVIDQEMQAIGGQKINMPSLSPAELWRATGRWDLMgRELLRLKDRHGKEYCLGPT----HeeavtALVASQKKLSYK 180
Cdd:cd00771    35 ELEDFLRELQRKRGYQEVETPIIYNKELWETSGHWDHY-RENMFPFEEEDEEYGLKPMncpgH-----CLIFKSKPRSYR 108
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2002300084 181 QLPLLLYQVTRKFRDEPRPRF-GLLRGREFYMKDMYTFDSSSEAAQE 226
Cdd:cd00771   109 DLPLRLAEFGTVHRYEQSGALhGLTRVRGFTQDDAHIFCTPDQIKEE 155
PRK03991 PRK03991
threonyl-tRNA synthetase; Validated
177-217 6.08e-05

threonyl-tRNA synthetase; Validated


Pssm-ID: 235190 [Multi-domain]  Cd Length: 613  Bit Score: 45.63  E-value: 6.08e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2002300084 177 LSYKQLPLLLYQVTRK-FRDEPRPRF-GLLRGREFYMKDMYTF 217
Cdd:PRK03991  302 ISYKNLPLKMYELSTYsFRLEQRGELvGLKRLRAFTMPDMHTL 344
GlyRS_anticodon cd00858
GlyRS Glycyl-anticodon binding domain. GlyRS belongs to class II aminoacyl-tRNA synthetases ...
367-450 4.44e-03

GlyRS Glycyl-anticodon binding domain. GlyRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only.


Pssm-ID: 238435 [Multi-domain]  Cd Length: 121  Bit Score: 37.15  E-value: 4.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084 367 RWPSLLAPYQVCIIPPkkgSKEAAATEIVERLYddvtEALPQLRGEVLLDDRThlTIGNRLKDANKLGYPFVIIASKRAL 446
Cdd:cd00858    19 RLPPALAPIKVAVLPL---VKRDELVEIAKEIS----EELRELGFSVKYDDSG--SIGRRYARQDEIGTPFCVTVDFDTL 89

                  ....
gi 2002300084 447 EDPA 450
Cdd:cd00858    90 EDGT 93
PLN02734 PLN02734
glycyl-tRNA synthetase
175-241 5.88e-03

glycyl-tRNA synthetase


Pssm-ID: 178335 [Multi-domain]  Cd Length: 684  Bit Score: 39.34  E-value: 5.88e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2002300084 175 KKLSY---KQLPLLLYQVTRKFRDEPRPRFGLLRGREFYMKDMYTFDSSSEAAQETYSLVCDAYCRLFDR 241
Cdd:PLN02734  264 RDLYYyngGKLPFAAAQIGQAFRNEISPRQGLLRVREFTLAEIEHFVDPEDKSHPKFSEVADLEFLLFPR 333
 
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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