|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09194 |
PRK09194 |
prolyl-tRNA synthetase; Provisional |
1-580 |
0e+00 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 236405 [Multi-domain] Cd Length: 565 Bit Score: 911.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080718084 1 MSQLFVRTLREDPADAEVPSHRWLVRAGYIRRVAPGVYSWLPLGLRVMRRIEAICREEMASIGAQEVSFPALLASDPYKE 80
Cdd:PRK09194 3 TSQLFLPTLKETPADAEVISHQLLLRAGYIRKLASGIYTYLPLGLRVLRKIENIVREEMNKIGAQEVLMPALQPAELWQE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080718084 81 TGRWVEYGDNLFRLKDRKGVDMLLGPTHEEMFTLMVKDLYSSYKDLPLCLYQIQNKYRDEARPRAGILRGREFVMMDAYS 160
Cdd:PRK09194 83 SGRWEEYGPELLRLKDRHGRDFVLGPTHEEVITDLVRNEIKSYKQLPLNLYQIQTKFRDEIRPRFGLMRGREFIMKDAYS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080718084 161 FDVAQEGLDEAYQAQRDAYIRIFNRLGFDYAIVKAMSGPMGGSRSEEFLAVAANGEDTFVRS-SGGYAANVEAVrVAVPD 239
Cdd:PRK09194 163 FHADEESLDETYDAMYQAYSRIFDRLGLDFRAVEADSGAIGGSASHEFMVLADSGEDTIVYSdESDYAANIEKA-EALPP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080718084 240 PLPIDgLPEAEVVDTPDARTIESLVRIANevrpradrpWTGADTLKNVVFMVAHpdgtrEPLAIGLPGDRDVDEKRLEAV 319
Cdd:PRK09194 242 PRAAA-EEALEKVDTPNAKTIEELAEFLN---------VPAEKTVKTLLVKADG-----ELVAVLVRGDHELNEVKLENL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080718084 320 LEPAVVEPFTEEDFAANPQLVKGYIGPGALGEDnsskVRYLVDPRVVTGTSWITGADQKDRHVFNLVAGRDFTPDGVIDV 399
Cdd:PRK09194 307 LGAAPLELATEEEIRAALGAVPGFLGPVGLPKD----VPIIADRSVADMSNFVVGANEDDYHYVGVNWGRDFPVPEVADL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080718084 400 AEIREGDPAPDGSGELHLARGIEIGHIFQLGKKYADALGLKVLDHNGKLVTVTMGSYGLGVSRAVAAIAEGTCDEKGLCW 479
Cdd:PRK09194 383 RNVVEGDPSPDGGGTLKIARGIEVGHIFQLGTKYSEAMNATVLDENGKAQPLIMGCYGIGVSRLVAAAIEQNHDEKGIIW 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080718084 480 PREVAPYDVQVLATG-KGTEILDEATRIASELAEAGLEVLLDDRKASPGVKFADSEILGMPTSVVVG-RGLKDGLVEVRD 557
Cdd:PRK09194 463 PKAIAPFDVHIVPVNmKDEEVKELAEKLYAELQAAGIEVLLDDRKERPGVKFADADLIGIPHRIVVGdRGLAEGIVEYKD 542
|
570 580
....*....|....*....|...
gi 1080718084 558 RSTGENRQVSVAEAVCAVLKEVR 580
Cdd:PRK09194 543 RRTGEKEEVPVDELVEFLKALKK 565
|
|
| ProS |
COG0442 |
Prolyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Prolyl-tRNA ... |
1-579 |
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: 765.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080718084 1 MSQLFVRTLREDPADAEVPSHRWLVRAGYIRRVAPGVYSWLPLGLRVMRRIEAICREEMASIGAQEVSFPALLASDPYKE 80
Cdd:COG0442 3 ASKLFIPTLKERPADAEVWSHQLMLRAGLIRKLASGIYTYLPLGYRVLEKIEAIVREEMKRTGAQEVLMPLLQPAELWEE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080718084 81 TGRWVEYGDNLFRLKDRKGVDMLLGPTHEEMFTLMVKDLYSSYKDLPLCLYQIQNKYRDEARPRAGILRGREFVMMDAYS 160
Cdd:COG0442 83 SGRWEGFGPELARVTDRLEREFCLGPTHEEVITDLVRNEIKSYRDLPLLLYQIQTKFRDEIRPRFGLLRTREFLMKDAYS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080718084 161 FDVAQEGLDEAYQAQRDAYIRIFNRLGFDYAIVKAMSGPMGGSRSEEFLAVAANGEDTFVRS-SGGYAANVEAVRVAVPD 239
Cdd:COG0442 163 FHATEEELDEEYQKMLDAYERIFERLGLPVRAVEADSGAIGGSESHEFMVLADSGEDTIVYCdACDYAANIEKAEALAPP 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080718084 240 PLPIDGLPEAEVVDTPDARTIESLVRIANevrpradrpWTGADTLKNVVFMVAHpdgtrEPLAIGLPGDRDVDEKRLEAV 319
Cdd:COG0442 243 AERAEPTKELEAVATPGAKTIEEVAEFLG---------VPAEKTVKTLVYKADG-----ELVAVLVRGDHELNEIKLENL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080718084 320 LEPAVVEPFTEEDFAANPQLVKGYIGPGALgednssKVRYLVDPRVVTGTSWITGADQKDRHVFNLVAGRDFTPDGVIDV 399
Cdd:COG0442 309 LGASELELATEEEIEAALGAVPGFLGPVGL------GVPYIADRSVAGMSNFVCGANEDDYHYTNVNWGRDFPVDEVADL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080718084 400 AEIREGDPAPDGSGELHLARGIEIGHIFQLGKKYADALGLKVLDHNGKLVTVTMGSYGLGVSRAVAAIAEGTCDEKGLCW 479
Cdd:COG0442 383 RNVVEGDPCPDCGGLLQDGRGIEVGHIFKLGTKYSKAMDATFLDENGKEQPVWMGCYGIGVTRLIAAAIEQHHDDKGIIW 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080718084 480 PREVAPYDVQVLATG-KGTEILDEATRIASELAEAGLEVLLDDRKASPGVKFADSEILGMPTSVVVG-RGLKDGLVEVRD 557
Cdd:COG0442 463 PPAIAPFQVVIVPINmKDEAVLEAAEELYAELKAAGIDVLLDDRDERPGVKFADAELIGIPLRIVIGpRDLEEGQVEVKR 542
|
570 580
....*....|....*....|..
gi 1080718084 558 RSTGENRQVSVAEAVCAVLKEV 579
Cdd:COG0442 543 RDTGEKEEVPLDELVETVKELL 564
|
|
| proS_fam_II |
TIGR00409 |
prolyl-tRNA synthetase, family II; Prolyl-tRNA synthetase is a class II tRNA synthetase and is ... |
2-572 |
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: 544.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080718084 2 SQLFVRTLREDPADAEVPSHRWLVRAGYIRRVAPGVYSWLPLGLRVMRRIEAICREEMASIGAQEVSFPALLASDPYKET 81
Cdd:TIGR00409 4 SQYLFPTLKETPADAEVKSHQLLLRAGFIRRLGSGLYNWLPLGLRVLKKVENIVREEMNKDGAIEVLLPALQPAELWQES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080718084 82 GRWVEYGDNLFRLKDRKGVDMLLGPTHEEMFTLMVKDLYSSYKDLPLCLYQIQNKYRDEARPRAGILRGREFVMMDAYSF 161
Cdd:TIGR00409 84 GRWDTYGPELLRLKDRKGREFVLGPTHEEVITDLARNEIKSYKQLPLNLYQIQTKFRDEIRPRFGLMRGREFIMKDAYSF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080718084 162 DVAQEGLDEAYQAQRDAYIRIFNRLGFDYAIVKAMSGPMGGSRSEEFLAVAANGEDTFVRSSGG-YAANVEAVRVAVPDP 240
Cdd:TIGR00409 164 HSDEESLDATYQKMYQAYSNIFSRLGLDFRPVQADSGAIGGSASHEFMVLAESGEDTIVYSDESdYAANIELAEALAPGE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080718084 241 LPIDgLPEAEVVDTPDARTIESLVRIANEvrpRADRpwtgadTLKNVVFMVAHPDGTRepLAIGLPGDRDVDEKRLEAVL 320
Cdd:TIGR00409 244 RNAP-TAELDKVDTPNTKTIAELVECFNL---PAEK------VVKTLLVKAVDKSEPL--VALLVRGDHELNEVKAPNLL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080718084 321 EPA-VVEPFTEEDFAANPQLVKGYIGPGALGEDnsskVRYLVDPRVVTGTSWITGADQKDRHVFNLVAGRDFTPDGVIDV 399
Cdd:TIGR00409 312 LVAqVLELATEEEIFQKIASGPGSLGPVNINGG----IPVLIDQTVALMSDFAAGANADDKHYFNVNWDRDVAIPEVADI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080718084 400 AEIREGDPAPDGSGELHLARGIEIGHIFQLGKKYADALGLKVLDHNGKLVTVTMGSYGLGVSRAVAAIAEGTCDEKGLCW 479
Cdd:TIGR00409 388 RKVKEGDPSPDGQGTLKIARGIEVGHIFQLGTKYSEALKATFLDENGKNQFMTMGCYGIGVSRLVSAIAEQHHDERGIIW 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080718084 480 PREVAPYDVQVLATGKGTEILDE-ATRIASELAEAGLEVLLDDRKASPGVKFADSEILGMPTSVVVG-RGLKDGLVEVRD 557
Cdd:TIGR00409 468 PKAIAPYDVVIVVMNMKDEEQQQlAEELYSELLAQGVDVLLDDRNERAGVKFADSELIGIPLRVVVGkKNLDNGEIEVKK 547
|
570
....*....|....*
gi 1080718084 558 RSTGENRQVSVAEAV 572
Cdd:TIGR00409 548 RRNGEKQLIKKDELV 562
|
|
| PRK12325 |
PRK12325 |
prolyl-tRNA synthetase; Provisional |
2-572 |
2.04e-146 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 237059 [Multi-domain] Cd Length: 439 Bit Score: 429.66 E-value: 2.04e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080718084 2 SQLFVRTLREDPADAEVPSHRWLVRAGYIRRVAPGVYSWLPLGLRVMRRIEAICREEMASIGAQEVSFPALLASDPYKET 81
Cdd:PRK12325 4 SRYFLPTLKENPKEAEIVSHRLMLRAGMIRQQAAGIYSWLPLGLKVLKKIENIVREEQNRAGAIEILMPTIQPADLWRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080718084 82 GRWVEYGDNLFRLKDRKGVDMLLGPTHEEMFTLMVKDLYSSYKDLPLCLYQIQNKYRDEARPRAGILRGREFVMMDAYSF 161
Cdd:PRK12325 84 GRYDAYGKEMLRIKDRHDREMLYGPTNEEMITDIFRSYVKSYKDLPLNLYHIQWKFRDEIRPRFGVMRGREFLMKDAYSF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080718084 162 DVAQEGLDEAYQAQRDAYIRIFNRLGFDYAIVKAMSGPMGGSRSEEFLAVAANGEDTfvrssggyaanveavrvavpdpl 241
Cdd:PRK12325 164 DLDEEGARHSYNRMFVAYLRTFARLGLKAIPMRADTGPIGGDLSHEFIILAETGEST----------------------- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080718084 242 pidglpeaevvdtpdartieslvrianevrpradrpwtgadtlknvVFmvahpdgtreplaiglpgdrdVDEKRLEAVLE 321
Cdd:PRK12325 221 ----------------------------------------------VF---------------------YDKDFLDLLVP 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080718084 322 PAVVEPfteeDFAANPQLVKGYigpgalgednsskvrylvdprvvtgTSWITGADQK-DRHVFNLVAGrdftpdgvidva 400
Cdd:PRK12325 234 GEDIDF----DVADLQPIVDEW-------------------------TSLYAATEEMhDEAAFAAVPE------------ 272
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080718084 401 eiregdpapdgsGELHLARGIEIGHIFQLGKKYADALGLKVLDHNGKLVTVTMGSYGLGVSRAVAAIAEGTCDEKGLCWP 480
Cdd:PRK12325 273 ------------ERRLSARGIEVGHIFYFGTKYSEPMNAKVQGPDGKEVPVHMGSYGIGVSRLVAAIIEASHDDKGIIWP 340
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080718084 481 REVAPYDVQVLATGKGTEILDEAT-RIASELAEAGLEVLLDDRKASPGVKFADSEILGMPTSVVVG-RGLKDGLVEVRDR 558
Cdd:PRK12325 341 ESVAPFKVGIINLKQGDEACDAACeKLYAALSAAGIDVLYDDTDERPGAKFATMDLIGLPWQIIVGpKGLAEGKVELKDR 420
|
570
....*....|....
gi 1080718084 559 STGENRQVSVAEAV 572
Cdd:PRK12325 421 KTGEREELSVEAAI 434
|
|
| ProRS_core_prok |
cd00779 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
15-213 |
3.04e-112 |
|
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: 335.32 E-value: 3.04e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080718084 15 DAEVPSHRWLVRAGYIRRVAPGVYSWLPLGLRVMRRIEAICREEMASIGAQEVSFPALLASDPYKETGRWVEYGDNLFRL 94
Cdd:cd00779 1 DAEIISHKLLLRAGFIRQTSSGLYSWLPLGLRVLKKIENIIREEMNKIGAQEILMPILQPAELWKESGRWDAYGPELLRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080718084 95 KDRKGVDMLLGPTHEEMFTLMVKDLYSSYKDLPLCLYQIQNKYRDEARPRAGILRGREFVMMDAYSFDVAQEGLDEAYQA 174
Cdd:cd00779 81 KDRHGKEFLLGPTHEEVITDLVANEIKSYKQLPLNLYQIQTKFRDEIRPRFGLMRGREFLMKDAYSFDIDEESLEETYEK 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 1080718084 175 QRDAYIRIFNRLGFDYAIVKAMSGPMGGSRSEEFLAVAA 213
Cdd:cd00779 161 MYQAYSRIFKRLGLPFVKVEADSGAIGGSLSHEFHVLSP 199
|
|
| ProRS_core |
cd00772 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
26-215 |
2.59e-32 |
|
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: 125.17 E-value: 2.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080718084 26 RAGYIRRV-APGVYSWLPLGLRVMRRIEAICREEMASIGAQEVSFPALLASDPYKETGRWVEYGD-NLFRLKDRKGV--- 100
Cdd:cd00772 12 KAELADQGpGRGIINFLPLAKAILDKIENVLDKMFKEHGAQNALFPFFILASFLEKEAEHDEGFSkELAVFKDAGDEele 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080718084 101 -DMLLGPTHEEMFTLMVKDLYSSYKDLPLCLYQIQNKYRDEARPRAGILRGREFVMMDAYSFDVAQEGLDEAYQAQRDAY 179
Cdd:cd00772 92 eDFALRPTLEENIGEIAAKFIKSWKDLPQHLNQIGNKFRDEIRPRFGFLRAREFIMKDGHSAHADAEEADEEFLNMLSAY 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 1080718084 180 IRIFNRLG-FDYAIVKAMSG--PMGGSRSEEFLAVAANG 215
Cdd:cd00772 172 AEIARDLAaIDFIEGEADEGakFAGASKSREFEALMEDG 210
|
|
| ProRS-INS |
cd04334 |
INS is an amino acid-editing domain inserted (INS) into the bacterial class II prolyl-tRNA ... |
223-399 |
6.62e-27 |
|
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: 106.83 E-value: 6.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080718084 223 SGGYAANVEAVRVAVPDPLPIDGLPEAEVVDTPDARTIESLVRIANevrpradrpWTGADTLKNVVFMVahpDGTREPLA 302
Cdd:cd04334 1 DCDYAANIEKAESLPPAAERPAPPKELEKVATPGQKTIEELAEFLG---------VPPSQTVKTLLVKA---DGEEELVA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080718084 303 IGLPGDRDVDEKRLEAVLEPAVVEPFTEEDFAANPQLVKGYIGPgalgeDNSSKVRYLVDPRVVTGTSWITGADQKDRHV 382
Cdd:cd04334 69 VLLRGDHELNEVKLENLLGAAPLELASEEEIEAATGAPPGFIGP-----VGLKKIPIIADRSVADLKNFVCGANEDDYHY 143
|
170
....*....|....*..
gi 1080718084 383 FNLVAGRDFTPDGVIDV 399
Cdd:cd04334 144 VNVNWGRDFPLPEVADL 160
|
|
| ProRS_anticodon_short |
cd00861 |
ProRS Prolyl-anticodon binding domain, short version found predominantly in bacteria. ProRS ... |
485-572 |
2.15e-23 |
|
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: 94.58 E-value: 2.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080718084 485 PYDVQVLATGKG-TEILDEATRIASELAEAGLEVLLDDRKASPGVKFADSEILGMPTSVVVG-RGLKDGLVEVRDRSTGE 562
Cdd:cd00861 1 PFDVVIIPMNMKdEVQQELAEKLYAELQAAGVDVLLDDRNERPGVKFADADLIGIPYRIVVGkKSAAEGIVEIKVRKTGE 80
|
90
....*....|
gi 1080718084 563 NRQVSVAEAV 572
Cdd:cd00861 81 KEEISIDELL 90
|
|
| 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 ... |
49-207 |
4.23e-18 |
|
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: 83.59 E-value: 4.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080718084 49 RRIEAICREEMASIGAQEVSFPALLASDPYKETGRWVEYGDNLFRLKDRKGV----DMLLGPTHEEMFTLMVKDLYSSYK 124
Cdd:cd00670 6 RALERFLDDRMAEYGYQEILFPFLAPTVLFFKGGHLDGYRKEMYTFEDKGRElrdtDLVLRPAACEPIYQIFSGEILSYR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080718084 125 DLPLCLYQIQNKYRDEARPRAGILRGREFVMMDAYSFdVAQEGLDEAYQAQRDAYIRIFNRLGFDYAIVKAMSGPMGGSR 204
Cdd:cd00670 86 ALPLRLDQIGPCFRHEPSGRRGLMRVREFRQVEYVVF-GEPEEAEEERREWLELAEEIARELGLPVRVVVADDPFFGRGG 164
|
...
gi 1080718084 205 SEE 207
Cdd:cd00670 165 KRG 167
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
487-578 |
3.91e-16 |
|
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: 73.77 E-value: 3.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080718084 487 DVQVLATGKGT-EILDEATRIASELAEAGLEVLLDDRKASPGVKFADSEILGMPTSVVVG-RGLKDGLVEVRDRSTGENR 564
Cdd:pfam03129 1 QVVVIPLGEKAeELEEYAQKLAEELRAAGIRVELDDRNESIGKKFRRADLIGIPFALVVGeKELEEGTVTVRRRDTGEQE 80
|
90
....*....|....
gi 1080718084 565 QVSVAEAVCAVLKE 578
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 ... |
92-211 |
5.21e-15 |
|
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: 73.21 E-value: 5.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080718084 92 FRLKDRKGVDMLLGPTHEEMFTLMVKDLYSSYKDLPLCLYQIQNKYRDEARPRA-GILRGREFVMMDAYSFdVAQEGLDE 170
Cdd:pfam00587 1 YKVEDENGDELALKPTNEPGHTLLFREEGLRSKDLPLKLAQFGTCFRHEASGDTrGLIRVRQFHQDDAHIF-HAPGQSPD 79
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1080718084 171 AYQAQRDAYIRIFNRLGFDYAIVKAMSGPMG--GSRSEEFLAV 211
Cdd:pfam00587 80 ELEDYIKLIDRVYSRLGLEVRVVRLSNSDGSafYGPKLDFEVV 122
|
|
| tRNA_edit |
pfam04073 |
Aminoacyl-tRNA editing domain; This domain is found either on its own or in association with ... |
254-391 |
8.04e-15 |
|
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: 71.09 E-value: 8.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080718084 254 TPDARTIESLVRIANevrpradrpWTGADTLKNVVFMvahpDGTREPLAIGLPGDRDVDEKRLEAVLEPAVVEPFTEEDF 333
Cdd:pfam04073 1 HPPAATIEELAAALG---------VPPGRIAKTLVLK----DKKGKYVLVVVPGDREVDLKKLAKLLGVKRLRLASEEEL 67
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1080718084 334 AANPQLVKGYIGPGALGEDNsskVRYLVDPRVVTGTSWITGADQKDRHVFNLVA-GRDF 391
Cdd:pfam04073 68 LELTGVEPGGVTPFGLKAKG---VPVLVDESLKDLPDVVVGAGENGATLRLSNAdLRKL 123
|
|
| HGTP_anticodon |
cd00738 |
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ... |
485-570 |
8.70e-14 |
|
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: 67.04 E-value: 8.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080718084 485 PYDVQVLA-TGKGTEILDEATRIASELAEAGLEVLLDDRKASPGVKFADSEILGMPTSVVVG-RGLKDGLVEVRDRSTGE 562
Cdd:cd00738 1 PIDVAIVPlTDPRVEAREYAQKLLNALLANGIRVLYDDRERKIGKKFREADLRGVPFAVVVGeDELENGKVTVKSRDTGE 80
|
....*...
gi 1080718084 563 NRQVSVAE 570
Cdd:cd00738 81 SETLHVDE 88
|
|
| ProRS_core_arch_euk |
cd00778 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
36-186 |
5.18e-13 |
|
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: 69.16 E-value: 5.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080718084 36 GVYSWLPLGLRVMRRIEAICREEMASIGAQEVSFPALLasdPYKETGR-------------WVEYG--DNLfrlkdrkGV 100
Cdd:cd00778 23 GCMVFRPYGYAIWENIQKILDKEIKETGHENVYFPLLI---PESELEKekehiegfapevaWVTHGglEEL-------EE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080718084 101 DMLLGPTHEEMFTLMVKDLYSSYKDLPLCLYQIQNKYRDEARPRAGILRGREFVMMDAYS-FDVAQEGLDEAYQAQrDAY 179
Cdd:cd00778 93 PLALRPTSETAIYPMFSKWIRSYRDLPLKINQWVNVFRWETKTTRPFLRTREFLWQEGHTaHATEEEAEEEVLQIL-DLY 171
|
....*..
gi 1080718084 180 IRIFNRL 186
Cdd:cd00778 172 KEFYEDL 178
|
|
| ThrRS_core |
cd00771 |
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ... |
33-161 |
2.17e-12 |
|
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is responsible for the attachment of threonine to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain.
Pssm-ID: 238394 [Multi-domain] Cd Length: 298 Bit Score: 67.96 E-value: 2.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080718084 33 VAPGVYSWLPLGLRVMRRIEAICREEMASIGAQEVSFPALLASDPYKETGRWVEYGDNLFRLkdrKGVDMLLG------P 106
Cdd:cd00771 18 AGPGLPFWLPKGAIIRNELEDFLRELQRKRGYQEVETPIIYNKELWETSGHWDHYRENMFPF---EEEDEEYGlkpmncP 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1080718084 107 THEEMFtlmvKDLYSSYKDLPLCLYQIQNKYRDEARPR-AGILRGREFVMMDAYSF 161
Cdd:cd00771 95 GHCLIF----KSKPRSYRDLPLRLAEFGTVHRYEQSGAlHGLTRVRGFTQDDAHIF 146
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
49-227 |
1.65e-11 |
|
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: 64.06 E-value: 1.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080718084 49 RRIEAICREEMASIGAQEVSFPALLASDPYKETGRWVEYgdnLFRLKDRKGVDMLLGPTHEEMFTLMVKdlySSYKDLPL 128
Cdd:cd00768 3 SKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGHEPKD---LLPVGAENEEDLYLRPTLEPGLVRLFV---SHIRKLPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080718084 129 CLYQIQNKYRDEARPRaGILRGREFVMMDAYSFdVAQEGLDEAYQAQRDAYIRIFNRLGFDYAIVkamsgPMGGSRSEEF 208
Cdd:cd00768 77 RLAEIGPAFRNEGGRR-GLRRVREFTQLEGEVF-GEDGEEASEFEELIELTEELLRALGIKLDIV-----FVEKTPGEFS 149
|
170
....*....|....*....
gi 1080718084 209 LAVAANGEDTFVRSSGGYA 227
Cdd:cd00768 150 PGGAGPGFEIEVDHPEGRG 168
|
|
| ProRS_anticodon_zinc |
cd00862 |
ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and ... |
476-572 |
5.28e-11 |
|
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: 62.31 E-value: 5.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080718084 476 GLCWPREVAPYDVQVLATGKGTE----ILDEATRIASELAEAGLEVLLDDR-KASPGVKFADSEILGMPTSVVVG-RGLK 549
Cdd:cd00862 1 GLVLPPRVAPIQVVIVPIGIKDEkreeVLEAADELAERLKAAGIRVHVDDRdNYTPGWKFNDWELKGVPLRIEIGpRDLE 80
|
90 100
....*....|....*....|...
gi 1080718084 550 DGLVEVRDRSTGENRQVSVAEAV 572
Cdd:cd00862 81 KNTVVIVRRDTGEKKTVPLAELV 103
|
|
| PRK12444 |
PRK12444 |
threonyl-tRNA synthetase; Reviewed |
34-192 |
2.21e-08 |
|
threonyl-tRNA synthetase; Reviewed
Pssm-ID: 183530 [Multi-domain] Cd Length: 639 Bit Score: 57.07 E-value: 2.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080718084 34 APGVYSWLPLGLRVMRRIEAICREEMASIGAQEVSFPALLASDPYKETGRWVEYGDNL-FRLKDRKgvDMLLGPTHEEMF 112
Cdd:PRK12444 263 APGMPFYLPKGQIIRNELEAFLREIQKEYNYQEVRTPFMMNQELWERSGHWDHYKDNMyFSEVDNK--SFALKPMNCPGH 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080718084 113 TLMVKDLYSSYKDLPLCLYQIQNKYRDE-ARPRAGILRGREFVMMDAYSFdVAQEGLDEAYQAQRDAYIRIFNRLGFDYA 191
Cdd:PRK12444 341 MLMFKNKLHSYRELPIRMCEFGQVHRHEfSGALNGLLRVRTFCQDDAHLF-VTPDQIEDEIKSVMAQIDYVYKTFGFEYE 419
|
.
gi 1080718084 192 I 192
Cdd:PRK12444 420 V 420
|
|
| PRK03991 |
PRK03991 |
threonyl-tRNA synthetase; Validated |
417-581 |
3.79e-08 |
|
threonyl-tRNA synthetase; Validated
Pssm-ID: 235190 [Multi-domain] Cd Length: 613 Bit Score: 56.03 E-value: 3.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080718084 417 LARGIEIGhIFQLGKKYADALGLKVLDHNGKLVTVTM------GSyglgVSRAVAAIAEGT----CDEKGLCWPREVAPY 486
Cdd:PRK03991 426 LGRPIENP-TVQIDVENAERFGIKYVDENGEEKYPIIlhcsptGS----IERVIYALLEKAakeeEEGKVPMLPTWLSPT 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080718084 487 DVQVLATGKgtEILDEATRIASELAEAGLEVLLDDRKASPGVKFADSEILGMPTSVVVG-RGLKDGLVEVRDRSTGENRQ 565
Cdd:PRK03991 501 QVRVIPVSE--RHLDYAEEVADKLEAAGIRVDVDDRDESLGKKIRDAGKEWIPYVVVIGdKEMESGKLTVTIREESEKVE 578
|
170
....*....|....*.
gi 1080718084 566 VSVAEAVCAVLKEVRG 581
Cdd:PRK03991 579 MTLEELIERIKEETKG 594
|
|
| YbaK_like |
cd04332 |
YbaK-like. The YbaK family of deacylase domains includes the INS amino acid-editing domain of ... |
250-375 |
1.20e-07 |
|
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: 51.00 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080718084 250 EVVDTPDARTIESLVRIANevrpradrpWTGADTLKNVVFMVAHpdgtREPLAIGLPGDRDVDEKRLEAVLEPAVVEPFT 329
Cdd:cd04332 4 EYEHTPGAKTIEEAAEALG---------VPPGQIAKTLVLKDDK----GGLVLVVVPGDHELDLKKLAKALGAKKLRLAS 70
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1080718084 330 EEDFAANPQLVKGYIGPgaLGEDNSSKVryLVDPRVVTGTSWITGA 375
Cdd:cd04332 71 EEELEELTGCEPGGVGP--FGLKKGVPV--VVDESLLELEDVYVGA 112
|
|
| GlyRS_anticodon |
cd00858 |
GlyRS Glycyl-anticodon binding domain. GlyRS belongs to class II aminoacyl-tRNA synthetases ... |
480-580 |
2.70e-06 |
|
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: 46.78 E-value: 2.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080718084 480 PREVAPYDVQVLATGKGTEILDEATRIASELAEAGLEVLLDDRkASPGVKFADSEILGMPTSVVV-GRGLKDGLVEVRDR 558
Cdd:cd00858 21 PPALAPIKVAVLPLVKRDELVEIAKEISEELRELGFSVKYDDS-GSIGRRYARQDEIGTPFCVTVdFDTLEDGTVTIRER 99
|
90 100
....*....|....*....|..
gi 1080718084 559 STGENRQVSVAEAVCAVLKEVR 580
Cdd:cd00858 100 DSMRQVRVKIEELPSYLRELIR 121
|
|
| PRK12444 |
PRK12444 |
threonyl-tRNA synthetase; Reviewed |
479-580 |
5.25e-06 |
|
threonyl-tRNA synthetase; Reviewed
Pssm-ID: 183530 [Multi-domain] Cd Length: 639 Bit Score: 49.36 E-value: 5.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080718084 479 WPREVAPYDVQVLATGKGTEiLDEATRIASELAEAGLEVLLDDRKASPGVKFADSEILGMPTSVVVG-RGLKDGLVEVRD 557
Cdd:PRK12444 535 FPAWLAPVQVKVIPVSNAVH-VQYADEVADKLAQAGIRVERDERDEKLGYKIREAQMQKIPYVLVIGdKEMENGAVNVRK 613
|
90 100
....*....|....*....|...
gi 1080718084 558 RSTGENRQVSVAEAVCAVLKEVR 580
Cdd:PRK12444 614 YGEEKSEVIELDMFVESIKEEIK 636
|
|
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
457-579 |
6.77e-06 |
|
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: 48.58 E-value: 6.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080718084 457 GLGVSRAVAAIaegtcDEKGLcWPREVAPYDVQVLATGKGTEilDEATRIASELAEAGLEVLLDDRKASPG--VKFADSe 534
Cdd:COG0124 305 AIGLERLLLLL-----EELGL-LPAAEPPPDVYVVPLGEEAR--AEALKLAQELRAAGIRVELDLGGRKLKkqLKYADK- 375
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1080718084 535 iLGMPTSVVVG-RGLKDGLVEVRDRSTGENRQVSVAEAVcAVLKEV 579
Cdd:COG0124 376 -SGAPFVLILGeDELANGTVTLKDLATGEQETVPLDELV-EYLKEL 419
|
|
| PLN02908 |
PLN02908 |
threonyl-tRNA synthetase |
34-190 |
7.24e-06 |
|
threonyl-tRNA synthetase
Pssm-ID: 178496 [Multi-domain] Cd Length: 686 Bit Score: 49.00 E-value: 7.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080718084 34 APGVYSWLPLGLRVMRRIEAICREEMASIGAQEVSFPALLASDPYKETGRWVEYGDNLFRLKDRK---GVDMLLGPTHEE 110
Cdd:PLN02908 310 SPGSCFFLPHGARIYNKLMDFIREQYWERGYDEVITPNIYNMDLWETSGHAAHYKENMFVFEIEKqefGLKPMNCPGHCL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080718084 111 MFTLMVKdlysSYKDLPLCLYQIQNKYRDEAR-PRAGILRGREFVMMDAYSFDVAQEGLDEAyQAQRDAYIRIFNRLGFD 189
Cdd:PLN02908 390 MFAHRVR----SYRELPLRLADFGVLHRNELSgALTGLTRVRRFQQDDAHIFCREDQIKDEV-KGVLDFLDYVYEVFGFT 464
|
.
gi 1080718084 190 Y 190
Cdd:PLN02908 465 Y 465
|
|
| HisRS_anticodon |
cd00859 |
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases ... |
487-572 |
2.32e-05 |
|
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: 43.30 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080718084 487 DVQVLATGKGTeiLDEATRIASELAEAGLEVLLDDRKASPGVKFADSEILGMPTSVVVG-RGLKDGLVEVRDRSTGENRQ 565
Cdd:cd00859 3 DVYVVPLGEGA--LSEALELAEQLRDAGIKAEIDYGGRKLKKQFKYADRSGARFAVILGeDELAAGVVTVKDLETGEQET 80
|
....*..
gi 1080718084 566 VSVAEAV 572
Cdd:cd00859 81 VALDELV 87
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
417-469 |
5.75e-05 |
|
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: 43.94 E-value: 5.75e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1080718084 417 LARGIEIGHIFQLGKKYADALGLKVLDHNGKLVTVTMGSYG-LGVSRAVAAIAE 469
Cdd:pfam00587 126 LGKQRQTGTIQNDGFRLPRRLGIRYKDEDNESKFPYMIHRAgLGVERFLAAILE 179
|
|
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
483-579 |
2.02e-04 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 44.35 E-value: 2.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080718084 483 VAPYDVQVLATGKGTEILDEATRIASELAEAGLEVLLDDRKASPGVKFADSEILGMPTSVVVGrglKDGLVEVRDRSTGE 562
Cdd:PLN02734 568 VAPIKCTVFPLVQNQQLNAVAKVISKELTAAGISHKIDITGTSIGKRYARTDELGVPFAVTVD---SDGSVTIRERDSKD 644
|
90
....*....|....*..
gi 1080718084 563 NRQVSVAEaVCAVLKEV 579
Cdd:PLN02734 645 QVRVPVEE-VASVVKDL 660
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
45-153 |
2.04e-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: 43.36 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080718084 45 LRVMRRIEAICREEMASIGAQEVSFPALLASDPY--KETGrwvEYGDNLFRLKDRKGVDMLLGPtheEMfTLMVKDLYSS 122
Cdd:cd00773 2 AALRRYIEDTLREVFERYGYEEIDTPVFEYTELFlrKSGD---EVSKEMYRFKDKGGRDLALRP---DL-TAPVARAVAE 74
|
90 100 110
....*....|....*....|....*....|....
gi 1080718084 123 YKD---LPLCLYQIQNKYRDEaRPRAGilRGREF 153
Cdd:cd00773 75 NLLslpLPLKLYYIGPVFRYE-RPQKG--RYREF 105
|
|
| ThrRS_anticodon |
cd00860 |
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases ... |
496-572 |
2.71e-04 |
|
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: 40.18 E-value: 2.71e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1080718084 496 GTEILDEATRIASELAEAGLEVLLDDRKASPGVKFADSEILGMPTSVVVG-RGLKDGLVEVRDRSTGENRQVSVAEAV 572
Cdd:cd00860 10 TDEHLDYAKEVAKKLSDAGIRVEVDLRNEKLGKKIREAQLQKIPYILVVGdKEVETGTVSVRTRDGGDLGSMSLDEFI 87
|
|
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
33-161 |
3.70e-04 |
|
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: 43.48 E-value: 3.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080718084 33 VAPGVYSWLPLGLRVMRRIEAICREEMASIGAQEVSFPALLASDPYKETGRWVEYGDNLFRLKDrKGVDMLLG----PTH 108
Cdd:COG0441 259 VGPGLPFWHPKGAIIRRELEDYIREKHRKAGYQEVKTPHILDRELWETSGHWDHYRENMFPTES-DGEEYALKpmncPGH 337
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1080718084 109 EEMFTLMVKdlysSYKDLPLCLYQIQNKYRDEarPR---AGILRGREFVMMDAYSF 161
Cdd:COG0441 338 ILIYKSGLR----SYRDLPLRLAEFGTVHRYE--PSgalHGLMRVRGFTQDDAHIF 387
|
|
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
117-155 |
1.28e-03 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 41.65 E-value: 1.28e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1080718084 117 KDL-YSSYKDLPLCLYQIQNKYRDEARPRAGILRGREFVM 155
Cdd:PLN02734 264 RDLyYYNGGKLPFAAAQIGQAFRNEISPRQGLLRVREFTL 303
|
|
| PRK14938 |
PRK14938 |
Ser-tRNA(Thr) hydrolase; Provisional |
480-572 |
1.29e-03 |
|
Ser-tRNA(Thr) hydrolase; Provisional
Pssm-ID: 184902 [Multi-domain] Cd Length: 387 Bit Score: 41.37 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080718084 480 PREVAPYDVQVLATGKgtEILDEATRIASELAEAGLEVLLDDRKASPGVKFADSEILGMPTSVVVG-RGLKDGLVEVRDR 558
Cdd:PRK14938 269 PDWLNPIQVRILPVKK--DFLDFSIQVAERLRKEGIRVNVDDLDDSLGNKIRRAGTEWIPFVIIIGeREVKTSTLTVKIR 346
|
90
....*....|....
gi 1080718084 559 STGENRQVSVAEAV 572
Cdd:PRK14938 347 ANNEQKSMTVEELV 360
|
|
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
500-580 |
1.94e-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: 41.17 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080718084 500 LDEATRIASELAEAGLEVLLDDRKASPGVKFADSEILGMPTSVVVG-RGLKDGLVEVRDRSTGENRQVSVAEAVCAVLKE 578
Cdd:COG0441 552 ADYAKEVAKKLRAAGIRVEVDLRNEKIGYKIREAQLQKVPYMLVVGdKEVENGTVSVRRRGGGDLGTMSLDEFIARLKEE 631
|
..
gi 1080718084 579 VR 580
Cdd:COG0441 632 IR 633
|
|
| PRK03991 |
PRK03991 |
threonyl-tRNA synthetase; Validated |
114-193 |
4.02e-03 |
|
threonyl-tRNA synthetase; Validated
Pssm-ID: 235190 [Multi-domain] Cd Length: 613 Bit Score: 40.24 E-value: 4.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080718084 114 LMVKDLYSSYKDLPLCLYQI-QNKYRDEARPR-AGILRGREFVMMDAYSFDVAQEGLDEAYQAQRDAYIRIFNRLGFDYA 191
Cdd:PRK03991 295 LMLKDMTISYKNLPLKMYELsTYSFRLEQRGElVGLKRLRAFTMPDMHTLCKDMEQAMEEFEKQYEMILETGEDLGRDYE 374
|
..
gi 1080718084 192 IV 193
Cdd:PRK03991 375 VA 376
|
|
| |
