|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09194 |
PRK09194 |
prolyl-tRNA synthetase; Provisional |
78-506 |
1.03e-146 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 236405 [Multi-domain] Cd Length: 565 Bit Score: 432.20 E-value: 1.03e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139948914 78 LSRMFQPqNLREDqvlslegrASDLTCKSQRLMLQVGLILPASPGCYHLMPYTVRAVEKLVRVIDQEMQAIGGQKINMPS 157
Cdd:PRK09194 3 TSQLFLP-TLKET--------PADAEVISHQLLLRAGYIRKLASGIYTYLPLGLRVLRKIENIVREEMNKIGAQEVLMPA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139948914 158 LSPAELWRATSRWDLMGRELLRLRDRHGKEYCLGPTHEEAVTALVASQKKlSYKQLPLLLYQVTRKFRDEPRPRFGLLRG 237
Cdd:PRK09194 74 LQPAELWQESGRWEEYGPELLRLKDRHGRDFVLGPTHEEVITDLVRNEIK-SYKQLPLNLYQIQTKFRDEIRPRFGLMRG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139948914 238 REFYMKDMYTFDSSSEAAQETYGLVCDAYCRLFDRLGLQWMKARADVGSIGGTMSHEFQLPVDIGEDRLVVCPSCHFSAN 317
Cdd:PRK09194 153 REFIMKDAYSFHADEESLDETYDAMYQAYSRIFDRLGLDFRAVEADSGAIGGSASHEFMVLADSGEDTIVYSDESDYAAN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139948914 318 TE--------------------------ILDLSQK--------------------------------------------- 326
Cdd:PRK09194 233 IEkaealpppraaaeealekvdtpnaktIEELAEFlnvpaektvktllvkadgelvavlvrgdhelnevklenllgaapl 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139948914 327 -----------------------------------------------------------------------------ICP 329
Cdd:PRK09194 313 elateeeiraalgavpgflgpvglpkdvpiiadrsvadmsnfvvganeddyhyvgvnwgrdfpvpevadlrnvvegdPSP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139948914 330 DCQGPLTETKGIEVGHTFYLSTKYSSIFNALFTNAHGESLLAEMGCYGLGVTRILAAAIEVLSTEDCIRWPRLLAPYQVC 409
Cdd:PRK09194 393 DGGGTLKIARGIEVGHIFQLGTKYSEAMNATVLDENGKAQPLIMGCYGIGVSRLVAAAIEQNHDEKGIIWPKAIAPFDVH 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139948914 410 VIPPkkGSKETAATEIVEKLYDDIMEAvpqlrG-EVLLDDRtHLTIGNRLKDANKLGYPFVIIAGKRALEDpAHFEVWSQ 488
Cdd:PRK09194 473 IVPV--NMKDEEVKELAEKLYAELQAA-----GiEVLLDDR-KERPGVKFADADLIGIPHRIVVGDRGLAE-GIVEYKDR 543
|
570
....*....|....*...
gi 139948914 489 NTGEVVFLTKEGVMELLT 506
Cdd:PRK09194 544 RTGEKEEVPVDELVEFLK 561
|
|
| ProRS_core_prok |
cd00779 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
101-390 |
4.35e-146 |
|
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: 418.90 E-value: 4.35e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139948914 101 DLTCKSQRLMLQVGLILPASPGCYHLMPYTVRAVEKLVRVIDQEMQAIGGQKINMPSLSPAELWRATSRWDLMGRELLRL 180
Cdd:cd00779 1 DAEIISHKLLLRAGFIRQTSSGLYSWLPLGLRVLKKIENIIREEMNKIGAQEILMPILQPAELWKESGRWDAYGPELLRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139948914 181 RDRHGKEYCLGPTHEEAVTALVASQKKlSYKQLPLLLYQVTRKFRDEPRPRFGLLRGREFYMKDMYTFDSSSEAAQETYG 260
Cdd:cd00779 81 KDRHGKEFLLGPTHEEVITDLVANEIK-SYKQLPLNLYQIQTKFRDEIRPRFGLMRGREFLMKDAYSFDIDEESLEETYE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139948914 261 LVCDAYCRLFDRLGLQWMKARADVGSIGGTMSHEFQLPVdigedrlvvcpschfsanteildlsqkicpdcqgPLTETKG 340
Cdd:cd00779 160 KMYQAYSRIFKRLGLPFVKVEADSGAIGGSLSHEFHVLS----------------------------------PLKITKG 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 139948914 341 IEVGHTFYLSTKYSSIFNALFTNAHGESLLAEMGCYGLGVTRILAAAIEV 390
Cdd:cd00779 206 IEVGHIFQLGTKYSKALGATFLDENGKPKPLEMGCYGIGVSRLLAAIIEQ 255
|
|
| ProS |
COG0442 |
Prolyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Prolyl-tRNA ... |
106-505 |
2.25e-145 |
|
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: 428.81 E-value: 2.25e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139948914 106 SQRLMLQVGLILPASPGCYHLMPYTVRAVEKLVRVIDQEMQAIGGQKINMPSLSPAELWRATSRWDLMGRELLRLRDRHG 185
Cdd:COG0442 22 SHQLMLRAGLIRKLASGIYTYLPLGYRVLEKIEAIVREEMKRTGAQEVLMPLLQPAELWEESGRWEGFGPELARVTDRLE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139948914 186 KEYCLGPTHEEAVTALVASQKKlSYKQLPLLLYQVTRKFRDEPRPRFGLLRGREFYMKDMYTFDSSSEAAQETYGLVCDA 265
Cdd:COG0442 102 REFCLGPTHEEVITDLVRNEIK-SYRDLPLLLYQIQTKFRDEIRPRFGLLRTREFLMKDAYSFHATEEELDEEYQKMLDA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139948914 266 YCRLFDRLGLQWMKARADVGSIGGTMSHEFQLPVDIGEDRLVVCPSCHFSANTE-------------------------- 319
Cdd:COG0442 181 YERIFERLGLPVRAVEADSGAIGGSESHEFMVLADSGEDTIVYCDACDYAANIEkaealappaeraeptkeleavatpga 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139948914 320 --ILDLSQK----------------------------------------------------------------------- 326
Cdd:COG0442 261 ktIEEVAEFlgvpaektvktlvykadgelvavlvrgdhelneiklenllgaselelateeeieaalgavpgflgpvglgv 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139948914 327 -------------------------------------------------ICPDCQGPLTETKGIEVGHTFYLSTKYSSIF 357
Cdd:COG0442 341 pyiadrsvagmsnfvcganeddyhytnvnwgrdfpvdevadlrnvvegdPCPDCGGLLQDGRGIEVGHIFKLGTKYSKAM 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139948914 358 NALFTNAHGESLLAEMGCYGLGVTRILAAAIEVLSTEDCIRWPRLLAPYQVCVIPPkkGSKETAATEIVEKLYDDIMEAv 437
Cdd:COG0442 421 DATFLDENGKEQPVWMGCYGIGVTRLIAAAIEQHHDDKGIIWPPAIAPFQVVIVPI--NMKDEAVLEAAEELYAELKAA- 497
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 139948914 438 pqlrG-EVLLDDRTHlTIGNRLKDANKLGYPFVIIAGKRALEDPAhFEVWSQNTGEVVFLTKEGVMELL 505
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 ... |
101-506 |
5.20e-115 |
|
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: 351.04 E-value: 5.20e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139948914 101 DLTCKSQRLMLQVGLILPASPGCYHLMPYTVRAVEKLVRVIDQEMQAIGGQKINMPSLSPAELWRATSRWDLMGRELLRL 180
Cdd:TIGR00409 17 DAEVKSHQLLLRAGFIRRLGSGLYNWLPLGLRVLKKVENIVREEMNKDGAIEVLLPALQPAELWQESGRWDTYGPELLRL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139948914 181 RDRHGKEYCLGPTHEEAVTALVASQKKlSYKQLPLLLYQVTRKFRDEPRPRFGLLRGREFYMKDMYTFDSSSEAAQETYG 260
Cdd:TIGR00409 97 KDRKGREFVLGPTHEEVITDLARNEIK-SYKQLPLNLYQIQTKFRDEIRPRFGLMRGREFIMKDAYSFHSDEESLDATYQ 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139948914 261 LVCDAYCRLFDRLGLQWMKARADVGSIGGTMSHEFQLPVDIGEDRLVVCPSCHFSANTEI-------------------- 320
Cdd:TIGR00409 176 KMYQAYSNIFSRLGLDFRPVQADSGAIGGSASHEFMVLAESGEDTIVYSDESDYAANIELaealapgernaptaeldkvd 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139948914 321 -------------LDLS------------------------------------------------------QKI------ 327
Cdd:TIGR00409 256 tpntktiaelvecFNLPaekvvktllvkavdkseplvallvrgdhelnevkapnlllvaqvlelateeeifQKIasgpgs 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139948914 328 ------------------------------------------------------------CPDCQGPLTETKGIEVGHTF 347
Cdd:TIGR00409 336 lgpvninggipvlidqtvalmsdfaaganaddkhyfnvnwdrdvaipevadirkvkegdpSPDGQGTLKIARGIEVGHIF 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139948914 348 YLSTKYSSIFNALFTNAHGESLLAEMGCYGLGVTRILAAAIEVLSTEDCIRWPRLLAPYQVCVIPPKkgSKETAATEIVE 427
Cdd:TIGR00409 416 QLGTKYSEALKATFLDENGKNQFMTMGCYGIGVSRLVSAIAEQHHDERGIIWPKAIAPYDVVIVVMN--MKDEEQQQLAE 493
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 139948914 428 KLYDDIMEAVPqlrgEVLLDDRTHlTIGNRLKDANKLGYPFVIIAGKRALEDpAHFEVWSQNTGEVVFLTKEGVMELLT 506
Cdd:TIGR00409 494 ELYSELLAQGV----DVLLDDRNE-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 ... |
179-390 |
1.07e-19 |
|
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely threonyl-tRNA members.
Pssm-ID: 395469 [Multi-domain] Cd Length: 181 Bit Score: 86.70 E-value: 1.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139948914 179 RLRDRHGKEYCLGPTHEEAVTALVaSQKKLSYKQLPLLLYQVTRKFRDEPRPRF-GLLRGREFYMKDMYTFDSSSEAAQE 257
Cdd:pfam00587 2 KVEDENGDELALKPTNEPGHTLLF-REEGLRSKDLPLKLAQFGTCFRHEASGDTrGLIRVRQFHQDDAHIFHAPGQSPDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139948914 258 TYGLVCDAYcRLFDRLGLQWMKARADvgsiggtmSHEFQLPVDIGEDRLVVCPSChfsanteildlsqkicpdcqgplte 337
Cdd:pfam00587 81 LEDYIKLID-RVYSRLGLEVRVVRLS--------NSDGSAFYGPKLDFEVVFPSL------------------------- 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 139948914 338 TKGIEVGHTFYLSTKYSSIFNALFTNAHGESLLAEMGCYG-LGVTRILAAAIEV 390
Cdd:pfam00587 127 GKQRQTGTIQNDGFRLPRRLGIRYKDEDNESKFPYMIHRAgLGVERFLAAILEN 180
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09194 |
PRK09194 |
prolyl-tRNA synthetase; Provisional |
78-506 |
1.03e-146 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 236405 [Multi-domain] Cd Length: 565 Bit Score: 432.20 E-value: 1.03e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139948914 78 LSRMFQPqNLREDqvlslegrASDLTCKSQRLMLQVGLILPASPGCYHLMPYTVRAVEKLVRVIDQEMQAIGGQKINMPS 157
Cdd:PRK09194 3 TSQLFLP-TLKET--------PADAEVISHQLLLRAGYIRKLASGIYTYLPLGLRVLRKIENIVREEMNKIGAQEVLMPA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139948914 158 LSPAELWRATSRWDLMGRELLRLRDRHGKEYCLGPTHEEAVTALVASQKKlSYKQLPLLLYQVTRKFRDEPRPRFGLLRG 237
Cdd:PRK09194 74 LQPAELWQESGRWEEYGPELLRLKDRHGRDFVLGPTHEEVITDLVRNEIK-SYKQLPLNLYQIQTKFRDEIRPRFGLMRG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139948914 238 REFYMKDMYTFDSSSEAAQETYGLVCDAYCRLFDRLGLQWMKARADVGSIGGTMSHEFQLPVDIGEDRLVVCPSCHFSAN 317
Cdd:PRK09194 153 REFIMKDAYSFHADEESLDETYDAMYQAYSRIFDRLGLDFRAVEADSGAIGGSASHEFMVLADSGEDTIVYSDESDYAAN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139948914 318 TE--------------------------ILDLSQK--------------------------------------------- 326
Cdd:PRK09194 233 IEkaealpppraaaeealekvdtpnaktIEELAEFlnvpaektvktllvkadgelvavlvrgdhelnevklenllgaapl 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139948914 327 -----------------------------------------------------------------------------ICP 329
Cdd:PRK09194 313 elateeeiraalgavpgflgpvglpkdvpiiadrsvadmsnfvvganeddyhyvgvnwgrdfpvpevadlrnvvegdPSP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139948914 330 DCQGPLTETKGIEVGHTFYLSTKYSSIFNALFTNAHGESLLAEMGCYGLGVTRILAAAIEVLSTEDCIRWPRLLAPYQVC 409
Cdd:PRK09194 393 DGGGTLKIARGIEVGHIFQLGTKYSEAMNATVLDENGKAQPLIMGCYGIGVSRLVAAAIEQNHDEKGIIWPKAIAPFDVH 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139948914 410 VIPPkkGSKETAATEIVEKLYDDIMEAvpqlrG-EVLLDDRtHLTIGNRLKDANKLGYPFVIIAGKRALEDpAHFEVWSQ 488
Cdd:PRK09194 473 IVPV--NMKDEEVKELAEKLYAELQAA-----GiEVLLDDR-KERPGVKFADADLIGIPHRIVVGDRGLAE-GIVEYKDR 543
|
570
....*....|....*...
gi 139948914 489 NTGEVVFLTKEGVMELLT 506
Cdd:PRK09194 544 RTGEKEEVPVDELVEFLK 561
|
|
| ProRS_core_prok |
cd00779 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
101-390 |
4.35e-146 |
|
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: 418.90 E-value: 4.35e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139948914 101 DLTCKSQRLMLQVGLILPASPGCYHLMPYTVRAVEKLVRVIDQEMQAIGGQKINMPSLSPAELWRATSRWDLMGRELLRL 180
Cdd:cd00779 1 DAEIISHKLLLRAGFIRQTSSGLYSWLPLGLRVLKKIENIIREEMNKIGAQEILMPILQPAELWKESGRWDAYGPELLRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139948914 181 RDRHGKEYCLGPTHEEAVTALVASQKKlSYKQLPLLLYQVTRKFRDEPRPRFGLLRGREFYMKDMYTFDSSSEAAQETYG 260
Cdd:cd00779 81 KDRHGKEFLLGPTHEEVITDLVANEIK-SYKQLPLNLYQIQTKFRDEIRPRFGLMRGREFLMKDAYSFDIDEESLEETYE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139948914 261 LVCDAYCRLFDRLGLQWMKARADVGSIGGTMSHEFQLPVdigedrlvvcpschfsanteildlsqkicpdcqgPLTETKG 340
Cdd:cd00779 160 KMYQAYSRIFKRLGLPFVKVEADSGAIGGSLSHEFHVLS----------------------------------PLKITKG 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 139948914 341 IEVGHTFYLSTKYSSIFNALFTNAHGESLLAEMGCYGLGVTRILAAAIEV 390
Cdd:cd00779 206 IEVGHIFQLGTKYSKALGATFLDENGKPKPLEMGCYGIGVSRLLAAIIEQ 255
|
|
| ProS |
COG0442 |
Prolyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Prolyl-tRNA ... |
106-505 |
2.25e-145 |
|
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: 428.81 E-value: 2.25e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139948914 106 SQRLMLQVGLILPASPGCYHLMPYTVRAVEKLVRVIDQEMQAIGGQKINMPSLSPAELWRATSRWDLMGRELLRLRDRHG 185
Cdd:COG0442 22 SHQLMLRAGLIRKLASGIYTYLPLGYRVLEKIEAIVREEMKRTGAQEVLMPLLQPAELWEESGRWEGFGPELARVTDRLE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139948914 186 KEYCLGPTHEEAVTALVASQKKlSYKQLPLLLYQVTRKFRDEPRPRFGLLRGREFYMKDMYTFDSSSEAAQETYGLVCDA 265
Cdd:COG0442 102 REFCLGPTHEEVITDLVRNEIK-SYRDLPLLLYQIQTKFRDEIRPRFGLLRTREFLMKDAYSFHATEEELDEEYQKMLDA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139948914 266 YCRLFDRLGLQWMKARADVGSIGGTMSHEFQLPVDIGEDRLVVCPSCHFSANTE-------------------------- 319
Cdd:COG0442 181 YERIFERLGLPVRAVEADSGAIGGSESHEFMVLADSGEDTIVYCDACDYAANIEkaealappaeraeptkeleavatpga 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139948914 320 --ILDLSQK----------------------------------------------------------------------- 326
Cdd:COG0442 261 ktIEEVAEFlgvpaektvktlvykadgelvavlvrgdhelneiklenllgaselelateeeieaalgavpgflgpvglgv 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139948914 327 -------------------------------------------------ICPDCQGPLTETKGIEVGHTFYLSTKYSSIF 357
Cdd:COG0442 341 pyiadrsvagmsnfvcganeddyhytnvnwgrdfpvdevadlrnvvegdPCPDCGGLLQDGRGIEVGHIFKLGTKYSKAM 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139948914 358 NALFTNAHGESLLAEMGCYGLGVTRILAAAIEVLSTEDCIRWPRLLAPYQVCVIPPkkGSKETAATEIVEKLYDDIMEAv 437
Cdd:COG0442 421 DATFLDENGKEQPVWMGCYGIGVTRLIAAAIEQHHDDKGIIWPPAIAPFQVVIVPI--NMKDEAVLEAAEELYAELKAA- 497
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 139948914 438 pqlrG-EVLLDDRTHlTIGNRLKDANKLGYPFVIIAGKRALEDPAhFEVWSQNTGEVVFLTKEGVMELL 505
Cdd:COG0442 498 ----GiDVLLDDRDE-RPGVKFADAELIGIPLRIVIGPRDLEEGQ-VEVKRRDTGEKEEVPLDELVETV 560
|
|
| PRK12325 |
PRK12325 |
prolyl-tRNA synthetase; Provisional |
78-507 |
6.21e-122 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 237059 [Multi-domain] Cd Length: 439 Bit Score: 364.57 E-value: 6.21e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139948914 78 LSRMFQPqNLREDqvlslegrASDLTCKSQRLMLQVGLILPASPGCYHLMPYTVRAVEKLVRVIDQEMQAIGGQKINMPS 157
Cdd:PRK12325 3 LSRYFLP-TLKEN--------PKEAEIVSHRLMLRAGMIRQQAAGIYSWLPLGLKVLKKIENIVREEQNRAGAIEILMPT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139948914 158 LSPAELWRATSRWDLMGRELLRLRDRHGKEYCLGPTHEEAVTALVASQKKlSYKQLPLLLYQVTRKFRDEPRPRFGLLRG 237
Cdd:PRK12325 74 IQPADLWRESGRYDAYGKEMLRIKDRHDREMLYGPTNEEMITDIFRSYVK-SYKDLPLNLYHIQWKFRDEIRPRFGVMRG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139948914 238 REFYMKDMYTFDSSSEAAQETYGLVCDAYCRLFDRLGLQWMKARADVGSIGGTMSHEFQLPVDIGED------RLVVCPS 311
Cdd:PRK12325 153 REFLMKDAYSFDLDEEGARHSYNRMFVAYLRTFARLGLKAIPMRADTGPIGGDLSHEFIILAETGEStvfydkDFLDLLV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139948914 312 CHFSANTEILDLS------------------QKICPD-CQGPLTETKGIEVGHTFYLSTKYSSIFNALFTNAHGESLLAE 372
Cdd:PRK12325 233 PGEDIDFDVADLQpivdewtslyaateemhdEAAFAAvPEERRLSARGIEVGHIFYFGTKYSEPMNAKVQGPDGKEVPVH 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139948914 373 MGCYGLGVTRILAAAIEVLSTEDCIRWPRLLAPYQVCVIPPKKGSKETaaTEIVEKLYDDIMEAvpqlRGEVLLDDRTHl 452
Cdd:PRK12325 313 MGSYGIGVSRLVAAIIEASHDDKGIIWPESVAPFKVGIINLKQGDEAC--DAACEKLYAALSAA----GIDVLYDDTDE- 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 139948914 453 TIGNRLKDANKLGYPFVIIAGKRALEDpAHFEVWSQNTGEVVFLTKEGVMELLTG 507
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 ... |
101-506 |
5.20e-115 |
|
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: 351.04 E-value: 5.20e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139948914 101 DLTCKSQRLMLQVGLILPASPGCYHLMPYTVRAVEKLVRVIDQEMQAIGGQKINMPSLSPAELWRATSRWDLMGRELLRL 180
Cdd:TIGR00409 17 DAEVKSHQLLLRAGFIRRLGSGLYNWLPLGLRVLKKVENIVREEMNKDGAIEVLLPALQPAELWQESGRWDTYGPELLRL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139948914 181 RDRHGKEYCLGPTHEEAVTALVASQKKlSYKQLPLLLYQVTRKFRDEPRPRFGLLRGREFYMKDMYTFDSSSEAAQETYG 260
Cdd:TIGR00409 97 KDRKGREFVLGPTHEEVITDLARNEIK-SYKQLPLNLYQIQTKFRDEIRPRFGLMRGREFIMKDAYSFHSDEESLDATYQ 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139948914 261 LVCDAYCRLFDRLGLQWMKARADVGSIGGTMSHEFQLPVDIGEDRLVVCPSCHFSANTEI-------------------- 320
Cdd:TIGR00409 176 KMYQAYSNIFSRLGLDFRPVQADSGAIGGSASHEFMVLAESGEDTIVYSDESDYAANIELaealapgernaptaeldkvd 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139948914 321 -------------LDLS------------------------------------------------------QKI------ 327
Cdd:TIGR00409 256 tpntktiaelvecFNLPaekvvktllvkavdkseplvallvrgdhelnevkapnlllvaqvlelateeeifQKIasgpgs 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139948914 328 ------------------------------------------------------------CPDCQGPLTETKGIEVGHTF 347
Cdd:TIGR00409 336 lgpvninggipvlidqtvalmsdfaaganaddkhyfnvnwdrdvaipevadirkvkegdpSPDGQGTLKIARGIEVGHIF 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139948914 348 YLSTKYSSIFNALFTNAHGESLLAEMGCYGLGVTRILAAAIEVLSTEDCIRWPRLLAPYQVCVIPPKkgSKETAATEIVE 427
Cdd:TIGR00409 416 QLGTKYSEALKATFLDENGKNQFMTMGCYGIGVSRLVSAIAEQHHDERGIIWPKAIAPYDVVIVVMN--MKDEEQQQLAE 493
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 139948914 428 KLYDDIMEAVPqlrgEVLLDDRTHlTIGNRLKDANKLGYPFVIIAGKRALEDpAHFEVWSQNTGEVVFLTKEGVMELLT 506
Cdd:TIGR00409 494 ELYSELLAQGV----DVLLDDRNE-RAGVKFADSELIGIPLRVVVGKKNLDN-GEIEVKKRRNGEKQLIKKDELVECLE 566
|
|
| ProRS_core |
cd00772 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
101-389 |
1.16e-37 |
|
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: 139.04 E-value: 1.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139948914 101 DLTCKSQRLMLQVGLI--LPASpGCYHLMPYTVRAVEKLVRVIDQEMQAIGGQKINMPSLSPAELWRATSRWDLMG-REL 177
Cdd:cd00772 1 DASEKSLEHIGKAELAdqGPGR-GIINFLPLAKAILDKIENVLDKMFKEHGAQNALFPFFILASFLEKEAEHDEGFsKEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139948914 178 LRLRDRHGKE----YCLGPTHEEAVTALVASQKKlSYKQLPLLLYQVTRKFRDEPRPRFGLLRGREFYMKDMYTFDSSSE 253
Cdd:cd00772 80 AVFKDAGDEEleedFALRPTLEENIGEIAAKFIK-SWKDLPQHLNQIGNKFRDEIRPRFGFLRAREFIMKDGHSAHADAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139948914 254 AAQETYGLVCDAYCRLFDRLG-LQWMKARADVGS--IGGTMSHEFQLPVDIGedrlvvcpschfsanteildlsqkicpd 330
Cdd:cd00772 159 EADEEFLNMLSAYAEIARDLAaIDFIEGEADEGAkfAGASKSREFEALMEDG---------------------------- 210
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 139948914 331 cqgpltETKGIEVGHTFYLSTKYSSIFNALFTNAHGESLLAEMGCYGLGVTRILAAAIE 389
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 ... |
135-386 |
4.77e-21 |
|
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: 92.07 E-value: 4.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139948914 135 EKLVRVIDQEMQAIGGQKINMPSLSPAELWRATSRWDLMGRELLRLRDR----HGKEYCLGPTHEEAVTAlVASQKKLSY 210
Cdd:cd00670 6 RALERFLDDRMAEYGYQEILFPFLAPTVLFFKGGHLDGYRKEMYTFEDKgrelRDTDLVLRPAACEPIYQ-IFSGEILSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139948914 211 KQLPLLLYQVTRKFRDEPRPRFGLLRGREFYMKDMYTFDSSSEAAQETYGLVcDAYCRLFDRLGLQWmkaRADVGSIGgt 290
Cdd:cd00670 85 RALPLRLDQIGPCFRHEPSGRRGLMRVREFRQVEYVVFGEPEEAEEERREWL-ELAEEIARELGLPV---RVVVADDP-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139948914 291 mshEFQLPVDIGEDRlvvcpscHFSANTEILDLSqkicPDCQGplteTKGIEVGHTFYLSTKYSSIFNalfTNAHGESLL 370
Cdd:cd00670 159 ---FFGRGGKRGLDA-------GRETVVEFELLL----PLPGR----AKETAVGSANVHLDHFGASFK---IDEDGGGRA 217
|
250
....*....|....*.
gi 139948914 371 AEMGCYGLGVTRILAA 386
Cdd:cd00670 218 HTGCGGAGGEERLVLA 233
|
|
| ProRS_anticodon_short |
cd00861 |
ProRS Prolyl-anticodon binding domain, short version found predominantly in bacteria. ProRS ... |
405-506 |
6.14e-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: 84.56 E-value: 6.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139948914 405 PYQVCVIPPKKGSkeTAATEIVEKLYDDIMEAvpqlRGEVLLDDRThLTIGNRLKDANKLGYPFVIIAGKRALEDPaHFE 484
Cdd:cd00861 1 PFDVVIIPMNMKD--EVQQELAEKLYAELQAA----GVDVLLDDRN-ERPGVKFADADLIGIPYRIVVGKKSAAEG-IVE 72
|
90 100
....*....|....*....|..
gi 139948914 485 VWSQNTGEVVFLTKEGVMELLT 506
Cdd:cd00861 73 IKVRKTGEKEEISIDELLEFLQ 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 ... |
179-390 |
1.07e-19 |
|
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely threonyl-tRNA members.
Pssm-ID: 395469 [Multi-domain] Cd Length: 181 Bit Score: 86.70 E-value: 1.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139948914 179 RLRDRHGKEYCLGPTHEEAVTALVaSQKKLSYKQLPLLLYQVTRKFRDEPRPRF-GLLRGREFYMKDMYTFDSSSEAAQE 257
Cdd:pfam00587 2 KVEDENGDELALKPTNEPGHTLLF-REEGLRSKDLPLKLAQFGTCFRHEASGDTrGLIRVRQFHQDDAHIFHAPGQSPDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139948914 258 TYGLVCDAYcRLFDRLGLQWMKARADvgsiggtmSHEFQLPVDIGEDRLVVCPSChfsanteildlsqkicpdcqgplte 337
Cdd:pfam00587 81 LEDYIKLID-RVYSRLGLEVRVVRLS--------NSDGSAFYGPKLDFEVVFPSL------------------------- 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 139948914 338 TKGIEVGHTFYLSTKYSSIFNALFTNAHGESLLAEMGCYG-LGVTRILAAAIEV 390
Cdd:pfam00587 127 GKQRQTGTIQNDGFRLPRRLGIRYKDEDNESKFPYMIHRAgLGVERFLAAILEN 180
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
135-383 |
2.31e-14 |
|
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: 72.15 E-value: 2.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139948914 135 EKLVRVIDQEMQAIGGQKINMPSLSPAELWRATSRWdlmGRELLRLRDRHGKEYCLGPTHEEAVTALVASQKKlsykQLP 214
Cdd:cd00768 3 SKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGHE---PKDLLPVGAENEEDLYLRPTLEPGLVRLFVSHIR----KLP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139948914 215 LLLYQVTRKFRDEPRPRfGLLRGREFYMKDMYTFDSSSEAAQETYGLVcDAYCRLFDRLGLQWmKARADVGSIGgtmshE 294
Cdd:cd00768 76 LRLAEIGPAFRNEGGRR-GLRRVREFTQLEGEVFGEDGEEASEFEELI-ELTEELLRALGIKL-DIVFVEKTPG-----E 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139948914 295 FQLPvdigedrlvvcpscHFSANTEILDLSQkicpdcqgpltETKGIEVGHTFYLSTKYSSIFNALFTNAHGESLLAEMG 374
Cdd:cd00768 148 FSPG--------------GAGPGFEIEVDHP-----------EGRGLEIGSGGYRQDEQARAADLYFLDEALEYRYPPTI 202
|
....*....
gi 139948914 375 CYGLGVTRI 383
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 ... |
122-388 |
2.67e-12 |
|
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: 66.85 E-value: 2.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139948914 122 GCYHLMPYTVRAVEKLVRVIDQEMQAIGGQKINMPSLSPAelwratsrwDLMGRELLRLRD---------RHGKE----- 187
Cdd:cd00778 23 GCMVFRPYGYAIWENIQKILDKEIKETGHENVYFPLLIPE---------SELEKEKEHIEGfapevawvtHGGLEeleep 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139948914 188 YCLGPTHEEAVTALVASQKKlSYKQLPLLLYQVTRKFRDE---PRPrfgLLRGREFYMKDMYT-FDSSSEAAQETYGLVc 263
Cdd:cd00778 94 LALRPTSETAIYPMFSKWIR-SYRDLPLKINQWVNVFRWEtktTRP---FLRTREFLWQEGHTaHATEEEAEEEVLQIL- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139948914 264 DAYCRLFDRLglqwmkaradvgsiggtmsheFQLPVDIGE----DRlvvcpschF--SANTEILDlsqKICPDcqGplte 337
Cdd:cd00778 169 DLYKEFYEDL---------------------LAIPVVKGRktewEK--------FagADYTYTIE---AMMPD--G---- 210
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 139948914 338 tKGIEVGHTFYLSTKYSSIFNALFTNAHGESLLAEMGCYGLGvTRILAAAI 388
Cdd:cd00778 211 -RALQSGTSHNLGQNFSKAFDIKYQDKDGQKEYVHQTSWGIS-TRLIGAII 259
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
407-479 |
2.00e-07 |
|
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: 48.74 E-value: 2.00e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 139948914 407 QVCVIPPkkGSKETAATEIVEKLYDDIMEAvpqlRGEVLLDDRtHLTIGNRLKDANKLGYPFVIIAGKRALED 479
Cdd:pfam03129 1 QVVVIPL--GEKAEELEEYAQKLAEELRAA----GIRVELDDR-NESIGKKFRRADLIGIPFALVVGEKELEE 66
|
|
| HGTP_anticodon |
cd00738 |
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ... |
405-505 |
2.65e-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: 45.85 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139948914 405 PYQVCVIPPKKGSKEtaATEIVEKLYDDIMEAvpqlRGEVLLDDRTHlTIGNRLKDANKLGYPFVIIAGKRALEDpAHFE 484
Cdd:cd00738 1 PIDVAIVPLTDPRVE--AREYAQKLLNALLAN----GIRVLYDDRER-KIGKKFREADLRGVPFAVVVGEDELEN-GKVT 72
|
90 100
....*....|....*....|.
gi 139948914 485 VWSQNTGEVVFLTKEGVMELL 505
Cdd:cd00738 73 VKSRDTGESETLHVDELPEFL 93
|
|
| PRK03991 |
PRK03991 |
threonyl-tRNA synthetase; Validated |
208-248 |
6.87e-05 |
|
threonyl-tRNA synthetase; Validated
Pssm-ID: 235190 [Multi-domain] Cd Length: 613 Bit Score: 45.63 E-value: 6.87e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 139948914 208 LSYKQLPLLLYQVTRK-FRDEPRPRF-GLLRGREFYMKDMYTF 248
Cdd:PRK03991 302 ISYKNLPLKMYELSTYsFRLEQRGELvGLKRLRAFTMPDMHTL 344
|
|
| ThrRS_anticodon |
cd00860 |
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases ... |
405-478 |
1.78e-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: 40.56 E-value: 1.78e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 139948914 405 PYQVCVIPPKKgSKETAATEIVEKLYDDIMEAVPQLRGEvllddrthlTIGNRLKDANKLGYPFVIIAGKRALE 478
Cdd:cd00860 1 PVQVVVIPVTD-EHLDYAKEVAKKLSDAGIRVEVDLRNE---------KLGKKIREAQLQKIPYILVVGDKEVE 64
|
|
| ThrRS_core |
cd00771 |
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ... |
136-257 |
3.07e-04 |
|
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: 42.92 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139948914 136 KLVRVIDQEMQAIGGQKINMPSLSPAELWRATSRWDLMGRELLRLrDRHGKEYCLGPT----HeeavtALVASQKKLSYK 211
Cdd:cd00771 35 ELEDFLRELQRKRGYQEVETPIIYNKELWETSGHWDHYRENMFPF-EEEDEEYGLKPMncpgH-----CLIFKSKPRSYR 108
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 139948914 212 QLPLLLYQVTRKFRDEPRPRF-GLLRGREFYMKDMYTFDSSSEAAQE 257
Cdd:cd00771 109 DLPLRLAEFGTVHRYEQSGALhGLTRVRGFTQDDAHIFCTPDQIKEE 155
|
|
| |
