|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09194 |
PRK09194 |
prolyl-tRNA synthetase; Provisional |
1-571 |
0e+00 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 236405 [Multi-domain] Cd Length: 565 Bit Score: 1122.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 1 MRTSQYLLSTLKETPADAEVISHQLMLRAGMIRKLASGLYTWLPTGVRVLKKVENIVREEMNNAGAIEVSMPVVQPADLW 80
Cdd:PRK09194 1 MRTSQLFLPTLKETPADAEVISHQLLLRAGYIRKLASGIYTYLPLGLRVLRKIENIVREEMNKIGAQEVLMPALQPAELW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 81 QESGRWEQYGPELLRFVDRGERPFVLGPTHEEVITDLIRNELSSYKQLPLNFFQIQTKFRDEVRPRFGVMRSREFLMKDA 160
Cdd:PRK09194 81 QESGRWEEYGPELLRLKDRHGRDFVLGPTHEEVITDLVRNEIKSYKQLPLNLYQIQTKFRDEIRPRFGLMRGREFIMKDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 161 YSFHTSQESLQETYDKMYEAYSKIFSRMGLDFRAVQADTGSIGGSASHEFQVLAQSGEDDVIFSDSSDYAANIEFAEALA 240
Cdd:PRK09194 161 YSFHADEESLDETYDAMYQAYSRIFDRLGLDFRAVEADSGAIGGSASHEFMVLADSGEDTIVYSDESDYAANIEKAEALP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 241 PkaPRAAATEEMTLVDTPHAKTIAELVEQFNLPVEKTVKTLLVKSTEgsayPLVALLVRGDHELNEVKAEKLPQVAsPLT 320
Cdd:PRK09194 241 P--PRAAAEEALEKVDTPNAKTIEELAEFLNVPAEKTVKTLLVKADG----ELVAVLVRGDHELNEVKLENLLGAA-PLE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 321 FATEAEIRAVVNAGPGSLGPVNMP--VPVVIDRTVAAMSDFAAGANIDGKHYFGINWDRDVATPEVADIRNVVAGDPSPD 398
Cdd:PRK09194 314 LATEEEIRAALGAVPGFLGPVGLPkdVPIIADRSVADMSNFVVGANEDDYHYVGVNWGRDFPVPEVADLRNVVEGDPSPD 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 399 GQGTLMIKRGIEVGHIFQLGDKYSRALNAAVQGEDGRNQILTMGCYGIGVTRVVAAAIEQNYDERGIVWPDNIAPFQVAI 478
Cdd:PRK09194 394 GGGTLKIARGIEVGHIFQLGTKYSEAMNATVLDENGKAQPLIMGCYGIGVSRLVAAAIEQNHDEKGIIWPKAIAPFDVHI 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 479 LPMNMhKSYRVQELAEKLYSELRAQGIEVLMDDRKERPGVMFADMELIGIPHTVVIGDRNLDSDDIEYKYRRSGEKQMIK 558
Cdd:PRK09194 474 VPVNM-KDEEVKELAEKLYAELQAAGIEVLLDDRKERPGVKFADADLIGIPHRIVVGDRGLAEGIVEYKDRRTGEKEEVP 552
|
570
....*....|...
gi 503934731 559 TGDILDYLVKAIK 571
Cdd:PRK09194 553 VDELVEFLKALKK 565
|
|
| ProS |
COG0442 |
Prolyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Prolyl-tRNA ... |
1-570 |
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: 1040.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 1 MRTSQYLLSTLKETPADAEVISHQLMLRAGMIRKLASGLYTWLPTGVRVLKKVENIVREEMNNAGAIEVSMPVVQPADLW 80
Cdd:COG0442 1 MRASKLFIPTLKERPADAEVWSHQLMLRAGLIRKLASGIYTYLPLGYRVLEKIEAIVREEMKRTGAQEVLMPLLQPAELW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 81 QESGRWEQYGPELLRFVDRGERPFVLGPTHEEVITDLIRNELSSYKQLPLNFFQIQTKFRDEVRPRFGVMRSREFLMKDA 160
Cdd:COG0442 81 EESGRWEGFGPELARVTDRLEREFCLGPTHEEVITDLVRNEIKSYRDLPLLLYQIQTKFRDEIRPRFGLLRTREFLMKDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 161 YSFHTSQESLQETYDKMYEAYSKIFSRMGLDFRAVQADTGSIGGSASHEFQVLAQSGEDDVIFSDSSDYAANIEFAEALA 240
Cdd:COG0442 161 YSFHATEEELDEEYQKMLDAYERIFERLGLPVRAVEADSGAIGGSESHEFMVLADSGEDTIVYCDACDYAANIEKAEALA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 241 PKAPRAAATEEMTLVDTPHAKTIAELVEQFNLPVEKTVKTLLVKSTEGsaypLVALLVRGDHELNEVKAEKLPQvASPLT 320
Cdd:COG0442 241 PPAERAEPTKELEAVATPGAKTIEEVAEFLGVPAEKTVKTLVYKADGE----LVAVLVRGDHELNEIKLENLLG-ASELE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 321 FATEAEIRAVVNAGPGSLGPVNMPVPVVIDRTVAAMSDFAAGANIDGKHYFGINWDRDVATPEVADIRNVVAGDPSPDGQ 400
Cdd:COG0442 316 LATEEEIEAALGAVPGFLGPVGLGVPYIADRSVAGMSNFVCGANEDDYHYTNVNWGRDFPVDEVADLRNVVEGDPCPDCG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 401 GTLMIKRGIEVGHIFQLGDKYSRALNAAVQGEDGRNQILTMGCYGIGVTRVVAAAIEQNYDERGIVWPDNIAPFQVAILP 480
Cdd:COG0442 396 GLLQDGRGIEVGHIFKLGTKYSKAMDATFLDENGKEQPVWMGCYGIGVTRLIAAAIEQHHDDKGIIWPPAIAPFQVVIVP 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 481 MNMhKSYRVQELAEKLYSELRAQGIEVLMDDRKERPGVMFADMELIGIPHTVVIGDRNLDSDDIEYKYRRSGEKQMIKTG 560
Cdd:COG0442 476 INM-KDEAVLEAAEELYAELKAAGIDVLLDDRDERPGVKFADAELIGIPLRIVIGPRDLEEGQVEVKRRDTGEKEEVPLD 554
|
570
....*....|
gi 503934731 561 DILDYLVKAI 570
Cdd:COG0442 555 ELVETVKELL 564
|
|
| proS_fam_II |
TIGR00409 |
prolyl-tRNA synthetase, family II; Prolyl-tRNA synthetase is a class II tRNA synthetase and is ... |
1-568 |
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: 976.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 1 MRTSQYLLSTLKETPADAEVISHQLMLRAGMIRKLASGLYTWLPTGVRVLKKVENIVREEMNNAGAIEVSMPVVQPADLW 80
Cdd:TIGR00409 1 MRTSQYLFPTLKETPADAEVKSHQLLLRAGFIRRLGSGLYNWLPLGLRVLKKVENIVREEMNKDGAIEVLLPALQPAELW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 81 QESGRWEQYGPELLRFVDRGERPFVLGPTHEEVITDLIRNELSSYKQLPLNFFQIQTKFRDEVRPRFGVMRSREFLMKDA 160
Cdd:TIGR00409 81 QESGRWDTYGPELLRLKDRKGREFVLGPTHEEVITDLARNEIKSYKQLPLNLYQIQTKFRDEIRPRFGLMRGREFIMKDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 161 YSFHTSQESLQETYDKMYEAYSKIFSRMGLDFRAVQADTGSIGGSASHEFQVLAQSGEDDVIFSDSSDYAANIEFAEALA 240
Cdd:TIGR00409 161 YSFHSDEESLDATYQKMYQAYSNIFSRLGLDFRPVQADSGAIGGSASHEFMVLAESGEDTIVYSDESDYAANIELAEALA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 241 PKApRAAATEEMTLVDTPHAKTIAELVEQFNLPVEKTVKTLLVKSTEGSAyPLVALLVRGDHELNEVKAEKLPQVASPLT 320
Cdd:TIGR00409 241 PGE-RNAPTAELDKVDTPNTKTIAELVECFNLPAEKVVKTLLVKAVDKSE-PLVALLVRGDHELNEVKAPNLLLVAQVLE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 321 FATEAEIRAVVNAGPGSLGPVNMP--VPVVIDRTVAAMSDFAAGANIDGKHYFGINWDRDVATPEVADIRNVVAGDPSPD 398
Cdd:TIGR00409 319 LATEEEIFQKIASGPGSLGPVNINggIPVLIDQTVALMSDFAAGANADDKHYFNVNWDRDVAIPEVADIRKVKEGDPSPD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 399 GQGTLMIKRGIEVGHIFQLGDKYSRALNAAVQGEDGRNQILTMGCYGIGVTRVVAAAIEQNYDERGIVWPDNIAPFQVAI 478
Cdd:TIGR00409 399 GQGTLKIARGIEVGHIFQLGTKYSEALKATFLDENGKNQFMTMGCYGIGVSRLVSAIAEQHHDERGIIWPKAIAPYDVVI 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 479 LPMNMHKSyRVQELAEKLYSELRAQGIEVLMDDRKERPGVMFADMELIGIPHTVVIGDRNLDSDDIEYKYRRSGEKQMIK 558
Cdd:TIGR00409 479 VVMNMKDE-EQQQLAEELYSELLAQGVDVLLDDRNERAGVKFADSELIGIPLRVVVGKKNLDNGEIEVKKRRNGEKQLIK 557
|
570
....*....|
gi 503934731 559 TGDILDYLVK 568
Cdd:TIGR00409 558 KDELVECLEE 567
|
|
| PRK12325 |
PRK12325 |
prolyl-tRNA synthetase; Provisional |
1-566 |
0e+00 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 237059 [Multi-domain] Cd Length: 439 Bit Score: 608.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 1 MRTSQYLLSTLKETPADAEVISHQLMLRAGMIRKLASGLYTWLPTGVRVLKKVENIVREEMNNAGAIEVSMPVVQPADLW 80
Cdd:PRK12325 1 MRLSRYFLPTLKENPKEAEIVSHRLMLRAGMIRQQAAGIYSWLPLGLKVLKKIENIVREEQNRAGAIEILMPTIQPADLW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 81 QESGRWEQYGPELLRFVDRGERPFVLGPTHEEVITDLIRNELSSYKQLPLNFFQIQTKFRDEVRPRFGVMRSREFLMKDA 160
Cdd:PRK12325 81 RESGRYDAYGKEMLRIKDRHDREMLYGPTNEEMITDIFRSYVKSYKDLPLNLYHIQWKFRDEIRPRFGVMRGREFLMKDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 161 YSFHTSQESLQETYDKMYEAYSKIFSRMGLDFRAVQADTGSIGGSASHEFQVLAQSGEDDVIFS------DSSDYAANIE 234
Cdd:PRK12325 161 YSFDLDEEGARHSYNRMFVAYLRTFARLGLKAIPMRADTGPIGGDLSHEFIILAETGESTVFYDkdfldlLVPGEDIDFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 235 FAEALAPKAPRA---AATEEMtlvdtphaktiaelveqfnlpvektvktllvkstegsayplvallvrgdHElnevkAEK 311
Cdd:PRK12325 241 VADLQPIVDEWTslyAATEEM-------------------------------------------------HD-----EAA 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 312 LPQVaspltfateaeiravvnagpgslgpvnmpvpvvidrtvaamsdfaaganidgkhyfginwdrdvatPEvadirnvv 391
Cdd:PRK12325 267 FAAV------------------------------------------------------------------PE-------- 272
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 392 agdpspdgqGTLMIKRGIEVGHIFQLGDKYSRALNAAVQGEDGRNQILTMGCYGIGVTRVVAAAIEQNYDERGIVWPDNI 471
Cdd:PRK12325 273 ---------ERRLSARGIEVGHIFYFGTKYSEPMNAKVQGPDGKEVPVHMGSYGIGVSRLVAAIIEASHDDKGIIWPESV 343
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 472 APFQVAILPMNMHKSyRVQELAEKLYSELRAQGIEVLMDDRKERPGVMFADMELIGIPHTVVIGDRNLDSDDIEYKYRRS 551
Cdd:PRK12325 344 APFKVGIINLKQGDE-ACDAACEKLYAALSAAGIDVLYDDTDERPGAKFATMDLIGLPWQIIVGPKGLAEGKVELKDRKT 422
|
570
....*....|....*
gi 503934731 552 GEKQMIKTGDILDYL 566
Cdd:PRK12325 423 GEREELSVEAAINRL 437
|
|
| ProRS_core_prok |
cd00779 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
17-458 |
6.83e-154 |
|
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: 441.25 E-value: 6.83e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 17 DAEVISHQLMLRAGMIRKLASGLYTWLPTGVRVLKKVENIVREEMNNAGAIEVSMPVVQPADLWQESGRWEQYGPELLRF 96
Cdd:cd00779 1 DAEIISHKLLLRAGFIRQTSSGLYSWLPLGLRVLKKIENIIREEMNKIGAQEILMPILQPAELWKESGRWDAYGPELLRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 97 VDRGERPFVLGPTHEEVITDLIRNELSSYKQLPLNFFQIQTKFRDEVRPRFGVMRSREFLMKDAYSFHTSQESLQETYDK 176
Cdd:cd00779 81 KDRHGKEFLLGPTHEEVITDLVANEIKSYKQLPLNLYQIQTKFRDEIRPRFGLMRGREFLMKDAYSFDIDEESLEETYEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 177 MYEAYSKIFSRMGLDFRAVQADTGSIGGSASHEFQVLAQsgeddvifsdssdyaaniefaealapkapraaateemtlvd 256
Cdd:cd00779 161 MYQAYSRIFKRLGLPFVKVEADSGAIGGSLSHEFHVLSP----------------------------------------- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 257 tphaktiaelveqfnlpvektvktllvkstegsayplvallvrgdhelnevkaeklpqvaspltfateaeiravvnagpg 336
Cdd:cd00779 --------------------------------------------------------------------------------
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 337 slgpvnmpvpvvidrtvaamsdfaaganidgkhyfginwdrdvatpevadirnvvagdpspdgqgtLMIKRGIEVGHIFQ 416
Cdd:cd00779 200 ------------------------------------------------------------------LKITKGIEVGHIFQ 213
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 503934731 417 LGDKYSRALNAAVQGEDGRNQILTMGCYGIGVTRVVAAAIEQ 458
Cdd:cd00779 214 LGTKYSKALGATFLDENGKPKPLEMGCYGIGVSRLLAAIIEQ 255
|
|
| ProRS-INS |
cd04334 |
INS is an amino acid-editing domain inserted (INS) into the bacterial class II prolyl-tRNA ... |
226-387 |
7.06e-77 |
|
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: 240.11 E-value: 7.06e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 226 SSDYAANIEFAEALAPKAPRAAATEEMTLVDTPHAKTIAELVEQFNLPVEKTVKTLLVKSTEgsAYPLVALLVRGDHELN 305
Cdd:cd04334 1 DCDYAANIEKAESLPPAAERPAPPKELEKVATPGQKTIEELAEFLGVPPSQTVKTLLVKADG--EEELVAVLLRGDHELN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 306 EVKAEKLPQVAsPLTFATEAEIRAVVNAGPGSLGPVNMP-VPVVIDRTVAAMSDFAAGANIDGKHYFGINWDRDVATPEV 384
Cdd:cd04334 79 EVKLENLLGAA-PLELASEEEIEAATGAPPGFIGPVGLKkIPIIADRSVADLKNFVCGANEDDYHYVNVNWGRDFPLPEV 157
|
...
gi 503934731 385 ADI 387
Cdd:cd04334 158 ADL 160
|
|
| ProRS_core |
cd00772 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
17-217 |
1.26e-47 |
|
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: 167.16 E-value: 1.26e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 17 DAEVISHQLMLRAGMIRKL-ASGLYTWLPTGVRVLKKVENIVREEMNNAGAIEVSMPVVQPADLWQESGRWEQYG-PELL 94
Cdd:cd00772 1 DASEKSLEHIGKAELADQGpGRGIINFLPLAKAILDKIENVLDKMFKEHGAQNALFPFFILASFLEKEAEHDEGFsKELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 95 RFVDRG----ERPFVLGPTHEEVITDLIRNELSSYKQLPLNFFQIQTKFRDEVRPRFGVMRSREFLMKDAYSFHTSQESL 170
Cdd:cd00772 81 VFKDAGdeelEEDFALRPTLEENIGEIAAKFIKSWKDLPQHLNQIGNKFRDEIRPRFGFLRAREFIMKDGHSAHADAEEA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 503934731 171 QETYDKMYEAYSKIFSRMG-LDFRAVQADTGS--IGGSASHEFQVLAQSG 217
Cdd:cd00772 161 DEEFLNMLSAYAEIARDLAaIDFIEGEADEGAkfAGASKSREFEALMEDG 210
|
|
| ProRS_anticodon_short |
cd00861 |
ProRS Prolyl-anticodon binding domain, short version found predominantly in bacteria. ProRS ... |
473-567 |
1.18e-41 |
|
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: 145.04 E-value: 1.18e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 473 PFQVAILPMNMHkSYRVQELAEKLYSELRAQGIEVLMDDRKERPGVMFADMELIGIPHTVVIGDRNLDSDDIEYKYRRSG 552
Cdd:cd00861 1 PFDVVIIPMNMK-DEVQQELAEKLYAELQAAGVDVLLDDRNERPGVKFADADLIGIPYRIVVGKKSAAEGIVEIKVRKTG 79
|
90
....*....|....*
gi 503934731 553 EKQMIKTGDILDYLV 567
Cdd:cd00861 80 EKEEISIDELLEFLQ 94
|
|
| YbaK_like |
cd04332 |
YbaK-like. The YbaK family of deacylase domains includes the INS amino acid-editing domain of ... |
250-385 |
5.16e-34 |
|
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: 125.73 E-value: 5.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 250 EEMTLVDTPHAKTIAELVEQFNLPVEKTVKTLLVKSTEGSaypLVALLVRGDHELNEVKAEKLPQVAsPLTFATEAEIRA 329
Cdd:cd04332 1 EYLEYEHTPGAKTIEEAAEALGVPPGQIAKTLVLKDDKGG---LVLVVVPGDHELDLKKLAKALGAK-KLRLASEEELEE 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 330 VVNAGPGSLGPVNMP--VPVVIDRTVAAMSDFAAGANIDGK--HYFGINWDRDVATPEVA 385
Cdd:cd04332 77 LTGCEPGGVGPFGLKkgVPVVVDESLLELEDVYVGAGERGAdlHLSPADLLRLLGEAEVA 136
|
|
| Gly_His_Pro_Ser_Thr_tRS_core |
cd00670 |
Gly_His_Pro_Ser_Thr_tRNA synthetase class II core domain. This domain is the core catalytic ... |
46-203 |
1.43e-30 |
|
Gly_His_Pro_Ser_Thr_tRNA synthetase class II core domain. This domain is the core catalytic domain of tRNA synthetases of the subgroup containing glycyl, histidyl, prolyl, seryl and threonyl tRNA synthetases. It is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. These enzymes belong to class II aminoacyl-tRNA synthetases (aaRS) based upon their structure and the presence of three characteristic sequence motifs in the core domain. This domain is also found at the C-terminus of eukaryotic GCN2 protein kinase and at the N-terminus of the ATP phosphoribosyltransferase accessory subunit, HisZ and the accessory subunit of mitochondrial polymerase gamma (Pol gamma b) . Most class II tRNA synthetases are dimers, with this subgroup consisting of mostly homodimers. These enzymes attach a specific amino acid to the 3' OH group of ribose of the appropriate tRNA.
Pssm-ID: 238359 [Multi-domain] Cd Length: 235 Bit Score: 119.42 E-value: 1.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 46 GVRVLKKVENIVREEMNNAGAIEVSMPVVQPADLWQESGRWEQYGPELLRFVDRG----ERPFVLGPTHEEVITDLIRNE 121
Cdd:cd00670 1 GTALWRALERFLDDRMAEYGYQEILFPFLAPTVLFFKGGHLDGYRKEMYTFEDKGrelrDTDLVLRPAACEPIYQIFSGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 122 LSSYKQLPLNFFQIQTKFRDEVRPRFGVMRSREFLMKDAYSFHTsQESLQETYDKMYEAYSKIFSRMGLDFRAVQADTGS 201
Cdd:cd00670 81 ILSYRALPLRLDQIGPCFRHEPSGRRGLMRVREFRQVEYVVFGE-PEEAEEERREWLELAEEIARELGLPVRVVVADDPF 159
|
..
gi 503934731 202 IG 203
Cdd:cd00670 160 FG 161
|
|
| tRNA_edit |
pfam04073 |
Aminoacyl-tRNA editing domain; This domain is found either on its own or in association with ... |
257-376 |
5.85e-28 |
|
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: 108.46 E-value: 5.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 257 TPHAKTIAELVEQFNLPVEKTVKTLLVKSTEGSaypLVALLVRGDHELNEVKAEKLPQVaSPLTFATEAEIRAVVNAGPG 336
Cdd:pfam04073 1 HPPAATIEELAAALGVPPGRIAKTLVLKDKKGK---YVLVVVPGDREVDLKKLAKLLGV-KRLRLASEEELLELTGVEPG 76
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 503934731 337 SLGPVNM---PVPVVIDRTVAAMSDFAAGANIDGKHYFGINWD 376
Cdd:pfam04073 77 GVTPFGLkakGVPVLVDESLKDLPDVVVGAGENGATLRLSNAD 119
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
475-568 |
5.72e-23 |
|
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: 93.42 E-value: 5.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 475 QVAILPMNMHKsYRVQELAEKLYSELRAQGIEVLMDDRKERPGVMFADMELIGIPHTVVIGDRNLDSDDIEYKYRRSGEK 554
Cdd:pfam03129 1 QVVVIPLGEKA-EELEEYAQKLAEELRAAGIRVELDDRNESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQ 79
|
90
....*....|....
gi 503934731 555 QMIKTGDILDYLVK 568
Cdd:pfam03129 80 ETVSLDELVEKLKE 93
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
95-207 |
6.48e-21 |
|
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: 90.16 E-value: 6.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 95 RFVDRGERPFVLGPTHEEVITDLIRNELSSYKQLPLNFFQIQTKFRDEVRPRF-GVMRSREFLMKDAYSFHTsQESLQET 173
Cdd:pfam00587 2 KVEDENGDELALKPTNEPGHTLLFREEGLRSKDLPLKLAQFGTCFRHEASGDTrGLIRVRQFHQDDAHIFHA-PGQSPDE 80
|
90 100 110
....*....|....*....|....*....|....
gi 503934731 174 YDKMYEAYSKIFSRMGLDFRAVQADTGSIGGSAS 207
Cdd:pfam00587 81 LEDYIKLIDRVYSRLGLEVRVVRLSNSDGSAFYG 114
|
|
| HGTP_anticodon |
cd00738 |
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ... |
473-567 |
5.67e-20 |
|
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: 84.76 E-value: 5.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 473 PFQVAILPMNMhKSYRVQELAEKLYSELRAQGIEVLMDDRKERPGVMFADMELIGIPHTVVIGDRNLDSDDIEYKYRRSG 552
Cdd:cd00738 1 PIDVAIVPLTD-PRVEAREYAQKLLNALLANGIRVLYDDRERKIGKKFREADLRGVPFAVVVGEDELENGKVTVKSRDTG 79
|
90
....*....|....*
gi 503934731 553 EKQMIKTGDILDYLV 567
Cdd:cd00738 80 ESETLHVDELPEFLV 94
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
49-220 |
5.89e-18 |
|
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: 82.55 E-value: 5.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 49 VLKKVENIVREEMNNAGAIEVSMPVVQPADLWQESGRWEQYgpeLLRFVDRGERPFVLGPTHEEVITDLIRNELssyKQL 128
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGHEPKD---LLPVGAENEEDLYLRPTLEPGLVRLFVSHI---RKL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 129 PLNFFQIQTKFRDEvRPRFGVMRSREFLMKDAYSFHTsQESLQETYDKMYEAYSKIFSRMG--LDFRAVQADTGSIG-GS 205
Cdd:cd00768 75 PLRLAEIGPAFRNE-GGRRGLRRVREFTQLEGEVFGE-DGEEASEFEELIELTEELLRALGikLDIVFVEKTPGEFSpGG 152
|
170
....*....|....*
gi 503934731 206 ASHEFQVLAQSGEDD 220
Cdd:cd00768 153 AGPGFEIEVDHPEGR 167
|
|
| ProRS_core_arch_euk |
cd00778 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
23-188 |
2.76e-16 |
|
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: 78.79 E-value: 2.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 23 HQLMLRAGMI-RKLASGLYTWLPTGVRVLKKVENIVREEMNNAGAIEVSMPVVQPADLWQ-ESGRWEQYGPELLrFVDRG 100
Cdd:cd00778 7 TEVITKAELIdYGPVKGCMVFRPYGYAIWENIQKILDKEIKETGHENVYFPLLIPESELEkEKEHIEGFAPEVA-WVTHG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 101 -----ERPFVLGPTHEEVITDLIRNELSSYKQLPLNFFQIQTKFRDEVRPRFGVMRSREFLMKDAYSFHTSQESLQETYD 175
Cdd:cd00778 86 gleelEEPLALRPTSETAIYPMFSKWIRSYRDLPLKINQWVNVFRWETKTTRPFLRTREFLWQEGHTAHATEEEAEEEVL 165
|
170
....*....|...
gi 503934731 176 KMYEAYSKIFSRM 188
Cdd:cd00778 166 QILDLYKEFYEDL 178
|
|
| ThrRS_core |
cd00771 |
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ... |
34-193 |
1.16e-13 |
|
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: 71.81 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 34 KLASGLYTWLPTGVRVLKKVENIVREEMNNAGAIEVSMPVVQPADLWQESGRWEQYGPELLRFvDRGERPFVLGPT---- 109
Cdd:cd00771 17 EAGPGLPFWLPKGAIIRNELEDFLRELQRKRGYQEVETPIIYNKELWETSGHWDHYRENMFPF-EEEDEEYGLKPMncpg 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 110 HEEVITDLIRnelsSYKQLPLNFFQIQTKFRDEVRPRF-GVMRSREFLMKDAYSFHTS---QESLQETYDKMYEAYSKIF 185
Cdd:cd00771 96 HCLIFKSKPR----SYRDLPLRLAEFGTVHRYEQSGALhGLTRVRGFTQDDAHIFCTPdqiKEEIKGVLDLIKEVYSDFG 171
|
....*...
gi 503934731 186 srmGLDFR 193
Cdd:cd00771 172 ---FFDYK 176
|
|
| ProRS_anticodon_zinc |
cd00862 |
ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and ... |
464-572 |
1.72e-10 |
|
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: 60.77 E-value: 1.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 464 GIVWPDNIAPFQVAILPM--NMHKSYRVQELAEKLYSELRAQGIEVLMDDRKE-RPGVMFADMELIGIPHTVVIGDRNLD 540
Cdd:cd00862 1 GLVLPPRVAPIQVVIVPIgiKDEKREEVLEAADELAERLKAAGIRVHVDDRDNyTPGWKFNDWELKGVPLRIEIGPRDLE 80
|
90 100 110
....*....|....*....|....*....|..
gi 503934731 541 SDDIEYKYRRSGEKQMIKtgdiLDYLVKAIKG 572
Cdd:cd00862 81 KNTVVIVRRDTGEKKTVP----LAELVEKVPE 108
|
|
| PRK03991 |
PRK03991 |
threonyl-tRNA synthetase; Validated |
466-571 |
2.82e-09 |
|
threonyl-tRNA synthetase; Validated
Pssm-ID: 235190 [Multi-domain] Cd Length: 613 Bit Score: 59.88 E-value: 2.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 466 VWpdnIAPFQVAILPMnmhkSYRVQELAEKLYSELRAQGIEVLMDDRKERPGVMFADMELIGIPHTVVIGDRNLDSDDIE 545
Cdd:PRK03991 495 TW---LSPTQVRVIPV----SERHLDYAEEVADKLEAAGIRVDVDDRDESLGKKIRDAGKEWIPYVVVIGDKEMESGKLT 567
|
90 100
....*....|....*....|....*.
gi 503934731 546 YKYRRSGEKQMIKtgdiLDYLVKAIK 571
Cdd:PRK03991 568 VTIREESEKVEMT----LEELIERIK 589
|
|
| PRK12444 |
PRK12444 |
threonyl-tRNA synthetase; Reviewed |
31-192 |
7.56e-09 |
|
threonyl-tRNA synthetase; Reviewed
Pssm-ID: 183530 [Multi-domain] Cd Length: 639 Bit Score: 58.61 E-value: 7.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 31 MIRKLASGLYTWLPTGVRVLKKVENIVREEMNNAGAIEVSMPVVQPADLWQESGRWEQYgPELLRFVDRGERPFVLGPTH 110
Cdd:PRK12444 258 MFSEEAPGMPFYLPKGQIIRNELEAFLREIQKEYNYQEVRTPFMMNQELWERSGHWDHY-KDNMYFSEVDNKSFALKPMN 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 111 EEVITDLIRNELSSYKQLPLNFFQIQTKFRDEVRPRF-GVMRSREFLMKDAYSFHTsQESLQETYDKMYEAYSKIFSRMG 189
Cdd:PRK12444 337 CPGHMLMFKNKLHSYRELPIRMCEFGQVHRHEFSGALnGLLRVRTFCQDDAHLFVT-PDQIEDEIKSVMAQIDYVYKTFG 415
|
...
gi 503934731 190 LDF 192
Cdd:PRK12444 416 FEY 418
|
|
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
445-572 |
9.85e-08 |
|
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: 54.36 E-value: 9.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 445 GIGVTRVVAAAIEQNydergiVWPDNIAPFQVAILPMNMHKSYRVQELAEklysELRAQGIEVLMD--DRKERPGVMFAD 522
Cdd:COG0124 305 AIGLERLLLLLEELG------LLPAAEPPPDVYVVPLGEEARAEALKLAQ----ELRAAGIRVELDlgGRKLKKQLKYAD 374
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 503934731 523 MelIGIPHTVVIGDRNLDSDDIEYKYRRSGEKQMIKTGDILDYLVKAIKG 572
Cdd:COG0124 375 K--SGAPFVLILGEDELANGTVTLKDLATGEQETVPLDELVEYLKELLAE 422
|
|
| EbsC |
COG2606 |
Cys-tRNA(Pro) deacylase, prolyl-tRNA editing enzyme YbaK/EbsC [Translation, ribosomal ... |
258-387 |
1.87e-07 |
|
Cys-tRNA(Pro) deacylase, prolyl-tRNA editing enzyme YbaK/EbsC [Translation, ribosomal structure and biogenesis];
Pssm-ID: 442018 [Multi-domain] Cd Length: 152 Bit Score: 50.86 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 258 PHAKTIAELVEQFNLPVEKTVKTLLVKSTEGsaypLVALLVRGDHELNEVKAEKLPQVASpLTFATEAEIRAVvnAG--P 335
Cdd:COG2606 21 EPAATAEEAAEALGVPPEQIAKTLVFRGDGG----PVLAVVPGDRRLDLKKLAAALGAKK-VEMADPEEVERL--TGyeV 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 503934731 336 GSLGPVNMP--VPVVIDRTVAAMSDFAAGAnidGKHY--FGINWD--RDVATPEVADI 387
Cdd:COG2606 94 GGVSPFGLKkgLPVYVDESLLEFDEVYVSA---GDRGllVELAPAdlARLTGATVADI 148
|
|
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
34-163 |
2.18e-07 |
|
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: 53.88 E-value: 2.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 34 KLASGLYTWLPTGVRVLKKVENIVREEMNNAGAIEVSMPVVQPADLWQESGRWEQYGpELLRFVDRGERPFVLG----PT 109
Cdd:COG0441 258 EVGPGLPFWHPKGAIIRRELEDYIREKHRKAGYQEVKTPHILDRELWETSGHWDHYR-ENMFPTESDGEEYALKpmncPG 336
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 503934731 110 HEEVitdlIRNELSSYKQLPLNFFQIQTKFRDEvrpRFGV----MRSREFLMKDAYSF 163
Cdd:COG0441 337 HILI----YKSGLRSYRDLPLRLAEFGTVHRYE---PSGAlhglMRVRGFTQDDAHIF 387
|
|
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
466-571 |
1.37e-06 |
|
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: 51.19 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 466 VWpdnIAPFQVAILPMnmhkSYRVQELAEKLYSELRAQGIEVLMDDRKERPGVMFADMELIGIPHTVVIGDRNLDSDDIE 545
Cdd:COG0441 535 LW---LAPVQVVVLPI----SDKHADYAKEVAKKLRAAGIRVEVDLRNEKIGYKIREAQLQKVPYMLVVGDKEVENGTVS 607
|
90 100
....*....|....*....|....*.
gi 503934731 546 YKYRRSGEKQMIKTGDILDYLVKAIK 571
Cdd:COG0441 608 VRRRGGGDLGTMSLDEFIARLKEEIR 633
|
|
| PRK12444 |
PRK12444 |
threonyl-tRNA synthetase; Reviewed |
464-571 |
1.70e-06 |
|
threonyl-tRNA synthetase; Reviewed
Pssm-ID: 183530 [Multi-domain] Cd Length: 639 Bit Score: 50.90 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 464 GIVWPDNIAPFQVAILPMN--MHKSYrvqelAEKLYSELRAQGIEVLMDDRKERPGVMFADMELIGIPHTVVIGDRNLDS 541
Cdd:PRK12444 532 GGAFPAWLAPVQVKVIPVSnaVHVQY-----ADEVADKLAQAGIRVERDERDEKLGYKIREAQMQKIPYVLVIGDKEMEN 606
|
90 100 110
....*....|....*....|....*....|
gi 503934731 542 DDIEYKYRRSGEKQMIKTGDILDYLVKAIK 571
Cdd:PRK12444 607 GAVNVRKYGEEKSEVIELDMFVESIKEEIK 636
|
|
| PLN02908 |
PLN02908 |
threonyl-tRNA synthetase |
31-163 |
6.01e-06 |
|
threonyl-tRNA synthetase
Pssm-ID: 178496 [Multi-domain] Cd Length: 686 Bit Score: 49.38 E-value: 6.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 31 MIRKLASGLYTWLPTGVRVLKKVENIVREEMNNAGAIEVSMPVVQPADLWQESGRWEQYGPELLRF-VDRGErpFVLGPT 109
Cdd:PLN02908 305 FFHELSPGSCFFLPHGARIYNKLMDFIREQYWERGYDEVITPNIYNMDLWETSGHAAHYKENMFVFeIEKQE--FGLKPM 382
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 503934731 110 HEEVITDLIRNELSSYKQLPLNFFQIQTKFRDEVRPRF-GVMRSREFLMKDAYSF 163
Cdd:PLN02908 383 NCPGHCLMFAHRVRSYRELPLRLADFGVLHRNELSGALtGLTRVRRFQQDDAHIF 437
|
|
| SerRS_core |
cd00770 |
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the ... |
17-207 |
7.19e-06 |
|
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the attachment of serine to the 3' OH group of ribose of the appropriate tRNA. This domain It is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain. SerRS synthetase is a homodimer.
Pssm-ID: 238393 [Multi-domain] Cd Length: 297 Bit Score: 47.94 E-value: 7.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 17 DAEVISH-QLMLRAGMIR-----KLA-SGLYTWLPTGVRVLKKVENIVREEMNNAGAIEVSMPVVQPADLWQESGRWEQY 89
Cdd:cd00770 15 DFKPKDHvELGEKLDILDfergaKVSgSRFYYLKGDGALLERALINFALDFLTKRGFTPVIPPFLVRKEVMEGTGQLPKF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 90 GPELLRFVDRGERpfvLGPTHEEVITDLIRNELSSYKQLPLNFFQIQTKFRDEV----RPRFGVMRSREFLMKDAYSFHT 165
Cdd:cd00770 95 DEQLYKVEGEDLY---LIATAEVPLAALHRDEILEEEELPLKYAGYSPCFRKEAgsagRDTRGLFRVHQFEKVEQFVFTK 171
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 503934731 166 SQESLQEtYDKMYEAYSKIFSRMGLDFRAVQADTGSIGGSAS 207
Cdd:cd00770 172 PEESWEE-LEELISNAEEILQELGLPYRVVNICTGDLGFAAA 212
|
|
| ThrRS_anticodon |
cd00860 |
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases ... |
473-571 |
2.63e-05 |
|
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: 42.88 E-value: 2.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 473 PFQVAILPMNMhksyRVQELAEKLYSELRAQGIEVLMDDRKERPGVMFADMELIGIPHTVVIGDRNLDSDDIEYKYRRSG 552
Cdd:cd00860 1 PVQVVVIPVTD----EHLDYAKEVAKKLSDAGIRVEVDLRNEKLGKKIREAQLQKIPYILVVGDKEVETGTVSVRTRDGG 76
|
90
....*....|....*....
gi 503934731 553 EKQMIKtgdiLDYLVKAIK 571
Cdd:cd00860 77 DLGSMS----LDEFIEKLK 91
|
|
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
42-155 |
6.28e-05 |
|
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: 45.50 E-value: 6.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 42 WLPTGVRVLKKVENIVREEMNNAGAIEVSMPVVQPADLWQESgrweqYGP-----ELLRFVDRGERPFVLGPtheevitD 116
Cdd:COG0124 13 ILPEESAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARK-----IGEdivekEMYTFEDRGGRSLTLRP-------E 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 503934731 117 L--------IRNelSSYKQLPLNFFQIQTKFRDEvRPRFGvmRSREF 155
Cdd:COG0124 81 GtapvaravAEH--GNELPFPFKLYYIGPVFRYE-RPQKG--RYRQF 122
|
|
| Pol_gamma_b_Cterm |
cd02426 |
C-terminal domain of mitochondrial DNA polymerase gamma B subunit, which is required for ... |
471-571 |
9.00e-05 |
|
C-terminal domain of mitochondrial DNA polymerase gamma B subunit, which is required for processivity. Polymerase gamma replicates and repairs mitochondrial DNA. The c-terminal domain of its B subunit is strikingly similar to the anticodon-binding domain of glycyl tRNA synthetase.
Pssm-ID: 239106 [Multi-domain] Cd Length: 128 Bit Score: 42.41 E-value: 9.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 471 IAPFQVAIlpmNMHKSYRVQ--ELAEKLYSELRAQGIEVLMDDRKERPGVM---FADMELIGIPHTVVIGDRNLDSDDIE 545
Cdd:cd02426 25 LAPYKVAI---DCGKGDTAElrDLCQGLKNELREAGLSVWPGYLETQHSSLeqlLDKYDEMGVLFTLLISEQTLENGLLQ 101
|
90 100
....*....|....*....|....*.
gi 503934731 546 YKYRRSGEKQMIKTGDILDYLVKAIK 571
Cdd:cd02426 102 LRSRDTTLKETIHISDLPDYLLRYIA 127
|
|
| GlyRS_anticodon |
cd00858 |
GlyRS Glycyl-anticodon binding domain. GlyRS belongs to class II aminoacyl-tRNA synthetases ... |
471-538 |
2.29e-04 |
|
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: 41.00 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 471 IAPFQVAILPMNMHKSYrvQELAEKLYSELRAQGIEVLMDD---------RKERPGVMFA---DMELIGiPHTVVIGDRN 538
Cdd:cd00858 24 LAPIKVAVLPLVKRDEL--VEIAKEISEELRELGFSVKYDDsgsigrryaRQDEIGTPFCvtvDFDTLE-DGTVTIRERD 100
|
|
| PRK14938 |
PRK14938 |
Ser-tRNA(Thr) hydrolase; Provisional |
468-571 |
3.59e-04 |
|
Ser-tRNA(Thr) hydrolase; Provisional
Pssm-ID: 184902 [Multi-domain] Cd Length: 387 Bit Score: 43.29 E-value: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 468 PDNIAPFQVAILPMnmhKSYRVQElAEKLYSELRAQGIEVLMDDRKERPGVMFADMELIGIPHTVVIGDRNLDSDDIEYK 547
Cdd:PRK14938 269 PDWLNPIQVRILPV---KKDFLDF-SIQVAERLRKEGIRVNVDDLDDSLGNKIRRAGTEWIPFVIIIGEREVKTSTLTVK 344
|
90 100
....*....|....*....|....
gi 503934731 548 YRRSGEKQMIKtgdiLDYLVKAIK 571
Cdd:PRK14938 345 IRANNEQKSMT----VEELVKEIK 364
|
|
| PRK04173 |
PRK04173 |
glycyl-tRNA synthetase; Provisional |
446-511 |
4.43e-04 |
|
glycyl-tRNA synthetase; Provisional
Pssm-ID: 235240 [Multi-domain] Cd Length: 456 Bit Score: 42.81 E-value: 4.43e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503934731 446 IGVTRVVAAAIEQNYDERGIVWPD---------NIAPFQVAILPMNmhKSYRVQELAEKLYSELRAQgIEVLMDD 511
Cdd:PRK04173 327 AGLDRLLLAFLEDAYTEEELGGGDkrtvlrlppALAPVKVAVLPLV--KKEKLSEKAREIYAELRKD-FNVDYDD 398
|
|
| PLN02837 |
PLN02837 |
threonine-tRNA ligase |
38-163 |
8.50e-04 |
|
threonine-tRNA ligase
Pssm-ID: 215450 [Multi-domain] Cd Length: 614 Bit Score: 42.19 E-value: 8.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 38 GLYTWLPTGVRVLKKVENIVREEMNNAGAIEVSMPVVQPADLWQESGRWEQYGPELLRFVDRGERPFVLGPTHEEVITDL 117
Cdd:PLN02837 238 GLVFWHPKGAIVRHIIEDSWKKMHFEHGYDLLYTPHVAKADLWKTSGHLDFYKENMYDQMDIEDELYQLRPMNCPYHILV 317
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 503934731 118 IRNELSSYKQLPLNFFQIQTKFRDEVRPRF-GVMRSREFLMKDAYSF 163
Cdd:PLN02837 318 YKRKLHSYRDLPIRVAELGTVYRYELSGSLhGLFRVRGFTQDDAHIF 364
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
47-155 |
1.88e-03 |
|
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: 40.28 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503934731 47 VRVLKKVENIVREEMNNAGAIEVSMPVVQPADLWQeSGRWEQYGPELLRFVDRGERPFVLGPtheEVITDLIR--NELSS 124
Cdd:cd00773 2 AALRRYIEDTLREVFERYGYEEIDTPVFEYTELFL-RKSGDEVSKEMYRFKDKGGRDLALRP---DLTAPVARavAENLL 77
|
90 100 110
....*....|....*....|....*....|.
gi 503934731 125 YKQLPLNFFQIQTKFRDEvRPRFGvmRSREF 155
Cdd:cd00773 78 SLPLPLKLYYIGPVFRYE-RPQKG--RYREF 105
|
|
| HisRS_anticodon |
cd00859 |
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases ... |
490-566 |
3.93e-03 |
|
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: 36.75 E-value: 3.93e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503934731 490 QELAEKLYSELRAQGIEVLMDDRKERPGVMFADMELIGIPHTVVIGDRNLDSDDIEYKYRRSGEKQMIKTGDILDYL 566
Cdd:cd00859 14 LSEALELAEQLRDAGIKAEIDYGGRKLKKQFKYADRSGARFAVILGEDELAAGVVTVKDLETGEQETVALDELVEEL 90
|
|
| |
