|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09194 |
PRK09194 |
prolyl-tRNA synthetase; Provisional |
1-570 |
0e+00 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 236405 [Multi-domain] Cd Length: 565 Bit Score: 1117.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491812279 1 MRTSQYLFSTLKETPNDAQVVSHQLMLRAGMIRPMASGLYNWLPTGIKVLKKVENIIREEMNKGGAIEVLMPVVQPAELW 80
Cdd:PRK09194 1 MRTSQLFLPTLKETPADAEVISHQLLLRAGYIRKLASGIYTYLPLGLRVLRKIENIVREEMNKIGAQEVLMPALQPAELW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491812279 81 QESGRWNDYGAELLRFVDRGSRDFVLGPTHEEVITDLVRREVSSYKQLPLNLYQIQTKFRDEVRPRFGVMRSREFVMKDA 160
Cdd:PRK09194 81 QESGRWEEYGPELLRLKDRHGRDFVLGPTHEEVITDLVRNEIKSYKQLPLNLYQIQTKFRDEIRPRFGLMRGREFIMKDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491812279 161 YSFHVDKASLQETYDVMYQVYSNIFTRLGLDFRAVQADTGSIGGSASHEFQVLASSGEDDVVFSTESDFAANIELAEAVA 240
Cdd:PRK09194 161 YSFHADEESLDETYDAMYQAYSRIFDRLGLDFRAVEADSGAIGGSASHEFMVLADSGEDTIVYSDESDYAANIEKAEALP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491812279 241 vGERQAPTAEMQLVDTPNAKTINELVEQFNLPIEKTVKTLIVKGATEeqpLVALVLRGDHELNEIKAQKHpLVADPLEFA 320
Cdd:PRK09194 241 -PPRAAAEEALEKVDTPNAKTIEELAEFLNVPAEKTVKTLLVKADGE---LVAVLVRGDHELNEVKLENL-LGAAPLELA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491812279 321 DEAEIKAKIGAGVGSLGVINL--NVPAIIDRSVAVMSDFGCGANIDGKHYFNVNWERDAAMPEVADLRNVVEGDPSPDGK 398
Cdd:PRK09194 316 TEEEIRAALGAVPGFLGPVGLpkDVPIIADRSVADMSNFVVGANEDDYHYVGVNWGRDFPVPEVADLRNVVEGDPSPDGG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491812279 399 GVLQIKRGIEVGHIFQLGTKYSEAMKATVQGEDGKPLVMTMGCYGIGVTRVVAAAIEQHHDDRGIIWPsDEIAPFTVAIV 478
Cdd:PRK09194 396 GTLKIARGIEVGHIFQLGTKYSEAMNATVLDENGKAQPLIMGCYGIGVSRLVAAAIEQNHDEKGIIWP-KAIAPFDVHIV 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491812279 479 PMNMhKSESVQQFSEELYRTLKAQGVDVIFDDRKERPGVMFADMELIGVPHMVVIGEKNLANGEIEYKNRRTGEKQMIAK 558
Cdd:PRK09194 475 PVNM-KDEEVKELAEKLYAELQAAGIEVLLDDRKERPGVKFADADLIGIPHRIVVGDRGLAEGIVEYKDRRTGEKEEVPV 553
|
570
....*....|..
gi 491812279 559 DQLLAFLKENVK 570
Cdd:PRK09194 554 DELVEFLKALKK 565
|
|
| ProS |
COG0442 |
Prolyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Prolyl-tRNA ... |
1-567 |
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: 1030.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491812279 1 MRTSQYLFSTLKETPNDAQVVSHQLMLRAGMIRPMASGLYNWLPTGIKVLKKVENIIREEMNKGGAIEVLMPVVQPAELW 80
Cdd:COG0442 1 MRASKLFIPTLKERPADAEVWSHQLMLRAGLIRKLASGIYTYLPLGYRVLEKIEAIVREEMKRTGAQEVLMPLLQPAELW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491812279 81 QESGRWNDYGAELLRFVDRGSRDFVLGPTHEEVITDLVRREVSSYKQLPLNLYQIQTKFRDEVRPRFGVMRSREFVMKDA 160
Cdd:COG0442 81 EESGRWEGFGPELARVTDRLEREFCLGPTHEEVITDLVRNEIKSYRDLPLLLYQIQTKFRDEIRPRFGLLRTREFLMKDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491812279 161 YSFHVDKASLQETYDVMYQVYSNIFTRLGLDFRAVQADTGSIGGSASHEFQVLASSGEDDVVFSTESDFAANIELAEAVA 240
Cdd:COG0442 161 YSFHATEEELDEEYQKMLDAYERIFERLGLPVRAVEADSGAIGGSESHEFMVLADSGEDTIVYCDACDYAANIEKAEALA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491812279 241 -VGERQAPTAEMQLVDTPNAKTINELVEQFNLPIEKTVKTLIVKGateEQPLVALVLRGDHELNEIKAQKHpLVADPLEF 319
Cdd:COG0442 241 pPAERAEPTKELEAVATPGAKTIEEVAEFLGVPAEKTVKTLVYKA---DGELVAVLVRGDHELNEIKLENL-LGASELEL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491812279 320 ADEAEIKAKIGAGVGSLGVINLNVPAIIDRSVAVMSDFGCGANIDGKHYFNVNWERDAAMPEVADLRNVVEGDPSPDGKG 399
Cdd:COG0442 317 ATEEEIEAALGAVPGFLGPVGLGVPYIADRSVAGMSNFVCGANEDDYHYTNVNWGRDFPVDEVADLRNVVEGDPCPDCGG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491812279 400 VLQIKRGIEVGHIFQLGTKYSEAMKATVQGEDGKPLVMTMGCYGIGVTRVVAAAIEQHHDDRGIIWPsDEIAPFTVAIVP 479
Cdd:COG0442 397 LLQDGRGIEVGHIFKLGTKYSKAMDATFLDENGKEQPVWMGCYGIGVTRLIAAAIEQHHDDKGIIWP-PAIAPFQVVIVP 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491812279 480 MNMhKSESVQQFSEELYRTLKAQGVDVIFDDRKERPGVMFADMELIGVPHMVVIGEKNLANGEIEYKNRRTGEKQMIAKD 559
Cdd:COG0442 476 INM-KDEAVLEAAEELYAELKAAGIDVLLDDRDERPGVKFADAELIGIPLRIVIGPRDLEEGQVEVKRRDTGEKEEVPLD 554
|
....*...
gi 491812279 560 QLLAFLKE 567
Cdd:COG0442 555 ELVETVKE 562
|
|
| proS_fam_II |
TIGR00409 |
prolyl-tRNA synthetase, family II; Prolyl-tRNA synthetase is a class II tRNA synthetase and is ... |
1-567 |
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: 974.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491812279 1 MRTSQYLFSTLKETPNDAQVVSHQLMLRAGMIRPMASGLYNWLPTGIKVLKKVENIIREEMNKGGAIEVLMPVVQPAELW 80
Cdd:TIGR00409 1 MRTSQYLFPTLKETPADAEVKSHQLLLRAGFIRRLGSGLYNWLPLGLRVLKKVENIVREEMNKDGAIEVLLPALQPAELW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491812279 81 QESGRWNDYGAELLRFVDRGSRDFVLGPTHEEVITDLVRREVSSYKQLPLNLYQIQTKFRDEVRPRFGVMRSREFVMKDA 160
Cdd:TIGR00409 81 QESGRWDTYGPELLRLKDRKGREFVLGPTHEEVITDLARNEIKSYKQLPLNLYQIQTKFRDEIRPRFGLMRGREFIMKDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491812279 161 YSFHVDKASLQETYDVMYQVYSNIFTRLGLDFRAVQADTGSIGGSASHEFQVLASSGEDDVVFSTESDFAANIELAEAVA 240
Cdd:TIGR00409 161 YSFHSDEESLDATYQKMYQAYSNIFSRLGLDFRPVQADSGAIGGSASHEFMVLAESGEDTIVYSDESDYAANIELAEALA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491812279 241 VGERQAPTAEMQLVDTPNAKTINELVEQFNLPIEKTVKTLIVKGATEEQPLVALVLRGDHELNEIKAQKHPLVADPLEFA 320
Cdd:TIGR00409 241 PGERNAPTAELDKVDTPNTKTIAELVECFNLPAEKVVKTLLVKAVDKSEPLVALLVRGDHELNEVKAPNLLLVAQVLELA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491812279 321 DEAEIKAKIGAGVGSLGVINLN--VPAIIDRSVAVMSDFGCGANIDGKHYFNVNWERDAAMPEVADLRNVVEGDPSPDGK 398
Cdd:TIGR00409 321 TEEEIFQKIASGPGSLGPVNINggIPVLIDQTVALMSDFAAGANADDKHYFNVNWDRDVAIPEVADIRKVKEGDPSPDGQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491812279 399 GVLQIKRGIEVGHIFQLGTKYSEAMKATVQGEDGKPLVMTMGCYGIGVTRVVAAAIEQHHDDRGIIWPsDEIAPFTVAIV 478
Cdd:TIGR00409 401 GTLKIARGIEVGHIFQLGTKYSEALKATFLDENGKNQFMTMGCYGIGVSRLVSAIAEQHHDERGIIWP-KAIAPYDVVIV 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491812279 479 PMNMHKsESVQQFSEELYRTLKAQGVDVIFDDRKERPGVMFADMELIGVPHMVVIGEKNLANGEIEYKNRRTGEKQMIAK 558
Cdd:TIGR00409 480 VMNMKD-EEQQQLAEELYSELLAQGVDVLLDDRNERAGVKFADSELIGIPLRVVVGKKNLDNGEIEVKKRRNGEKQLIKK 558
|
....*....
gi 491812279 559 DQLLAFLKE 567
Cdd:TIGR00409 559 DELVECLEE 567
|
|
| PRK12325 |
PRK12325 |
prolyl-tRNA synthetase; Provisional |
1-567 |
0e+00 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 237059 [Multi-domain] Cd Length: 439 Bit Score: 616.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491812279 1 MRTSQYLFSTLKETPNDAQVVSHQLMLRAGMIRPMASGLYNWLPTGIKVLKKVENIIREEMNKGGAIEVLMPVVQPAELW 80
Cdd:PRK12325 1 MRLSRYFLPTLKENPKEAEIVSHRLMLRAGMIRQQAAGIYSWLPLGLKVLKKIENIVREEQNRAGAIEILMPTIQPADLW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491812279 81 QESGRWNDYGAELLRFVDRGSRDFVLGPTHEEVITDLVRREVSSYKQLPLNLYQIQTKFRDEVRPRFGVMRSREFVMKDA 160
Cdd:PRK12325 81 RESGRYDAYGKEMLRIKDRHDREMLYGPTNEEMITDIFRSYVKSYKDLPLNLYHIQWKFRDEIRPRFGVMRGREFLMKDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491812279 161 YSFHVDKASLQETYDVMYQVYSNIFTRLGLDFRAVQADTGSIGGSASHEFQVLASSGEDDVVFSTEsdfaanielaeava 240
Cdd:PRK12325 161 YSFDLDEEGARHSYNRMFVAYLRTFARLGLKAIPMRADTGPIGGDLSHEFIILAETGESTVFYDKD-------------- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491812279 241 VGERQAPTAEMQLVDTPNAKTINELVEQFNlpiektvktlivkgATEEqplvalvlrgdhelneikaqKHplvadplefa 320
Cdd:PRK12325 227 FLDLLVPGEDIDFDVADLQPIVDEWTSLYA--------------ATEE--------------------MH---------- 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491812279 321 DEAeikakigagvgslgvinlnvpaiidrsvavmsdfgcganidgkhyfnvnweRDAAMPEvADLRNvvegdpspdgkgv 400
Cdd:PRK12325 263 DEA---------------------------------------------------AFAAVPE-ERRLS------------- 277
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491812279 401 lqiKRGIEVGHIFQLGTKYSEAMKATVQGEDGKPLVMTMGCYGIGVTRVVAAAIEQHHDDRGIIWPsDEIAPFTVAIVPM 480
Cdd:PRK12325 278 ---ARGIEVGHIFYFGTKYSEPMNAKVQGPDGKEVPVHMGSYGIGVSRLVAAIIEASHDDKGIIWP-ESVAPFKVGIINL 353
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491812279 481 NMHKSESVqQFSEELYRTLKAQGVDVIFDDRKERPGVMFADMELIGVPHMVVIGEKNLANGEIEYKNRRTGEKQMIAKDQ 560
Cdd:PRK12325 354 KQGDEACD-AACEKLYAALSAAGIDVLYDDTDERPGAKFATMDLIGLPWQIIVGPKGLAEGKVELKDRKTGEREELSVEA 432
|
....*..
gi 491812279 561 LLAFLKE 567
Cdd:PRK12325 433 AINRLTA 439
|
|
| ProRS_core_prok |
cd00779 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
17-456 |
8.79e-152 |
|
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: 435.85 E-value: 8.79e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491812279 17 DAQVVSHQLMLRAGMIRPMASGLYNWLPTGIKVLKKVENIIREEMNKGGAIEVLMPVVQPAELWQESGRWNDYGAELLRF 96
Cdd:cd00779 1 DAEIISHKLLLRAGFIRQTSSGLYSWLPLGLRVLKKIENIIREEMNKIGAQEILMPILQPAELWKESGRWDAYGPELLRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491812279 97 VDRGSRDFVLGPTHEEVITDLVRREVSSYKQLPLNLYQIQTKFRDEVRPRFGVMRSREFVMKDAYSFHVDKASLQETYDV 176
Cdd:cd00779 81 KDRHGKEFLLGPTHEEVITDLVANEIKSYKQLPLNLYQIQTKFRDEIRPRFGLMRGREFLMKDAYSFDIDEESLEETYEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491812279 177 MYQVYSNIFTRLGLDFRAVQADTGSIGGSASHEFQVLASsgeddvvfstesdfaanielaeavavgerqaptaemqlvdt 256
Cdd:cd00779 161 MYQAYSRIFKRLGLPFVKVEADSGAIGGSLSHEFHVLSP----------------------------------------- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491812279 257 pnaktinelveqfnlpiektvktlivkgateeqplvalvlrgdhelneikaqkhplvadplefadeaeikakigagvgsl 336
Cdd:cd00779 --------------------------------------------------------------------------------
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491812279 337 gvinlnvpaiidrsvavmsdfgcganidgkhyfnvnwerdaampevadlrnvvegdpspdgkgvLQIKRGIEVGHIFQLG 416
Cdd:cd00779 200 ----------------------------------------------------------------LKITKGIEVGHIFQLG 215
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 491812279 417 TKYSEAMKATVQGEDGKPLVMTMGCYGIGVTRVVAAAIEQ 456
Cdd:cd00779 216 TKYSKALGATFLDENGKPKPLEMGCYGIGVSRLLAAIIEQ 255
|
|
| ProRS-INS |
cd04334 |
INS is an amino acid-editing domain inserted (INS) into the bacterial class II prolyl-tRNA ... |
226-385 |
5.64e-75 |
|
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: 235.10 E-value: 5.64e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491812279 226 ESDFAANIELAEAVAV-GERQAPTAEMQLVDTPNAKTINELVEQFNLPIEKTVKTLIVKGATEEQPlVALVLRGDHELNE 304
Cdd:cd04334 1 DCDYAANIEKAESLPPaAERPAPPKELEKVATPGQKTIEELAEFLGVPPSQTVKTLLVKADGEEEL-VAVLLRGDHELNE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491812279 305 IKAQKHPLvADPLEFADEAEIKAKIGAGVGSLGVINL-NVPAIIDRSVAVMSDFGCGANIDGKHYFNVNWERDAAMPEVA 383
Cdd:cd04334 80 VKLENLLG-AAPLELASEEEIEAATGAPPGFIGPVGLkKIPIIADRSVADLKNFVCGANEDDYHYVNVNWGRDFPLPEVA 158
|
..
gi 491812279 384 DL 385
Cdd:cd04334 159 DL 160
|
|
| ProRS_core |
cd00772 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
37-217 |
1.57e-46 |
|
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain.
Pssm-ID: 238395 [Multi-domain] Cd Length: 264 Bit Score: 164.08 E-value: 1.57e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491812279 37 SGLYNWLPTGIKVLKKVENIIREEMNKGGAIEVLMPVVQPAELWQESGRWNDYGA-ELLRFVDRG----SRDFVLGPTHE 111
Cdd:cd00772 22 RGIINFLPLAKAILDKIENVLDKMFKEHGAQNALFPFFILASFLEKEAEHDEGFSkELAVFKDAGdeelEEDFALRPTLE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491812279 112 EVITDLVRREVSSYKQLPLNLYQIQTKFRDEVRPRFGVMRSREFVMKDAYSFHVDKASLQETYDVMYQVYSNIFTRLG-L 190
Cdd:cd00772 102 ENIGEIAAKFIKSWKDLPQHLNQIGNKFRDEIRPRFGFLRAREFIMKDGHSAHADAEEADEEFLNMLSAYAEIARDLAaI 181
|
170 180
....*....|....*....|....*....
gi 491812279 191 DFRAVQADTGS--IGGSASHEFQVLASSG 217
Cdd:cd00772 182 DFIEGEADEGAkfAGASKSREFEALMEDG 210
|
|
| ProRS_anticodon_short |
cd00861 |
ProRS Prolyl-anticodon binding domain, short version found predominantly in bacteria. ProRS ... |
472-566 |
2.56e-42 |
|
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: 146.97 E-value: 2.56e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491812279 472 PFTVAIVPMNMhKSESVQQFSEELYRTLKAQGVDVIFDDRKERPGVMFADMELIGVPHMVVIGEKNLANGEIEYKNRRTG 551
Cdd:cd00861 1 PFDVVIIPMNM-KDEVQQELAEKLYAELQAAGVDVLLDDRNERPGVKFADADLIGIPYRIVVGKKSAAEGIVEIKVRKTG 79
|
90
....*....|....*
gi 491812279 552 EKQMIAKDQLLAFLK 566
Cdd:cd00861 80 EKEEISIDELLEFLQ 94
|
|
| YbaK_like |
cd04332 |
YbaK-like. The YbaK family of deacylase domains includes the INS amino acid-editing domain of ... |
249-383 |
6.30e-33 |
|
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: 122.65 E-value: 6.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491812279 249 AEMQLVDTPNAKTINELVEQFNLPIEKTVKTLIVKGATEEqpLVALVLRGDHELNEIKAQKHPLVAdPLEFADEAEIKAK 328
Cdd:cd04332 1 EYLEYEHTPGAKTIEEAAEALGVPPGQIAKTLVLKDDKGG--LVLVVVPGDHELDLKKLAKALGAK-KLRLASEEELEEL 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 491812279 329 IGAGVGSLGVINL--NVPAIIDRSVAVMSDFGCGANIDGK--HYFNVNWERDAAMPEVA 383
Cdd:cd04332 78 TGCEPGGVGPFGLkkGVPVVVDESLLELEDVYVGAGERGAdlHLSPADLLRLLGEAEVA 136
|
|
| tRNA_edit |
pfam04073 |
Aminoacyl-tRNA editing domain; This domain is found either on its own or in association with ... |
256-374 |
2.26e-26 |
|
Aminoacyl-tRNA editing domain; This domain is found either on its own or in association with the tRNA synthetase class II core domain (pfam00587). It is involved in the tRNA editing of mis-charged tRNAs including Cys-tRNA(Pro), Cys-tRNA(Cys), Ala-tRNA(Pro). The structure of this domain shows a novel fold.
Pssm-ID: 427693 [Multi-domain] Cd Length: 123 Bit Score: 103.84 E-value: 2.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491812279 256 TPNAKTINELVEQFNLPIEKTVKTLIVKGATEEqpLVALVLRGDHELNEIKAQKHPLVADpLEFADEAEIKAKIGAGVGS 335
Cdd:pfam04073 1 HPPAATIEELAAALGVPPGRIAKTLVLKDKKGK--YVLVVVPGDREVDLKKLAKLLGVKR-LRLASEEELLELTGVEPGG 77
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 491812279 336 LGVINL---NVPAIIDRSVAVMSDFGCGANIDGKHYFNVNWE 374
Cdd:pfam04073 78 VTPFGLkakGVPVLVDESLKDLPDVVVGAGENGATLRLSNAD 119
|
|
| 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 |
7.97e-26 |
|
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: 105.94 E-value: 7.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491812279 46 GIKVLKKVENIIREEMNKGGAIEVLMPVVQPAELWQESGRWNDYGAELLRFVDRGS----RDFVLGPTHEEVITDLVRRE 121
Cdd:cd00670 1 GTALWRALERFLDDRMAEYGYQEILFPFLAPTVLFFKGGHLDGYRKEMYTFEDKGRelrdTDLVLRPAACEPIYQIFSGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491812279 122 VSSYKQLPLNLYQIQTKFRDEVRPRFGVMRSREFVMKDAYSFHVDkASLQETYDVMYQVYSNIFTRLGLDFRAVQADTGS 201
Cdd:cd00670 81 ILSYRALPLRLDQIGPCFRHEPSGRRGLMRVREFRQVEYVVFGEP-EEAEEERREWLELAEEIARELGLPVRVVVADDPF 159
|
..
gi 491812279 202 IG 203
Cdd:cd00670 160 FG 161
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
475-568 |
1.78e-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: 94.58 E-value: 1.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491812279 475 VAIVPMNMHKsESVQQFSEELYRTLKAQGVDVIFDDRKERPGVMFADMELIGVPHMVVIGEKNLANGEIEYKNRRTGEKQ 554
Cdd:pfam03129 2 VVVIPLGEKA-EELEEYAQKLAEELRAAGIRVELDDRNESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQE 80
|
90
....*....|....
gi 491812279 555 MIAKDQLLAFLKEN 568
Cdd:pfam03129 81 TVSLDELVEKLKEL 94
|
|
| HGTP_anticodon |
cd00738 |
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ... |
472-566 |
4.23e-21 |
|
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: 87.84 E-value: 4.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491812279 472 PFTVAIVPMNMhKSESVQQFSEELYRTLKAQGVDVIFDDRKERPGVMFADMELIGVPHMVVIGEKNLANGEIEYKNRRTG 551
Cdd:cd00738 1 PIDVAIVPLTD-PRVEAREYAQKLLNALLANGIRVLYDDRERKIGKKFREADLRGVPFAVVVGEDELENGKVTVKSRDTG 79
|
90
....*....|....*
gi 491812279 552 EKQMIAKDQLLAFLK 566
Cdd:cd00738 80 ESETLHVDELPEFLV 94
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
95-207 |
4.37e-20 |
|
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely threonyl-tRNA members.
Pssm-ID: 395469 [Multi-domain] Cd Length: 181 Bit Score: 87.85 E-value: 4.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491812279 95 RFVDRGSRDFVLGPTHEEVITDLVRREVSSYKQLPLNLYQIQTKFRDEVRPRF-GVMRSREFVMKDAYSFHVDKASLQET 173
Cdd:pfam00587 2 KVEDENGDELALKPTNEPGHTLLFREEGLRSKDLPLKLAQFGTCFRHEASGDTrGLIRVRQFHQDDAHIFHAPGQSPDEL 81
|
90 100 110
....*....|....*....|....*....|....
gi 491812279 174 YDvMYQVYSNIFTRLGLDFRAVQADTGSIGGSAS 207
Cdd:pfam00587 82 ED-YIKLIDRVYSRLGLEVRVVRLSNSDGSAFYG 114
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
49-220 |
2.54e-17 |
|
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: 81.01 E-value: 2.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491812279 49 VLKKVENIIREEMNKGGAIEVLMPVVQPAELWQESGRWndyGAELLRFVDRGSRDFVLGPTHEEVItdlVRREVSSYKQL 128
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGHE---PKDLLPVGAENEEDLYLRPTLEPGL---VRLFVSHIRKL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491812279 129 PLNLYQIQTKFRDEvRPRFGVMRSREFVMKDAYSFHVDKASLQETYDVMYQVYSnIFTRLG--LDFRAVQADTGSIG-GS 205
Cdd:cd00768 75 PLRLAEIGPAFRNE-GGRRGLRRVREFTQLEGEVFGEDGEEASEFEELIELTEE-LLRALGikLDIVFVEKTPGEFSpGG 152
|
170
....*....|....*
gi 491812279 206 ASHEFQVLASSGEDD 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 |
1.64e-15 |
|
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain. This subfamily contains the core domain of ProRS from archaea, the cytoplasm of eukaryotes and some bacteria.
Pssm-ID: 238401 [Multi-domain] Cd Length: 261 Bit Score: 76.48 E-value: 1.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491812279 23 HQLMLRAGMI--RPMaSGLYNWLPTGIKVLKKVENIIREEMNKGGAIEVLMPVVQP-AELWQESGRWNDYGAELLrFVDR 99
Cdd:cd00778 7 TEVITKAELIdyGPV-KGCMVFRPYGYAIWENIQKILDKEIKETGHENVYFPLLIPeSELEKEKEHIEGFAPEVA-WVTH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491812279 100 GSRD-----FVLGPTHEEVITDLVRREVSSYKQLPLNLYQIQTKFRDEVRPRFGVMRSREFVMKDAYSFHVDKASLQETY 174
Cdd:cd00778 85 GGLEeleepLALRPTSETAIYPMFSKWIRSYRDLPLKINQWVNVFRWETKTTRPFLRTREFLWQEGHTAHATEEEAEEEV 164
|
170
....*....|....
gi 491812279 175 DVMYQVYSNIFTRL 188
Cdd:cd00778 165 LQILDLYKEFYEDL 178
|
|
| ProRS_anticodon_zinc |
cd00862 |
ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and ... |
469-567 |
5.33e-13 |
|
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: 68.09 E-value: 5.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491812279 469 EIAPFTVAIVPM--NMHKSESVQQFSEELYRTLKAQGVDVIFDDRKE-RPGVMFADMELIGVPHMVVIGEKNLANGEIEY 545
Cdd:cd00862 7 RVAPIQVVIVPIgiKDEKREEVLEAADELAERLKAAGIRVHVDDRDNyTPGWKFNDWELKGVPLRIEIGPRDLEKNTVVI 86
|
90 100
....*....|....*....|..
gi 491812279 546 KNRRTGEKQMIAKDQLLAFLKE 567
Cdd:cd00862 87 VRRDTGEKKTVPLAELVEKVPE 108
|
|
| ThrRS_core |
cd00771 |
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ... |
36-163 |
9.05e-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: 69.12 E-value: 9.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491812279 36 ASGLYNWLPTGIKVLKKVENIIREEMNKGGAIEVLMPVVQPAELWQESGRWNDYGAELLRFvDRGSRDFVLGPT----HE 111
Cdd:cd00771 19 GPGLPFWLPKGAIIRNELEDFLRELQRKRGYQEVETPIIYNKELWETSGHWDHYRENMFPF-EEEDEEYGLKPMncpgHC 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 491812279 112 EVITDLVRrevsSYKQLPLNLYQIQTKFRDEVRPRF-GVMRSREFVMKDAYSF 163
Cdd:cd00771 98 LIFKSKPR----SYRDLPLRLAEFGTVHRYEQSGALhGLTRVRGFTQDDAHIF 146
|
|
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
443-571 |
2.80e-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: 56.28 E-value: 2.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491812279 443 GIGVTRVVAAAIEQhhddrGIIWPSDEIAPftVAIVPMnmhkSESVQQFSEELYRTLKAQG--VDVIFDDRKERPGVMFA 520
Cdd:COG0124 305 AIGLERLLLLLEEL-----GLLPAAEPPPD--VYVVPL----GEEARAEALKLAQELRAAGirVELDLGGRKLKKQLKYA 373
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 491812279 521 DMelIGVPHMVVIGEKNLANGEIEYKNRRTGEKQMIAKDQLLAFLKENVKA 571
Cdd:COG0124 374 DK--SGAPFVLILGEDELANGTVTLKDLATGEQETVPLDELVEYLKELLAE 422
|
|
| PRK03991 |
PRK03991 |
threonyl-tRNA synthetase; Validated |
470-570 |
1.86e-07 |
|
threonyl-tRNA synthetase; Validated
Pssm-ID: 235190 [Multi-domain] Cd Length: 613 Bit Score: 54.11 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491812279 470 IAPFTVAIVPMnmhkSESVQQFSEELYRTLKAQGVDVIFDDRKERPGVMFADMELIGVPHMVVIGEKNLANGEIEYKNRR 549
Cdd:PRK03991 497 LSPTQVRVIPV----SERHLDYAEEVADKLEAAGIRVDVDDRDESLGKKIRDAGKEWIPYVVVIGDKEMESGKLTVTIRE 572
|
90 100
....*....|....*....|.
gi 491812279 550 TGEKQMIAKDQLLAFLKENVK 570
Cdd:PRK03991 573 ESEKVEMTLEELIERIKEETK 593
|
|
| ThrRS_anticodon |
cd00860 |
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases ... |
472-566 |
2.78e-07 |
|
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only.
Pssm-ID: 238437 [Multi-domain] Cd Length: 91 Bit Score: 48.65 E-value: 2.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491812279 472 PFTVAIVPMNmhksESVQQFSEELYRTLKAQGVDVIFDDRKERPGVMFADMELIGVPHMVVIGEKNLANGEIEYKNRRTG 551
Cdd:cd00860 1 PVQVVVIPVT----DEHLDYAKEVAKKLSDAGIRVEVDLRNEKLGKKIREAQLQKIPYILVVGDKEVETGTVSVRTRDGG 76
|
90
....*....|....*
gi 491812279 552 EKQMIAKDQLLAFLK 566
Cdd:cd00860 77 DLGSMSLDEFIEKLK 91
|
|
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
470-570 |
2.82e-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: 53.50 E-value: 2.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491812279 470 IAPFTVAIVPMnmhkSESVQQFSEELYRTLKAQGVDVIFDDRKERPGVMFADMELIGVPHMVVIGEKNLANGEIEYKNRR 549
Cdd:COG0441 537 LAPVQVVVLPI----SDKHADYAKEVAKKLRAAGIRVEVDLRNEKIGYKIREAQLQKVPYMLVVGDKEVENGTVSVRRRG 612
|
90 100
....*....|....*....|.
gi 491812279 550 TGEKQMIAKDQLLAFLKENVK 570
Cdd:COG0441 613 GGDLGTMSLDEFIARLKEEIR 633
|
|
| HisRS_anticodon |
cd00859 |
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases ... |
494-566 |
2.93e-06 |
|
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: 45.61 E-value: 2.93e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491812279 494 ELYRTLKAQGVDVIFDDRKERPGVMFADMELIGVPHMVVIGEKNLANGEIEYKNRRTGEKQMIAKDQLLAFLK 566
Cdd:cd00859 19 ELAEQLRDAGIKAEIDYGGRKLKKQFKYADRSGARFAVILGEDELAAGVVTVKDLETGEQETVALDELVEELK 91
|
|
| PLN02908 |
PLN02908 |
threonyl-tRNA synthetase |
31-192 |
3.09e-06 |
|
threonyl-tRNA synthetase
Pssm-ID: 178496 [Multi-domain] Cd Length: 686 Bit Score: 50.15 E-value: 3.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491812279 31 MIRPMASGLYNWLPTGIKVLKKVENIIREEMNKGGAIEVLMPVVQPAELWQESGRWNDYGAELLRFvDRGSRDFVLGPT- 109
Cdd:PLN02908 305 FFHELSPGSCFFLPHGARIYNKLMDFIREQYWERGYDEVITPNIYNMDLWETSGHAAHYKENMFVF-EIEKQEFGLKPMn 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491812279 110 ---HEEVITDLVRrevsSYKQLPLNLYQIQTKFRDEVRPRF-GVMRSREFVMKDAYSFHVD---KASLQETYDVMYQVYs 182
Cdd:PLN02908 384 cpgHCLMFAHRVR----SYRELPLRLADFGVLHRNELSGALtGLTRVRRFQQDDAHIFCREdqiKDEVKGVLDFLDYVY- 458
|
170
....*....|
gi 491812279 183 NIFtrlGLDF 192
Cdd:PLN02908 459 EVF---GFTY 465
|
|
| PRK12444 |
PRK12444 |
threonyl-tRNA synthetase; Reviewed |
31-163 |
6.68e-06 |
|
threonyl-tRNA synthetase; Reviewed
Pssm-ID: 183530 [Multi-domain] Cd Length: 639 Bit Score: 48.98 E-value: 6.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491812279 31 MIRPMASGLYNWLPTGIKVLKKVENIIREEMNKGGAIEVLMPVVQPAELWQESGRWNDYgAELLRFVDRGSRDFVLGPTH 110
Cdd:PRK12444 258 MFSEEAPGMPFYLPKGQIIRNELEAFLREIQKEYNYQEVRTPFMMNQELWERSGHWDHY-KDNMYFSEVDNKSFALKPMN 336
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 491812279 111 EEVITDLVRREVSSYKQLPLNLYQIQTKFRDEVRPRF-GVMRSREFVMKDAYSF 163
Cdd:PRK12444 337 CPGHMLMFKNKLHSYRELPIRMCEFGQVHRHEFSGALnGLLRVRTFCQDDAHLF 390
|
|
| PRK12444 |
PRK12444 |
threonyl-tRNA synthetase; Reviewed |
403-570 |
8.50e-06 |
|
threonyl-tRNA synthetase; Reviewed
Pssm-ID: 183530 [Multi-domain] Cd Length: 639 Bit Score: 48.59 E-value: 8.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491812279 403 IKRGIEVGHIfQLGTKYSEAMKATVQGEDG---KPLVMTMGCYGiGVTRVVAAAIEqHHDDRGIIWpsdeIAPFTVAIVP 479
Cdd:PRK12444 476 LNRSHQCGTI-QLDFQMPEKFDLNYIDEKNekrRPVVIHRAVLG-SLDRFLAILIE-HFGGAFPAW----LAPVQVKVIP 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491812279 480 MnmhkSESVQ-QFSEELYRTLKAQGVDVIFDDRKERPGVMFADMELIGVPHMVVIGEKNLANGEIEYKNRRTGEKQMIAK 558
Cdd:PRK12444 549 V----SNAVHvQYADEVADKLAQAGIRVERDERDEKLGYKIREAQMQKIPYVLVIGDKEMENGAVNVRKYGEEKSEVIEL 624
|
170
....*....|..
gi 491812279 559 DQLLAFLKENVK 570
Cdd:PRK12444 625 DMFVESIKEEIK 636
|
|
| EbsC |
COG2606 |
Cys-tRNA(Pro) deacylase, prolyl-tRNA editing enzyme YbaK/EbsC [Translation, ribosomal ... |
264-352 |
3.02e-05 |
|
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: 44.31 E-value: 3.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491812279 264 ELVEQFNLPIEKTVKTLIVKGatEEQPLVAlVLRGDHELNEIKAQKHpLVADPLEFADEAEIKA----KIGaGVGSLGVI 339
Cdd:COG2606 28 EAAEALGVPPEQIAKTLVFRG--DGGPVLA-VVPGDRRLDLKKLAAA-LGAKKVEMADPEEVERltgyEVG-GVSPFGLK 102
|
90
....*....|...
gi 491812279 340 NlNVPAIIDRSVA 352
Cdd:COG2606 103 K-GLPVYVDESLL 114
|
|
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
42-155 |
4.05e-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: 46.27 E-value: 4.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491812279 42 WLPTGIKVLKKVENIIREEMNKGGAIEVLMPVVQPAELWQESgrwndYGA-----ELLRFVDRGSRDFVLGPtheevitD 116
Cdd:COG0124 13 ILPEESAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARK-----IGEdivekEMYTFEDRGGRSLTLRP-------E 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 491812279 117 L----VRR--EVSSYKQLPLNLYQIQTKFRDEvRPRFGvmRSREF 155
Cdd:COG0124 81 GtapvARAvaEHGNELPFPFKLYYIGPVFRYE-RPQKG--RYRQF 122
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
48-155 |
4.31e-05 |
|
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: 45.29 E-value: 4.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491812279 48 KVLKKVENIIREEMNKGGAIEVLMPVVQPAELWQeSGRWNDYGAELLRFVDRGSRDFVLGPtheevitDL---VRREVSS 124
Cdd:cd00773 3 ALRRYIEDTLREVFERYGYEEIDTPVFEYTELFL-RKSGDEVSKEMYRFKDKGGRDLALRP-------DLtapVARAVAE 74
|
90 100 110
....*....|....*....|....*....|....
gi 491812279 125 YKQ---LPLNLYQIQTKFRDEvRPRFGvmRSREF 155
Cdd:cd00773 75 NLLslpLPLKLYYIGPVFRYE-RPQKG--RYREF 105
|
|
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
36-163 |
4.90e-05 |
|
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440210 [Multi-domain] Cd Length: 639 Bit Score: 46.18 E-value: 4.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491812279 36 ASGLYNWLPTGIKVLKKVENIIREEMNKGGAIEVLMPVVQPAELWQESGRWNDYgAELLRFVDRGSRDFVLG----PTHE 111
Cdd:COG0441 260 GPGLPFWHPKGAIIRRELEDYIREKHRKAGYQEVKTPHILDRELWETSGHWDHY-RENMFPTESDGEEYALKpmncPGHI 338
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 491812279 112 EVItdlvRREVSSYKQLPLNLYQIQTKFRDEvrpRFGV----MRSREFVMKDAYSF 163
Cdd:COG0441 339 LIY----KSGLRSYRDLPLRLAEFGTVHRYE---PSGAlhglMRVRGFTQDDAHIF 387
|
|
| PLN02908 |
PLN02908 |
threonyl-tRNA synthetase |
465-571 |
5.67e-04 |
|
threonyl-tRNA synthetase
Pssm-ID: 178496 [Multi-domain] Cd Length: 686 Bit Score: 42.84 E-value: 5.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491812279 465 WPSdEIAPFTVAIVPMnmhkSESVQQFSEELYRTLKAQG--VDVIFDDRKERPGVMFADMELIGvpHMVVIGEKNLANGE 542
Cdd:PLN02908 583 WPF-WLSPRQAIVVPI----SEKSQDYAEEVRAQLHAAGfyVDVDVTDRKIQKKVREAQLAQYN--YILVVGEAEAATGT 655
|
90 100
....*....|....*....|....*....
gi 491812279 543 IEYKNRRTGEKQMIAKDQLLAFLKENVKA 571
Cdd:PLN02908 656 VNVRTRDNVVHGEKKIEELLTEFKEERAE 684
|
|
| SerRS_core |
cd00770 |
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the ... |
61-207 |
3.66e-03 |
|
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the attachment of serine to the 3' OH group of ribose of the appropriate tRNA. This domain It is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain. SerRS synthetase is a homodimer.
Pssm-ID: 238393 [Multi-domain] Cd Length: 297 Bit Score: 39.47 E-value: 3.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491812279 61 MNKGGAIEVLMPVVQPAELWQESGRWNDYGAELLRFVDRgsrDFVLGPTHEEVITDLVRREVSSYKQLPLNLYQIQTKFR 140
Cdd:cd00770 66 LTKRGFTPVIPPFLVRKEVMEGTGQLPKFDEQLYKVEGE---DLYLIATAEVPLAALHRDEILEEEELPLKYAGYSPCFR 142
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491812279 141 DEV----RPRFGVMRSREFVMKDAYSFHVDKASLQEtYDVMYQVYSNIFTRLGLDFRAVQADTGSIGGSAS 207
Cdd:cd00770 143 KEAgsagRDTRGLFRVHQFEKVEQFVFTKPEESWEE-LEELISNAEEILQELGLPYRVVNICTGDLGFAAA 212
|
|
| PLN02837 |
PLN02837 |
threonine-tRNA ligase |
38-163 |
3.85e-03 |
|
threonine-tRNA ligase
Pssm-ID: 215450 [Multi-domain] Cd Length: 614 Bit Score: 40.27 E-value: 3.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491812279 38 GLYNWLPTGIKVLKKVENIIREEMNKGGAIEVLMPVVQPAELWQESGRWNDYGAELLRFVDRGSRDFVLGPTHEEVITDL 117
Cdd:PLN02837 238 GLVFWHPKGAIVRHIIEDSWKKMHFEHGYDLLYTPHVAKADLWKTSGHLDFYKENMYDQMDIEDELYQLRPMNCPYHILV 317
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 491812279 118 VRREVSSYKQLPLNLYQIQTKFRDEVRPRF-GVMRSREFVMKDAYSF 163
Cdd:PLN02837 318 YKRKLHSYRDLPIRVAELGTVYRYELSGSLhGLFRVRGFTQDDAHIF 364
|
|
| |
