|
Name |
Accession |
Description |
Interval |
E-value |
| proS_fam_I |
TIGR00408 |
prolyl-tRNA synthetase, family I; Prolyl-tRNA synthetase is a class II tRNA synthetase and is ... |
52-530 |
0e+00 |
|
prolyl-tRNA synthetase, family I; 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 families. This family includes the archaeal enzyme, the Pro-specific domain of a human multifunctional tRNA ligase, and the enzyme from the spirochete Borrelia burgdorferi. The other family includes enzymes from Escherichia coli, Bacillus subtilis, Synechocystis PCC6803, and one of the two prolyL-tRNA synthetases of Saccharomyces cerevisiae. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273062 [Multi-domain] Cd Length: 472 Bit Score: 563.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695549 52 VKKDENFGEWYSEVC-KQDMIEYYDISGCYILRPWSMAIWEIMQIFFDAEIKKMKVKNCYFPLFVSPGVLEKEKDHIEGF 130
Cdd:TIGR00408 2 ASKMQDFSEWYHQILeKAEIIDYYPVKGCYVWLPYGFKIWKNIQKILRNILDEIGHEEVYFPMLIPESELAKEKDHIKGF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695549 131 APEVAWVTKSGKSDLEVPIAIRPTSETVMYPYYSKWIRGHRDLPLKLNQWCNVVRWEFSNPTPFIRSREFLWQEGHTAFA 210
Cdd:TIGR00408 82 EPEVYWITHGGLSKLDEPLALRPTSETAMYPMFKKWVKSYTDLPLKINQWVNVFRYETKHTRPFLRTREFTWQEAHTAHA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695549 211 TKAEADEEVLQILELYRRIYEEYLAVPVVKGMKSENEKFAGGLYTTSVEAFIPNtGRGVQGATSHCLGQNFAKMFEINFE 290
Cdd:TIGR00408 162 TAEEAEEQVLRALDIYKEFIENSLAIPYFVGRKPEWEKFAGAEYTWAFETIMPD-GRTLQIATSHNLGQNFAKTFEIKFE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695549 291 NEKAETEMVWQNSWAYSTRTIGVMIMTHGDDKGLVLPPKVASVQVVVIPVPYKDANTQGIYDACTATASALCEAGIRAEE 370
Cdd:TIGR00408 241 TPTGDKEYAYQTSYGISTRVIGALIAIHSDEKGLVLPPRVAPIQVVIIPIIFKKKENEKVMEAAREVRSRLKKAGFRVHI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695549 371 DLRDNySPGWKYSDWEMKGVPLRIEIGPRDLENDQVRTVRRDNGVKEDIPRGSLVEHVKELLEKIQQNMYEVAKQKREAC 450
Cdd:TIGR00408 321 DDRDN-RPGRKFYQWEIKGIPLRIEVGPNDIEKNIAVISRRDTGEKYQVSLDQLEERVVELLNNIQENLRNRAWERFEQK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695549 451 VQEVKTWDEFIKALNEKK-LILAPWCDEEEVERDVKartkgETGAAKTLCSPFDQPELpegTLCFASGKPAKKWTYWGRS 529
Cdd:TIGR00408 400 IVIVETLEEIKQALNEKRgVVLVPWCGEEECEEDLK-----EKVQVTILCIPEDGDVL---QLCIFCGRKAPDYVLIART 471
|
.
gi 30695549 530 Y 530
Cdd:TIGR00408 472 Y 472
|
|
| ProRS_core_arch_euk |
cd00778 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
57-317 |
1.25e-160 |
|
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: 457.06 E-value: 1.25e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695549 57 NFGEWYSEVC-KQDMIEYYDISGCYILRPWSMAIWEIMQIFFDAEIKKMKVKNCYFPLFVSPGVLEKEKDHIEGFAPEVA 135
Cdd:cd00778 1 DFSEWYTEVItKAELIDYGPVKGCMVFRPYGYAIWENIQKILDKEIKETGHENVYFPLLIPESELEKEKEHIEGFAPEVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695549 136 WVTKSGKSDLEVPIAIRPTSETVMYPYYSKWIRGHRDLPLKLNQWCNVVRWEFSNPTPFIRSREFLWQEGHTAFATKAEA 215
Cdd:cd00778 81 WVTHGGLEELEEPLALRPTSETAIYPMFSKWIRSYRDLPLKINQWVNVFRWETKTTRPFLRTREFLWQEGHTAHATEEEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695549 216 DEEVLQILELYRRIYEEYLAVPVVKGMKSENEKFAGGLYTTSVEAFIPNtGRGVQGATSHCLGQNFAKMFEINFENEKAE 295
Cdd:cd00778 161 EEEVLQILDLYKEFYEDLLAIPVVKGRKTEWEKFAGADYTYTIEAMMPD-GRALQSGTSHNLGQNFSKAFDIKYQDKDGQ 239
|
250 260
....*....|....*....|..
gi 30695549 296 TEMVWQNSWAYSTRTIGVMIMT 317
Cdd:cd00778 240 KEYVHQTSWGISTRLIGAIIMI 261
|
|
| ProS |
COG0442 |
Prolyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Prolyl-tRNA ... |
56-432 |
2.97e-92 |
|
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: 292.45 E-value: 2.97e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695549 56 ENFGEWYSEVCKQ-DMIEYYdISGCYILRPWSMAIWE-IMQIFfDAEIKKMKVKNCYFPLFVsPGVLEKEKDHIEGFAPE 133
Cdd:COG0442 16 ADAEVWSHQLMLRaGLIRKL-ASGIYTYLPLGYRVLEkIEAIV-REEMKRTGAQEVLMPLLQ-PAELWEESGRWEGFGPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695549 134 VAWVTKSGKSDLevpiAIRPTSETVMYPYYSKWIRGHRDLPLKLNQWCNVVRWEFSNPTPFIRSREFLWQEGHTAFATKA 213
Cdd:COG0442 93 LARVTDRLEREF----CLGPTHEEVITDLVRNEIKSYRDLPLLLYQIQTKFRDEIRPRFGLLRTREFLMKDAYSFHATEE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695549 214 EADEEVLQILELYRRIYEEyLAVPVVKGMK-------SENEKFA--------------GGLYTTSVEAFI---------- 262
Cdd:COG0442 169 ELDEEYQKMLDAYERIFER-LGLPVRAVEAdsgaiggSESHEFMvladsgedtivycdACDYAANIEKAEalappaerae 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695549 263 ----------PNT------------------------------------------------------------------- 265
Cdd:COG0442 248 ptkeleavatPGAktieevaeflgvpaektvktlvykadgelvavlvrgdhelneiklenllgaselelateeeieaalg 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695549 266 -------------------------------------------------------------------------GRGVQGA 272
Cdd:COG0442 328 avpgflgpvglgvpyiadrsvagmsnfvcganeddyhytnvnwgrdfpvdevadlrnvvegdpcpdcggllqdGRGIEVG 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695549 273 TSHCLGQNFAKMFEINFENEKAETEMVWQNSWAYS-TRTIGVMIMTHGDDKGLVLPPKVASVQVVVIPVPYKDAntqGIY 351
Cdd:COG0442 408 HIFKLGTKYSKAMDATFLDENGKEQPVWMGCYGIGvTRLIAAAIEQHHDDKGIIWPPAIAPFQVVIVPINMKDE---AVL 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695549 352 DACTATASALCEAGIRAEEDLRDNySPGWKYSDWEMKGVPLRIEIGPRDLENDQVRTVRRDNGVKEDIPRGSLVEHVKEL 431
Cdd:COG0442 485 EAAEELYAELKAAGIDVLLDDRDE-RPGVKFADAELIGIPLRIVIGPRDLEEGQVEVKRRDTGEKEEVPLDELVETVKEL 563
|
.
gi 30695549 432 L 432
Cdd:COG0442 564 L 564
|
|
| ProRS-C_1 |
pfam09180 |
Prolyl-tRNA synthetase, C-terminal; Members of this family are predominantly found in ... |
457-530 |
1.55e-26 |
|
Prolyl-tRNA synthetase, C-terminal; Members of this family are predominantly found in prokaryotic prolyl-tRNA synthetase. They contain a zinc binding site, and adopt a structure consisting of alpha helices and antiparallel beta sheets arranged in 2 layers, in a beta-alpha-beta-alpha-beta motif.
Pssm-ID: 462709 Cd Length: 67 Bit Score: 102.21 E-value: 1.55e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30695549 457 WDEFIKALNEKKLILAPWCDEEEVERDVKARTKgetgaAKTLCSPFDQPElpEGTLCFASGKPAKKWTYWGRSY 530
Cdd:pfam09180 1 WEEFKEALEEKGFVLAPWCGDEECEDKIKEETG-----ATSRCIPFDQEE--EGGKCIVCGKPAKKWVLFARSY 67
|
|
| ProRS-C_1 |
smart00946 |
Prolyl-tRNA synthetase, C-terminal; Members of this family are predominantly found in ... |
457-530 |
7.64e-23 |
|
Prolyl-tRNA synthetase, C-terminal; Members of this family are predominantly found in prokaryotic prolyl-tRNA synthetase. They contain a zinc binding site, and adopt a structure consisting of alpha helices and antiparallel beta sheets arranged in 2 layers, in a beta-alpha-beta-alpha-beta motif.
Pssm-ID: 198014 Cd Length: 67 Bit Score: 91.86 E-value: 7.64e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30695549 457 WDEFIKALNEKKLILAPWCDEEEVERDVKARTKgetgaAKTLCSPFDQPELPEGtlCFASGKPAKKWTYWGRSY 530
Cdd:smart00946 1 LEEFKKALEEGKFVLAPWCGDEECEEKIKEETG-----ATIRCIPFDQDEEPGK--CVVCGKPAKKWVLFARSY 67
|
|
| PRK09194 |
PRK09194 |
prolyl-tRNA synthetase; Provisional |
277-432 |
4.16e-19 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 236405 [Multi-domain] Cd Length: 565 Bit Score: 90.53 E-value: 4.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695549 277 LGQNFAKMFEINFENEKAETEMVWQNSwaYS---TRTIGVMIMTHGDDKGLVLPPKVASVQVVVIPVPYKDANtqgIYDA 353
Cdd:PRK09194 412 LGTKYSEAMNATVLDENGKAQPLIMGC--YGigvSRLVAAAIEQNHDEKGIIWPKAIAPFDVHIVPVNMKDEE---VKEL 486
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30695549 354 CTATASALCEAGIRAEEDLRDNySPGWKYSDWEMKGVPLRIEIGPRDLENDQVRTVRRDNGVKEDIPRGSLVEHVKELL 432
Cdd:PRK09194 487 AEKLYAELQAAGIEVLLDDRKE-RPGVKFADADLIGIPHRIVVGDRGLAEGIVEYKDRRTGEKEEVPVDELVEFLKALK 564
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| proS_fam_I |
TIGR00408 |
prolyl-tRNA synthetase, family I; Prolyl-tRNA synthetase is a class II tRNA synthetase and is ... |
52-530 |
0e+00 |
|
prolyl-tRNA synthetase, family I; 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 families. This family includes the archaeal enzyme, the Pro-specific domain of a human multifunctional tRNA ligase, and the enzyme from the spirochete Borrelia burgdorferi. The other family includes enzymes from Escherichia coli, Bacillus subtilis, Synechocystis PCC6803, and one of the two prolyL-tRNA synthetases of Saccharomyces cerevisiae. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273062 [Multi-domain] Cd Length: 472 Bit Score: 563.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695549 52 VKKDENFGEWYSEVC-KQDMIEYYDISGCYILRPWSMAIWEIMQIFFDAEIKKMKVKNCYFPLFVSPGVLEKEKDHIEGF 130
Cdd:TIGR00408 2 ASKMQDFSEWYHQILeKAEIIDYYPVKGCYVWLPYGFKIWKNIQKILRNILDEIGHEEVYFPMLIPESELAKEKDHIKGF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695549 131 APEVAWVTKSGKSDLEVPIAIRPTSETVMYPYYSKWIRGHRDLPLKLNQWCNVVRWEFSNPTPFIRSREFLWQEGHTAFA 210
Cdd:TIGR00408 82 EPEVYWITHGGLSKLDEPLALRPTSETAMYPMFKKWVKSYTDLPLKINQWVNVFRYETKHTRPFLRTREFTWQEAHTAHA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695549 211 TKAEADEEVLQILELYRRIYEEYLAVPVVKGMKSENEKFAGGLYTTSVEAFIPNtGRGVQGATSHCLGQNFAKMFEINFE 290
Cdd:TIGR00408 162 TAEEAEEQVLRALDIYKEFIENSLAIPYFVGRKPEWEKFAGAEYTWAFETIMPD-GRTLQIATSHNLGQNFAKTFEIKFE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695549 291 NEKAETEMVWQNSWAYSTRTIGVMIMTHGDDKGLVLPPKVASVQVVVIPVPYKDANTQGIYDACTATASALCEAGIRAEE 370
Cdd:TIGR00408 241 TPTGDKEYAYQTSYGISTRVIGALIAIHSDEKGLVLPPRVAPIQVVIIPIIFKKKENEKVMEAAREVRSRLKKAGFRVHI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695549 371 DLRDNySPGWKYSDWEMKGVPLRIEIGPRDLENDQVRTVRRDNGVKEDIPRGSLVEHVKELLEKIQQNMYEVAKQKREAC 450
Cdd:TIGR00408 321 DDRDN-RPGRKFYQWEIKGIPLRIEVGPNDIEKNIAVISRRDTGEKYQVSLDQLEERVVELLNNIQENLRNRAWERFEQK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695549 451 VQEVKTWDEFIKALNEKK-LILAPWCDEEEVERDVKartkgETGAAKTLCSPFDQPELpegTLCFASGKPAKKWTYWGRS 529
Cdd:TIGR00408 400 IVIVETLEEIKQALNEKRgVVLVPWCGEEECEEDLK-----EKVQVTILCIPEDGDVL---QLCIFCGRKAPDYVLIART 471
|
.
gi 30695549 530 Y 530
Cdd:TIGR00408 472 Y 472
|
|
| ProRS_core_arch_euk |
cd00778 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
57-317 |
1.25e-160 |
|
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: 457.06 E-value: 1.25e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695549 57 NFGEWYSEVC-KQDMIEYYDISGCYILRPWSMAIWEIMQIFFDAEIKKMKVKNCYFPLFVSPGVLEKEKDHIEGFAPEVA 135
Cdd:cd00778 1 DFSEWYTEVItKAELIDYGPVKGCMVFRPYGYAIWENIQKILDKEIKETGHENVYFPLLIPESELEKEKEHIEGFAPEVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695549 136 WVTKSGKSDLEVPIAIRPTSETVMYPYYSKWIRGHRDLPLKLNQWCNVVRWEFSNPTPFIRSREFLWQEGHTAFATKAEA 215
Cdd:cd00778 81 WVTHGGLEELEEPLALRPTSETAIYPMFSKWIRSYRDLPLKINQWVNVFRWETKTTRPFLRTREFLWQEGHTAHATEEEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695549 216 DEEVLQILELYRRIYEEYLAVPVVKGMKSENEKFAGGLYTTSVEAFIPNtGRGVQGATSHCLGQNFAKMFEINFENEKAE 295
Cdd:cd00778 161 EEEVLQILDLYKEFYEDLLAIPVVKGRKTEWEKFAGADYTYTIEAMMPD-GRALQSGTSHNLGQNFSKAFDIKYQDKDGQ 239
|
250 260
....*....|....*....|..
gi 30695549 296 TEMVWQNSWAYSTRTIGVMIMT 317
Cdd:cd00778 240 KEYVHQTSWGISTRLIGAIIMI 261
|
|
| ProRS_anticodon_zinc |
cd00862 |
ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and ... |
323-530 |
7.78e-99 |
|
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: 297.29 E-value: 7.78e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695549 323 GLVLPPKVASVQVVVIPVPYKDANTQGIYDACTATASALCEAGIRAEEDLRDNYSPGWKYSDWEMKGVPLRIEIGPRDLE 402
Cdd:cd00862 1 GLVLPPRVAPIQVVIVPIGIKDEKREEVLEAADELAERLKAAGIRVHVDDRDNYTPGWKFNDWELKGVPLRIEIGPRDLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695549 403 NDQVRTVRRDNGVKEDIPRGSLVEHVKELLEKIQQNMYEVAKQKREAcVQEVKTWDEFIKALNEKKLILAPWCDEEEVER 482
Cdd:cd00862 81 KNTVVIVRRDTGEKKTVPLAELVEKVPELLDEIQEDLYERALEFRDA-TRIVDTWEEFKEALNEKGIVLAPWCGEEECEE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 30695549 483 DVKARTKgetgaAKTLCSPFDQPELPEGTLCFASGKPAKKWTYWGRSY 530
Cdd:cd00862 160 EIKEETA-----ATILCIPFDEAKLEEGGKCVVCGRPAKAYARFAKSY 202
|
|
| ProS |
COG0442 |
Prolyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Prolyl-tRNA ... |
56-432 |
2.97e-92 |
|
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: 292.45 E-value: 2.97e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695549 56 ENFGEWYSEVCKQ-DMIEYYdISGCYILRPWSMAIWE-IMQIFfDAEIKKMKVKNCYFPLFVsPGVLEKEKDHIEGFAPE 133
Cdd:COG0442 16 ADAEVWSHQLMLRaGLIRKL-ASGIYTYLPLGYRVLEkIEAIV-REEMKRTGAQEVLMPLLQ-PAELWEESGRWEGFGPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695549 134 VAWVTKSGKSDLevpiAIRPTSETVMYPYYSKWIRGHRDLPLKLNQWCNVVRWEFSNPTPFIRSREFLWQEGHTAFATKA 213
Cdd:COG0442 93 LARVTDRLEREF----CLGPTHEEVITDLVRNEIKSYRDLPLLLYQIQTKFRDEIRPRFGLLRTREFLMKDAYSFHATEE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695549 214 EADEEVLQILELYRRIYEEyLAVPVVKGMK-------SENEKFA--------------GGLYTTSVEAFI---------- 262
Cdd:COG0442 169 ELDEEYQKMLDAYERIFER-LGLPVRAVEAdsgaiggSESHEFMvladsgedtivycdACDYAANIEKAEalappaerae 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695549 263 ----------PNT------------------------------------------------------------------- 265
Cdd:COG0442 248 ptkeleavatPGAktieevaeflgvpaektvktlvykadgelvavlvrgdhelneiklenllgaselelateeeieaalg 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695549 266 -------------------------------------------------------------------------GRGVQGA 272
Cdd:COG0442 328 avpgflgpvglgvpyiadrsvagmsnfvcganeddyhytnvnwgrdfpvdevadlrnvvegdpcpdcggllqdGRGIEVG 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695549 273 TSHCLGQNFAKMFEINFENEKAETEMVWQNSWAYS-TRTIGVMIMTHGDDKGLVLPPKVASVQVVVIPVPYKDAntqGIY 351
Cdd:COG0442 408 HIFKLGTKYSKAMDATFLDENGKEQPVWMGCYGIGvTRLIAAAIEQHHDDKGIIWPPAIAPFQVVIVPINMKDE---AVL 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695549 352 DACTATASALCEAGIRAEEDLRDNySPGWKYSDWEMKGVPLRIEIGPRDLENDQVRTVRRDNGVKEDIPRGSLVEHVKEL 431
Cdd:COG0442 485 EAAEELYAELKAAGIDVLLDDRDE-RPGVKFADAELIGIPLRIVIGPRDLEEGQVEVKRRDTGEKEEVPLDELVETVKEL 563
|
.
gi 30695549 432 L 432
Cdd:COG0442 564 L 564
|
|
| ProRS_core |
cd00772 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
57-317 |
3.90e-68 |
|
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: 220.32 E-value: 3.90e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695549 57 NFGEWYSEVC-KQDMIEYYDISGCYILRPWSMAIWEIMQIFFDAEIKKMKVKNCYFPLFVSPGVLEKEKDHIEGFAPEVA 135
Cdd:cd00772 1 DASEKSLEHIgKAELADQGPGRGIINFLPLAKAILDKIENVLDKMFKEHGAQNALFPFFILASFLEKEAEHDEGFSKELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695549 136 WVTKSGKSDLEVPIAIRPTSETVMYPYYSKWIRGHRDLPLKLNQWCNVVRWEFSNPTPFIRSREFLWQEGHTAFATKAEA 215
Cdd:cd00772 81 VFKDAGDEELEEDFALRPTLEENIGEIAAKFIKSWKDLPQHLNQIGNKFRDEIRPRFGFLRAREFIMKDGHSAHADAEEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695549 216 DEEVLQILELYRRIYEEYLAVPVVKGMKSENEKFAGGLYTTSVEAFIPNtGRGVQGATSHCLGQNFAKMFE--INFENEK 293
Cdd:cd00772 161 DEEFLNMLSAYAEIARDLAAIDFIEGEADEGAKFAGASKSREFEALMED-GKAKQAETGHIFGEGFARAFDlkAKFLDKD 239
|
250 260
....*....|....*....|....*
gi 30695549 294 AETEMVWQNSWAYS-TRTIGVMIMT 317
Cdd:cd00772 240 GKEKFFEMGCWGIGiSRFIGAIIEQ 264
|
|
| 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 ... |
88-304 |
1.60e-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: 119.03 E-value: 1.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695549 88 AIWEIMQIFFDAEIKKMKVKNCYFPLFVSPGVLEKEkDHIEGFAPEVAWVTKSGKSDLEVPIAIRPTSETVMYPYYSKWI 167
Cdd:cd00670 3 ALWRALERFLDDRMAEYGYQEILFPFLAPTVLFFKG-GHLDGYRKEMYTFEDKGRELRDTDLVLRPAACEPIYQIFSGEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695549 168 RGHRDLPLKLNQWCNVVRWEFSNPTPFIRSREFLWQEGHTaFATKAEADEEVLQILELYRRIYEEyLAVPVVKGMKSENE 247
Cdd:cd00670 82 LSYRALPLRLDQIGPCFRHEPSGRRGLMRVREFRQVEYVV-FGEPEEAEEERREWLELAEEIARE-LGLPVRVVVADDPF 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30695549 248 KFAGGL--------YTTSVEAFIPNTGRGVQGATSHCL--GQNFAKMFEINFEN-EKAETEMVWQNSW 304
Cdd:cd00670 160 FGRGGKrgldagreTVVEFELLLPLPGRAKETAVGSANvhLDHFGASFKIDEDGgGRAHTGCGGAGGE 227
|
|
| ProRS-C_1 |
pfam09180 |
Prolyl-tRNA synthetase, C-terminal; Members of this family are predominantly found in ... |
457-530 |
1.55e-26 |
|
Prolyl-tRNA synthetase, C-terminal; Members of this family are predominantly found in prokaryotic prolyl-tRNA synthetase. They contain a zinc binding site, and adopt a structure consisting of alpha helices and antiparallel beta sheets arranged in 2 layers, in a beta-alpha-beta-alpha-beta motif.
Pssm-ID: 462709 Cd Length: 67 Bit Score: 102.21 E-value: 1.55e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30695549 457 WDEFIKALNEKKLILAPWCDEEEVERDVKARTKgetgaAKTLCSPFDQPElpEGTLCFASGKPAKKWTYWGRSY 530
Cdd:pfam09180 1 WEEFKEALEEKGFVLAPWCGDEECEDKIKEETG-----ATSRCIPFDQEE--EGGKCIVCGKPAKKWVLFARSY 67
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
334-431 |
4.64e-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: 4.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695549 334 QVVVIPVpykDANTQGIYDACTATASALCEAGIRAEEDLRdNYSPGWKYSDWEMKGVPLRIEIGPRDLENDQVRTVRRDN 413
Cdd:pfam03129 1 QVVVIPL---GEKAEELEEYAQKLAEELRAAGIRVELDDR-NESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDT 76
|
90
....*....|....*...
gi 30695549 414 GVKEDIPRGSLVEHVKEL 431
Cdd:pfam03129 77 GEQETVSLDELVEKLKEL 94
|
|
| ProRS-C_1 |
smart00946 |
Prolyl-tRNA synthetase, C-terminal; Members of this family are predominantly found in ... |
457-530 |
7.64e-23 |
|
Prolyl-tRNA synthetase, C-terminal; Members of this family are predominantly found in prokaryotic prolyl-tRNA synthetase. They contain a zinc binding site, and adopt a structure consisting of alpha helices and antiparallel beta sheets arranged in 2 layers, in a beta-alpha-beta-alpha-beta motif.
Pssm-ID: 198014 Cd Length: 67 Bit Score: 91.86 E-value: 7.64e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30695549 457 WDEFIKALNEKKLILAPWCDEEEVERDVKARTKgetgaAKTLCSPFDQPELPEGtlCFASGKPAKKWTYWGRSY 530
Cdd:smart00946 1 LEEFKKALEEGKFVLAPWCGDEECEEKIKEETG-----ATIRCIPFDQDEEPGK--CVVCGKPAKKWVLFARSY 67
|
|
| PRK09194 |
PRK09194 |
prolyl-tRNA synthetase; Provisional |
277-432 |
4.16e-19 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 236405 [Multi-domain] Cd Length: 565 Bit Score: 90.53 E-value: 4.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695549 277 LGQNFAKMFEINFENEKAETEMVWQNSwaYS---TRTIGVMIMTHGDDKGLVLPPKVASVQVVVIPVPYKDANtqgIYDA 353
Cdd:PRK09194 412 LGTKYSEAMNATVLDENGKAQPLIMGC--YGigvSRLVAAAIEQNHDEKGIIWPKAIAPFDVHIVPVNMKDEE---VKEL 486
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30695549 354 CTATASALCEAGIRAEEDLRDNySPGWKYSDWEMKGVPLRIEIGPRDLENDQVRTVRRDNGVKEDIPRGSLVEHVKELL 432
Cdd:PRK09194 487 AEKLYAELQAAGIEVLLDDRKE-RPGVKFADADLIGIPHRIVVGDRGLAEGIVEYKDRRTGEKEEVPVDELVEFLKALK 564
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
142-299 |
6.54e-15 |
|
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely threonyl-tRNA members.
Pssm-ID: 395469 [Multi-domain] Cd Length: 181 Bit Score: 72.83 E-value: 6.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695549 142 KSDLEVPIAIRPTSETVMYPYYSKWIRGHRDLPLKLNQWCNVVRWEFSNPT-PFIRSREFLWQEGHTaFATKAEADEEVL 220
Cdd:pfam00587 4 EDENGDELALKPTNEPGHTLLFREEGLRSKDLPLKLAQFGTCFRHEASGDTrGLIRVRQFHQDDAHI-FHAPGQSPDELE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695549 221 QILELYRRIYE-EYLAVPVVKGMKSENEKFAGglYTTSVEAFIPNTGRGVQGATSHCLGQNFAKMFEINFENEKAETEMV 299
Cdd:pfam00587 83 DYIKLIDRVYSrLGLEVRVVRLSNSDGSAFYG--PKLDFEVVFPSLGKQRQTGTIQNDGFRLPRRLGIRYKDEDNESKFP 160
|
|
| HGTP_anticodon |
cd00738 |
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ... |
333-429 |
3.58e-14 |
|
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and prolyl tRNA synthetases, which are classified as a group of class II aminoacyl-tRNA synthetases (aaRS). In aaRSs, the anticodon binding domain is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only. This domain is also found in the accessory subunit of mitochondrial polymerase gamma (Pol gamma b).
Pssm-ID: 238379 [Multi-domain] Cd Length: 94 Bit Score: 68.19 E-value: 3.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695549 333 VQVVVIPVpykDANTQGIYDACTATASALCEAGIRAEEDLRDNySPGWKYSDWEMKGVPLRIEIGPRDLENDQVRTVRRD 412
Cdd:cd00738 2 IDVAIVPL---TDPRVEAREYAQKLLNALLANGIRVLYDDRER-KIGKKFREADLRGVPFAVVVGEDELENGKVTVKSRD 77
|
90
....*....|....*..
gi 30695549 413 NGVKEDIPRGSLVEHVK 429
Cdd:cd00738 78 TGESETLHVDELPEFLV 94
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
110-308 |
2.33e-13 |
|
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: 69.07 E-value: 2.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695549 110 YFPLFVSPGVLEKEKDHiegFAPEVAwvtksGKSDLEVPIAIRPTSETVMYPYYSKWIRghrDLPLKLNQWCNVVRWEFS 189
Cdd:cd00768 22 ETPIVEREPLLEKAGHE---PKDLLP-----VGAENEEDLYLRPTLEPGLVRLFVSHIR---KLPLRLAEIGPAFRNEGG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695549 190 nPTPFIRSREFLWQEGHTAFATkAEADEEVLQILELYRRIYEEY-LAVPVVKGMKSENEKFAGGlYTTSVEAFIPN-TGR 267
Cdd:cd00768 91 -RRGLRRVREFTQLEGEVFGED-GEEASEFEELIELTEELLRALgIKLDIVFVEKTPGEFSPGG-AGPGFEIEVDHpEGR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 30695549 268 GVQGATSHCLGQNFAKMFEINFENEKAETEMVWQNSWAYST 308
Cdd:cd00768 168 GLEIGSGGYRQDEQARAADLYFLDEALEYRYPPTIGFGLGL 208
|
|
| PRK12325 |
PRK12325 |
prolyl-tRNA synthetase; Provisional |
308-430 |
6.47e-11 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 237059 [Multi-domain] Cd Length: 439 Bit Score: 64.50 E-value: 6.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695549 308 TRTIGVMIMTHGDDKGLVLPPKVASVQVVVIPVPYKDANTQGiydACTATASALCEAGIRAEEDLRDNySPGWKYSDWEM 387
Cdd:PRK12325 321 SRLVAAIIEASHDDKGIIWPESVAPFKVGIINLKQGDEACDA---ACEKLYAALSAAGIDVLYDDTDE-RPGAKFATMDL 396
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 30695549 388 KGVPLRIEIGPRDLENDQVRTVRRDNGVKEDIPRGSLVEHVKE 430
Cdd:PRK12325 397 IGLPWQIIVGPKGLAEGKVELKDRKTGEREELSVEAAINRLTA 439
|
|
| ThrRS_anticodon |
cd00860 |
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases ... |
333-436 |
2.61e-09 |
|
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: 54.05 E-value: 2.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695549 333 VQVVVIPVpykdanTQGIYDACTATASALCEAGIRAEEDLRDNySPGWKYSDWEMKGVPLRIEIGPRDLENDQVrTVR-R 411
Cdd:cd00860 2 VQVVVIPV------TDEHLDYAKEVAKKLSDAGIRVEVDLRNE-KLGKKIREAQLQKIPYILVVGDKEVETGTV-SVRtR 73
|
90 100
....*....|....*....|....*
gi 30695549 412 DNGVKEDIPrgslvehVKELLEKIQ 436
Cdd:cd00860 74 DGGDLGSMS-------LDEFIEKLK 91
|
|
| ProRS_anticodon_short |
cd00861 |
ProRS Prolyl-anticodon binding domain, short version found predominantly in bacteria. ProRS ... |
334-429 |
6.07e-08 |
|
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: 50.28 E-value: 6.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695549 334 QVVVIPVPYKDANtqgIYDACTATASALCEAGIraeEDLRD--NYSPGWKYSDWEMKGVPLRIEIGPRDLENDQVRTVRR 411
Cdd:cd00861 3 DVVIIPMNMKDEV---QQELAEKLYAELQAAGV---DVLLDdrNERPGVKFADADLIGIPYRIVVGKKSAAEGIVEIKVR 76
|
90
....*....|....*...
gi 30695549 412 DNGVKEDIPRGSLVEHVK 429
Cdd:cd00861 77 KTGEKEEISIDELLEFLQ 94
|
|
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
309-448 |
6.31e-08 |
|
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: 55.42 E-value: 6.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695549 309 RTIGVMIMTHgddKGlVLPPKVASVQVVVIPVpykdANTQGIYdaCTATASALCEAGIRAEEDLRDNySPGWKYSDWEMK 388
Cdd:COG0441 520 RFIGILIEHY---AG-AFPLWLAPVQVVVLPI----SDKHADY--AKEVAKKLRAAGIRVEVDLRNE-KIGYKIREAQLQ 588
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30695549 389 GVPLRIEIGPRDLENDQVrTVR-RDNGVKEDIPrgslvehVKELLEKIQQnmyEVAKQKRE 448
Cdd:COG0441 589 KVPYMLVVGDKEVENGTV-SVRrRGGGDLGTMS-------LDEFIARLKE---EIRSRSLE 638
|
|
| PRK12444 |
PRK12444 |
threonyl-tRNA synthetase; Reviewed |
167-433 |
1.47e-07 |
|
threonyl-tRNA synthetase; Reviewed
Pssm-ID: 183530 [Multi-domain] Cd Length: 639 Bit Score: 53.98 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695549 167 IRGHRDLPLKLNQWCNVVRWEFSNP-TPFIRSREFLWQEGHTaFATKAEADEEVLQILELYRRIYE----EY-------- 233
Cdd:PRK12444 348 LHSYRELPIRMCEFGQVHRHEFSGAlNGLLRVRTFCQDDAHL-FVTPDQIEDEIKSVMAQIDYVYKtfgfEYevelstrp 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695549 234 --------------LAVPVVK---GMKSENEKFAGGLYTTSVEAFIPNT-GRGVQGATSHcLGQNFAKMFE---INFENE 292
Cdd:PRK12444 427 edsmgddelweqaeASLENVLqslNYKYRLNEGDGAFYGPKIDFHIKDAlNRSHQCGTIQ-LDFQMPEKFDlnyIDEKNE 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695549 293 KAETEMVWQNSWAYSTRTIGVMIMTHGDdkglVLPPKVASVQVVVIPVpykdanTQGIY-DACTATASALCEAGIRAEED 371
Cdd:PRK12444 506 KRRPVVIHRAVLGSLDRFLAILIEHFGG----AFPAWLAPVQVKVIPV------SNAVHvQYADEVADKLAQAGIRVERD 575
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30695549 372 LRDNySPGWKYSDWEMKGVPLRIEIGPRDLENDQVRTVRRDNGVKEDIPRGSLVEHVKELLE 433
Cdd:PRK12444 576 ERDE-KLGYKIREAQMQKIPYVLVIGDKEMENGAVNVRKYGEEKSEVIELDMFVESIKEEIK 636
|
|
| PRK03991 |
PRK03991 |
threonyl-tRNA synthetase; Validated |
326-433 |
8.84e-05 |
|
threonyl-tRNA synthetase; Validated
Pssm-ID: 235190 [Multi-domain] Cd Length: 613 Bit Score: 45.25 E-value: 8.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695549 326 LPPKVASVQVVVIPVpykdanTQGIYDACTATASALCEAGIRAEEDLRDNySPGWKYSDWEMKGVPLRIEIGPRDLENDQ 405
Cdd:PRK03991 493 LPTWLSPTQVRVIPV------SERHLDYAEEVADKLEAAGIRVDVDDRDE-SLGKKIRDAGKEWIPYVVVIGDKEMESGK 565
|
90 100
....*....|....*....|....*...
gi 30695549 406 VRTVRRDNGVKEDIPRGSLVEHVKELLE 433
Cdd:PRK03991 566 LTVTIREESEKVEMTLEELIERIKEETK 593
|
|
| ProRS_core_prok |
cd00779 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
153-240 |
1.70e-03 |
|
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: 40.25 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695549 153 PTSETVMYPYYSKWIRGHRDLPLKLNQwcnvVRWEFSN-PTP---FIRSREFLWQEGHTAFATKAEADEEVLQILELYRR 228
Cdd:cd00779 92 PTHEEVITDLVANEIKSYKQLPLNLYQ----IQTKFRDeIRPrfgLMRGREFLMKDAYSFDIDEESLEETYEKMYQAYSR 167
|
90
....*....|..
gi 30695549 229 IYEEyLAVPVVK 240
Cdd:cd00779 168 IFKR-LGLPFVK 178
|
|
| HisRS_anticodon |
cd00859 |
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases ... |
332-429 |
6.84e-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: 35.98 E-value: 6.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695549 332 SVQVVVIPVpykDANTQGIYdacTATASALCEAGIRAEEDLRD-NYSPGWKYSDweMKGVPLRIEIGPRDLENDQVrTVR 410
Cdd:cd00859 1 EVDVYVVPL---GEGALSEA---LELAEQLRDAGIKAEIDYGGrKLKKQFKYAD--RSGARFAVILGEDELAAGVV-TVK 71
|
90 100
....*....|....*....|
gi 30695549 411 R-DNGVKEDIPRGSLVEHVK 429
Cdd:cd00859 72 DlETGEQETVALDELVEELK 91
|
|
| |
