|
Name |
Accession |
Description |
Interval |
E-value |
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
1-642 |
0e+00 |
|
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: 1153.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 1 MIKITFPDGAVREFESGVTTFDIAESISKSLAKKALAGKFNDQLIDTTRAIEEDGSIEIVTPDHKDAYEVLRHSAAHLFA 80
Cdd:COG0441 1 MIKITLPDGSVREFEAGVTVLDVAKSISPGLAKAAVAAKVNGELVDLSTPIEEDAELEIVTFDDEEGLEILRHSAAHLLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 81 QAAKRLFPNLHLGVGPAIAEGFYYDTDNAEgQISNEDLPRIEAEMQKIVTENYPCIREEVTKEEALELFK--DDPYKVEL 158
Cdd:COG0441 81 QAVKRLYPDAKLTIGPVIENGFYYDFDLER-PFTPEDLEKIEKEMKEIIKEDLPIEREEVSREEAIELFKekGEPYKVEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 159 INEHAGAG-LTVYRQGEFVDLCRGPHVPSTGRIQVFHLLNVAGAYWRGNSDNNMMQRIYGTAWFDKKDLKAYLTRLEEAK 237
Cdd:COG0441 160 IEDIPEDEeISLYRQGEFVDLCRGPHVPSTGKIKAFKLLSVAGAYWRGDEKNKMLQRIYGTAFPKKKELDAYLHRLEEAK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 238 ERDHRKLGKELDLFMISQEVGQGLPFWLPDGATIRRTLERYITDKELASGYQHVYTPPLASVELYKTSGHWDHYQEDMFP 317
Cdd:COG0441 240 KRDHRKLGKELDLFHFQEEVGPGLPFWHPKGAIIRRELEDYIREKHRKAGYQEVKTPHILDRELWETSGHWDHYRENMFP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 318 vMDMgDGEEFVLRPMNCPHHIQVYKNHVRSYRELPIRIAELGMMHRYEKSGALSGLQRVREMTLNDGHIFVTPEQIQEEF 397
Cdd:COG0441 320 -TES-DGEEYALKPMNCPGHILIYKSGLRSYRDLPLRLAEFGTVHRYEPSGALHGLMRVRGFTQDDAHIFCTPDQIEDEI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 398 QRALQLIIDVYADFNLTDYRFRLSYRdpndTHKYYDNDEMWENAQSMLKAALDEMGVDYFEAEGEAAFYGPKLDIQVKTA 477
Cdd:COG0441 398 KKVIDLVLEVYKDFGFEDYYVKLSTR----PEKRIGSDEIWDKAEAALREALEELGLEYVINPGEGAFYGPKIDFQLKDA 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 478 LGNEETLSTIQLDFLLPERFDLKYIGADGEEHRPVMIHRGVISTMERFTAILIETYKGAFPTWLAPHQVTVIPISnEAHI 557
Cdd:COG0441 474 IGREWQCGTIQLDFNLPERFDLTYVGEDGEKHRPVMIHRAILGSIERFIGILIEHYAGAFPLWLAPVQVVVLPIS-DKHA 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 558 DYAWEVAKTLRDRGVRADVDDRNEKMQYKIRASQTSKIPYQLIVGDKEMEDKSVNVRRYGSKATHTESVEEFVENILADI 637
Cdd:COG0441 553 DYAKEVAKKLRAAGIRVEVDLRNEKIGYKIREAQLQKVPYMLVVGDKEVENGTVSVRRRGGGDLGTMSLDEFIARLKEEI 632
|
....*
gi 489075724 638 ARKSR 642
Cdd:COG0441 633 RSRSL 637
|
|
| thrS |
TIGR00418 |
threonyl-tRNA synthetase; This model represents the threonyl-tRNA synthetase found in most ... |
72-637 |
0e+00 |
|
threonyl-tRNA synthetase; This model represents the threonyl-tRNA synthetase found in most organisms. This protein is a class II tRNA synthetase, and is recognized by the pfam model tRNA-synt_2b. Note that B. subtilis has closely related isozymes thrS and thrZ. The N-terminal regions are quite dissimilar between archaeal and eubacterial forms, while some eukaryotic forms are missing sequence there altogether. . [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273068 [Multi-domain] Cd Length: 563 Bit Score: 789.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 72 RHSAAHLFAQAAKRLFPNLHLGVGPAIAEGFYYDTDNAEgQISNEDLPRIEAEMQKIVTENYPCIREEVTKEEALELFK- 150
Cdd:TIGR00418 1 RHSIAHLLAEALKQLYPDVKLAIGPVVEDGFYYDFELDR-SFTQEDLEKIEKDMKEIAKKNYPVAKLSVSLEEALEAFKv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 151 DDPYKVELINEHA-GAGLTVYRQGE-FVDLCRGPHVPSTGRIQVFHLLNVAGAYWRGNSDNNMMQRIYGTAWFDKKDLKA 228
Cdd:TIGR00418 80 LEPYKLELLDEIPnGVKRTPYGWGKaFVDLCKGPHLPNTSFIKAFKLEKVAGAYWRGDSKNKMLQRIYGTAWADKKQLAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 229 YLTRLEEAKERDHRKLGKELDLFMISQEVGQGLPFWLPDGATIRRTLERYITDKELASGYQHVYTPPLASVELYKTSGHW 308
Cdd:TIGR00418 160 YLLRLEEAKKRDHRKLGKELELFSFEPEIGPGLPFWLPKGATIRNLLEDFVRQKQIKYGYMEVETPIMYDLELWEISGHW 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 309 DHYQEDMFPVMDMgDGEEFVLRPMNCPHHIQVYKNHVRSYRELPIRIAELGMMHRYEKSGALSGLQRVREMTLNDGHIFV 388
Cdd:TIGR00418 240 DNYKERMFPFTEL-DNREFMLKPMNCPGHFLIFKSSLRSYRDLPLRIAELGYSHRYEQSGELHGLMRVRGFTQDDAHIFC 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 389 TPEQIQEEFQRALQLIIDVYADFNLTDYRFRLSYRDPNDthkYYDNDEMWENAQSMLKAALDEMGVDYFEAEGEAAFYGP 468
Cdd:TIGR00418 319 TEDQIKEEFKNQFRLIQKVYSDFGFSFDKYELSTRDPED---FIGEDELWEKAEAALEEALKELGVPYEIDPGRGAFYGP 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 469 KLDIQVKTALGNEETLSTIQLDFLLPERFDLKYIGADGEEHRPVMIHRGVISTMERFTAILIETYKGAFPTWLAPHQVTV 548
Cdd:TIGR00418 396 KIDFAFKDALGREWQCATVQLDFELPERFDLTYVDEDNEEKRPVMIHRAILGSIERFIAILLEKYAGNFPLWLAPVQVVV 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 549 IPISNEaHIDYAWEVAKTLRDRGVRADVDDRNEKMQYKIRASQTSKIPYQLIVGDKEMEDKSVNVRRYGSKATHTESVEE 628
Cdd:TIGR00418 476 IPVNER-HLDYAKKVAQKLKKAGIRVDVDDRNERLGKKIREAQKQKIPYMLVVGDKEMESLAVNVRTRKGQKLEKMSLDE 554
|
....*....
gi 489075724 629 FVENILADI 637
Cdd:TIGR00418 555 FLEKLRKEV 563
|
|
| PRK12444 |
PRK12444 |
threonyl-tRNA synthetase; Reviewed |
1-641 |
0e+00 |
|
threonyl-tRNA synthetase; Reviewed
Pssm-ID: 183530 [Multi-domain] Cd Length: 639 Bit Score: 768.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 1 MIKITFPDGAVREFESGVTTFDIAESISKSLAKKALAGKFNDQLIDTTRAIEEDGSIEIVTPDHKDAYEVLRHSAAHLFA 80
Cdd:PRK12444 5 MIEIKFPDGSVKEFVKGITLEEIAGSISSSLKKKAVAGKVNDKLYDLRRNLEEDAEVEIITIDSNEGVEIARHSAAHILA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 81 QAAKRLFPNLHLGVGPAIAEGFYYDTDnAEGQISNEDLPRIEAEMQKIVTENYPCIREEVTKEEALELFK--DDPYKVEL 158
Cdd:PRK12444 85 QAVKRLYGDVNLGVGPVIENGFYYDMD-LPSSVNVEDLRKIEKEMKKIINENIKIERVEVSREEAAKLFQemNDRLKLEL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 159 INE-HAGAGLTVYRQGEFVDLCRGPHVPSTGRIQVFHLLNVAGAYWRGNSDNNMMQRIYGTAWFDKKDLKAYLTRLEEAK 237
Cdd:PRK12444 164 LEAiPSGESITLYKQGEFVDLCRGPHLPSTGYLKAFQLTHVSGAYWRGDSNNQVLQRIYGVAFSSQKELEEYLHFVEEAA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 238 ERDHRKLGKELDLFMISQEvGQGLPFWLPDGATIRRTLERYITDKELASGYQHVYTPPLASVELYKTSGHWDHYQEDMFp 317
Cdd:PRK12444 244 KRNHRKLGKELELFMFSEE-APGMPFYLPKGQIIRNELEAFLREIQKEYNYQEVRTPFMMNQELWERSGHWDHYKDNMY- 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 318 vMDMGDGEEFVLRPMNCPHHIQVYKNHVRSYRELPIRIAELGMMHRYEKSGALSGLQRVREMTLNDGHIFVTPEQIQEEF 397
Cdd:PRK12444 322 -FSEVDNKSFALKPMNCPGHMLMFKNKLHSYRELPIRMCEFGQVHRHEFSGALNGLLRVRTFCQDDAHLFVTPDQIEDEI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 398 QRALQLIIDVYADFNLtDYRFRLSYRdPNDThkyYDNDEMWENAQSMLKAALDEMGVDYFEAEGEAAFYGPKLDIQVKTA 477
Cdd:PRK12444 401 KSVMAQIDYVYKTFGF-EYEVELSTR-PEDS---MGDDELWEQAEASLENVLQSLNYKYRLNEGDGAFYGPKIDFHIKDA 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 478 LGNEETLSTIQLDFLLPERFDLKYIGADGEEHRPVMIHRGVISTMERFTAILIETYKGAFPTWLAPHQVTVIPISNEAHI 557
Cdd:PRK12444 476 LNRSHQCGTIQLDFQMPEKFDLNYIDEKNEKRRPVVIHRAVLGSLDRFLAILIEHFGGAFPAWLAPVQVKVIPVSNAVHV 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 558 DYAWEVAKTLRDRGVRADVDDRNEKMQYKIRASQTSKIPYQLIVGDKEMEDKSVNVRRYGSKATHTESVEEFVENILADI 637
Cdd:PRK12444 556 QYADEVADKLAQAGIRVERDERDEKLGYKIREAQMQKIPYVLVIGDKEMENGAVNVRKYGEEKSEVIELDMFVESIKEEI 635
|
....
gi 489075724 638 ARKS 641
Cdd:PRK12444 636 KNRK 639
|
|
| PLN02908 |
PLN02908 |
threonyl-tRNA synthetase |
2-641 |
0e+00 |
|
threonyl-tRNA synthetase
Pssm-ID: 178496 [Multi-domain] Cd Length: 686 Bit Score: 622.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 2 IKITFPDGAVREFESGVTT-FDIAESISKSLAKKALAGKFNDQLIDTTRAIEEDGSIEIVTPDHKDAYEVLRHSAAHLFA 80
Cdd:PLN02908 52 IKVTLPDGAVKDGKKWVTTpMDIAKEISKGLANSALIAQVDGVLWDMTRPLEGDCKLKLFKFDDDEGRDTFWHSSAHILG 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 81 QAAKRLFpNLHLGVGPAIA--EGFYYDTDNAEGQISNEDLPRIEAEMQKIVTENYPCIREEVTKEEALELFKDDPYKVEL 158
Cdd:PLN02908 132 EALELEY-GCKLCIGPCTTrgEGFYYDAFYGDRTLNEEDFKPIEARAEKAVKEKQPFERIEVTREEALEMFSENKFKVEI 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 159 INE-HAGAGLTVYRQGEFVDLCRGPHVPSTGRIQVFHLLNVAGAYWRGNSDNNMMQRIYGTAWFDKKDLKAYLTRLEEAK 237
Cdd:PLN02908 211 INDlPEDATITVYRCGPLVDLCRGPHIPNTSFVKAFACLKASSAYWRGDVDRESLQRVYGISFPDKKLLKEYKHRIEEAK 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 238 ERDHRKLGKELDLFMiSQEVGQGLPFWLPDGATIRRTLERYITDKELASGYQHVYTPPLASVELYKTSGHWDHYQEDMFp 317
Cdd:PLN02908 291 KRDHRLLGQKQELFF-FHELSPGSCFFLPHGARIYNKLMDFIREQYWERGYDEVITPNIYNMDLWETSGHAAHYKENMF- 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 318 VMDMgDGEEFVLRPMNCPHHIQVYKNHVRSYRELPIRIAELGMMHRYEKSGALSGLQRVREMTLNDGHIFVTPEQIQEEF 397
Cdd:PLN02908 369 VFEI-EKQEFGLKPMNCPGHCLMFAHRVRSYRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCREDQIKDEV 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 398 QRALQLIIDVYADFNLTdYRFRLSYRdpndTHKYYDNDEMWENAQSMLKAALDEMGVDYFEAEGEAAFYGPKLDIQVKTA 477
Cdd:PLN02908 448 KGVLDFLDYVYEVFGFT-YELKLSTR----PEKYLGDLETWDKAEAALTEALNAFGKPWQLNEGDGAFYGPKIDITVSDA 522
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 478 LGNEETLSTIQLDFLLPERFDLKYIGADGEE-HRPVMIHRGVISTMERFTAILIETYKGAFPTWLAPHQVTVIPISnEAH 556
Cdd:PLN02908 523 LKRKFQCATVQLDFQLPIRFKLSYSAEDEAKiERPVMIHRAILGSVERMFAILLEHYAGKWPFWLSPRQAIVVPIS-EKS 601
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 557 IDYAWEVAKTLRDRGVRADVDDRNEKMQYKIRASQTSKIPYQLIVGDKEMEDKSVNVRRYGSKATHTESVEEFVENILAD 636
Cdd:PLN02908 602 QDYAEEVRAQLHAAGFYVDVDVTDRKIQKKVREAQLAQYNYILVVGEAEAATGTVNVRTRDNVVHGEKKIEELLTEFKEE 681
|
....*
gi 489075724 637 IARKS 641
Cdd:PLN02908 682 RAEFK 686
|
|
| PLN02837 |
PLN02837 |
threonine-tRNA ligase |
51-641 |
0e+00 |
|
threonine-tRNA ligase
Pssm-ID: 215450 [Multi-domain] Cd Length: 614 Bit Score: 548.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 51 IEEDGSIEIVTPDHKDAYEVLRHSAAHLFAQAAKRLFPNLHLGVGPAIAEGFYYDTDNAEgqISNEDLPRIEAEMQKIVT 130
Cdd:PLN02837 26 EAEPERVVLPTNESSEKLLKIRHTCAHVMAMAVQKLFPDAKVTIGPWIENGFYYDFDMEP--LTDKDLKRIKKEMDRIIS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 131 ENYPCIREEVTKEEALELFK--DDPYKVELINEHAGAGLTVYRQG-EFVDLCRGPHVPSTGRI--QVFHLLNVAGAYWRG 205
Cdd:PLN02837 104 RNLPLVREEVSREEAQKRIMaiNEPYKLEILEGIKEEPITIYHIGeEWWDLCAGPHVERTGKInkKAVELESVAGAYWRG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 206 NSDNNMMQRIYGTAWFDKKDLKAYLTRLEEAKERDHRKLGKELDLFMISQEVGQGLPFWLPDGATIRRTLERYITDKELA 285
Cdd:PLN02837 184 DEKNQMLQRIYGTAWESEEQLKAYLHFKEEAKRRDHRRLGQDLDLFSIQDDAGGGLVFWHPKGAIVRHIIEDSWKKMHFE 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 286 SGYQHVYTPPLASVELYKTSGHWDHYQEDMFPVMDMGDgEEFVLRPMNCPHHIQVYKNHVRSYRELPIRIAELGMMHRYE 365
Cdd:PLN02837 264 HGYDLLYTPHVAKADLWKTSGHLDFYKENMYDQMDIED-ELYQLRPMNCPYHILVYKRKLHSYRDLPIRVAELGTVYRYE 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 366 KSGALSGLQRVREMTLNDGHIFVTPEQIQEEFQRALQLIIDVYADFNLTDYRFRLSYRdpndTHKYYDNDEMWENAQSML 445
Cdd:PLN02837 343 LSGSLHGLFRVRGFTQDDAHIFCLEDQIKDEIRGVLDLTEEILKQFGFSKYEINLSTR----PEKSVGSDDIWEKATTAL 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 446 KAALDEMGVDYFEAEGEAAFYGPKLDIQVKTALGNEETLSTIQLDFLLPERFDLKYIGADGEEHRPVMIHRGVISTMERF 525
Cdd:PLN02837 419 RDALDDKGWEYKVDEGGGAFYGPKIDLKIEDALGRKWQCSTIQVDFNLPERFDITYVDSNSEKKRPIMIHRAILGSLERF 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 526 TAILIETYKGAFPTWLAPHQVTVIPISNEaHIDYAWEVAKTLRDRGVRADVdDRNEKMQYKIRASQTSKIPYQLIVGDKE 605
Cdd:PLN02837 499 FGVLIEHYAGDFPLWLAPVQARVLPVTDN-ELEYCKEVVAKLKAKGIRAEV-CHGERLPKLIRNAETQKIPLMAVVGPKE 576
|
570 580 590
....*....|....*....|....*....|....*.
gi 489075724 606 MEDKSVNVRRYGSKATHTESVEEFVENILADIARKS 641
Cdd:PLN02837 577 VETRTLTVRSRHGGELGTMPVDDFINRIQLAVENRT 612
|
|
| ThrRS_core |
cd00771 |
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ... |
240-543 |
1.04e-169 |
|
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: 485.90 E-value: 1.04e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 240 DHRKLGKELDLFMISQEVGQGLPFWLPDGATIRRTLERYITDKELASGYQHVYTPPLASVELYKTSGHWDHYQEDMFPVM 319
Cdd:cd00771 1 DHRRLGGELELFFFFDEAGPGLPFWLPKGAIIRNELEDFLRELQRKRGYQEVETPIIYNKELWETSGHWDHYRENMFPFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 320 dmGDGEEFVLRPMNCPHHIQVYKNHVRSYRELPIRIAELGMMHRYEKSGALSGLQRVREMTLNDGHIFVTPEQIQEEFQR 399
Cdd:cd00771 81 --EEDEEYGLKPMNCPGHCLIFKSKPRSYRDLPLRLAEFGTVHRYEQSGALHGLTRVRGFTQDDAHIFCTPDQIKEEIKG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 400 ALQLIIDVYADFNLTDYRFRLSYRDpndtHKYYDNDEMWENAQSMLKAALDEMGVDYFEAEGEAAFYGPKLDIQVKTALG 479
Cdd:cd00771 159 VLDLIKEVYSDFGFFDYKVELSTRP----EKFIGSDEVWEKAEAALREALEEIGLPYEINEGEGAFYGPKIDFHVKDALG 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489075724 480 NEETLSTIQLDFLLPERFDLKYIGADGEEHRPVMIHRGVISTMERFTAILIETYKGAFPTWLAP 543
Cdd:cd00771 235 REWQCSTIQLDFNLPERFDLTYIGEDGEKKRPVMIHRAILGSIERFIGILIEHYAGKFPLWLAP 298
|
|
| PRK03991 |
PRK03991 |
threonyl-tRNA synthetase; Validated |
264-643 |
4.16e-54 |
|
threonyl-tRNA synthetase; Validated
Pssm-ID: 235190 [Multi-domain] Cd Length: 613 Bit Score: 195.09 E-value: 4.16e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 264 WLPDGATIRRTLERYITDKELASGYQHVYTP---PLASVELYKtsgHWDHYQEDMFPVMdmGDGEEFVLRPMNCPHHIQV 340
Cdd:PRK03991 222 YYPKGRLIRDLLEDYVYNLVVELGAMPVETPimyDLSHPAIRE---HADKFGERQYRVK--SDKKDLMLRFAACFGQFLM 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 341 YKNHVRSYRELPIRIAELGMM-HRYEKSGALSGLQRVREMTLNDGHIFVTP-EQIQEEFQRALQLIIDVYADFNLT---D 415
Cdd:PRK03991 297 LKDMTISYKNLPLKMYELSTYsFRLEQRGELVGLKRLRAFTMPDMHTLCKDmEQAMEEFEKQYEMILETGEDLGRDyevA 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 416 YRFrlsyrdpndTHKYYDNDEMW--ENAQSMLKAALDEM---GVDYFEAegeaafygpKLDIQVKTALGNEETLSTIQLD 490
Cdd:PRK03991 377 IRF---------TEDFYEENKDWivELVKREGKPVLLEIlpeRKHYWVL---------KVEFAFIDSLGRPIENPTVQID 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 491 FLLPERFDLKYIGADGEEHRPVMIHRGVISTMERFT-AIL----IETYKG---AFPTWLAPHQVTVIPISnEAHIDYAWE 562
Cdd:PRK03991 439 VENAERFGIKYVDENGEEKYPIILHCSPTGSIERVIyALLekaaKEEEEGkvpMLPTWLSPTQVRVIPVS-ERHLDYAEE 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 563 VAKTLRDRGVRADVDDRNEKMQYKIRASQTSKIPYQLIVGDKEMEDKSVNVRRYGSKATHTESVEEFVENILADIA---R 639
Cdd:PRK03991 518 VADKLEAAGIRVDVDDRDESLGKKIRDAGKEWIPYVVVIGDKEMESGKLTVTIREESEKVEMTLEELIERIKEETKgypY 597
|
....
gi 489075724 640 KSRP 643
Cdd:PRK03991 598 RPLP 601
|
|
| ThrRS_anticodon |
cd00860 |
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases ... |
543-634 |
4.40e-39 |
|
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: 138.79 E-value: 4.40e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 543 PHQVTVIPIsNEAHIDYAWEVAKTLRDRGVRADVDDRNEKMQYKIRASQTSKIPYQLIVGDKEMEDKSVNVRRYGSKATH 622
Cdd:cd00860 1 PVQVVVIPV-TDEHLDYAKEVAKKLSDAGIRVEVDLRNEKLGKKIREAQLQKIPYILVVGDKEVETGTVSVRTRDGGDLG 79
|
90
....*....|..
gi 489075724 623 TESVEEFVENIL 634
Cdd:cd00860 80 SMSLDEFIEKLK 91
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
324-533 |
1.57e-35 |
|
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: 132.15 E-value: 1.57e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 324 GEEFVLRPMNCPHHIQVYKNH-VRSYReLPIRIAELGMMHRYEKSGALSGLQRVREMTLNDGHIFVTPEQIQEEFQRALQ 402
Cdd:pfam00587 8 GDELALKPTNEPGHTLLFREEgLRSKD-LPLKLAQFGTCFRHEASGDTRGLIRVRQFHQDDAHIFHAPGQSPDELEDYIK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 403 LIIDVYADFNLTDYRFRLSYRDpndthkyydndemwenaqsmlkaaldemgvdyfeaegEAAFYGPKLDIQVKT-ALGNE 481
Cdd:pfam00587 87 LIDRVYSRLGLEVRVVRLSNSD-------------------------------------GSAFYGPKLDFEVVFpSLGKQ 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489075724 482 ETLSTIQLD-FLLPERFDLKYIGADGEEHRPVMIHRGVIStMERFTAILIETY 533
Cdd:pfam00587 130 RQTGTIQNDgFRLPRRLGIRYKDEDNESKFPYMIHRAGLG-VERFLAAILENN 181
|
|
| 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 ... |
268-530 |
1.60e-29 |
|
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: 117.11 E-value: 1.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 268 GATIRRTLERYITDKELASGYQHVYTPPLASVELYKTSGHWDHYQEDMFPVMDMGD---GEEFVLRPMNCPHHIQVYKNH 344
Cdd:cd00670 1 GTALWRALERFLDDRMAEYGYQEILFPFLAPTVLFFKGGHLDGYRKEMYTFEDKGRelrDTDLVLRPAACEPIYQIFSGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 345 VRSYRELPIRIAELGMMHRYEKSGAlSGLQRVREMTLNDGHIFVTPEQIQEEFQRALQLIIDVYADFNLtDYRFRLSyrd 424
Cdd:cd00670 81 ILSYRALPLRLDQIGPCFRHEPSGR-RGLMRVREFRQVEYVVFGEPEEAEEERREWLELAEEIARELGL-PVRVVVA--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 425 pndthkyydNDEmwenaqsmlkaaldemgvDYFEA--EGEAAFYGPKLDIQVKTALGNEE-TLSTIQLDFLLPERFDLKY 501
Cdd:cd00670 156 ---------DDP------------------FFGRGgkRGLDAGRETVVEFELLLPLPGRAkETAVGSANVHLDHFGASFK 208
|
250 260
....*....|....*....|....*....
gi 489075724 502 IGADGEEHRPVMIHRGVIstMERFTAILI 530
Cdd:cd00670 209 IDEDGGGRAHTGCGGAGG--EERLVLALL 235
|
|
| TGS_ThrRS |
cd01667 |
TGS (ThrRS, GTPase and SpoT) domain found in threonyl-tRNA synthetase (ThrRS) and similar ... |
2-66 |
1.52e-26 |
|
TGS (ThrRS, GTPase and SpoT) domain found in threonyl-tRNA synthetase (ThrRS) and similar proteins; ThrRS, also termed cytoplasmic threonine--tRNA ligase, is a class II aminoacyl-tRNA synthetase (aaRS) that plays an essential role in protein synthesis by catalyzing the aminoacylation of tRNA(Thr), generating aminoacyl-tRNA, and editing misacylation. In addition to its catalytic and anticodon-binding domains, ThrRS has an N-terminal TGS domain, named after the ThrRS, GTPase, and SpoT/RelA proteins where it occurs. TGS is a small domain with a beta-grasp ubiquitin-like fold, a common structure involved in protein-protein interactions.
Pssm-ID: 340458 [Multi-domain] Cd Length: 65 Bit Score: 102.57 E-value: 1.52e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489075724 2 IKITFPDGAVREFESGVTTFDIAESISKSLAKKALAGKFNDQLIDTTRAIEEDGSIEIVTPDHKD 66
Cdd:cd01667 1 IKITLPDGSVKEFPKGTTPLDIAKSISPGLAKKAVAAKVNGELVDLSRPLEEDAELEILTFDDPE 65
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
545-635 |
7.68e-25 |
|
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: 98.81 E-value: 7.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 545 QVTVIPISN--EAHIDYAWEVAKTLRDRGVRADVDDRNEKMQYKIRASQTSKIPYQLIVGDKEMEDKSVNVRRYGSKATH 622
Cdd:pfam03129 1 QVVVIPLGEkaEELEEYAQKLAEELRAAGIRVELDDRNESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQE 80
|
90
....*....|...
gi 489075724 623 TESVEEFVENILA 635
Cdd:pfam03129 81 TVSLDELVEKLKE 93
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
271-525 |
4.74e-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: 83.32 E-value: 4.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 271 IRRTLERYITDKELASGYQHVYTPPLASVELYKTSGHWdhyQEDMFPVMDmGDGEEFVLRPMNCPHHIQVYKNHVRSyre 350
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGHE---PKDLLPVGA-ENEEDLYLRPTLEPGLVRLFVSHIRK--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 351 LPIRIAELGMMHRYEKSGAlsGLQRVREMTLNDGHIFVTPEQIQEEFQRALQLIIDVYAD-FNLTDYRFRLSYrdpndth 429
Cdd:cd00768 74 LPLRLAEIGPAFRNEGGRR--GLRRVREFTQLEGEVFGEDGEEASEFEELIELTEELLRAlGIKLDIVFVEKT------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 430 kyydNDEMWenaqsmlkaaldemgvdyfeaegeAAFYGPKLDIQVKTALGNEETLSTIQLDFLLPER-FDLKYIGADGEE 508
Cdd:cd00768 145 ----PGEFS------------------------PGGAGPGFEIEVDHPEGRGLEIGSGGYRQDEQARaADLYFLDEALEY 196
|
250
....*....|....*..
gi 489075724 509 HRPVMIHRGVisTMERF 525
Cdd:cd00768 197 RYPPTIGFGL--GLERL 211
|
|
| tRNA_SAD |
smart00863 |
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active form of ... |
167-215 |
6.02e-15 |
|
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active form of threonyl/alanyl tRNA synthetase is a dimer. Within the tRNA synthetase class II dimer, the bound tRNA interacts with both monomers making specific interactions with the catalytic domain, the C-terminal domain, and this SAD domain (the second additional domain). The second additional domain is comprised of a pair of perpendicularly orientated antiparallel beta sheets, of four and three strands, respectively, that surround a central alpha helix that forms the core of the domain.
Pssm-ID: 197931 [Multi-domain] Cd Length: 43 Bit Score: 68.95 E-value: 6.02e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 489075724 167 LTVYRQGEF-VDLCRGPHVPSTGRIQVFHLLNVAGAYWRgnsdnnmMQRI 215
Cdd:smart00863 1 VRVVSIGDFsVELCGGTHVPNTGEIGAFKILSVSGAYWG-------LQRI 43
|
|
| TGS |
pfam02824 |
TGS domain; The TGS domain is named after ThrRS, GTPase, and SpoT. Interestingly, TGS domain ... |
2-61 |
1.09e-14 |
|
TGS domain; The TGS domain is named after ThrRS, GTPase, and SpoT. Interestingly, TGS domain was detected also at the amino terminus of the uridine kinase from the spirochaete Treponema pallidum (but not any other organizm, including the related spirochaete Borrelia burgdorferi). TGS is a small domain that consists of ~50 amino acid residues and is predicted to possess a predominantly beta-sheet structure. There is no direct information on the functions of the TGS domain, but its presence in two types of regulatory proteins (the GTPases and guanosine polyphosphate phosphohydrolases/synthetases) suggests a ligand (most likely nucleotide)-binding, regulatory role.
Pssm-ID: 427005 [Multi-domain] Cd Length: 60 Bit Score: 68.73 E-value: 1.09e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 2 IKITFPDGAVREFESGVTTFDIAESISKSLAKKALAGKFNDQLIDTTRAIEEDGSIEIVT 61
Cdd:pfam02824 1 IRVYTPDGKVPDLPRGATPEDFAYAIHTSLAKKFIYAKVNGQLVGLDHPLEDGDVVEIVT 60
|
|
| PRK14938 |
PRK14938 |
Ser-tRNA(Thr) hydrolase; Provisional |
528-633 |
5.39e-13 |
|
Ser-tRNA(Thr) hydrolase; Provisional
Pssm-ID: 184902 [Multi-domain] Cd Length: 387 Bit Score: 71.03 E-value: 5.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 528 ILIETYKGAFPT---WLAPHQVTVIPISNEaHIDYAWEVAKTLRDRGVRADVDDRNEKMQYKIRASQTSKIPYQLIVGDK 604
Cdd:PRK14938 256 FLLESIRKQPPTlpdWLNPIQVRILPVKKD-FLDFSIQVAERLRKEGIRVNVDDLDDSLGNKIRRAGTEWIPFVIIIGER 334
|
90 100
....*....|....*....|....*....
gi 489075724 605 EMEDKSVNVRRYGSKATHTESVEEFVENI 633
Cdd:PRK14938 335 EVKTSTLTVKIRANNEQKSMTVEELVKEI 363
|
|
| tRNA_SAD |
pfam07973 |
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active from of ... |
167-215 |
7.02e-13 |
|
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active from of threonyl/alanyl tRNA synthetase is a dimer. Within the tRNA synthetase class II dimer, the bound tRNA interacts with both monomers making specific interactions with the catalytic domain, the C-terminal domain, and this domain (the second additional domain). The second additional domain is comprised of a pair of perpendicularly orientated antiparallel beta sheets, of four and three strands, respectively, that surround a central alpha helix that forms the core of the domain.
Pssm-ID: 429764 [Multi-domain] Cd Length: 43 Bit Score: 63.23 E-value: 7.02e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 489075724 167 LTVYRQGE-FVDLCRGPHVPSTGRIQVFHLLnvagaywRGNSDNNMMQRI 215
Cdd:pfam07973 1 VRVVSIGDfDVDLCGGTHVPNTGEIGAFKIL-------KGESKNKGLRRI 43
|
|
| ProRS_core_prok |
cd00779 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
235-399 |
6.01e-11 |
|
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: 63.36 E-value: 6.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 235 EAKERDHRKLgkeLDLFMISQeVGQGLPFWLPDGATIRRTLERyITDKEL-ASGYQHVYTPPLASVELYKTSGHWDHYQE 313
Cdd:cd00779 1 DAEIISHKLL---LRAGFIRQ-TSSGLYSWLPLGLRVLKKIEN-IIREEMnKIGAQEILMPILQPAELWKESGRWDAYGP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 314 DMFPVMDMGdGEEFVLRPMNCPHHIQVYKNHVRSYRELPIRIAELGMMHRYEKSGALsGLQRVREMTLNDGHIF-VTPEQ 392
Cdd:cd00779 76 ELLRLKDRH-GKEFLLGPTHEEVITDLVANEIKSYKQLPLNLYQIQTKFRDEIRPRF-GLMRGREFLMKDAYSFdIDEES 153
|
....*..
gi 489075724 393 IQEEFQR 399
Cdd:cd00779 154 LEETYEK 160
|
|
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
522-639 |
1.28e-10 |
|
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: 63.99 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 522 MERFTAILIEtyKGAFPTWLAPHQVTVIPISNEAhIDYAWEVAKTLRDRGVRADVDDRNEKMQYKIRASQTSKIPYQLIV 601
Cdd:COG0124 308 LERLLLLLEE--LGLLPAAEPPPDVYVVPLGEEA-RAEALKLAQELRAAGIRVELDLGGRKLKKQLKYADKSGAPFVLIL 384
|
90 100 110
....*....|....*....|....*....|....*...
gi 489075724 602 GDKEMEDKSVNVRRYGSKATHTESVEEFVENILADIAR 639
Cdd:COG0124 385 GEDELANGTVTLKDLATGEQETVPLDELVEYLKELLAE 422
|
|
| ProRS_core_arch_euk |
cd00778 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
264-411 |
1.34e-10 |
|
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: 62.23 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 264 WLPDGATIRRTLERYITDKELASGYQHVYTPPLASV-ELYKTSGHWDHYQEDMFPVMDMGD---GEEFVLRPMN----CP 335
Cdd:cd00778 27 FRPYGYAIWENIQKILDKEIKETGHENVYFPLLIPEsELEKEKEHIEGFAPEVAWVTHGGLeelEEPLALRPTSetaiYP 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489075724 336 hhiqVYKNHVRSYRELPIRIAELGMMHRYEKSGALSGLqRVREMTLNDGH-IFVTPEQIQEEfqrALQlIIDVYADF 411
Cdd:cd00778 107 ----MFSKWIRSYRDLPLKINQWVNVFRWETKTTRPFL-RTREFLWQEGHtAHATEEEAEEE---VLQ-ILDLYKEF 174
|
|
| HisRS_anticodon |
cd00859 |
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases ... |
545-633 |
1.38e-10 |
|
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: 57.93 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 545 QVTVIPIsNEAHIDYAWEVAKTLRDRGVRADVDDRNEKMQYKIRASQTSKIPYQLIVGDKEMEDKSVNVRRYGSKATHTE 624
Cdd:cd00859 3 DVYVVPL-GEGALSEALELAEQLRDAGIKAEIDYGGRKLKKQFKYADRSGARFAVILGEDELAAGVVTVKDLETGEQETV 81
|
....*....
gi 489075724 625 SVEEFVENI 633
Cdd:cd00859 82 ALDELVEEL 90
|
|
| ProRS_core |
cd00772 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
252-417 |
5.66e-10 |
|
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: 60.46 E-value: 5.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 252 MISQEVGQGLPFWLPDGATIRRTLERyITDKELA-SGYQHVYTPPLASVELYKTSGHWDHY-QEDMFPVMDMGDGE---E 326
Cdd:cd00772 15 LADQGPGRGIINFLPLAKAILDKIEN-VLDKMFKeHGAQNALFPFFILASFLEKEAEHDEGfSKELAVFKDAGDEEleeD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 327 FVLRPMNCPHHIQVYKNHVRSYRELPIRIAELGMMHRYEKSgALSGLQRVREMTLNDGHIF-VTPEQIQEEFQRALQLII 405
Cdd:cd00772 94 FALRPTLEENIGEIAAKFIKSWKDLPQHLNQIGNKFRDEIR-PRFGFLRAREFIMKDGHSAhADAEEADEEFLNMLSAYA 172
|
170
....*....|..
gi 489075724 406 DVYADFNLTDYR 417
Cdd:cd00772 173 EIARDLAAIDFI 184
|
|
| PRK12325 |
PRK12325 |
prolyl-tRNA synthetase; Provisional |
252-635 |
4.74e-09 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 237059 [Multi-domain] Cd Length: 439 Bit Score: 59.10 E-value: 4.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 252 MISQEvGQGLPFWLPDGATIRRTLERYITDKELASGYQHVYTPPLASVELYKTSGHWDHYQEDMFPVMDMGDgEEFVLRP 331
Cdd:PRK12325 31 MIRQQ-AAGIYSWLPLGLKVLKKIENIVREEQNRAGAIEILMPTIQPADLWRESGRYDAYGKEMLRIKDRHD-REMLYGP 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 332 MNCPHHIQVYKNHVRSYRELPiriaeLGMMH-----------RYeksgalsGLQRVREMTLNDGHIF-VTPEQIQEEFQR 399
Cdd:PRK12325 109 TNEEMITDIFRSYVKSYKDLP-----LNLYHiqwkfrdeirpRF-------GVMRGREFLMKDAYSFdLDEEGARHSYNR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 400 ALQLIIDVYADFNLTDYRFR---------LSYR-----DPNDTHKYYDNDEM----------WENAQsmLKAALDEMGVD 455
Cdd:PRK12325 177 MFVAYLRTFARLGLKAIPMRadtgpiggdLSHEfiilaETGESTVFYDKDFLdllvpgedidFDVAD--LQPIVDEWTSL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 456 YFEAE---GEAAFYGPKLDiQVKTALGNEetLSTIqldFLlperFDLKY--------IGADGEEHRPVMIHRGV-IStme 523
Cdd:PRK12325 255 YAATEemhDEAAFAAVPEE-RRLSARGIE--VGHI---FY----FGTKYsepmnakvQGPDGKEVPVHMGSYGIgVS--- 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 524 RFTAILIETY---KG-AFPTWLAPHQVTVIPI--SNEAHIDYAWEVAKTLRDRGVRADVDDRNEKMQYKIRASQTSKIPY 597
Cdd:PRK12325 322 RLVAAIIEAShddKGiIWPESVAPFKVGIINLkqGDEACDAACEKLYAALSAAGIDVLYDDTDERPGAKFATMDLIGLPW 401
|
410 420 430
....*....|....*....|....*....|....*...
gi 489075724 598 QLIVGDKEMEDKSVNVRRYGSKATHTESVEEFVENILA 635
Cdd:PRK12325 402 QIIVGPKGLAEGKVELKDRKTGEREELSVEAAINRLTA 439
|
|
| HGTP_anticodon |
cd00738 |
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ... |
543-631 |
1.44e-08 |
|
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: 52.40 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 543 PHQVTVIPI--SNEAHIDYAWEVAKTLRDRGVRADVDDRNEKMQYKIRASQTSKIPYQLIVGDKEMEDKSVNVRRYGSKA 620
Cdd:cd00738 1 PIDVAIVPLtdPRVEAREYAQKLLNALLANGIRVLYDDRERKIGKKFREADLRGVPFAVVVGEDELENGKVTVKSRDTGE 80
|
90
....*....|.
gi 489075724 621 THTESVEEFVE 631
Cdd:cd00738 81 SETLHVDELPE 91
|
|
| PRK09194 |
PRK09194 |
prolyl-tRNA synthetase; Provisional |
495-635 |
1.00e-07 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 236405 [Multi-domain] Cd Length: 565 Bit Score: 55.09 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 495 ERFDLKYIGADGEEHRPVM----IhrGVistmERFTAILIETY---KG-AFPTWLAPHQVTVIPIS--NEAHIDYAWEVA 564
Cdd:PRK09194 418 EAMNATVLDENGKAQPLIMgcygI--GV----SRLVAAAIEQNhdeKGiIWPKAIAPFDVHIVPVNmkDEEVKELAEKLY 491
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489075724 565 KTLRDRGVRADVDDRNEkmqykiRASqtSK--------IPYQLIVGDKEMEDKSVNVRRYGSKATHTESVEEFVENILA 635
Cdd:PRK09194 492 AELQAAGIEVLLDDRKE------RPG--VKfadadligIPHRIVVGDRGLAEGIVEYKDRRTGEKEEVPVDELVEFLKA 562
|
|
| ProRS_anticodon_short |
cd00861 |
ProRS Prolyl-anticodon binding domain, short version found predominantly in bacteria. ProRS ... |
543-634 |
1.60e-07 |
|
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: 49.51 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 543 PHQVTVIPIS--NEAHIDYAWEVAKTLRDRGVRADVDDRNEKMQYKIRASQTSKIPYQLIVGDKEMEDKSVNVRRYGSKA 620
Cdd:cd00861 1 PFDVVIIPMNmkDEVQQELAEKLYAELQAAGVDVLLDDRNERPGVKFADADLIGIPYRIVVGKKSAAEGIVEIKVRKTGE 80
|
90
....*....|....
gi 489075724 621 THTESVEEFVENIL 634
Cdd:cd00861 81 KEEISIDELLEFLQ 94
|
|
| ProRS_anticodon_zinc |
cd00862 |
ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and ... |
542-647 |
7.80e-07 |
|
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: 49.99 E-value: 7.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 542 APHQVTVIPI-----SNEAHIDYAWEVAKTLRDRGVRADVDDRNEKM------QYKIRAsqtskIPYQLIVGDKEMEDKS 610
Cdd:cd00862 9 APIQVVIVPIgikdeKREEVLEAADELAERLKAAGIRVHVDDRDNYTpgwkfnDWELKG-----VPLRIEIGPRDLEKNT 83
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 489075724 611 VNVRRYGSKATHTESVEEFVENI---LADIARKSRPDAQA 647
Cdd:cd00862 84 VVIVRRDTGEKKTVPLAELVEKVpelLDEIQEDLYERALE 123
|
|
| AlaX |
COG2872 |
Ser-tRNA(Ala) deacylase AlaX (editing enzyme) [Translation, ribosomal structure and biogenesis] ... |
72-192 |
9.13e-05 |
|
Ser-tRNA(Ala) deacylase AlaX (editing enzyme) [Translation, ribosomal structure and biogenesis];
Pssm-ID: 442119 [Multi-domain] Cd Length: 238 Bit Score: 44.41 E-value: 9.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 72 RHSAAHLFAQAAKRLFPNLHLGVgpAI-AEGFYYDTDNAEgqISNEDLPRIEAEMQKIVTENYPCIREEVTKEEALELfk 150
Cdd:COG2872 99 LHTALHLLSAVVYREYGAPVTGG--QIgEDRARIDFDLPE--FDEEDLEEIEAEANELIAADLPVRIYWITREELEAI-- 172
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 489075724 151 ddPYKVELINEHAGAGLTVYR----QGefVDL--CRGPHVPST---GRIQV 192
Cdd:COG2872 173 --PGLVRTMSVLPPPGVGRVRiveiGG--VDLqpCGGTHVANTgeiGRIKI 219
|
|
| GlyRS_anticodon |
cd00858 |
GlyRS Glycyl-anticodon binding domain. GlyRS belongs to class II aminoacyl-tRNA synthetases ... |
537-579 |
3.27e-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: 40.62 E-value: 3.27e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 489075724 537 FPTWLAPHQVTVIPISNEAHI-DYAWEVAKTLRDRGVRADVDDR 579
Cdd:cd00858 20 LPPALAPIKVAVLPLVKRDELvEIAKEISEELRELGFSVKYDDS 63
|
|
| PRK09194 |
PRK09194 |
prolyl-tRNA synthetase; Provisional |
252-353 |
4.45e-04 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 236405 [Multi-domain] Cd Length: 565 Bit Score: 43.15 E-value: 4.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 252 MISQeVGQGLPFWLPDGATIRRTLERyITDKEL-ASGYQHVYTPPLASVELYKTSGHWDHYQEDMFPVMDMGDGeEFVLR 330
Cdd:PRK09194 31 YIRK-LASGIYTYLPLGLRVLRKIEN-IVREEMnKIGAQEVLMPALQPAELWQESGRWEEYGPELLRLKDRHGR-DFVLG 107
|
90 100
....*....|....*....|....*..
gi 489075724 331 PMncphHIQVY----KNHVRSYRELPI 353
Cdd:PRK09194 108 PT----HEEVItdlvRNEIKSYKQLPL 130
|
|
| SerRS_core |
cd00770 |
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the ... |
232-408 |
6.23e-04 |
|
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: 42.16 E-value: 6.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 232 RLEEAKERDHRKLGKELDLF---MISQEVGQGLPFWLPDGATIRRTLERYITDKELASGYQHVYTPPLASVELYKTSGHW 308
Cdd:cd00770 12 RVFDFKPKDHVELGEKLDILdfeRGAKVSGSRFYYLKGDGALLERALINFALDFLTKRGFTPVIPPFLVRKEVMEGTGQL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075724 309 DHYQEDMFPVmdmgDGEEFVLRPMNcphHIQV---YKNHVRSYRELPIRIAELGMMHRYEKSGA---LSGLQRVREMTLN 382
Cdd:cd00770 92 PKFDEQLYKV----EGEDLYLIATA---EVPLaalHRDEILEEEELPLKYAGYSPCFRKEAGSAgrdTRGLFRVHQFEKV 164
|
170 180
....*....|....*....|....*.
gi 489075724 383 DGHIFVTPEQIQEEFQRALQLIIDVY 408
Cdd:cd00770 165 EQFVFTKPEESWEELEELISNAEEIL 190
|
|
| |
