|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02908 |
PLN02908 |
threonyl-tRNA synthetase |
1-688 |
0e+00 |
|
threonyl-tRNA synthetase
Pssm-ID: 178496 [Multi-domain] Cd Length: 686 Bit Score: 1091.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 1 MSEEKASSPSGKMDGEKPLNPWPEYINTRLDMYHKLKAEHdsiLAEKAAKDSKPIKVTLPDGKQVDAESWKTTPYQIACG 80
Cdd:PLN02908 1 MAMPAATASAAAPSHPSDEEYLSAVIKKRIELFEKIQARQ---LARLESAGGDPIKVTLPDGAVKDGKKWVTTPMDIAKE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 81 ISQGLADNTVVAKVNKVVWDLDRPLETDCTLELLKFEDEEAQAVYWHSSAHIMGEAMERVYGGCLCYGPPIEN--GFYYD 158
Cdd:PLN02908 78 ISKGLANSALIAQVDGVLWDMTRPLEGDCKLKLFKFDDDEGRDTFWHSSAHILGEALELEYGCKLCIGPCTTRgeGFYYD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 159 MYLEEGGVSSNDFSSLETLCKKIIKEKQTFERLEVKKETLLEMFKYNKFKCRILNEKVNTPTTTVYRCGPLIDLCRGPHV 238
Cdd:PLN02908 158 AFYGDRTLNEEDFKPIEARAEKAVKEKQPFERIEVTREEALEMFSENKFKVEIINDLPEDATITVYRCGPLVDLCRGPHI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 239 RHTGKIKTLKIHKNSSTYWEGKADMETLQRIYGISFPDPKLLKEWEKFQEEAKNRDHRKIGRDQELYFFHELSPGSCFFL 318
Cdd:PLN02908 238 PNTSFVKAFACLKASSAYWRGDVDRESLQRVYGISFPDKKLLKEYKHRIEEAKKRDHRLLGQKQELFFFHELSPGSCFFL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 319 PKGAYIYNTLMEFIRSEYRKRGFQEVVTPNIFNSRLWMTSGHWQHYSENMFSFEVEKEQFALKPMNCPGHCLMFDHRPRS 398
Cdd:PLN02908 318 PHGARIYNKLMDFIREQYWERGYDEVITPNIYNMDLWETSGHAAHYKENMFVFEIEKQEFGLKPMNCPGHCLMFAHRVRS 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 399 WRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCAMEQIEDEIKGCLDFLRTVYSVFGFSFKLNLSTRPEKFL 478
Cdd:PLN02908 398 YRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCREDQIKDEVKGVLDFLDYVYEVFGFTYELKLSTRPEKYL 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 479 GDIEIWNQAEKQLENSLNEFGEKWELNPGDGAFYGPKIDIQIKDAIGRYHQCATIQLDFQLPIRFNLTYVSHDGDDKKRP 558
Cdd:PLN02908 478 GDLETWDKAEAALTEALNAFGKPWQLNEGDGAFYGPKIDITVSDALKRKFQCATVQLDFQLPIRFKLSYSAEDEAKIERP 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 559 VIVHRAILGSVERMIAILTENYGGKWPFWLSPRQVMVVPVGPTCDEYAQKVRQEFHDAKFMVDIDLDPGcTLNKKIRNAQ 638
Cdd:PLN02908 558 VMIHRAILGSVERMFAILLEHYAGKWPFWLSPRQAIVVPISEKSQDYAEEVRAQLHAAGFYVDVDVTDR-KIQKKVREAQ 636
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 55741823 639 LAQYNFILVVGEKEKASGTVNIRTRDNKVHGERTVGETVERLQQLKQLRS 688
Cdd:PLN02908 637 LAQYNYILVVGEAEAATGTVNVRTRDNVVHGEKKIEELLTEFKEERAEFK 686
|
|
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
55-682 |
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: 894.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 55 IKVTLPDGKQVDAESwKTTPYQIACGISQGLADNTVVAKVNKVVWDLDRPLETDCTLELLKFEDEEAQAVYWHSSAHIMG 134
Cdd:COG0441 2 IKITLPDGSVREFEA-GVTVLDVAKSISPGLAKAAVAAKVNGELVDLSTPIEEDAELEIVTFDDEEGLEILRHSAAHLLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 135 EAMERVYGGC-LCYGPPIENGFYYDMYLEEGgVSSNDFSSLETLCKKIIKEKQTFERLEVKKETLLEMFKY--NKFKCRI 211
Cdd:COG0441 81 QAVKRLYPDAkLTIGPVIENGFYYDFDLERP-FTPEDLEKIEKEMKEIIKEDLPIEREEVSREEAIELFKEkgEPYKVEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 212 LNEKVNTPTTTVYRCGPLIDLCRGPHVRHTGKIKTLKIHKNSSTYWEGKADMETLQRIYGISFPDPKLLKEWEKFQEEAK 291
Cdd:COG0441 160 IEDIPEDEEISLYRQGEFVDLCRGPHVPSTGKIKAFKLLSVAGAYWRGDEKNKMLQRIYGTAFPKKKELDAYLHRLEEAK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 292 NRDHRKIGRDQELYFFH-ELSPGSCFFLPKGAYIYNTLMEFIRSEYRKRGFQEVVTPNIFNSRLWMTSGHWQHYSENMFS 370
Cdd:COG0441 240 KRDHRKLGKELDLFHFQeEVGPGLPFWHPKGAIIRRELEDYIREKHRKAGYQEVKTPHILDRELWETSGHWDHYRENMFP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 371 FEVEKEQFALKPMNCPGHCLMFDHRPRSWRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCAMEQIEDEIKG 450
Cdd:COG0441 320 TESDGEEYALKPMNCPGHILIYKSGLRSYRDLPLRLAEFGTVHRYEPSGALHGLMRVRGFTQDDAHIFCTPDQIEDEIKK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 451 CLDFLRTVYSVFGFS-FKLNLSTRPEKFLGDIEIWNQAEKQLENSLNEFGEKWELNPGDGAFYGPKIDIQIKDAIGRYHQ 529
Cdd:COG0441 400 VIDLVLEVYKDFGFEdYYVKLSTRPEKRIGSDEIWDKAEAALREALEELGLEYVINPGEGAFYGPKIDFQLKDAIGREWQ 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 530 CATIQLDFQLPIRFNLTYVSHDGdDKKRPVIVHRAILGSVERMIAILTENYGGKWPFWLSPRQVMVVPVGPTCDEYAQKV 609
Cdd:COG0441 480 CGTIQLDFNLPERFDLTYVGEDG-EKHRPVMIHRAILGSIERFIGILIEHYAGAFPLWLAPVQVVVLPISDKHADYAKEV 558
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 55741823 610 RQEFHDAKFMVDIDLDPGcTLNKKIRNAQLAQYNFILVVGEKEKASGTVNIRTRDNKVHGERTVGETVERLQQ 682
Cdd:COG0441 559 AKKLRAAGIRVEVDLRNE-KIGYKIREAQLQKVPYMLVVGDKEVENGTVSVRRRGGGDLGTMSLDEFIARLKE 630
|
|
| thrS |
TIGR00418 |
threonyl-tRNA synthetase; This model represents the threonyl-tRNA synthetase found in most ... |
126-682 |
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: 677.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 126 WHSSAHIMGEAMERVYGG-CLCYGPPIENGFYYDMYLEEGgVSSNDFSSLETLCKKIIKEKQTFERLEVKKETLLEMFKY 204
Cdd:TIGR00418 1 RHSIAHLLAEALKQLYPDvKLAIGPVVEDGFYYDFELDRS-FTQEDLEKIEKDMKEIAKKNYPVAKLSVSLEEALEAFKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 205 NK-FKCRILNEKVNTPTTTVYRCG-PLIDLCRGPHVRHTGKIKTLKIHKNSSTYWEGKADMETLQRIYGISFPDPKLLKE 282
Cdd:TIGR00418 80 LEpYKLELLDEIPNGVKRTPYGWGkAFVDLCKGPHLPNTSFIKAFKLEKVAGAYWRGDSKNKMLQRIYGTAWADKKQLAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 283 WEKFQEEAKNRDHRKIGRDQELYFFHELS-PGSCFFLPKGAYIYNTLMEFIRSEYRKRGFQEVVTPNIFNSRLWMTSGHW 361
Cdd:TIGR00418 160 YLLRLEEAKKRDHRKLGKELELFSFEPEIgPGLPFWLPKGATIRNLLEDFVRQKQIKYGYMEVETPIMYDLELWEISGHW 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 362 QHYSENMFSFEVEKEQ-FALKPMNCPGHCLMFDHRPRSWRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCA 440
Cdd:TIGR00418 240 DNYKERMFPFTELDNReFMLKPMNCPGHFLIFKSSLRSYRDLPLRIAELGYSHRYEQSGELHGLMRVRGFTQDDAHIFCT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 441 MEQIEDEIKGCLDFLRTVYSVFGFSF-KLNLSTR-PEKFLGDIEIWNQAEKQLENSLNEFGEKWELNPGDGAFYGPKIDI 518
Cdd:TIGR00418 320 EDQIKEEFKNQFRLIQKVYSDFGFSFdKYELSTRdPEDFIGEDELWEKAEAALEEALKELGVPYEIDPGRGAFYGPKIDF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 519 QIKDAIGRYHQCATIQLDFQLPIRFNLTYVSHDGdDKKRPVIVHRAILGSVERMIAILTENYGGKWPFWLSPRQVMVVPV 598
Cdd:TIGR00418 400 AFKDALGREWQCATVQLDFELPERFDLTYVDEDN-EEKRPVMIHRAILGSIERFIAILLEKYAGNFPLWLAPVQVVVIPV 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 599 GPTCDEYAQKVRQEFHDAKFMVDIDlDPGCTLNKKIRNAQLAQYNFILVVGEKEKASGTVNIRTRDNKVHGERTVGETVE 678
Cdd:TIGR00418 479 NERHLDYAKKVAQKLKKAGIRVDVD-DRNERLGKKIREAQKQKIPYMLVVGDKEMESLAVNVRTRKGQKLEKMSLDEFLE 557
|
....
gi 55741823 679 RLQQ 682
Cdd:TIGR00418 558 KLRK 561
|
|
| ThrRS_core |
cd00771 |
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ... |
293-590 |
0e+00 |
|
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: 546.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 293 RDHRKIGRDQELYFFHELSPGSCFFLPKGAYIYNTLMEFIRSEYRKRGFQEVVTPNIFNSRLWMTSGHWQHYSENMFSFE 372
Cdd:cd00771 1 DHRRLGGELELFFFFDEAGPGLPFWLPKGAIIRNELEDFLRELQRKRGYQEVETPIIYNKELWETSGHWDHYRENMFPFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 373 VEKEQFALKPMNCPGHCLMFDHRPRSWRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCAMEQIEDEIKGCL 452
Cdd:cd00771 81 EEDEEYGLKPMNCPGHCLIFKSKPRSYRDLPLRLAEFGTVHRYEQSGALHGLTRVRGFTQDDAHIFCTPDQIKEEIKGVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 453 DFLRTVYSVFGF-SFKLNLSTRPEKFLGDIEIWNQAEKQLENSLNEFGEKWELNPGDGAFYGPKIDIQIKDAIGRYHQCA 531
Cdd:cd00771 161 DLIKEVYSDFGFfDYKVELSTRPEKFIGSDEVWEKAEAALREALEEIGLPYEINEGEGAFYGPKIDFHVKDALGREWQCS 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 55741823 532 TIQLDFQLPIRFNLTYVSHDGdDKKRPVIVHRAILGSVERMIAILTENYGGKWPFWLSP 590
Cdd:cd00771 241 TIQLDFNLPERFDLTYIGEDG-EKKRPVMIHRAILGSIERFIGILIEHYAGKFPLWLAP 298
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
369-580 |
2.48e-39 |
|
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: 142.94 E-value: 2.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 369 FSFEVE-KEQFALKPMNCPGHCLMF-DHRPRSWReLPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCAMEQIED 446
Cdd:pfam00587 1 YKVEDEnGDELALKPTNEPGHTLLFrEEGLRSKD-LPLKLAQFGTCFRHEASGDTRGLIRVRQFHQDDAHIFHAPGQSPD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 447 EIKGCLDFLRTVYSVFGFSF-KLNLSTRPEkflgdieiwnqaekqlenslnefgekwelnpgdGAFYGPKIDIQIKDAI- 524
Cdd:pfam00587 80 ELEDYIKLIDRVYSRLGLEVrVVRLSNSDG---------------------------------SAFYGPKLDFEVVFPSl 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 55741823 525 GRYHQCATIQLD-FQLPIRFNLTYVSHDgDDKKRPVIVHRAILGsVERMIAILTENY 580
Cdd:pfam00587 127 GKQRQTGTIQNDgFRLPRRLGIRYKDED-NESKFPYMIHRAGLG-VERFLAAILENN 181
|
|
| tRNA_SAD |
smart00863 |
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active form of ... |
222-269 |
7.81e-12 |
|
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: 60.09 E-value: 7.81e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 55741823 222 TVYRCGPL-IDLCRGPHVRHTGKIKTLKIHKNSSTYWEgkadmetLQRI 269
Cdd:smart00863 2 RVVSIGDFsVELCGGTHVPNTGEIGAFKILSVSGAYWG-------LQRI 43
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02908 |
PLN02908 |
threonyl-tRNA synthetase |
1-688 |
0e+00 |
|
threonyl-tRNA synthetase
Pssm-ID: 178496 [Multi-domain] Cd Length: 686 Bit Score: 1091.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 1 MSEEKASSPSGKMDGEKPLNPWPEYINTRLDMYHKLKAEHdsiLAEKAAKDSKPIKVTLPDGKQVDAESWKTTPYQIACG 80
Cdd:PLN02908 1 MAMPAATASAAAPSHPSDEEYLSAVIKKRIELFEKIQARQ---LARLESAGGDPIKVTLPDGAVKDGKKWVTTPMDIAKE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 81 ISQGLADNTVVAKVNKVVWDLDRPLETDCTLELLKFEDEEAQAVYWHSSAHIMGEAMERVYGGCLCYGPPIEN--GFYYD 158
Cdd:PLN02908 78 ISKGLANSALIAQVDGVLWDMTRPLEGDCKLKLFKFDDDEGRDTFWHSSAHILGEALELEYGCKLCIGPCTTRgeGFYYD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 159 MYLEEGGVSSNDFSSLETLCKKIIKEKQTFERLEVKKETLLEMFKYNKFKCRILNEKVNTPTTTVYRCGPLIDLCRGPHV 238
Cdd:PLN02908 158 AFYGDRTLNEEDFKPIEARAEKAVKEKQPFERIEVTREEALEMFSENKFKVEIINDLPEDATITVYRCGPLVDLCRGPHI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 239 RHTGKIKTLKIHKNSSTYWEGKADMETLQRIYGISFPDPKLLKEWEKFQEEAKNRDHRKIGRDQELYFFHELSPGSCFFL 318
Cdd:PLN02908 238 PNTSFVKAFACLKASSAYWRGDVDRESLQRVYGISFPDKKLLKEYKHRIEEAKKRDHRLLGQKQELFFFHELSPGSCFFL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 319 PKGAYIYNTLMEFIRSEYRKRGFQEVVTPNIFNSRLWMTSGHWQHYSENMFSFEVEKEQFALKPMNCPGHCLMFDHRPRS 398
Cdd:PLN02908 318 PHGARIYNKLMDFIREQYWERGYDEVITPNIYNMDLWETSGHAAHYKENMFVFEIEKQEFGLKPMNCPGHCLMFAHRVRS 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 399 WRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCAMEQIEDEIKGCLDFLRTVYSVFGFSFKLNLSTRPEKFL 478
Cdd:PLN02908 398 YRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCREDQIKDEVKGVLDFLDYVYEVFGFTYELKLSTRPEKYL 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 479 GDIEIWNQAEKQLENSLNEFGEKWELNPGDGAFYGPKIDIQIKDAIGRYHQCATIQLDFQLPIRFNLTYVSHDGDDKKRP 558
Cdd:PLN02908 478 GDLETWDKAEAALTEALNAFGKPWQLNEGDGAFYGPKIDITVSDALKRKFQCATVQLDFQLPIRFKLSYSAEDEAKIERP 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 559 VIVHRAILGSVERMIAILTENYGGKWPFWLSPRQVMVVPVGPTCDEYAQKVRQEFHDAKFMVDIDLDPGcTLNKKIRNAQ 638
Cdd:PLN02908 558 VMIHRAILGSVERMFAILLEHYAGKWPFWLSPRQAIVVPISEKSQDYAEEVRAQLHAAGFYVDVDVTDR-KIQKKVREAQ 636
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 55741823 639 LAQYNFILVVGEKEKASGTVNIRTRDNKVHGERTVGETVERLQQLKQLRS 688
Cdd:PLN02908 637 LAQYNYILVVGEAEAATGTVNVRTRDNVVHGEKKIEELLTEFKEERAEFK 686
|
|
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
55-682 |
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: 894.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 55 IKVTLPDGKQVDAESwKTTPYQIACGISQGLADNTVVAKVNKVVWDLDRPLETDCTLELLKFEDEEAQAVYWHSSAHIMG 134
Cdd:COG0441 2 IKITLPDGSVREFEA-GVTVLDVAKSISPGLAKAAVAAKVNGELVDLSTPIEEDAELEIVTFDDEEGLEILRHSAAHLLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 135 EAMERVYGGC-LCYGPPIENGFYYDMYLEEGgVSSNDFSSLETLCKKIIKEKQTFERLEVKKETLLEMFKY--NKFKCRI 211
Cdd:COG0441 81 QAVKRLYPDAkLTIGPVIENGFYYDFDLERP-FTPEDLEKIEKEMKEIIKEDLPIEREEVSREEAIELFKEkgEPYKVEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 212 LNEKVNTPTTTVYRCGPLIDLCRGPHVRHTGKIKTLKIHKNSSTYWEGKADMETLQRIYGISFPDPKLLKEWEKFQEEAK 291
Cdd:COG0441 160 IEDIPEDEEISLYRQGEFVDLCRGPHVPSTGKIKAFKLLSVAGAYWRGDEKNKMLQRIYGTAFPKKKELDAYLHRLEEAK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 292 NRDHRKIGRDQELYFFH-ELSPGSCFFLPKGAYIYNTLMEFIRSEYRKRGFQEVVTPNIFNSRLWMTSGHWQHYSENMFS 370
Cdd:COG0441 240 KRDHRKLGKELDLFHFQeEVGPGLPFWHPKGAIIRRELEDYIREKHRKAGYQEVKTPHILDRELWETSGHWDHYRENMFP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 371 FEVEKEQFALKPMNCPGHCLMFDHRPRSWRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCAMEQIEDEIKG 450
Cdd:COG0441 320 TESDGEEYALKPMNCPGHILIYKSGLRSYRDLPLRLAEFGTVHRYEPSGALHGLMRVRGFTQDDAHIFCTPDQIEDEIKK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 451 CLDFLRTVYSVFGFS-FKLNLSTRPEKFLGDIEIWNQAEKQLENSLNEFGEKWELNPGDGAFYGPKIDIQIKDAIGRYHQ 529
Cdd:COG0441 400 VIDLVLEVYKDFGFEdYYVKLSTRPEKRIGSDEIWDKAEAALREALEELGLEYVINPGEGAFYGPKIDFQLKDAIGREWQ 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 530 CATIQLDFQLPIRFNLTYVSHDGdDKKRPVIVHRAILGSVERMIAILTENYGGKWPFWLSPRQVMVVPVGPTCDEYAQKV 609
Cdd:COG0441 480 CGTIQLDFNLPERFDLTYVGEDG-EKHRPVMIHRAILGSIERFIGILIEHYAGAFPLWLAPVQVVVLPISDKHADYAKEV 558
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 55741823 610 RQEFHDAKFMVDIDLDPGcTLNKKIRNAQLAQYNFILVVGEKEKASGTVNIRTRDNKVHGERTVGETVERLQQ 682
Cdd:COG0441 559 AKKLRAAGIRVEVDLRNE-KIGYKIREAQLQKVPYMLVVGDKEVENGTVSVRRRGGGDLGTMSLDEFIARLKE 630
|
|
| thrS |
TIGR00418 |
threonyl-tRNA synthetase; This model represents the threonyl-tRNA synthetase found in most ... |
126-682 |
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: 677.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 126 WHSSAHIMGEAMERVYGG-CLCYGPPIENGFYYDMYLEEGgVSSNDFSSLETLCKKIIKEKQTFERLEVKKETLLEMFKY 204
Cdd:TIGR00418 1 RHSIAHLLAEALKQLYPDvKLAIGPVVEDGFYYDFELDRS-FTQEDLEKIEKDMKEIAKKNYPVAKLSVSLEEALEAFKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 205 NK-FKCRILNEKVNTPTTTVYRCG-PLIDLCRGPHVRHTGKIKTLKIHKNSSTYWEGKADMETLQRIYGISFPDPKLLKE 282
Cdd:TIGR00418 80 LEpYKLELLDEIPNGVKRTPYGWGkAFVDLCKGPHLPNTSFIKAFKLEKVAGAYWRGDSKNKMLQRIYGTAWADKKQLAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 283 WEKFQEEAKNRDHRKIGRDQELYFFHELS-PGSCFFLPKGAYIYNTLMEFIRSEYRKRGFQEVVTPNIFNSRLWMTSGHW 361
Cdd:TIGR00418 160 YLLRLEEAKKRDHRKLGKELELFSFEPEIgPGLPFWLPKGATIRNLLEDFVRQKQIKYGYMEVETPIMYDLELWEISGHW 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 362 QHYSENMFSFEVEKEQ-FALKPMNCPGHCLMFDHRPRSWRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCA 440
Cdd:TIGR00418 240 DNYKERMFPFTELDNReFMLKPMNCPGHFLIFKSSLRSYRDLPLRIAELGYSHRYEQSGELHGLMRVRGFTQDDAHIFCT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 441 MEQIEDEIKGCLDFLRTVYSVFGFSF-KLNLSTR-PEKFLGDIEIWNQAEKQLENSLNEFGEKWELNPGDGAFYGPKIDI 518
Cdd:TIGR00418 320 EDQIKEEFKNQFRLIQKVYSDFGFSFdKYELSTRdPEDFIGEDELWEKAEAALEEALKELGVPYEIDPGRGAFYGPKIDF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 519 QIKDAIGRYHQCATIQLDFQLPIRFNLTYVSHDGdDKKRPVIVHRAILGSVERMIAILTENYGGKWPFWLSPRQVMVVPV 598
Cdd:TIGR00418 400 AFKDALGREWQCATVQLDFELPERFDLTYVDEDN-EEKRPVMIHRAILGSIERFIAILLEKYAGNFPLWLAPVQVVVIPV 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 599 GPTCDEYAQKVRQEFHDAKFMVDIDlDPGCTLNKKIRNAQLAQYNFILVVGEKEKASGTVNIRTRDNKVHGERTVGETVE 678
Cdd:TIGR00418 479 NERHLDYAKKVAQKLKKAGIRVDVD-DRNERLGKKIREAQKQKIPYMLVVGDKEMESLAVNVRTRKGQKLEKMSLDEFLE 557
|
....
gi 55741823 679 RLQQ 682
Cdd:TIGR00418 558 KLRK 561
|
|
| PRK12444 |
PRK12444 |
threonyl-tRNA synthetase; Reviewed |
52-682 |
0e+00 |
|
threonyl-tRNA synthetase; Reviewed
Pssm-ID: 183530 [Multi-domain] Cd Length: 639 Bit Score: 653.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 52 SKPIKVTLPDG--KQVDAeswKTTPYQIACGISQGLADNTVVAKVNKVVWDLDRPLETDCTLELLKFEDEEAQAVYWHSS 129
Cdd:PRK12444 3 EQMIEIKFPDGsvKEFVK---GITLEEIAGSISSSLKKKAVAGKVNDKLYDLRRNLEEDAEVEIITIDSNEGVEIARHSA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 130 AHIMGEAMERVYGGC-LCYGPPIENGFYYDMYLEEGgVSSNDFSSLETLCKKIIKEKQTFERLEVKKETLLEMFKYN--K 206
Cdd:PRK12444 80 AHILAQAVKRLYGDVnLGVGPVIENGFYYDMDLPSS-VNVEDLRKIEKEMKKIINENIKIERVEVSREEAAKLFQEMndR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 207 FKCRILNEKVNTPTTTVYRCGPLIDLCRGPHVRHTGKIKTLKIHKNSSTYWEGKADMETLQRIYGISFPDPKLLKEWEKF 286
Cdd:PRK12444 159 LKLELLEAIPSGESITLYKQGEFVDLCRGPHLPSTGYLKAFQLTHVSGAYWRGDSNNQVLQRIYGVAFSSQKELEEYLHF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 287 QEEAKNRDHRKIGRDQELYFFHELSPGSCFFLPKGAYIYNTLMEFIRSEYRKRGFQEVVTPNIFNSRLWMTSGHWQHYSE 366
Cdd:PRK12444 239 VEEAAKRNHRKLGKELELFMFSEEAPGMPFYLPKGQIIRNELEAFLREIQKEYNYQEVRTPFMMNQELWERSGHWDHYKD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 367 NMFSFEVEKEQFALKPMNCPGHCLMFDHRPRSWRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCAMEQIED 446
Cdd:PRK12444 319 NMYFSEVDNKSFALKPMNCPGHMLMFKNKLHSYRELPIRMCEFGQVHRHEFSGALNGLLRVRTFCQDDAHLFVTPDQIED 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 447 EIKGCLDFLRTVYSVFGFSFKLNLSTRPEKFLGDIEIWNQAEKQLENSLNEFGEKWELNPGDGAFYGPKIDIQIKDAIGR 526
Cdd:PRK12444 399 EIKSVMAQIDYVYKTFGFEYEVELSTRPEDSMGDDELWEQAEASLENVLQSLNYKYRLNEGDGAFYGPKIDFHIKDALNR 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 527 YHQCATIQLDFQLPIRFNLTYVSHDgDDKKRPVIVHRAILGSVERMIAILTENYGGKWPFWLSPRQVMVVPVGPTC-DEY 605
Cdd:PRK12444 479 SHQCGTIQLDFQMPEKFDLNYIDEK-NEKRRPVVIHRAVLGSLDRFLAILIEHFGGAFPAWLAPVQVKVIPVSNAVhVQY 557
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 55741823 606 AQKVRQEFHDAKFMVDIDLDPGcTLNKKIRNAQLAQYNFILVVGEKEKASGTVNIRTRDNKVHGERTVGETVERLQQ 682
Cdd:PRK12444 558 ADEVADKLAQAGIRVERDERDE-KLGYKIREAQMQKIPYVLVIGDKEMENGAVNVRKYGEEKSEVIELDMFVESIKE 633
|
|
| ThrRS_core |
cd00771 |
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ... |
293-590 |
0e+00 |
|
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: 546.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 293 RDHRKIGRDQELYFFHELSPGSCFFLPKGAYIYNTLMEFIRSEYRKRGFQEVVTPNIFNSRLWMTSGHWQHYSENMFSFE 372
Cdd:cd00771 1 DHRRLGGELELFFFFDEAGPGLPFWLPKGAIIRNELEDFLRELQRKRGYQEVETPIIYNKELWETSGHWDHYRENMFPFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 373 VEKEQFALKPMNCPGHCLMFDHRPRSWRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCAMEQIEDEIKGCL 452
Cdd:cd00771 81 EEDEEYGLKPMNCPGHCLIFKSKPRSYRDLPLRLAEFGTVHRYEQSGALHGLTRVRGFTQDDAHIFCTPDQIKEEIKGVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 453 DFLRTVYSVFGF-SFKLNLSTRPEKFLGDIEIWNQAEKQLENSLNEFGEKWELNPGDGAFYGPKIDIQIKDAIGRYHQCA 531
Cdd:cd00771 161 DLIKEVYSDFGFfDYKVELSTRPEKFIGSDEVWEKAEAALREALEEIGLPYEINEGEGAFYGPKIDFHVKDALGREWQCS 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 55741823 532 TIQLDFQLPIRFNLTYVSHDGdDKKRPVIVHRAILGSVERMIAILTENYGGKWPFWLSP 590
Cdd:cd00771 241 TIQLDFNLPERFDLTYIGEDG-EKKRPVMIHRAILGSIERFIGILIEHYAGKFPLWLAP 298
|
|
| PLN02837 |
PLN02837 |
threonine-tRNA ligase |
127-681 |
6.80e-154 |
|
threonine-tRNA ligase
Pssm-ID: 215450 [Multi-domain] Cd Length: 614 Bit Score: 459.36 E-value: 6.80e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 127 HSSAHIMGEAMERVYGGC-LCYGPPIENGFYYDMYLEEggVSSNDFSSLETLCKKIIKEKQTFERLEVKKETLLEMFKY- 204
Cdd:PLN02837 48 HTCAHVMAMAVQKLFPDAkVTIGPWIENGFYYDFDMEP--LTDKDLKRIKKEMDRIISRNLPLVREEVSREEAQKRIMAi 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 205 -NKFKCRILnEKVNTPTTTVYRCG-PLIDLCRGPHVRHTGKI--KTLKIHKNSSTYWEGKADMETLQRIYGISFPDPKLL 280
Cdd:PLN02837 126 nEPYKLEIL-EGIKEEPITIYHIGeEWWDLCAGPHVERTGKInkKAVELESVAGAYWRGDEKNQMLQRIYGTAWESEEQL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 281 KEWEKFQEEAKNRDHRKIGRDQELYFFHELSPGS-CFFLPKGAYIYNTLMEFIRSEYRKRGFQEVVTPNIFNSRLWMTSG 359
Cdd:PLN02837 205 KAYLHFKEEAKRRDHRRLGQDLDLFSIQDDAGGGlVFWHPKGAIVRHIIEDSWKKMHFEHGYDLLYTPHVAKADLWKTSG 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 360 HWQHYSENMFS-FEVEKEQFALKPMNCPGHCLMFDHRPRSWRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIF 438
Cdd:PLN02837 285 HLDFYKENMYDqMDIEDELYQLRPMNCPYHILVYKRKLHSYRDLPIRVAELGTVYRYELSGSLHGLFRVRGFTQDDAHIF 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 439 CAMEQIEDEIKGCLDFLRTVYSVFGFS-FKLNLSTRPEKFLGDIEIWNQAEKQLENSLNEFGEKWELNPGDGAFYGPKID 517
Cdd:PLN02837 365 CLEDQIKDEIRGVLDLTEEILKQFGFSkYEINLSTRPEKSVGSDDIWEKATTALRDALDDKGWEYKVDEGGGAFYGPKID 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 518 IQIKDAIGRYHQCATIQLDFQLPIRFNLTYVSHDgDDKKRPVIVHRAILGSVERMIAILTENYGGKWPFWLSPRQVMVVP 597
Cdd:PLN02837 445 LKIEDALGRKWQCSTIQVDFNLPERFDITYVDSN-SEKKRPIMIHRAILGSLERFFGVLIEHYAGDFPLWLAPVQARVLP 523
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 598 VGPTCDEYAQKVRQEFHDAKFMVDIDLdpGCTLNKKIRNAQLAQYNFILVVGEKEKASGTVNIRTRDNKVHGERTVGETV 677
Cdd:PLN02837 524 VTDNELEYCKEVVAKLKAKGIRAEVCH--GERLPKLIRNAETQKIPLMAVVGPKEVETRTLTVRSRHGGELGTMPVDDFI 601
|
....
gi 55741823 678 ERLQ 681
Cdd:PLN02837 602 NRIQ 605
|
|
| PRK03991 |
PRK03991 |
threonyl-tRNA synthetase; Validated |
273-682 |
1.01e-45 |
|
threonyl-tRNA synthetase; Validated
Pssm-ID: 235190 [Multi-domain] Cd Length: 613 Bit Score: 172.36 E-value: 1.01e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 273 SFPDPKLLKEWEKFQEEAKNRD--HRKIGRDQELYFFHELS-PGSCFFLPKGAYIYNTLMEFIRSEYRKRGFQEVVTPNI 349
Cdd:PRK03991 175 GYEDLKALVDYEVGKKELVGGEppHVKLMREKELADYEPASdVGHMRYYPKGRLIRDLLEDYVYNLVVELGAMPVETPIM 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 350 FNSRLWMTSGHWQHYSENMFSFEVEKEQFALKPMNCPGHCLMFDHRPRSWRELPLR---LADFGvlHRNELSGALTGLTR 426
Cdd:PRK03991 255 YDLSHPAIREHADKFGERQYRVKSDKKDLMLRFAACFGQFLMLKDMTISYKNLPLKmyeLSTYS--FRLEQRGELVGLKR 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 427 VRRFQQDDAHIFC-----AMEQIEDEIKGCL----DFLRTVYSVFGFSfklnlstrpEKFlgdieiWNQAEKQLENSLNE 497
Cdd:PRK03991 333 LRAFTMPDMHTLCkdmeqAMEEFEKQYEMILetgeDLGRDYEVAIRFT---------EDF------YEENKDWIVELVKR 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 498 FG-----EKWElnpgDGAFYGP-KIDIQIKDAIGRYHQCATIQLDFQLPIRFNLTYVsHDGDDKKRPVIVHRAILGSVER 571
Cdd:PRK03991 398 EGkpvllEILP----ERKHYWVlKVEFAFIDSLGRPIENPTVQIDVENAERFGIKYV-DENGEEKYPIILHCSPTGSIER 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 572 MIAILTEN-----YGGK---WPFWLSPRQVMVVPVGPTCDEYAQKVRQEFHDAKFMVDIDlDPGCTLNKKIRNAQLAQYN 643
Cdd:PRK03991 473 VIYALLEKaakeeEEGKvpmLPTWLSPTQVRVIPVSERHLDYAEEVADKLEAAGIRVDVD-DRDESLGKKIRDAGKEWIP 551
|
410 420 430
....*....|....*....|....*....|....*....
gi 55741823 644 FILVVGEKEKASGTVNIRTRDNKVHGERTVGETVERLQQ 682
Cdd:PRK03991 552 YVVVIGDKEMESGKLTVTIREESEKVEMTLEELIERIKE 590
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
369-580 |
2.48e-39 |
|
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: 142.94 E-value: 2.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 369 FSFEVE-KEQFALKPMNCPGHCLMF-DHRPRSWReLPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCAMEQIED 446
Cdd:pfam00587 1 YKVEDEnGDELALKPTNEPGHTLLFrEEGLRSKD-LPLKLAQFGTCFRHEASGDTRGLIRVRQFHQDDAHIFHAPGQSPD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 447 EIKGCLDFLRTVYSVFGFSF-KLNLSTRPEkflgdieiwnqaekqlenslnefgekwelnpgdGAFYGPKIDIQIKDAI- 524
Cdd:pfam00587 80 ELEDYIKLIDRVYSRLGLEVrVVRLSNSDG---------------------------------SAFYGPKLDFEVVFPSl 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 55741823 525 GRYHQCATIQLD-FQLPIRFNLTYVSHDgDDKKRPVIVHRAILGsVERMIAILTENY 580
Cdd:pfam00587 127 GKQRQTGTIQNDgFRLPRRLGIRYKDED-NESKFPYMIHRAGLG-VERFLAAILENN 181
|
|
| ThrRS_anticodon |
cd00860 |
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases ... |
590-681 |
1.11e-35 |
|
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: 129.55 E-value: 1.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 590 PRQVMVVPVGPTCDEYAQKVRQEFHDAKFMVDIDLDpGCTLNKKIRNAQLAQYNFILVVGEKEKASGTVNIRTRDNKVHG 669
Cdd:cd00860 1 PVQVVVIPVTDEHLDYAKEVAKKLSDAGIRVEVDLR-NEKLGKKIREAQLQKIPYILVVGDKEVETGTVSVRTRDGGDLG 79
|
90
....*....|..
gi 55741823 670 ERTVGETVERLQ 681
Cdd:cd00860 80 SMSLDEFIEKLK 91
|
|
| 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 ... |
321-577 |
2.84e-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: 107.86 E-value: 2.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 321 GAYIYNTLMEFIRSEYRKRGFQEVVTPNIFNSRLWMTSGHWQHYSENMFSFEVEKEQ-----FALKPMNCPGHCLMFDHR 395
Cdd:cd00670 1 GTALWRALERFLDDRMAEYGYQEILFPFLAPTVLFFKGGHLDGYRKEMYTFEDKGRElrdtdLVLRPAACEPIYQIFSGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 396 PRSWRELPLRLADFGVLHRNELSGAlTGLTRVRRFQQDDAHIFCAMEQIEDEIKGCLDFLRTVYSVFGFSFKLNLSTRPE 475
Cdd:cd00670 81 ILSYRALPLRLDQIGPCFRHEPSGR-RGLMRVREFRQVEYVVFGEPEEAEEERREWLELAEEIARELGLPVRVVVADDPF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 476 KFLGDieiwnqaekqlenslnefgekwelNPGDGAFYGPKIDIQIKDAI-GRYHQCATIQLDFQLPIRFNLTYVSHDGDD 554
Cdd:cd00670 160 FGRGG------------------------KRGLDAGRETVVEFELLLPLpGRAKETAVGSANVHLDHFGASFKIDEDGGG 215
|
250 260
....*....|....*....|...
gi 55741823 555 KKrPVIVHRAilGSVERMIAILT 577
Cdd:cd00670 216 RA-HTGCGGA--GGEERLVLALL 235
|
|
| TGS_ThrRS |
cd01667 |
TGS (ThrRS, GTPase and SpoT) domain found in threonyl-tRNA synthetase (ThrRS) and similar ... |
55-120 |
1.11e-25 |
|
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: 100.25 E-value: 1.11e-25
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 55741823 55 IKVTLPDGKQVDAESwKTTPYQIACGISQGLADNTVVAKVNKVVWDLDRPLETDCTLELLKFEDEE 120
Cdd:cd01667 1 IKITLPDGSVKEFPK-GTTPLDIAKSISPGLAKKAVAAKVNGELVDLSRPLEEDAELEILTFDDPE 65
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
592-683 |
1.56e-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: 95.35 E-value: 1.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 592 QVMVVPVGPTCD---EYAQKVRQEFHDAKFMVDIDLDPGcTLNKKIRNAQLAQYNFILVVGEKEKASGTVNIRTRDNKVH 668
Cdd:pfam03129 1 QVVVIPLGEKAEeleEYAQKLAEELRAAGIRVELDDRNE-SIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQ 79
|
90
....*....|....*
gi 55741823 669 GERTVGETVERLQQL 683
Cdd:pfam03129 80 ETVSLDELVEKLKEL 94
|
|
| TGS |
pfam02824 |
TGS domain; The TGS domain is named after ThrRS, GTPase, and SpoT. Interestingly, TGS domain ... |
55-115 |
1.55e-17 |
|
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: 76.82 E-value: 1.55e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 55741823 55 IKVTLPDGKQVDAESWkTTPYQIACGISQGLADNTVVAKVNKVVWDLDRPLETDCTLELLK 115
Cdd:pfam02824 1 IRVYTPDGKVPDLPRG-ATPEDFAYAIHTSLAKKFIYAKVNGQLVGLDHPLEDGDVVEIVT 60
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
324-492 |
7.61e-16 |
|
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: 76.77 E-value: 7.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 324 IYNTLMEFIRSeyrkRGFQEVVTPNIFNSRLWMTSGHWqhYSENMFSFEVEKEQFALKPMNCPGHCLMF-DHRprswREL 402
Cdd:cd00768 5 IEQKLRRFMAE----LGFQEVETPIVEREPLLEKAGHE--PKDLLPVGAENEEDLYLRPTLEPGLVRLFvSHI----RKL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 403 PLRLADFGVLHRNELSGAltGLTRVRRFQQDDAHIFCAMEQIEDEIKGCLDFLRTVYSVFGFS--FKLNLSTRPEKFLG- 479
Cdd:cd00768 75 PLRLAEIGPAFRNEGGRR--GLRRVREFTQLEGEVFGEDGEEASEFEELIELTEELLRALGIKldIVFVEKTPGEFSPGg 152
|
170
....*....|....*...
gi 55741823 480 -----DIEIWNQAEKQLE 492
Cdd:cd00768 153 agpgfEIEVDHPEGRGLE 170
|
|
| tRNA_SAD |
smart00863 |
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active form of ... |
222-269 |
7.81e-12 |
|
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: 60.09 E-value: 7.81e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 55741823 222 TVYRCGPL-IDLCRGPHVRHTGKIKTLKIHKNSSTYWEgkadmetLQRI 269
Cdd:smart00863 2 RVVSIGDFsVELCGGTHVPNTGEIGAFKILSVSGAYWG-------LQRI 43
|
|
| tRNA_SAD |
pfam07973 |
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active from of ... |
222-269 |
2.89e-09 |
|
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: 52.83 E-value: 2.89e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 55741823 222 TVYRCGPL-IDLCRGPHVRHTGKIKTLKIHKnsstyWEGKADMetLQRI 269
Cdd:pfam07973 2 RVVSIGDFdVDLCGGTHVPNTGEIGAFKILK-----GESKNKG--LRRI 43
|
|
| PRK14938 |
PRK14938 |
Ser-tRNA(Thr) hydrolase; Provisional |
585-690 |
1.32e-07 |
|
Ser-tRNA(Thr) hydrolase; Provisional
Pssm-ID: 184902 [Multi-domain] Cd Length: 387 Bit Score: 54.47 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 585 PFWLSPRQVMVVPVGPTCDEYAQKVRQEFHDAKFMVDID-LDPGctLNKKIRNAQLAQYNFILVVGEKEKASGTVNIRTR 663
Cdd:PRK14938 269 PDWLNPIQVRILPVKKDFLDFSIQVAERLRKEGIRVNVDdLDDS--LGNKIRRAGTEWIPFVIIIGEREVKTSTLTVKIR 346
|
90 100
....*....|....*....|....*..
gi 55741823 664 DNKVHGERTVGETVERLQQLKQLRSKQ 690
Cdd:PRK14938 347 ANNEQKSMTVEELVKEIKRADELKERS 373
|
|
| ProRS_core |
cd00772 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
313-479 |
1.52e-06 |
|
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: 50.06 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 313 GSCFFLPKGAYIYNTLMEFIRSEYRKRGFQEVVTPNIFNSRLWMTSG-HWQHYSENMFSF-----EVEKEQFALKPMNCP 386
Cdd:cd00772 23 GIINFLPLAKAILDKIENVLDKMFKEHGAQNALFPFFILASFLEKEAeHDEGFSKELAVFkdagdEELEEDFALRPTLEE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 387 GHCLMFDHRPRSWRELPLRLADFGVLHRNELSgALTGLTRVRRFQQDDAHIFCA-MEQIEDEIKGCLDFLRTVYSVFG-F 464
Cdd:cd00772 103 NIGEIAAKFIKSWKDLPQHLNQIGNKFRDEIR-PRFGFLRAREFIMKDGHSAHAdAEEADEEFLNMLSAYAEIARDLAaI 181
|
170
....*....|....*
gi 55741823 465 SFKLNLSTRPEKFLG 479
Cdd:cd00772 182 DFIEGEADEGAKFAG 196
|
|
| PLN02320 |
PLN02320 |
seryl-tRNA synthetase |
293-484 |
3.16e-06 |
|
seryl-tRNA synthetase
Pssm-ID: 177954 [Multi-domain] Cd Length: 502 Bit Score: 50.31 E-value: 3.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 293 RDHRKIGRDQELYFFH---ELSPGSCFFLPKGAYIYN-TLMEFIRSEYRKRGFQEVVTPNIFNSRLWMTSGhWQHYSENM 368
Cdd:PLN02320 200 KDHLQLGKELDLFDFDaaaEVSGSKFYYLKNEAVLLEmALVNWTLSEVMKKGFTPLTTPEIVRSSVVEKCG-FQPRGDNT 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 369 FSFEVE-KEQFALKPMNCP-GHCLMFDHRPRSwrELPLRLADFGVLHRNE--LSGALT-GLTRVRRFQQDDAHIFCAMEQ 443
Cdd:PLN02320 279 QVYSIDgSDQCLIGTAEIPvGGIHMDSILLES--ALPLKYVAFSHCFRTEagAAGAATrGLYRVHQFSKVEMFVICRPEE 356
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 55741823 444 IEDEIKGCLDFLRTVYSVFGFSFK-LNLSTRP------EKFlgDIEIW 484
Cdd:PLN02320 357 SESFHEELIQIEEDLFTSLGLHFKtLDMATADlgapayRKF--DIEAW 402
|
|
| HGTP_anticodon |
cd00738 |
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ... |
590-681 |
5.25e-06 |
|
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and prolyl tRNA synthetases, which are classified as a group of class II aminoacyl-tRNA synthetases (aaRS). In aaRSs, the anticodon binding domain is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only. This domain is also found in the accessory subunit of mitochondrial polymerase gamma (Pol gamma b).
Pssm-ID: 238379 [Multi-domain] Cd Length: 94 Bit Score: 45.47 E-value: 5.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 590 PRQVMVVPVG---PTCDEYAQKVRQEFHDAKFMVDIDlDPGCTLNKKIRNAQLAQYNFILVVGEKEKASGTVNIRTRDNK 666
Cdd:cd00738 1 PIDVAIVPLTdprVEAREYAQKLLNALLANGIRVLYD-DRERKIGKKFREADLRGVPFAVVVGEDELENGKVTVKSRDTG 79
|
90
....*....|....*
gi 55741823 667 VHGERTVGETVERLQ 681
Cdd:cd00738 80 ESETLHVDELPEFLV 94
|
|
| ProRS_core_prok |
cd00779 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
310-446 |
5.89e-06 |
|
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: 48.34 E-value: 5.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 310 LSPGSCFFLPKGAYIYNTLMEFIRSEYRKRGFQEVVTPNIFNSRLWMTSGHWQHYSENMFSF-EVEKEQFALKPMNCPGH 388
Cdd:cd00779 19 TSSGLYSWLPLGLRVLKKIENIIREEMNKIGAQEILMPILQPAELWKESGRWDAYGPELLRLkDRHGKEFLLGPTHEEVI 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 55741823 389 CLMFDHRPRSWRELPLRLADFGVLHRNELSGALtGLTRVRRFQQDDAHIF-----CAMEQIED 446
Cdd:cd00779 99 TDLVANEIKSYKQLPLNLYQIQTKFRDEIRPRF-GLMRGREFLMKDAYSFdideeSLEETYEK 160
|
|
| HisRS_anticodon |
cd00859 |
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases ... |
592-681 |
1.58e-04 |
|
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: 40.99 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 592 QVMVVPVGPTCDEYAQKVRQEFHDAKFMVDIDLdpgctLNKKIRnAQLAQYN-----FILVVGEKEKASGTVNIrtRDNK 666
Cdd:cd00859 3 DVYVVPLGEGALSEALELAEQLRDAGIKAEIDY-----GGRKLK-KQFKYADrsgarFAVILGEDELAAGVVTV--KDLE 74
|
90
....*....|....*..
gi 55741823 667 VHGERTVGET--VERLQ 681
Cdd:cd00859 75 TGEQETVALDelVEELK 91
|
|
| PRK09194 |
PRK09194 |
prolyl-tRNA synthetase; Provisional |
537-684 |
1.66e-03 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 236405 [Multi-domain] Cd Length: 565 Bit Score: 41.61 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 537 FQLPIR----FNLTYVSHDGddKKRPVIvhraiLGS----VERMIAILTE-NY---GGKWPFWLSPRQVMVVPVGPTCD- 603
Cdd:PRK09194 410 FQLGTKyseaMNATVLDENG--KAQPLI-----MGCygigVSRLVAAAIEqNHdekGIIWPKAIAPFDVHIVPVNMKDEe 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 604 --EYAQKVRQEFHDAKfmVDIDLD-----PGCtlnkKIRNAQLAQYNFILVVGEKEKASGTVNIRTRDNKVHGERTVGET 676
Cdd:PRK09194 483 vkELAEKLYAELQAAG--IEVLLDdrkerPGV----KFADADLIGIPHRIVVGDRGLAEGIVEYKDRRTGEKEEVPVDEL 556
|
....*...
gi 55741823 677 VERLQQLK 684
Cdd:PRK09194 557 VEFLKALK 564
|
|
| ProRS_anticodon_zinc |
cd00862 |
ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and ... |
585-666 |
3.03e-03 |
|
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: 39.59 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 585 PFWLSPRQVMVVPVGPTCD------EYAQKVRQEFHDAKFMVDIDLDPGCTLNKKIRNAQLAQYNFILVVGEKEKASGTV 658
Cdd:cd00862 5 PPRVAPIQVVIVPIGIKDEkreevlEAADELAERLKAAGIRVHVDDRDNYTPGWKFNDWELKGVPLRIEIGPRDLEKNTV 84
|
....*...
gi 55741823 659 NIRTRDNK 666
Cdd:cd00862 85 VIVRRDTG 92
|
|
| ProRS_core_arch_euk |
cd00778 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
317-460 |
5.78e-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 archaea, the cytoplasm of eukaryotes and some bacteria.
Pssm-ID: 238401 [Multi-domain] Cd Length: 261 Bit Score: 39.12 E-value: 5.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741823 317 FLPKGAYIYNTLMEFIRSEYRKRGFQEVVTPN-IFNSRLWMTSGHWQHYSENMF-----SFEVEKEQFALKPMNCPGHCL 390
Cdd:cd00778 27 FRPYGYAIWENIQKILDKEIKETGHENVYFPLlIPESELEKEKEHIEGFAPEVAwvthgGLEELEEPLALRPTSETAIYP 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 55741823 391 MFDHRPRSWRELPLRLADFGVLHRNELSgALTGLTRVRRFQQDDAH-IFCAMEQIEDEIKGCLDFLRTVYS 460
Cdd:cd00778 107 MFSKWIRSYRDLPLKINQWVNVFRWETK-TTRPFLRTREFLWQEGHtAHATEEEAEEEVLQILDLYKEFYE 176
|
|
| |
