|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02908 |
PLN02908 |
threonyl-tRNA synthetase |
44-749 |
0e+00 |
|
threonyl-tRNA synthetase
Pssm-ID: 178496 [Multi-domain] Cd Length: 686 Bit Score: 1065.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 44 RAELNPWpeyIYTRLEMYNILKAEHdsiLAEKAEKDSKPIKVTLPDGKQVDAESWKTTPYQIACGIShtascknlsslas 123
Cdd:PLN02908 19 EEYLSAV---IKKRIELFEKIQARQ---LARLESAGGDPIKVTLPDGAVKDGKKWVTTPMDIAKEIS------------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 124 llasvaipssgmpwpplfflQGLADNTVIAKVNNVVWDLDRPLEEDCTLELLKFEDEEAQAVYWHSSAHIMGEAMERVYG 203
Cdd:PLN02908 80 --------------------KGLANSALIAQVDGVLWDMTRPLEGDCKLKLFKFDDDEGRDTFWHSSAHILGEALELEYG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 204 GCLCYGPPIEN--GFYYDMYLEEGGVSSNDFSSLEALCKKIIKEKQAFERLEVKKETLLAMFKYNKFKCRILNEKVNTPT 281
Cdd:PLN02908 140 CKLCIGPCTTRgeGFYYDAFYGDRTLNEEDFKPIEARAEKAVKEKQPFERIEVTREEALEMFSENKFKVEIINDLPEDAT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 282 TTVYRCGPLIDLCRGPHVRHTGKIKALKIHKNSSTYWEGKADMETLQRIYGISFPDPKMLKEWEKFQEEAKNRDHRKIGR 361
Cdd:PLN02908 220 ITVYRCGPLVDLCRGPHIPNTSFVKAFACLKASSAYWRGDVDRESLQRVYGISFPDKKLLKEYKHRIEEAKKRDHRLLGQ 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 362 DQELYFFHELSPGSCFFLPKGAYIYNALIEFIRSEYRKRGFQEVVTPNIFNSRLWMTSGHWQHYSENMFSFEVEKELFAL 441
Cdd:PLN02908 300 KQELFFFHELSPGSCFFLPHGARIYNKLMDFIREQYWERGYDEVITPNIYNMDLWETSGHAAHYKENMFVFEIEKQEFGL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 442 KPMNCPGHCLMFDHRPRSWRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCAMEQIEDEIKGCLDFLRTVYS 521
Cdd:PLN02908 380 KPMNCPGHCLMFAHRVRSYRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCREDQIKDEVKGVLDFLDYVYE 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 522 VFGFSFKLNLSTRPEKFLGDIEVWDQAEKQLENSLNEFGEKWELNSGDGAFYGPKIDIQIKDAIGRYHQCATIQLDFQLP 601
Cdd:PLN02908 460 VFGFTYELKLSTRPEKYLGDLETWDKAEAALTEALNAFGKPWQLNEGDGAFYGPKIDITVSDALKRKFQCATVQLDFQLP 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 602 IRFNLTYVSHDGDDKKRPVIVHRAILGSVERMIAILTENYGGKWPFWLSPRQVMVVPVGPTCDEYAQKVRQQFHDAKFMA 681
Cdd:PLN02908 540 IRFKLSYSAEDEAKIERPVMIHRAILGSVERMFAILLEHYAGKWPFWLSPRQAIVVPISEKSQDYAEEVRAQLHAAGFYV 619
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386642862 682 DIDLDPGcTLNKKIRNAQLAQYNFILVVGEKEKISGTVNIRTRDNKVHGERTISETIERLQQLKEFRS 749
Cdd:PLN02908 620 DVDVTDR-KIQKKVREAQLAQYNYILVVGEAEAATGTVNVRTRDNVVHGEKKIEELLTEFKEERAEFK 686
|
|
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
83-750 |
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: 877.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 83 IKVTLPDGKQVDAESwKTTPYQIACGIShtascknlsslasllasvaipssgmpwpplfflQGLADNTVIAKVNNVVWDL 162
Cdd:COG0441 2 IKITLPDGSVREFEA-GVTVLDVAKSIS---------------------------------PGLAKAAVAAKVNGELVDL 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 163 DRPLEEDCTLELLKFEDEEAQAVYWHSSAHIMGEAMERVYGGC-LCYGPPIENGFYYDMYLEEGgVSSNDFSSLEALCKK 241
Cdd:COG0441 48 STPIEEDAELEIVTFDDEEGLEILRHSAAHLLAQAVKRLYPDAkLTIGPVIENGFYYDFDLERP-FTPEDLEKIEKEMKE 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 242 IIKEKQAFERLEVKKETLLAMFKY--NKFKCRILNEKVNTPTTTVYRCGPLIDLCRGPHVRHTGKIKALKIHKNSSTYWE 319
Cdd:COG0441 127 IIKEDLPIEREEVSREEAIELFKEkgEPYKVELIEDIPEDEEISLYRQGEFVDLCRGPHVPSTGKIKAFKLLSVAGAYWR 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 320 GKADMETLQRIYGISFPDPKMLKEWEKFQEEAKNRDHRKIGRDQELYFFH-ELSPGSCFFLPKGAYIYNALIEFIRSEYR 398
Cdd:COG0441 207 GDEKNKMLQRIYGTAFPKKKELDAYLHRLEEAKKRDHRKLGKELDLFHFQeEVGPGLPFWHPKGAIIRRELEDYIREKHR 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 399 KRGFQEVVTPNIFNSRLWMTSGHWQHYSENMFSFEVEKELFALKPMNCPGHCLMFDHRPRSWRELPLRLADFGVLHRNEL 478
Cdd:COG0441 287 KAGYQEVKTPHILDRELWETSGHWDHYRENMFPTESDGEEYALKPMNCPGHILIYKSGLRSYRDLPLRLAEFGTVHRYEP 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 479 SGALTGLTRVRRFQQDDAHIFCAMEQIEDEIKGCLDFLRTVYSVFGFS-FKLNLSTRPEKFLGDIEVWDQAEKQLENSLN 557
Cdd:COG0441 367 SGALHGLMRVRGFTQDDAHIFCTPDQIEDEIKKVIDLVLEVYKDFGFEdYYVKLSTRPEKRIGSDEIWDKAEAALREALE 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 558 EFGEKWELNSGDGAFYGPKIDIQIKDAIGRYHQCATIQLDFQLPIRFNLTYVSHDGdDKKRPVIVHRAILGSVERMIAIL 637
Cdd:COG0441 447 ELGLEYVINPGEGAFYGPKIDFQLKDAIGREWQCGTIQLDFNLPERFDLTYVGEDG-EKHRPVMIHRAILGSIERFIGIL 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 638 TENYGGKWPFWLSPRQVMVVPVGPTCDEYAQKVRQQFHDAKFMADIDLDPGcTLNKKIRNAQLAQYNFILVVGEKEKISG 717
Cdd:COG0441 526 IEHYAGAFPLWLAPVQVVVLPISDKHADYAKEVAKKLRAAGIRVEVDLRNE-KIGYKIREAQLQKVPYMLVVGDKEVENG 604
|
650 660 670
....*....|....*....|....*....|...
gi 386642862 718 TVNIRTRDNKVHGERTISETIERLQQlkEFRSK 750
Cdd:COG0441 605 TVSVRRRGGGDLGTMSLDEFIARLKE--EIRSR 635
|
|
| thrS |
TIGR00418 |
threonyl-tRNA synthetase; This model represents the threonyl-tRNA synthetase found in most ... |
187-743 |
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: 674.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 187 WHSSAHIMGEAMERVYGG-CLCYGPPIENGFYYDMYLEEGgVSSNDFSSLEALCKKIIKEKQAFERLEVKKETLLAMFKY 265
Cdd:TIGR00418 1 RHSIAHLLAEALKQLYPDvKLAIGPVVEDGFYYDFELDRS-FTQEDLEKIEKDMKEIAKKNYPVAKLSVSLEEALEAFKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 266 NK-FKCRILNEKVNTPTTTVYRCG-PLIDLCRGPHVRHTGKIKALKIHKNSSTYWEGKADMETLQRIYGISFPDPKMLKE 343
Cdd:TIGR00418 80 LEpYKLELLDEIPNGVKRTPYGWGkAFVDLCKGPHLPNTSFIKAFKLEKVAGAYWRGDSKNKMLQRIYGTAWADKKQLAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 344 WEKFQEEAKNRDHRKIGRDQELYFFHELS-PGSCFFLPKGAYIYNALIEFIRSEYRKRGFQEVVTPNIFNSRLWMTSGHW 422
Cdd:TIGR00418 160 YLLRLEEAKKRDHRKLGKELELFSFEPEIgPGLPFWLPKGATIRNLLEDFVRQKQIKYGYMEVETPIMYDLELWEISGHW 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 423 QHYSENMFSF-EVEKELFALKPMNCPGHCLMFDHRPRSWRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCA 501
Cdd:TIGR00418 240 DNYKERMFPFtELDNREFMLKPMNCPGHFLIFKSSLRSYRDLPLRIAELGYSHRYEQSGELHGLMRVRGFTQDDAHIFCT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 502 MEQIEDEIKGCLDFLRTVYSVFGFSF-KLNLSTR-PEKFLGDIEVWDQAEKQLENSLNEFGEKWELNSGDGAFYGPKIDI 579
Cdd:TIGR00418 320 EDQIKEEFKNQFRLIQKVYSDFGFSFdKYELSTRdPEDFIGEDELWEKAEAALEEALKELGVPYEIDPGRGAFYGPKIDF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 580 QIKDAIGRYHQCATIQLDFQLPIRFNLTYVSHDGdDKKRPVIVHRAILGSVERMIAILTENYGGKWPFWLSPRQVMVVPV 659
Cdd:TIGR00418 400 AFKDALGREWQCATVQLDFELPERFDLTYVDEDN-EEKRPVMIHRAILGSIERFIAILLEKYAGNFPLWLAPVQVVVIPV 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 660 GPTCDEYAQKVRQQFHDAKFMADIDlDPGCTLNKKIRNAQLAQYNFILVVGEKEKISGTVNIRTRDNKVHGERTISETIE 739
Cdd:TIGR00418 479 NERHLDYAKKVAQKLKKAGIRVDVD-DRNERLGKKIREAQKQKIPYMLVVGDKEMESLAVNVRTRKGQKLEKMSLDEFLE 557
|
....
gi 386642862 740 RLQQ 743
Cdd:TIGR00418 558 KLRK 561
|
|
| ThrRS_core |
cd00771 |
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ... |
354-651 |
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: 544.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 354 RDHRKIGRDQELYFFHELSPGSCFFLPKGAYIYNALIEFIRSEYRKRGFQEVVTPNIFNSRLWMTSGHWQHYSENMFSFE 433
Cdd:cd00771 1 DHRRLGGELELFFFFDEAGPGLPFWLPKGAIIRNELEDFLRELQRKRGYQEVETPIIYNKELWETSGHWDHYRENMFPFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 434 VEKELFALKPMNCPGHCLMFDHRPRSWRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCAMEQIEDEIKGCL 513
Cdd:cd00771 81 EEDEEYGLKPMNCPGHCLIFKSKPRSYRDLPLRLAEFGTVHRYEQSGALHGLTRVRGFTQDDAHIFCTPDQIKEEIKGVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 514 DFLRTVYSVFGF-SFKLNLSTRPEKFLGDIEVWDQAEKQLENSLNEFGEKWELNSGDGAFYGPKIDIQIKDAIGRYHQCA 592
Cdd:cd00771 161 DLIKEVYSDFGFfDYKVELSTRPEKFIGSDEVWEKAEAALREALEEIGLPYEINEGEGAFYGPKIDFHVKDALGREWQCS 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 386642862 593 TIQLDFQLPIRFNLTYVSHDGdDKKRPVIVHRAILGSVERMIAILTENYGGKWPFWLSP 651
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 ... |
430-641 |
1.09e-38 |
|
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: 141.78 E-value: 1.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 430 FSFEVE-KELFALKPMNCPGHCLMF-DHRPRSWReLPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCAMEQIED 507
Cdd:pfam00587 1 YKVEDEnGDELALKPTNEPGHTLLFrEEGLRSKD-LPLKLAQFGTCFRHEASGDTRGLIRVRQFHQDDAHIFHAPGQSPD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 508 EIKGCLDFLRTVYSVFGFSF-KLNLSTRPEkflgdievwdqaekqlenslnefgekwelnsgdGAFYGPKIDIQIKDAI- 585
Cdd:pfam00587 80 ELEDYIKLIDRVYSRLGLEVrVVRLSNSDG---------------------------------SAFYGPKLDFEVVFPSl 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 386642862 586 GRYHQCATIQLD-FQLPIRFNLTYVSHDgDDKKRPVIVHRAILGsVERMIAILTENY 641
Cdd:pfam00587 127 GKQRQTGTIQNDgFRLPRRLGIRYKDED-NESKFPYMIHRAGLG-VERFLAAILENN 181
|
|
| tRNA_SAD |
smart00863 |
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active form of ... |
283-330 |
2.23e-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: 62.01 E-value: 2.23e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 386642862 283 TVYRCGPL-IDLCRGPHVRHTGKIKALKIHKNSSTYWEgkadmetLQRI 330
Cdd:smart00863 2 RVVSIGDFsVELCGGTHVPNTGEIGAFKILSVSGAYWG-------LQRI 43
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02908 |
PLN02908 |
threonyl-tRNA synthetase |
44-749 |
0e+00 |
|
threonyl-tRNA synthetase
Pssm-ID: 178496 [Multi-domain] Cd Length: 686 Bit Score: 1065.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 44 RAELNPWpeyIYTRLEMYNILKAEHdsiLAEKAEKDSKPIKVTLPDGKQVDAESWKTTPYQIACGIShtascknlsslas 123
Cdd:PLN02908 19 EEYLSAV---IKKRIELFEKIQARQ---LARLESAGGDPIKVTLPDGAVKDGKKWVTTPMDIAKEIS------------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 124 llasvaipssgmpwpplfflQGLADNTVIAKVNNVVWDLDRPLEEDCTLELLKFEDEEAQAVYWHSSAHIMGEAMERVYG 203
Cdd:PLN02908 80 --------------------KGLANSALIAQVDGVLWDMTRPLEGDCKLKLFKFDDDEGRDTFWHSSAHILGEALELEYG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 204 GCLCYGPPIEN--GFYYDMYLEEGGVSSNDFSSLEALCKKIIKEKQAFERLEVKKETLLAMFKYNKFKCRILNEKVNTPT 281
Cdd:PLN02908 140 CKLCIGPCTTRgeGFYYDAFYGDRTLNEEDFKPIEARAEKAVKEKQPFERIEVTREEALEMFSENKFKVEIINDLPEDAT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 282 TTVYRCGPLIDLCRGPHVRHTGKIKALKIHKNSSTYWEGKADMETLQRIYGISFPDPKMLKEWEKFQEEAKNRDHRKIGR 361
Cdd:PLN02908 220 ITVYRCGPLVDLCRGPHIPNTSFVKAFACLKASSAYWRGDVDRESLQRVYGISFPDKKLLKEYKHRIEEAKKRDHRLLGQ 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 362 DQELYFFHELSPGSCFFLPKGAYIYNALIEFIRSEYRKRGFQEVVTPNIFNSRLWMTSGHWQHYSENMFSFEVEKELFAL 441
Cdd:PLN02908 300 KQELFFFHELSPGSCFFLPHGARIYNKLMDFIREQYWERGYDEVITPNIYNMDLWETSGHAAHYKENMFVFEIEKQEFGL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 442 KPMNCPGHCLMFDHRPRSWRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCAMEQIEDEIKGCLDFLRTVYS 521
Cdd:PLN02908 380 KPMNCPGHCLMFAHRVRSYRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCREDQIKDEVKGVLDFLDYVYE 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 522 VFGFSFKLNLSTRPEKFLGDIEVWDQAEKQLENSLNEFGEKWELNSGDGAFYGPKIDIQIKDAIGRYHQCATIQLDFQLP 601
Cdd:PLN02908 460 VFGFTYELKLSTRPEKYLGDLETWDKAEAALTEALNAFGKPWQLNEGDGAFYGPKIDITVSDALKRKFQCATVQLDFQLP 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 602 IRFNLTYVSHDGDDKKRPVIVHRAILGSVERMIAILTENYGGKWPFWLSPRQVMVVPVGPTCDEYAQKVRQQFHDAKFMA 681
Cdd:PLN02908 540 IRFKLSYSAEDEAKIERPVMIHRAILGSVERMFAILLEHYAGKWPFWLSPRQAIVVPISEKSQDYAEEVRAQLHAAGFYV 619
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386642862 682 DIDLDPGcTLNKKIRNAQLAQYNFILVVGEKEKISGTVNIRTRDNKVHGERTISETIERLQQLKEFRS 749
Cdd:PLN02908 620 DVDVTDR-KIQKKVREAQLAQYNYILVVGEAEAATGTVNVRTRDNVVHGEKKIEELLTEFKEERAEFK 686
|
|
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
83-750 |
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: 877.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 83 IKVTLPDGKQVDAESwKTTPYQIACGIShtascknlsslasllasvaipssgmpwpplfflQGLADNTVIAKVNNVVWDL 162
Cdd:COG0441 2 IKITLPDGSVREFEA-GVTVLDVAKSIS---------------------------------PGLAKAAVAAKVNGELVDL 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 163 DRPLEEDCTLELLKFEDEEAQAVYWHSSAHIMGEAMERVYGGC-LCYGPPIENGFYYDMYLEEGgVSSNDFSSLEALCKK 241
Cdd:COG0441 48 STPIEEDAELEIVTFDDEEGLEILRHSAAHLLAQAVKRLYPDAkLTIGPVIENGFYYDFDLERP-FTPEDLEKIEKEMKE 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 242 IIKEKQAFERLEVKKETLLAMFKY--NKFKCRILNEKVNTPTTTVYRCGPLIDLCRGPHVRHTGKIKALKIHKNSSTYWE 319
Cdd:COG0441 127 IIKEDLPIEREEVSREEAIELFKEkgEPYKVELIEDIPEDEEISLYRQGEFVDLCRGPHVPSTGKIKAFKLLSVAGAYWR 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 320 GKADMETLQRIYGISFPDPKMLKEWEKFQEEAKNRDHRKIGRDQELYFFH-ELSPGSCFFLPKGAYIYNALIEFIRSEYR 398
Cdd:COG0441 207 GDEKNKMLQRIYGTAFPKKKELDAYLHRLEEAKKRDHRKLGKELDLFHFQeEVGPGLPFWHPKGAIIRRELEDYIREKHR 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 399 KRGFQEVVTPNIFNSRLWMTSGHWQHYSENMFSFEVEKELFALKPMNCPGHCLMFDHRPRSWRELPLRLADFGVLHRNEL 478
Cdd:COG0441 287 KAGYQEVKTPHILDRELWETSGHWDHYRENMFPTESDGEEYALKPMNCPGHILIYKSGLRSYRDLPLRLAEFGTVHRYEP 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 479 SGALTGLTRVRRFQQDDAHIFCAMEQIEDEIKGCLDFLRTVYSVFGFS-FKLNLSTRPEKFLGDIEVWDQAEKQLENSLN 557
Cdd:COG0441 367 SGALHGLMRVRGFTQDDAHIFCTPDQIEDEIKKVIDLVLEVYKDFGFEdYYVKLSTRPEKRIGSDEIWDKAEAALREALE 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 558 EFGEKWELNSGDGAFYGPKIDIQIKDAIGRYHQCATIQLDFQLPIRFNLTYVSHDGdDKKRPVIVHRAILGSVERMIAIL 637
Cdd:COG0441 447 ELGLEYVINPGEGAFYGPKIDFQLKDAIGREWQCGTIQLDFNLPERFDLTYVGEDG-EKHRPVMIHRAILGSIERFIGIL 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 638 TENYGGKWPFWLSPRQVMVVPVGPTCDEYAQKVRQQFHDAKFMADIDLDPGcTLNKKIRNAQLAQYNFILVVGEKEKISG 717
Cdd:COG0441 526 IEHYAGAFPLWLAPVQVVVLPISDKHADYAKEVAKKLRAAGIRVEVDLRNE-KIGYKIREAQLQKVPYMLVVGDKEVENG 604
|
650 660 670
....*....|....*....|....*....|...
gi 386642862 718 TVNIRTRDNKVHGERTISETIERLQQlkEFRSK 750
Cdd:COG0441 605 TVSVRRRGGGDLGTMSLDEFIARLKE--EIRSR 635
|
|
| thrS |
TIGR00418 |
threonyl-tRNA synthetase; This model represents the threonyl-tRNA synthetase found in most ... |
187-743 |
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: 674.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 187 WHSSAHIMGEAMERVYGG-CLCYGPPIENGFYYDMYLEEGgVSSNDFSSLEALCKKIIKEKQAFERLEVKKETLLAMFKY 265
Cdd:TIGR00418 1 RHSIAHLLAEALKQLYPDvKLAIGPVVEDGFYYDFELDRS-FTQEDLEKIEKDMKEIAKKNYPVAKLSVSLEEALEAFKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 266 NK-FKCRILNEKVNTPTTTVYRCG-PLIDLCRGPHVRHTGKIKALKIHKNSSTYWEGKADMETLQRIYGISFPDPKMLKE 343
Cdd:TIGR00418 80 LEpYKLELLDEIPNGVKRTPYGWGkAFVDLCKGPHLPNTSFIKAFKLEKVAGAYWRGDSKNKMLQRIYGTAWADKKQLAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 344 WEKFQEEAKNRDHRKIGRDQELYFFHELS-PGSCFFLPKGAYIYNALIEFIRSEYRKRGFQEVVTPNIFNSRLWMTSGHW 422
Cdd:TIGR00418 160 YLLRLEEAKKRDHRKLGKELELFSFEPEIgPGLPFWLPKGATIRNLLEDFVRQKQIKYGYMEVETPIMYDLELWEISGHW 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 423 QHYSENMFSF-EVEKELFALKPMNCPGHCLMFDHRPRSWRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCA 501
Cdd:TIGR00418 240 DNYKERMFPFtELDNREFMLKPMNCPGHFLIFKSSLRSYRDLPLRIAELGYSHRYEQSGELHGLMRVRGFTQDDAHIFCT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 502 MEQIEDEIKGCLDFLRTVYSVFGFSF-KLNLSTR-PEKFLGDIEVWDQAEKQLENSLNEFGEKWELNSGDGAFYGPKIDI 579
Cdd:TIGR00418 320 EDQIKEEFKNQFRLIQKVYSDFGFSFdKYELSTRdPEDFIGEDELWEKAEAALEEALKELGVPYEIDPGRGAFYGPKIDF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 580 QIKDAIGRYHQCATIQLDFQLPIRFNLTYVSHDGdDKKRPVIVHRAILGSVERMIAILTENYGGKWPFWLSPRQVMVVPV 659
Cdd:TIGR00418 400 AFKDALGREWQCATVQLDFELPERFDLTYVDEDN-EEKRPVMIHRAILGSIERFIAILLEKYAGNFPLWLAPVQVVVIPV 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 660 GPTCDEYAQKVRQQFHDAKFMADIDlDPGCTLNKKIRNAQLAQYNFILVVGEKEKISGTVNIRTRDNKVHGERTISETIE 739
Cdd:TIGR00418 479 NERHLDYAKKVAQKLKKAGIRVDVD-DRNERLGKKIREAQKQKIPYMLVVGDKEMESLAVNVRTRKGQKLEKMSLDEFLE 557
|
....
gi 386642862 740 RLQQ 743
Cdd:TIGR00418 558 KLRK 561
|
|
| PRK12444 |
PRK12444 |
threonyl-tRNA synthetase; Reviewed |
145-743 |
0e+00 |
|
threonyl-tRNA synthetase; Reviewed
Pssm-ID: 183530 [Multi-domain] Cd Length: 639 Bit Score: 636.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 145 GLADNTVIAKVNNVVWDLDRPLEEDCTLELLKFEDEEAQAVYWHSSAHIMGEAMERVYGGC-LCYGPPIENGFYYDMYLE 223
Cdd:PRK12444 34 SLKKKAVAGKVNDKLYDLRRNLEEDAEVEIITIDSNEGVEIARHSAAHILAQAVKRLYGDVnLGVGPVIENGFYYDMDLP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 224 EGgVSSNDFSSLEALCKKIIKEKQAFERLEVKKETLLAMFKYN--KFKCRILNEKVNTPTTTVYRCGPLIDLCRGPHVRH 301
Cdd:PRK12444 114 SS-VNVEDLRKIEKEMKKIINENIKIERVEVSREEAAKLFQEMndRLKLELLEAIPSGESITLYKQGEFVDLCRGPHLPS 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 302 TGKIKALKIHKNSSTYWEGKADMETLQRIYGISFPDPKMLKEWEKFQEEAKNRDHRKIGRDQELYFFHELSPGSCFFLPK 381
Cdd:PRK12444 193 TGYLKAFQLTHVSGAYWRGDSNNQVLQRIYGVAFSSQKELEEYLHFVEEAAKRNHRKLGKELELFMFSEEAPGMPFYLPK 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 382 GAYIYNALIEFIRSEYRKRGFQEVVTPNIFNSRLWMTSGHWQHYSENMFSFEVEKELFALKPMNCPGHCLMFDHRPRSWR 461
Cdd:PRK12444 273 GQIIRNELEAFLREIQKEYNYQEVRTPFMMNQELWERSGHWDHYKDNMYFSEVDNKSFALKPMNCPGHMLMFKNKLHSYR 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 462 ELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCAMEQIEDEIKGCLDFLRTVYSVFGFSFKLNLSTRPEKFLGD 541
Cdd:PRK12444 353 ELPIRMCEFGQVHRHEFSGALNGLLRVRTFCQDDAHLFVTPDQIEDEIKSVMAQIDYVYKTFGFEYEVELSTRPEDSMGD 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 542 IEVWDQAEKQLENSLNEFGEKWELNSGDGAFYGPKIDIQIKDAIGRYHQCATIQLDFQLPIRFNLTYVSHDgDDKKRPVI 621
Cdd:PRK12444 433 DELWEQAEASLENVLQSLNYKYRLNEGDGAFYGPKIDFHIKDALNRSHQCGTIQLDFQMPEKFDLNYIDEK-NEKRRPVV 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 622 VHRAILGSVERMIAILTENYGGKWPFWLSPRQVMVVPVGPTC-DEYAQKVRQQFHDAKFMADIDLDPGcTLNKKIRNAQL 700
Cdd:PRK12444 512 IHRAVLGSLDRFLAILIEHFGGAFPAWLAPVQVKVIPVSNAVhVQYADEVADKLAQAGIRVERDERDE-KLGYKIREAQM 590
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 386642862 701 AQYNFILVVGEKEKISGTVNIRTRDNKVHGERTISETIERLQQ 743
Cdd:PRK12444 591 QKIPYVLVIGDKEMENGAVNVRKYGEEKSEVIELDMFVESIKE 633
|
|
| ThrRS_core |
cd00771 |
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ... |
354-651 |
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: 544.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 354 RDHRKIGRDQELYFFHELSPGSCFFLPKGAYIYNALIEFIRSEYRKRGFQEVVTPNIFNSRLWMTSGHWQHYSENMFSFE 433
Cdd:cd00771 1 DHRRLGGELELFFFFDEAGPGLPFWLPKGAIIRNELEDFLRELQRKRGYQEVETPIIYNKELWETSGHWDHYRENMFPFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 434 VEKELFALKPMNCPGHCLMFDHRPRSWRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCAMEQIEDEIKGCL 513
Cdd:cd00771 81 EEDEEYGLKPMNCPGHCLIFKSKPRSYRDLPLRLAEFGTVHRYEQSGALHGLTRVRGFTQDDAHIFCTPDQIKEEIKGVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 514 DFLRTVYSVFGF-SFKLNLSTRPEKFLGDIEVWDQAEKQLENSLNEFGEKWELNSGDGAFYGPKIDIQIKDAIGRYHQCA 592
Cdd:cd00771 161 DLIKEVYSDFGFfDYKVELSTRPEKFIGSDEVWEKAEAALREALEEIGLPYEINEGEGAFYGPKIDFHVKDALGREWQCS 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 386642862 593 TIQLDFQLPIRFNLTYVSHDGdDKKRPVIVHRAILGSVERMIAILTENYGGKWPFWLSP 651
Cdd:cd00771 241 TIQLDFNLPERFDLTYIGEDG-EKKRPVMIHRAILGSIERFIGILIEHYAGKFPLWLAP 298
|
|
| PLN02837 |
PLN02837 |
threonine-tRNA ligase |
188-749 |
5.52e-155 |
|
threonine-tRNA ligase
Pssm-ID: 215450 [Multi-domain] Cd Length: 614 Bit Score: 463.99 E-value: 5.52e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 188 HSSAHIMGEAMERVYGGC-LCYGPPIENGFYYDMYLEEggVSSNDFSSLEALCKKIIKEKQAFERLEVKKETLLAMFKY- 265
Cdd:PLN02837 48 HTCAHVMAMAVQKLFPDAkVTIGPWIENGFYYDFDMEP--LTDKDLKRIKKEMDRIISRNLPLVREEVSREEAQKRIMAi 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 266 -NKFKCRILnEKVNTPTTTVYRCG-PLIDLCRGPHVRHTGKI--KALKIHKNSSTYWEGKADMETLQRIYGISFPDPKML 341
Cdd:PLN02837 126 nEPYKLEIL-EGIKEEPITIYHIGeEWWDLCAGPHVERTGKInkKAVELESVAGAYWRGDEKNQMLQRIYGTAWESEEQL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 342 KEWEKFQEEAKNRDHRKIGRDQELYFFHELSPGS-CFFLPKGAYIYNALIEFIRSEYRKRGFQEVVTPNIFNSRLWMTSG 420
Cdd:PLN02837 205 KAYLHFKEEAKRRDHRRLGQDLDLFSIQDDAGGGlVFWHPKGAIVRHIIEDSWKKMHFEHGYDLLYTPHVAKADLWKTSG 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 421 HWQHYSENMFS-FEVEKELFALKPMNCPGHCLMFDHRPRSWRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIF 499
Cdd:PLN02837 285 HLDFYKENMYDqMDIEDELYQLRPMNCPYHILVYKRKLHSYRDLPIRVAELGTVYRYELSGSLHGLFRVRGFTQDDAHIF 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 500 CAMEQIEDEIKGCLDFLRTVYSVFGFS-FKLNLSTRPEKFLGDIEVWDQAEKQLENSLNEFGEKWELNSGDGAFYGPKID 578
Cdd:PLN02837 365 CLEDQIKDEIRGVLDLTEEILKQFGFSkYEINLSTRPEKSVGSDDIWEKATTALRDALDDKGWEYKVDEGGGAFYGPKID 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 579 IQIKDAIGRYHQCATIQLDFQLPIRFNLTYVSHDgDDKKRPVIVHRAILGSVERMIAILTENYGGKWPFWLSPRQVMVVP 658
Cdd:PLN02837 445 LKIEDALGRKWQCSTIQVDFNLPERFDITYVDSN-SEKKRPIMIHRAILGSLERFFGVLIEHYAGDFPLWLAPVQARVLP 523
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 659 VGPTCDEYAQKVRQQFHDAKFMADIDLdpGCTLNKKIRNAQLAQYNFILVVGEKEKISGTVNIRTRDNKVHGERTISETI 738
Cdd:PLN02837 524 VTDNELEYCKEVVAKLKAKGIRAEVCH--GERLPKLIRNAETQKIPLMAVVGPKEVETRTLTVRSRHGGELGTMPVDDFI 601
|
570
....*....|.
gi 386642862 739 ERLQQLKEFRS 749
Cdd:PLN02837 602 NRIQLAVENRT 612
|
|
| PRK03991 |
PRK03991 |
threonyl-tRNA synthetase; Validated |
334-743 |
5.52e-44 |
|
threonyl-tRNA synthetase; Validated
Pssm-ID: 235190 [Multi-domain] Cd Length: 613 Bit Score: 168.13 E-value: 5.52e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 334 SFPDPKMLKEWEKFQEEAKNRD--HRKIGRDQELYFFHELS-PGSCFFLPKGAYIYNALIEFIRSEYRKRGFQEVVTPNI 410
Cdd:PRK03991 175 GYEDLKALVDYEVGKKELVGGEppHVKLMREKELADYEPASdVGHMRYYPKGRLIRDLLEDYVYNLVVELGAMPVETPIM 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 411 FNSRLWMTSGHWQHYSENMFSFEVEKELFALKPMNCPGHCLMFDHRPRSWRELPLR---LADFGvlHRNELSGALTGLTR 487
Cdd:PRK03991 255 YDLSHPAIREHADKFGERQYRVKSDKKDLMLRFAACFGQFLMLKDMTISYKNLPLKmyeLSTYS--FRLEQRGELVGLKR 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 488 VRRFQQDDAHIFC-----AMEQIEDEIKGCL----DFLRTVYSVFGFSfklnlstrpEKFlgdievWDQAEKQLENSLNE 558
Cdd:PRK03991 333 LRAFTMPDMHTLCkdmeqAMEEFEKQYEMILetgeDLGRDYEVAIRFT---------EDF------YEENKDWIVELVKR 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 559 FG-----EKWElnsgDGAFYGP-KIDIQIKDAIGRYHQCATIQLDFQLPIRFNLTYVsHDGDDKKRPVIVHRAILGSVER 632
Cdd:PRK03991 398 EGkpvllEILP----ERKHYWVlKVEFAFIDSLGRPIENPTVQIDVENAERFGIKYV-DENGEEKYPIILHCSPTGSIER 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 633 MIAILTEN-----YGGK---WPFWLSPRQVMVVPVGPTCDEYAQKVRQQFHDAKFMADIDlDPGCTLNKKIRNAQLAQYN 704
Cdd:PRK03991 473 VIYALLEKaakeeEEGKvpmLPTWLSPTQVRVIPVSERHLDYAEEVADKLEAAGIRVDVD-DRDESLGKKIRDAGKEWIP 551
|
410 420 430
....*....|....*....|....*....|....*....
gi 386642862 705 FILVVGEKEKISGTVNIRTRDNKVHGERTISETIERLQQ 743
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 ... |
430-641 |
1.09e-38 |
|
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: 141.78 E-value: 1.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 430 FSFEVE-KELFALKPMNCPGHCLMF-DHRPRSWReLPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCAMEQIED 507
Cdd:pfam00587 1 YKVEDEnGDELALKPTNEPGHTLLFrEEGLRSKD-LPLKLAQFGTCFRHEASGDTRGLIRVRQFHQDDAHIFHAPGQSPD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 508 EIKGCLDFLRTVYSVFGFSF-KLNLSTRPEkflgdievwdqaekqlenslnefgekwelnsgdGAFYGPKIDIQIKDAI- 585
Cdd:pfam00587 80 ELEDYIKLIDRVYSRLGLEVrVVRLSNSDG---------------------------------SAFYGPKLDFEVVFPSl 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 386642862 586 GRYHQCATIQLD-FQLPIRFNLTYVSHDgDDKKRPVIVHRAILGsVERMIAILTENY 641
Cdd:pfam00587 127 GKQRQTGTIQNDgFRLPRRLGIRYKDED-NESKFPYMIHRAGLG-VERFLAAILENN 181
|
|
| ThrRS_anticodon |
cd00860 |
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases ... |
651-742 |
5.24e-36 |
|
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: 130.70 E-value: 5.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 651 PRQVMVVPVGPTCDEYAQKVRQQFHDAKFMADIDLDpGCTLNKKIRNAQLAQYNFILVVGEKEKISGTVNIRTRDNKVHG 730
Cdd:cd00860 1 PVQVVVIPVTDEHLDYAKEVAKKLSDAGIRVEVDLR-NEKLGKKIREAQLQKIPYILVVGDKEVETGTVSVRTRDGGDLG 79
|
90
....*....|..
gi 386642862 731 ERTISETIERLQ 742
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 ... |
382-638 |
7.24e-27 |
|
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: 109.79 E-value: 7.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 382 GAYIYNALIEFIRSEYRKRGFQEVVTPNIFNSRLWMTSGHWQHYSENMFSFEVEKE-----LFALKPMNCPGHCLMFDHR 456
Cdd:cd00670 1 GTALWRALERFLDDRMAEYGYQEILFPFLAPTVLFFKGGHLDGYRKEMYTFEDKGRelrdtDLVLRPAACEPIYQIFSGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 457 PRSWRELPLRLADFGVLHRNELSGAlTGLTRVRRFQQDDAHIFCAMEQIEDEIKGCLDFLRTVYSVFGFSFKLNLSTRPE 536
Cdd:cd00670 81 ILSYRALPLRLDQIGPCFRHEPSGR-RGLMRVREFRQVEYVVFGEPEEAEEERREWLELAEEIARELGLPVRVVVADDPF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 537 KFLGDievwdqaekqlenslnefgekwelNSGDGAFYGPKIDIQIKDAI-GRYHQCATIQLDFQLPIRFNLTYVSHDGDD 615
Cdd:cd00670 160 FGRGG------------------------KRGLDAGRETVVEFELLLPLpGRAKETAVGSANVHLDHFGASFKIDEDGGG 215
|
250 260
....*....|....*....|...
gi 386642862 616 KKrPVIVHRAilGSVERMIAILT 638
Cdd:cd00670 216 RA-HTGCGGA--GGEERLVLALL 235
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
653-744 |
1.34e-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: 1.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 653 QVMVVPVGPTCD---EYAQKVRQQFHDAKFMADIDLDPGcTLNKKIRNAQLAQYNFILVVGEKEKISGTVNIRTRDNKVH 729
Cdd:pfam03129 1 QVVVIPLGEKAEeleEYAQKLAEELRAAGIRVELDDRNE-SIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQ 79
|
90
....*....|....*
gi 386642862 730 GERTISETIERLQQL 744
Cdd:pfam03129 80 ETVSLDELVEKLKEL 94
|
|
| TGS_ThrRS |
cd01667 |
TGS (ThrRS, GTPase and SpoT) domain found in threonyl-tRNA synthetase (ThrRS) and similar ... |
83-181 |
4.81e-21 |
|
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: 87.16 E-value: 4.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 83 IKVTLPDGKQVDAESwKTTPYQIACGIShtascknlsslasllasvaipssgmpwpplfflQGLADNTVIAKVNNVVWDL 162
Cdd:cd01667 1 IKITLPDGSVKEFPK-GTTPLDIAKSIS---------------------------------PGLAKKAVAAKVNGELVDL 46
|
90
....*....|....*....
gi 386642862 163 DRPLEEDCTLELLKFEDEE 181
Cdd:cd01667 47 SRPLEEDAELEILTFDDPE 65
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
385-553 |
1.97e-15 |
|
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: 75.62 E-value: 1.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 385 IYNALIEFIRSEYRKRGFQEVVTPNIFNSRLWMTSGHWqhYSENMFSFEVEKELFALKPMNCPGHCLMF-DHRprswREL 463
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGHE--PKDLLPVGAENEEDLYLRPTLEPGLVRLFvSHI----RKL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 464 PLRLADFGVLHRNELSGAltGLTRVRRFQQDDAHIFCAMEQIEDEIKGCLDFLRTVYSVFGFS--FKLNLSTRPEKFLG- 540
Cdd:cd00768 75 PLRLAEIGPAFRNEGGRR--GLRRVREFTQLEGEVFGEDGEEASEFEELIELTEELLRALGIKldIVFVEKTPGEFSPGg 152
|
170
....*....|....*...
gi 386642862 541 -----DIEVWDQAEKQLE 553
Cdd:cd00768 153 agpgfEIEVDHPEGRGLE 170
|
|
| tRNA_SAD |
smart00863 |
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active form of ... |
283-330 |
2.23e-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: 62.01 E-value: 2.23e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 386642862 283 TVYRCGPL-IDLCRGPHVRHTGKIKALKIHKNSSTYWEgkadmetLQRI 330
Cdd:smart00863 2 RVVSIGDFsVELCGGTHVPNTGEIGAFKILSVSGAYWG-------LQRI 43
|
|
| TGS |
pfam02824 |
TGS domain; The TGS domain is named after ThrRS, GTPase, and SpoT. Interestingly, TGS domain ... |
83-176 |
3.49e-12 |
|
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: 61.79 E-value: 3.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 83 IKVTLPDGKQVDAESWkTTPYQIACGIShtascknlsslasllasvaipssgmpwpplfflQGLADNTVIAKVNNVVWDL 162
Cdd:pfam02824 1 IRVYTPDGKVPDLPRG-ATPEDFAYAIH---------------------------------TSLAKKFIYAKVNGQLVGL 46
|
90
....*....|....
gi 386642862 163 DRPLEEDCTLELLK 176
Cdd:pfam02824 47 DHPLEDGDVVEIVT 60
|
|
| tRNA_SAD |
pfam07973 |
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active from of ... |
283-330 |
8.62e-10 |
|
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: 54.37 E-value: 8.62e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 386642862 283 TVYRCGPL-IDLCRGPHVRHTGKIKALKIHKnsstyWEGKADMetLQRI 330
Cdd:pfam07973 2 RVVSIGDFdVDLCGGTHVPNTGEIGAFKILK-----GESKNKG--LRRI 43
|
|
| PRK14938 |
PRK14938 |
Ser-tRNA(Thr) hydrolase; Provisional |
646-751 |
2.44e-06 |
|
Ser-tRNA(Thr) hydrolase; Provisional
Pssm-ID: 184902 [Multi-domain] Cd Length: 387 Bit Score: 50.61 E-value: 2.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 646 PFWLSPRQVMVVPVGPTCDEYAQKVRQQFHDAKFMADID-LDPGctLNKKIRNAQLAQYNFILVVGEKEKISGTVNIRTR 724
Cdd:PRK14938 269 PDWLNPIQVRILPVKKDFLDFSIQVAERLRKEGIRVNVDdLDDS--LGNKIRRAGTEWIPFVIIIGEREVKTSTLTVKIR 346
|
90 100
....*....|....*....|....*..
gi 386642862 725 DNKVHGERTISETIERLQQLKEFRSKQ 751
Cdd:PRK14938 347 ANNEQKSMTVEELVKEIKRADELKERS 373
|
|
| ProRS_core |
cd00772 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
374-540 |
8.15e-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: 48.13 E-value: 8.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 374 GSCFFLPKGAYIYNALIEFIRSEYRKRGFQEVVTPNIFNSRLWMTSG-HWQHYSENMFSF-----EVEKELFALKPMNCP 447
Cdd:cd00772 23 GIINFLPLAKAILDKIENVLDKMFKEHGAQNALFPFFILASFLEKEAeHDEGFSKELAVFkdagdEELEEDFALRPTLEE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 448 GHCLMFDHRPRSWRELPLRLADFGVLHRNELSgALTGLTRVRRFQQDDAHIFCA-MEQIEDEIKGCLDFLRTVYSVFG-F 525
Cdd:cd00772 103 NIGEIAAKFIKSWKDLPQHLNQIGNKFRDEIR-PRFGFLRAREFIMKDGHSAHAdAEEADEEFLNMLSAYAEIARDLAaI 181
|
170
....*....|....*
gi 386642862 526 SFKLNLSTRPEKFLG 540
Cdd:cd00772 182 DFIEGEADEGAKFAG 196
|
|
| ProRS_core_prok |
cd00779 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
371-507 |
1.68e-05 |
|
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: 47.19 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 371 LSPGSCFFLPKGAYIYNALIEFIRSEYRKRGFQEVVTPNIFNSRLWMTSGHWQHYSENMFSF-EVEKELFALKPMNCPGH 449
Cdd:cd00779 19 TSSGLYSWLPLGLRVLKKIENIIREEMNKIGAQEILMPILQPAELWKESGRWDAYGPELLRLkDRHGKEFLLGPTHEEVI 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386642862 450 CLMFDHRPRSWRELPLRLADFGVLHRNELSGALtGLTRVRRFQQDDAHIF-----CAMEQIED 507
Cdd:cd00779 99 TDLVANEIKSYKQLPLNLYQIQTKFRDEIRPRF-GLMRGREFLMKDAYSFdideeSLEETYEK 160
|
|
| HGTP_anticodon |
cd00738 |
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ... |
651-742 |
1.75e-05 |
|
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: 43.93 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 651 PRQVMVVPVG---PTCDEYAQKVRQQFHDAKFMADIDlDPGCTLNKKIRNAQLAQYNFILVVGEKEKISGTVNIRTRDNK 727
Cdd:cd00738 1 PIDVAIVPLTdprVEAREYAQKLLNALLANGIRVLYD-DRERKIGKKFREADLRGVPFAVVVGEDELENGKVTVKSRDTG 79
|
90
....*....|....*
gi 386642862 728 VHGERTISETIERLQ 742
Cdd:cd00738 80 ESETLHVDELPEFLV 94
|
|
| HisRS_anticodon |
cd00859 |
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases ... |
653-742 |
1.25e-03 |
|
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only.
Pssm-ID: 238436 [Multi-domain] Cd Length: 91 Bit Score: 38.67 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 653 QVMVVPVGPTCDEYAQKVRQQFHDAKFMADIDLdpgctLNKKIRnAQLAQYN-----FILVVGEKEKISGTVNIrtRDNK 727
Cdd:cd00859 3 DVYVVPLGEGALSEALELAEQLRDAGIKAEIDY-----GGRKLK-KQFKYADrsgarFAVILGEDELAAGVVTV--KDLE 74
|
90
....*....|....*..
gi 386642862 728 VHGERTISET--IERLQ 742
Cdd:cd00859 75 TGEQETVALDelVEELK 91
|
|
| ProRS_anticodon_zinc |
cd00862 |
ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and ... |
646-756 |
9.01e-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: 38.05 E-value: 9.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386642862 646 PFWLSPRQVMVVPVGPTCD------EYAQKVRQQFHDAKFMADIDLDPGCTLNKKIRNAQLAQYNFILVVGEKEKISGTV 719
Cdd:cd00862 5 PPRVAPIQVVIVPIGIKDEkreevlEAADELAERLKAAGIRVHVDDRDNYTPGWKFNDWELKGVPLRIEIGPRDLEKNTV 84
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 386642862 720 NIRTRDNK----VHGERTISETIERLQQLKEFRSKQAEEEF 756
Cdd:cd00862 85 VIVRRDTGekktVPLAELVEKVPELLDEIQEDLYERALEFR 125
|
|
| |
