|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02678 |
PLN02678 |
seryl-tRNA synthetase |
3-510 |
0e+00 |
|
seryl-tRNA synthetase
Pssm-ID: 215364 [Multi-domain] Cd Length: 448 Bit Score: 627.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33468931 3 LDLDLFRVDKGGDPALIRETQEKRFKDPGLVDQLVKADSEWRRCRFRADNLNKLKNLCSKTIGEKMKKKEavgddesvpe 82
Cdd:PLN02678 2 LDINLFREEKGGDPELIRESQRRRFASVELVDEVIALDKEWRQRQFELDSLRKEFNKLNKEVAKLKIAKE---------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33468931 83 nvlNFDDLTADALAalkvsqikkvrllIDEAIQKCDGERVKLEAERFENLREIGNLLHPSVPISNDEDaDNKVERIWGDC 162
Cdd:PLN02678 72 ---DATELIAETKE-------------LKKEITEKEAEVQEAKAALDAKLKTIGNLVHDSVPVSNDEA-NNAVVRTWGEK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33468931 163 TVRKK-YSHVDLVVMVDGFEGEKGAVVAGSRGYFLKGPLVFLEQALIQYALRTLGSRGYTPIYTPFFMRKEVMQEVAQLS 241
Cdd:PLN02678 135 RQEPKlKNHVDLVELLGIVDTERGADVAGGRGYYLKGAGVLLNQALINFGLAFLRKRGYTPLQTPFFMRKDVMAKCAQLA 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33468931 242 QFDEELYKVIGKGseksddnsyDEKYLIATSEQPIAALHRDEWLRPEDLPIKYAGLSTCFRQEVGSHGRDTRGIFRVHQF 321
Cdd:PLN02678 215 QFDEELYKVTGEG---------DDKYLIATSEQPLCAYHRGDWIDPKELPIRYAGYSTCFRKEAGSHGRDTLGIFRVHQF 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33468931 322 EKIEQFVYSSPHDNKSWEMFDEMIATAEEFYQSLGIPYHIVNIVSGSLNHAASKKLDLEAWFPGSGAFRELVSCSNCTDY 401
Cdd:PLN02678 286 EKVEQFCITSPNGNESWEMHEEMLKNSEDFYQSLGIPYQVVSIVSGALNDAAAKKYDLEAWFPASKTYRELVSCSNCTDY 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33468931 402 QARRLRIRYGQTKKmmdkkknnlrfSTQNKlkamsslfspkkvEFVHMLNATMCATTRTICAILENYQAEKGIAVPEKLR 481
Cdd:PLN02678 366 QSRRLEIRYGQKKS-----------NEQTK-------------QYVHLLNSTLTATERTLCCILENYQTEDGVRVPEVLQ 421
|
490 500
....*....|....*....|....*....
gi 33468931 482 EFMppGLQELIPFVKPAPIDQEPSKKQKK 510
Cdd:PLN02678 422 PFM--GGIEFLPFKKKPPAKGKGKKKKKK 448
|
|
| SerRS_core |
cd00770 |
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the ... |
152-484 |
0e+00 |
|
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the attachment of serine to the 3' OH group of ribose of the appropriate tRNA. This domain It is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain. SerRS synthetase is a homodimer.
Pssm-ID: 238393 [Multi-domain] Cd Length: 297 Bit Score: 511.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33468931 152 DNKVERIWGDCTV--RKKYSHVDLVVMVDGFEGEKGAVVAGSRGYFLKGPLVFLEQALIQYALRTLGSRGYTPIYTPFFM 229
Cdd:cd00770 1 DNVEIRRWGEPRVfdFKPKDHVELGEKLDILDFERGAKVSGSRFYYLKGDGALLERALINFALDFLTKRGFTPVIPPFLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33468931 230 RKEVMQEVAQLSQFDEELYKVIGkgseksddnsyDEKYLIATSEQPIAALHRDEWLRPEDLPIKYAGLSTCFRQEVGSHG 309
Cdd:cd00770 81 RKEVMEGTGQLPKFDEQLYKVEG-----------EDLYLIATAEVPLAALHRDEILEEEELPLKYAGYSPCFRKEAGSAG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33468931 310 RDTRGIFRVHQFEKIEQFVYSSPhdNKSWEMFDEMIATAEEFYQSLGIPYHIVNIVSGSLNHAASKKLDLEAWFPGSGAF 389
Cdd:cd00770 150 RDTRGLFRVHQFEKVEQFVFTKP--EESWEELEELISNAEEILQELGLPYRVVNICTGDLGFAAAKKYDIEAWMPGQGKY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33468931 390 RELVSCSNCTDYQARRLRIRYGQTKKmmdkkknnlrfstqnklkamsslfspKKVEFVHMLNATMCATTRTICAILENYQ 469
Cdd:cd00770 228 REISSCSNCTDFQARRLNIRYRDKKD--------------------------GKKQYVHTLNGTALATPRTIVAILENYQ 281
|
330
....*....|....*.
gi 33468931 470 AEKGIA-VPEKLREFM 484
Cdd:cd00770 282 TEDGSVvIPEVLRPYM 297
|
|
| SerS |
COG0172 |
Seryl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Seryl-tRNA synthetase ... |
3-493 |
5.03e-158 |
|
Seryl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Seryl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439942 [Multi-domain] Cd Length: 421 Bit Score: 456.77 E-value: 5.03e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33468931 3 LDLDLFRvdkgGDPALIRETQEKRFKDPgLVDQLVKADSEWRRCRFRADNLNKLKNLCSKTIGEKMKKKEAvgddesvpe 82
Cdd:COG0172 2 LDIKLIR----ENPEAVKEALAKRGFDL-DVDELLELDEERRELQTEVEELRAERNALSKEIGKAKKKGEE--------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33468931 83 nvlnfddltADALAAlKVSQIKkvrllidEAIQKCDGERVKLEAERFENLREIGNLLHPSVPISNDEDaDNKVERIWG-- 160
Cdd:COG0172 68 ---------AEALIA-EVKELK-------EEIKELEEELKELEEELDELLLSIPNLPHESVPVGKDES-DNVEVRRWGep 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33468931 161 ---DCTVRkkySHVDLVVMVDGFEGEKGAVVAGSRGYFLKGPLVFLEQALIQYALRTLGSRGYTPIYTPFFMRKEVMQEV 237
Cdd:COG0172 130 refDFEPK---DHWELGEKLGILDFERAAKVSGSRFYVLKGDGARLERALIQFMLDLHTEHGYTEVIPPYLVNEESMYGT 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33468931 238 AQLSQFDEELYKVIGkgseksddnsyDEKYLIATSEQPIAALHRDEWLRPEDLPIKYAGLSTCFRQEVGSHGRDTRGIFR 317
Cdd:COG0172 207 GQLPKFEEDLYKIEG-----------DDLYLIPTAEVPLTNLHRDEILDEEDLPLRYTAYTPCFRREAGSYGRDTRGLIR 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33468931 318 VHQFEKIEQFVYSSPHDnkSWEMFDEMIATAEEFYQSLGIPYHIVNIVSGSLNHAASKKLDLEAWFPGSGAFRELVSCSN 397
Cdd:COG0172 276 QHQFDKVEMVQFVKPED--SYEELEELTAHAEEILQKLGLPYRVVLLCTGDLGFSAAKTYDLEVWLPGQNKYREISSCSN 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33468931 398 CTDYQARRLRIRYgqtkkmmdkkknnlRFSTqnklkamsslfspKKVEFVHMLNATMCATTRTICAILENYQAEKG-IAV 476
Cdd:COG0172 354 CTDFQARRLNIRY--------------RDED-------------GKPEFVHTLNGSGLAVGRTLVAILENYQQADGsVRI 406
|
490
....*....|....*..
gi 33468931 477 PEKLREFMppGLQELIP 493
Cdd:COG0172 407 PEVLRPYM--GGLEVIE 421
|
|
| serS |
TIGR00414 |
seryl-tRNA synthetase; This model represents the seryl-tRNA synthetase found in most organisms. ... |
7-484 |
1.30e-136 |
|
seryl-tRNA synthetase; This model represents the seryl-tRNA synthetase found in most organisms. This protein is a class II tRNA synthetase, and is recognized by the pfam model tRNA-synt_2b. The seryl-tRNA synthetases of two archaeal species, Methanococcus jannaschii and Methanobacterium thermoautotrophicum, differ considerably and are included in a different model. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273066 [Multi-domain] Cd Length: 418 Bit Score: 402.13 E-value: 1.30e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33468931 7 LFRVDKGGDPALIRETQEKR---FKDPglVDQLVKADSEWRRCRFRADNLNKLKNLCSKTIGEKMKKKEavgddesvpen 83
Cdd:TIGR00414 2 LDRKLLRNNPDLVKESLKARglsVDID--LEKLIALDDERKKLLSEIEELQAKRNELSKQIGKAKGQKK----------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33468931 84 vlnfdDLTADALAalkvsQIKKVRLLIDEAIQKCDgervKLEAERFENLREIGNLLHPSVPISNDEDaDNKVERIWGDCT 163
Cdd:TIGR00414 69 -----DKIEEIKK-----ELKELKEELTELSAALK----ALEAELQDKLLSIPNIPHESVPVGKDEE-DNLEVKRWGTPP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33468931 164 VR--KKYSHVDLVVMVDGFEGEKGAVVAGSRGYFLKGPLVFLEQALIQYALRTLGSRGYTPIYTPFFMRKEVMQEVAQLS 241
Cdd:TIGR00414 134 VFdfKPKPHWELGEKLGGLDFDRAVKVTGSRFYYLKNDGAKLERALINFMLDLLEKNGYQEIYPPYLVNEESLDGTGQLP 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33468931 242 QFDEELYKVIGkgseksddnsyDEKYLIATSEQPIAALHRDEWLRPEDLPIKYAGLSTCFRQEVGSHGRDTRGIFRVHQF 321
Cdd:TIGR00414 214 KFEEDIFKLED-----------TDLYLIPTAEVPLTNLHRNEILEEEELPIKYTAHSPCFRSEAGSYGKDTKGLIRVHQF 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33468931 322 EKIEQFVYSSPhdNKSWEMFDEMIATAEEFYQSLGIPYHIVNIVSGSLNHAASKKLDLEAWFPGSGAFRELVSCSNCTDY 401
Cdd:TIGR00414 283 NKVELVKFCKP--EESAEELEEMTSDAEQILQELELPYRVVNLCSGDLGFSAAKKYDLEVWMPGQNTYREISSCSNCTDF 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33468931 402 QARRLRIRYGQtkkmmdkkknnlrfstQNKlkamsslfspKKVEFVHMLNATMCATTRTICAILENYQAEKG-IAVPEKL 480
Cdd:TIGR00414 361 QARRLNIRYKD----------------KNK----------GKNKYVHTLNGTALAIGRTIVAILENYQTEDGsVEIPEVL 414
|
....
gi 33468931 481 REFM 484
Cdd:TIGR00414 415 RKYL 418
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
258-468 |
9.80e-58 |
|
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: 190.32 E-value: 9.80e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33468931 258 SDDNSyDEKYLIATSEQPIAALHRDEWLRPEDLPIKYAGLSTCFRQEVGshgRDTRGIFRVHQFEKIEQFVYSSPhdNKS 337
Cdd:pfam00587 4 EDENG-DELALKPTNEPGHTLLFREEGLRSKDLPLKLAQFGTCFRHEAS---GDTRGLIRVRQFHQDDAHIFHAP--GQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33468931 338 WEMFDEMIATAEEFYQSLGIPYHIVNIVSGSLNHAASKKLDLEAWFPGSGAFRELVSCSNCTDYQARRLRIRYgqtkkmm 417
Cdd:pfam00587 78 PDELEDYIKLIDRVYSRLGLEVRVVRLSNSDGSAFYGPKLDFEVVFPSLGKQRQTGTIQNDGFRLPRRLGIRY------- 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 33468931 418 dkkknnlrfstqnklkamssLFSPKKVEFVHMLNATMCATTRTICAILENY 468
Cdd:pfam00587 151 --------------------KDEDNESKFPYMIHRAGLGVERFLAAILENN 181
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02678 |
PLN02678 |
seryl-tRNA synthetase |
3-510 |
0e+00 |
|
seryl-tRNA synthetase
Pssm-ID: 215364 [Multi-domain] Cd Length: 448 Bit Score: 627.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33468931 3 LDLDLFRVDKGGDPALIRETQEKRFKDPGLVDQLVKADSEWRRCRFRADNLNKLKNLCSKTIGEKMKKKEavgddesvpe 82
Cdd:PLN02678 2 LDINLFREEKGGDPELIRESQRRRFASVELVDEVIALDKEWRQRQFELDSLRKEFNKLNKEVAKLKIAKE---------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33468931 83 nvlNFDDLTADALAalkvsqikkvrllIDEAIQKCDGERVKLEAERFENLREIGNLLHPSVPISNDEDaDNKVERIWGDC 162
Cdd:PLN02678 72 ---DATELIAETKE-------------LKKEITEKEAEVQEAKAALDAKLKTIGNLVHDSVPVSNDEA-NNAVVRTWGEK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33468931 163 TVRKK-YSHVDLVVMVDGFEGEKGAVVAGSRGYFLKGPLVFLEQALIQYALRTLGSRGYTPIYTPFFMRKEVMQEVAQLS 241
Cdd:PLN02678 135 RQEPKlKNHVDLVELLGIVDTERGADVAGGRGYYLKGAGVLLNQALINFGLAFLRKRGYTPLQTPFFMRKDVMAKCAQLA 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33468931 242 QFDEELYKVIGKGseksddnsyDEKYLIATSEQPIAALHRDEWLRPEDLPIKYAGLSTCFRQEVGSHGRDTRGIFRVHQF 321
Cdd:PLN02678 215 QFDEELYKVTGEG---------DDKYLIATSEQPLCAYHRGDWIDPKELPIRYAGYSTCFRKEAGSHGRDTLGIFRVHQF 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33468931 322 EKIEQFVYSSPHDNKSWEMFDEMIATAEEFYQSLGIPYHIVNIVSGSLNHAASKKLDLEAWFPGSGAFRELVSCSNCTDY 401
Cdd:PLN02678 286 EKVEQFCITSPNGNESWEMHEEMLKNSEDFYQSLGIPYQVVSIVSGALNDAAAKKYDLEAWFPASKTYRELVSCSNCTDY 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33468931 402 QARRLRIRYGQTKKmmdkkknnlrfSTQNKlkamsslfspkkvEFVHMLNATMCATTRTICAILENYQAEKGIAVPEKLR 481
Cdd:PLN02678 366 QSRRLEIRYGQKKS-----------NEQTK-------------QYVHLLNSTLTATERTLCCILENYQTEDGVRVPEVLQ 421
|
490 500
....*....|....*....|....*....
gi 33468931 482 EFMppGLQELIPFVKPAPIDQEPSKKQKK 510
Cdd:PLN02678 422 PFM--GGIEFLPFKKKPPAKGKGKKKKKK 448
|
|
| SerRS_core |
cd00770 |
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the ... |
152-484 |
0e+00 |
|
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the attachment of serine to the 3' OH group of ribose of the appropriate tRNA. This domain It is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain. SerRS synthetase is a homodimer.
Pssm-ID: 238393 [Multi-domain] Cd Length: 297 Bit Score: 511.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33468931 152 DNKVERIWGDCTV--RKKYSHVDLVVMVDGFEGEKGAVVAGSRGYFLKGPLVFLEQALIQYALRTLGSRGYTPIYTPFFM 229
Cdd:cd00770 1 DNVEIRRWGEPRVfdFKPKDHVELGEKLDILDFERGAKVSGSRFYYLKGDGALLERALINFALDFLTKRGFTPVIPPFLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33468931 230 RKEVMQEVAQLSQFDEELYKVIGkgseksddnsyDEKYLIATSEQPIAALHRDEWLRPEDLPIKYAGLSTCFRQEVGSHG 309
Cdd:cd00770 81 RKEVMEGTGQLPKFDEQLYKVEG-----------EDLYLIATAEVPLAALHRDEILEEEELPLKYAGYSPCFRKEAGSAG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33468931 310 RDTRGIFRVHQFEKIEQFVYSSPhdNKSWEMFDEMIATAEEFYQSLGIPYHIVNIVSGSLNHAASKKLDLEAWFPGSGAF 389
Cdd:cd00770 150 RDTRGLFRVHQFEKVEQFVFTKP--EESWEELEELISNAEEILQELGLPYRVVNICTGDLGFAAAKKYDIEAWMPGQGKY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33468931 390 RELVSCSNCTDYQARRLRIRYGQTKKmmdkkknnlrfstqnklkamsslfspKKVEFVHMLNATMCATTRTICAILENYQ 469
Cdd:cd00770 228 REISSCSNCTDFQARRLNIRYRDKKD--------------------------GKKQYVHTLNGTALATPRTIVAILENYQ 281
|
330
....*....|....*.
gi 33468931 470 AEKGIA-VPEKLREFM 484
Cdd:cd00770 282 TEDGSVvIPEVLRPYM 297
|
|
| SerS |
COG0172 |
Seryl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Seryl-tRNA synthetase ... |
3-493 |
5.03e-158 |
|
Seryl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Seryl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439942 [Multi-domain] Cd Length: 421 Bit Score: 456.77 E-value: 5.03e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33468931 3 LDLDLFRvdkgGDPALIRETQEKRFKDPgLVDQLVKADSEWRRCRFRADNLNKLKNLCSKTIGEKMKKKEAvgddesvpe 82
Cdd:COG0172 2 LDIKLIR----ENPEAVKEALAKRGFDL-DVDELLELDEERRELQTEVEELRAERNALSKEIGKAKKKGEE--------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33468931 83 nvlnfddltADALAAlKVSQIKkvrllidEAIQKCDGERVKLEAERFENLREIGNLLHPSVPISNDEDaDNKVERIWG-- 160
Cdd:COG0172 68 ---------AEALIA-EVKELK-------EEIKELEEELKELEEELDELLLSIPNLPHESVPVGKDES-DNVEVRRWGep 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33468931 161 ---DCTVRkkySHVDLVVMVDGFEGEKGAVVAGSRGYFLKGPLVFLEQALIQYALRTLGSRGYTPIYTPFFMRKEVMQEV 237
Cdd:COG0172 130 refDFEPK---DHWELGEKLGILDFERAAKVSGSRFYVLKGDGARLERALIQFMLDLHTEHGYTEVIPPYLVNEESMYGT 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33468931 238 AQLSQFDEELYKVIGkgseksddnsyDEKYLIATSEQPIAALHRDEWLRPEDLPIKYAGLSTCFRQEVGSHGRDTRGIFR 317
Cdd:COG0172 207 GQLPKFEEDLYKIEG-----------DDLYLIPTAEVPLTNLHRDEILDEEDLPLRYTAYTPCFRREAGSYGRDTRGLIR 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33468931 318 VHQFEKIEQFVYSSPHDnkSWEMFDEMIATAEEFYQSLGIPYHIVNIVSGSLNHAASKKLDLEAWFPGSGAFRELVSCSN 397
Cdd:COG0172 276 QHQFDKVEMVQFVKPED--SYEELEELTAHAEEILQKLGLPYRVVLLCTGDLGFSAAKTYDLEVWLPGQNKYREISSCSN 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33468931 398 CTDYQARRLRIRYgqtkkmmdkkknnlRFSTqnklkamsslfspKKVEFVHMLNATMCATTRTICAILENYQAEKG-IAV 476
Cdd:COG0172 354 CTDFQARRLNIRY--------------RDED-------------GKPEFVHTLNGSGLAVGRTLVAILENYQQADGsVRI 406
|
490
....*....|....*..
gi 33468931 477 PEKLREFMppGLQELIP 493
Cdd:COG0172 407 PEVLRPYM--GGLEVIE 421
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
3-493 |
1.35e-155 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 450.67 E-value: 1.35e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33468931 3 LDLDLFRvdkgGDPALIRETQEKRFkDPGLVDQLVKADSEWRRCRFRADNLNKLKNLCSKTIGEKMKKKEAvgddesvpe 82
Cdd:PRK05431 2 LDIKLIR----ENPEAVKEALAKRG-FPLDVDELLELDEERRELQTELEELQAERNALSKEIGQAKRKGED--------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33468931 83 nvlnfddltADALaalkvsqIKKVRLLIDEaIQKCDGERVKLEAERFENLREIGNLLHPSVPISNDEDaDNKVERIWG-- 160
Cdd:PRK05431 68 ---------AEAL-------IAEVKELKEE-IKALEAELDELEAELEELLLRIPNLPHDSVPVGKDED-DNVEVRRWGep 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33468931 161 ---DCTVRkkySHVDLVVMVDGFEGEKGAVVAGSRGYFLKGPLVFLEQALIQYALRTL-GSRGYTPIYTPFFMRKEVMQE 236
Cdd:PRK05431 130 refDFEPK---DHWELGEKLGILDFERAAKVSGSRFYVLKGDGARLERALIQFMLDLHtEEHGYTEVIPPYLVNEESMYG 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33468931 237 VAQLSQFDEELYKVIGkgseksddnsyDEKYLIATSEQPIAALHRDEWLRPEDLPIKYAGLSTCFRQEVGSHGRDTRGIF 316
Cdd:PRK05431 207 TGQLPKFEEDLYKIED-----------DDLYLIPTAEVPLTNLHRDEILDEEELPLKYTAYSPCFRSEAGSAGRDTRGLI 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33468931 317 RVHQFEKIEQFVYSSPHDnkSWEMFDEMIATAEEFYQSLGIPYHIVNIVSGSLNHAASKKLDLEAWFPGSGAFRELVSCS 396
Cdd:PRK05431 276 RVHQFDKVELVKFTKPED--SYAELEELTANAEEILQKLELPYRVVLLCTGDLGFSAAKTYDLEVWLPSQNTYREISSCS 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33468931 397 NCTDYQARRLRIRYgqtkkmmdkkknnlRFSTQnklkamsslfspKKVEFVHMLNATMCATTRTICAILENYQAEKG-IA 475
Cdd:PRK05431 354 NCTDFQARRANIRY--------------RDEGD------------GKPELVHTLNGSGLAVGRTLVAILENYQQADGsVT 407
|
490
....*....|....*...
gi 33468931 476 VPEKLREFMppGLQELIP 493
Cdd:PRK05431 408 IPEVLRPYM--GGLEVIP 423
|
|
| serS |
TIGR00414 |
seryl-tRNA synthetase; This model represents the seryl-tRNA synthetase found in most organisms. ... |
7-484 |
1.30e-136 |
|
seryl-tRNA synthetase; This model represents the seryl-tRNA synthetase found in most organisms. This protein is a class II tRNA synthetase, and is recognized by the pfam model tRNA-synt_2b. The seryl-tRNA synthetases of two archaeal species, Methanococcus jannaschii and Methanobacterium thermoautotrophicum, differ considerably and are included in a different model. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273066 [Multi-domain] Cd Length: 418 Bit Score: 402.13 E-value: 1.30e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33468931 7 LFRVDKGGDPALIRETQEKR---FKDPglVDQLVKADSEWRRCRFRADNLNKLKNLCSKTIGEKMKKKEavgddesvpen 83
Cdd:TIGR00414 2 LDRKLLRNNPDLVKESLKARglsVDID--LEKLIALDDERKKLLSEIEELQAKRNELSKQIGKAKGQKK----------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33468931 84 vlnfdDLTADALAalkvsQIKKVRLLIDEAIQKCDgervKLEAERFENLREIGNLLHPSVPISNDEDaDNKVERIWGDCT 163
Cdd:TIGR00414 69 -----DKIEEIKK-----ELKELKEELTELSAALK----ALEAELQDKLLSIPNIPHESVPVGKDEE-DNLEVKRWGTPP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33468931 164 VR--KKYSHVDLVVMVDGFEGEKGAVVAGSRGYFLKGPLVFLEQALIQYALRTLGSRGYTPIYTPFFMRKEVMQEVAQLS 241
Cdd:TIGR00414 134 VFdfKPKPHWELGEKLGGLDFDRAVKVTGSRFYYLKNDGAKLERALINFMLDLLEKNGYQEIYPPYLVNEESLDGTGQLP 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33468931 242 QFDEELYKVIGkgseksddnsyDEKYLIATSEQPIAALHRDEWLRPEDLPIKYAGLSTCFRQEVGSHGRDTRGIFRVHQF 321
Cdd:TIGR00414 214 KFEEDIFKLED-----------TDLYLIPTAEVPLTNLHRNEILEEEELPIKYTAHSPCFRSEAGSYGKDTKGLIRVHQF 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33468931 322 EKIEQFVYSSPhdNKSWEMFDEMIATAEEFYQSLGIPYHIVNIVSGSLNHAASKKLDLEAWFPGSGAFRELVSCSNCTDY 401
Cdd:TIGR00414 283 NKVELVKFCKP--EESAEELEEMTSDAEQILQELELPYRVVNLCSGDLGFSAAKKYDLEVWMPGQNTYREISSCSNCTDF 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33468931 402 QARRLRIRYGQtkkmmdkkknnlrfstQNKlkamsslfspKKVEFVHMLNATMCATTRTICAILENYQAEKG-IAVPEKL 480
Cdd:TIGR00414 361 QARRLNIRYKD----------------KNK----------GKNKYVHTLNGTALAIGRTIVAILENYQTEDGsVEIPEVL 414
|
....
gi 33468931 481 REFM 484
Cdd:TIGR00414 415 RKYL 418
|
|
| PLN02320 |
PLN02320 |
seryl-tRNA synthetase |
122-493 |
1.17e-74 |
|
seryl-tRNA synthetase
Pssm-ID: 177954 [Multi-domain] Cd Length: 502 Bit Score: 245.22 E-value: 1.17e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33468931 122 VKLEAERFENLREIGNLLHPSVPISNDEDAdnkveriwgdcTVRKKY-----------SHVDLVVMVDGFEGEKGAVVAG 190
Cdd:PLN02320 154 VKLTDELQLEAQSIPNMTHPDVPVGGEDSS-----------AVRKEVgsprefsfpikDHLQLGKELDLFDFDAAAEVSG 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33468931 191 SRGYFLKGPLVFLEQALIQYALRTLGSRGYTPIYTPFFMRKEVMQEVA-QLSQFDEELYKVigkgsEKSDdnsydeKYLI 269
Cdd:PLN02320 223 SKFYYLKNEAVLLEMALVNWTLSEVMKKGFTPLTTPEIVRSSVVEKCGfQPRGDNTQVYSI-----DGSD------QCLI 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33468931 270 ATSEQPIAALHRDEWLRPEDLPIKYAGLSTCFRQEVGSHGRDTRGIFRVHQFEKIEQFVYSSPHDNKSWEmfDEMIATAE 349
Cdd:PLN02320 292 GTAEIPVGGIHMDSILLESALPLKYVAFSHCFRTEAGAAGAATRGLYRVHQFSKVEMFVICRPEESESFH--EELIQIEE 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33468931 350 EFYQSLGIPYHIVNIVSGSLNHAASKKLDLEAWFPGSGAFRELVSCSNCTDYQARRLRIRYGQTKKmmdkkknnlrfSTQ 429
Cdd:PLN02320 370 DLFTSLGLHFKTLDMATADLGAPAYRKFDIEAWMPGLGRYGEISSASNCTDYQSRRLGIRYRPSEP-----------PQT 438
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 33468931 430 NKLKAMSSLfSPKKveFVHMLNATMCATTRTICAILENYQAEKG-IAVPEKLREFMpPGLQELIP 493
Cdd:PLN02320 439 NPKKGKGSL-GPTK--FVHTLNATACAVPRMIVCLLENYQQEDGsVVIPEPLRPFM-GGLELIKP 499
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
258-468 |
9.80e-58 |
|
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: 190.32 E-value: 9.80e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33468931 258 SDDNSyDEKYLIATSEQPIAALHRDEWLRPEDLPIKYAGLSTCFRQEVGshgRDTRGIFRVHQFEKIEQFVYSSPhdNKS 337
Cdd:pfam00587 4 EDENG-DELALKPTNEPGHTLLFREEGLRSKDLPLKLAQFGTCFRHEAS---GDTRGLIRVRQFHQDDAHIFHAP--GQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33468931 338 WEMFDEMIATAEEFYQSLGIPYHIVNIVSGSLNHAASKKLDLEAWFPGSGAFRELVSCSNCTDYQARRLRIRYgqtkkmm 417
Cdd:pfam00587 78 PDELEDYIKLIDRVYSRLGLEVRVVRLSNSDGSAFYGPKLDFEVVFPSLGKQRQTGTIQNDGFRLPRRLGIRY------- 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 33468931 418 dkkknnlrfstqnklkamssLFSPKKVEFVHMLNATMCATTRTICAILENY 468
Cdd:pfam00587 151 --------------------KDEDNESKFPYMIHRAGLGVERFLAAILENN 181
|
|
| Gly_His_Pro_Ser_Thr_tRS_core |
cd00670 |
Gly_His_Pro_Ser_Thr_tRNA synthetase class II core domain. This domain is the core catalytic ... |
203-405 |
3.74e-22 |
|
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: 95.15 E-value: 3.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33468931 203 LEQALIQYALRTLGSRGYTPIYTPFFMRKEVMQEVAQLSQFDEELYKVigkgSEKSDDNSYDEKYLIATSEQPIAALHRD 282
Cdd:cd00670 4 LWRALERFLDDRMAEYGYQEILFPFLAPTVLFFKGGHLDGYRKEMYTF----EDKGRELRDTDLVLRPAACEPIYQIFSG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33468931 283 EWLRPEDLPIKYAGLSTCFRQEvgshGRDTRGIFRVHQFEKIEQFVYSSPHDNKSWemFDEMIATAEEFYQSLGIPYHIV 362
Cdd:cd00670 80 EILSYRALPLRLDQIGPCFRHE----PSGRRGLMRVREFRQVEYVVFGEPEEAEEE--RREWLELAEEIARELGLPVRVV 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 33468931 363 NIVSGS--------LNHAASKKLDLEAWFPGSGAFRELVSCSNCTDYQARR 405
Cdd:cd00670 154 VADDPFfgrggkrgLDAGRETVVEFELLLPLPGRAKETAVGSANVHLDHFG 204
|
|
| Seryl_tRNA_N |
pfam02403 |
Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA ... |
2-109 |
1.62e-17 |
|
Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA synthetase class II domain (pfam00587) and represents the N-terminal domain of seryl-tRNA synthetase.
Pssm-ID: 426757 [Multi-domain] Cd Length: 108 Bit Score: 78.01 E-value: 1.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33468931 2 VLDLDLFRVDkggdPALIRETQEKRFKDPGLVDQLVKADSEWRRCRFRADNLNKLKNLCSKTIGEKMKKKE-AVGDDESV 80
Cdd:pfam02403 1 MLDIKLIREN----PEAVKESLKKRGVDVLDVDELLELDEKRRELQVELEELQAERNELSKEIGQAKKKKEdADALIAEV 76
|
90 100
....*....|....*....|....*....
gi 33468931 81 PENVLNFDDLTAdALAALKVSQIKKVRLL 109
Cdd:pfam02403 77 KELKDELKALEA-ELKELEAELDKLLLTI 104
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
203-410 |
1.62e-10 |
|
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: 60.98 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33468931 203 LEQALIQYALRTLGSRGYTPIYTPFFMRKEVmqevaqLSQFDEELYKVIGKGSEKSDDnsydeKYLIATSEQPIAALHRd 282
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREPL------LEKAGHEPKDLLPVGAENEED-----LYLRPTLEPGLVRLFV- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33468931 283 EWLRpeDLPIKYAGLSTCFRQEvgshgRDTRGIFRVHQFEKIEQFVYSSPHDNKSWemFDEMIATAEEFYQSLGIPYHIV 362
Cdd:cd00768 69 SHIR--KLPLRLAEIGPAFRNE-----GGRRGLRRVREFTQLEGEVFGEDGEEASE--FEELIELTEELLRALGIKLDIV 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 33468931 363 NIVS--GSL-NHAASKKLDLEAWFPgSGAFRELVSCSNCTDYQARRLRIRY 410
Cdd:cd00768 140 FVEKtpGEFsPGGAGPGFEIEVDHP-EGRGLEIGSGGYRQDEQARAADLYF 189
|
|
| PRK04173 |
PRK04173 |
glycyl-tRNA synthetase; Provisional |
314-401 |
1.09e-04 |
|
glycyl-tRNA synthetase; Provisional
Pssm-ID: 235240 [Multi-domain] Cd Length: 456 Bit Score: 44.73 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33468931 314 GIFRVHQFEK--IEQFVYssPHDNKSWemFDEMIATAEEFYQSLGIP---YHIVNIVSGSLNHAASKKLDLEAWFPGSGA 388
Cdd:PRK04173 205 FIFRTREFEQmeLEFFVK--PGTDNEW--FAYWIELRKNWLLDLGIDpenLRFREHLPEELAHYSKATWDIEYKFPFGRF 280
|
90
....*....|...
gi 33468931 389 FRELVSCSNCTDY 401
Cdd:PRK04173 281 WGELEGIANRTDY 293
|
|
| PRK14894 |
PRK14894 |
glycyl-tRNA synthetase; Provisional |
268-401 |
1.39e-03 |
|
glycyl-tRNA synthetase; Provisional
Pssm-ID: 237851 [Multi-domain] Cd Length: 539 Bit Score: 41.53 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33468931 268 LIATSEQPIAALHRDEWLRPE------------------DLPIKYAGLSTCFRQEVGSHGRdtrgIFRVHQFEKIEQFVY 329
Cdd:PRK14894 124 MFRTQIGPVADSDSFAYLRPEtaqgifvnfanvlatsarKLPFGIAQVGKAFRNEINPRNF----LFRVREFEQMEIEYF 199
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 33468931 330 SSPHDNKSWEM--FDEMIAtaeeFYQSLGIP---YHIVNIVSGSLNHAASKKLDLEAWFPGSGaFRELVSCSNCTDY 401
Cdd:PRK14894 200 VMPGTDEEWHQrwLEARLA----WWEQIGIPrsrITIYDVPPDELAHYSKRTFDLMYDYPNIG-VQEIEGIANRTDY 271
|
|
|