|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02678 |
PLN02678 |
seryl-tRNA synthetase |
3-486 |
0e+00 |
|
seryl-tRNA synthetase
Pssm-ID: 215364 [Multi-domain] Cd Length: 448 Bit Score: 642.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306548 3 LDLDLFRVDKGGDPALIRETQEKRFKDPGLVDQLVKADSEWRRCRFRADNLNKLKNLCSKTIGEKMKKKEPvgddesvpe 82
Cdd:PLN02678 2 LDINLFREEKGGDPELIRESQRRRFASVELVDEVIALDKEWRQRQFELDSLRKEFNKLNKEVAKLKIAKED--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306548 83 nvlsfddlTADALANLKVsqikkvrllIDEAILKCDAERIKLEAERFENLREIGNLLHPSVPISNDEDvDNKVERIWGDC 162
Cdd:PLN02678 73 --------ATELIAETKE---------LKKEITEKEAEVQEAKAALDAKLKTIGNLVHDSVPVSNDEA-NNAVVRTWGEK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306548 163 TVRKK-YSHVDLVVMVDGFEGEKGAVVAGSRGYFLKGVLVFLEQALIQYALRTLGSRGYIPIYTPFFMRKEVMQEVAQLS 241
Cdd:PLN02678 135 RQEPKlKNHVDLVELLGIVDTERGADVAGGRGYYLKGAGVLLNQALINFGLAFLRKRGYTPLQTPFFMRKDVMAKCAQLA 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306548 242 QFDEELYKVIGKGseksddnsyDEKYLIATSEQPIAALHRDEWLRPEDLPIKYAGLSTCFRQEVGSHGRDTRGIFRVHQF 321
Cdd:PLN02678 215 QFDEELYKVTGEG---------DDKYLIATSEQPLCAYHRGDWIDPKELPIRYAGYSTCFRKEAGSHGRDTLGIFRVHQF 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306548 322 EKIEQFVYSSPHDNKSWEMFEEMITTAEEFYQSLGIPYHIVNIVSGSLNHAASKKLDLEAWFPGSGAFRELVSCSNCTDY 401
Cdd:PLN02678 286 EKVEQFCITSPNGNESWEMHEEMLKNSEDFYQSLGIPYQVVSIVSGALNDAAAKKYDLEAWFPASKTYRELVSCSNCTDY 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306548 402 QARRLRIRYGQTKKMMDKVEFVHMLNATMCATTRTICAILENYQTEKGITVPEKLKEFMppGLQELIPFVKPAPIEQEPS 481
Cdd:PLN02678 366 QSRRLEIRYGQKKSNEQTKQYVHLLNSTLTATERTLCCILENYQTEDGVRVPEVLQPFM--GGIEFLPFKKKPPAKGKGK 443
|
....*
gi 16306548 482 KKQKK 486
Cdd:PLN02678 444 KKKKK 448
|
|
| SerRS_core |
cd00770 |
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the ... |
152-460 |
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: 525.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306548 152 DNKVERIWGDCTV--RKKYSHVDLVVMVDGFEGEKGAVVAGSRGYFLKGVLVFLEQALIQYALRTLGSRGYIPIYTPFFM 229
Cdd:cd00770 1 DNVEIRRWGEPRVfdFKPKDHVELGEKLDILDFERGAKVSGSRFYYLKGDGALLERALINFALDFLTKRGFTPVIPPFLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306548 230 RKEVMQEVAQLSQFDEELYKVIGkgseksddnsyDEKYLIATSEQPIAALHRDEWLRPEDLPIKYAGLSTCFRQEVGSHG 309
Cdd:cd00770 81 RKEVMEGTGQLPKFDEQLYKVEG-----------EDLYLIATAEVPLAALHRDEILEEEELPLKYAGYSPCFRKEAGSAG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306548 310 RDTRGIFRVHQFEKIEQFVYSSPhdNKSWEMFEEMITTAEEFYQSLGIPYHIVNIVSGSLNHAASKKLDLEAWFPGSGAF 389
Cdd:cd00770 150 RDTRGLFRVHQFEKVEQFVFTKP--EESWEELEELISNAEEILQELGLPYRVVNICTGDLGFAAAKKYDIEAWMPGQGKY 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16306548 390 RELVSCSNCTDYQARRLRIRYGQTKKMmdKVEFVHMLNATMCATTRTICAILENYQTEKG-ITVPEKLKEFM 460
Cdd:cd00770 228 REISSCSNCTDFQARRLNIRYRDKKDG--KKQYVHTLNGTALATPRTIVAILENYQTEDGsVVIPEVLRPYM 297
|
|
| SerS |
COG0172 |
Seryl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Seryl-tRNA synthetase ... |
3-469 |
2.38e-160 |
|
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: 461.78 E-value: 2.38e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306548 3 LDLDLFRvdkgGDPALIRETQEKRFKDPgLVDQLVKADSEWRRCRFRADNLNKLKNLCSKTIGEKMKKKEPvgddesvpe 82
Cdd:COG0172 2 LDIKLIR----ENPEAVKEALAKRGFDL-DVDELLELDEERRELQTEVEELRAERNALSKEIGKAKKKGEE--------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306548 83 nvlsfddltADALanlkvsqIKKVRLLIDEaILKCDAERIKLEAERFENLREIGNLLHPSVPISNDEDvDNKVERIWG-- 160
Cdd:COG0172 68 ---------AEAL-------IAEVKELKEE-IKELEEELKELEEELDELLLSIPNLPHESVPVGKDES-DNVEVRRWGep 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306548 161 ---DCTVRkkySHVDLVVMVDGFEGEKGAVVAGSRGYFLKGVLVFLEQALIQYALRTLGSRGYIPIYTPFFMRKEVMQEV 237
Cdd:COG0172 130 refDFEPK---DHWELGEKLGILDFERAAKVSGSRFYVLKGDGARLERALIQFMLDLHTEHGYTEVIPPYLVNEESMYGT 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306548 238 AQLSQFDEELYKVIGkgseksddnsyDEKYLIATSEQPIAALHRDEWLRPEDLPIKYAGLSTCFRQEVGSHGRDTRGIFR 317
Cdd:COG0172 207 GQLPKFEEDLYKIEG-----------DDLYLIPTAEVPLTNLHRDEILDEEDLPLRYTAYTPCFRREAGSYGRDTRGLIR 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306548 318 VHQFEKIEQFVYSSPHDnkSWEMFEEMITTAEEFYQSLGIPYHIVNIVSGSLNHAASKKLDLEAWFPGSGAFRELVSCSN 397
Cdd:COG0172 276 QHQFDKVEMVQFVKPED--SYEELEELTAHAEEILQKLGLPYRVVLLCTGDLGFSAAKTYDLEVWLPGQNKYREISSCSN 353
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16306548 398 CTDYQARRLRIRYGQTKKmmdKVEFVHMLNATMCATTRTICAILENYQTEKG-ITVPEKLKEFMppGLQELIP 469
Cdd:COG0172 354 CTDFQARRLNIRYRDEDG---KPEFVHTLNGSGLAVGRTLVAILENYQQADGsVRIPEVLRPYM--GGLEVIE 421
|
|
| serS |
TIGR00414 |
seryl-tRNA synthetase; This model represents the seryl-tRNA synthetase found in most organisms. ... |
7-460 |
8.71e-142 |
|
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: 414.45 E-value: 8.71e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306548 7 LFRVDKGGDPALIRETQEKR---FKDPglVDQLVKADSEWRRCRFRADNLNKLKNLCSKTIGEKMKKKEpvgddesvpen 83
Cdd:TIGR00414 2 LDRKLLRNNPDLVKESLKARglsVDID--LEKLIALDDERKKLLSEIEELQAKRNELSKQIGKAKGQKK----------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306548 84 vlsfdDLTADALAnlkvsQIKKVRLLIDEAilkcDAERIKLEAERFENLREIGNLLHPSVPISNDEDvDNKVERIWGDCT 163
Cdd:TIGR00414 69 -----DKIEEIKK-----ELKELKEELTEL----SAALKALEAELQDKLLSIPNIPHESVPVGKDEE-DNLEVKRWGTPP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306548 164 VR--KKYSHVDLVVMVDGFEGEKGAVVAGSRGYFLKGVLVFLEQALIQYALRTLGSRGYIPIYTPFFMRKEVMQEVAQLS 241
Cdd:TIGR00414 134 VFdfKPKPHWELGEKLGGLDFDRAVKVTGSRFYYLKNDGAKLERALINFMLDLLEKNGYQEIYPPYLVNEESLDGTGQLP 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306548 242 QFDEELYKVIGkgseksddnsyDEKYLIATSEQPIAALHRDEWLRPEDLPIKYAGLSTCFRQEVGSHGRDTRGIFRVHQF 321
Cdd:TIGR00414 214 KFEEDIFKLED-----------TDLYLIPTAEVPLTNLHRNEILEEEELPIKYTAHSPCFRSEAGSYGKDTKGLIRVHQF 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306548 322 EKIEQFVYSSPhdNKSWEMFEEMITTAEEFYQSLGIPYHIVNIVSGSLNHAASKKLDLEAWFPGSGAFRELVSCSNCTDY 401
Cdd:TIGR00414 283 NKVELVKFCKP--EESAEELEEMTSDAEQILQELELPYRVVNLCSGDLGFSAAKKYDLEVWMPGQNTYREISSCSNCTDF 360
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306548 402 QARRLRIRYGQtkKMMDKVEFVHMLNATMCATTRTICAILENYQTEKG-ITVPEKLKEFM 460
Cdd:TIGR00414 361 QARRLNIRYKD--KNKGKNKYVHTLNGTALAIGRTIVAILENYQTEDGsVEIPEVLRKYL 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 ... |
258-444 |
3.60e-65 |
|
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: 209.19 E-value: 3.60e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306548 258 SDDNSyDEKYLIATSEQPIAALHRDEWLRPEDLPIKYAGLSTCFRQEVGshgRDTRGIFRVHQFEKIEQFVYSSPhdNKS 337
Cdd:pfam00587 4 EDENG-DELALKPTNEPGHTLLFREEGLRSKDLPLKLAQFGTCFRHEAS---GDTRGLIRVRQFHQDDAHIFHAP--GQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306548 338 WEMFEEMITTAEEFYQSLGIPYHIVNIVSGSLNHAASKKLDLEAWFPGSGAFRELVSCSNCTDYQARRLRIRYgqtKKMM 417
Cdd:pfam00587 78 PDELEDYIKLIDRVYSRLGLEVRVVRLSNSDGSAFYGPKLDFEVVFPSLGKQRQTGTIQNDGFRLPRRLGIRY---KDED 154
|
170 180
....*....|....*....|....*..
gi 16306548 418 DKVEFVHMLNATMCATTRTICAILENY 444
Cdd:pfam00587 155 NESKFPYMIHRAGLGVERFLAAILENN 181
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02678 |
PLN02678 |
seryl-tRNA synthetase |
3-486 |
0e+00 |
|
seryl-tRNA synthetase
Pssm-ID: 215364 [Multi-domain] Cd Length: 448 Bit Score: 642.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306548 3 LDLDLFRVDKGGDPALIRETQEKRFKDPGLVDQLVKADSEWRRCRFRADNLNKLKNLCSKTIGEKMKKKEPvgddesvpe 82
Cdd:PLN02678 2 LDINLFREEKGGDPELIRESQRRRFASVELVDEVIALDKEWRQRQFELDSLRKEFNKLNKEVAKLKIAKED--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306548 83 nvlsfddlTADALANLKVsqikkvrllIDEAILKCDAERIKLEAERFENLREIGNLLHPSVPISNDEDvDNKVERIWGDC 162
Cdd:PLN02678 73 --------ATELIAETKE---------LKKEITEKEAEVQEAKAALDAKLKTIGNLVHDSVPVSNDEA-NNAVVRTWGEK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306548 163 TVRKK-YSHVDLVVMVDGFEGEKGAVVAGSRGYFLKGVLVFLEQALIQYALRTLGSRGYIPIYTPFFMRKEVMQEVAQLS 241
Cdd:PLN02678 135 RQEPKlKNHVDLVELLGIVDTERGADVAGGRGYYLKGAGVLLNQALINFGLAFLRKRGYTPLQTPFFMRKDVMAKCAQLA 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306548 242 QFDEELYKVIGKGseksddnsyDEKYLIATSEQPIAALHRDEWLRPEDLPIKYAGLSTCFRQEVGSHGRDTRGIFRVHQF 321
Cdd:PLN02678 215 QFDEELYKVTGEG---------DDKYLIATSEQPLCAYHRGDWIDPKELPIRYAGYSTCFRKEAGSHGRDTLGIFRVHQF 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306548 322 EKIEQFVYSSPHDNKSWEMFEEMITTAEEFYQSLGIPYHIVNIVSGSLNHAASKKLDLEAWFPGSGAFRELVSCSNCTDY 401
Cdd:PLN02678 286 EKVEQFCITSPNGNESWEMHEEMLKNSEDFYQSLGIPYQVVSIVSGALNDAAAKKYDLEAWFPASKTYRELVSCSNCTDY 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306548 402 QARRLRIRYGQTKKMMDKVEFVHMLNATMCATTRTICAILENYQTEKGITVPEKLKEFMppGLQELIPFVKPAPIEQEPS 481
Cdd:PLN02678 366 QSRRLEIRYGQKKSNEQTKQYVHLLNSTLTATERTLCCILENYQTEDGVRVPEVLQPFM--GGIEFLPFKKKPPAKGKGK 443
|
....*
gi 16306548 482 KKQKK 486
Cdd:PLN02678 444 KKKKK 448
|
|
| SerRS_core |
cd00770 |
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the ... |
152-460 |
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: 525.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306548 152 DNKVERIWGDCTV--RKKYSHVDLVVMVDGFEGEKGAVVAGSRGYFLKGVLVFLEQALIQYALRTLGSRGYIPIYTPFFM 229
Cdd:cd00770 1 DNVEIRRWGEPRVfdFKPKDHVELGEKLDILDFERGAKVSGSRFYYLKGDGALLERALINFALDFLTKRGFTPVIPPFLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306548 230 RKEVMQEVAQLSQFDEELYKVIGkgseksddnsyDEKYLIATSEQPIAALHRDEWLRPEDLPIKYAGLSTCFRQEVGSHG 309
Cdd:cd00770 81 RKEVMEGTGQLPKFDEQLYKVEG-----------EDLYLIATAEVPLAALHRDEILEEEELPLKYAGYSPCFRKEAGSAG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306548 310 RDTRGIFRVHQFEKIEQFVYSSPhdNKSWEMFEEMITTAEEFYQSLGIPYHIVNIVSGSLNHAASKKLDLEAWFPGSGAF 389
Cdd:cd00770 150 RDTRGLFRVHQFEKVEQFVFTKP--EESWEELEELISNAEEILQELGLPYRVVNICTGDLGFAAAKKYDIEAWMPGQGKY 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16306548 390 RELVSCSNCTDYQARRLRIRYGQTKKMmdKVEFVHMLNATMCATTRTICAILENYQTEKG-ITVPEKLKEFM 460
Cdd:cd00770 228 REISSCSNCTDFQARRLNIRYRDKKDG--KKQYVHTLNGTALATPRTIVAILENYQTEDGsVVIPEVLRPYM 297
|
|
| SerS |
COG0172 |
Seryl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Seryl-tRNA synthetase ... |
3-469 |
2.38e-160 |
|
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: 461.78 E-value: 2.38e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306548 3 LDLDLFRvdkgGDPALIRETQEKRFKDPgLVDQLVKADSEWRRCRFRADNLNKLKNLCSKTIGEKMKKKEPvgddesvpe 82
Cdd:COG0172 2 LDIKLIR----ENPEAVKEALAKRGFDL-DVDELLELDEERRELQTEVEELRAERNALSKEIGKAKKKGEE--------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306548 83 nvlsfddltADALanlkvsqIKKVRLLIDEaILKCDAERIKLEAERFENLREIGNLLHPSVPISNDEDvDNKVERIWG-- 160
Cdd:COG0172 68 ---------AEAL-------IAEVKELKEE-IKELEEELKELEEELDELLLSIPNLPHESVPVGKDES-DNVEVRRWGep 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306548 161 ---DCTVRkkySHVDLVVMVDGFEGEKGAVVAGSRGYFLKGVLVFLEQALIQYALRTLGSRGYIPIYTPFFMRKEVMQEV 237
Cdd:COG0172 130 refDFEPK---DHWELGEKLGILDFERAAKVSGSRFYVLKGDGARLERALIQFMLDLHTEHGYTEVIPPYLVNEESMYGT 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306548 238 AQLSQFDEELYKVIGkgseksddnsyDEKYLIATSEQPIAALHRDEWLRPEDLPIKYAGLSTCFRQEVGSHGRDTRGIFR 317
Cdd:COG0172 207 GQLPKFEEDLYKIEG-----------DDLYLIPTAEVPLTNLHRDEILDEEDLPLRYTAYTPCFRREAGSYGRDTRGLIR 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306548 318 VHQFEKIEQFVYSSPHDnkSWEMFEEMITTAEEFYQSLGIPYHIVNIVSGSLNHAASKKLDLEAWFPGSGAFRELVSCSN 397
Cdd:COG0172 276 QHQFDKVEMVQFVKPED--SYEELEELTAHAEEILQKLGLPYRVVLLCTGDLGFSAAKTYDLEVWLPGQNKYREISSCSN 353
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16306548 398 CTDYQARRLRIRYGQTKKmmdKVEFVHMLNATMCATTRTICAILENYQTEKG-ITVPEKLKEFMppGLQELIP 469
Cdd:COG0172 354 CTDFQARRLNIRYRDEDG---KPEFVHTLNGSGLAVGRTLVAILENYQQADGsVRIPEVLRPYM--GGLEVIE 421
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
3-469 |
1.87e-158 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 457.22 E-value: 1.87e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306548 3 LDLDLFRvdkgGDPALIRETQEKRFkDPGLVDQLVKADSEWRRCRFRADNLNKLKNLCSKTIGEKMKKKEPvgddesvpe 82
Cdd:PRK05431 2 LDIKLIR----ENPEAVKEALAKRG-FPLDVDELLELDEERRELQTELEELQAERNALSKEIGQAKRKGED--------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306548 83 nvlsfddltADALanlkvsqIKKVRLLIDEaILKCDAERIKLEAERFENLREIGNLLHPSVPISNDEDvDNKVERIWG-- 160
Cdd:PRK05431 68 ---------AEAL-------IAEVKELKEE-IKALEAELDELEAELEELLLRIPNLPHDSVPVGKDED-DNVEVRRWGep 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306548 161 ---DCTVRkkySHVDLVVMVDGFEGEKGAVVAGSRGYFLKGVLVFLEQALIQYALRTL-GSRGYIPIYTPFFMRKEVMQE 236
Cdd:PRK05431 130 refDFEPK---DHWELGEKLGILDFERAAKVSGSRFYVLKGDGARLERALIQFMLDLHtEEHGYTEVIPPYLVNEESMYG 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306548 237 VAQLSQFDEELYKVIGkgseksddnsyDEKYLIATSEQPIAALHRDEWLRPEDLPIKYAGLSTCFRQEVGSHGRDTRGIF 316
Cdd:PRK05431 207 TGQLPKFEEDLYKIED-----------DDLYLIPTAEVPLTNLHRDEILDEEELPLKYTAYSPCFRSEAGSAGRDTRGLI 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306548 317 RVHQFEKIEQFVYSSPHDnkSWEMFEEMITTAEEFYQSLGIPYHIVNIVSGSLNHAASKKLDLEAWFPGSGAFRELVSCS 396
Cdd:PRK05431 276 RVHQFDKVELVKFTKPED--SYAELEELTANAEEILQKLELPYRVVLLCTGDLGFSAAKTYDLEVWLPSQNTYREISSCS 353
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16306548 397 NCTDYQARRLRIRYgqTKKMMDKVEFVHMLNATMCATTRTICAILENYQTEKG-ITVPEKLKEFMppGLQELIP 469
Cdd:PRK05431 354 NCTDFQARRANIRY--RDEGDGKPELVHTLNGSGLAVGRTLVAILENYQQADGsVTIPEVLRPYM--GGLEVIP 423
|
|
| serS |
TIGR00414 |
seryl-tRNA synthetase; This model represents the seryl-tRNA synthetase found in most organisms. ... |
7-460 |
8.71e-142 |
|
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: 414.45 E-value: 8.71e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306548 7 LFRVDKGGDPALIRETQEKR---FKDPglVDQLVKADSEWRRCRFRADNLNKLKNLCSKTIGEKMKKKEpvgddesvpen 83
Cdd:TIGR00414 2 LDRKLLRNNPDLVKESLKARglsVDID--LEKLIALDDERKKLLSEIEELQAKRNELSKQIGKAKGQKK----------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306548 84 vlsfdDLTADALAnlkvsQIKKVRLLIDEAilkcDAERIKLEAERFENLREIGNLLHPSVPISNDEDvDNKVERIWGDCT 163
Cdd:TIGR00414 69 -----DKIEEIKK-----ELKELKEELTEL----SAALKALEAELQDKLLSIPNIPHESVPVGKDEE-DNLEVKRWGTPP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306548 164 VR--KKYSHVDLVVMVDGFEGEKGAVVAGSRGYFLKGVLVFLEQALIQYALRTLGSRGYIPIYTPFFMRKEVMQEVAQLS 241
Cdd:TIGR00414 134 VFdfKPKPHWELGEKLGGLDFDRAVKVTGSRFYYLKNDGAKLERALINFMLDLLEKNGYQEIYPPYLVNEESLDGTGQLP 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306548 242 QFDEELYKVIGkgseksddnsyDEKYLIATSEQPIAALHRDEWLRPEDLPIKYAGLSTCFRQEVGSHGRDTRGIFRVHQF 321
Cdd:TIGR00414 214 KFEEDIFKLED-----------TDLYLIPTAEVPLTNLHRNEILEEEELPIKYTAHSPCFRSEAGSYGKDTKGLIRVHQF 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306548 322 EKIEQFVYSSPhdNKSWEMFEEMITTAEEFYQSLGIPYHIVNIVSGSLNHAASKKLDLEAWFPGSGAFRELVSCSNCTDY 401
Cdd:TIGR00414 283 NKVELVKFCKP--EESAEELEEMTSDAEQILQELELPYRVVNLCSGDLGFSAAKKYDLEVWMPGQNTYREISSCSNCTDF 360
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306548 402 QARRLRIRYGQtkKMMDKVEFVHMLNATMCATTRTICAILENYQTEKG-ITVPEKLKEFM 460
Cdd:TIGR00414 361 QARRLNIRYKD--KNKGKNKYVHTLNGTALAIGRTIVAILENYQTEDGsVEIPEVLRKYL 418
|
|
| PLN02320 |
PLN02320 |
seryl-tRNA synthetase |
110-469 |
1.10e-75 |
|
seryl-tRNA synthetase
Pssm-ID: 177954 [Multi-domain] Cd Length: 502 Bit Score: 247.14 E-value: 1.10e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306548 110 IDEAILKCDAERIKLEAERFENLREIGNLLHPSVPISNDEDvdnkveriwgdCTVRKKY-----------SHVDLVVMVD 178
Cdd:PLN02320 142 LKEGLVTLEEDLVKLTDELQLEAQSIPNMTHPDVPVGGEDS-----------SAVRKEVgsprefsfpikDHLQLGKELD 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306548 179 GFEGEKGAVVAGSRGYFLKGVLVFLEQALIQYALRTLGSRGYIPIYTPFFMRKEVMQEVA-QLSQFDEELYKVigkgsEK 257
Cdd:PLN02320 211 LFDFDAAAEVSGSKFYYLKNEAVLLEMALVNWTLSEVMKKGFTPLTTPEIVRSSVVEKCGfQPRGDNTQVYSI-----DG 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306548 258 SDdnsydeKYLIATSEQPIAALHRDEWLRPEDLPIKYAGLSTCFRQEVGSHGRDTRGIFRVHQFEKIEQFVYSSPHDNKS 337
Cdd:PLN02320 286 SD------QCLIGTAEIPVGGIHMDSILLESALPLKYVAFSHCFRTEAGAAGAATRGLYRVHQFSKVEMFVICRPEESES 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306548 338 WEmfEEMITTAEEFYQSLGIPYHIVNIVSGSLNHAASKKLDLEAWFPGSGAFRELVSCSNCTDYQARRLRIRY------- 410
Cdd:PLN02320 360 FH--EELIQIEEDLFTSLGLHFKTLDMATADLGAPAYRKFDIEAWMPGLGRYGEISSASNCTDYQSRRLGIRYrpseppq 437
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16306548 411 ---GQTKKMMDKVEFVHMLNATMCATTRTICAILENYQTEKG-ITVPEKLKEFMpPGLQELIP 469
Cdd:PLN02320 438 tnpKKGKGSLGPTKFVHTLNATACAVPRMIVCLLENYQQEDGsVVIPEPLRPFM-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 ... |
258-444 |
3.60e-65 |
|
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: 209.19 E-value: 3.60e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306548 258 SDDNSyDEKYLIATSEQPIAALHRDEWLRPEDLPIKYAGLSTCFRQEVGshgRDTRGIFRVHQFEKIEQFVYSSPhdNKS 337
Cdd:pfam00587 4 EDENG-DELALKPTNEPGHTLLFREEGLRSKDLPLKLAQFGTCFRHEAS---GDTRGLIRVRQFHQDDAHIFHAP--GQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306548 338 WEMFEEMITTAEEFYQSLGIPYHIVNIVSGSLNHAASKKLDLEAWFPGSGAFRELVSCSNCTDYQARRLRIRYgqtKKMM 417
Cdd:pfam00587 78 PDELEDYIKLIDRVYSRLGLEVRVVRLSNSDGSAFYGPKLDFEVVFPSLGKQRQTGTIQNDGFRLPRRLGIRY---KDED 154
|
170 180
....*....|....*....|....*..
gi 16306548 418 DKVEFVHMLNATMCATTRTICAILENY 444
Cdd:pfam00587 155 NESKFPYMIHRAGLGVERFLAAILENN 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 ... |
203-441 |
8.31e-23 |
|
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: 97.08 E-value: 8.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306548 203 LEQALIQYALRTLGSRGYIPIYTPFFMRKEVMQEVAQLSQFDEELYKVigkgSEKSDDNSYDEKYLIATSEQPIAALHRD 282
Cdd:cd00670 4 LWRALERFLDDRMAEYGYQEILFPFLAPTVLFFKGGHLDGYRKEMYTF----EDKGRELRDTDLVLRPAACEPIYQIFSG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306548 283 EWLRPEDLPIKYAGLSTCFRQEvgshGRDTRGIFRVHQFEKIEQFVYSSPHDNKSWemFEEMITTAEEFYQSLGIPYHIV 362
Cdd:cd00670 80 EILSYRALPLRLDQIGPCFRHE----PSGRRGLMRVREFRQVEYVVFGEPEEAEEE--RREWLELAEEIARELGLPVRVV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306548 363 NIVSGS--------LNHAASKKLDLEAWFPGSGAFRELVSCSNCTDYQARRLRIRYGQTkkmmDKVEFVHMLNATMcATT 434
Cdd:cd00670 154 VADDPFfgrggkrgLDAGRETVVEFELLLPLPGRAKETAVGSANVHLDHFGASFKIDED----GGGRAHTGCGGAG-GEE 228
|
....*..
gi 16306548 435 RTICAIL 441
Cdd:cd00670 229 RLVLALL 235
|
|
| Seryl_tRNA_N |
pfam02403 |
Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA ... |
2-72 |
2.29e-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: 77.63 E-value: 2.29e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16306548 2 VLDLDLFRVDkggdPALIRETQEKRFKDPGLVDQLVKADSEWRRCRFRADNLNKLKNLCSKTIGEKMKKKE 72
Cdd:pfam02403 1 MLDIKLIREN----PEAVKESLKKRGVDVLDVDELLELDEKRRELQVELEELQAERNELSKEIGQAKKKKE 67
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
203-430 |
1.23e-12 |
|
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: 67.14 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306548 203 LEQALIQYALRTLGSRGYIPIYTPFFMRKEVmqevaqLSQFDEELYKVIGKGSEKSDDnsydeKYLIATSEQPIAALHRd 282
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREPL------LEKAGHEPKDLLPVGAENEED-----LYLRPTLEPGLVRLFV- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306548 283 EWLRpeDLPIKYAGLSTCFRQEvgshgRDTRGIFRVHQFEKIEQFVYSSPHDNKSWemFEEMITTAEEFYQSLGIPYHIV 362
Cdd:cd00768 69 SHIR--KLPLRLAEIGPAFRNE-----GGRRGLRRVREFTQLEGEVFGEDGEEASE--FEELIELTEELLRALGIKLDIV 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16306548 363 NIVS--GSL-NHAASKKLDLEAWFPgSGAFRELVSCSNCTDYQARRLRIRYGQTKkmmDKVEFVHMLNATM 430
Cdd:cd00768 140 FVEKtpGEFsPGGAGPGFEIEVDHP-EGRGLEIGSGGYRQDEQARAADLYFLDEA---LEYRYPPTIGFGL 206
|
|
| PRK04173 |
PRK04173 |
glycyl-tRNA synthetase; Provisional |
314-401 |
2.28e-04 |
|
glycyl-tRNA synthetase; Provisional
Pssm-ID: 235240 [Multi-domain] Cd Length: 456 Bit Score: 43.58 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306548 314 GIFRVHQFEK--IEQFVYssPHDNKSWemFEEMITTAEEFYQSLGIP---YHIVNIVSGSLNHAASKKLDLEAWFPGSGA 388
Cdd:PRK04173 205 FIFRTREFEQmeLEFFVK--PGTDNEW--FAYWIELRKNWLLDLGIDpenLRFREHLPEELAHYSKATWDIEYKFPFGRF 280
|
90
....*....|...
gi 16306548 389 FRELVSCSNCTDY 401
Cdd:PRK04173 281 WGELEGIANRTDY 293
|
|
| PRK14894 |
PRK14894 |
glycyl-tRNA synthetase; Provisional |
268-401 |
7.27e-04 |
|
glycyl-tRNA synthetase; Provisional
Pssm-ID: 237851 [Multi-domain] Cd Length: 539 Bit Score: 42.30 E-value: 7.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306548 268 LIATSEQPIAALHRDEWLRPE------------------DLPIKYAGLSTCFRQEVGSHGRdtrgIFRVHQFEKIEQFVY 329
Cdd:PRK14894 124 MFRTQIGPVADSDSFAYLRPEtaqgifvnfanvlatsarKLPFGIAQVGKAFRNEINPRNF----LFRVREFEQMEIEYF 199
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16306548 330 SSPHDNKSWEmfEEMITTAEEFYQSLGIP---YHIVNIVSGSLNHAASKKLDLEAWFPGSGaFRELVSCSNCTDY 401
Cdd:PRK14894 200 VMPGTDEEWH--QRWLEARLAWWEQIGIPrsrITIYDVPPDELAHYSKRTFDLMYDYPNIG-VQEIEGIANRTDY 271
|
|
| |
