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Conserved domains on  [gi|1061214056|ref|NP_001317598|]
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serine--tRNA ligase, cytoplasmic isoform b [Homo sapiens]

Protein Classification

serine--tRNA ligase( domain architecture ID 1002694)

serine--tRNA ligase catalyzes the attachment of serine to tRNA(Ser)

CATH:  3.30.930.10
EC:  6.1.1.11
Gene Ontology:  GO:0005524|GO:0004828
PubMed:  10447505

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN02678 super family cl33544
seryl-tRNA synthetase
3-508 0e+00

seryl-tRNA synthetase


The actual alignment was detected with superfamily member PLN02678:

Pssm-ID: 215364 [Multi-domain]  Cd Length: 448  Bit Score: 634.05  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056   3 LDLDLFRVDKGGDPALIRETQEKRFKDPGLVDQLVKADSEWRRCRFRADNLNKLKNLCSKTIGEKMKKKEPvgddesvpe 82
Cdd:PLN02678    2 LDINLFREEKGGDPELIRESQRRRFASVELVDEVIALDKEWRQRQFELDSLRKEFNKLNKEVAKLKIAKED--------- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056  83 nvlsfddlTADALANLKVsqikkvrllIDEAILKCDAERIKLEAERFENLREIGNLLHPSVPISNDEDvDNKVERIWGDC 162
Cdd:PLN02678   73 --------ATELIAETKE---------LKKEITEKEAEVQEAKAALDAKLKTIGNLVHDSVPVSNDEA-NNAVVRTWGEK 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056 163 TVRKK-YSHVDLVVMVDGFEGEKGAVVAGSRGYFLKGVLVFLEQALIQYALRTLGSRGYIPIYTPFFMRKEVMQEVAQLS 241
Cdd:PLN02678  135 RQEPKlKNHVDLVELLGIVDTERGADVAGGRGYYLKGAGVLLNQALINFGLAFLRKRGYTPLQTPFFMRKDVMAKCAQLA 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056 242 QFDEELYKVIGKGseksddnsyDEKYLIATSEQPIAALHRDEWLRPEDLPIKYAGLSTCFRQEVGSHGRDTRGIFRVHQF 321
Cdd:PLN02678  215 QFDEELYKVTGEG---------DDKYLIATSEQPLCAYHRGDWIDPKELPIRYAGYSTCFRKEAGSHGRDTLGIFRVHQF 285
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056 322 EKIEQFVYSSPHDNKSWEMFEEMITTAEEFYQSLGIPYHIVNIVSGSLNHAASKKLDLEAWFPGSGAFRELVSCSNCTDY 401
Cdd:PLN02678  286 EKVEQFCITSPNGNESWEMHEEMLKNSEDFYQSLGIPYQVVSIVSGALNDAAAKKYDLEAWFPASKTYRELVSCSNCTDY 365
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056 402 QARRLRIRYGQtKKMMDKRKNnlhlstqnkleaslfspkkveFVHMLNATMCATTRTICAILENYQTEKGITVPEKLKEF 481
Cdd:PLN02678  366 QSRRLEIRYGQ-KKSNEQTKQ---------------------YVHLLNSTLTATERTLCCILENYQTEDGVRVPEVLQPF 423
                         490       500
                  ....*....|....*....|....*..
gi 1061214056 482 MppGLQELIPFVKPAPIEQEPSKKQKK 508
Cdd:PLN02678  424 M--GGIEFLPFKKKPPAKGKGKKKKKK 448
 
Name Accession Description Interval E-value
PLN02678 PLN02678
seryl-tRNA synthetase
3-508 0e+00

seryl-tRNA synthetase


Pssm-ID: 215364 [Multi-domain]  Cd Length: 448  Bit Score: 634.05  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056   3 LDLDLFRVDKGGDPALIRETQEKRFKDPGLVDQLVKADSEWRRCRFRADNLNKLKNLCSKTIGEKMKKKEPvgddesvpe 82
Cdd:PLN02678    2 LDINLFREEKGGDPELIRESQRRRFASVELVDEVIALDKEWRQRQFELDSLRKEFNKLNKEVAKLKIAKED--------- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056  83 nvlsfddlTADALANLKVsqikkvrllIDEAILKCDAERIKLEAERFENLREIGNLLHPSVPISNDEDvDNKVERIWGDC 162
Cdd:PLN02678   73 --------ATELIAETKE---------LKKEITEKEAEVQEAKAALDAKLKTIGNLVHDSVPVSNDEA-NNAVVRTWGEK 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056 163 TVRKK-YSHVDLVVMVDGFEGEKGAVVAGSRGYFLKGVLVFLEQALIQYALRTLGSRGYIPIYTPFFMRKEVMQEVAQLS 241
Cdd:PLN02678  135 RQEPKlKNHVDLVELLGIVDTERGADVAGGRGYYLKGAGVLLNQALINFGLAFLRKRGYTPLQTPFFMRKDVMAKCAQLA 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056 242 QFDEELYKVIGKGseksddnsyDEKYLIATSEQPIAALHRDEWLRPEDLPIKYAGLSTCFRQEVGSHGRDTRGIFRVHQF 321
Cdd:PLN02678  215 QFDEELYKVTGEG---------DDKYLIATSEQPLCAYHRGDWIDPKELPIRYAGYSTCFRKEAGSHGRDTLGIFRVHQF 285
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056 322 EKIEQFVYSSPHDNKSWEMFEEMITTAEEFYQSLGIPYHIVNIVSGSLNHAASKKLDLEAWFPGSGAFRELVSCSNCTDY 401
Cdd:PLN02678  286 EKVEQFCITSPNGNESWEMHEEMLKNSEDFYQSLGIPYQVVSIVSGALNDAAAKKYDLEAWFPASKTYRELVSCSNCTDY 365
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056 402 QARRLRIRYGQtKKMMDKRKNnlhlstqnkleaslfspkkveFVHMLNATMCATTRTICAILENYQTEKGITVPEKLKEF 481
Cdd:PLN02678  366 QSRRLEIRYGQ-KKSNEQTKQ---------------------YVHLLNSTLTATERTLCCILENYQTEDGVRVPEVLQPF 423
                         490       500
                  ....*....|....*....|....*..
gi 1061214056 482 MppGLQELIPFVKPAPIEQEPSKKQKK 508
Cdd:PLN02678  424 M--GGIEFLPFKKKPPAKGKGKKKKKK 448
SerRS_core cd00770
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the ...
152-482 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: 518.27  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056 152 DNKVERIWGDCTV--RKKYSHVDLVVMVDGFEGEKGAVVAGSRGYFLKGVLVFLEQALIQYALRTLGSRGYIPIYTPFFM 229
Cdd:cd00770     1 DNVEIRRWGEPRVfdFKPKDHVELGEKLDILDFERGAKVSGSRFYYLKGDGALLERALINFALDFLTKRGFTPVIPPFLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056 230 RKEVMQEVAQLSQFDEELYKVIGkgseksddnsyDEKYLIATSEQPIAALHRDEWLRPEDLPIKYAGLSTCFRQEVGSHG 309
Cdd:cd00770    81 RKEVMEGTGQLPKFDEQLYKVEG-----------EDLYLIATAEVPLAALHRDEILEEEELPLKYAGYSPCFRKEAGSAG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056 310 RDTRGIFRVHQFEKIEQFVYSSPhdNKSWEMFEEMITTAEEFYQSLGIPYHIVNIVSGSLNHAASKKLDLEAWFPGSGAF 389
Cdd:cd00770   150 RDTRGLFRVHQFEKVEQFVFTKP--EESWEELEELISNAEEILQELGLPYRVVNICTGDLGFAAAKKYDIEAWMPGQGKY 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056 390 RELVSCSNCTDYQARRLRIRYGQTKKmmdkrknnlhlstqnkleaslfspKKVEFVHMLNATMCATTRTICAILENYQTE 469
Cdd:cd00770   228 REISSCSNCTDFQARRLNIRYRDKKD------------------------GKKQYVHTLNGTALATPRTIVAILENYQTE 283
                         330
                  ....*....|....
gi 1061214056 470 KG-ITVPEKLKEFM 482
Cdd:cd00770   284 DGsVVIPEVLRPYM 297
SerS COG0172
Seryl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Seryl-tRNA synthetase ...
3-491 6.93e-159

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: 459.08  E-value: 6.93e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056   3 LDLDLFRvdkgGDPALIRETQEKRFKDPgLVDQLVKADSEWRRCRFRADNLNKLKNLCSKTIGEKMKKKEPvgddesvpe 82
Cdd:COG0172     2 LDIKLIR----ENPEAVKEALAKRGFDL-DVDELLELDEERRELQTEVEELRAERNALSKEIGKAKKKGEE--------- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056  83 nvlsfddltADALanlkvsqIKKVRLLIDEaILKCDAERIKLEAERFENLREIGNLLHPSVPISNDEDvDNKVERIWG-- 160
Cdd:COG0172    68 ---------AEAL-------IAEVKELKEE-IKELEEELKELEEELDELLLSIPNLPHESVPVGKDES-DNVEVRRWGep 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056 161 ---DCTVRkkySHVDLVVMVDGFEGEKGAVVAGSRGYFLKGVLVFLEQALIQYALRTLGSRGYIPIYTPFFMRKEVMQEV 237
Cdd:COG0172   130 refDFEPK---DHWELGEKLGILDFERAAKVSGSRFYVLKGDGARLERALIQFMLDLHTEHGYTEVIPPYLVNEESMYGT 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056 238 AQLSQFDEELYKVIGkgseksddnsyDEKYLIATSEQPIAALHRDEWLRPEDLPIKYAGLSTCFRQEVGSHGRDTRGIFR 317
Cdd:COG0172   207 GQLPKFEEDLYKIEG-----------DDLYLIPTAEVPLTNLHRDEILDEEDLPLRYTAYTPCFRREAGSYGRDTRGLIR 275
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056 318 VHQFEKIEQFVYSSPHDnkSWEMFEEMITTAEEFYQSLGIPYHIVNIVSGSLNHAASKKLDLEAWFPGSGAFRELVSCSN 397
Cdd:COG0172   276 QHQFDKVEMVQFVKPED--SYEELEELTAHAEEILQKLGLPYRVVLLCTGDLGFSAAKTYDLEVWLPGQNKYREISSCSN 353
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056 398 CTDYQARRLRIRYgqtkkmmdKRKNnlhlstqnkleaslfspKKVEFVHMLNATMCATTRTICAILENYQTEKG-ITVPE 476
Cdd:COG0172   354 CTDFQARRLNIRY--------RDED-----------------GKPEFVHTLNGSGLAVGRTLVAILENYQQADGsVRIPE 408
                         490
                  ....*....|....*
gi 1061214056 477 KLKEFMppGLQELIP 491
Cdd:COG0172   409 VLRPYM--GGLEVIE 421
serS TIGR00414
seryl-tRNA synthetase; This model represents the seryl-tRNA synthetase found in most organisms. ...
7-482 1.01e-138

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: 407.52  E-value: 1.01e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056   7 LFRVDKGGDPALIRETQEKR---FKDPglVDQLVKADSEWRRCRFRADNLNKLKNLCSKTIGEKMKKKEpvgddesvpen 83
Cdd:TIGR00414   2 LDRKLLRNNPDLVKESLKARglsVDID--LEKLIALDDERKKLLSEIEELQAKRNELSKQIGKAKGQKK----------- 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056  84 vlsfdDLTADALAnlkvsQIKKVRLLIDEAilkcDAERIKLEAERFENLREIGNLLHPSVPISNDEDvDNKVERIWGDCT 163
Cdd:TIGR00414  69 -----DKIEEIKK-----ELKELKEELTEL----SAALKALEAELQDKLLSIPNIPHESVPVGKDEE-DNLEVKRWGTPP 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056 164 VR--KKYSHVDLVVMVDGFEGEKGAVVAGSRGYFLKGVLVFLEQALIQYALRTLGSRGYIPIYTPFFMRKEVMQEVAQLS 241
Cdd:TIGR00414 134 VFdfKPKPHWELGEKLGGLDFDRAVKVTGSRFYYLKNDGAKLERALINFMLDLLEKNGYQEIYPPYLVNEESLDGTGQLP 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056 242 QFDEELYKVIGkgseksddnsyDEKYLIATSEQPIAALHRDEWLRPEDLPIKYAGLSTCFRQEVGSHGRDTRGIFRVHQF 321
Cdd:TIGR00414 214 KFEEDIFKLED-----------TDLYLIPTAEVPLTNLHRNEILEEEELPIKYTAHSPCFRSEAGSYGKDTKGLIRVHQF 282
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056 322 EKIEQFVYSSPhdNKSWEMFEEMITTAEEFYQSLGIPYHIVNIVSGSLNHAASKKLDLEAWFPGSGAFRELVSCSNCTDY 401
Cdd:TIGR00414 283 NKVELVKFCKP--EESAEELEEMTSDAEQILQELELPYRVVNLCSGDLGFSAAKKYDLEVWMPGQNTYREISSCSNCTDF 360
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056 402 QARRLRIRYgqtkkmmdKRKNNlhlstqnkleaslfspKKVEFVHMLNATMCATTRTICAILENYQTEKG-ITVPEKLKE 480
Cdd:TIGR00414 361 QARRLNIRY--------KDKNK----------------GKNKYVHTLNGTALAIGRTIVAILENYQTEDGsVEIPEVLRK 416

                  ..
gi 1061214056 481 FM 482
Cdd:TIGR00414 417 YL 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 ...
258-466 1.69e-60

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: 197.63  E-value: 1.69e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056 258 SDDNSyDEKYLIATSEQPIAALHRDEWLRPEDLPIKYAGLSTCFRQEVGshgRDTRGIFRVHQFEKIEQFVYSSPhdNKS 337
Cdd:pfam00587   4 EDENG-DELALKPTNEPGHTLLFREEGLRSKDLPLKLAQFGTCFRHEAS---GDTRGLIRVRQFHQDDAHIFHAP--GQS 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056 338 WEMFEEMITTAEEFYQSLGIPYHIVNIVSGSLNHAASKKLDLEAWFPGSGAFRELVSCSNCTDYQARRLRIRYgqtKKMM 417
Cdd:pfam00587  78 PDELEDYIKLIDRVYSRLGLEVRVVRLSNSDGSAFYGPKLDFEVVFPSLGKQRQTGTIQNDGFRLPRRLGIRY---KDED 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1061214056 418 DKRKnnlhlstqnkleaslfspkkveFVHMLNATMCATTRTICAILENY 466
Cdd:pfam00587 155 NESK----------------------FPYMIHRAGLGVERFLAAILENN 181
 
Name Accession Description Interval E-value
PLN02678 PLN02678
seryl-tRNA synthetase
3-508 0e+00

seryl-tRNA synthetase


Pssm-ID: 215364 [Multi-domain]  Cd Length: 448  Bit Score: 634.05  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056   3 LDLDLFRVDKGGDPALIRETQEKRFKDPGLVDQLVKADSEWRRCRFRADNLNKLKNLCSKTIGEKMKKKEPvgddesvpe 82
Cdd:PLN02678    2 LDINLFREEKGGDPELIRESQRRRFASVELVDEVIALDKEWRQRQFELDSLRKEFNKLNKEVAKLKIAKED--------- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056  83 nvlsfddlTADALANLKVsqikkvrllIDEAILKCDAERIKLEAERFENLREIGNLLHPSVPISNDEDvDNKVERIWGDC 162
Cdd:PLN02678   73 --------ATELIAETKE---------LKKEITEKEAEVQEAKAALDAKLKTIGNLVHDSVPVSNDEA-NNAVVRTWGEK 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056 163 TVRKK-YSHVDLVVMVDGFEGEKGAVVAGSRGYFLKGVLVFLEQALIQYALRTLGSRGYIPIYTPFFMRKEVMQEVAQLS 241
Cdd:PLN02678  135 RQEPKlKNHVDLVELLGIVDTERGADVAGGRGYYLKGAGVLLNQALINFGLAFLRKRGYTPLQTPFFMRKDVMAKCAQLA 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056 242 QFDEELYKVIGKGseksddnsyDEKYLIATSEQPIAALHRDEWLRPEDLPIKYAGLSTCFRQEVGSHGRDTRGIFRVHQF 321
Cdd:PLN02678  215 QFDEELYKVTGEG---------DDKYLIATSEQPLCAYHRGDWIDPKELPIRYAGYSTCFRKEAGSHGRDTLGIFRVHQF 285
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056 322 EKIEQFVYSSPHDNKSWEMFEEMITTAEEFYQSLGIPYHIVNIVSGSLNHAASKKLDLEAWFPGSGAFRELVSCSNCTDY 401
Cdd:PLN02678  286 EKVEQFCITSPNGNESWEMHEEMLKNSEDFYQSLGIPYQVVSIVSGALNDAAAKKYDLEAWFPASKTYRELVSCSNCTDY 365
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056 402 QARRLRIRYGQtKKMMDKRKNnlhlstqnkleaslfspkkveFVHMLNATMCATTRTICAILENYQTEKGITVPEKLKEF 481
Cdd:PLN02678  366 QSRRLEIRYGQ-KKSNEQTKQ---------------------YVHLLNSTLTATERTLCCILENYQTEDGVRVPEVLQPF 423
                         490       500
                  ....*....|....*....|....*..
gi 1061214056 482 MppGLQELIPFVKPAPIEQEPSKKQKK 508
Cdd:PLN02678  424 M--GGIEFLPFKKKPPAKGKGKKKKKK 448
SerRS_core cd00770
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the ...
152-482 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: 518.27  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056 152 DNKVERIWGDCTV--RKKYSHVDLVVMVDGFEGEKGAVVAGSRGYFLKGVLVFLEQALIQYALRTLGSRGYIPIYTPFFM 229
Cdd:cd00770     1 DNVEIRRWGEPRVfdFKPKDHVELGEKLDILDFERGAKVSGSRFYYLKGDGALLERALINFALDFLTKRGFTPVIPPFLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056 230 RKEVMQEVAQLSQFDEELYKVIGkgseksddnsyDEKYLIATSEQPIAALHRDEWLRPEDLPIKYAGLSTCFRQEVGSHG 309
Cdd:cd00770    81 RKEVMEGTGQLPKFDEQLYKVEG-----------EDLYLIATAEVPLAALHRDEILEEEELPLKYAGYSPCFRKEAGSAG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056 310 RDTRGIFRVHQFEKIEQFVYSSPhdNKSWEMFEEMITTAEEFYQSLGIPYHIVNIVSGSLNHAASKKLDLEAWFPGSGAF 389
Cdd:cd00770   150 RDTRGLFRVHQFEKVEQFVFTKP--EESWEELEELISNAEEILQELGLPYRVVNICTGDLGFAAAKKYDIEAWMPGQGKY 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056 390 RELVSCSNCTDYQARRLRIRYGQTKKmmdkrknnlhlstqnkleaslfspKKVEFVHMLNATMCATTRTICAILENYQTE 469
Cdd:cd00770   228 REISSCSNCTDFQARRLNIRYRDKKD------------------------GKKQYVHTLNGTALATPRTIVAILENYQTE 283
                         330
                  ....*....|....
gi 1061214056 470 KG-ITVPEKLKEFM 482
Cdd:cd00770   284 DGsVVIPEVLRPYM 297
SerS COG0172
Seryl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Seryl-tRNA synthetase ...
3-491 6.93e-159

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: 459.08  E-value: 6.93e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056   3 LDLDLFRvdkgGDPALIRETQEKRFKDPgLVDQLVKADSEWRRCRFRADNLNKLKNLCSKTIGEKMKKKEPvgddesvpe 82
Cdd:COG0172     2 LDIKLIR----ENPEAVKEALAKRGFDL-DVDELLELDEERRELQTEVEELRAERNALSKEIGKAKKKGEE--------- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056  83 nvlsfddltADALanlkvsqIKKVRLLIDEaILKCDAERIKLEAERFENLREIGNLLHPSVPISNDEDvDNKVERIWG-- 160
Cdd:COG0172    68 ---------AEAL-------IAEVKELKEE-IKELEEELKELEEELDELLLSIPNLPHESVPVGKDES-DNVEVRRWGep 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056 161 ---DCTVRkkySHVDLVVMVDGFEGEKGAVVAGSRGYFLKGVLVFLEQALIQYALRTLGSRGYIPIYTPFFMRKEVMQEV 237
Cdd:COG0172   130 refDFEPK---DHWELGEKLGILDFERAAKVSGSRFYVLKGDGARLERALIQFMLDLHTEHGYTEVIPPYLVNEESMYGT 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056 238 AQLSQFDEELYKVIGkgseksddnsyDEKYLIATSEQPIAALHRDEWLRPEDLPIKYAGLSTCFRQEVGSHGRDTRGIFR 317
Cdd:COG0172   207 GQLPKFEEDLYKIEG-----------DDLYLIPTAEVPLTNLHRDEILDEEDLPLRYTAYTPCFRREAGSYGRDTRGLIR 275
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056 318 VHQFEKIEQFVYSSPHDnkSWEMFEEMITTAEEFYQSLGIPYHIVNIVSGSLNHAASKKLDLEAWFPGSGAFRELVSCSN 397
Cdd:COG0172   276 QHQFDKVEMVQFVKPED--SYEELEELTAHAEEILQKLGLPYRVVLLCTGDLGFSAAKTYDLEVWLPGQNKYREISSCSN 353
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056 398 CTDYQARRLRIRYgqtkkmmdKRKNnlhlstqnkleaslfspKKVEFVHMLNATMCATTRTICAILENYQTEKG-ITVPE 476
Cdd:COG0172   354 CTDFQARRLNIRY--------RDED-----------------GKPEFVHTLNGSGLAVGRTLVAILENYQQADGsVRIPE 408
                         490
                  ....*....|....*
gi 1061214056 477 KLKEFMppGLQELIP 491
Cdd:COG0172   409 VLRPYM--GGLEVIE 421
PRK05431 PRK05431
seryl-tRNA synthetase; Provisional
3-491 5.92e-157

seryl-tRNA synthetase; Provisional


Pssm-ID: 235461 [Multi-domain]  Cd Length: 425  Bit Score: 454.14  E-value: 5.92e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056   3 LDLDLFRvdkgGDPALIRETQEKRFkDPGLVDQLVKADSEWRRCRFRADNLNKLKNLCSKTIGEKMKKKEPvgddesvpe 82
Cdd:PRK05431    2 LDIKLIR----ENPEAVKEALAKRG-FPLDVDELLELDEERRELQTELEELQAERNALSKEIGQAKRKGED--------- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056  83 nvlsfddltADALanlkvsqIKKVRLLIDEaILKCDAERIKLEAERFENLREIGNLLHPSVPISNDEDvDNKVERIWG-- 160
Cdd:PRK05431   68 ---------AEAL-------IAEVKELKEE-IKALEAELDELEAELEELLLRIPNLPHDSVPVGKDED-DNVEVRRWGep 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056 161 ---DCTVRkkySHVDLVVMVDGFEGEKGAVVAGSRGYFLKGVLVFLEQALIQYALRTL-GSRGYIPIYTPFFMRKEVMQE 236
Cdd:PRK05431  130 refDFEPK---DHWELGEKLGILDFERAAKVSGSRFYVLKGDGARLERALIQFMLDLHtEEHGYTEVIPPYLVNEESMYG 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056 237 VAQLSQFDEELYKVIGkgseksddnsyDEKYLIATSEQPIAALHRDEWLRPEDLPIKYAGLSTCFRQEVGSHGRDTRGIF 316
Cdd:PRK05431  207 TGQLPKFEEDLYKIED-----------DDLYLIPTAEVPLTNLHRDEILDEEELPLKYTAYSPCFRSEAGSAGRDTRGLI 275
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056 317 RVHQFEKIEQFVYSSPHDnkSWEMFEEMITTAEEFYQSLGIPYHIVNIVSGSLNHAASKKLDLEAWFPGSGAFRELVSCS 396
Cdd:PRK05431  276 RVHQFDKVELVKFTKPED--SYAELEELTANAEEILQKLELPYRVVLLCTGDLGFSAAKTYDLEVWLPSQNTYREISSCS 353
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056 397 NCTDYQARRLRIRYgqtkkmmdKRKNNlhlstqnkleaslfspKKVEFVHMLNATMCATTRTICAILENYQTEKG-ITVP 475
Cdd:PRK05431  354 NCTDFQARRANIRY--------RDEGD----------------GKPELVHTLNGSGLAVGRTLVAILENYQQADGsVTIP 409
                         490
                  ....*....|....*.
gi 1061214056 476 EKLKEFMppGLQELIP 491
Cdd:PRK05431  410 EVLRPYM--GGLEVIP 423
serS TIGR00414
seryl-tRNA synthetase; This model represents the seryl-tRNA synthetase found in most organisms. ...
7-482 1.01e-138

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: 407.52  E-value: 1.01e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056   7 LFRVDKGGDPALIRETQEKR---FKDPglVDQLVKADSEWRRCRFRADNLNKLKNLCSKTIGEKMKKKEpvgddesvpen 83
Cdd:TIGR00414   2 LDRKLLRNNPDLVKESLKARglsVDID--LEKLIALDDERKKLLSEIEELQAKRNELSKQIGKAKGQKK----------- 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056  84 vlsfdDLTADALAnlkvsQIKKVRLLIDEAilkcDAERIKLEAERFENLREIGNLLHPSVPISNDEDvDNKVERIWGDCT 163
Cdd:TIGR00414  69 -----DKIEEIKK-----ELKELKEELTEL----SAALKALEAELQDKLLSIPNIPHESVPVGKDEE-DNLEVKRWGTPP 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056 164 VR--KKYSHVDLVVMVDGFEGEKGAVVAGSRGYFLKGVLVFLEQALIQYALRTLGSRGYIPIYTPFFMRKEVMQEVAQLS 241
Cdd:TIGR00414 134 VFdfKPKPHWELGEKLGGLDFDRAVKVTGSRFYYLKNDGAKLERALINFMLDLLEKNGYQEIYPPYLVNEESLDGTGQLP 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056 242 QFDEELYKVIGkgseksddnsyDEKYLIATSEQPIAALHRDEWLRPEDLPIKYAGLSTCFRQEVGSHGRDTRGIFRVHQF 321
Cdd:TIGR00414 214 KFEEDIFKLED-----------TDLYLIPTAEVPLTNLHRNEILEEEELPIKYTAHSPCFRSEAGSYGKDTKGLIRVHQF 282
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056 322 EKIEQFVYSSPhdNKSWEMFEEMITTAEEFYQSLGIPYHIVNIVSGSLNHAASKKLDLEAWFPGSGAFRELVSCSNCTDY 401
Cdd:TIGR00414 283 NKVELVKFCKP--EESAEELEEMTSDAEQILQELELPYRVVNLCSGDLGFSAAKKYDLEVWMPGQNTYREISSCSNCTDF 360
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056 402 QARRLRIRYgqtkkmmdKRKNNlhlstqnkleaslfspKKVEFVHMLNATMCATTRTICAILENYQTEKG-ITVPEKLKE 480
Cdd:TIGR00414 361 QARRLNIRY--------KDKNK----------------GKNKYVHTLNGTALAIGRTIVAILENYQTEDGsVEIPEVLRK 416

                  ..
gi 1061214056 481 FM 482
Cdd:TIGR00414 417 YL 418
PLN02320 PLN02320
seryl-tRNA synthetase
110-491 5.70e-75

seryl-tRNA synthetase


Pssm-ID: 177954 [Multi-domain]  Cd Length: 502  Bit Score: 245.99  E-value: 5.70e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056 110 IDEAILKCDAERIKLEAERFENLREIGNLLHPSVPISNDEDvdnkveriwgdCTVRKKY-----------SHVDLVVMVD 178
Cdd:PLN02320  142 LKEGLVTLEEDLVKLTDELQLEAQSIPNMTHPDVPVGGEDS-----------SAVRKEVgsprefsfpikDHLQLGKELD 210
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056 179 GFEGEKGAVVAGSRGYFLKGVLVFLEQALIQYALRTLGSRGYIPIYTPFFMRKEVMQEVA-QLSQFDEELYKVigkgsEK 257
Cdd:PLN02320  211 LFDFDAAAEVSGSKFYYLKNEAVLLEMALVNWTLSEVMKKGFTPLTTPEIVRSSVVEKCGfQPRGDNTQVYSI-----DG 285
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056 258 SDdnsydeKYLIATSEQPIAALHRDEWLRPEDLPIKYAGLSTCFRQEVGSHGRDTRGIFRVHQFEKIEQFVYSSPHDNKS 337
Cdd:PLN02320  286 SD------QCLIGTAEIPVGGIHMDSILLESALPLKYVAFSHCFRTEAGAAGAATRGLYRVHQFSKVEMFVICRPEESES 359
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056 338 WEmfEEMITTAEEFYQSLGIPYHIVNIVSGSLNHAASKKLDLEAWFPGSGAFRELVSCSNCTDYQARRLRIRYgqtkkmm 417
Cdd:PLN02320  360 FH--EELIQIEEDLFTSLGLHFKTLDMATADLGAPAYRKFDIEAWMPGLGRYGEISSASNCTDYQSRRLGIRY------- 430
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1061214056 418 dkRKNNLHLSTQNKLEASLfSPKKveFVHMLNATMCATTRTICAILENYQTEKG-ITVPEKLKEFMpPGLQELIP 491
Cdd:PLN02320  431 --RPSEPPQTNPKKGKGSL-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 ...
258-466 1.69e-60

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: 197.63  E-value: 1.69e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056 258 SDDNSyDEKYLIATSEQPIAALHRDEWLRPEDLPIKYAGLSTCFRQEVGshgRDTRGIFRVHQFEKIEQFVYSSPhdNKS 337
Cdd:pfam00587   4 EDENG-DELALKPTNEPGHTLLFREEGLRSKDLPLKLAQFGTCFRHEAS---GDTRGLIRVRQFHQDDAHIFHAP--GQS 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056 338 WEMFEEMITTAEEFYQSLGIPYHIVNIVSGSLNHAASKKLDLEAWFPGSGAFRELVSCSNCTDYQARRLRIRYgqtKKMM 417
Cdd:pfam00587  78 PDELEDYIKLIDRVYSRLGLEVRVVRLSNSDGSAFYGPKLDFEVVFPSLGKQRQTGTIQNDGFRLPRRLGIRY---KDED 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1061214056 418 DKRKnnlhlstqnkleaslfspkkveFVHMLNATMCATTRTICAILENY 466
Cdd:pfam00587 155 NESK----------------------FPYMIHRAGLGVERFLAAILENN 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 ...
203-415 6.06e-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: 94.77  E-value: 6.06e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056 203 LEQALIQYALRTLGSRGYIPIYTPFFMRKEVMQEVAQLSQFDEELYKVigkgSEKSDDNSYDEKYLIATSEQPIAALHRD 282
Cdd:cd00670     4 LWRALERFLDDRMAEYGYQEILFPFLAPTVLFFKGGHLDGYRKEMYTF----EDKGRELRDTDLVLRPAACEPIYQIFSG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056 283 EWLRPEDLPIKYAGLSTCFRQEvgshGRDTRGIFRVHQFEKIEQFVYSSPHDNKSWemFEEMITTAEEFYQSLGIPYHIV 362
Cdd:cd00670    80 EILSYRALPLRLDQIGPCFRHE----PSGRRGLMRVREFRQVEYVVFGEPEEAEEE--RREWLELAEEIARELGLPVRVV 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1061214056 363 NIVSGS--------LNHAASKKLDLEAWFPGSGAFRELVSCSNCTDYQARRLRIRYGQTKK 415
Cdd:cd00670   154 VADDPFfgrggkrgLDAGRETVVEFELLLPLPGRAKETAVGSANVHLDHFGASFKIDEDGG 214
Seryl_tRNA_N pfam02403
Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA ...
2-72 3.78e-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: 77.24  E-value: 3.78e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1061214056   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 ...
203-410 3.66e-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: 65.60  E-value: 3.66e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056 203 LEQALIQYALRTLGSRGYIPIYTPFFMRKEVmqevaqLSQFDEELYKVIGKGSEKSDDnsydeKYLIATSEQPIAALHRd 282
Cdd:cd00768     1 IRSKIEQKLRRFMAELGFQEVETPIVEREPL------LEKAGHEPKDLLPVGAENEED-----LYLRPTLEPGLVRLFV- 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056 283 EWLRpeDLPIKYAGLSTCFRQEvgshgRDTRGIFRVHQFEKIEQFVYSSPHDNKSWemFEEMITTAEEFYQSLGIPYHIV 362
Cdd:cd00768    69 SHIR--KLPLRLAEIGPAFRNE-----GGRRGLRRVREFTQLEGEVFGEDGEEASE--FEELIELTEELLRALGIKLDIV 139
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1061214056 363 NIVS--GSL-NHAASKKLDLEAWFPgSGAFRELVSCSNCTDYQARRLRIRY 410
Cdd:cd00768   140 FVEKtpGEFsPGGAGPGFEIEVDHP-EGRGLEIGSGGYRQDEQARAADLYF 189
PRK04173 PRK04173
glycyl-tRNA synthetase; Provisional
314-401 2.26e-04

glycyl-tRNA synthetase; Provisional


Pssm-ID: 235240 [Multi-domain]  Cd Length: 456  Bit Score: 43.58  E-value: 2.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056 314 GIFRVHQFEK--IEQFVYssPHDNKSWemFEEMITTAEEFYQSLGIP---YHIVNIVSGSLNHAASKKLDLEAWFPGSGA 388
Cdd:PRK04173  205 FIFRTREFEQmeLEFFVK--PGTDNEW--FAYWIELRKNWLLDLGIDpenLRFREHLPEELAHYSKATWDIEYKFPFGRF 280
                          90
                  ....*....|...
gi 1061214056 389 FRELVSCSNCTDY 401
Cdd:PRK04173  281 WGELEGIANRTDY 293
PRK14894 PRK14894
glycyl-tRNA synthetase; Provisional
268-401 7.71e-04

glycyl-tRNA synthetase; Provisional


Pssm-ID: 237851 [Multi-domain]  Cd Length: 539  Bit Score: 42.30  E-value: 7.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214056 268 LIATSEQPIAALHRDEWLRPE------------------DLPIKYAGLSTCFRQEVGSHGRdtrgIFRVHQFEKIEQFVY 329
Cdd:PRK14894  124 MFRTQIGPVADSDSFAYLRPEtaqgifvnfanvlatsarKLPFGIAQVGKAFRNEINPRNF----LFRVREFEQMEIEYF 199
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1061214056 330 SSPHDNKSWEmfEEMITTAEEFYQSLGIP---YHIVNIVSGSLNHAASKKLDLEAWFPGSGaFRELVSCSNCTDY 401
Cdd:PRK14894  200 VMPGTDEEWH--QRWLEARLAWWEQIGIPrsrITIYDVPPDELAHYSKRTFDLMYDYPNIG-VQEIEGIANRTDY 271
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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