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Conserved domains on  [gi|975087557|ref|XP_015267607|]
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PREDICTED: LOW QUALITY PROTEIN: serine--tRNA ligase, cytoplasmic [Gekko japonicus]

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
3-489 0e+00

seryl-tRNA synthetase


The actual alignment was detected with superfamily member PLN02678:

Pssm-ID: 215364 [Multi-domain]  Cd Length: 448  Bit Score: 632.89  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975087557   3 LDLDLFRADKGGDPALVRETQLKRFKDPALVDALVAADGAWRRCRFRADNLNKLKNLCSKTIGEKMKV*fidiidvidsd 82
Cdd:PLN02678   2 LDINLFREEKGGDPELIRESQRRRFASVELVDEVIALDKEWRQRQFELDSLRKEFNKLNKEVAKLKIAK----------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975087557  83 sllENlelcrlcsfvf*SLQVNQIKKIRLLIDEAILKCDEERLKLDAErfenLREIGNLLHPSVPISNDEDaDNKVERMW 162
Cdd:PLN02678  71 ---ED-----------ATELIAETKELKKEITEKEAEVQEAKAALDAK----LKTIGNLVHDSVPVSNDEA-NNAVVRTW 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975087557 163 GDCTVRKK-YSHVDLVVMVDGYEGEKGAIVAGSRGYFLKGPLVFLEQALIQYALQTLLSKGYTPVYTPFFMRKEVMQEVA 241
Cdd:PLN02678 132 GEKRQEPKlKNHVDLVELLGIVDTERGADVAGGRGYYLKGAGVLLNQALINFGLAFLRKRGYTPLQTPFFMRKDVMAKCA 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975087557 242 QLSQFDEELYKVIGKGseksddntiDEKYLIATSEQPIAALHRDEWLKPEDLPIKYAGLSTCFRQEVGSHGRDTRGIFRV 321
Cdd:PLN02678 212 QLAQFDEELYKVTGEG---------DDKYLIATSEQPLCAYHRGDWIDPKELPIRYAGYSTCFRKEAGSHGRDTLGIFRV 282
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975087557 322 HQFEKIEQFVYASPHDNKSWEMFDEMIAVAEEFYQSLGIPYHIVNIVSGSLNHAASKKLDLEAWFPGSGAFRELVSCSNC 401
Cdd:PLN02678 283 HQFEKVEQFCITSPNGNESWEMHEEMLKNSEDFYQSLGIPYQVVSIVSGALNDAAAKKYDLEAWFPASKTYRELVSCSNC 362
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975087557 402 TDYQARRLRIRYGQTKKMMDKVEFVHMLNATMCATTRAICAILENYQTEEGIAVPERLRSFMppGLKEMIKFVRPAPIDQ 481
Cdd:PLN02678 363 TDYQSRRLEIRYGQKKSNEQTKQYVHLLNSTLTATERTLCCILENYQTEDGVRVPEVLQPFM--GGIEFLPFKKKPPAKG 440

                 ....*...
gi 975087557 482 ELSKKQKK 489
Cdd:PLN02678 441 KGKKKKKK 448
 
Name Accession Description Interval E-value
PLN02678 PLN02678
seryl-tRNA synthetase
3-489 0e+00

seryl-tRNA synthetase


Pssm-ID: 215364 [Multi-domain]  Cd Length: 448  Bit Score: 632.89  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975087557   3 LDLDLFRADKGGDPALVRETQLKRFKDPALVDALVAADGAWRRCRFRADNLNKLKNLCSKTIGEKMKV*fidiidvidsd 82
Cdd:PLN02678   2 LDINLFREEKGGDPELIRESQRRRFASVELVDEVIALDKEWRQRQFELDSLRKEFNKLNKEVAKLKIAK----------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975087557  83 sllENlelcrlcsfvf*SLQVNQIKKIRLLIDEAILKCDEERLKLDAErfenLREIGNLLHPSVPISNDEDaDNKVERMW 162
Cdd:PLN02678  71 ---ED-----------ATELIAETKELKKEITEKEAEVQEAKAALDAK----LKTIGNLVHDSVPVSNDEA-NNAVVRTW 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975087557 163 GDCTVRKK-YSHVDLVVMVDGYEGEKGAIVAGSRGYFLKGPLVFLEQALIQYALQTLLSKGYTPVYTPFFMRKEVMQEVA 241
Cdd:PLN02678 132 GEKRQEPKlKNHVDLVELLGIVDTERGADVAGGRGYYLKGAGVLLNQALINFGLAFLRKRGYTPLQTPFFMRKDVMAKCA 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975087557 242 QLSQFDEELYKVIGKGseksddntiDEKYLIATSEQPIAALHRDEWLKPEDLPIKYAGLSTCFRQEVGSHGRDTRGIFRV 321
Cdd:PLN02678 212 QLAQFDEELYKVTGEG---------DDKYLIATSEQPLCAYHRGDWIDPKELPIRYAGYSTCFRKEAGSHGRDTLGIFRV 282
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975087557 322 HQFEKIEQFVYASPHDNKSWEMFDEMIAVAEEFYQSLGIPYHIVNIVSGSLNHAASKKLDLEAWFPGSGAFRELVSCSNC 401
Cdd:PLN02678 283 HQFEKVEQFCITSPNGNESWEMHEEMLKNSEDFYQSLGIPYQVVSIVSGALNDAAAKKYDLEAWFPASKTYRELVSCSNC 362
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975087557 402 TDYQARRLRIRYGQTKKMMDKVEFVHMLNATMCATTRAICAILENYQTEEGIAVPERLRSFMppGLKEMIKFVRPAPIDQ 481
Cdd:PLN02678 363 TDYQSRRLEIRYGQKKSNEQTKQYVHLLNSTLTATERTLCCILENYQTEDGVRVPEVLQPFM--GGIEFLPFKKKPPAKG 440

                 ....*...
gi 975087557 482 ELSKKQKK 489
Cdd:PLN02678 441 KGKKKKKK 448
SerRS_core cd00770
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the ...
155-463 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: 523.28  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975087557 155 DNKVERMWGDCTV--RKKYSHVDLVVMVDGYEGEKGAIVAGSRGYFLKGPLVFLEQALIQYALQTLLSKGYTPVYTPFFM 232
Cdd:cd00770    1 DNVEIRRWGEPRVfdFKPKDHVELGEKLDILDFERGAKVSGSRFYYLKGDGALLERALINFALDFLTKRGFTPVIPPFLV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975087557 233 RKEVMQEVAQLSQFDEELYKVIGkgseksddntiDEKYLIATSEQPIAALHRDEWLKPEDLPIKYAGLSTCFRQEVGSHG 312
Cdd:cd00770   81 RKEVMEGTGQLPKFDEQLYKVEG-----------EDLYLIATAEVPLAALHRDEILEEEELPLKYAGYSPCFRKEAGSAG 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975087557 313 RDTRGIFRVHQFEKIEQFVYASPhdNKSWEMFDEMIAVAEEFYQSLGIPYHIVNIVSGSLNHAASKKLDLEAWFPGSGAF 392
Cdd:cd00770  150 RDTRGLFRVHQFEKVEQFVFTKP--EESWEELEELISNAEEILQELGLPYRVVNICTGDLGFAAAKKYDIEAWMPGQGKY 227
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 975087557 393 RELVSCSNCTDYQARRLRIRYGQTKKMmdKVEFVHMLNATMCATTRAICAILENYQTEEGIA-VPERLRSFM 463
Cdd:cd00770  228 REISSCSNCTDFQARRLNIRYRDKKDG--KKQYVHTLNGTALATPRTIVAILENYQTEDGSVvIPEVLRPYM 297
SerS COG0172
Seryl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Seryl-tRNA synthetase ...
3-472 2.88e-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: 2.88e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975087557   3 LDLDLFRADkggdPALVRETQLKRFKDPAlVDALVAADGAWRRCRFRADNLNKLKNLCSKTIGEKMKv*fidiiDVIDSD 82
Cdd:COG0172    2 LDIKLIREN----PEAVKEALAKRGFDLD-VDELLELDEERRELQTEVEELRAERNALSKEIGKAKK-------KGEEAE 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975087557  83 SLLEnlelcrlcsfvf*slQVNQIKKirlLIDEAilkcdEERLK-LDAERFENLREIGNLLHPSVPISNDEDaDNKVERM 161
Cdd:COG0172   70 ALIA---------------EVKELKE---EIKEL-----EEELKeLEEELDELLLSIPNLPHESVPVGKDES-DNVEVRR 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975087557 162 WG-----DCTVRkkySHVDLVVMVDGYEGEKGAIVAGSRGYFLKGPLVFLEQALIQYALQTLLSKGYTPVYTPFFMRKEV 236
Cdd:COG0172  126 WGeprefDFEPK---DHWELGEKLGILDFERAAKVSGSRFYVLKGDGARLERALIQFMLDLHTEHGYTEVIPPYLVNEES 202
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975087557 237 MQEVAQLSQFDEELYKVigkgseksddnTIDEKYLIATSEQPIAALHRDEWLKPEDLPIKYAGLSTCFRQEVGSHGRDTR 316
Cdd:COG0172  203 MYGTGQLPKFEEDLYKI-----------EGDDLYLIPTAEVPLTNLHRDEILDEEDLPLRYTAYTPCFRREAGSYGRDTR 271
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975087557 317 GIFRVHQFEKIEQFVYASPHDnkSWEMFDEMIAVAEEFYQSLGIPYHIVNIVSGSLNHAASKKLDLEAWFPGSGAFRELV 396
Cdd:COG0172  272 GLIRQHQFDKVEMVQFVKPED--SYEELEELTAHAEEILQKLGLPYRVVLLCTGDLGFSAAKTYDLEVWLPGQNKYREIS 349
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 975087557 397 SCSNCTDYQARRLRIRYGQTKKmmdKVEFVHMLNATMCATTRAICAILENYQTEEG-IAVPERLRSFMppGLKEMIK 472
Cdd:COG0172  350 SCSNCTDFQARRLNIRYRDEDG---KPEFVHTLNGSGLAVGRTLVAILENYQQADGsVRIPEVLRPYM--GGLEVIE 421
serS TIGR00414
seryl-tRNA synthetase; This model represents the seryl-tRNA synthetase found in most organisms. ...
7-463 1.29e-140

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: 411.76  E-value: 1.29e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975087557    7 LFRADKGGDPALVRETQLKR---FKDPalVDALVAADGAWRRCRFRADNLNKLKNLCSKTIGEKMKv*fidiidviDSDS 83
Cdd:TIGR00414   2 LDRKLLRNNPDLVKESLKARglsVDID--LEKLIALDDERKKLLSEIEELQAKRNELSKQIGKAKG----------QKKD 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975087557   84 LLENLELcrlcsfvf*slQVNQIKkirllidEAILKCDEERLKLDAERFENLREIGNLLHPSVPISNDEDaDNKVERMWG 163
Cdd:TIGR00414  70 KIEEIKK-----------ELKELK-------EELTELSAALKALEAELQDKLLSIPNIPHESVPVGKDEE-DNLEVKRWG 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975087557  164 DCTVR--KKYSHVDLVVMVDGYEGEKGAIVAGSRGYFLKGPLVFLEQALIQYALQTLLSKGYTPVYTPFFMRKEVMQEVA 241
Cdd:TIGR00414 131 TPPVFdfKPKPHWELGEKLGGLDFDRAVKVTGSRFYYLKNDGAKLERALINFMLDLLEKNGYQEIYPPYLVNEESLDGTG 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975087557  242 QLSQFDEELYKVIGkgseksddntiDEKYLIATSEQPIAALHRDEWLKPEDLPIKYAGLSTCFRQEVGSHGRDTRGIFRV 321
Cdd:TIGR00414 211 QLPKFEEDIFKLED-----------TDLYLIPTAEVPLTNLHRNEILEEEELPIKYTAHSPCFRSEAGSYGKDTKGLIRV 279
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975087557  322 HQFEKIEQFVYASPhdNKSWEMFDEMIAVAEEFYQSLGIPYHIVNIVSGSLNHAASKKLDLEAWFPGSGAFRELVSCSNC 401
Cdd:TIGR00414 280 HQFNKVELVKFCKP--EESAEELEEMTSDAEQILQELELPYRVVNLCSGDLGFSAAKKYDLEVWMPGQNTYREISSCSNC 357
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 975087557  402 TDYQARRLRIRYGQtkKMMDKVEFVHMLNATMCATTRAICAILENYQTEEG-IAVPERLRSFM 463
Cdd:TIGR00414 358 TDFQARRLNIRYKD--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 ...
260-447 1.15e-62

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: 202.64  E-value: 1.15e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975087557  260 KSDDNTIDEKYLIATSEQPIAALHRDEWLKPEDLPIKYAGLSTCFRQEVGshgRDTRGIFRVHQFEKIEQFVYASPhdNK 339
Cdd:pfam00587   2 KVEDENGDELALKPTNEPGHTLLFREEGLRSKDLPLKLAQFGTCFRHEAS---GDTRGLIRVRQFHQDDAHIFHAP--GQ 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975087557  340 SWEMFDEMIAVAEEFYQSLGIPYHIVNIVSGSLNHAASKKLDLEAWFPGSGAFRELVSCSNCTDYQARRLRIRYgqtKKM 419
Cdd:pfam00587  77 SPDELEDYIKLIDRVYSRLGLEVRVVRLSNSDGSAFYGPKLDFEVVFPSLGKQRQTGTIQNDGFRLPRRLGIRY---KDE 153
                         170       180
                  ....*....|....*....|....*...
gi 975087557  420 MDKVEFVHMLNATMCATTRAICAILENY 447
Cdd:pfam00587 154 DNESKFPYMIHRAGLGVERFLAAILENN 181
 
Name Accession Description Interval E-value
PLN02678 PLN02678
seryl-tRNA synthetase
3-489 0e+00

seryl-tRNA synthetase


Pssm-ID: 215364 [Multi-domain]  Cd Length: 448  Bit Score: 632.89  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975087557   3 LDLDLFRADKGGDPALVRETQLKRFKDPALVDALVAADGAWRRCRFRADNLNKLKNLCSKTIGEKMKV*fidiidvidsd 82
Cdd:PLN02678   2 LDINLFREEKGGDPELIRESQRRRFASVELVDEVIALDKEWRQRQFELDSLRKEFNKLNKEVAKLKIAK----------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975087557  83 sllENlelcrlcsfvf*SLQVNQIKKIRLLIDEAILKCDEERLKLDAErfenLREIGNLLHPSVPISNDEDaDNKVERMW 162
Cdd:PLN02678  71 ---ED-----------ATELIAETKELKKEITEKEAEVQEAKAALDAK----LKTIGNLVHDSVPVSNDEA-NNAVVRTW 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975087557 163 GDCTVRKK-YSHVDLVVMVDGYEGEKGAIVAGSRGYFLKGPLVFLEQALIQYALQTLLSKGYTPVYTPFFMRKEVMQEVA 241
Cdd:PLN02678 132 GEKRQEPKlKNHVDLVELLGIVDTERGADVAGGRGYYLKGAGVLLNQALINFGLAFLRKRGYTPLQTPFFMRKDVMAKCA 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975087557 242 QLSQFDEELYKVIGKGseksddntiDEKYLIATSEQPIAALHRDEWLKPEDLPIKYAGLSTCFRQEVGSHGRDTRGIFRV 321
Cdd:PLN02678 212 QLAQFDEELYKVTGEG---------DDKYLIATSEQPLCAYHRGDWIDPKELPIRYAGYSTCFRKEAGSHGRDTLGIFRV 282
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975087557 322 HQFEKIEQFVYASPHDNKSWEMFDEMIAVAEEFYQSLGIPYHIVNIVSGSLNHAASKKLDLEAWFPGSGAFRELVSCSNC 401
Cdd:PLN02678 283 HQFEKVEQFCITSPNGNESWEMHEEMLKNSEDFYQSLGIPYQVVSIVSGALNDAAAKKYDLEAWFPASKTYRELVSCSNC 362
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975087557 402 TDYQARRLRIRYGQTKKMMDKVEFVHMLNATMCATTRAICAILENYQTEEGIAVPERLRSFMppGLKEMIKFVRPAPIDQ 481
Cdd:PLN02678 363 TDYQSRRLEIRYGQKKSNEQTKQYVHLLNSTLTATERTLCCILENYQTEDGVRVPEVLQPFM--GGIEFLPFKKKPPAKG 440

                 ....*...
gi 975087557 482 ELSKKQKK 489
Cdd:PLN02678 441 KGKKKKKK 448
SerRS_core cd00770
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the ...
155-463 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: 523.28  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975087557 155 DNKVERMWGDCTV--RKKYSHVDLVVMVDGYEGEKGAIVAGSRGYFLKGPLVFLEQALIQYALQTLLSKGYTPVYTPFFM 232
Cdd:cd00770    1 DNVEIRRWGEPRVfdFKPKDHVELGEKLDILDFERGAKVSGSRFYYLKGDGALLERALINFALDFLTKRGFTPVIPPFLV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975087557 233 RKEVMQEVAQLSQFDEELYKVIGkgseksddntiDEKYLIATSEQPIAALHRDEWLKPEDLPIKYAGLSTCFRQEVGSHG 312
Cdd:cd00770   81 RKEVMEGTGQLPKFDEQLYKVEG-----------EDLYLIATAEVPLAALHRDEILEEEELPLKYAGYSPCFRKEAGSAG 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975087557 313 RDTRGIFRVHQFEKIEQFVYASPhdNKSWEMFDEMIAVAEEFYQSLGIPYHIVNIVSGSLNHAASKKLDLEAWFPGSGAF 392
Cdd:cd00770  150 RDTRGLFRVHQFEKVEQFVFTKP--EESWEELEELISNAEEILQELGLPYRVVNICTGDLGFAAAKKYDIEAWMPGQGKY 227
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 975087557 393 RELVSCSNCTDYQARRLRIRYGQTKKMmdKVEFVHMLNATMCATTRAICAILENYQTEEGIA-VPERLRSFM 463
Cdd:cd00770  228 REISSCSNCTDFQARRLNIRYRDKKDG--KKQYVHTLNGTALATPRTIVAILENYQTEDGSVvIPEVLRPYM 297
SerS COG0172
Seryl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Seryl-tRNA synthetase ...
3-472 2.88e-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: 2.88e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975087557   3 LDLDLFRADkggdPALVRETQLKRFKDPAlVDALVAADGAWRRCRFRADNLNKLKNLCSKTIGEKMKv*fidiiDVIDSD 82
Cdd:COG0172    2 LDIKLIREN----PEAVKEALAKRGFDLD-VDELLELDEERRELQTEVEELRAERNALSKEIGKAKK-------KGEEAE 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975087557  83 SLLEnlelcrlcsfvf*slQVNQIKKirlLIDEAilkcdEERLK-LDAERFENLREIGNLLHPSVPISNDEDaDNKVERM 161
Cdd:COG0172   70 ALIA---------------EVKELKE---EIKEL-----EEELKeLEEELDELLLSIPNLPHESVPVGKDES-DNVEVRR 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975087557 162 WG-----DCTVRkkySHVDLVVMVDGYEGEKGAIVAGSRGYFLKGPLVFLEQALIQYALQTLLSKGYTPVYTPFFMRKEV 236
Cdd:COG0172  126 WGeprefDFEPK---DHWELGEKLGILDFERAAKVSGSRFYVLKGDGARLERALIQFMLDLHTEHGYTEVIPPYLVNEES 202
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975087557 237 MQEVAQLSQFDEELYKVigkgseksddnTIDEKYLIATSEQPIAALHRDEWLKPEDLPIKYAGLSTCFRQEVGSHGRDTR 316
Cdd:COG0172  203 MYGTGQLPKFEEDLYKI-----------EGDDLYLIPTAEVPLTNLHRDEILDEEDLPLRYTAYTPCFRREAGSYGRDTR 271
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975087557 317 GIFRVHQFEKIEQFVYASPHDnkSWEMFDEMIAVAEEFYQSLGIPYHIVNIVSGSLNHAASKKLDLEAWFPGSGAFRELV 396
Cdd:COG0172  272 GLIRQHQFDKVEMVQFVKPED--SYEELEELTAHAEEILQKLGLPYRVVLLCTGDLGFSAAKTYDLEVWLPGQNKYREIS 349
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 975087557 397 SCSNCTDYQARRLRIRYGQTKKmmdKVEFVHMLNATMCATTRAICAILENYQTEEG-IAVPERLRSFMppGLKEMIK 472
Cdd:COG0172  350 SCSNCTDFQARRLNIRYRDEDG---KPEFVHTLNGSGLAVGRTLVAILENYQQADGsVRIPEVLRPYM--GGLEVIE 421
PRK05431 PRK05431
seryl-tRNA synthetase; Provisional
3-472 5.05e-157

seryl-tRNA synthetase; Provisional


Pssm-ID: 235461 [Multi-domain]  Cd Length: 425  Bit Score: 453.76  E-value: 5.05e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975087557   3 LDLDLFRADkggdPALVRETQLKRFkDPALVDALVAADGAWRRCRFRADNLNKLKNLCSKTIGEKMKv*fidiiDVIDSD 82
Cdd:PRK05431   2 LDIKLIREN----PEAVKEALAKRG-FPLDVDELLELDEERRELQTELEELQAERNALSKEIGQAKR-------KGEDAE 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975087557  83 SLLEnlelcrlcsfvf*slQVNQIKKirlLIDEAilkcdEERLK-LDAERFENLREIGNLLHPSVPISNDEDaDNKVERM 161
Cdd:PRK05431  70 ALIA---------------EVKELKE---EIKAL-----EAELDeLEAELEELLLRIPNLPHDSVPVGKDED-DNVEVRR 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975087557 162 WG-----DCTVRkkySHVDLVVMVDGYEGEKGAIVAGSRGYFLKGPLVFLEQALIQYALQTLLSK-GYTPVYTPFFMRKE 235
Cdd:PRK05431 126 WGeprefDFEPK---DHWELGEKLGILDFERAAKVSGSRFYVLKGDGARLERALIQFMLDLHTEEhGYTEVIPPYLVNEE 202
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975087557 236 VMQEVAQLSQFDEELYKVIGkgseksddntiDEKYLIATSEQPIAALHRDEWLKPEDLPIKYAGLSTCFRQEVGSHGRDT 315
Cdd:PRK05431 203 SMYGTGQLPKFEEDLYKIED-----------DDLYLIPTAEVPLTNLHRDEILDEEELPLKYTAYSPCFRSEAGSAGRDT 271
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975087557 316 RGIFRVHQFEKIEQFVYASPHDnkSWEMFDEMIAVAEEFYQSLGIPYHIVNIVSGSLNHAASKKLDLEAWFPGSGAFREL 395
Cdd:PRK05431 272 RGLIRVHQFDKVELVKFTKPED--SYAELEELTANAEEILQKLELPYRVVLLCTGDLGFSAAKTYDLEVWLPSQNTYREI 349
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 975087557 396 VSCSNCTDYQARRLRIRYgqTKKMMDKVEFVHMLNATMCATTRAICAILENYQTEEG-IAVPERLRSFMppGLKEMIK 472
Cdd:PRK05431 350 SSCSNCTDFQARRANIRY--RDEGDGKPELVHTLNGSGLAVGRTLVAILENYQQADGsVTIPEVLRPYM--GGLEVIP 423
serS TIGR00414
seryl-tRNA synthetase; This model represents the seryl-tRNA synthetase found in most organisms. ...
7-463 1.29e-140

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: 411.76  E-value: 1.29e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975087557    7 LFRADKGGDPALVRETQLKR---FKDPalVDALVAADGAWRRCRFRADNLNKLKNLCSKTIGEKMKv*fidiidviDSDS 83
Cdd:TIGR00414   2 LDRKLLRNNPDLVKESLKARglsVDID--LEKLIALDDERKKLLSEIEELQAKRNELSKQIGKAKG----------QKKD 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975087557   84 LLENLELcrlcsfvf*slQVNQIKkirllidEAILKCDEERLKLDAERFENLREIGNLLHPSVPISNDEDaDNKVERMWG 163
Cdd:TIGR00414  70 KIEEIKK-----------ELKELK-------EELTELSAALKALEAELQDKLLSIPNIPHESVPVGKDEE-DNLEVKRWG 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975087557  164 DCTVR--KKYSHVDLVVMVDGYEGEKGAIVAGSRGYFLKGPLVFLEQALIQYALQTLLSKGYTPVYTPFFMRKEVMQEVA 241
Cdd:TIGR00414 131 TPPVFdfKPKPHWELGEKLGGLDFDRAVKVTGSRFYYLKNDGAKLERALINFMLDLLEKNGYQEIYPPYLVNEESLDGTG 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975087557  242 QLSQFDEELYKVIGkgseksddntiDEKYLIATSEQPIAALHRDEWLKPEDLPIKYAGLSTCFRQEVGSHGRDTRGIFRV 321
Cdd:TIGR00414 211 QLPKFEEDIFKLED-----------TDLYLIPTAEVPLTNLHRNEILEEEELPIKYTAHSPCFRSEAGSYGKDTKGLIRV 279
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975087557  322 HQFEKIEQFVYASPhdNKSWEMFDEMIAVAEEFYQSLGIPYHIVNIVSGSLNHAASKKLDLEAWFPGSGAFRELVSCSNC 401
Cdd:TIGR00414 280 HQFNKVELVKFCKP--EESAEELEEMTSDAEQILQELELPYRVVNLCSGDLGFSAAKKYDLEVWMPGQNTYREISSCSNC 357
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 975087557  402 TDYQARRLRIRYGQtkKMMDKVEFVHMLNATMCATTRAICAILENYQTEEG-IAVPERLRSFM 463
Cdd:TIGR00414 358 TDFQARRLNIRYKD--KNKGKNKYVHTLNGTALAIGRTIVAILENYQTEDGsVEIPEVLRKYL 418
PLN02320 PLN02320
seryl-tRNA synthetase
113-472 3.17e-79

seryl-tRNA synthetase


Pssm-ID: 177954 [Multi-domain]  Cd Length: 502  Bit Score: 256.39  E-value: 3.17e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975087557 113 IDEAILKCDEERLKLDAERFENLREIGNLLHPSVPISNDEDAdnKVERMWG-----DCTVRkkySHVDLVVMVDGYEGEK 187
Cdd:PLN02320 142 LKEGLVTLEEDLVKLTDELQLEAQSIPNMTHPDVPVGGEDSS--AVRKEVGsprefSFPIK---DHLQLGKELDLFDFDA 216
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975087557 188 GAIVAGSRGYFLKGPLVFLEQALIQYALQTLLSKGYTPVYTPFFMRKEVMQEVA-QLSQFDEELYKVigkgsEKSDdnti 266
Cdd:PLN02320 217 AAEVSGSKFYYLKNEAVLLEMALVNWTLSEVMKKGFTPLTTPEIVRSSVVEKCGfQPRGDNTQVYSI-----DGSD---- 287
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975087557 267 deKYLIATSEQPIAALHRDEWLKPEDLPIKYAGLSTCFRQEVGSHGRDTRGIFRVHQFEKIEQFVYASPHDNKSWEmfDE 346
Cdd:PLN02320 288 --QCLIGTAEIPVGGIHMDSILLESALPLKYVAFSHCFRTEAGAAGAATRGLYRVHQFSKVEMFVICRPEESESFH--EE 363
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975087557 347 MIAVAEEFYQSLGIPYHIVNIVSGSLNHAASKKLDLEAWFPGSGAFRELVSCSNCTDYQARRLRIRY----------GQT 416
Cdd:PLN02320 364 LIQIEEDLFTSLGLHFKTLDMATADLGAPAYRKFDIEAWMPGLGRYGEISSASNCTDYQSRRLGIRYrpseppqtnpKKG 443
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 975087557 417 KKMMDKVEFVHMLNATMCATTRAICAILENYQTEEG-IAVPERLRSFMppGLKEMIK 472
Cdd:PLN02320 444 KGSLGPTKFVHTLNATACAVPRMIVCLLENYQQEDGsVVIPEPLRPFM--GGLELIK 498
tRNA-synt_2b pfam00587
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ...
260-447 1.15e-62

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: 202.64  E-value: 1.15e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975087557  260 KSDDNTIDEKYLIATSEQPIAALHRDEWLKPEDLPIKYAGLSTCFRQEVGshgRDTRGIFRVHQFEKIEQFVYASPhdNK 339
Cdd:pfam00587   2 KVEDENGDELALKPTNEPGHTLLFREEGLRSKDLPLKLAQFGTCFRHEAS---GDTRGLIRVRQFHQDDAHIFHAP--GQ 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975087557  340 SWEMFDEMIAVAEEFYQSLGIPYHIVNIVSGSLNHAASKKLDLEAWFPGSGAFRELVSCSNCTDYQARRLRIRYgqtKKM 419
Cdd:pfam00587  77 SPDELEDYIKLIDRVYSRLGLEVRVVRLSNSDGSAFYGPKLDFEVVFPSLGKQRQTGTIQNDGFRLPRRLGIRY---KDE 153
                         170       180
                  ....*....|....*....|....*...
gi 975087557  420 MDKVEFVHMLNATMCATTRAICAILENY 447
Cdd:pfam00587 154 DNESKFPYMIHRAGLGVERFLAAILENN 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 ...
206-444 3.64e-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: 3.64e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975087557 206 LEQALIQYALQTLLSKGYTPVYTPFFMRKEVMQEVAQLSQFDEELYKVigkgSEKSDDNTIDEKYLIATSEQPIAALHRD 285
Cdd:cd00670    4 LWRALERFLDDRMAEYGYQEILFPFLAPTVLFFKGGHLDGYRKEMYTF----EDKGRELRDTDLVLRPAACEPIYQIFSG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975087557 286 EWLKPEDLPIKYAGLSTCFRQEvgshGRDTRGIFRVHQFEKIEQFVYASPHDNKSWemFDEMIAVAEEFYQSLGIPYHIV 365
Cdd:cd00670   80 EILSYRALPLRLDQIGPCFRHE----PSGRRGLMRVREFRQVEYVVFGEPEEAEEE--RREWLELAEEIARELGLPVRVV 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975087557 366 NIVSGS--------LNHAASKKLDLEAWFPGSGAFRELVSCSNCTDYQARRLRIRYGQTkkmmDKVEFVHMLNATMcATT 437
Cdd:cd00670  154 VADDPFfgrggkrgLDAGRETVVEFELLLPLPGRAKETAVGSANVHLDHFGASFKIDED----GGGRAHTGCGGAG-GEE 228

                 ....*..
gi 975087557 438 RAICAIL 444
Cdd:cd00670  229 RLVLALL 235
Seryl_tRNA_N pfam02403
Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA ...
2-69 1.39e-15

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: 72.62  E-value: 1.39e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 975087557    2 VLDLDLFRADkggdPALVRETQLKRFKDPALVDALVAADGAWRRCRFRADNLNKLKNLCSKTIGEKMK 69
Cdd:pfam02403   1 MLDIKLIREN----PEAVKESLKKRGVDVLDVDELLELDEKRRELQVELEELQAERNELSKEIGQAKK 64
class_II_aaRS-like_core cd00768
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ...
206-433 3.19e-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: 59.82  E-value: 3.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975087557 206 LEQALIQYALQTLLSKGYTPVYTPFFMRKEVmqevaqLSQFDEELYKVIGKGSEKSDDntideKYLIATSEQPIAALHRd 285
Cdd:cd00768    1 IRSKIEQKLRRFMAELGFQEVETPIVEREPL------LEKAGHEPKDLLPVGAENEED-----LYLRPTLEPGLVRLFV- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975087557 286 EWLKpeDLPIKYAGLSTCFRQEvgshgRDTRGIFRVHQFEKIEQFVYASPHDNKSWemFDEMIAVAEEFYQSLGIPYHIV 365
Cdd:cd00768   69 SHIR--KLPLRLAEIGPAFRNE-----GGRRGLRRVREFTQLEGEVFGEDGEEASE--FEELIELTEELLRALGIKLDIV 139
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 975087557 366 NIVS--GSL-NHAASKKLDLEAWFPgSGAFRELVSCSNCTDYQARRLRIRYGQTKkmmDKVEFVHMLNATM 433
Cdd:cd00768  140 FVEKtpGEFsPGGAGPGFEIEVDHP-EGRGLEIGSGGYRQDEQARAADLYFLDEA---LEYRYPPTIGFGL 206
PRK04173 PRK04173
glycyl-tRNA synthetase; Provisional
317-404 1.08e-04

glycyl-tRNA synthetase; Provisional


Pssm-ID: 235240 [Multi-domain]  Cd Length: 456  Bit Score: 44.73  E-value: 1.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975087557 317 GIFRVHQFEK--IEQFVYasPHDNKSWemFDEMIAVAEEFYQSLGIP---YHIVNIVSGSLNHAASKKLDLEAWFPGSGA 391
Cdd:PRK04173 205 FIFRTREFEQmeLEFFVK--PGTDNEW--FAYWIELRKNWLLDLGIDpenLRFREHLPEELAHYSKATWDIEYKFPFGRF 280
                         90
                 ....*....|...
gi 975087557 392 FRELVSCSNCTDY 404
Cdd:PRK04173 281 WGELEGIANRTDY 293
PRK14894 PRK14894
glycyl-tRNA synthetase; Provisional
293-404 1.28e-03

glycyl-tRNA synthetase; Provisional


Pssm-ID: 237851 [Multi-domain]  Cd Length: 539  Bit Score: 41.53  E-value: 1.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975087557 293 LPIKYAGLSTCFRQEVGSHGRdtrgIFRVHQFEKIEQFVYASPHDNKSWEM--FDEMIAvaeeFYQSLGIP---YHIVNI 367
Cdd:PRK14894 164 LPFGIAQVGKAFRNEINPRNF----LFRVREFEQMEIEYFVMPGTDEEWHQrwLEARLA----WWEQIGIPrsrITIYDV 235
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 975087557 368 VSGSLNHAASKKLDLEAWFPGSGaFRELVSCSNCTDY 404
Cdd:PRK14894 236 PPDELAHYSKRTFDLMYDYPNIG-VQEIEGIANRTDY 271
PRK00960 PRK00960
seryl-tRNA synthetase; Provisional
194-385 8.98e-03

seryl-tRNA synthetase; Provisional


Pssm-ID: 234876 [Multi-domain]  Cd Length: 517  Bit Score: 38.46  E-value: 8.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975087557 194 SRGYFLKGP-LVFLEQALIQYALQTLLSK-GYTPVYTPFFMRKEVMQEVAQLSQFDEELYKVIgkgSEKSDDNTIDE--K 269
Cdd:PRK00960 212 GRGQWFYTPpMTKLFRAFEKLVIEEVLKPlGFDECLFPKLIPLEVMYKMRYLEGLPEGMYYVC---PPKRDPEYFEEfvD 288
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975087557 270 YLIATSEQPIAALHR----------------------DEWLKPEDLPIKYAGLS-TCFRQEVGShgrdTRGIFRVHQFEK 326
Cdd:PRK00960 289 EMMVKKEVPIEKLKEklrdpgyvlapaqcepfyqffqGETVDVDELPIKFFDRSgWTYRWEGGG----AHGLERVNEFHR 364
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 975087557 327 IEQFVYASPhdnkswemfDEMIAVAEEFYQslgipyhivnivsgsLNHAASKKLDLEAW 385
Cdd:PRK00960 365 IEIVWLGTP---------EQVEEIRDELLK---------------YAHILAEKLDLEYW 399
 
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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