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Conserved domains on  [gi|1868909158|gb|QLG43369|]
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serine--tRNA ligase [Mesomycoplasma hyopneumoniae]

Protein Classification

serine--tRNA ligase( domain architecture ID 11480938)

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

EC:  6.1.1.11
Gene Ontology:  GO:0005737|GO:0005524|GO:0006434|GO:0004828|GO:0016260
PubMed:  7986071|9889265|7540217

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
PRK05431 PRK05431
seryl-tRNA synthetase; Provisional
 3-412 0e+00

seryl-tRNA synthetase; Provisional


:

Pssm-ID: 235461 [Multi-domain]  Cd Length: 425  Bit Score: 619.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868909158   3 IRLILNNKSFVEKKLATRGFDiSIINELYIKGQKRNILRQKIDALLAKKNLISKEIGAFSRQEKDSSFLKSQVSKIKTEI 82
Cdd:PRK05431    4 IKLIRENPEAVKEALAKRGFP-LDVDELLELDEERRELQTELEELQAERNALSKEIGQAKRKGEDAEALIAEVKELKEEI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868909158  83 ETLEAEWYQLDTWLNQKILEIPNLPDDSVPFGTSELDNQVISHWGIPKKFDQKCKPHYEFGISNKILDFKRAVKISGNRF 162
Cdd:PRK05431   83 KALEAELDELEAELEELLLRIPNLPHDSVPVGKDEDDNVEVRRWGEPREFDFEPKDHWELGEKLGILDFERAAKVSGSRF 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868909158 163 VIYKNLGAKLVRSLINFMIDTHI-ANDYQEIIPNTLILSESLYGTGQLPKFHNDLYPLKDPNRWLIPTAEVPLTNYFREE 241
Cdd:PRK05431  163 YVLKGDGARLERALIQFMLDLHTeEHGYTEVIPPYLVNEESMYGTGQLPKFEEDLYKIEDDDLYLIPTAEVPLTNLHRDE 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868909158 242 IIDLAK-PISLVGYSKCYRSEAGSGGRDTKGLIRLHEFHKVELVKITKEADGLTEFENLVKDASRILKLLEIPFRVVVLS 320
Cdd:PRK05431  243 ILDEEElPLKYTAYSPCFRSEAGSAGRDTRGLIRVHQFDKVELVKFTKPEDSYAELEELTANAEEILQKLELPYRVVLLC 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868909158 321 TYDLGFSSKKTVDLEAWLPSENTYREVSSISYCGDFQARRAKIRYRE--GKNNHYAHTINGSGLAIDRLVAILLEQYQNL 398
Cdd:PRK05431  323 TGDLGFSAAKTYDLEVWLPSQNTYREISSCSNCTDFQARRANIRYRDegDGKPELVHTLNGSGLAVGRTLVAILENYQQA 402

                         410
                  ....*....|....
gi 1868909158 399 DGSWTVPKVLEPYF 412
Cdd:PRK05431  403 DGSVTIPEVLRPYM 416
 
Name Accession Description Interval E-value
PRK05431 PRK05431
seryl-tRNA synthetase; Provisional
 3-412 0e+00

seryl-tRNA synthetase; Provisional


Pssm-ID: 235461 [Multi-domain]  Cd Length: 425  Bit Score: 619.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868909158   3 IRLILNNKSFVEKKLATRGFDiSIINELYIKGQKRNILRQKIDALLAKKNLISKEIGAFSRQEKDSSFLKSQVSKIKTEI 82
Cdd:PRK05431    4 IKLIRENPEAVKEALAKRGFP-LDVDELLELDEERRELQTELEELQAERNALSKEIGQAKRKGEDAEALIAEVKELKEEI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868909158  83 ETLEAEWYQLDTWLNQKILEIPNLPDDSVPFGTSELDNQVISHWGIPKKFDQKCKPHYEFGISNKILDFKRAVKISGNRF 162
Cdd:PRK05431   83 KALEAELDELEAELEELLLRIPNLPHDSVPVGKDEDDNVEVRRWGEPREFDFEPKDHWELGEKLGILDFERAAKVSGSRF 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868909158 163 VIYKNLGAKLVRSLINFMIDTHI-ANDYQEIIPNTLILSESLYGTGQLPKFHNDLYPLKDPNRWLIPTAEVPLTNYFREE 241
Cdd:PRK05431  163 YVLKGDGARLERALIQFMLDLHTeEHGYTEVIPPYLVNEESMYGTGQLPKFEEDLYKIEDDDLYLIPTAEVPLTNLHRDE 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868909158 242 IIDLAK-PISLVGYSKCYRSEAGSGGRDTKGLIRLHEFHKVELVKITKEADGLTEFENLVKDASRILKLLEIPFRVVVLS 320
Cdd:PRK05431  243 ILDEEElPLKYTAYSPCFRSEAGSAGRDTRGLIRVHQFDKVELVKFTKPEDSYAELEELTANAEEILQKLELPYRVVLLC 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868909158 321 TYDLGFSSKKTVDLEAWLPSENTYREVSSISYCGDFQARRAKIRYRE--GKNNHYAHTINGSGLAIDRLVAILLEQYQNL 398
Cdd:PRK05431  323 TGDLGFSAAKTYDLEVWLPSQNTYREISSCSNCTDFQARRANIRYRDegDGKPELVHTLNGSGLAVGRTLVAILENYQQA 402

                         410
                  ....*....|....
gi 1868909158 399 DGSWTVPKVLEPYF 412
Cdd:PRK05431  403 DGSVTIPEVLRPYM 416
SerS COG0172
Seryl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Seryl-tRNA synthetase ...
 3-412 0e+00

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: 581.96  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868909158   3 IRLILNNKSFVEKKLATRGFDISI--INELYikgQKRNILRQKIDALLAKKNLISKEIGAFSRQEKDSSFLKSQVSKIKT 80
Cdd:COG0172     4 IKLIRENPEAVKEALAKRGFDLDVdeLLELD---EERRELQTEVEELRAERNALSKEIGKAKKKGEEAEALIAEVKELKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868909158  81 EIETLEAEWYQLDTWLNQKILEIPNLPDDSVPFGTSELDNQVISHWGIPKKFDQKCKPHYEFGISNKILDFKRAVKISGN 160
Cdd:COG0172    81 EIKELEEELKELEEELDELLLSIPNLPHESVPVGKDESDNVEVRRWGEPREFDFEPKDHWELGEKLGILDFERAAKVSGS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868909158 161 RFVIYKNLGAKLVRSLINFMIDTHIANDYQEIIPNTLILSESLYGTGQLPKFHNDLYPLKDPNRWLIPTAEVPLTNYFRE 240
Cdd:COG0172   161 RFYVLKGDGARLERALIQFMLDLHTEHGYTEVIPPYLVNEESMYGTGQLPKFEEDLYKIEGDDLYLIPTAEVPLTNLHRD 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868909158 241 EIIDLAK-PISLVGYSKCYRSEAGSGGRDTKGLIRLHEFHKVELVKITKEADGLTEFENLVKDASRILKLLEIPFRVVVL 319
Cdd:COG0172   241 EILDEEDlPLRYTAYTPCFRREAGSYGRDTRGLIRQHQFDKVEMVQFVKPEDSYEELEELTAHAEEILQKLGLPYRVVLL 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868909158 320 STYDLGFSSKKTVDLEAWLPSENTYREVSSISYCGDFQARRAKIRYR-EGKNNHYAHTINGSGLAIDR-LVAIlLEQYQN 397
Cdd:COG0172   321 CTGDLGFSAAKTYDLEVWLPGQNKYREISSCSNCTDFQARRLNIRYRdEDGKPEFVHTLNGSGLAVGRtLVAI-LENYQQ 399

                         410
                  ....*....|....*
gi 1868909158 398 LDGSWTVPKVLEPYF 412
Cdd:COG0172   400 ADGSVRIPEVLRPYM 414
serS TIGR00414
seryl-tRNA synthetase; This model represents the seryl-tRNA synthetase found in most organisms. ...
 3-411 3.39e-163

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: 464.91  E-value: 3.39e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868909158   3 IRLILNNKSFVEKKLATRGFDISIINELYIKGQKRNI-LRQKIDALLAKKNLISKEIGAFSRQEKDSSF-LKSQVSKIKT 80
Cdd:TIGR00414   4 RKLLRNNPDLVKESLKARGLSVDIDLEKLIALDDERKkLLSEIEELQAKRNELSKQIGKAKGQKKDKIEeIKKELKELKE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868909158  81 EIETLEAEWYQLDTWLNQKILEIPNLPDDSVPFGTSELDNQVISHWGIPKKFDQKCKPHYEFGISNKILDFKRAVKISGN 160
Cdd:TIGR00414  84 ELTELSAALKALEAELQDKLLSIPNIPHESVPVGKDEEDNLEVKRWGTPPVFDFKPKPHWELGEKLGGLDFDRAVKVTGS 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868909158 161 RFVIYKNLGAKLVRSLINFMIDTHIANDYQEIIPNTLILSESLYGTGQLPKFHNDLYPLKDPNRWLIPTAEVPLTNYFRE 240
Cdd:TIGR00414 164 RFYYLKNDGAKLERALINFMLDLLEKNGYQEIYPPYLVNEESLDGTGQLPKFEEDIFKLEDTDLYLIPTAEVPLTNLHRN 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868909158 241 EIIDLAK-PISLVGYSKCYRSEAGSGGRDTKGLIRLHEFHKVELVKITKEADGLTEFENLVKDASRILKLLEIPFRVVVL 319
Cdd:TIGR00414 244 EILEEEElPIKYTAHSPCFRSEAGSYGKDTKGLIRVHQFNKVELVKFCKPEESAEELEEMTSDAEQILQELELPYRVVNL 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868909158 320 STYDLGFSSKKTVDLEAWLPSENTYREVSSISYCGDFQARRAKIRYRE--GKNNHYAHTINGSGLAIDRLVAILLEQYQN 397
Cdd:TIGR00414 324 CSGDLGFSAAKKYDLEVWMPGQNTYREISSCSNCTDFQARRLNIRYKDknKGKNKYVHTLNGTALAIGRTIVAILENYQT 403

                         410
                  ....*....|....
gi 1868909158 398 LDGSWTVPKVLEPY 411
Cdd:TIGR00414 404 EDGSVEIPEVLRKY 417
SerRS_core cd00770
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the ...
 119-411 2.34e-145

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: 415.03  E-value: 2.34e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868909158 119 DNQVISHWGIPKKFDQKCKPHYEFGISNKILDFKRAVKISGNRFVIYKNLGAKLVRSLINFMIDTHIANDYQEIIPNTLI 198
Cdd:cd00770     1 DNVEIRRWGEPRVFDFKPKDHVELGEKLDILDFERGAKVSGSRFYYLKGDGALLERALINFALDFLTKRGFTPVIPPFLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868909158 199 LSESLYGTGQLPKFHNDLYPLKDPNRWLIPTAEVPLTNYFREEIIDLAK-PISLVGYSKCYRSEAGSGGRDTKGLIRLHE 277
Cdd:cd00770    81 RKEVMEGTGQLPKFDEQLYKVEGEDLYLIATAEVPLAALHRDEILEEEElPLKYAGYSPCFRKEAGSAGRDTRGLFRVHQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868909158 278 FHKVELVKITKEADGLTEFENLVKDASRILKLLEIPFRVVVLSTYDLGFSSKKTVDLEAWLPSENTYREVSSISYCGDFQ 357
Cdd:cd00770   161 FEKVEQFVFTKPEESWEELEELISNAEEILQELGLPYRVVNICTGDLGFAAAKKYDIEAWMPGQGKYREISSCSNCTDFQ 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1868909158 358 ARRAKIRYREGKN--NHYAHTINGSGLAIDRLVAILLEQYQNLDGSWTVPKVLEPY 411
Cdd:cd00770   241 ARRLNIRYRDKKDgkKQYVHTLNGTALATPRTIVAILENYQTEDGSVVIPEVLRPY 296
tRNA-synt_2b pfam00587
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ...
 217-395 8.39e-40

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: 140.24  E-value: 8.39e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868909158 217 YPLKDPNR---WLIPTAEVPLTNYFREEII---DLakPISLVGYSKCYRSEAGsggRDTKGLIRLHEFHKVELVKITKEA 290
Cdd:pfam00587   1 YKVEDENGdelALKPTNEPGHTLLFREEGLrskDL--PLKLAQFGTCFRHEAS---GDTRGLIRVRQFHQDDAHIFHAPG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868909158 291 DGLTEFENLVKDASRILKLLEIPFRVVVLSTYDLGFSSKKTVDLEAWLPSENTYREVSSISYCGDFQARRAKIRYREGKN 370
Cdd:pfam00587  76 QSPDELEDYIKLIDRVYSRLGLEVRVVRLSNSDGSAFYGPKLDFEVVFPSLGKQRQTGTIQNDGFRLPRRLGIRYKDEDN 155

                         170       180
                  ....*....|....*....|....*.
gi 1868909158 371 -NHYAHTINGSGLAIDRLVAILLEQY 395
Cdd:pfam00587 156 eSKFPYMIHRAGLGVERFLAAILENN 181
 
Name Accession Description Interval E-value
PRK05431 PRK05431
seryl-tRNA synthetase; Provisional
 3-412 0e+00

seryl-tRNA synthetase; Provisional


Pssm-ID: 235461 [Multi-domain]  Cd Length: 425  Bit Score: 619.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868909158   3 IRLILNNKSFVEKKLATRGFDiSIINELYIKGQKRNILRQKIDALLAKKNLISKEIGAFSRQEKDSSFLKSQVSKIKTEI 82
Cdd:PRK05431    4 IKLIRENPEAVKEALAKRGFP-LDVDELLELDEERRELQTELEELQAERNALSKEIGQAKRKGEDAEALIAEVKELKEEI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868909158  83 ETLEAEWYQLDTWLNQKILEIPNLPDDSVPFGTSELDNQVISHWGIPKKFDQKCKPHYEFGISNKILDFKRAVKISGNRF 162
Cdd:PRK05431   83 KALEAELDELEAELEELLLRIPNLPHDSVPVGKDEDDNVEVRRWGEPREFDFEPKDHWELGEKLGILDFERAAKVSGSRF 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868909158 163 VIYKNLGAKLVRSLINFMIDTHI-ANDYQEIIPNTLILSESLYGTGQLPKFHNDLYPLKDPNRWLIPTAEVPLTNYFREE 241
Cdd:PRK05431  163 YVLKGDGARLERALIQFMLDLHTeEHGYTEVIPPYLVNEESMYGTGQLPKFEEDLYKIEDDDLYLIPTAEVPLTNLHRDE 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868909158 242 IIDLAK-PISLVGYSKCYRSEAGSGGRDTKGLIRLHEFHKVELVKITKEADGLTEFENLVKDASRILKLLEIPFRVVVLS 320
Cdd:PRK05431  243 ILDEEElPLKYTAYSPCFRSEAGSAGRDTRGLIRVHQFDKVELVKFTKPEDSYAELEELTANAEEILQKLELPYRVVLLC 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868909158 321 TYDLGFSSKKTVDLEAWLPSENTYREVSSISYCGDFQARRAKIRYRE--GKNNHYAHTINGSGLAIDRLVAILLEQYQNL 398
Cdd:PRK05431  323 TGDLGFSAAKTYDLEVWLPSQNTYREISSCSNCTDFQARRANIRYRDegDGKPELVHTLNGSGLAVGRTLVAILENYQQA 402

                         410
                  ....*....|....
gi 1868909158 399 DGSWTVPKVLEPYF 412
Cdd:PRK05431  403 DGSVTIPEVLRPYM 416
SerS COG0172
Seryl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Seryl-tRNA synthetase ...
 3-412 0e+00

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: 581.96  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868909158   3 IRLILNNKSFVEKKLATRGFDISI--INELYikgQKRNILRQKIDALLAKKNLISKEIGAFSRQEKDSSFLKSQVSKIKT 80
Cdd:COG0172     4 IKLIRENPEAVKEALAKRGFDLDVdeLLELD---EERRELQTEVEELRAERNALSKEIGKAKKKGEEAEALIAEVKELKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868909158  81 EIETLEAEWYQLDTWLNQKILEIPNLPDDSVPFGTSELDNQVISHWGIPKKFDQKCKPHYEFGISNKILDFKRAVKISGN 160
Cdd:COG0172    81 EIKELEEELKELEEELDELLLSIPNLPHESVPVGKDESDNVEVRRWGEPREFDFEPKDHWELGEKLGILDFERAAKVSGS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868909158 161 RFVIYKNLGAKLVRSLINFMIDTHIANDYQEIIPNTLILSESLYGTGQLPKFHNDLYPLKDPNRWLIPTAEVPLTNYFRE 240
Cdd:COG0172   161 RFYVLKGDGARLERALIQFMLDLHTEHGYTEVIPPYLVNEESMYGTGQLPKFEEDLYKIEGDDLYLIPTAEVPLTNLHRD 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868909158 241 EIIDLAK-PISLVGYSKCYRSEAGSGGRDTKGLIRLHEFHKVELVKITKEADGLTEFENLVKDASRILKLLEIPFRVVVL 319
Cdd:COG0172   241 EILDEEDlPLRYTAYTPCFRREAGSYGRDTRGLIRQHQFDKVEMVQFVKPEDSYEELEELTAHAEEILQKLGLPYRVVLL 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868909158 320 STYDLGFSSKKTVDLEAWLPSENTYREVSSISYCGDFQARRAKIRYR-EGKNNHYAHTINGSGLAIDR-LVAIlLEQYQN 397
Cdd:COG0172   321 CTGDLGFSAAKTYDLEVWLPGQNKYREISSCSNCTDFQARRLNIRYRdEDGKPEFVHTLNGSGLAVGRtLVAI-LENYQQ 399

                         410
                  ....*....|....*
gi 1868909158 398 LDGSWTVPKVLEPYF 412
Cdd:COG0172   400 ADGSVRIPEVLRPYM 414
serS TIGR00414
seryl-tRNA synthetase; This model represents the seryl-tRNA synthetase found in most organisms. ...
 3-411 3.39e-163

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: 464.91  E-value: 3.39e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868909158   3 IRLILNNKSFVEKKLATRGFDISIINELYIKGQKRNI-LRQKIDALLAKKNLISKEIGAFSRQEKDSSF-LKSQVSKIKT 80
Cdd:TIGR00414   4 RKLLRNNPDLVKESLKARGLSVDIDLEKLIALDDERKkLLSEIEELQAKRNELSKQIGKAKGQKKDKIEeIKKELKELKE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868909158  81 EIETLEAEWYQLDTWLNQKILEIPNLPDDSVPFGTSELDNQVISHWGIPKKFDQKCKPHYEFGISNKILDFKRAVKISGN 160
Cdd:TIGR00414  84 ELTELSAALKALEAELQDKLLSIPNIPHESVPVGKDEEDNLEVKRWGTPPVFDFKPKPHWELGEKLGGLDFDRAVKVTGS 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868909158 161 RFVIYKNLGAKLVRSLINFMIDTHIANDYQEIIPNTLILSESLYGTGQLPKFHNDLYPLKDPNRWLIPTAEVPLTNYFRE 240
Cdd:TIGR00414 164 RFYYLKNDGAKLERALINFMLDLLEKNGYQEIYPPYLVNEESLDGTGQLPKFEEDIFKLEDTDLYLIPTAEVPLTNLHRN 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868909158 241 EIIDLAK-PISLVGYSKCYRSEAGSGGRDTKGLIRLHEFHKVELVKITKEADGLTEFENLVKDASRILKLLEIPFRVVVL 319
Cdd:TIGR00414 244 EILEEEElPIKYTAHSPCFRSEAGSYGKDTKGLIRVHQFNKVELVKFCKPEESAEELEEMTSDAEQILQELELPYRVVNL 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868909158 320 STYDLGFSSKKTVDLEAWLPSENTYREVSSISYCGDFQARRAKIRYRE--GKNNHYAHTINGSGLAIDRLVAILLEQYQN 397
Cdd:TIGR00414 324 CSGDLGFSAAKKYDLEVWMPGQNTYREISSCSNCTDFQARRLNIRYKDknKGKNKYVHTLNGTALAIGRTIVAILENYQT 403

                         410
                  ....*....|....
gi 1868909158 398 LDGSWTVPKVLEPY 411
Cdd:TIGR00414 404 EDGSVEIPEVLRKY 417
SerRS_core cd00770
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the ...
 119-411 2.34e-145

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: 415.03  E-value: 2.34e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868909158 119 DNQVISHWGIPKKFDQKCKPHYEFGISNKILDFKRAVKISGNRFVIYKNLGAKLVRSLINFMIDTHIANDYQEIIPNTLI 198
Cdd:cd00770     1 DNVEIRRWGEPRVFDFKPKDHVELGEKLDILDFERGAKVSGSRFYYLKGDGALLERALINFALDFLTKRGFTPVIPPFLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868909158 199 LSESLYGTGQLPKFHNDLYPLKDPNRWLIPTAEVPLTNYFREEIIDLAK-PISLVGYSKCYRSEAGSGGRDTKGLIRLHE 277
Cdd:cd00770    81 RKEVMEGTGQLPKFDEQLYKVEGEDLYLIATAEVPLAALHRDEILEEEElPLKYAGYSPCFRKEAGSAGRDTRGLFRVHQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868909158 278 FHKVELVKITKEADGLTEFENLVKDASRILKLLEIPFRVVVLSTYDLGFSSKKTVDLEAWLPSENTYREVSSISYCGDFQ 357
Cdd:cd00770   161 FEKVEQFVFTKPEESWEELEELISNAEEILQELGLPYRVVNICTGDLGFAAAKKYDIEAWMPGQGKYREISSCSNCTDFQ 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1868909158 358 ARRAKIRYREGKN--NHYAHTINGSGLAIDRLVAILLEQYQNLDGSWTVPKVLEPY 411
Cdd:cd00770   241 ARRLNIRYRDKKDgkKQYVHTLNGTALATPRTIVAILENYQTEDGSVVIPEVLRPY 296
PLN02678 PLN02678
seryl-tRNA synthetase
 23-411 3.26e-78

seryl-tRNA synthetase


Pssm-ID: 215364 [Multi-domain]  Cd Length: 448  Bit Score: 248.85  E-value: 3.26e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868909158  23 DISIINELYIKGQKRNILRQKIDALLAKKNLISKEIGAFSRQEKDSSFLKSQVSKIKTEIETLEAEWYQLDTWLNQKILE 102
Cdd:PLN02678   28 SVELVDEVIALDKEWRQRQFELDSLRKEFNKLNKEVAKLKIAKEDATELIAETKELKKEITEKEAEVQEAKAALDAKLKT 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868909158 103 IPNLPDDSVPFGTSELDNQVISHWGiPKKFDQKCKPHYEFGISNKILDFKRAVKISGNRFVIYKNLGAKLVRSLINFMID 182
Cdd:PLN02678  108 IGNLVHDSVPVSNDEANNAVVRTWG-EKRQEPKLKNHVDLVELLGIVDTERGADVAGGRGYYLKGAGVLLNQALINFGLA 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868909158 183 THIANDYQEIIPNTLILSESLYGTGQLPKFHNDLYPLK-DPN-RWLIPTAEVPLTNYFREEIIDLAK-PISLVGYSKCYR 259
Cdd:PLN02678  187 FLRKRGYTPLQTPFFMRKDVMAKCAQLAQFDEELYKVTgEGDdKYLIATSEQPLCAYHRGDWIDPKElPIRYAGYSTCFR 266

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868909158 260 SEAGSGGRDTKGLIRLHEFHKVELVKITKEADGLT--EFENLVKDASRILKLLEIPFRVVVLSTYDLGFSSKKTVDLEAW 337
Cdd:PLN02678  267 KEAGSHGRDTLGIFRVHQFEKVEQFCITSPNGNESweMHEEMLKNSEDFYQSLGIPYQVVSIVSGALNDAAAKKYDLEAW 346

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1868909158 338 LPSENTYREVSSISYCGDFQARRAKIRYREGKNN----HYAHTINGSGLAIDRLVAILLEQYQNLDGSwTVPKVLEPY 411
Cdd:PLN02678  347 FPASKTYRELVSCSNCTDYQSRRLEIRYGQKKSNeqtkQYVHLLNSTLTATERTLCCILENYQTEDGV-RVPEVLQPF 423
PLN02320 PLN02320
seryl-tRNA synthetase
 1-411 2.46e-58

seryl-tRNA synthetase


Pssm-ID: 177954 [Multi-domain]  Cd Length: 502  Bit Score: 198.22  E-value: 2.46e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868909158   1 MNIRLILNNKSFVEKKLATRG--FDISIINELYikgQKRNILRQKIDALLAKKNLISKEI-GAFSRQEKDSsfLKSQVSK 77
Cdd:PLN02320   67 IDFKWIRDNKEAVAINIRNRNsnANLELVLELY---ENMLALQKEVERLRAERNAVANKMkGKLEPSERQA--LVEEGKN 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868909158  78 IKTEIETLEAEWYQLDTWLNQKILEIPNLPDDSVPFGTSElDNQVISHWGIPKKFDQKCKPHYEFGISNKILDFKRAVKI 157
Cdd:PLN02320  142 LKEGLVTLEEDLVKLTDELQLEAQSIPNMTHPDVPVGGED-SSAVRKEVGSPREFSFPIKDHLQLGKELDLFDFDAAAEV 220

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868909158 158 SGNRFVIYKNLGAKLVRSLINFMIDTHIANDYQEIIPNTLILSESLYGTGQLPKFHN-DLYPLKDPNRWLIPTAEVPLTN 236
Cdd:PLN02320  221 SGSKFYYLKNEAVLLEMALVNWTLSEVMKKGFTPLTTPEIVRSSVVEKCGFQPRGDNtQVYSIDGSDQCLIGTAEIPVGG 300

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868909158 237 YFREEII-DLAKPISLVGYSKCYRSEAGSGGRDTKGLIRLHEFHKVELVKITKEADGLTEFENLVKDASRILKLLEIPFR 315
Cdd:PLN02320  301 IHMDSILlESALPLKYVAFSHCFRTEAGAAGAATRGLYRVHQFSKVEMFVICRPEESESFHEELIQIEEDLFTSLGLHFK 380

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868909158 316 VVVLSTYDLGFSSKKTVDLEAWLPSENTYREVSSISYCGDFQARRAKIRYR----------EGKNN----HYAHTINGSG 381
Cdd:PLN02320  381 TLDMATADLGAPAYRKFDIEAWMPGLGRYGEISSASNCTDYQSRRLGIRYRpseppqtnpkKGKGSlgptKFVHTLNATA 460

                         410       420       430
                  ....*....|....*....|....*....|
gi 1868909158 382 LAIDRLVAILLEQYQNLDGSWTVPKVLEPY 411
Cdd:PLN02320  461 CAVPRMIVCLLENYQQEDGSVVIPEPLRPF 490
tRNA-synt_2b pfam00587
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ...
 217-395 8.39e-40

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: 140.24  E-value: 8.39e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868909158 217 YPLKDPNR---WLIPTAEVPLTNYFREEII---DLakPISLVGYSKCYRSEAGsggRDTKGLIRLHEFHKVELVKITKEA 290
Cdd:pfam00587   1 YKVEDENGdelALKPTNEPGHTLLFREEGLrskDL--PLKLAQFGTCFRHEAS---GDTRGLIRVRQFHQDDAHIFHAPG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868909158 291 DGLTEFENLVKDASRILKLLEIPFRVVVLSTYDLGFSSKKTVDLEAWLPSENTYREVSSISYCGDFQARRAKIRYREGKN 370
Cdd:pfam00587  76 QSPDELEDYIKLIDRVYSRLGLEVRVVRLSNSDGSAFYGPKLDFEVVFPSLGKQRQTGTIQNDGFRLPRRLGIRYKDEDN 155

                         170       180
                  ....*....|....*....|....*.
gi 1868909158 371 -NHYAHTINGSGLAIDRLVAILLEQY 395
Cdd:pfam00587 156 eSKFPYMIHRAGLGVERFLAAILENN 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 ...
 169-392 5.93e-29

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: 112.87  E-value: 5.93e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868909158 169 GAKLVRSLINFMIDTHIANDYQEIIPNTLILSESLYGTGQLPKFHNDLYPLKDPNRW-------LIPTAEVPLTNYFREE 241
Cdd:cd00670     1 GTALWRALERFLDDRMAEYGYQEILFPFLAPTVLFFKGGHLDGYRKEMYTFEDKGRElrdtdlvLRPAACEPIYQIFSGE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868909158 242 IIDLAK-PISLVGYSKCYRSEAgsggRDTKGLIRLHEFHKVELVKITKEADGLTEFENLVKDASRILKLLEIPFRVVVLS 320
Cdd:cd00670    81 ILSYRAlPLRLDQIGPCFRHEP----SGRRGLMRVREFRQVEYVVFGEPEEAEEERREWLELAEEIARELGLPVRVVVAD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868909158 321 TYDLGFSSK--------KTVDLEAWLPSENTYREVSSISYCGDFQARRAKIRYREGKNNHYAHTINGSGLaIDRLVAILL 392
Cdd:cd00670   157 DPFFGRGGKrgldagreTVVEFELLLPLPGRAKETAVGSANVHLDHFGASFKIDEDGGGRAHTGCGGAGG-EERLVLALL 235
Seryl_tRNA_N pfam02403
Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA ...
 2-107 2.52e-20

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: 85.33  E-value: 2.52e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868909158   2 NIRLILNNKSFVEKKLATRGFDISIINELYIKGQKRNILRQKIDALLAKKNLISKEIGAFSRQEKDSSFLKSQVSKIKTE 81
Cdd:pfam02403   3 DIKLIRENPEAVKESLKKRGVDVLDVDELLELDEKRRELQVELEELQAERNELSKEIGQAKKKKEDADALIAEVKELKDE 82

                          90       100
                  ....*....|....*....|....*.
gi 1868909158  82 IETLEAEWYQLDTWLNQKILEIPNLP 107
Cdd:pfam02403  83 LKALEAELKELEAELDKLLLTIPNIP 108
PRK00960 PRK00960
seryl-tRNA synthetase; Provisional
 219-395 3.81e-06

seryl-tRNA synthetase; Provisional


Pssm-ID: 234876 [Multi-domain]  Cd Length: 517  Bit Score: 48.86  E-value: 3.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868909158 219 LKDPNRWLIPTAEVPLTNYFREEIIDLAK-PISLV---GYSkcYRSEagSGGrdTKGLIRLHEFHKVELVKITKEADGLT 294
Cdd:PRK00960  305 LRDPGYVLAPAQCEPFYQFFQGETVDVDElPIKFFdrsGWT--YRWE--GGG--AHGLERVNEFHRIEIVWLGTPEQVEE 378

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868909158 295 EFENLVKDASRILKLLEIPFRVVV-----------LSTYDLGFSSKKTVDLEAWLP---SENTYREVSSISYCGDfqarr 360
Cdd:PRK00960  379 IRDELLKYAHILAEKLDLEYWREVgddpfylegrgLEDRGIEFPDVPKYEMELWLPyrgDERKWVAVTSANVHGT----- 453

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1868909158 361 akiRYREG---KNNHYAHTING-SGLAIDRLVAILLEQY 395
Cdd:PRK00960  454 ---HFVEGfniKDYKGRKLWTGcTGYGLERWVIGFLAQK 489
ThrS COG0441
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ...
 169-224 5.70e-04

Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


Pssm-ID: 440210 [Multi-domain]  Cd Length: 639  Bit Score: 41.94  E-value: 5.70e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1868909158 169 GAKLVRSLINFMIDTHIANDYQEIipNT-LILSESLYGT-GQLPKFHNDLYPLKDPNR 224
Cdd:COG0441   270 GAIIRRELEDYIREKHRKAGYQEV--KTpHILDRELWETsGHWDHYRENMFPTESDGE 325
 
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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