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Conserved domains on  [gi|515869651|ref|NP_001265519|]
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lipoyl synthase, mitochondrial isoform 3 precursor [Homo sapiens]

Protein Classification

lipoyl synthase( domain architecture ID 1003513)

lipoyl synthase catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives; belongs to the radical SAM superfamily

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN02428 super family cl33489
lipoic acid synthase
22-327 1.44e-170

lipoic acid synthase


The actual alignment was detected with superfamily member PLN02428:

Pssm-ID: 215236 [Multi-domain]  Cd Length: 349  Bit Score: 477.32  E-value: 1.44e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515869651  22 CSPVRPLSSLPDKKKELLQNGPDLQDFVSGDladrsTWDEYKGNLKRQkgerLRLPPWLKTEIPMGKNYNKLKNTLRNLN 101
Cdd:PLN02428   6 TTAPQTPQTLAALRARLASESPSLGDFVSLG-----PYTLGSYGRDKP----LPKPKWLRQRAPGGEKYTEIKEKLRELK 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515869651 102 LHTVCEEARCPNIGECWGGGEYATATATIMLMGDTCTRGCRFCSVKTARNPPPLDASEPYNTAKAIAEWGLDYVVLTSVD 181
Cdd:PLN02428  77 LNTVCEEAQCPNIGECWNGGGTGTATATIMILGDTCTRGCRFCAVKTSRTPPPPDPDEPENVAEAIASWGVDYVVLTSVD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515869651 182 RDDMPDGGAEHIAKTVSYLKESK-------------------------------------------VRDPRANFDQSLRV 218
Cdd:PLN02428 157 RDDLPDGGSGHFAETVRRLKQLKpeilvealvpdfrgdlgavetvatsgldvfahnietverlqriVRDPRAGYKQSLDV 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515869651 219 LKHAKKVQPDVISKTSIMLGLGENDEQVYATMKALREADVDCLTLGQYMQPTRRHLKVEEYITPEKFKYWEKVGNELGFH 298
Cdd:PLN02428 237 LKHAKESKPGLLTKTSIMLGLGETDEEVVQTMEDLRAAGVDVVTFGQYLRPTKRHLPVKEYVTPEKFEFWREYGEEMGFR 316
                        330       340
                 ....*....|....*....|....*....
gi 515869651 299 YTASGPLVRSSYKAGEFFLKNLVAKRKTK 327
Cdd:PLN02428 317 YVASGPLVRSSYKAGEFFIKSMIREDRAK 345
 
Name Accession Description Interval E-value
PLN02428 PLN02428
lipoic acid synthase
22-327 1.44e-170

lipoic acid synthase


Pssm-ID: 215236 [Multi-domain]  Cd Length: 349  Bit Score: 477.32  E-value: 1.44e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515869651  22 CSPVRPLSSLPDKKKELLQNGPDLQDFVSGDladrsTWDEYKGNLKRQkgerLRLPPWLKTEIPMGKNYNKLKNTLRNLN 101
Cdd:PLN02428   6 TTAPQTPQTLAALRARLASESPSLGDFVSLG-----PYTLGSYGRDKP----LPKPKWLRQRAPGGEKYTEIKEKLRELK 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515869651 102 LHTVCEEARCPNIGECWGGGEYATATATIMLMGDTCTRGCRFCSVKTARNPPPLDASEPYNTAKAIAEWGLDYVVLTSVD 181
Cdd:PLN02428  77 LNTVCEEAQCPNIGECWNGGGTGTATATIMILGDTCTRGCRFCAVKTSRTPPPPDPDEPENVAEAIASWGVDYVVLTSVD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515869651 182 RDDMPDGGAEHIAKTVSYLKESK-------------------------------------------VRDPRANFDQSLRV 218
Cdd:PLN02428 157 RDDLPDGGSGHFAETVRRLKQLKpeilvealvpdfrgdlgavetvatsgldvfahnietverlqriVRDPRAGYKQSLDV 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515869651 219 LKHAKKVQPDVISKTSIMLGLGENDEQVYATMKALREADVDCLTLGQYMQPTRRHLKVEEYITPEKFKYWEKVGNELGFH 298
Cdd:PLN02428 237 LKHAKESKPGLLTKTSIMLGLGETDEEVVQTMEDLRAAGVDVVTFGQYLRPTKRHLPVKEYVTPEKFEFWREYGEEMGFR 316
                        330       340
                 ....*....|....*....|....*....
gi 515869651 299 YTASGPLVRSSYKAGEFFLKNLVAKRKTK 327
Cdd:PLN02428 317 YVASGPLVRSSYKAGEFFIKSMIREDRAK 345
LipA COG0320
Lipoate synthase [Coenzyme transport and metabolism]; Lipoate synthase is part of the Pathway ...
67-324 7.15e-143

Lipoate synthase [Coenzyme transport and metabolism]; Lipoate synthase is part of the Pathway/BioSystem: Lipoate biosynthesis


Pssm-ID: 440089 [Multi-domain]  Cd Length: 306  Bit Score: 405.64  E-value: 7.15e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515869651  67 KRQKGERLRLPPWLKTEIPMGKNYNKLKNTLRNLNLHTVCEEARCPNIGECWGGGeyataTATIMLMGDTCTRGCRFCSV 146
Cdd:COG0320   13 RNPETPILRKPDWLRVKLPTGPEYAEVKKLLREHKLHTVCEEARCPNIGECWSRG-----TATFMILGDICTRRCRFCDV 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515869651 147 KTARnPPPLDASEPYNTAKAIAEWGLDYVVLTSVDRDDMPDGGAEHIAKTVSYLKE------------------------ 202
Cdd:COG0320   88 ATGR-PLPLDPDEPERVAEAVAEMGLKYVVITSVDRDDLPDGGAGHFAETIRAIRElnpgttievlipdfrgreealdiv 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515869651 203 -------------------SKVRdPRANFDQSLRVLKHAKKVQPDVISKTSIMLGLGENDEQVYATMKALREADVDCLTL 263
Cdd:COG0320  167 vdarpdvfnhnletvprlyKRVR-PGADYERSLELLKRAKELDPGIPTKSGLMLGLGETDEEVLEVMRDLRAAGVDILTI 245
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515869651 264 GQYMQPTRRHLKVEEYITPEKFKYWEKVGNELGFHYTASGPLVRSSYKAGEFFLKNLVAKR 324
Cdd:COG0320  246 GQYLQPSKKHLPVDRYVTPEEFEELKEIALELGFLHVASGPLVRSSYHADEQAAKARAARG 306
lipA TIGR00510
lipoate synthase; This enzyme is an iron-sulfur protein. It is localized to mitochondria in ...
65-324 6.44e-113

lipoate synthase; This enzyme is an iron-sulfur protein. It is localized to mitochondria in yeast and Arabidopsis. It generates lipoic acid, a thiol antioxidant that is linked to a specific Lys as prosthetic group for the pyruvate and alpha-ketoglutarate dehydrogenase complexes and the glycine-cleavage system. The family shows strong sequence conservation. [Biosynthesis of cofactors, prosthetic groups, and carriers, Lipoate]


Pssm-ID: 273111  Cd Length: 302  Bit Score: 329.49  E-value: 6.44e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515869651   65 NLKRQKGERLRLPPWLKTEIPMGKNYNKLKNTLRNLNLHTVCEEARCPNIGECWGGGeyataTATIMLMGDTCTRGCRFC 144
Cdd:TIGR00510   6 NPIPNKEILLRKPEWLKIKLPLGTVIAQIKNTMKNKGLHTVCEEASCPNLTECWNHG-----TATFMILGDICTRRCPFC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515869651  145 SVKTARNPPPLDASEPYNTAKAIAEWGLDYVVLTSVDRDDMPDGGAEHIAKTVSYLKES--------------------- 203
Cdd:TIGR00510  81 DVAHGRNPLPPDPEEPAKLAETIKDMGLKYVVITSVDRDDLEDGGASHLAECIEAIREKlpnikietlvpdfrgniaald 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515869651  204 ----------------------KVRdPRANFDQSLRVLKHAKKVQPDVISKTSIMLGLGENDEQVYATMKALREADVDCL 261
Cdd:TIGR00510 161 illdappdvynhnletverltpFVR-PGATYRWSLKLLERAKEYLPNLPTKSGIMVGLGETNEEIKQTLKDLRDHGVTMV 239
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515869651  262 TLGQYMQPTRRHLKVEEYITPEKFKYWEKVGNELGFHYTASGPLVRSSYKAGEFFLKNLVAKR 324
Cdd:TIGR00510 240 TLGQYLRPSRRHLPVKRYVSPEEFDYYRSVALEMGFLHAACGPFVRSSYHADSLFAAGRLVKT 302
LIAS_N pfam16881
N-terminal domain of lipoyl synthase of Radical_SAM family; LIAS_N is found as the N-terminal ...
15-111 5.79e-66

N-terminal domain of lipoyl synthase of Radical_SAM family; LIAS_N is found as the N-terminal domain of the Radical_SAM family in the members that are lipoyl synthase enzymes, particularly the mitochondrial ones in metazoa but also those in bacteria.


Pssm-ID: 465296 [Multi-domain]  Cd Length: 97  Bit Score: 202.36  E-value: 5.79e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515869651   15 RVFGRYFCSPVRPLSSLPDKKKELLQNGPDLQDFVSGDLADRSTWDEYKGNLKRQKGERLRLPPWLKTEIPMGKNYNKLK 94
Cdd:pfam16881   1 RVFGSHLCSPASTSSSLPDEKREFLQNGPDLQDFVSGDLSDKSTWAEYKGNLKRPKGERLRLPPWLKTKIPLGKNYNKIK 80
                          90
                  ....*....|....*..
gi 515869651   95 NTLRNLNLHTVCEEARC 111
Cdd:pfam16881  81 NTLRNLNLHTVCEEARC 97
 
Name Accession Description Interval E-value
PLN02428 PLN02428
lipoic acid synthase
22-327 1.44e-170

lipoic acid synthase


Pssm-ID: 215236 [Multi-domain]  Cd Length: 349  Bit Score: 477.32  E-value: 1.44e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515869651  22 CSPVRPLSSLPDKKKELLQNGPDLQDFVSGDladrsTWDEYKGNLKRQkgerLRLPPWLKTEIPMGKNYNKLKNTLRNLN 101
Cdd:PLN02428   6 TTAPQTPQTLAALRARLASESPSLGDFVSLG-----PYTLGSYGRDKP----LPKPKWLRQRAPGGEKYTEIKEKLRELK 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515869651 102 LHTVCEEARCPNIGECWGGGEYATATATIMLMGDTCTRGCRFCSVKTARNPPPLDASEPYNTAKAIAEWGLDYVVLTSVD 181
Cdd:PLN02428  77 LNTVCEEAQCPNIGECWNGGGTGTATATIMILGDTCTRGCRFCAVKTSRTPPPPDPDEPENVAEAIASWGVDYVVLTSVD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515869651 182 RDDMPDGGAEHIAKTVSYLKESK-------------------------------------------VRDPRANFDQSLRV 218
Cdd:PLN02428 157 RDDLPDGGSGHFAETVRRLKQLKpeilvealvpdfrgdlgavetvatsgldvfahnietverlqriVRDPRAGYKQSLDV 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515869651 219 LKHAKKVQPDVISKTSIMLGLGENDEQVYATMKALREADVDCLTLGQYMQPTRRHLKVEEYITPEKFKYWEKVGNELGFH 298
Cdd:PLN02428 237 LKHAKESKPGLLTKTSIMLGLGETDEEVVQTMEDLRAAGVDVVTFGQYLRPTKRHLPVKEYVTPEKFEFWREYGEEMGFR 316
                        330       340
                 ....*....|....*....|....*....
gi 515869651 299 YTASGPLVRSSYKAGEFFLKNLVAKRKTK 327
Cdd:PLN02428 317 YVASGPLVRSSYKAGEFFIKSMIREDRAK 345
LipA COG0320
Lipoate synthase [Coenzyme transport and metabolism]; Lipoate synthase is part of the Pathway ...
67-324 7.15e-143

Lipoate synthase [Coenzyme transport and metabolism]; Lipoate synthase is part of the Pathway/BioSystem: Lipoate biosynthesis


Pssm-ID: 440089 [Multi-domain]  Cd Length: 306  Bit Score: 405.64  E-value: 7.15e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515869651  67 KRQKGERLRLPPWLKTEIPMGKNYNKLKNTLRNLNLHTVCEEARCPNIGECWGGGeyataTATIMLMGDTCTRGCRFCSV 146
Cdd:COG0320   13 RNPETPILRKPDWLRVKLPTGPEYAEVKKLLREHKLHTVCEEARCPNIGECWSRG-----TATFMILGDICTRRCRFCDV 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515869651 147 KTARnPPPLDASEPYNTAKAIAEWGLDYVVLTSVDRDDMPDGGAEHIAKTVSYLKE------------------------ 202
Cdd:COG0320   88 ATGR-PLPLDPDEPERVAEAVAEMGLKYVVITSVDRDDLPDGGAGHFAETIRAIRElnpgttievlipdfrgreealdiv 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515869651 203 -------------------SKVRdPRANFDQSLRVLKHAKKVQPDVISKTSIMLGLGENDEQVYATMKALREADVDCLTL 263
Cdd:COG0320  167 vdarpdvfnhnletvprlyKRVR-PGADYERSLELLKRAKELDPGIPTKSGLMLGLGETDEEVLEVMRDLRAAGVDILTI 245
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515869651 264 GQYMQPTRRHLKVEEYITPEKFKYWEKVGNELGFHYTASGPLVRSSYKAGEFFLKNLVAKR 324
Cdd:COG0320  246 GQYLQPSKKHLPVDRYVTPEEFEELKEIALELGFLHVASGPLVRSSYHADEQAAKARAARG 306
PRK05481 PRK05481
lipoyl synthase; Provisional
75-322 2.73e-139

lipoyl synthase; Provisional


Pssm-ID: 235493 [Multi-domain]  Cd Length: 289  Bit Score: 396.00  E-value: 2.73e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515869651  75 RLPPWLKTEIPMGKNYNKLKNTLRNLNLHTVCEEARCPNIGECWGGGeyataTATIMLMGDTCTRGCRFCSVKTARnPPP 154
Cdd:PRK05481   6 RKPDWLRVKLPTGEEYTEIKKLLRELGLHTVCEEASCPNIGECWSRG-----TATFMILGDICTRRCPFCDVATGR-PLP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515869651 155 LDASEPYNTAKAIAEWGLDYVVLTSVDRDDMPDGGAEHIAKTVSYLKE-------------------------------- 202
Cdd:PRK05481  80 LDPDEPERVAEAVARMGLKYVVITSVDRDDLPDGGAQHFAETIRAIRElnpgttievlipdfrgrmdalltvldarpdvf 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515869651 203 -----------SKVRdPRANFDQSLRVLKHAKKVQPDVISKTSIMLGLGENDEQVYATMKALREADVDCLTLGQYMQPTR 271
Cdd:PRK05481 160 nhnletvprlyKRVR-PGADYERSLELLKRAKELHPGIPTKSGLMVGLGETDEEVLEVMDDLRAAGVDILTIGQYLQPSR 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 515869651 272 RHLKVEEYITPEKFKYWEKVGNELGFHYTASGPLVRSSYKAGEFFLKNLVA 322
Cdd:PRK05481 239 KHLPVERYVTPEEFDEYKEIALELGFLHVASGPLVRSSYHADEQAAGAEVA 289
PTZ00413 PTZ00413
lipoate synthase; Provisional
70-326 5.70e-139

lipoate synthase; Provisional


Pssm-ID: 240408 [Multi-domain]  Cd Length: 398  Bit Score: 399.20  E-value: 5.70e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515869651  70 KGERLRLPPWLKTEIPMGKN----YNKLKNTLRNLNLHTVCEEARCPNIGECWGGG-EYATATATIMLMGDTCTRGCRFC 144
Cdd:PTZ00413  87 KRGEEPLPPWFKVKVPKGASrrprFNRIRRSMREKKLHTVCEEAKCPNIGECWGGGdEEGTATATIMVMGDHCTRGCRFC 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515869651 145 SVKTARNPPPLDASEPYNTAKAIAEWGLDYVVLTSVDRDDMPDGGAEHIAKTVSYLKESK-------------------- 204
Cdd:PTZ00413 167 SVKTSRKPPPLDPNEPEKVAKAVAEMGVDYIVMTMVDRDDLPDGGASHVARCVELIKESNpelllealvgdfhgdlksve 246
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515869651 205 -----------------------VRDPRANFDQSLRVLKHAKKV-QPDVISKTSIMLGLGENDEQVYATMKALREADVDC 260
Cdd:PTZ00413 247 klansplsvyahniecveritpyVRDRRASYRQSLKVLEHVKEFtNGAMLTKSSIMLGLGETEEEVRQTLRDLRTAGVSA 326
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515869651 261 LTLGQYMQPTRRHLKVEEYITPEKFKYWEKVGNELGFHYTASGPLVRSSYKAGEFFLKNLVAKRKT 326
Cdd:PTZ00413 327 VTLGQYLQPTKTRLKVSRYAHPKEFEMWEEEAMKMGFLYCASGPLVRSSYRAGEYYIKNLVKQRRK 392
lipA TIGR00510
lipoate synthase; This enzyme is an iron-sulfur protein. It is localized to mitochondria in ...
65-324 6.44e-113

lipoate synthase; This enzyme is an iron-sulfur protein. It is localized to mitochondria in yeast and Arabidopsis. It generates lipoic acid, a thiol antioxidant that is linked to a specific Lys as prosthetic group for the pyruvate and alpha-ketoglutarate dehydrogenase complexes and the glycine-cleavage system. The family shows strong sequence conservation. [Biosynthesis of cofactors, prosthetic groups, and carriers, Lipoate]


Pssm-ID: 273111  Cd Length: 302  Bit Score: 329.49  E-value: 6.44e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515869651   65 NLKRQKGERLRLPPWLKTEIPMGKNYNKLKNTLRNLNLHTVCEEARCPNIGECWGGGeyataTATIMLMGDTCTRGCRFC 144
Cdd:TIGR00510   6 NPIPNKEILLRKPEWLKIKLPLGTVIAQIKNTMKNKGLHTVCEEASCPNLTECWNHG-----TATFMILGDICTRRCPFC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515869651  145 SVKTARNPPPLDASEPYNTAKAIAEWGLDYVVLTSVDRDDMPDGGAEHIAKTVSYLKES--------------------- 203
Cdd:TIGR00510  81 DVAHGRNPLPPDPEEPAKLAETIKDMGLKYVVITSVDRDDLEDGGASHLAECIEAIREKlpnikietlvpdfrgniaald 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515869651  204 ----------------------KVRdPRANFDQSLRVLKHAKKVQPDVISKTSIMLGLGENDEQVYATMKALREADVDCL 261
Cdd:TIGR00510 161 illdappdvynhnletverltpFVR-PGATYRWSLKLLERAKEYLPNLPTKSGIMVGLGETNEEIKQTLKDLRDHGVTMV 239
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515869651  262 TLGQYMQPTRRHLKVEEYITPEKFKYWEKVGNELGFHYTASGPLVRSSYKAGEFFLKNLVAKR 324
Cdd:TIGR00510 240 TLGQYLRPSRRHLPVKRYVSPEEFDYYRSVALEMGFLHAACGPFVRSSYHADSLFAAGRLVKT 302
PRK12928 PRK12928
lipoyl synthase; Provisional
72-314 1.65e-107

lipoyl synthase; Provisional


Pssm-ID: 237261  Cd Length: 290  Bit Score: 315.32  E-value: 1.65e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515869651  72 ERLRLPPWLKTEIPMGKNYNKLKNTLRNLNLHTVCEEARCPNIGECWGGGeyataTATIMLMGDTCTRGCRFCSVKTARn 151
Cdd:PRK12928  10 PVERLPEWLRAPIGKASELETVQRLVKQRRLHTICEEARCPNRGECYAQG-----TATFLIMGSICTRRCAFCQVDKGR- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515869651 152 PPPLDASEPYNTAKAIAEWGLDYVVLTSVDRDDMPDGGAEHIAKTVSYLKE----------------------------- 202
Cdd:PRK12928  84 PMPLDPDEPERVAEAVAALGLRYVVLTSVARDDLPDGGAAHFVATIAAIRArnpgtgievltpdfwggqrerlatvlaak 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515869651 203 ---------------SKVRdPRANFDQSLRVLKHAKKVQPDVISKTSIMLGLGENDEQVYATMKALREADVDCLTLGQYM 267
Cdd:PRK12928 164 pdvfnhnletvprlqKAVR-RGADYQRSLDLLARAKELAPDIPTKSGLMLGLGETEDEVIETLRDLRAVGCDRLTIGQYL 242
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 515869651 268 QPTRRHLKVEEYITPEKFKYWEKVGNELGFHYTASGPLVRSSYKAGE 314
Cdd:PRK12928 243 RPSLAHLPVQRYWTPEEFEALGQIARELGFSHVRSGPLVRSSYHAGE 289
LIAS_N pfam16881
N-terminal domain of lipoyl synthase of Radical_SAM family; LIAS_N is found as the N-terminal ...
15-111 5.79e-66

N-terminal domain of lipoyl synthase of Radical_SAM family; LIAS_N is found as the N-terminal domain of the Radical_SAM family in the members that are lipoyl synthase enzymes, particularly the mitochondrial ones in metazoa but also those in bacteria.


Pssm-ID: 465296 [Multi-domain]  Cd Length: 97  Bit Score: 202.36  E-value: 5.79e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515869651   15 RVFGRYFCSPVRPLSSLPDKKKELLQNGPDLQDFVSGDLADRSTWDEYKGNLKRQKGERLRLPPWLKTEIPMGKNYNKLK 94
Cdd:pfam16881   1 RVFGSHLCSPASTSSSLPDEKREFLQNGPDLQDFVSGDLSDKSTWAEYKGNLKRPKGERLRLPPWLKTKIPLGKNYNKIK 80
                          90
                  ....*....|....*..
gi 515869651   95 NTLRNLNLHTVCEEARC 111
Cdd:pfam16881  81 NTLRNLNLHTVCEEARC 97
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
133-249 7.54e-10

Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual methylations, isomerization, sulphur insertion, ring formation, anaerobic oxidation and protein radical formation.


Pssm-ID: 427681 [Multi-domain]  Cd Length: 159  Bit Score: 56.77  E-value: 7.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515869651  133 MGDTCTRGCRFCSVKTARNPPP---LDASEPYNTAKAIAEWGLDYVVLTSVDRDDMPDGGAEHIA--------------- 194
Cdd:pfam04055   1 ITRGCNLRCTYCAFPSIRARGKgreLSPEEILEEAKELKRLGVEVVILGGGEPLLLPDLVELLERllklelaegiritle 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515869651  195 --------KTVSYLKES-----------------KVRDPRANFDQSLRVLKHAKKVQPDViSKTSIMLGLGENDEQVYAT 249
Cdd:pfam04055  81 tngtlldeELLELLKEAgldrvsiglesgddevlKLINRGHTFEEVLEALELLREAGIPV-VTDNIVGLPGETDEDLEET 159
 
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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