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Database: UniProt
Entry: W9XBN8_9EURO
LinkDB: W9XBN8_9EURO
Original site: W9XBN8_9EURO 
ID   W9XBN8_9EURO            Unreviewed;       440 AA.
AC   W9XBN8;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=lipoyl(octanoyl) transferase {ECO:0000256|ARBA:ARBA00012334};
DE            EC=2.3.1.181 {ECO:0000256|ARBA:ARBA00012334};
DE   AltName: Full=Lipoyl/octanoyl transferase {ECO:0000256|ARBA:ARBA00033331};
DE   AltName: Full=Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase {ECO:0000256|ARBA:ARBA00031131};
GN   ORFNames=A1O3_09871 {ECO:0000313|EMBL:EXJ77643.1};
OS   Capronia epimyces CBS 606.96.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Capronia.
OX   NCBI_TaxID=1182542 {ECO:0000313|EMBL:EXJ77643.1, ECO:0000313|Proteomes:UP000019478};
RN   [1] {ECO:0000313|EMBL:EXJ77643.1, ECO:0000313|Proteomes:UP000019478}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 606.96 {ECO:0000313|EMBL:EXJ77643.1,
RC   ECO:0000313|Proteomes:UP000019478};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Capronia epimyces CBS 606.96.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Protein modification; protein lipoylation via endogenous
CC       pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-
CC       protein]: step 1/2. {ECO:0000256|ARBA:ARBA00004821}.
CC   -!- SIMILARITY: Belongs to the LipB family.
CC       {ECO:0000256|ARBA:ARBA00007907}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EXJ77643.1}.
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DR   EMBL; AMGY01000010; EXJ77643.1; -; Genomic_DNA.
DR   RefSeq; XP_007738153.1; XM_007739963.1.
DR   AlphaFoldDB; W9XBN8; -.
DR   STRING; 1182542.W9XBN8; -.
DR   GeneID; 19173953; -.
DR   eggNOG; KOG0325; Eukaryota.
DR   HOGENOM; CLU_035168_0_0_1; -.
DR   OrthoDB; 166876at2759; -.
DR   UniPathway; UPA00538; UER00592.
DR   Proteomes; UP000019478; Unassembled WGS sequence.
DR   GO; GO:0033819; F:lipoyl(octanoyl) transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR   GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR   GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR004143; BPL_LPL_catalytic.
DR   InterPro; IPR000544; Octanoyltransferase.
DR   InterPro; IPR020605; Octanoyltransferase_CS.
DR   NCBIfam; TIGR00214; lipB; 1.
DR   PANTHER; PTHR10993:SF7; LIPOYLTRANSFERASE 2, MITOCHONDRIAL-RELATED; 1.
DR   PANTHER; PTHR10993; OCTANOYLTRANSFERASE; 1.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
DR   PROSITE; PS01313; LIPB; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019478};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          144..341
FT                   /note="BPL/LPL catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51733"
FT   REGION          38..141
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          348..392
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        54..70
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        71..91
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        105..141
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        370..392
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   440 AA;  47994 MW;  461F5BF01E21F1C7 CRC64;
     MRLAHVHIPH LIPYAHSLRL QNALVERQFA HKDWLRRAAQ RGGEPTSTSE PEKSNHVVHS
     DAEAYKNGRT EHHSTGTGLR SSSSSSGHSP DTDRRPIADG DPSRNLNPNP RNGNRSHTSD
     RVSITGPGSA PNNLTSSWFD LESSPPDPTL LTFSTLPTYT VGRRHLLANP ISSEQQAFLT
     ANGRATFHAS PRGGLLTYHA PGQLTGYIVV DLRRHGITAR CWVRLLEESV IRTCAAWGVP
     TTRTDDPGVW IKDQQPSQEL PVAAHPLSDR KICAIGVQVS RGVTAHGIGL NVFDAALPTS
     TANAYDFTPA QKMSGSYSPL SKGYLSWGFS RIVACGLEGK SVTWLTRERG RDVRPQQSYG
     PGSAPEPNHR EGPSHSQNQS HGRMMESGSS ETPIQLESVG EVFAQELCHG LNSMRGAGKE
     SVDGVYRVQE ADVLSWERKP
//
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