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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//