GenomeNet

Database: UniProt
Entry: Q0CC32_ASPTN
LinkDB: Q0CC32_ASPTN
Original site: Q0CC32_ASPTN 
ID   Q0CC32_ASPTN            Unreviewed;       527 AA.
AC   Q0CC32;
DT   17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   17-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   RecName: Full=lipoyl(octanoyl) transferase {ECO:0000256|ARBA:ARBA00012334};
DE            EC=2.3.1.181 {ECO:0000256|ARBA:ARBA00012334};
GN   ORFNames=ATEG_08752 {ECO:0000313|EMBL:EAU30884.1};
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663 {ECO:0000313|EMBL:EAU30884.1, ECO:0000313|Proteomes:UP000007963};
RN   [1] {ECO:0000313|Proteomes:UP000007963}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156 {ECO:0000313|Proteomes:UP000007963};
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) 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   ---------------------------------------------------------------------------
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; CH476606; EAU30884.1; -; Genomic_DNA.
DR   RefSeq; XP_001217338.1; XM_001217337.1.
DR   AlphaFoldDB; Q0CC32; -.
DR   STRING; 341663.Q0CC32; -.
DR   EnsemblFungi; EAU30884; EAU30884; ATEG_08752.
DR   GeneID; 4323525; -.
DR   VEuPathDB; FungiDB:ATEG_08752; -.
DR   eggNOG; KOG0325; Eukaryota.
DR   HOGENOM; CLU_516759_0_0_1; -.
DR   OMA; NEFAPLI; -.
DR   OrthoDB; 166876at2759; -.
DR   UniPathway; UPA00538; UER00592.
DR   Proteomes; UP000007963; Unassembled WGS sequence.
DR   GO; GO:0033819; F:lipoyl(octanoyl) transferase activity; IEA:UniProtKB-EC.
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   InterPro; IPR011576; Pyridox_Oxase_put.
DR   InterPro; IPR012349; Split_barrel_FMN-bd.
DR   NCBIfam; TIGR00214; lipB; 1.
DR   PANTHER; PTHR28040; PYRIDOXAMINE 5'-PHOSPHATE OXIDASE YLR456W HOMOLOG-RELATED; 1.
DR   PANTHER; PTHR28040:SF1; PYRIDOXAMINE 5'-PHOSPHATE OXIDASE YLR456W HOMOLOG-RELATED; 1.
DR   Pfam; PF01243; Putative_PNPOx; 1.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   SUPFAM; SSF50475; FMN-binding split barrel; 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:UP000007963};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          289..501
FT                   /note="BPL/LPL catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51733"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          118..143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          306..327
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   527 AA;  57310 MW;  46E103701862E92C CRC64;
     MADPVNPPLS YEASATTTHP HVATTLPPEV ISSLKNSRFV RGSTCLVSRS LAPSLTKQLH
     LATCDGLQPH ISLMSYTYLP STPYDPYPTI IMTTNPSSRK TNHLLTNPRV SLLVHDWVSH
     RPPTRAPNPG SERDGSPPPA ATRSSLASLL LNLNTSALSS ISTTITGTAR FLEPGSEEEA
     WCKERHLENN TFEEEMSVFG QQQPQQGSRR PSLSIDSDVR VVTVRVREGR IADWKGGVRD
     WVVVREGEEE NQGGLVNGIT SFTRVSNLQQ TLTTRLLAHK KHHDDTTTPP PDPTIITFTP
     NPVYTTGRRD LPPSNTTPQT ASLSLPPSLE PIRSLLTAPN ASSSPGQAEY HPTLRGGQTT
     YHGPGQMVAY TILDLRRLGL TPRCHIRLLE NSVVDVLRGF GVQGLITEDP GVWVSPGTGA
     ATELPRKITA VGVHLRRNIS SYGIGFNVTD EPMWYFRQIV ACGLEGREAT SLQALGVRGA
     SVDDVAERFV RAFVQRVNAD FACGGSRAGE GIEGVYAASE EELLRGD
//
DBGET integrated database retrieval system