ID G9MDM6_HYPVG Unreviewed; 1017 AA.
AC G9MDM6;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=[acyl-carrier-protein] S-malonyltransferase {ECO:0000256|ARBA:ARBA00013258};
DE EC=2.3.1.39 {ECO:0000256|ARBA:ARBA00013258};
GN ORFNames=TRIVIDRAFT_73127 {ECO:0000313|EMBL:EHK27185.1};
OS Hypocrea virens (strain Gv29-8 / FGSC 10586) (Gliocladium virens)
OS (Trichoderma virens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=413071 {ECO:0000313|EMBL:EHK27185.1, ECO:0000313|Proteomes:UP000007115};
RN [1] {ECO:0000313|EMBL:EHK27185.1, ECO:0000313|Proteomes:UP000007115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gv29-8 / FGSC 10586 {ECO:0000313|Proteomes:UP000007115};
RX PubMed=21501500; DOI=10.1186/gb-2011-12-4-r40;
RA Kubicek C.P., Herrera-Estrella A., Seidl-Seiboth V., Martinez D.A.,
RA Druzhinina I.S., Thon M., Zeilinger S., Casas-Flores S., Horwitz B.A.,
RA Mukherjee P.K., Mukherjee M., Kredics L., Alcaraz L.D., Aerts A., Antal Z.,
RA Atanasova L., Cervantes-Badillo M.G., Challacombe J., Chertkov O.,
RA McCluskey K., Coulpier F., Deshpande N., von Doehren H., Ebbole D.J.,
RA Esquivel-Naranjo E.U., Fekete E., Flipphi M., Glaser F.,
RA Gomez-Rodriguez E.Y., Gruber S., Han C., Henrissat B., Hermosa R.,
RA Hernandez-Onate M., Karaffa L., Kosti I., Le Crom S., Lindquist E.,
RA Lucas S., Luebeck M., Luebeck P.S., Margeot A., Metz B., Misra M.,
RA Nevalainen H., Omann M., Packer N., Perrone G., Uresti-Rivera E.E.,
RA Salamov A., Schmoll M., Seiboth B., Shapiro H., Sukno S.,
RA Tamayo-Ramos J.A., Tisch D., Wiest A., Wilkinson H.H., Zhang M.,
RA Coutinho P.M., Kenerley C.M., Monte E., Baker S.E., Grigoriev I.V.;
RT "Comparative genome sequence analysis underscores mycoparasitism as the
RT ancestral life style of Trichoderma.";
RL Genome Biol. 12:R40.1-R40.15(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=holo-[ACP] + malonyl-CoA = CoA + malonyl-[ACP];
CC Xref=Rhea:RHEA:41792, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78449; EC=2.3.1.39;
CC Evidence={ECO:0000256|ARBA:ARBA00000936};
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:EHK27185.1}.
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DR EMBL; ABDF02000001; EHK27185.1; -; Genomic_DNA.
DR RefSeq; XP_013961395.1; XM_014105920.1.
DR AlphaFoldDB; G9MDM6; -.
DR STRING; 413071.G9MDM6; -.
DR EnsemblFungi; EHK27185; EHK27185; TRIVIDRAFT_73127.
DR GeneID; 25797593; -.
DR VEuPathDB; FungiDB:TRIVIDRAFT_73127; -.
DR eggNOG; KOG2740; Eukaryota.
DR eggNOG; KOG2926; Eukaryota.
DR HOGENOM; CLU_309719_0_0_1; -.
DR InParanoid; G9MDM6; -.
DR OMA; MKRFAGP; -.
DR OrthoDB; 2785720at2759; -.
DR Proteomes; UP000007115; Unassembled WGS sequence.
DR GO; GO:0030131; C:clathrin adaptor complex; IEA:InterPro.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0008152; P:metabolic process; IEA:UniProt.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR CDD; cd14837; AP3_Mu_N; 1.
DR Gene3D; 3.30.450.60; -; 1.
DR Gene3D; 3.30.70.250; Malonyl-CoA ACP transacylase, ACP-binding; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 2.60.40.1170; Mu homology domain, subdomain B; 3.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR036168; AP2_Mu_C_sf.
DR InterPro; IPR018240; Clathrin_mu_CS.
DR InterPro; IPR011012; Longin-like_dom_sf.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR028565; MHD.
DR PANTHER; PTHR42681; MALONYL-COA-ACYL CARRIER PROTEIN TRANSACYLASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR42681:SF1; MALONYL-COA-ACYL CARRIER PROTEIN TRANSACYLASE, MITOCHONDRIAL; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00928; Adap_comp_sub; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF49447; Second domain of Mu2 adaptin subunit (ap50) of ap2 adaptor; 1.
DR SUPFAM; SSF64356; SNARE-like; 1.
DR PROSITE; PS00991; CLAT_ADAPTOR_M_2; 1.
DR PROSITE; PS51072; MHD; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000007115};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 187..491
FT /note="MHD"
FT /evidence="ECO:0000259|PROSITE:PS51072"
FT REGION 431..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1017 AA; 111346 MW; 77E26DD0D967F5FB CRC64;
MNGVIEALHI YDDNRNPILS HTYTGRPLSA SHLLSLYLEH PFPRPSLIYL PNANPPTLVF
SLTHSNLLFL ATSSTEIEPL LVLEFLHRIV DAFEDFVGAP LLAVKLENNY DVVAQLLTEM
CDAGTVSTTE PNALREVVEM EGWVDKLLGS INLPGKNPLN TTSNAPSLIA SNTPALPWRR
ANVRHTSNEL YADVVETLSV TLAPSGRPLA AFANGTIAFT SKVSGVPDVL VTLGSPSGKH
NIGGIMELPV FHPCVRLNKW NERPGELSFI PPDGRFILAG YEVDLLPFTS GKSGSVNSNN
LKLPVTLEMK TGLGPVGSEF EVRLQTNKIF GTPNSSAASQ LARSGVPGIP GRLSSPHPGT
PSSPLLDDLT VTIPLPEDVR NLSDIRPSRG DASFNRAEGR LEWHIPAKEI SGPTSHFGLR
CTVVGSLADD DEEEEFDPTG FGFGTDYSYN EPYQSTPATK KGKEKQGADD EQDPKRVAQN
KILMPSSASV SFSVKGWLAS GLKIESIVID TRKSRGLGEG VKPYKGVKYL TVSKGGHTLA
VSLCVIAPYP SHELLLPSNF DILDSPCHVD SSRVEHEYRA ERRRILRGSN IGCRKAMKRF
AGPVLRSRRG ARVSRDASWL TWASRCCAPA SGGRSVRWSS SRPGRPRTAI FFPGQGVQKV
GMLSPWLEAF PTTASQIIEE IDHCAGFKIS DVIQNGPSKV LTQTTMAQPA IMATSIFILR
ILEREFNFRV ADHFDFTLGH SLGEFTALVA GGYIAFEDSY YLVQRRAAAM SEATKKAIQE
YGGEYGMVAV ITEPEYLQGL IKAIRDFVGH SSDGSKSESN QDVPPIEQVL IANINSKNQI
VLSGNMERIK MLIAHVRQFL GHDPRAVRLH SDSPFHSPIM KPAVTVMKTL LEKKSRVPGR
ENEDIVTFPG LMPCISNVSA RPFQSKEQLK DLLARGCLET VRWWAAIKYL DQEEKVRRWV
GIGPGKVGRN LVGKEVGMRG KDLVKGGGVW AITDPYEVEE VLRGLEETAN ILDDEDE
//
