ID M1VXK9_CLAP2 Unreviewed; 1024 AA.
AC M1VXK9;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=[acyl-carrier-protein] S-malonyltransferase {ECO:0000256|ARBA:ARBA00013258};
DE EC=2.3.1.39 {ECO:0000256|ARBA:ARBA00013258};
GN ORFNames=CPUR_07126 {ECO:0000313|EMBL:CCE33202.1};
OS Claviceps purpurea (strain 20.1) (Ergot fungus) (Sphacelia segetum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Claviceps.
OX NCBI_TaxID=1111077 {ECO:0000313|EMBL:CCE33202.1, ECO:0000313|Proteomes:UP000016801};
RN [1] {ECO:0000313|EMBL:CCE33202.1, ECO:0000313|Proteomes:UP000016801}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=20.1 {ECO:0000313|EMBL:CCE33202.1,
RC ECO:0000313|Proteomes:UP000016801};
RX PubMed=23468653; DOI=10.1371/journal.pgen.1003323;
RA Schardl C.L., Young C.A., Hesse U., Amyotte S.G., Andreeva K., Calie P.J.,
RA Fleetwood D.J., Haws D.C., Moore N., Oeser B., Panaccione D.G.,
RA Schweri K.K., Voisey C.R., Farman M.L., Jaromczyk J.W., Roe B.A.,
RA O'Sullivan D.M., Scott B., Tudzynski P., An Z., Arnaoudova E.G.,
RA Bullock C.T., Charlton N.D., Chen L., Cox M., Dinkins R.D., Florea S.,
RA Glenn A.E., Gordon A., Gueldener U., Harris D.R., Hollin W., Jaromczyk J.,
RA Johnson R.D., Khan A.K., Leistner E., Leuchtmann A., Li C., Liu J., Liu J.,
RA Liu M., Mace W., Machado C., Nagabhyru P., Pan J., Schmid J., Sugawara K.,
RA Steiner U., Takach J.E., Tanaka E., Webb J.S., Wilson E.V., Wiseman J.L.,
RA Yoshida R., Zeng Z.;
RT "Plant-symbiotic fungi as chemical engineers: Multi-genome analysis of the
RT Clavicipitaceae reveals dynamics of alkaloid loci.";
RL PLoS Genet. 9:E1003323-E1003323(2013).
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:CCE33202.1}.
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DR EMBL; CAGA01000053; CCE33202.1; -; Genomic_DNA.
DR AlphaFoldDB; M1VXK9; -.
DR STRING; 1111077.M1VXK9; -.
DR VEuPathDB; FungiDB:CPUR_07126; -.
DR eggNOG; KOG2740; Eukaryota.
DR eggNOG; KOG2926; Eukaryota.
DR HOGENOM; CLU_309719_0_0_1; -.
DR OrthoDB; 2785720at2759; -.
DR Proteomes; UP000016801; 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; 1.
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; IPR022775; AP_mu_sigma_su.
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 Pfam; PF01217; Clat_adaptor_s; 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:UP000016801};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 209..564
FT /note="MHD"
FT /evidence="ECO:0000259|PROSITE:PS51072"
FT REGION 356..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 471..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 596..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..611
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1024 AA; 111577 MW; 29570C888341EB1B CRC64;
MNGVIEALHI YDENRLAFVT PRANSESLTR AYSSSAILSH TYTGRPLPAT HLLALYLEHP
TPRPNLIYLP NTSPATLVFS LIHANLLFLV TSSTEIEPLL VLEFLHRVVD VLEDFIGAPL
LALKIEQNYH VVAQLLTEMC DAGTISTTEP NALRENVEIE GWMGKLLGSI NLPGKSPLSS
NFSNAPTPAL PITNTPALPW RRANVRHTSN ELYADVIETL SVTLAPSGRP LAAFANGSIA
FTAKVSGVPD VTVSLSSPSG VHNIGSIMEL PVFHPCVRLN RWQERPGQLS FIPPDGRFIL
AGYQVDLLPF AGETSGNIRA NKLNLPVSLE IKTGLGPTGA EFEVRLQVNK TLGSQTSSSQ
LNQYGRGIGS GRLGAPHPGS PGAPLVDEVT VTVPLPEDVR NLSDIRPSRG DASFYPRERM
LEWRVPAKEL AGPTSHFGLR CTVGGIIVDE GEDFDPSGFA LSGTDHSSYN ESYQSYSAAD
PAASEEGAKT DQGGQQDAKK VAQNKMLMPS SAMVSFSVKG WLASGLKVDS IMIDARKSRG
LGEGVKPYKG VKYLTVTAVC FALEGVVPRH QRRPVRHAGA HLLGLSAWEA GRMKNMTKDD
DRCRPRPWDD PDGRGQPSSF PVRNAVQTCK NTSTMDGQAM LGITKRNQVT NSCEHCISRN
KAGQGTQKVG MLNPWLEAFP TTAKEIIQEA DHYAGFKLSD VIRDGPSKLL TQTTNAQPAI
MATSIVILKI LEREFDVKVA DRFDVTLGHS LGEFAALVAG GYMDFQDSLY MVTRRAAAMS
DATKKAVQEY GGEYGMVAIV TEPEYLRELI AAIREFVGHS SAGSKAESSE DVPPIEQVLI
ANINSKNQIV LSGNLERIAT LMAHVRQFLG HEPRAVRLHS DSPFHSPIMK PAVSVMHDLL
ESRSRVPGRE REDIINFPGD IPCISNVTAR PFKSREQLKD LLARGCLETV RWWDSIRYLD
QQEKVRRWVG IGPGKVGRNL VGKEVGMRGK DLVKGGGVWA ITDPMDVEEV LRGLQETDGV
VDEA
//
