ID V2XGZ4_MONRO Unreviewed; 827 AA.
AC V2XGZ4;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE SubName: Full=Atp-binding cassette transporter {ECO:0000313|EMBL:ESK91755.1};
GN ORFNames=Moror_10584 {ECO:0000313|EMBL:ESK91755.1};
OS Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS (Crinipellis roreri).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK91755.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK91755.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK91755.1,
RC ECO:0000313|Proteomes:UP000017559};
RX PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT mechanisms of the biotrophic and necrotrophic phases.";
RL BMC Genomics 15:164-164(2014).
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCD family.
CC Peroxisomal fatty acyl CoA transporter (TC 3.A.1.203) subfamily.
CC {ECO:0000256|ARBA:ARBA00008575}.
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:ESK91755.1}.
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DR EMBL; AWSO01000321; ESK91755.1; -; Genomic_DNA.
DR RefSeq; XP_007848923.1; XM_007850732.1.
DR AlphaFoldDB; V2XGZ4; -.
DR STRING; 1381753.V2XGZ4; -.
DR KEGG; mrr:Moror_10584; -.
DR HOGENOM; CLU_007587_1_1_1; -.
DR OrthoDB; 7698at2759; -.
DR Proteomes; UP000017559; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR CDD; cd03223; ABCD_peroxisomal_ALDP; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11384; ATP-BINDING CASSETTE, SUB-FAMILY D MEMBER; 1.
DR PANTHER; PTHR11384:SF56; PEROXISOMAL LONG-CHAIN FATTY ACID IMPORT PROTEIN 2; 1.
DR Pfam; PF06472; ABC_membrane_2; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:ESK91755.1};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000017559};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 555..796
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 514..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 799..826
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 514..531
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 827 AA; 92731 MW; 510C35A7BB1F15F5 CRC64;
MSSAVFSKPL RPDQLFSLVR RHKSTSQVVF VVLLILRSRL VPSLSFKHRK DDEKKGLTAH
ELGVVLQTLY TEDEEKKGRK EILVPYNNRL TRVPYDPTPQ EFIDINQEAF LQQPSQDAEP
TEKAQKKKHL FDPVFLRTLR LLLFRIVFPL PNKPSLFSTL TSPVTLTVSA YTTFLILRTY
LSLLVAKLDG IIVRDLVRAD GRGFAKGLAL WYILAVPSIL VNVMIRHMQG VLSEEVRGRL
TRFITDLYLG VPGAKERALR CVLSHDPQSS SSVATEGVDQ YITSDIEAFS EGLSGLYGNL
LKPSLDLLLF TSQLSRSLGV RGTVMLFGTY WATVHTLRAL SPAFGRLSAV EARLEGEYRA
GMGRLGRGSE EVAFYDGGAR ERDILTRAYM RLIKHVNSIY KIRIAYEWTE DYVIKYLWSA
AGYGLIAVPL LFTRALGISP AFTTRDGTSY ASRIASRTQT YISNRRLLLS LADAGGRLMY
AYKDILEMQG VVGRLGGVIG ELYACVLPPS NTDTPEVTVT PPSAESSHII NATPSEEKEE
PEEEKEDDDD ESIVLRHVDI TIPGTSTVLV KDLSLKLRRG EHLMITGSNG VGKTSVCRVL
GGLWEAEGNG VVKTPEGNKV MFIPQRTYHP QGTLLDQVIY PYTYQEFLGR WRERRAAGET
TDADPLAEIE EILHAVYLGY LPEREGGWLT RKEWRDVLSG GEKQRISLAR VLYHRPLFAV
LDEATSAVSS DVEGRLYETI KGWGKGIGVV SVSLRPSLQK YHTHQLTIHG DGSGGWEFTQ
LSSVDTQISK NNQAEIEELE ARLLEVEEWE RRVEELDAML RIHEVET
//