ID A0A139I141_9PEZI Unreviewed; 831 AA.
AC A0A139I141;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=ABC transporter domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=AC579_9932 {ECO:0000313|EMBL:KXT08349.1};
OS Pseudocercospora musae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX NCBI_TaxID=113226 {ECO:0000313|EMBL:KXT08349.1, ECO:0000313|Proteomes:UP000073492};
RN [1] {ECO:0000313|EMBL:KXT08349.1, ECO:0000313|Proteomes:UP000073492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 116634 {ECO:0000313|EMBL:KXT08349.1,
RC ECO:0000313|Proteomes:UP000073492};
RA Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT link between parallel evolutionary changes in Pseudocercospora fijiensis
RT and Pseudocercospora eumusae and increased virulence on the banana host.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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:KXT08349.1}.
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DR EMBL; LFZO01000458; KXT08349.1; -; Genomic_DNA.
DR EMBL; LFZO01000458; KXT08350.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A139I141; -.
DR STRING; 113226.A0A139I141; -.
DR Proteomes; UP000073492; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 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; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11384:SF59; ATP-BINDING CASSETTE SUB-FAMILY D MEMBER; 1.
DR PANTHER; PTHR11384; ATP-BINDING CASSETTE, SUB-FAMILY D MEMBER; 1.
DR Pfam; PF06472; ABC_membrane_2; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF90123; ABC transporter transmembrane region; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50929; ABC_TM1F; 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};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000073492};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 43..61
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 178..410
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 543..777
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 438..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 812..831
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 763..800
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 816..831
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 831 AA; 93592 MW; AE09D589A7EC4803 CRC64;
MANQSTLRQR PADRFSQWFD YFYERLSNKL QNRSPLDKRT TQLIATLALS LTIITGSYGG
YRLYRRKQKE QDEGRKLLRR NSGLKVKDGT RTLFVPYKDR ASKVVIHPTR PTTFDAHRRF
FLNPIRQRVS GRAIELGAPP SDVKPGLNVA FVHQFLAIMQ IAVPRLGSKE SGLLTMHAFF
LMLRTYLSLV VARMDGEIVR DLIAGEGKAF LFGLTKWLSL GVVASYTNSV IKFLQAKISI
AFRTRLTRYV HDLYLSANMT YYKMHNTDGS IDHGADQFIC QDLTLFCDSA ANLYSSLGKP
FIDLITFNYQ LYKSLGPLAL SGLLSNYFAT AILLKRLSPP FGKLKAAEGR KEGEFRGLHS
RLIANAEEIA FYAGGPTEHE LLDKGFRELR KWMEGIYRVK VGYNMLEDFV LKYTWSALGF
VITSLPVFLP GLNIAPEPRS KSSSNSSIDA AESDEGSDRS GARTKQFITN KRLMLNLADA
GSRMMYSIKD LSELAGQTSR VFMLISTLHR VHANAYHLPR GHQPEPYNLT DVHGTLHKGY
DGVRLEDVPV VAPSPFPMGG EELLENLSFI VGPGDHLLIT GPNGAGKSAV ARIVAGLWPT
YRGLTSRPRE TGQDGIMFLP QKVYLTVGTL RDQVIYPHTE MDMREAGRRE SELQAILEES
KLGYIPDREG GWDTRKTWQD VLSGGEKQRM GIARLLYHEP RYAFIDEGTS AVSSDVEGIL
YETCKRKGIT LITISTRASL KRYHSYTLTL GLGEDANEYE FNRIGTASEK DSVEKEIQEL
REKLSQVEGW KQRRREIDEE LNKVWVAGQE LEAPEYHNGQ NGSSEAETVS L
//