ID A8PYC7_MALGO Unreviewed; 905 AA.
AC A8PYC7;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE RecName: Full=ABC transporter domain-containing protein {ECO:0000259|PROSITE:PS50893};
GN ORFNames=MGL_1636 {ECO:0000313|EMBL:EDP44239.1};
OS Malassezia globosa (strain ATCC MYA-4612 / CBS 7966) (Dandruff-associated
OS fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX NCBI_TaxID=425265 {ECO:0000313|EMBL:EDP44239.1, ECO:0000313|Proteomes:UP000008837};
RN [1] {ECO:0000313|EMBL:EDP44239.1, ECO:0000313|Proteomes:UP000008837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4612 / CBS 7966 {ECO:0000313|Proteomes:UP000008837};
RX PubMed=18000048; DOI=10.1073/pnas.0706756104;
RA Xu J., Saunders C.W., Hu P., Grant R.A., Boekhout T., Kuramae E.E.,
RA Kronstad J.W., Deangelis Y.M., Reeder N.L., Johnstone K.R., Leland M.,
RA Fieno A.M., Begley W.M., Sun Y., Lacey M.P., Chaudhary T., Keough T.,
RA Chu L., Sears R., Yuan B., Dawson T.L.Jr.;
RT "Dandruff-associated Malassezia genomes reveal convergent and divergent
RT virulence traits shared with plant and human fungal pathogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:18730-18735(2007).
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:EDP44239.1}.
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DR EMBL; AAYY01000004; EDP44239.1; -; Genomic_DNA.
DR RefSeq; XP_001731453.1; XM_001731401.1.
DR AlphaFoldDB; A8PYC7; -.
DR STRING; 425265.A8PYC7; -.
DR GeneID; 5855760; -.
DR KEGG; mgl:MGL_1636; -.
DR VEuPathDB; FungiDB:MGL_1636; -.
DR InParanoid; A8PYC7; -.
DR OMA; CHRTSLW; -.
DR OrthoDB; 7698at2759; -.
DR Proteomes; UP000008837; 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; 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; ATP-BINDING CASSETTE, SUB-FAMILY D MEMBER; 1.
DR PANTHER; PTHR11384:SF69; PEROXISOMAL LONG-CHAIN FATTY ACID IMPORT PROTEIN 1; 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; 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000008837};
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 39..57
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 122..143
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 165..186
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 481..707
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 63..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 733..905
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..80
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 739..761
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 782..835
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 905 AA; 102574 MW; 600E03B2432CAC06 CRC64;
MAAQSRLRTT LDSAKLESIN RLLAFTSLYG RNYASIQRVL RVVYLIGVAC GVILMFAPKS
QNKKSSKKST ANESRKESNR PDAALISPPN AQKKRVAIDR VFYARLFRLL RITFPTWRSA
SFGHLIGLSF TLLLRTLISL YVAELDGRIV SSLVRGDKAL FLRRVVAWMC IAVPAVLTNS
MISFFVNSLS LSIRSRLTNV IQNVYLKNLT FYKLTNLDDR IRNADQLLTV DVQKFSRAIS
LLYGNIFMPM IDSIVYNLRL SQTVGVEMLI MTTTVIRLTA MLVKILTPPF GQYAATEQQL
EGEYRFSHAR LLENAEEIGF YRGQELEKKL IDRSYFSLLK HMNRIFHIRI YYGMMEESIV
KWLWGAIGLV ICSAPVFFKI PGFVTRGIKS DAGSRTETFV TNRRLLLSTS DAFGRVMLSY
KEMSELAGYT SRLTELMEVM DEINSGRAKK RLVTSVGQEA IDQKNEIFSR RGEIIEGTDE
VVFEDVPIVS PNGDVLLEKL SFRIEPGNNL LIIGPNGCGK SSMFRILGGL WPVYGGRVYK
PANHDFTYIP QRPYLSLGSL RDQIIYPDTV DEMHAKGIKD EDLVDILKLL QIDNIVEREG
GWDAEREWRD ALSGGDKQRI AMARLFYHKP KYAILDECTS AVTLEIERIM YEHATDLGIT
MLTVSHRPSL WKYHSHVLQY DGQGGYVFTE LDADKRLKLQ DEKQQLEQNL LLLPKWQERL
RDLQGIKTAH ERLIKSSGHG NQQKESTSQP PKQGESAKQD QTLRQESQKD GSKPEPSQQD
QTSKQESKKD ESKPEPSQQD QTSEKESRIE DSKLEKPKQE SKQRSKDEDS RQEPPKIQNE
IPAAGAKVSQ PPKLKKKASK KSQNLKSPSD PAGEVPSKSP ENGDDKVGKP APAIDFASIH
QHPKK
//
