ID A0A2S5B6M5_9BASI Unreviewed; 1113 AA.
AC A0A2S5B6M5;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=ABC transporter domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=BMF94_4260 {ECO:0000313|EMBL:POY72434.1};
OS Rhodotorula taiwanensis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=741276 {ECO:0000313|EMBL:POY72434.1, ECO:0000313|Proteomes:UP000237144};
RN [1] {ECO:0000313|EMBL:POY72434.1, ECO:0000313|Proteomes:UP000237144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD1149 {ECO:0000313|EMBL:POY72434.1,
RC ECO:0000313|Proteomes:UP000237144};
RX PubMed=29375494;
RA Tkavc R., Matrosova V.Y., Grichenko O.E., Gostincar C., Volpe R.P.,
RA Klimenkova P., Gaidamakova E.K., Zhou C.E., Stewart B.J., Lyman M.G.,
RA Malfatti S.A., Rubinfeld B., Courtot M., Singh J., Dalgard C.L.,
RA Hamilton T., Frey K.G., Gunde-Cimerman N., Dugan L., Daly M.J.;
RT "Prospects for Fungal Bioremediation of Acidic Radioactive Waste Sites:
RT Characterization and Genome Sequence of Rhodotorula taiwanensis MD1149.";
RL Front. Microbiol. 8:2528-2528(2018).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family.
CC Eye pigment precursor importer (TC 3.A.1.204) subfamily.
CC {ECO:0000256|ARBA:ARBA00005814}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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:POY72434.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PJQD01000048; POY72434.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S5B6M5; -.
DR STRING; 741276.A0A2S5B6M5; -.
DR OrthoDB; 359054at2759; -.
DR Proteomes; UP000237144; 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; cd03213; ABCG_EPDR; 1.
DR CDD; cd00055; EGF_Lam; 1.
DR Gene3D; 2.10.25.10; Laminin; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR013525; ABC2_TM.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR043926; ABCG_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR002049; LE_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR48041; ABC TRANSPORTER G FAMILY MEMBER 28; 1.
DR PANTHER; PTHR48041:SF139; PROTEIN SCARLET; 1.
DR Pfam; PF01061; ABC2_membrane; 1.
DR Pfam; PF19055; ABC2_membrane_7; 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.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000237144};
KW Signal {ECO:0000256|SAM:SignalP};
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 SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1113
FT /note="ABC transporter domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015597502"
FT TRANSMEM 368..392
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 857..880
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 892..913
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 934..958
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 970..993
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1000..1022
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1089..1109
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 93..129
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 438..679
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 712..765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 808..827
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 743..757
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 119..128
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1113 AA; 121258 MW; 2A761C940E613326 CRC64;
MRPLQLGWAA TALLSTSLAS NSLAQVLQES NSAPKAAVWP DRPAIADSSL PPHLNSTTGR
RRIQAYQHQL AAPALFADAS AYGERPPECP PCNPFNCVLP AFPCLNTGKC NDYNGQCICQ
PGFGGEDCSK PLCGSLADGH ERYPREGDQC ECQEGWTGLN CNVCETDESC EDLITRDSPP
SLRGGGSTPD DDLDRPVCYK EGFGVKEMYQ MCDVTNRKIL DMLPDRPPQV TFTCDIPSET
CGFQFWIGRV ESFYCGLSNC TASRDVQYGS NTTEYKCDKV ECACIPGRML CGENGSVDIT
DFLAEEIKGP GKFTTKTGEA SKFEEPAMNQ LINDIFGDTY ITLKCNSGEC MRRGSVPGFM
PPRKPSSIVW LGVSIISVVA VLILGLFLFW YFGRGSSTAE YSFLGGRIRL PTNGHGPNGG
AAAVSGKSLL EDHIPTALQF SDLSYTLTSG KRVLDGISGA VQPGEIMAVL GASGAGKSTF
LDLLARKAKR GSVQGDILVN GRTVSSTEYR RVVGFVDQED TLMGTLTVYE TVLYSALLRL
PRDMSFEDKR LRTLETMHEL GILGIRNSRV GESGARGISG GEKRRVSIAC ELVTSPSILF
LDEPTSGLDS YNAFNVIEAL VQLARTYKRT VVFTIHQPQS NIVALFDKLI LLARGKVVYS
GRADESQAYF QKIGCDCPPG FNIADYLIDL TMQNEKSGQS DATVADALNQ LEHRNGSPNG
RGRNGNDPEL GGPSSGSTTA ASDSDLDERR TEPDTPTRGG HGLKQFLPSA VSGQATSHES
SLSPELARLV AAFSTSSISE ATRKEISQAK AAGATRGAGG GTDPRDLSLR NYKRASPWSQ
FKILSGRSFK NLYRDPMLML SHYAVAVIAA GICAFLFRGL TEDIPGFQNR MGMIFFSLAL
FGFGCLTTLS TFASERLLFT RERANGYYNP ATYFAAKLLF DIIPLRVIPA FLFGAIVYAP
VGLVPEIVSF WRFILVLVLF NLTASSVVLL LSIVIKNAGV ANLIGSLVML FNLLFAGLLI
NRDKLPRWLR WLETFSFFHA AFEALLVNEV RYLQLKDHRY GVDIEVPAAT ILSMFGFNAQ
AFWFPDVTLL LACFGGFVVL SYVCLVVLVR ERR
//
