ID H2AVU6_KAZAF Unreviewed; 1549 AA.
AC H2AVU6;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=ABC transporter domain-containing protein {ECO:0000259|PROSITE:PS50893};
GN Name=KAFR0E03440 {ECO:0000313|EMBL:CCF58496.1};
GN ORFNames=KAFR_0E03440 {ECO:0000313|EMBL:CCF58496.1};
OS Kazachstania africana (strain ATCC 22294 / BCRC 22015 / CBS 2517 / CECT
OS 1963 / NBRC 1671 / NRRL Y-8276) (Yeast) (Kluyveromyces africanus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kazachstania.
OX NCBI_TaxID=1071382 {ECO:0000313|EMBL:CCF58496.1, ECO:0000313|Proteomes:UP000005220};
RN [1] {ECO:0000313|EMBL:CCF58496.1, ECO:0000313|Proteomes:UP000005220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22294 / BCRC 22015 / CBS 2517 / CECT 1963 / NBRC 1671 /
RC NRRL Y-8276 {ECO:0000313|Proteomes:UP000005220};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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 PDR (TC 3.A.1.205) subfamily. {ECO:0000256|ARBA:ARBA00006012}.
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DR EMBL; HE650825; CCF58496.1; -; Genomic_DNA.
DR RefSeq; XP_003957631.1; XM_003957582.1.
DR GeneID; 13883312; -.
DR KEGG; kaf:KAFR_0E03440; -.
DR eggNOG; KOG0065; Eukaryota.
DR HOGENOM; CLU_000604_35_0_1; -.
DR InParanoid; H2AVU6; -.
DR OrthoDB; 5473955at2759; -.
DR Proteomes; UP000005220; Chromosome 5.
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 GO; GO:1990961; P:xenobiotic detoxification by transmembrane export across the plasma membrane; IEA:InterPro.
DR CDD; cd03233; ABCG_PDR_domain1; 1.
DR CDD; cd03232; ABCG_PDR_domain2; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR013525; ABC2_TM.
DR InterPro; IPR029481; ABC_trans_N.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR043926; ABCG_dom.
DR InterPro; IPR034001; ABCG_PDR_1.
DR InterPro; IPR034003; ABCG_PDR_2.
DR InterPro; IPR005285; Drug-R_PDR/CDR.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010929; PDR_CDR_ABC.
DR NCBIfam; TIGR00956; 3a01205; 1.
DR PANTHER; PTHR19241; ATP-BINDING CASSETTE TRANSPORTER; 1.
DR PANTHER; PTHR19241:SF625; ATP-DEPENDENT PERMEASE PDR10-RELATED; 1.
DR Pfam; PF01061; ABC2_membrane; 2.
DR Pfam; PF19055; ABC2_membrane_7; 1.
DR Pfam; PF00005; ABC_tran; 2.
DR Pfam; PF14510; ABC_trans_N; 1.
DR Pfam; PF06422; PDR_CDR; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
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:UP000005220};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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 524..543
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 555..575
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 614..630
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 637..656
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 668..687
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 776..794
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1311..1339
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1360..1384
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1390..1409
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1513..1534
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 163..412
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 904..1147
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 821..885
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 821..839
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 840..885
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1549 AA; 174985 MW; DB93A4DF5235FA70 CRC64;
MYERSVSDSA STISGNSTDS IAQSDSHPYL GFDVNAEDQI RNLARTLTQN SFVSSNTNLS
RITSNATAVS TGLSFIPTEG INPINDNEEP ENYNSKLDPN SDDFSSKAWV KNMANIATSE
PEYYKPYSLG CVWQNLAASG DSADVAYQST FANLPLKLLG SLLRLCRPTK ESEIFQILKP
MDGCLNPGEL LVVLGRPGSG CTTLLKSISS NTHGFNIAKD STISYNGIIP KELKKYYRGE
VVYQAESDVH LPHLTVYQTL VTVAKLKTPE NRIKGVTREA FANHLADVAM ATYGLLHTRD
TKVGDEYVRG VSGGERKRVS IAEVWICGAK FQCWDNATRG LDSATALEFV RALKTQAEIA
NRTATVAIYQ CSQDAYDLFD KVCVLYEGYQ IFYGSTQKAK QYFLDMGYTC PPRQTTADFL
TSITSPAERI VNQDFVNQGK NVPQTPKEMN DYWMQSQIYE ELKDEINTVL NKDNVKNKEA
MKESHIAKQS NKLRSTSPYV VNYGMQIKYL LTRNIWRMKN NPSITLFQVF GNSGIAFILG
SMFYKVMLHT TTATFYYRGA AMFFAVLFNA FSALLEIFKL YEARPITEKH RTYALYHPSA
DAFASIISEI PPKIATAIMF NIVFYFLVNF RRTAGSFFFY FLISIVAVFA MSHLNRCIGA
LTKTLQEAMV PASLLLLALG MYTGFVIPRT KMLGWSRWIW YINPLAYLFE SLMVNEFHDR
WFPCSSFVPS GPAYQNISGT ERVCSVVGAR AGYDSVLGDD YINESFQYEH IHKWRGFGIG
MAYIIFFLIL YLILCELNEG AKQKGEMLVF PKAVVRRMKR QGQISDKNER EEEKYDVEKT
GSANTYTTDS SMVRDTDVST SPSYAHQGNK AASSNPSSIN STLAKDPTTV SEDYINLAKS
ESIFHWRDLC YDIKIKTETR RILNKVDGWV KPGTLTALMG ASGAGKTTLL DCLAERVTMG
VITGNIFVDG RLRDESFPRS IGYCQQQDLH LKTATVRESL RFSAYLRQPA SVTKEEKDHY
VEEVIKILEM ETYADAVVGI PGEGLNVEQR KRLTIGVELA AKPKLLVFLD EPTSGLDSQT
AWSTCQLMRK LANHGQAILC TIHQPSAILM QEFDRLLFLQ KGGKTVYFGD LGKGCKTMIE
YFEKHGAQAC PPDANPAEWM LEVVGAAPGS HAKQDYYKVW RESDEYRSVQ EELDHMEKEL
PLKTTEADSE QKKEFGTKIP YQFKLVSLRL FQQYWRTPDY LWSKFLLTIF NQLFIGFTFF
KADRSLQGLQ NQMLSMFMYT VILNPLIQQY LPSFVQQRDL YEARERPSRT FSWVSFFCAQ
IVVEVPWNIL AGTISYCIYY YSVGFYNNAS QANQLHERGA LFWLLSCAYY VYIGSLALLT
ISFLEVADNA AHLASLMFSM ALSFCGVMVQ SSQMPGFWIF MYRVSPLTYF IDAFLSTGVA
NVDIECATYE LVQFSPPSGE TCGEYMEAYI SYTGTGYLAD PNSTTQCNFC SYSKTNSYLS
QVGSAYYRRW RNYGIFLCYI IFNYVAGFFL YWLARVPKKT GKISGGAKN
//
