ID E4ZI74_LEPMJ Unreviewed; 1277 AA.
AC E4ZI74;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Mitochondrial potassium channel ATP-binding subunit {ECO:0000256|ARBA:ARBA00040439};
DE AltName: Full=ATP-binding cassette sub-family B member 8, mitochondrial {ECO:0000256|ARBA:ARBA00042968};
DE AltName: Full=Mitochondrial sulfonylurea-receptor {ECO:0000256|ARBA:ARBA00041416};
GN ORFNames=LEMA_P057690.1 {ECO:0000313|EMBL:CBX90735.1};
OS Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
OS (Blackleg fungus) (Phoma lingam).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC Plenodomus; Plenodomus lingam/Leptosphaeria maculans species complex.
OX NCBI_TaxID=985895 {ECO:0000313|Proteomes:UP000002668};
RN [1] {ECO:0000313|Proteomes:UP000002668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8
RC {ECO:0000313|Proteomes:UP000002668};
RX PubMed=21326234; DOI=10.1038/ncomms1189;
RA Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P.,
RA Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S.,
RA Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L.,
RA Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J.,
RA Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J.,
RA Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G.,
RA Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H.,
RA Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.;
RT "Effector diversification within compartments of the Leptosphaeria maculans
RT genome affected by Repeat-Induced Point mutations.";
RL Nat. Commun. 2:202-202(2011).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; FP929065; CBX90735.1; -; Genomic_DNA.
DR RefSeq; XP_003834100.1; XM_003834052.1.
DR AlphaFoldDB; E4ZI74; -.
DR STRING; 985895.E4ZI74; -.
DR EnsemblFungi; CBX90735; CBX90735; LEMA_P057690.1.
DR GeneID; 13285425; -.
DR eggNOG; KOG0055; Eukaryota.
DR HOGENOM; CLU_000604_17_2_1; -.
DR InParanoid; E4ZI74; -.
DR OMA; IDVCDTK; -.
DR OrthoDB; 1067095at2759; -.
DR Proteomes; UP000002668; Genome.
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; cd18577; ABC_6TM_Pgp_ABCB1_D1_like; 1.
DR CDD; cd18578; ABC_6TM_Pgp_ABCB1_D2_like; 1.
DR CDD; cd03249; ABC_MTABC3_MDL1_MDL2; 2.
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; 2.
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 InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24221; ATP-BINDING CASSETTE SUB-FAMILY B; 1.
DR PANTHER; PTHR24221:SF643; MITOCHONDRIAL POTASSIUM CHANNEL ATP-BINDING SUBUNIT; 1.
DR Pfam; PF00664; ABC_membrane; 2.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF90123; ABC transporter transmembrane region; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50929; ABC_TM1F; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ion transport {ECO:0000256|ARBA:ARBA00022538};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Potassium {ECO:0000256|ARBA:ARBA00022958};
KW Potassium transport {ECO:0000256|ARBA:ARBA00022538};
KW Reference proteome {ECO:0000313|Proteomes:UP000002668};
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 52..83
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 103..126
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 179..198
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 204..225
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 282..305
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 317..338
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 832..853
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 859..878
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 939..959
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 56..339
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 384..626
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 713..1000
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 1034..1272
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
SQ SEQUENCE 1277 AA; 138046 MW; 384F1780A6053B63 CRC64;
MAATPLPAAL KVADDSETKT ASEQDILAQH IATPNLDISY FQLFRYATKI DIVIIAVSLL
CAIIAGAITT MPALLIGLLI GSIQDNWSGG TSQNESSREL TRFTIYFVYL FVGELVTCYI
ATIGFIRTGI VLSSRIREQY LRALLRQNIA FFDNIGAGEI ATHITADANL IRDGISEKVN
IAVQCTSSIV TAFVISFIKD WKLSLILVSS PLCICIILAL SGLVLTKYRQ RWLGETAEAG
NIAEEVLSSI RTVVGLNAQS ELAARHDEIL ARAERWAVMS RLLTGSVLGA VYAVIYMAIG
LGFWMGSRFL VAGTTSYIDI LTIILATVTG IACLGGIVPP LQVFAVATSA GSRLYSTIDR
KPPGASDPLP TKTLDTVVGR IEFVNVKHIY PSRPDITVLH NLSMVVEPGK TTAIVGPSGS
GKSTIIELIE RFYDPIAGQV LLDGHKLDSL NLNWLRQHVS LVQQSPTLFA TTIFENIRHG
LVGTPHEDAS GEKIHGLVYD AARIANAHDF ISKLPDGYDT LVGEAGVLLS GGQKQRIAIA
RALVRDPKIL LLDEATSALD STSEAIVQAA IDKASQGRTT VVVAHRLSTI KAADHIVVLA
DGRLVEQGTH HALLENNGTY ASLAKTQIIN LDKQNSSDRD VSLEVSNSRI AVDLSEKDNV
ITQDPEKQTC DETQVNANTA KRLETPNKAY RLRTLFKFVL GFHKDHKLLM LQGLLWSIQA
GAGAPVQAVF LAKCLVALAQ SPGNYGQLRS ETNLWAGMHV LIGFAQLFAY TAQAYTLGKC
TEALVRQVSN KILKALLDQN MTFFDMEEHG VGALVSFIST EPSSVAGMGC SVLGALIMAF
TTLIAAVATS IAVGWKLGLV GAATVPVLLI CGFFRYRILA QLDAHLRKSY QETASLAGEA
VTAIRTVMSL NRQERVTGKF HDQLAEQDMR SIRSSLKSSV LYAFSQSAGM LCTALGLWYG
GTLVISGEYN LFQFILSFAA INICGEATGS IFSSSPDLAK AIHSAARLKS LFEQDQTGHS
SCDTETQPLL EGEVDFRGVH FAYPTRPERR ILNGLDLSID KGKYIALVGG SGCGKSTVVA
LVERFYSPLA GTVKIDGIDV ASMDMKAARQ QVVLVDQEPT LFQGTIRQNL LLGLDPSQYT
QQDLEDACKG AHILEFIVSL PNGFDTQCGG KGNNFSGGQK QRLAIARALL RRPKILLLDE
VTSALDSESQ RMVQTALDEA AKERTTIAIA HRLSAIQNAD LICYLENGIV VEAGTHAELI
QRRGRYFAMS SLQSLEG
//
