ID A0A0J6YQI9_COCIT Unreviewed; 819 AA.
AC A0A0J6YQI9;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=ATP-dependent permease MDL2 {ECO:0000313|EMBL:KMP10005.1};
GN ORFNames=CIRG_09238 {ECO:0000313|EMBL:KMP10005.1};
OS Coccidioides immitis RMSCC 2394.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=404692 {ECO:0000313|EMBL:KMP10005.1, ECO:0000313|Proteomes:UP000054565};
RN [1] {ECO:0000313|Proteomes:UP000054565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RMSCC 2394 {ECO:0000313|Proteomes:UP000054565};
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
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. ABCB family.
CC Multidrug resistance exporter (TC 3.A.1.201) subfamily.
CC {ECO:0000256|ARBA:ARBA00007577}.
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DR EMBL; DS028100; KMP10005.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J6YQI9; -.
DR STRING; 404692.A0A0J6YQI9; -.
DR Proteomes; UP000054565; 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; cd18573; ABC_6TM_ABCB10_like; 1.
DR CDD; cd03249; ABC_MTABC3_MDL1_MDL2; 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 InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR43394:SF1; ATP-BINDING CASSETTE SUB-FAMILY B MEMBER 10, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43394; ATP-DEPENDENT PERMEASE MDL1, MITOCHONDRIAL; 1.
DR Pfam; PF00664; ABC_membrane; 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 180..206
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 226..253
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 329..348
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 405..427
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 447..468
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 183..470
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 503..740
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 98..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 749..819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 773..795
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 796..813
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 819 AA; 88657 MW; 36BE0A15DBAA49FB CRC64;
MRSPNVLTTF TSRIPSRHVA HQSNTRFTVG SQRLFTRRAI EASRKYRNAH QTLDLRGIER
QGLSTPGSPL LAIKNAVDPS AFAPARLEHV RFLSTSRSIQ EPARPATSAN KSKVAEEPTQ
VVLTEQDDLQ KGFELSEKAS QAAHINLSAK LAKDGLAHGK KAGIREIWRL VKIARPEAKV
LSVAFMFLLA SSSVSMSIPF SIGKILDIAT NPSSEALELF GLSLPWFYGA LAGVLSLGAA
ANYGRIIILR IVGERIVARL RSRLFRRTYV QDAEFFDANR VGDLISRLSS DTIIVGKSIT
QNLSDGLRSA VSGIAGFGMM AYVSLKLSGI LALLFPPVAI AAFFYGRAIR NLSRKIQKNL
GTLTKIAEER LGNVRTSQSF AGERLEVSRY NHQVKRIFEL GKKESFISAT FFSATGFTGN
MTILALLYVG GGMVQSGGIT IGELTSFLMY TVYAGSSMFG LSSFYSELMK GVGAASRLFE
LQDRAPTISP TVGTKVKSAQ GPIRFENVKF SYPTRPAVTI FKDLDFEIPQ GANVAIVGPS
GGGKSTIAAL LLRFYSPNTG KIFIDGKDIT TMNAKSLRRK IGVVSQEPVL FSGTIAENIS
YGKPEATRAE IIVAARKANC QFISDFPDGL DTHVGARGAQ LSGGQKQRIA IARALIKDPD
ILILDEATSA LDAESETLVN SALAALFRGS NTTISIAHRL STIKRSDTII VLDSDGRVAE
QGSYKDLSSR PDGAFTKLME WQMNGGESGM TPVAHYEGSA IRGPPSEAEE LQQMLQEGED
EEYDESGEVE EEEQDQAKQL ESAKSDGEVG ERASAAPKL
//
