ID B9WDK5_CANDC Unreviewed; 1013 AA.
AC B9WDK5;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 63.
DE SubName: Full=Magnesium transporter, putative {ECO:0000313|EMBL:CAX42761.1};
GN OrderedLocusNames=Cd36_82340 {ECO:0000313|CGD:CAL0000160196};
GN ORFNames=CD36_82340 {ECO:0000313|EMBL:CAX42761.1};
OS Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 /
OS NRRL Y-17841) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=573826 {ECO:0000313|EMBL:CAX42761.1, ECO:0000313|Proteomes:UP000002605};
RN [1] {ECO:0000313|EMBL:CAX42761.1, ECO:0000313|Proteomes:UP000002605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841
RC {ECO:0000313|Proteomes:UP000002605};
RX PubMed=19745113; DOI=10.1101/gr.097501.109;
RA Jackson A.P., Gamble J.A., Yeomans T., Moran G.P., Saunders D., Harris D.,
RA Aslett M., Barrell J.F., Butler G., Citiulo F., Coleman D.C.,
RA de Groot P.W.J., Goodwin T.J., Quail M.A., McQuillan J., Munro C.A.,
RA Pain A., Poulter R.T., Rajandream M.A., Renauld H., Spiering M.J.,
RA Tivey A., Gow N.A.R., Barrell B., Sullivan D.J., Berriman M.;
RT "Comparative genomics of the fungal pathogens Candida dubliniensis and
RT Candida albicans.";
RL Genome Res. 19:2231-2244(2009).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the CorA metal ion transporter (MIT) (TC 1.A.35)
CC family. {ECO:0000256|ARBA:ARBA00009765}.
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DR EMBL; FM992690; CAX42761.1; -; Genomic_DNA.
DR RefSeq; XP_002419172.1; XM_002419127.1.
DR AlphaFoldDB; B9WDK5; -.
DR GeneID; 8046656; -.
DR KEGG; cdu:CD36_82340; -.
DR CGD; CAL0000160196; Cd36_82340.
DR VEuPathDB; FungiDB:CD36_82340; -.
DR eggNOG; ENOG502QPTQ; Eukaryota.
DR HOGENOM; CLU_007127_6_0_1; -.
DR OrthoDB; 1358357at2759; -.
DR Proteomes; UP000002605; Chromosome 3.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015095; F:magnesium ion transmembrane transporter activity; IEA:InterPro.
DR CDD; cd12829; Alr1p-like; 1.
DR Gene3D; 3.30.460.20; CorA soluble domain-like; 1.
DR Gene3D; 1.20.58.340; Magnesium transport protein CorA, transmembrane region; 2.
DR InterPro; IPR044089; Alr1-like.
DR InterPro; IPR045861; CorA_cytoplasmic_dom.
DR InterPro; IPR045863; CorA_TM1_TM2.
DR InterPro; IPR002523; MgTranspt_CorA/ZnTranspt_ZntB.
DR PANTHER; PTHR21535; MAGNESIUM AND COBALT TRANSPORT PROTEIN/MITOCHONDRIAL IMPORT INNER MEMBRANE TRANSLOCASE SUBUNIT TIM8; 1.
DR PANTHER; PTHR21535:SF55; MAGNESIUM TRANSPORTER ALR1-RELATED; 1.
DR Pfam; PF01544; CorA; 2.
DR SUPFAM; SSF143865; CorA soluble domain-like; 1.
DR SUPFAM; SSF144083; Magnesium transport protein CorA, transmembrane region; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 885..908
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 920..945
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 34..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 434..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 724..746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 774..822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..55
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..192
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..467
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 791..809
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1013 AA; 112410 MW; 1B10D37C52B421F2 CRC64;
MSDSESYYQN STTNQPILHS DEVLNDHRNQ IINDCAISDG DDNDNDNDND EVELEVEVEK
QQQQQEQQQE INPENVKPLT HKSGSSIKKK SHIIKENKDK DKEKVKVKVP NPMGLSSYDD
NIIGGSGGSG HYKNRNYNMS TLRKEFYLKD TNDDDDDDNN NNNNSTNNTN TTHLQIPTPI
ITNSNKSRRK SQLDNLPPLI KKKTIGRNNS NNFENDLVSP MTKMKTNDSE DITNPTTNPT
TTGIKLGIGA TTLGAGIAPG ATGTGTATGI GTATATATGR RPSRSSIDSE ADSHASRSSQ
ETEEDVCFPM VGDHIRVNGI DFDEIDEFIR EEREEALLQK QMIAKNISRI DEFQNLSNTT
SGASRHPYHS NNNNNNNKKG NNNNYSGGGS GGSSIAALKY TPKNILKKTL SRFEITHENS
SSSDEIYELK NHHFHHQKSP KYDDNDDDDD QLSLTSSSSS SSGQVKFGGA RISDGINGGS
LPDRFSLFHS ESEETIHAPD IPSLVSSSSS SSSGQSISVR DLFRNGEETW WLDCTCPTDS
EMKMLAKAFG IHPLTAEDIR MQETREKVEL FKSYYFVCFH TFEADKESED YLEPINVYIV
VFHDGILTFH FSPINHPANV RRRVRQLRDY VDVSADWLCY ALIDEITDGF APVIHGIEYE
ADAIEDAVFT ARDTDFSSML QRIGESRRKV MTLMRLLSGK ADVIKMFAKR CQEEANSGYY
QRQYNNNNNN NHLHHQHQHQ HQQTHHTLPT NIITSPITST LNLNNLTTST STGGGALGVN
FGPNPNPNPN LNPVGGNNNN NNNTNSPSPP QQPKDFPLGT GKSLLIPDAR PRADIALYLG
DIQDHIITMF QNLLAYEKIF SRSHSNYLAQ LQVESFNSNN KITEMFSKIT LIGTMLVPLN
LVTGLFGMNV RVPGEGGNNL GWFFGIVGVL IFIIIGSFIF AQWWLKKLNN SIEGQKKINR
PIFNHSSRRS IRSLGLRKHG NARGGNGNGN GNGGAGVGVG ANKSIISFPN KYE
//
