ID A0A072PKW3_9EURO Unreviewed; 1141 AA.
AC A0A072PKW3;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KEF60521.1};
GN ORFNames=A1O9_02082 {ECO:0000313|EMBL:KEF60521.1};
OS Exophiala aquamarina CBS 119918.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1182545 {ECO:0000313|EMBL:KEF60521.1, ECO:0000313|Proteomes:UP000027920};
RN [1] {ECO:0000313|EMBL:KEF60521.1, ECO:0000313|Proteomes:UP000027920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 119918 {ECO:0000313|EMBL:KEF60521.1,
RC ECO:0000313|Proteomes:UP000027920};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala aquamarina CBS 119918.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:KEF60521.1}.
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DR EMBL; AMGV01000002; KEF60521.1; -; Genomic_DNA.
DR RefSeq; XP_013263111.1; XM_013407657.1.
DR AlphaFoldDB; A0A072PKW3; -.
DR STRING; 1182545.A0A072PKW3; -.
DR GeneID; 25277027; -.
DR VEuPathDB; FungiDB:A1O9_02082; -.
DR HOGENOM; CLU_003599_0_0_1; -.
DR OrthoDB; 2477520at2759; -.
DR Proteomes; UP000027920; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046873; F:metal ion transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015693; P:magnesium ion transport; IEA:UniProt.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 3.
DR Gene3D; 1.20.58.340; Magnesium transport protein CorA, transmembrane region; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR045863; CorA_TM1_TM2.
DR InterPro; IPR002523; MgTranspt_CorA/ZnTranspt_ZntB.
DR PANTHER; PTHR24173; ANKYRIN REPEAT CONTAINING; 1.
DR PANTHER; PTHR24173:SF74; UVEAL AUTOANTIGEN WITH COILED-COIL DOMAINS AND ANKYRIN REPEATS; 1.
DR Pfam; PF12796; Ank_2; 3.
DR Pfam; PF01544; CorA; 1.
DR SMART; SM00248; ANK; 9.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF144083; Magnesium transport protein CorA, transmembrane region; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 2.
DR PROSITE; PS50088; ANK_REPEAT; 3.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000027920};
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}.
FT TRANSMEM 936..958
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 978..1002
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REPEAT 78..114
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 115..147
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 224..256
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 462..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1020..1047
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1080..1141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 829..856
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 521..537
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1080..1109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1111..1133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1141 AA; 129054 MW; 7A543B35422C5AA8 CRC64;
MSQPPGVGLD PRQVRVAFAK AIKPDEAAEL KNLLENPDLV RHTDENYLRE LLGRAISYGN
DLAVELLLQA GAKTDVTAGN GPIHRSIRSQ KNKTRNIIIN LLLDYNSDIE FRDTEGKTPF
IAAALRGQAE TVATLLARGA NADAVDYHGR NILHRMASEV PPTVKWNSDM LSLILSRLKD
FELRDNENRT PLLWAAAKGS LQLAGVLLPS KGKRLADISV ANDQGHTALH LAAKNDQPAM
VKLLLNSGAN IEARSDGRWT PLLMAAKAGS EAAIDALLTH TQSANINART STGMTALHWA
AEKGKLAAVQ RILKVPHAYK NAKDSSDSTP LIRAAHNGHW EIVDALRHHV LEGPTKRATR
KACERFKAAV VSFFFDQKGP RGLKSKVDKY TVWQVLYERV KDTDKFAIPT VFENIETKKP
DFRWIHLPAN NISWLEALLT KHFLEGESRD LSALKSVLRL MGQQQHRGRK VHSRFMRPSC
KRIGLGSRRP ADVASAASRR SSHSNRGEIN AALHGSYRPP TREPPIQPPP TVPQSQLQPQ
RPPQLQEEDM MVLFLPYLHW ETDKNRKALT ESIKGPPGNT DSLEDSQMWQ IPKDTLLIHG
YPVTQSTDLH PRRTLDQFKH HSTDTDPQDV DQVVYRYCDN NKQELKVYMV DQLWLFIIGD
LLITCFPERW GQPRRDPLNL FDGIVEDINS TTRPPIRSVH ELATLVTERC CGIFDRHQWD
NDELLFAEMF ELSIGLLTLK ETALFRRFKS DSVVAAHWLR AHGKSSAIYE QQLIEAQEAY
VSEQELYATD ADVAAMLGQD GWRERDTDAE EFVNKLLNID EEAALLVECK DIEDELDILA
NILRQQKQAL RNMEDVFRTS KLVPYDKRID LYVQLEEQQR NLDADILDIT RMTQQARSVN
ENLTQVLDLK QKHANAVEAR FQRYQAQEAT RQGQTIMVFT VVTIVFLPLS FLASLFTINI
IEFPRPRNAD GGELHLGWVL KWILGIGLGV SVPLILFAFV VGDVKAWWVE RRLNKYHTKR
RQIGQRQQQW DESSEKGENP PDEGFSWTRN ILRSRRSHAS KDGTGDEALN ATTTIIQPRS
SKYSVVNTQP TTIPTPGRKP MSSMESQDRA ANPFRRLRRS ATERTEKSVA TEDLEVGRAY
G
//
