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Database: UniProt
Entry: A0A1L9R765_ASPWE
LinkDB: A0A1L9R765_ASPWE
Original site: A0A1L9R765_ASPWE 
ID   A0A1L9R765_ASPWE        Unreviewed;       863 AA.
AC   A0A1L9R765;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   03-MAY-2023, entry version 20.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OJJ30756.1};
GN   ORFNames=ASPWEDRAFT_54145 {ECO:0000313|EMBL:OJJ30756.1};
OS   Aspergillus wentii DTO 134E9.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Cremei.
OX   NCBI_TaxID=1073089 {ECO:0000313|EMBL:OJJ30756.1, ECO:0000313|Proteomes:UP000184383};
RN   [1] {ECO:0000313|Proteomes:UP000184383}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DTO 134E9 {ECO:0000313|Proteomes:UP000184383};
RX   PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA   de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA   Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA   Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA   Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA   Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA   Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA   Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA   Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA   Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA   Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA   Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA   Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA   Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA   Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA   Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA   Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA   van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA   Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA   Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA   Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA   Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT   "Comparative genomics reveals high biological diversity and specific
RT   adaptations in the industrially and medically important fungal genus
RT   Aspergillus.";
RL   Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
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; KV878216; OJJ30756.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1L9R765; -.
DR   STRING; 1073089.A0A1L9R765; -.
DR   VEuPathDB; FungiDB:ASPWEDRAFT_54145; -.
DR   OrthoDB; 1358357at2759; -.
DR   Proteomes; UP000184383; Unassembled WGS sequence.
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:SF51; MANGANESE RESISTANCE PROTEIN MNR2; 1.
DR   Pfam; PF01544; CorA; 1.
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   Reference proteome {ECO:0000313|Proteomes:UP000184383};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        800..822
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        837..856
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          1..224
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          263..289
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          308..329
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          420..459
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          473..494
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          683..702
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..34
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        74..88
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        107..141
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        155..169
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        177..196
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        683..701
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   863 AA;  97671 MW;  569C965E93A81CE1 CRC64;
     MAPETTQESR SDSKSGTSKS AKRRKNRNRK RRTRRQSFLA AEEPHAGAAS VPGPDTETTA
     PLAANHPTTP FYKLGRRLSN TSLESEALLD HRNQPMIPPR RDSRLAQSFR PGSSSTPFRS
     GDGGSLNPLS AMRNNNTGND SDDSEAVDDR TPLMRPSSGH TSNLPRYGAD SRSSPYPSRP
     RPASVHTISS RCSPRHNSPM IPEPDRDYDI NNPPSMPTSP KVGPEMGYDD AVVTGAEFDF
     SLARSVENRR GSISLPHDMV IDMDGDETQH SHSDPPSPSS SRPGLQDSLR RRRTVAFPVE
     EDVCLPIAEP SEMAEEDMPQ VSRDGSRRRR RHRQWPDLSI LDEWSREEKE DRHGDFRTKQ
     ISEPMLIEGR LRPQYRTWRR EEDEVPYRFT YFNEEFDSTI HAQTISELVQ PGGSFRDLFI
     PEPPELEDSS DEDDVETDHP IRESTLGTDI HSNGIKTPSN GTYAANHHYN MKNNNGSYDI
     KSNHTPTENK QQPRAHSIIS EAVSDARVSE ARLSAEMPAF KEQQQSKPKR YGPRPAFWLD
     VLCPTDAEMR VIAKAFGIHA LTAEDIMMQE AREKVELFRN YYFVNYRTFE QDPSSENYLQ
     PVNMYVVVFR EGVISFHFSQ TPHPANVRRR IRQLMDYLIL SSDWISYALI DDITDVFGPL
     IQAIEDEVDE IDENIMHMHS LGRTATSSNK EEGNDGVSTS LTPGEMLRRV GESRKKVMGM
     YRLLSNKADV VKGFAKRCNE QWEVAPKSEI GLYLGDIQDH IMTMTSSLTY YETILSRAHS
     NYLAQINILM NERQEQTADV LGKLTVLGTI VLPLNIICGM WGMNVKVPGQ DVDSLDWFWS
     ITAGLILFAI ASFYIAKRVY KIV
//
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