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Database: UniProt
Entry: A0A1V6Q525_9EURO
LinkDB: A0A1V6Q525_9EURO
Original site: A0A1V6Q525_9EURO 
ID   A0A1V6Q525_9EURO        Unreviewed;       586 AA.
AC   A0A1V6Q525;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Magnesium transporter {ECO:0000256|RuleBase:RU366042};
GN   ORFNames=PENANT_c015G09240 {ECO:0000313|EMBL:OQD83886.1};
OS   Penicillium antarcticum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=416450 {ECO:0000313|EMBL:OQD83886.1, ECO:0000313|Proteomes:UP000191672};
RN   [1] {ECO:0000313|Proteomes:UP000191672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 31811 {ECO:0000313|Proteomes:UP000191672};
RX   PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA   Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA   Frisvad J.C., Workman M., Nielsen J.;
RT   "Global analysis of biosynthetic gene clusters reveals vast potential of
RT   secondary metabolite production in Penicillium species.";
RL   Nat. Microbiol. 2:17044-17044(2017).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion
CC       inner membrane {ECO:0000256|RuleBase:RU366042}; Multi-pass membrane
CC       protein {ECO:0000256|RuleBase:RU366042}.
CC   -!- SIMILARITY: Belongs to the CorA metal ion transporter (MIT) (TC 1.A.35)
CC       family. {ECO:0000256|ARBA:ARBA00009765, ECO:0000256|RuleBase:RU366042}.
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:OQD83886.1}.
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DR   EMBL; MDYN01000015; OQD83886.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V6Q525; -.
DR   STRING; 416450.A0A1V6Q525; -.
DR   OrthoDB; 73031at2759; -.
DR   Proteomes; UP000191672; Unassembled WGS sequence.
DR   GO; GO:0005743; C:mitochondrial inner 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   CDD; cd12823; Mrs2_Mfm1p-like; 1.
DR   Gene3D; 2.40.128.330; -; 1.
DR   Gene3D; 1.20.58.340; Magnesium transport protein CorA, transmembrane region; 1.
DR   InterPro; IPR002523; MgTranspt_CorA/ZnTranspt_ZntB.
DR   InterPro; IPR039204; MRS2-like.
DR   PANTHER; PTHR13890:SF26; MAGNESIUM TRANSPORTER MRS2 HOMOLOG, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR13890; RNA SPLICING PROTEIN MRS2, MITOCHONDRIAL; 1.
DR   Pfam; PF01544; CorA; 1.
PE   3: Inferred from homology;
KW   Ion transport {ECO:0000256|RuleBase:RU366042};
KW   Magnesium {ECO:0000256|RuleBase:RU366042};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU366042};
KW   Mitochondrion {ECO:0000256|RuleBase:RU366042};
KW   Mitochondrion inner membrane {ECO:0000256|RuleBase:RU366042};
KW   Reference proteome {ECO:0000313|Proteomes:UP000191672};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU366042};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU366042};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU366042}.
FT   TRANSMEM        408..426
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU366042"
FT   TRANSMEM        438..460
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU366042"
FT   REGION          523..586
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        535..554
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        562..576
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   586 AA;  64629 MW;  79D535C9789B86C1 CRC64;
     MLSPKLSAPS ASLLRFLHTQ SGFTTAPACA RPKRLGRDKP FSTVRASKLP SWTHPTTLCP
     ARNDGAANGR SSAIRPMLVP SMPTQVTFSR LASTKSRPFL RRLFDLKRNK ASEYQNQRPA
     GSGLVDEGTE GLFNIGRSLS AKASNELRIR CTEFDINGDV TLVNGEFRKL ELIAKYGLLP
     RDLRKIDSST LPHILVRPSA ILINLLHLRV LIKADRVLVF DAYGSTDSYM QSLFIYDLEG
     KLRQKQSQLA SQLSQSLPYE FRALEAVLIS VTSGLEEEFN GVRDPVVRVL RALEEDIDRD
     KLRHLLIYSK KLGTFEQKAR LVRDAIDDLL EADDDLAAMY LSERSKGKER EEDDHQEVEM
     LLESYHKVCD EIVQASGNLV TNIRNTEEVV KAILDANRNS LMLMDLKFSI GTLGLATGTL
     FSALYGMNLK NFIEESDFGF GSVSVICFAL TGIVCVYGLA RLRKLQRVRM WGEAGVGGTS
     PLAPLSPKRS AFGVNRNNWR ADSIEPVWGS LPGEGRPERM KRLREHAAAQ AASRNTKFGV
     PNSPSATAAQ TPASAPHNKP RAEGSKGTEK ETAVHGEGNA KPGSHA
//
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