ID A0A2H3HZJ7_9EURO Unreviewed; 489 AA.
AC A0A2H3HZJ7;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Magnesium transporter {ECO:0000256|RuleBase:RU366042};
GN ORFNames=PENO1_108050 {ECO:0000313|EMBL:PCG88831.1};
OS Penicillium occitanis (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=290292 {ECO:0000313|EMBL:PCG88831.1, ECO:0000313|Proteomes:UP000218381};
RN [1] {ECO:0000313|EMBL:PCG88831.1, ECO:0000313|Proteomes:UP000218381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL100 {ECO:0000313|EMBL:PCG88831.1,
RC ECO:0000313|Proteomes:UP000218381};
RX PubMed=28951729; DOI=10.3389/fmicb.2017.01627;
RA Bravo-Ruiz G., Sassi A.H., Marcet-Houben M., Di Pietro A., Gargouri A.,
RA Gabaldon T., Roncero M.I.G.;
RT "Regulatory Mechanisms of a Highly Pectinolytic Mutant of Penicillium
RT occitanis and Functional Analysis of a Candidate Gene in the Plant Pathogen
RT Fusarium oxysporum.";
RL Front. Microbiol. 8:1627-1627(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:PCG88831.1}.
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DR EMBL; NPFK01000725; PCG88831.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3HZJ7; -.
DR STRING; 290292.A0A2H3HZJ7; -.
DR OrthoDB; 73031at2759; -.
DR Proteomes; UP000218381; Unassembled WGS sequence.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006811; P:monoatomic ion transport; IEA:UniProtKB-KW.
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; IPR039204; MRS2-like.
DR PANTHER; PTHR13890:SF26; MAGNESIUM TRANSPORTER MRS2 HOMOLOG, MITOCHONDRIAL; 1.
DR PANTHER; PTHR13890; RNA SPLICING PROTEIN MRS2, MITOCHONDRIAL; 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:UP000218381};
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 325..343
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU366042"
FT TRANSMEM 355..377
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU366042"
FT REGION 439..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..475
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 489 AA; 54069 MW; FE4F82383FDE8124 CRC64;
MACSENLNTA KVISATYLTH DTLGSDKESY QKWKNSTSPP ITSFTDDGAE GNLFNLGRTL
ASKTLDEPRL RCTEFDENGN VTLVNGEFRK SELIAKYGLL NRDLRKIDSS VLPHILVRPS
TILISLLHLR VLIKADRVLV FDAYGSADSY TQSVFMYDLE GKLRQRQAPG SGALPYELRA
LESVLISVTS GLESEFEGVR DPVVRVLRAL EEDIDRDKLR HLLVYSKKLG SFEQKARLVR
DAIDDLLEAD DDLAAMYLSD RAHGKVRAEN DHQEVEMLLE SYHKICDEIV QASGNLVTAI
RNTEEVVKAI LDANRNSLML LDLKFSIGTL GLAAGTLISA LYGMNLKNFI EESDFGFGAV
SITCFISSII VSLYGLAKLR KVQRVRMWGE GMDTAGMGPL QSRSLALTNR GNWRSDAIEP
MLAGLPGEGR SERLKRFKEA VKSAAKGDSP TDAARRMAIS QARRTASQSQ DKNGTKPEEN
TSDETIPKA
//