MRS2_GIBZE
ID MRS2_GIBZE Reviewed; 537 AA.
AC Q4I298; A0A0E0S0M9; V6RL29;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-SEP-2016, sequence version 2.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Mitochondrial inner membrane magnesium transporter MRS2;
DE AltName: Full=RNA-splicing protein MRS2;
DE Flags: Precursor;
GN Name=MRS2; ORFNames=FGRRES_16995, FGSG_08660;
OS Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=229533;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=17823352; DOI=10.1126/science.1143708;
RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT "The Fusarium graminearum genome reveals a link between localized
RT polymorphism and pathogen specialization.";
RL Science 317:1400-1402(2007).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
RA Hammond-Kosack K.E.;
RT "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT graminearum.";
RL BMC Genomics 16:544-544(2015).
CC -!- FUNCTION: High-conductance magnesium-selective channel that mediates
CC the influx of magnesium into the mitochondrial matrix. Essential for
CC the splicing of mRNA group II introns in mitochondria by affecting
CC mitochondrial magnesium concentrations, which are critical for group II
CC intron splicing. It also suppresses a variety of mitochondrial intron
CC mutations and its absence may disturb the assembly of mitochondrial
CC membrane complexes. {ECO:0000250|UniProtKB:Q01926}.
CC -!- SUBUNIT: Homopentamer. Forms homooligomers. Interacts with MFM1.
CC {ECO:0000250|UniProtKB:Q01926}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q01926}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q01926}.
CC -!- SIMILARITY: Belongs to the CorA metal ion transporter (MIT) (TC 1.A.35)
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ESU14657.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DS231667; ESU14657.1; ALT_SEQ; Genomic_DNA.
DR EMBL; HG970333; CEF77054.1; -; Genomic_DNA.
DR RefSeq; XP_011320082.1; XM_011321780.1.
DR AlphaFoldDB; Q4I298; -.
DR SMR; Q4I298; -.
DR STRING; 5518.FGSG_08660P0; -.
DR EnsemblFungi; ESU14657; ESU14657; FGSG_08660.
DR GeneID; 23555654; -.
DR KEGG; fgr:FGSG_08660; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G10503; -.
DR eggNOG; KOG2662; Eukaryota.
DR HOGENOM; CLU_025144_2_0_1; -.
DR InParanoid; Q4I298; -.
DR Proteomes; UP000070720; Chromosome 2.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0015095; F:magnesium ion transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0045016; P:mitochondrial magnesium ion transmembrane transport; ISS:UniProtKB.
DR CDD; cd12823; Mrs2_Mfm1p-like; 1.
DR InterPro; IPR045863; CorA_TM1_TM2.
DR InterPro; IPR002523; MgTranspt_CorA/ZnTranspt_ZntB.
DR InterPro; IPR039204; MRS2-like.
DR PANTHER; PTHR13890; PTHR13890; 1.
DR Pfam; PF01544; CorA; 1.
DR SUPFAM; SSF144083; SSF144083; 1.
PE 3: Inferred from homology;
KW Ion transport; Magnesium; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Transit peptide;
KW Transmembrane; Transmembrane helix; Transport.
FT TRANSIT 1..26
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 27..537
FT /note="Mitochondrial inner membrane magnesium transporter
FT MRS2"
FT /id="PRO_0000043245"
FT TRANSMEM 425..445
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 456..476
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 79..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 442..445
FT /note="YGMN"
FT COMPBIAS 87..112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 537 AA; 60936 MW; D48E13EB1094CCCA CRC64;
MQSTLCLPVP SRSLLRFLRC QSKRAFASAN HGRDTITTSA IRCRARSLNT VAIRKQSLAL
TTACERRVTT VEPSLFDKDP VTRKLPDRNQ PLTSQNHFST SRNAQGFWSG RKSSSSYMPT
WNSFLKFAGK KNEKALKPDD LPNHDEFGDN SSIFNNRRTL AAKAASEPRL RCTEVDEHGN
VILVDGEFKK TELIAKFGLL PRDLRKIDSS NLPHILIRPS AILLNLLHLK VLIKHDRVLL
FDIYGSKTSY PQSAFMYDLQ GKLQQKTAPG NASLPYEFRA LEAVLTSVTS ELEADFEAVR
EPVMHILSEL EDDIDRHKLR MLLILSKRVS TFEQKAKLVR DAIEDLLEAD DDLADMYLTE
KTHDLYRGED DHTEVEMLLE SYHKLTDEIV QEAGNLVSGI RNTEEIVRAI LDANRNALML
LDLKFSVGTL GLAMGTFLAG LYGMNLENFI EETNWGFAGV TGVSVVFSLI VCWYGLTKLR
RVQRIKMMDA ERPAIARGQS YFPDDRSALG LLDNRNREML RRINMQKAVS QQKKKWL
