ID A0A090CDG0_PODAN Unreviewed; 869 AA.
AC A0A090CDG0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Metal ion transporter {ECO:0000313|EMBL:CDP23329.1};
OS Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
OS (Pleurage anserina).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Podosporaceae; Podospora;
OC Podospora anserina.
OX NCBI_TaxID=515849 {ECO:0000313|EMBL:CDP23329.1, ECO:0000313|Proteomes:UP000001197};
RN [1] {ECO:0000313|EMBL:CDP23329.1, ECO:0000313|Proteomes:UP000001197}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC {ECO:0000313|Proteomes:UP000001197};
RX PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77;
RA Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O., Porcel B.M.,
RA Couloux A., Aury J.-M., Segurens B., Poulain J., Anthouard V.,
RA Grossetete S., Khalili H., Coppin E., Dequard-Chablat M., Picard M.,
RA Contamine V., Arnaise S., Bourdais A., Berteaux-Lecellier V., Gautheret D.,
RA de Vries R.P., Battaglia E., Coutinho P.M., Danchin E.G.J., Henrissat B.,
RA El Khoury R., Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H.,
RA Debuchy R., Wincker P., Weissenbach J., Silar P.;
RT "The genome sequence of the model ascomycete fungus Podospora anserina.";
RL Genome Biol. 9:R77.1-R77.22(2008).
RN [2] {ECO:0000313|Proteomes:UP000001197}
RP GENOME REANNOTATION.
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC {ECO:0000313|Proteomes:UP000001197};
RX PubMed=24558260; DOI=10.1534/genetics.113.159988;
RA Grognet P., Bidard F., Kuchly C., Tong L.C.H., Coppin E., Benkhali J.A.,
RA Couloux A., Wincker P., Debuchy R., Silar P.;
RT "Maintaining two mating types: Structure of the mating type locus and its
RT role in heterokaryosis in Podospora anserina.";
RL Genetics 197:421-432(2014).
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; FO904936; CDP23329.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A090CDG0; -.
DR eggNOG; ENOG502QPTQ; Eukaryota.
DR InParanoid; A0A090CDG0; -.
DR Proteomes; UP000001197; Chromosome 1.
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; 2.
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:UP000001197};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 805..828
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 840..862
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 679..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..31
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..54
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..88
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..233
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..421
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..457
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..515
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..706
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 869 AA; 98474 MW; 320ED7FA7143A40E CRC64;
MEPNAPSTSA HAPRKRKNHR GGKKKKQTRR KSFAGLTPDD VESGLDRPED MGTGREGFYS
RPGRNASNTS LDSDALLDHR EHKSFIRPRR PSMMTASGSL LATPGGSRLK HMSRGDTSEE
DGEGAPLLSS SVFQRGETFP SYGSGEATLR RSGPGSRHES SRSSSKRRFL GSGNDTYNVN
YPPSVPGTPP MRPLDRMDMS FGDALLRDEL ENGDSQRRDY DEDDHESFHN SPLERRKTIA
ALQAEEDVCF PQEGLSDIAD DELGIRDAHG YRGRARRRRR KWPDIALLNE WSRVEKEGRS
EERRVKRMVE PQLINGRLRP VHRGWFQAEE EAPYRFTYFN EEFQSTIHSQ TIGELVQPGG
SFKELFIPDP PILSDSSESE DEDEDPTVSL SQVLAGQNGD PRIPVRQPSL ATSTTANVQH
QDFAELRRER TGSANNGRPM STEPKSHHSE QKAYSGEHTP SRMRSPVPDH VKSPQPDNNS
SNNNNNSSNN NNNNNNNNNN NNNNNNNNNN NFHPTPHKEP KPIRYGERPV WWLDILSPTE
QEMKIISKAF GIHPLTAEDI MMQEQREKVE LFRHYYFVNY RSFDQDQSSE NFMEPVNMYV
VVFRECVLSF HFSVTPHPAN VRRRIRQLRD YLILSSDWIS YAIIDDITDV FGPLIQSIED
EVDDIDDEIL QLHSTTAAAT TDPYGSRNNK QDGSSNEKRE LGDDAEAGRD MLRRVGDCRK
KVMSLYRLLG NKADVIKGFA KRCNEHWEVA PRSEIGLYLG DIQDHIVTMT SNLSHYEKIL
ARSHGNYLAQ INIRMNERQE QTADVLGKLT VLGTIVLPMN IITGLWGMNV LVPGQESEAG
LVWFWCITGG LLVFGLACYL IAKRVYNIV
//
