ID B2ACQ6_PODAN Unreviewed; 538 AA.
AC B2ACQ6;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 24-JAN-2024, entry version 64.
DE SubName: Full=MFS transporter {ECO:0000313|EMBL:CDP26667.1};
DE SubName: Full=Podospora anserina S mat+ genomic DNA chromosome 3, supercontig 1 {ECO:0000313|EMBL:CAP61221.1};
GN ORFNames=PODANS_3_1760 {ECO:0000313|EMBL:CAP61221.1};
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:CAP61221.1};
RN [1] {ECO:0000313|EMBL:CAP61221.1, 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}, and S mat+
RC {ECO:0000313|EMBL:CAP61221.1};
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|EMBL:CAP61221.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=S mat+ {ECO:0000313|EMBL:CAP61221.1};
RA Genoscope - CEA;
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN [3] {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).
RN [4] {ECO:0000313|EMBL:CDP26667.1}
RP NUCLEOTIDE SEQUENCE.
RA Grognet P., Bidard F., Kuchly C., Chan Ho Tong L., Coppin E.,
RA Ait Benkhali J., 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 Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CU633448; CAP61221.1; -; Genomic_DNA.
DR EMBL; FO904938; CDP26667.1; -; Genomic_DNA.
DR RefSeq; XP_001903446.1; XM_001903411.1.
DR AlphaFoldDB; B2ACQ6; -.
DR GeneID; 6187472; -.
DR KEGG; pan:PODANSg461; -.
DR VEuPathDB; FungiDB:PODANS_3_1760; -.
DR eggNOG; KOG0255; Eukaryota.
DR HOGENOM; CLU_008455_8_4_1; -.
DR OrthoDB; 1701613at2759; -.
DR Proteomes; UP000001197; Chromosome 3.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1.
DR Gene3D; 1.20.1720.10; Multidrug resistance protein D; 1.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR PANTHER; PTHR23502; MAJOR FACILITATOR SUPERFAMILY; 1.
DR PANTHER; PTHR23502:SF51; QUINIDINE RESISTANCE PROTEIN 1-RELATED; 1.
DR Pfam; PF07690; MFS_1; 1.
DR PRINTS; PR01036; TCRTETB.
DR SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR PROSITE; PS50850; MFS; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001197};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 98..121
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 133..150
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 162..184
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 221..239
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 306..326
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 346..364
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 397..417
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 429..453
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 465..483
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 489..510
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 67..514
FT /note="Major facilitator superfamily (MFS) profile"
FT /evidence="ECO:0000259|PROSITE:PS50850"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 538 AA; 59055 MW; 672C4F93022B2019 CRC64;
MMDPHQDPPL QRESQKYDAE DAGDGRPADN SSSNINDTTS DSDPEALAQV PSGPAYSVFS
KSTKRWIVTM IAFSSFVSPM TANIYFPALV PIARDLDVSV SMINLTLTTY MIFQAIAPTL
VGDLADAAGR RPAFLICFVI YIFANLGLAL QKNFAALLVL RMVQSAGSSG TVALSFAVIA
DVAVSAERGK YMGIVGAGIN IGPALSPVFG GLLAEYLGWP AIFWFCMIYA AVWLVPYALT
VPETCRNVVG NGSIPAQSWW NMTAVDLCRA RRRKRNGESL GGARTKQKLR FPNPFNTLKV
AFEKDLALLL FYGTLTYLVF ILIAATLSTE LEAIYHYSDL QLGLCYLPYG VGCCFAAVMQ
GYILDHNYRR IARKIGFTID YKRGDDLSNF PIEKARILPA SPFLFAGVAA VICYGWVLHF
ETHVAGPLAL VFLIGLCVTG SFSILNTLLV DLYPEAPATA VAAMNLVRCL FGAGGTAVIE
YMLRAMGRGW TFTFWGLVLV LFSPILWVLA KWGPGWREER RVRKLKEEEK ERAVTSRP
//