ID M2QNQ9_CERS8 Unreviewed; 528 AA.
AC M2QNQ9;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Major facilitator superfamily (MFS) profile domain-containing protein {ECO:0000259|PROSITE:PS50850};
GN ORFNames=CERSUDRAFT_87123 {ECO:0000313|EMBL:EMD33795.1};
OS Ceriporiopsis subvermispora (strain B) (White-rot fungus) (Gelatoporia
OS subvermispora).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Gelatoporiaceae; Gelatoporia.
OX NCBI_TaxID=914234 {ECO:0000313|EMBL:EMD33795.1, ECO:0000313|Proteomes:UP000016930};
RN [1] {ECO:0000313|EMBL:EMD33795.1, ECO:0000313|Proteomes:UP000016930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B {ECO:0000313|EMBL:EMD33795.1,
RC ECO:0000313|Proteomes:UP000016930};
RX PubMed=22434909; DOI=10.1073/pnas.1119912109;
RA Fernandez-Fueyo E., Ruiz-Duenas F.J., Ferreira P., Floudas D.,
RA Hibbett D.S., Canessa P., Larrondo L.F., James T.Y., Seelenfreund D.,
RA Lobos S., Polanco R., Tello M., Honda Y., Watanabe T., Watanabe T.,
RA Ryu J.S., Kubicek C.P., Schmoll M., Gaskell J., Hammel K.E., St John F.J.,
RA Vanden Wymelenberg A., Sabat G., Splinter BonDurant S., Syed K.,
RA Yadav J.S., Doddapaneni H., Subramanian V., Lavin J.L., Oguiza J.A.,
RA Perez G., Pisabarro A.G., Ramirez L., Santoyo F., Master E., Coutinho P.M.,
RA Henrissat B., Lombard V., Magnuson J.K., Kuees U., Hori C., Igarashi K.,
RA Samejima M., Held B.W., Barry K.W., LaButti K.M., Lapidus A.,
RA Lindquist E.A., Lucas S.M., Riley R., Salamov A.A., Hoffmeister D.,
RA Schwenk D., Hadar Y., Yarden O., de Vries R.P., Wiebenga A., Stenlid J.,
RA Eastwood D., Grigoriev I.V., Berka R.M., Blanchette R.A., Kersten P.,
RA Martinez A.T., Vicuna R., Cullen D.;
RT "Comparative genomics of Ceriporiopsis subvermispora and Phanerochaete
RT chrysosporium provide insight into selective ligninolysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:5458-5463(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(out) + myo-inositol(out) = H(+)(in) + myo-inositol(in);
CC Xref=Rhea:RHEA:60364, ChEBI:CHEBI:15378, ChEBI:CHEBI:17268;
CC Evidence={ECO:0000256|ARBA:ARBA00034449};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC transporter (TC 2.A.1.1) family. {ECO:0000256|ARBA:ARBA00010992,
CC ECO:0000256|RuleBase:RU003346}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KB445805; EMD33795.1; -; Genomic_DNA.
DR AlphaFoldDB; M2QNQ9; -.
DR STRING; 914234.M2QNQ9; -.
DR HOGENOM; CLU_001265_30_13_1; -.
DR OrthoDB; 3601645at2759; -.
DR Proteomes; UP000016930; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR005828; MFS_sugar_transport-like.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR003663; Sugar/inositol_transpt.
DR NCBIfam; TIGR00879; SP; 1.
DR PANTHER; PTHR48022:SF64; MAJOR FACILITATOR SUPERFAMILY (MFS) PROFILE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR48022; PLASTIDIC GLUCOSE TRANSPORTER 4; 1.
DR Pfam; PF00083; Sugar_tr; 1.
DR SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR PROSITE; PS50850; MFS; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000016930};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|RuleBase:RU003346}.
FT TRANSMEM 31..50
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 105..123
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 135..157
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 286..304
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 324..345
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 352..375
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 387..411
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 423..440
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 452..472
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 37..475
FT /note="Major facilitator superfamily (MFS) profile"
FT /evidence="ECO:0000259|PROSITE:PS50850"
FT REGION 508..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 528 AA; 58557 MW; A034311D03043414 CRC64;
MGGPAAVSAG GNNAFTHLVD SSKPWWMNRR LLALNGWILL LLITSTTNGY DGSMMNGLQS
LPQWESAFNH PTGGMLGLLN AIQNIGCLAA YPFSPYMSDG LGRRTAVAFG AFIMCAATIL
QTASHSVGMF IGARFMIGFG LTFAASAAPV LVTEIAYPTQ RAPVTSLYNS LWFLGSIVAS
WTTFGTFHIP TSWSWRIPSA LQGLPSVCQI CLIWFVPESP RWLCSKGREA EALRILAYYH
ANGNEEDPLV EYEFEEIKAA LRLDREVAAN VGWKSLFKTP GNRRRLRIMI AIAFFSQWSG
NNLISYYMNK IFISIGITSA TTQLLINGIL NIYNFIIAIL AGLLCDRIGR RPMFIVSTIG
MFVFWTLQTI CFALYSEHGN IAAAHTFIAM IFLFYAFCEI AFTPLIVSYT VEILPFAVRA
KGFTIFNFSV TLSLIFNQYV NPIALAALGW KYYLVYVCWL AFEIVFIFLF LVETKNRTLE
ETAALFDGEA TAERLAYTAA EHAGVVASEE HSEREKASTE DITEVANV
//