ID A0A093XS54_TALMA Unreviewed; 1050 AA.
AC A0A093XS54;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Putative MFS-type transporter C16A3.17c {ECO:0000313|EMBL:KFX48068.1};
GN ORFNames=GQ26_0131410 {ECO:0000313|EMBL:KFX48068.1};
OS Talaromyces marneffei PM1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=1077442 {ECO:0000313|EMBL:KFX48068.1, ECO:0000313|Proteomes:UP000029285};
RN [1] {ECO:0000313|EMBL:KFX48068.1, ECO:0000313|Proteomes:UP000029285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PM1 {ECO:0000313|EMBL:KFX48068.1,
RC ECO:0000313|Proteomes:UP000029285};
RX PubMed=25330172; DOI=10.1371/journal.pgen.1004662;
RA Yang E., Wang G., Cai J., Woo P.C., Lau S.K., Yuen K.-Y., Chow W.-N.,
RA Lin X.;
RT "Signature Gene Expression Reveals Novel Clues to the Molecular Mechanisms
RT of Dimorphic Transition in Penicillium marneffei.";
RL PLoS Genet. 10:e1004662-e1004662(2014).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:KFX48068.1}.
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DR EMBL; JPOX01000013; KFX48068.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093XS54; -.
DR eggNOG; KOG3867; Eukaryota.
DR HOGENOM; CLU_291055_0_0_1; -.
DR Proteomes; UP000029285; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR CDD; cd17502; MFS_Azr1_MDR_like; 1.
DR CDD; cd16150; sulfatase_like; 1.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
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; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR000917; Sulfatase_N.
DR PANTHER; PTHR23501; MAJOR FACILITATOR SUPERFAMILY; 1.
DR PANTHER; PTHR23501:SF158; TRANSPORTER, PUTATIVE (AFU_ORTHOLOGUE AFUA_5G14490)-RELATED; 1.
DR Pfam; PF07690; MFS_1; 1.
DR Pfam; PF00884; Sulfatase; 1.
DR PRINTS; PR01036; TCRTETB.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
DR SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR PROSITE; PS50850; MFS; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..46
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 58..77
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 89..112
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 118..139
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 146..165
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 177..200
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 212..234
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 246..263
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 284..303
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 323..342
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 349..366
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 378..399
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 420..438
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 24..509
FT /note="Major facilitator superfamily (MFS) profile"
FT /evidence="ECO:0000259|PROSITE:PS50850"
SQ SEQUENCE 1050 AA; 116638 MW; 970995A0045ECA6C CRC64;
MASEIFTLEE HRQNPRSRLR VLTLLSVLYA ALFISAVNTT IVTTALPTIA KHFQSTSGYT
WVGAAYVLAD TASGPVWTNF SDIWGRKVVF LMAVALFMVS SFVCGFSTSM GMLISGRALQ
GAAAGAIMLL VNIVISDMFD MRRRTLYLGI CDVIWAMSGA IGPVVGGAFA EYAGWRWIWY
TNIPIAAVTF LVVCLFMDVH NPRTPIWRGL KAVDWLGSAS LLAVTLMVLL GLNIGGEYTD
WTSSKVLVLI IVGLALSGVF FSVEAKVAKY PVMPVQVFKN RSNAAAIAIG ALHAFAMMGP
EYYLPLYFQS SKLAQPLQSG LLGLPFVFLE GMGGIISGLV IHYTGRYNAL LWAGAVLMTL
GFGLLIDLKS STGLAKIMIY QIIGALGSGL LIQPPLVAIQ ANVSQQETAT ATSTLTFMRG
LAQAVSIVIG GVVFQSSMNL KQSDLVNAGL APDMVATFSG QDAQGLSRVI PERDPVHFGE
TPGLSWILMT GYYPRSAAII PVPPIEKTEN SQLSEKLELH PFSIIFSKMA SYSQPPKPLP
LKISSPNGGD RPNYVIFMPD QLRYNSLGCT TDGNAGINTP NIDAFRRRGT LYTNCFTQAS
VCSQSRCSMF TGCYPHVSGH RSLQNLIKPW EPNIFRSMKE NGYHIACLAP RGDTFAPTVT
ELSATEYGFL ETPEFTPKFA RGSGGEDIDK ENIWNRLFYK GLRNANQALD YDEAVVRSAL
KWLECPPDDK PWVLFMPLLF PHCPFQVEEP YFSMYDRDKM ASVVSKPEKK TGYEPRYMKA
IRERYGTGRA TEEIWREVKA TYFGMITRLD DQFGRILNKV DELGLWKDTV TMFFTDHGEY
LGDHGLIEKW PSGLSETLVR EPLIIAGAGI PENKTINSMT EMVDLVPTML EMSGIGEHFP
HNGKSWVPIL VGDATKHKEY AFSEGGFLTS EEPLLEQGPY PYDIKASLQH EDTIIVGKAI
SLRDEKYTYI YRLYEPAELY DRVSDSHEMH NLAADPAYCE LIAKYERLVL RWLVDGSDFL
PWQKDNRFPE VNLKSPKEQM EERLRKRGRA
//
