ID A0A0W0FC44_9AGAR Unreviewed; 1385 AA.
AC A0A0W0FC44;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=SSD domain-containing protein {ECO:0000259|PROSITE:PS50156};
GN ORFNames=WG66_13345 {ECO:0000313|EMBL:KTB33919.1};
OS Moniliophthora roreri.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=221103 {ECO:0000313|EMBL:KTB33919.1, ECO:0000313|Proteomes:UP000054988};
RN [1] {ECO:0000313|EMBL:KTB33919.1, ECO:0000313|Proteomes:UP000054988}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2952 {ECO:0000313|EMBL:KTB33919.1,
RC ECO:0000313|Proteomes:UP000054988};
RA Aime M.C., Diaz-Valderrama J.R., Kijpornyongpan T., Phillips-Mora W.;
RT "Draft genome sequence of Moniliophthora roreri, the causal agent of frosty
RT pod rot of cacao.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the patched family.
CC {ECO:0000256|ARBA:ARBA00005585}.
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:KTB33919.1}.
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DR EMBL; LATX01002123; KTB33919.1; -; Genomic_DNA.
DR eggNOG; KOG1933; Eukaryota.
DR Proteomes; UP000054988; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015918; P:sterol transport; IEA:UniProt.
DR Gene3D; 1.20.1640.10; Multidrug efflux transporter AcrB transmembrane domain; 2.
DR InterPro; IPR032190; NPC1_N.
DR InterPro; IPR003392; Ptc/Disp.
DR InterPro; IPR000731; SSD.
DR PANTHER; PTHR45727; NPC INTRACELLULAR CHOLESTEROL TRANSPORTER 1; 1.
DR PANTHER; PTHR45727:SF2; NPC INTRACELLULAR CHOLESTEROL TRANSPORTER 1; 1.
DR Pfam; PF16414; NPC1_N; 1.
DR Pfam; PF02460; Patched; 2.
DR SUPFAM; SSF82866; Multidrug efflux transporter AcrB transmembrane domain; 2.
DR PROSITE; PS50156; SSD; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000054988};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 249..270
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 685..708
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 715..737
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 839..864
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 920..940
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1186..1204
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1210..1231
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1238..1260
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1293..1312
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1324..1352
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 605..864
FT /note="SSD"
FT /evidence="ECO:0000259|PROSITE:PS50156"
FT REGION 752..786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 761..786
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1385 AA; 152797 MW; 88573ADB13446798 CRC64;
MAVDEFTLAM DQEPRCSMRD SCGKKGIFGR DLPCPYDGPP QEPDDRQHLV DICGPEFAEG
PTCCTTAQVD ELAKNFQQVE PIISPCPACR NNFRSFFCTF TCSPYQAAFL NITSTQESSS
GREAVESADF FVGERYGTGF FDSCKDLKLG AASDFVMDVI FGGAKDYPSF LKFLGDKSDT
GSPFQINFPP ANTTPSDLTA LDPPARNCYD SELASRCSCI DCSDVCPTLP PQSPPNGPPI
CHVGLLPCLS FILILAYGLA VLGFGIGFVV ERTIRRRRER MYERVALSAE TNSLSSPRIH
TRGLVGAGSL AQYVDEDSQP ASRDFGRNLL DPVETVQPRQ YKLNNILRRF FYRLGLWTST
KPFLTFAVVF LIMGLLNIGW KKFEVETDPV RLWVAKTSES RQQKEFFDEN FGPFYRPQQI
FITSAPSPTT NEKPPVLSYE HLKYWFKVEK DIRNLKSEPN GYTLRDVCFK PAGPRGACVV
QSVAAWFGND FDDYDEDTWA GQLEHCAAYP TDCLPDFQQP LKPVNVLGGI PKNESVLNSE
AIVVTYVVSD SLDIEIQAKA LEWERSLREY LVNLSERIEA EAGLRIAFST GVSLEEEINK
STNTDVKIVV LSYLAMFLYV SLTLGNGSVS PGEESLGSSL LRWAKNFPKL FSRSGSSSSA
LSVDSRSAPR LFPRFPSSLF TGSKFTLGLF GIALVILSVS TSVGFFSLCG VKVTLIIAEV
IPFLVLAVGV DNVFILVHEL DRQNLLHGPN AAMQAHHHPS SRGALSPTNS SHRSPFGNGS
SSTHEDDADV ASMPLFLSAE ERVARTLARM GPSILLSTIT ETTAFFLGAL VPMPAVRNFA
LYAAGSVFIN AMLQVTVFMS ALLLDLKRVE ASRVDCFPCI RLPSRIALVD APPSGSGIGR
LARLIRRYYA PWLLKPTVKA AVLVMFSGLF IVSVIMIQYL KLGLDQKLAL PSESYLVNYF
DHMAAYLEVG PPVYFVSRNV DTTQRTGQQA LCGRFTTCQP YSLANILEVE RQRKESSFIS
EPTASWIDDF FAWLNPDQEQ CCRVRKGDPS MFCTPRDRDS LCRPCFEGRE PAWNITMKGL
PEGEEFMTYL KRWLESPTNE DCPVAGKASF GTALSLDSEG NSVTASHFRT FHSPLKTQDD
FINSFEAAHR VAQEISDYTG TDVFPYSLHY VFFDQYAHII AMTQEVLGLG LAAVLLVTAI
LLGSWRTGMI VTGVVGLTVV SVMGVMALWG IMLNAISLVN LVISLGIAVE FCAHVARAFM
NAGSGVTLEV GHPAGQKERD ERMWTALVDV GPSVLSGITF TKLIGMCVLA LTRSKLLEIY
YFRMWLTLII SGALHGLVLL PVVLSIAGGA GFPMQEVDEE WMSNVMRHDY EYAPFLTDAD
SVASE
//