ID A0A0F4ZLC7_9PEZI Unreviewed; 1311 AA.
AC A0A0F4ZLC7;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=SSD domain-containing protein {ECO:0000259|PROSITE:PS50156};
GN ORFNames=TD95_000858 {ECO:0000313|EMBL:KKA30628.1};
OS Thielaviopsis punctulata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Microascales; Ceratocystidaceae; Thielaviopsis.
OX NCBI_TaxID=72032 {ECO:0000313|EMBL:KKA30628.1, ECO:0000313|Proteomes:UP000033483};
RN [1] {ECO:0000313|EMBL:KKA30628.1, ECO:0000313|Proteomes:UP000033483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CR-DP1 {ECO:0000313|EMBL:KKA30628.1};
RA Radwan O., Al-Naeli F.A., Rendon G.A., Fields C.;
RL Submitted (MAR-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:KKA30628.1}.
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DR EMBL; LAEV01000350; KKA30628.1; -; Genomic_DNA.
DR OrthoDB; 2786103at2759; -.
DR Proteomes; UP000033483; 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; 1.
DR Pfam; PF12349; Sterol-sensing; 1.
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:UP000033483};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1311
FT /note="SSD domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002482785"
FT TRANSMEM 283..303
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 606..626
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 647..671
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 677..699
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 729..748
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 754..779
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 845..862
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1086..1108
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1115..1139
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1145..1166
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1238..1262
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 605..779
FT /note="SSD"
FT /evidence="ECO:0000259|PROSITE:PS50156"
FT REGION 1288..1311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1297..1311
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1311 AA; 142281 MW; A9435127AD9C45DB CRC64;
MAPYGAWATM AAALASFVSP ALAAADVSPA GSPLTPVHEA GRCAMRGQCG SKSWFGKQLP
CVDNGLAKDP DAETRAMLVD LCGPQWSSGP ICCTTEQVAA LKSELSTPTQ IVGSCPACKE
NFFNLFCTFT CSPDQSLFLN VTKTMSKAGK SLVTEIDQLI SKDFGSGFYD SCKNVKFGPS
NANAMDFIGG GAKDYHQLLK FLGDEKAIGS PFQINFPDPK KYTDDEPAMS PLEKMKPKSC
NDEDPNFRCA CVDCPDVCPA LAPVKEAGSC HVGKLPCLSF ASIITYGALL LSVVGVYFGR
IVWRTHVNRY RGQVLFRDVS QVDEDDEDDE DLMHGSDLFQ RPQCYHRINT WCDTAFSQLG
HLAARFPAIT IMTSVVVVAV LSCGWVRFDL ERDPARLWVS PVSDAARDKA FFDSNFGPFY
RAEQAFLVND TLPSGPGPVL SYDTLMWWMD VEKSVAELKG DKYGTTLDDV CFKPLGNACV
VQSVSGYWQG EPSLVSRTGW GAYLENCARS PVECRPEYGQ PIEPNMVFGG VGTGSVLDAN
ALVVSWVVAN AQEGSPQVDK AVDFEIALKD RLLKAQAEAA ERGLRLSFTT EASLEEELNK
STNTDAGIVV LSYLVMFLYA SIALGSTTMS MRDLLSNPSV ALVQSKFTLG IFGIVIVLMS
IAASIGLFSW FGLKATLIIA EVIPFIVLAV GVDNIFLIVH EFERVNNTHP DEMVEARIAK
ALGRIGPSIL FSAVTETLSF SLGAFVGMPA VRNFAVYAAG AVFINAVLQV TMFVSILALN
QIRVEDNRAD CMPCVQVKAA RIRLNGGGYH HYSSARYYQV PEESLLQQFI RNCYAPALLT
KKAKMVVVGV FLALFAAGVA LLPEIELGLD QRVAIPDDSY LIPYFNDLYD YFNAGPPVYF
VTKSVNASQR AQQQHLCARF TTCDQLSLAN ILEGERKRPD VSFIASPTAS WLDDFFMWLN
PALGDSCCVN HANACFADRD PAWNVTLSGM PEGAEFTEYL QRFLAAPTTD DCPLAGRAAY
GSAVVVDAES DVVVASHFRT MHSPLRSQQD FIDAYASARR IATDISRETG LEVFPYSVFY
IFFDQYATIV SLTGTLLGSA VGLIFIVASV LLGSVWTAAV VALTVVMSVV DIMGAMAVFG
VSLNAVSLVN LVICVGISVE FCAHIARAFM FPSRTLMDAA KSLPLASDRT APLSADRNAR
AWAALVNVGS SVFSGITVTK LLGVSVLAFT RSKIFEIYYF RVWLALVVFA GLHALVFLPV
ALSVAGGEGY VDPESEGGLE DELARRRARL PVAGYDSDES DDDQDDEDDE H
//
