ID A0A0D2DFJ5_9EURO Unreviewed; 1309 AA.
AC A0A0D2DFJ5;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=SSD domain-containing protein {ECO:0000259|PROSITE:PS50156};
GN ORFNames=PV06_06770 {ECO:0000313|EMBL:KIW41190.1};
OS Exophiala oligosperma.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=215243 {ECO:0000313|EMBL:KIW41190.1, ECO:0000313|Proteomes:UP000053342};
RN [1] {ECO:0000313|EMBL:KIW41190.1, ECO:0000313|Proteomes:UP000053342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 72588 {ECO:0000313|EMBL:KIW41190.1,
RC ECO:0000313|Proteomes:UP000053342};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala oligosperma CBS72588.";
RL Submitted (JAN-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}.
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DR EMBL; KN847337; KIW41190.1; -; Genomic_DNA.
DR RefSeq; XP_016261406.1; XM_016407926.1.
DR STRING; 215243.A0A0D2DFJ5; -.
DR GeneID; 27358844; -.
DR VEuPathDB; FungiDB:PV06_06770; -.
DR HOGENOM; CLU_002359_0_1_1; -.
DR OrthoDB; 2786103at2759; -.
DR Proteomes; UP000053342; 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 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:UP000053342};
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..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1309
FT /note="SSD domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002251388"
FT TRANSMEM 268..293
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 355..375
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 596..621
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 633..657
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 663..685
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 715..734
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 740..765
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 825..848
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1062..1084
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1096..1119
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1125..1147
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1168..1197
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1209..1232
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1239..1259
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 591..765
FT /note="SSD"
FT /evidence="ECO:0000259|PROSITE:PS50156"
SQ SEQUENCE 1309 AA; 144008 MW; 5756CFDC4A4B72B3 CRC64;
MRFSTSAIAA LAAFSSIPLT IASVGTPLHE VGRCAIRGHC GKQGFFGSDL PCPDNDKASP
PSDTLREKLV DLCGTKWEDT DVCCEEDQVD TLKKNLKLAE RIIASCPACK ENFFNIFCTF
TCSPDQSLFI NVTETGKASN GKDVVTELDN IWSKEYQSGF YDSCKEVKNG ASGGKAMAFI
GGGAENYTEF LKFLGDKKLL GSPFQINFLD EARHDDSEGM KPEDPRVYAC NDTNPDYRCS
CVDCPAVCPT LEPVSSAKSC HVGKLPCLSF AVVIIYSVAL LLLITAISGH VAYRKHKQWK
SERLQLLQDA APSDDEDEGD LVHNPGLLER PQRNYYLNQV FDRAFNKLGG FCARYPALTI
GTNIVIVGLL SIGWVRFEVE RDPVRLWVSP SSDAAQEKAF FDANFGPFYR TEQVFLVNDS
SPTGSVLNYD NLDWWFDIEQ RVSRMMTPEN GITLKDVCFK PTESACVVQS VSGWFGAGLT
SDWEDQINLC AAHPGDQRCL PEFMDPLQPG RVLGGYDNVD NITQAKAMFT TWVVNNDQPG
TEGEARAEEW ERALKHELLI YQEAARSRGL RLSFNTEISL EEELNKSTNT DAKIVAISYV
VMFIYASLSL GSASLSLKSL LGNPSNALVQ SKFTLGVVGI VIVLMSVSGS VGLFSAVGVK
VTLIIAEVIP FLVLAVGVDN IFLIVHEFER VNVSHPDEEI DQRVAKALGR MGPSILLSAS
TETIAFAMGA FVGMPAVKNF AVYAAGAVFL NACLQVTMFV SILALNQRRV ESLRADCFPC
ITVRGANSVS MPGGHFFGSD EEGWLQKFIR KSYAPTLLDK KVKTFVVAFF VSIFAAAIAL
LPGIQLGLDQ RIALPSDSYM IPYFNDMYAY FGSGPPVYFV TRNVNLTERA HQRQVCGRFT
TCNEYSLEYI LEQESKRPEV SYINSATASW VDDFFYWLNP ISDCCKDDKG NTCFNEGEWN
ITLSGMPVGE EFINFANKWI RAPTDEECPN GGQAAYSTAV VIDEENVDIP ASHFRTFHTP
LKGQKDFIES YAAAKRIASE VSDKNEGIDV FAYSKHYIFF DMYSSIVRLT ATLVGVAILI
IFVLSSSLLG SIATGAVVSA SVVMIVVDVM GVMAIAGVSL NAVSLVNLVI CVGIGVEFCA
HIARAFMFPS KSVMERARHK FRGRDVRAWT ALVNVGGSVF SGIGVTKFLG VVVLAFTRSK
IFEVYYFRVW LALVVLASAH ALVWLPVALS FLGGDGKSLF CFVFCPAVLQ DMIICLCLTP
DKLRTLTDHD CVTLGYIDPE SEGGLEEDLA SRRYRSLLPD DDYDSDEEY
//
