ID A0A369GY62_9HYPO Unreviewed; 1269 AA.
AC A0A369GY62;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=SSD domain-containing protein {ECO:0000259|PROSITE:PS50156};
GN ORFNames=CP532_2995 {ECO:0000313|EMBL:RDA87832.1};
OS Ophiocordyceps camponoti-leonardi (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX NCBI_TaxID=2039875 {ECO:0000313|EMBL:RDA87832.1, ECO:0000313|Proteomes:UP000252748};
RN [1] {ECO:0000313|EMBL:RDA87832.1, ECO:0000313|Proteomes:UP000252748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCC 80369 {ECO:0000313|EMBL:RDA87832.1,
RC ECO:0000313|Proteomes:UP000252748};
RA Kobmoo N., Wichadakul D., Arnamnart N., Rodriguez De La Vega R.C.,
RA Luangsa-Ard J.-J., Giraud T.;
RT "A genome scan of diversifying selection in the zombie-ant fungus
RT Ophiocordyceps unilateralis complex supports a role of enterotoxins in
RT coevolution and host-specificity.";
RL Submitted (OCT-2017) 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:RDA87832.1}.
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DR EMBL; PDHP01000016; RDA87832.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A369GY62; -.
DR STRING; 2039875.A0A369GY62; -.
DR Proteomes; UP000252748; 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:UP000252748};
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..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1269
FT /note="SSD domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016893367"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 591..613
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 625..649
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 655..677
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 707..726
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 732..757
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 822..839
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1062..1088
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1095..1115
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1121..1146
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1167..1196
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1208..1231
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 586..757
FT /note="SSD"
FT /evidence="ECO:0000259|PROSITE:PS50156"
SQ SEQUENCE 1269 AA; 139298 MW; C34DEDD3860D798B CRC64;
MRHQLAPLVV AAAPVLLAES LTPKHESGRC AFRGQCGKQS LFGKELPCVD NGRASEPDSE
LRKELVDLCG AEWSHSPVCC SLDQLKALKS ELGTPNTLIG SCPACKYNFF NLFCKFTCSP
DQSLFVNVTA SVEKSGNRLV TEVDQLISDE YGSGFYDSCK EVKFGGANSR AMDLIGGGAK
DYHQLLKFLG DKKPFVGSPF QINFPTSYSQ PGMDPLEEMH PKKCNDTDPD YRCVCVDCPE
VCPNLPAVKE QGSCKVGALP CLSFASIFTY CILLAALVAS VFGHVAWKKY AQHQVERTRL
LHGSSHSDDE DEGGPVLTDA ARDRPTRRYW LNDMCDKALG KLGHTSARFP GLTIGTSLLV
VAILSAGWFR FDLEKEPARL WVSPSSPAAQ EKEYFDNHFG PFYRAEKIFL VNDTQPSGPG
PVLSYETLKW WSEVEQSIER IVSPAFGDTL QDVCYKPVND ACVVQSVTSY WWSRGGLSPT
NWKDQLRNCA RSPVDCRPKF GQPIEPSMIL GGYGDDVADA KALTVTWVVN NAQGGTAFLA
RAIDWENALR DRLLEVQGEA ESRGLRLSFS TEISLEQELN KSTNTDAKIV VISYIVMFIY
ACMALGTPFK HIFRNPALLL VESKVTLGLV GIIIVLMSIT ASIGFFSWVG LKATLIIVEV
IPFIVLAVGV DNIFLIVHEL ERVNISCPDQ MVEERVARAL GRMGPSILFS ALTETVAFAL
GAAVGMPAVR NFAAYAAGAV LVNAILQMTM FVSFLALNQM RVEDHRCELW PWWQVTKARV
HMDGSNGFAS GGRGTHDDEE GPLQVFIKNT YAPHLLRRHV KLTVVAVFFG VFAAALALLP
RMQLGLDQRV AIPDGSYLIP YFDDMYDYLE TGPPVYFVTR DVDASRRPEQ QGLCSRFTTC
QQLSLTNTLE LERQRPDVSF ISSPTASWID DYLLWLNPVY EQCCVEQGSA CFAGRDPPWN
TSLSGMPEGS EFFRYLQKFL SSPADDECPL GGQAAYGEAV VVNGDNSAVQ ASHFRTAHTP
LRSQDDFINA YSAARRITAE ITEKTGADVF PYSVFYIFFD QYLSIVSLTA GLLCAAVGII
FVIASLLLGS VLTSAVVAVS VVMSVVDIMG AMAVFNVSLN AVSLVNLIIC VGISVEFCAH
IARAFTFPSR TVMEGNNNAF RGRDARAWTA LVNVGGSVFS GITVTKLLGV CVLAFTRSKI
FEIYYFRVWL ALVVFAALHA LVFLPVALSF VGGGGYVDPE SEGTAAQDLT DRRWRAIRDH
DNSDSEDGF
//
