ID A0A423VYA3_9PEZI Unreviewed; 1278 AA.
AC A0A423VYA3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 12.
DE RecName: Full=SSD domain-containing protein {ECO:0000259|PROSITE:PS50156};
GN ORFNames=VMCG_07992 {ECO:0000313|EMBL:ROV96005.1};
OS Valsa malicola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX NCBI_TaxID=356882 {ECO:0000313|EMBL:ROV96005.1, ECO:0000313|Proteomes:UP000283895};
RN [1] {ECO:0000313|EMBL:ROV96005.1, ECO:0000313|Proteomes:UP000283895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=03-1 {ECO:0000313|EMBL:ROV96005.1,
RC ECO:0000313|Proteomes:UP000283895};
RA Yin Z., Huang L.;
RT "Host preference determinants of Valsa canker pathogens revealed by
RT comparative genomics.";
RL Submitted (SEP-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:ROV96005.1}.
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DR EMBL; LKEA01000034; ROV96005.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A423VYA3; -.
DR STRING; 356882.A0A423VYA3; -.
DR Proteomes; UP000283895; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005319; F:lipid transporter activity; IEA:InterPro.
DR GO; GO:0015918; P:sterol transport; IEA:UniProt.
DR Gene3D; 1.20.1640.10; Multidrug efflux transporter AcrB transmembrane domain; 2.
DR InterPro; IPR004765; NPC1-like.
DR InterPro; IPR032190; NPC1_N.
DR InterPro; IPR003392; Ptc/Disp.
DR InterPro; IPR000731; SSD.
DR NCBIfam; TIGR00917; 2A060601; 1.
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:UP000283895};
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..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1278
FT /note="SSD domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019523365"
FT TRANSMEM 269..289
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 353..373
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 596..617
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 637..659
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 665..687
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 717..736
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 742..767
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 829..848
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1079..1098
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1105..1127
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1133..1155
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1176..1203
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1215..1237
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 593..767
FT /note="SSD"
FT /evidence="ECO:0000259|PROSITE:PS50156"
SQ SEQUENCE 1278 AA; 140333 MW; 6CAAB73CC7820FF7 CRC64;
MTKLIALAAA GALALAALGE ADQLYTPKHE AGRCAIRDHC GKKSFFGKEL PCVDNGLAEE
PDQDLRKQLV DLCGPKWNDG PVCCTSDQVE SLKNELSTAN TIVSSCPACK DNFYNLFCTF
TCSPDQSLFI NVTNTMSKND KTLVTELDQL VSEDYGTGFY DSCKDVKFGP SNSEAMKLIG
GGAKNYTQLL KYLGDEKMLG SPFQINFPSS YEEPVMGPLA MTPKKCNDED PNFRCACVDC
PDVCPELPKV EESGSCRVGV LPCLSFASIF VYSVLLLTSI VATVGHVWYR KRAARLQEER
TLLHGGIDVS DDEDDEGRLV QNGAMLDRPT RPYRLNTWCD AAFFKLGHWA ARFPAITIFS
SLIVIIILSA GWVRFEIEKD PARLWVSPTS AAAQEKLFFD TNFGPFYRAE KVFLVNDTLP
SGPGPVLSYD TLIWWMQVEK DIAELESETY RMRLHDVCLK PTGSACVVQS VAAYFENEPS
LVDKHGWEDK LRACAQAPAE CRPAYGQPLE PNMILGGYPE GGDVANAPAM TVTWVVNNFA
EGTPEVARAM DWEKALKERL LELQKEAASR GLRLSLSTEI SLEEELNKTT NTDAKIIVIS
YVIMFLYASI ALGSTTLSLR DMIRNPAVSI VESKFSLGIA GIVIVLMSIS ASIGLFSWAN
LKATLIIVDV IPFIVLAVGV DNIFLIVHEF ERVNIRNPDD DVEVRVAKAL GRMGPSILLS
AITETVSFAL GAFVGMPAVR NFAIYAAGAV FINALLQVTL FISLLSYNQK RVEDSRMDCL
PCVPIKAARV HLNGSNGNMG ARLYEMPEEG ILQRFIIRYY APTLLGKKVK VVIVAVFLGL
FAAGVALIPE VKLGLDQRVA IPDESYLIPY FNDLYDYFDS GPPVYFVAKD VDATQRKHQK
EICARFTTCN SMSLTNILEQ ERKRTEVSYI SSPAASWIDD FFLWLNPQFE ECCVEKGSAC
FEGRDPAWNI TMSGMPEGDE FLHYLDKFLA APTTDDCPLG GQASYGAAVV IDEQKQTVPA
SHFRTMHSPL RSQDDFINAY SSARRIAADF SSKTGAEVFP YSVFYIFFDQ YLTIVGQTAG
LLCAAIGIIF ILSSILLGSA LTGGAVAITV VMTIVDIIGA MAVFGVSLNA VSLVNLIICV
GIAVEFCAHI ARAFMFPSRT FMERAKNRFR GRDARAWTAL VNVGGSVFSG ITVTKLLGVF
VLAFTRSKIF EIYYFRIWVA LVAFAATHAL IFLPVLLSLM GGDGYVDPEG EGGLEEDLAS
RRYRAVAGAD YGSDSEGE
//
