ID A0A178AG62_9PLEO Unreviewed; 1277 AA.
AC A0A178AG62;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Multidrug efflux transporter AcrB transmembrane domain-containing protein {ECO:0000313|EMBL:OAK96644.1};
GN ORFNames=IQ06DRAFT_380236 {ECO:0000313|EMBL:OAK96644.1};
OS Stagonospora sp. SRC1lsM3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Massarinaceae; Stagonospora.
OX NCBI_TaxID=765868 {ECO:0000313|EMBL:OAK96644.1, ECO:0000313|Proteomes:UP000077206};
RN [1] {ECO:0000313|EMBL:OAK96644.1, ECO:0000313|Proteomes:UP000077206}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lsM3a {ECO:0000313|EMBL:OAK96644.1,
RC ECO:0000313|Proteomes:UP000077206};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) 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; KV441719; OAK96644.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178AG62; -.
DR STRING; 765868.A0A178AG62; -.
DR InParanoid; A0A178AG62; -.
DR OrthoDB; 2786103at2759; -.
DR Proteomes; UP000077206; 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:UP000077206};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius, ECO:0000313|EMBL:OAK96644.1};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..1277
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008081736"
FT TRANSMEM 271..296
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 356..378
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 600..625
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 637..661
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 667..689
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 719..738
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 744..769
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 828..846
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1075..1095
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1102..1125
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1131..1152
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1212..1236
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 595..769
FT /note="SSD"
FT /evidence="ECO:0000259|PROSITE:PS50156"
SQ SEQUENCE 1277 AA; 140808 MW; 2B6D7EEDAA9E63DC CRC64;
MVQQCSRGWR AFTVGLLSIL AGSALAGPDL TTKHEKGRCA IRGQCGKQSF FGSELPCPDN
GLAKTPDADV RKKLVDICGD KWTDTDVCCE ENQLDALKTN LDRATPIINA CPACKENFFN
LFCTFTCSPD QSLFINVTNT ESKGDKYLVT ELDNLVSNDY ASTFYDSCKD VKFGATNGKA
MDFIGGGAKN FTQFLKFLGD KKFLGSPFQI NFPRPDEKDY PDMDPMNKHA YPCNTTDEKY
RCACLDCGGS CTELPEVQEV KQCHVGKLPC LSFAVIIIYS FFLALLCTAV AGHVAYQKHS
RHKDQRMRLL QDLEPSDDED EGDIVHNVGM LDRPTKHYSV NTWCDRMFSR LGYVCARFPV
ITIFTSTLVV VLMSLGWLRF QIETDPVRLW VSPDSAAAQD KAFFDEKFGP FFRAEQVFLV
NDTAHGPSPV LSYETLDWWF GVEDQIRRIK SYEGGVTLDQ VCFKPIEDAC VVQSITGYFQ
GDFANVSPSS WQDDLLECVD NPSQCLPAFQ QPLDPHLLFG GVNESVLDAK ALVVTWVVKN
HAEGTPEIDR AMHFENEMKN YLKLVAEDAK SRGLRLSFNT EASLEQELNK STNTDAKIVV
VSYIIMFLYA SLALGSTTLT VRSILRNPAN ALVQSKFMLG TVGIIIVLMS VSASVGLFSA
AGIKVTLIIA EVIPFLVLAV GVDNIFLIVH EFERINISHP EGSIPERVSR ALGRMGPSIL
LSATTETTAF ALGCAVGMPA VRNFAAYAAG AVFINALLQV TMFIAVLSLN QQRVESNRAD
CFPFVRVSKA DPGYLNGGMG HGAGEEGALQ RFIRKTYAPA LLGKKAKVGI IAVFFGIFTL
GVALFPRVEL GLDQRIAVPS DSYLIPYFND LYDYLDVGPP VYFVTKELNV TQRAPQKELC
GRFSTCDEGS LANIIEAERK RPEVSYLSAS AANWLDDFFL WLNPENEKCC VDAKGNTCFK
DRQPPWNMTL HGMPEGEEFI HYLERWVEAP TTEDCPIGGK AAYSDALLID SKHLTIPASH
FRTSHTPLRS QKDFIAAYTA ARRISREISE DVETEVFPYS KFYIFFDQYV SIVRLAGALL
GSALAAVLVI TTILLGSIST ALIVTLVVGM TLSAIIGSMA VMGVSLNAVS LVNLIICVGI
SVEFTAHIAR AFTFPSSTTM ARAPKHSFRG RDARAWTAMV NVASSVISGI TITKVLGVAT
LAFTRSKIFE IYYFRVWVAL VLWASTHSLI LLPVLLSLFG GRGYVDPEGE GGLEQDLRSR
QYPALLGDDD DEYDSDD
//
