ID A0A1I8CGF7_9BILA Unreviewed; 1276 AA.
AC A0A1I8CGF7;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Exocyst complex component 6 {ECO:0000313|WBParaSite:RSKR_0000406200.1};
OS Rhabditophanes sp. KR3021.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Alloionematidae;
OC Rhabditophanes.
OX NCBI_TaxID=114890 {ECO:0000313|Proteomes:UP000095286, ECO:0000313|WBParaSite:RSKR_0000406200.1};
RN [1] {ECO:0000313|WBParaSite:RSKR_0000406200.1}
RP IDENTIFICATION.
RC STRAIN=KR3021 {ECO:0000313|WBParaSite:RSKR_0000406200.1};
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
CC -!- SIMILARITY: Belongs to the SEC15 family.
CC {ECO:0000256|ARBA:ARBA00007944}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family.
CC {ECO:0000256|ARBA:ARBA00005993}.
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DR AlphaFoldDB; A0A1I8CGF7; -.
DR WBParaSite; RSKR_0000406200.1; RSKR_0000406200.1; RSKR_0000406200.
DR Proteomes; UP000095286; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0090522; P:vesicle tethering involved in exocytosis; IEA:InterPro.
DR CDD; cd06960; NR_DBD_HNF4A; 1.
DR Gene3D; 1.20.58.670; Dsl1p vesicle tethering complex, Tip20p subunit, domain D; 1.
DR Gene3D; 3.30.50.10; Erythroid Transcription Factor GATA-1, subunit A; 1.
DR Gene3D; 1.10.357.30; Exocyst complex subunit Sec15 C-terminal domain, N-terminal subdomain; 1.
DR Gene3D; 1.10.565.10; Retinoid X Receptor; 1.
DR InterPro; IPR007225; EXOC6/Sec15.
DR InterPro; IPR046361; EXOC6/Sec15_C.
DR InterPro; IPR042045; EXOC6/Sec15_C_dom1.
DR InterPro; IPR048359; EXOC6_Sec15_N.
DR InterPro; IPR042044; EXOC6PINT-1/Sec15/Tip20_C_dom2.
DR InterPro; IPR049636; HNF4-like_DBD.
DR InterPro; IPR035500; NHR-like_dom_sf.
DR InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR InterPro; IPR001628; Znf_hrmn_rcpt.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR PANTHER; PTHR12702:SF0; EXOCYST COMPLEX COMPONENT 6; 1.
DR PANTHER; PTHR12702; SEC15; 1.
DR Pfam; PF20651; EXOC6_Sec15_N; 1.
DR Pfam; PF00104; Hormone_recep; 1.
DR Pfam; PF04091; Sec15_C; 1.
DR Pfam; PF00105; zf-C4; 1.
DR PRINTS; PR00047; STROIDFINGER.
DR SMART; SM00430; HOLI; 1.
DR SMART; SM00399; ZnF_C4; 1.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR SUPFAM; SSF48508; Nuclear receptor ligand-binding domain; 1.
DR PROSITE; PS51843; NR_LBD; 1.
DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Exocytosis {ECO:0000256|ARBA:ARBA00022483};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transport {ECO:0000256|ARBA:ARBA00022448};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 868..943
FT /note="Nuclear receptor"
FT /evidence="ECO:0000259|PROSITE:PS51030"
FT DOMAIN 1022..1271
FT /note="NR LBD"
FT /evidence="ECO:0000259|PROSITE:PS51843"
FT REGION 277..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 995..1014
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 997..1014
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1276 AA; 146127 MW; 4D06A719F19F01E1 CRC64;
MFANDSVVPK IGGHQAIDSE STNFEGNTHA DINAEQEFFL YELETTDSGS VGLVLRAIYE
GGDVAKFTKA LESRIAHYDK SILKVSNYHY QGFVESMKQL STLKSKVEDI KGEGQIINTI
IQRDSVDLLI KGNEVLKYKK LQRNAKIAMD QLTQTLPILD SYAKLKDLMN QEKYYQALKV
LEEMEHTYGD QLQKYRFTVS LAKTFPSIRK QIKDKSFSEF TDFLEMIRQV SQKIGQEVMK
QVAENFDFTK YSSDQQSGIE RKKSTITGTL MELSSDGSVH KTSIAKRQRT SRQEDEDEDD
ETFNRVGNLV DYTPIHRCCQ IFNILGEKAQ FQKEYSTQRT AQVNVVIGPI TKMSSLNVNP
YMPYLENIVG FFVVEEHIMQ TEPLLANAAY IEGLWEMALR KIKATMDTHF GQCVDVGMML
KIKKMIFLFA ETMKSYGYEI SPLYQLLKNF RDQYNEILMS EYCGLFEGAL KNDNYAPILC
EDEEEFLAVL KQFPFHKRGL DKEDFPRKFP FSQFVPTVFQ QAKQYLDGCL KFMDHLQMGQ
NEIDDTIRRY ANVLLARWSG SLKAFSKDKK RSLVQLTQII VNIGYLEKGV TSLEEFIKKL
TKKDNSLGQG TGHLVSLKEQ LFRDARCEVE GQIDAKLKSK IDEFFEISRY DWDLPSARGT
ASDYITDLLA FMNSIFTSFS NLPSNLARHA CMQMCKYLSE SLTKTILSAS VKSVSVGAIE
QFSLDVLQCE IFTMRCPVPG FEDESLSMTF LSLRQLLDLV IQSDWASYLA DCGKNNNGKY
QRVKPTEAMT LLEKMIEFEK KTSSFLSIGK GERRKLLDTI MKQLRNYMYG TNQQLTNESF
QGYLEIDNNQ PSTSTNNNGL NLEILRKREF CAVCNEEADS FHYNTLSCRG CNSFFRRAIT
LKMKFTCRHG GKCVIDKDTR CSCRACRFAK CIEKGMDPGA VQPKRDALSN GQSLINKPDE
NTVEWNAISN FNIIEGETSK EKFENQLKKL FLADEGSSKA STPNSPASTD SNPESHFILP
DLVEQHNQQS TRRHILCCNS VADMLKPQPL PIQPCYLHDI LVTYNVQMTL MYELIHNIPE
FKEIDEFSEK ARLLRCFAAP YFVINNVMHT VENGIHDRIV LVNNTCILAS NCPITDVNNE
MNNIIASKLY GMNCRSVLTD LLIPIYTEEF DYHEMMAVRL LIFWHCGSIG ADEKRYKSCQ
KGIDRVVSEL LKHYETKGRH GTEGTLRLSK LMLLIPTFLI HANYMREIID LSNKQMKVTN
MDPSIEQILN TPLMYN
//
