ID   A0A0R3RQ46_9BILA        Unreviewed;       857 AA.
AC   A0A0R3RQ46;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=RabBD domain-containing protein {ECO:0000313|WBParaSite:EEL_0000376601-mRNA-1};
OS   Elaeophora elaphi.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Elaeophora.
OX   NCBI_TaxID=1147741 {ECO:0000313|Proteomes:UP000050640, ECO:0000313|WBParaSite:EEL_0000376601-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:EEL_0000376601-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
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DR   AlphaFoldDB; A0A0R3RQ46; -.
DR   STRING; 1147741.A0A0R3RQ46; -.
DR   WBParaSite; EEL_0000376601-mRNA-1; EEL_0000376601-mRNA-1; EEL_0000376601.
DR   Proteomes; UP000050640; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0045202; C:synapse; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   CDD; cd04035; C2A_Rabphilin_Doc2; 1.
DR   CDD; cd08384; C2B_Rabphilin_Doc2; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 2.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR041282; FYVE_2.
DR   InterPro; IPR010911; Rab_BD.
DR   InterPro; IPR043566; Rabphilin/DOC2/Noc2.
DR   InterPro; IPR047022; Rabphilin_Doc2_C2A.
DR   InterPro; IPR001565; Synaptotagmin.
DR   InterPro; IPR017455; Znf_FYVE-rel.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR45729:SF4; RAB EFFECTOR NOC2; 1.
DR   PANTHER; PTHR45729; RABPHILIN, ISOFORM A; 1.
DR   Pfam; PF00168; C2; 2.
DR   Pfam; PF02318; FYVE_2; 1.
DR   PRINTS; PR00360; C2DOMAIN.
DR   PRINTS; PR00399; SYNAPTOTAGMN.
DR   SMART; SM00239; C2; 2.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 2.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   PROSITE; PS50004; C2; 2.
DR   PROSITE; PS50916; RABBD; 1.
DR   PROSITE; PS50178; ZF_FYVE; 1.
PE   4: Predicted;
KW   Exocytosis {ECO:0000256|ARBA:ARBA00022483};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Synapse {ECO:0000256|ARBA:ARBA00023018};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00091}.
FT   DOMAIN          18..140
FT                   /note="RabBD"
FT                   /evidence="ECO:0000259|PROSITE:PS50916"
FT   DOMAIN          66..127
FT                   /note="FYVE-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50178"
FT   DOMAIN          581..702
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          718..837
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          207..236
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          265..309
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          438..472
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..22
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        207..223
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        285..309
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   857 AA;  96258 MW;  1780CD9D2B64BB3C CRC64;
     MLKTGWSVRT ASARSPTNTR KNGITDSEKK HITAVLARAE ERRVREQQRI GRMIDRLEKM
     KARATGNGIT QCYICSTDFG LLASRSYAAM CLQCRRYVCQ KNCGVEAYDC ARRENIFLCK
     ICSEYREVMW KKSGAWFYKE IPEYIRPVED LELHSPLSRY PKTSWQHYTK PETSNLTYLT
     DKLQQSRKER YSSTAFNRSR INPSWLHQKV RQSLSNGDGS EEENAENSAS EETEAFSKGN
     LQLAQSVTSN RHIRIPKRKE AQEVPIVHRF TVGGRSRITD TEGSESHHAT PSTSPRHSPS
     SYGDDLSQNQ SSILASESID SGVVPSDHSM RVSKIHASAE TVNPTMTMSD HADESCRLIR
     HSNCSRTLSS SSGIQKTLLS SEMHTNLEQE IPPQVDGKKC FFPAQQASKS SKKAPGSKDI
     LLESQFKKIF PLMLFTNEPS PSAASQPSQQ DQFSAFSSTH TSSPSSPAGT TVAAGLTKQL
     APNQEPAASS ASSTSSARKS VMSLESLPAN LEQIKTVKVQ MWQHKSGIAM QLPMKGLSTT
     RSAVCLQSSV ATEVMLRGQA VVRHAISGHD IINLQDSDTD VLGSIQFTLR YSAQQMKLRV
     RLTGAKNLRA MDKNGFSDPY VKLYLIPGAS KATKMVSKTI EKTLNPLWNE EFTYYGITDE
     DHLKKSLRLL VLDRDRIGSD FLGEIRVPLK NLKDEEETFY NVRLEEEMLE QGVDINNERG
     KICLSLLYNV QQGSLYVTIK RCAELLGMDK TGFSDPYVKV SLLPLTNKAH RQKTSTKKRT
     LNPEFNETLT FVIPFKDLPK KTLQVDVFDK DVGMHDDYIG GVLLSTSAKG EREKQWNSCI
     QNPGYEFEQW HKLEFIE
//