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Database: UniProt
Entry: A0A1V9X0W5_9ACAR
LinkDB: A0A1V9X0W5_9ACAR
Original site: A0A1V9X0W5_9ACAR 
ID   A0A1V9X0W5_9ACAR        Unreviewed;       619 AA.
AC   A0A1V9X0W5;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Arf-GAP with coiled-coil {ECO:0000313|EMBL:OQR67036.1};
GN   ORFNames=BIW11_04863 {ECO:0000313|EMBL:OQR67036.1};
OS   Tropilaelaps mercedesae.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Parasitiformes; Mesostigmata; Gamasina; Dermanyssoidea; Laelapidae;
OC   Tropilaelaps.
OX   NCBI_TaxID=418985 {ECO:0000313|EMBL:OQR67036.1, ECO:0000313|Proteomes:UP000192247};
RN   [1] {ECO:0000313|EMBL:OQR67036.1, ECO:0000313|Proteomes:UP000192247}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Wuxi-XJTLU {ECO:0000313|EMBL:OQR67036.1};
RX   PubMed=28327890; DOI=10.1093/gigascience/gix008;
RA   Dong X., Armstrong S.D., Xia D., Makepeace B.L., Darby A.C., Kadowaki T.;
RT   "Draft genome of the honey bee ectoparasitic mite, Tropilaelaps mercedesae,
RT   is shaped by the parasitic life history.";
RL   Gigascience 6:1-17(2017).
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
CC       Target cell membrane {ECO:0000256|ARBA:ARBA00004175}.
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:OQR67036.1}.
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DR   EMBL; MNPL01030221; OQR67036.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V9X0W5; -.
DR   STRING; 418985.A0A1V9X0W5; -.
DR   InParanoid; A0A1V9X0W5; -.
DR   OrthoDB; 1449795at2759; -.
DR   Proteomes; UP000192247; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0044231; C:host cell presynaptic membrane; IEA:UniProtKB-KW.
DR   GO; GO:0044218; C:other organism cell membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR   CDD; cd13250; PH_ACAP; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR   Gene3D; 1.10.220.150; Arf GTPase activating protein; 1.
DR   Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR045258; ACAP1/2/3-like.
DR   InterPro; IPR027267; AH/BAR_dom_sf.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR037278; ARFGAP/RecO.
DR   InterPro; IPR001164; ArfGAP_dom.
DR   InterPro; IPR038508; ArfGAP_dom_sf.
DR   InterPro; IPR004148; BAR_dom.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   PANTHER; PTHR23180:SF399; BLOWN FUSE, ISOFORM A-RELATED; 1.
DR   PANTHER; PTHR23180; CENTAURIN/ARF; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF01412; ArfGap; 1.
DR   Pfam; PF16746; BAR_3; 1.
DR   Pfam; PF00169; PH; 1.
DR   PRINTS; PR00405; REVINTRACTNG.
DR   SMART; SM00248; ANK; 2.
DR   SMART; SM00105; ArfGap; 1.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF57863; ArfGap/RecO-like zinc finger; 1.
DR   SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 1.
DR   PROSITE; PS50115; ARFGAP; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   4: Predicted;
KW   ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW   ProRule:PRU00023}; Exocytosis {ECO:0000256|ARBA:ARBA00022483};
KW   Membrane {ECO:0000256|ARBA:ARBA00023298};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Neurotoxin {ECO:0000256|ARBA:ARBA00022699};
KW   Presynaptic neurotoxin {ECO:0000256|ARBA:ARBA00023028};
KW   Reference proteome {ECO:0000313|Proteomes:UP000192247};
KW   Target cell membrane {ECO:0000256|ARBA:ARBA00022537};
KW   Target membrane {ECO:0000256|ARBA:ARBA00023298};
KW   Toxin {ECO:0000256|ARBA:ARBA00022656};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00288}.
FT   DOMAIN          156..253
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          272..386
FT                   /note="Arf-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50115"
FT   REPEAT          523..555
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
SQ   SEQUENCE   619 AA;  68874 MW;  1BC484446420300A CRC64;
     MASLSCFSDV KKLKEVHSAF TKISSELDGS LQRHAQLPKN KSVELEETGK LLTANRTCFQ
     HTALEYVGQL SRVQVAKRHK MMEALLGQMH AVRTFHSQAL KTFAEHETPL ENASKYFSEI
     RTKYERECMS LSKEVETYLR QVTGEPHCPA SRGAGGHQLE GYLFKRTTNA FKTWNRRWFV
     LDHGSLYYIK RDGDPKDMTV VERDLRLCTV KEVLDGERRF CFEVLSPHKS HALQADSEKA
     QKMWVEALKQ GINNAHNQNG AHVKRLTSSS ALRTVPGNER CVDCGARDPE WASVNLGATL
     CIQCSGIHRS LGVHISKVRS LKLDSWEDDT VKIMERLGND SVNKIFAYEV DENLRAQPES
     ERSFREAWIR AKYLDRKFVR PLRPAGTGDD HKTAKITRWA VARPGGRCIR TEGVLVFGED
     INRNCTSCPP PGTSPGSDAD KDAELETFPI SDLTPSRLLY EAAGADNLTA MLHALALGAE
     PNYRCEEDRL RTSLHKAIAD GPWVAAAEFL LLNGAQHTVV DLEGLTPLHL ASRASSVSLV
     GLLLKKGADR DALDREGNSA LALAVANGNA EVVTLIRLDQ FRDDLKLEDS DFSSGGDVFD
     RALQDFSSRG RESARATAT
//
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