ID   V5H882_IXORI            Unreviewed;       362 AA.
AC   V5H882;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   08-NOV-2023, entry version 32.
DE   SubName: Full=Putative myosin-rhogap protein myr {ECO:0000313|EMBL:JAB73319.1};
DE   Flags: Fragment;
OS   Ixodes ricinus (Common tick) (Acarus ricinus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Ixodinae; Ixodes.
OX   NCBI_TaxID=34613 {ECO:0000313|EMBL:JAB73319.1};
RN   [1] {ECO:0000313|EMBL:JAB73319.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Salivary gland and midgut {ECO:0000313|EMBL:JAB73319.1};
RX   PubMed=25765539;
RA   Kotsyfakis M., Schwarz A., Erhart J., Ribeiro J.M.;
RT   "Tissue- and time-dependent transcription in Ixodes ricinus salivary glands
RT   and midguts when blood feeding on the vertebrate host.";
RL   Sci. Rep. 5:9103-9103(2015).
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; GANP01011149; JAB73319.1; -; mRNA.
DR   AlphaFoldDB; V5H882; -.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000146; F:microfilament motor activity; IEA:InterPro.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   CDD; cd20818; C1_Myosin-IX; 1.
DR   Gene3D; 3.30.60.20; -; 1.
DR   Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR   InterPro; IPR046349; C1-like_sf.
DR   InterPro; IPR046987; Myo9.
DR   InterPro; IPR002219; PE/DAG-bd.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   PANTHER; PTHR46184:SF5; HEAVY CHAIN, UNCONVENTIONAL MYOSIN; 1.
DR   PANTHER; PTHR46184; UNCONVENTIONAL MYOSIN-IXB-LIKE PROTEIN; 1.
DR   Pfam; PF00130; C1_1; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE   2: Evidence at transcript level;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          1..49
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          64..252
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          343..362
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:JAB73319.1"
FT   NON_TER         362
FT                   /evidence="ECO:0000313|EMBL:JAB73319.1"
SQ   SEQUENCE   362 AA;  40824 MW;  D5C3BFDE037F5468 CRC64;
     HVFSLVVINI PTSCEVCSNS MWLTERGLVC QGCKLTCHKK CYQKVASSCR DVNILQQGRK
     VFGVPLGRLV SEEVRIPVVV ERLITAIEMK GLYVEGIYRK CGITSRLNQL KQDMDDDPEG
     VDLDSYPIHV LTATLKAFFR EMPEPLMTFE LYDSYLLATN FQDPEERVQA IFMETKKLPP
     AHYDLFERLA FHLARVAQHQ EFNRMSPESL AIVFAPCILR TNKRLQAQDT LDCVNKQTIC
     VRCIIQEQLK KVQDTLNDID SLDTAVNTVV SRLSTLRSSR LSLALEPDGG HLPQPMGMRD
     EEEELLTQQI ENLQKEKAML TTVLPTLQLA LSGSDDDLLS TDLDSAAGSL DDVRPYDDPT
     MA
//