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Database: UniProt
Entry: A0A1I7TPV2_9PELO
LinkDB: A0A1I7TPV2_9PELO
Original site: A0A1I7TPV2_9PELO 
ID   A0A1I7TPV2_9PELO        Unreviewed;       339 AA.
AC   A0A1I7TPV2;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Protein XRP2 {ECO:0000256|PIRNR:PIRNR037947};
OS   Caenorhabditis tropicalis.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=1561998 {ECO:0000313|Proteomes:UP000095282, ECO:0000313|WBParaSite:Csp11.Scaffold629.g10588.t1};
RN   [1] {ECO:0000313|WBParaSite:Csp11.Scaffold629.g10588.t1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-2016) to UniProtKB.
CC   -!- FUNCTION: Acts as a GTPase-activating protein (GAP) for tubulin in
CC       concert with tubulin-specific chaperone C, but does not enhance tubulin
CC       heterodimerization. {ECO:0000256|PIRNR:PIRNR037947}.
CC   -!- SIMILARITY: Belongs to the TBCC family. {ECO:0000256|ARBA:ARBA00008848,
CC       ECO:0000256|PIRNR:PIRNR037947}.
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DR   AlphaFoldDB; A0A1I7TPV2; -.
DR   STRING; 1561998.A0A1I7TPV2; -.
DR   WBParaSite; Csp11.Scaffold629.g10588.t1; Csp11.Scaffold629.g10588.t1; Csp11.Scaffold629.g10588.
DR   eggNOG; KOG2512; Eukaryota.
DR   Proteomes; UP000095282; Unplaced.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.160.20.70; -; 1.
DR   InterPro; IPR017901; C-CAP_CF_C-like.
DR   InterPro; IPR016098; CAP/MinC_C.
DR   InterPro; IPR006599; CARP_motif.
DR   InterPro; IPR012945; Tubulin-bd_cofactor_C_dom.
DR   InterPro; IPR039093; XRP2.
DR   PANTHER; PTHR15440:SF0; PROTEIN XRP2; 1.
DR   PANTHER; PTHR15440; XRP2 PROTEIN; 1.
DR   Pfam; PF07986; TBCC; 1.
DR   PIRSF; PIRSF037947; Protein_XRP2; 1.
DR   SMART; SM00673; CARP; 2.
DR   PROSITE; PS51329; C_CAP_COFACTOR_C; 1.
PE   3: Inferred from homology;
KW   GTP-binding {ECO:0000256|PIRNR:PIRNR037947, ECO:0000256|PIRSR:PIRSR037947-
KW   1}; GTPase activation {ECO:0000256|PIRNR:PIRNR037947};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR037947}.
FT   DOMAIN          34..186
FT                   /note="C-CAP/cofactor C-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51329"
FT   BINDING         105..106
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037947-1"
FT   BINDING         122..125
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037947-1"
SQ   SEQUENCE   339 AA;  38272 MW;  41691B509D6822A7 CRC64;
     MSCCFSKKCF ARGHREDAYK VTDEVPNAEG DEAPKYSWDR RDKVDPSEYT IRDIHTTSVK
     KTGKDGGPLQ IENCTDATIM FLHTTSQVII DDCRHCTIVL GPTQGSVFIR DSTNCTVLTA
     CQQLRTRDCT SIQIGILCST EPIVENSMDI HFYSLPMKYS NLQEQMHSVG LRPYTNRVTS
     AYDFSPVGTG GKINFTVTAE ALKLTDSQNQ ILTVNGIITK PTDDDFLPRF EKRSDEDPVY
     LYVLGKSKPM DVLEARAKKI CHSIYKCGMK ITATYDVDRS IQEPNFLPLF GPTCERMILI
     EAIGPLEKFE CDEEFDFMSD TDMEKLSVQL SQMKCTKSE
//
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