ID A0A2G5V134_9PELO Unreviewed; 585 AA.
AC A0A2G5V134;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Rho-GAP domain-containing protein {ECO:0008006|Google:ProtNLM};
GN Name=Cni-spv-1 {ECO:0000313|EMBL:PIC45457.1};
GN Synonyms=Cnig_chr_II.g5471 {ECO:0000313|EMBL:PIC45457.1};
GN ORFNames=B9Z55_005471 {ECO:0000313|EMBL:PIC45457.1};
OS Caenorhabditis nigoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1611254 {ECO:0000313|EMBL:PIC45457.1, ECO:0000313|Proteomes:UP000230233};
RN [1] {ECO:0000313|Proteomes:UP000230233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JU1422 {ECO:0000313|Proteomes:UP000230233};
RA Yin D., Schwarz E.M., Thomas C.G., Felde R.L., Korf I.F., Cutter A.D.,
RA Schartner C.M., Ralston E.J., Meyer B.J., Haag E.S.;
RT "Rapid genome shrinkage in a self-fertile nematode reveals novel sperm
RT competition proteins.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
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:PIC45457.1}.
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DR EMBL; PDUG01000002; PIC45457.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5V134; -.
DR Proteomes; UP000230233; Chromosome ii.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd00159; RhoGAP; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR PANTHER; PTHR15228; SPERMATHECAL PHYSIOLOGY VARIANT; 1.
DR PANTHER; PTHR15228:SF25; SPERMATHECAL PHYSIOLOGY VARIANT; 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; PS50081; ZF_DAG_PE_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000230233};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 145..190
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 206..407
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 447..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..463
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 474..513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 585 AA; 66585 MW; 924C80CB1B38E5CC CRC64;
MFSLWEFSFE SVVERLRELI FQCEQTTKAC TVHYFTSLAA LWARLPGAFH ELSNATRDYQ
PGTEYMAFLQ TLPTRAASSS SLVRSDRSID EGVASCDGSS SLTSLRRNAI NPDDEGALPD
TKRHKKTSYA GRTFDNHEIS TAAQSHHIQR TVQPSKCSAC DTLSILYTVQ CIDCGGQWHK
ACFPRIQQVC GQASKLVDRR TSIFGVPLKG LLEHQNRHIP LIIEKSIDQL QRRGLRAKGI
YRTCGVKSKI EEICNSFERS SSDEEICLEN ENPMNLASVV KLYLRKLPEP LLTYELYDDF
VKLGTECCSA QASGSNCEEE KVEKLRQLVR KLPVHNYETL KFIMLHLNRV SWFHEVNLMG
AANLSTVIAP SLIWMSPKRI DHTSAIMHAQ YTNKAIEVMI RNSYSIFGMD RQADWQSFFS
RYSVEEPPKE EEDCGNESDI EDDIEEDLDE QERSDDDEDE AIFLPPTPDI LKTTRKPVEQ
TTSLPNPKLP VERVSSGRRS NNNEPPPTVQ RRTTDVTRRS DMGDKRKSYT TSIVIAPRDG
SPDHVDQIQI IERDVYDKRS SLEQDKVFFY DSNSLYPSVL FSLSC
//
