ID A0A016S9V0_9BILA Unreviewed; 736 AA.
AC A0A016S9V0;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Rho-GAP domain-containing protein {ECO:0000259|PROSITE:PS50238};
GN Name=Acey_s0262.g571 {ECO:0000313|EMBL:EYB87463.1};
GN Synonyms=Acey-Y34B4A.8 {ECO:0000313|EMBL:EYB87463.1};
GN ORFNames=Y032_0262g571 {ECO:0000313|EMBL:EYB87463.1};
OS Ancylostoma ceylanicum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYB87463.1, ECO:0000313|Proteomes:UP000024635};
RN [1] {ECO:0000313|Proteomes:UP000024635}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX PubMed=25730766; DOI=10.1038/ng.3237;
RA Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA Aroian R.V.;
RT "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT ceylanicum identify infection-specific gene families.";
RL Nat. Genet. 47:416-422(2015).
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:EYB87463.1}.
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DR EMBL; JARK01001598; EYB87463.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A016S9V0; -.
DR STRING; 53326.A0A016S9V0; -.
DR Proteomes; UP000024635; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
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; IPR004148; BAR_dom.
DR InterPro; IPR047165; RHG17/44/SH3BP1-like.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR PANTHER; PTHR14130; 3BP-1 RELATED RHOGAP; 1.
DR PANTHER; PTHR14130:SF14; RHO GTPASE-ACTIVATING PROTEIN 92B; 1.
DR Pfam; PF03114; BAR; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000024635}.
FT DOMAIN 252..435
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 445..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 544..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 159..193
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 447..483
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..532
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..585
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..609
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..646
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 736 AA; 82130 MW; ACB8F01948D8F2D9 CRC64;
MEKAKKDVGQ KFRRIKHNLV NSTRKDDDDD LKIVNALEHR NQRVVNAVYT YRKHVSNTVK
TGLREENVDK RRKKLDEFSL CTDLREISTE LEALHTTCLH KVIQKITQAL QVVVDEKVKH
DMMIEKRVLD DLVQFQDMEK ALTKSRERLN NAFTDVDIAK KALEKADSTS SNISQLQDTL
DAAQLKLENQ KDNTITDVYS LAAKEQEIAK VFTALLEEQL EYHRVAMRTL EMVLPEIRRD
IDNARPRPVF GVDLTEHLRH TQGRVAIVLE KCCSMLRASG FTEKGLFRVN GNNTKIRRMK
AAFDAGQIDT DERAYYLDPH SVCSVLKSYL RELPDPLLTH RLHNEWVNAA KLEDEAKLQA
FERCIGELPA CHRHNLTYLI NFLSEMLQHQ DQTAMNCGNL AIVFGPNLLG GDIDGNNAVG
TKIVETLLKH ASRLFGCPVV NNGSGGGHQP AGRSLTVDTN SPPKPGQSKD RSEYGSISSW
GTSPRGRPKE RAPPPPYVTP KTGSLIDLSD ECNNTDQTAH TSTTARIDPS LTQSQSLMSA
DLSESFGMSP TATAESDDSF DEYQDESLPG SMSRSQGDIT AASLTTPQRP PPPTFRNGSE
SSNNRPLSYN KAVGAEPIPV PRSRTSRSVV MENNSSSSSG SGSIKRPSIL NREDIVGADV
SNRTPPEFPT PGFSSDQGVC SPVPLWSAPE ITLVLTVFRY HVNDSPICRN YEVKYIATSF
ITNHSSWNRI WSLYQV
//