ID A0A0N5BJT9_STREA Unreviewed; 1014 AA.
AC A0A0N5BJT9;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Rho-GAP domain-containing protein {ECO:0000313|WBParaSite:SPAL_0000620800.1};
OS Strongyloides papillosus (Intestinal threadworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=174720 {ECO:0000313|Proteomes:UP000046392, ECO:0000313|WBParaSite:SPAL_0000620800.1};
RN [1] {ECO:0000313|WBParaSite:SPAL_0000620800.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
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DR AlphaFoldDB; A0A0N5BJT9; -.
DR STRING; 174720.A0A0N5BJT9; -.
DR WBParaSite; SPAL_0000620800.1; SPAL_0000620800.1; SPAL_0000620800.
DR Proteomes; UP000046392; Unplaced.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0008289; F:lipid binding; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 3.30.530.20; -; 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR023393; START-like_dom_sf.
DR InterPro; IPR002913; START_lipid-bd_dom.
DR PANTHER; PTHR12659:SF7; CROSSVEINLESS C, ISOFORM C; 1.
DR PANTHER; PTHR12659; RHO-TYPE GTPASE ACTIVATING PROTEIN; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR Pfam; PF01852; START; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF55961; Bet v1-like; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS50848; START; 1.
PE 4: Predicted;
FT DOMAIN 533..753
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT DOMAIN 812..988
FT /note="START"
FT /evidence="ECO:0000259|PROSITE:PS50848"
FT REGION 129..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 196..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..328
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1014 AA; 115705 MW; A224200F0AA1C35D CRC64;
MNERKFHFYG TTNQQQNIKI VPFEYMLKGS PSSEECTNKK KNEKKIDVIY DDVPSTSSLL
SISPTNNIKT PNEDKNFSSS INERKIEKFM SSMLINAKEL CSIDQYQDSV KESKDNSNLR
YFNKNYNQTE MGNRHNKSGV EKNSEDKIKD DKIVDEKNVI TTSRKLNLGS PLSNSDSHII
YQPTYNINNG KKSLITNSTT SGDSPTLSSS SSIVSTTDYH NYSREQANEP PKKIILKGNN
THSIGDGKVE VSSNKLIPNN YNIIKIDGYS NQNLYNNNIQ VEKKNKKEKD NHYIKEGEYS
QSSSILLQSS SLSSDHHQPT TNKDKNNSIS DKLIMKDKDK NFSSNLVKSS TIISVNPLRS
LIVNDDGYYS HSPDPTKKYS NNRKNPSMTL KNSLTYHHSF FSPVKSNRSG YGSQLIDRQS
SWLPNVTRIS TSIISDSSDD GGKLDETILD DDTHVHRNLL YQTAINIDFL VDSTSSCLFG
LLDKHSTSRL NNTKKIGVLG SNIRRFFSSS KHTSKNGDIT FYRTSKVPSC FGMSLSDVQG
YCEGEVLPKC IFEIMKFLLN HASTTDGIFR KSGVRSRIEK LKSQCIVKFP NERVFYKDNG
ECLLTMTQVH DVADTMKQYF REIPGKLFSE KISDFLICIA NGLPSDKQIE ALRYVILLME
DTNRYAALAL FSFLNRISSW ASENNMSAEN LAVCFTPSLF NLNTESDKGT NSMSNLRLKR
RKTIAMPSEQ ELMEYQGAQK SLALLIKHYE HLFNLPTDLH RQLKVRSPFF NFGCYNEPTI
NINNITDIDI KECQNQIRGL VYEIVNDYGL DWNTWIPDCC YRDIAIYRKP VERCKFHFIR
ASFTVGVSPH EMWKVLSKNR KAWEKNVDYT SSVFVINNES DIQLISYKNY DERQEFSKKC
LLFRTWKKDS PELRGGVVLI ERSVEDKEFT HSNGHNIFPE VTCSCFLIMP SGNGSSKVNY
IHRADVKGRG DLYYSKVYPK VITQKMVNLK NYFNITSSAR NPSNGPVKGK ETSF
//