ID A0A0V1GVX5_9BILA Unreviewed; 864 AA.
AC A0A0V1GVX5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=RalA-binding protein 1-A {ECO:0000313|EMBL:KRZ02395.1};
GN Name=VTA1 {ECO:0000313|EMBL:KRZ02395.1};
GN ORFNames=T11_833 {ECO:0000313|EMBL:KRZ02395.1};
OS Trichinella zimbabwensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ02395.1, ECO:0000313|Proteomes:UP000055024};
RN [1] {ECO:0000313|EMBL:KRZ02395.1, ECO:0000313|Proteomes:UP000055024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ02395.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) 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:KRZ02395.1}.
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DR EMBL; JYDP01000231; KRZ02395.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1GVX5; -.
DR Proteomes; UP000055024; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR Gene3D; 1.20.58.90; -; 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR Gene3D; 1.25.40.270; Vacuolar protein sorting-associated protein vta1; 1.
DR InterPro; IPR039767; RALBP1.
DR InterPro; IPR049041; RalBP1-like_Ral-bd.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR039431; Vta1/CALS_N.
DR InterPro; IPR023175; Vta1/CALS_N_sf.
DR PANTHER; PTHR12783; RALA BINDING PROTEIN 1 RALBP1; 1.
DR PANTHER; PTHR12783:SF5; RALA-BINDING PROTEIN 1; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR Pfam; PF20924; RLIP76_Ral-bd; 1.
DR Pfam; PF04652; Vta1; 1.
DR SMART; SM00324; RhoGAP; 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 GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000055024}.
FT DOMAIN 382..573
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 335..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 614..682
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 335..365
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 864 AA; 100049 MW; C96BFA923E7A455D CRC64;
MHCSKVLQCF NSAIIHFKKN FKKICPGVML PSNTGLRYVF REALRLDRTS PECQTFTIFV
LSYLNMLEDG NKVDERLNNE NVAQKYMKRV ALNVFQEADK IDCSGKFSIT VVRLFIRASN
LINVLTIFGD LDDSLIEARK YGRWRGAYLF DCFNSSKNPL PALEEVNESL DQVRYHGELS
YGPCDNYNVY GVAEKIVVPL HYSEMPDDGA LADVKLEEAL EQFADFNNAH DLCKMAVVAL
QHEKVADSIF NFEQAYKIME KYKKNHTLYW KIDLWKMQQM IVKLYRSSES LYQCDEWTSK
KGKREKKDKG YCYLHRLSSE EQLVHIRPKP KKTVFGKLKE KSREKEKEKE KEQKSKSKSK
LKCKNKAETV TPAAPARPVF AVPLARALCN NPSYDRVPVP AFVRRCIDYI NENGLDQEGL
YRVSAVKNSL EELRNAVDNG EEPSFGDAHQ AACLLKLFIR ELPESLFTEE LLDKFEHAAH
IAECLGRLCE LIERLPAPNK FFLAYFFLHL HEITQRQERN KMTIAKMCFI LQPLFNVSQQ
LLNAFLQNPQ ILFPNVSLKK YISPLRPASG KSLPNLPTDP KAILEELAKQ EFLLSHLHDE
INSGINDPQK EEQLWDVQRL VTQLKRELKS LKKKNINAFD EVEQESGPCI EMFEEKQLLA
VHMDLRNKIE IQRALIEELI RQMDDIGGQH AVLSARSVAR FSDAELSSEK KYDAKWPEQY
SALEDRKREL IESIVSERQK CVRLLAEMEM LAYALDALPC KHYTTYNYIK TYILRIRTKV
STFSTLGILN FILYNFAAHN FNHFAIFSSQ FRKFFLQQQT NNKFTYNISM KSDKKQTNKR
TPGIFDTAID VSAEMQKTAD IILL
//
