ID A0A0S3SS61_PHAAN Unreviewed; 451 AA.
AC A0A0S3SS61;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 13-SEP-2023, entry version 19.
DE RecName: Full=Rho-GAP domain-containing protein {ECO:0008006|Google:ProtNLM};
GN Name=Vigan.08G242100 {ECO:0000313|EMBL:BAT95660.1};
GN ORFNames=VIGAN_08242100 {ECO:0000313|EMBL:BAT95660.1};
OS Vigna angularis var. angularis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=157739 {ECO:0000313|EMBL:BAT95660.1, ECO:0000313|Proteomes:UP000291084};
RN [1] {ECO:0000313|EMBL:BAT95660.1, ECO:0000313|Proteomes:UP000291084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Shumari {ECO:0000313|Proteomes:UP000291084};
RX PubMed=26616024; DOI=10.1038/srep16780;
RA Sakai H., Naito K., Ogiso-Tanaka E., Takahashi Y., Iseki K., Muto C.,
RA Satou K., Teruya K., Shiroma A., Shimoji M., Hirano T., Itoh T., Kaga A.,
RA Tomooka N.;
RT "The power of single molecule real-time sequencing technology in the de
RT novo assembly of a eukaryotic genome.";
RL Sci. Rep. 5:16780-16780(2015).
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DR EMBL; AP015041; BAT95660.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S3SS61; -.
DR Proteomes; UP000291084; Chromosome 8.
DR GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd00159; RhoGAP; 1.
DR Gene3D; 3.90.810.10; CRIB domain; 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR000095; CRIB_dom.
DR InterPro; IPR036936; CRIB_dom_sf.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR044785; RopGAP1-5.
DR PANTHER; PTHR23177; MKIAA1688 PROTEIN; 1.
DR PANTHER; PTHR23177:SF35; RHO GTPASE-ACTIVATING PROTEIN GACA; 1.
DR Pfam; PF00786; PBD; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00285; PBD; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR PROSITE; PS50108; CRIB; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000291084}.
FT DOMAIN 70..83
FT /note="CRIB"
FT /evidence="ECO:0000259|PROSITE:PS50108"
FT DOMAIN 115..296
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 296..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..351
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 451 AA; 49634 MW; 3444407DCC9D9BDE CRC64;
MTGVVMVTKG GRCGGGGKRS RAARTAEEEE EQQNQLSLVA FLLAAIRKSM VSCRVDPPDD
VISTVHNMEI GWPTNVQHIT HVTFDRFNGF LGLPYEFEVE IPARVPSASV SVFGVSAESM
QCSYDSKGNS VPTILLLMQD RLYSQRGLKA EGIFRINPEN SQEEHVRDQL NRGIVPDDID
VHCLAGLIKA WFRELPSGVL DGLSPEQVLQ CNTEEESVDL VKQLKPTESA LLSWAIDLMA
DVVEEEEFNK MNARNIAMVF APNMTQMSDP LTALMHAVQV MNLLKTLIMK TLREREETTP
GGYSSMSFHS SGRQSEDEYD SQREMDTSGE LRGAKSDYDA HYGHSSEGEA ESLSEIEECF
LKQLDENTKG FSQEPAGHLE KYVSTISYSA YSMEPSISVT DNKAGNSCLR TTLTSSVDTS
SSSIGCTSTK DVEMVDKFAD SISPVTLLAS S
//
