ID D2VNA8_NAEGR Unreviewed; 549 AA.
AC D2VNA8;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Rho GTPase activating protein {ECO:0000313|EMBL:EFC41620.1};
GN ORFNames=NAEGRDRAFT_70430 {ECO:0000313|EMBL:EFC41620.1};
OS Naegleria gruberi (Amoeba).
OC Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC Vahlkampfiidae; Naegleria.
OX NCBI_TaxID=5762 {ECO:0000313|Proteomes:UP000006671};
RN [1] {ECO:0000313|EMBL:EFC41620.1, ECO:0000313|Proteomes:UP000006671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEG-M {ECO:0000313|EMBL:EFC41620.1,
RC ECO:0000313|Proteomes:UP000006671};
RX PubMed=20211133; DOI=10.1016/j.cell.2010.01.032;
RA Fritz-Laylin L.K., Prochnik S.E., Ginger M.L., Dacks J.B., Carpenter M.L.,
RA Field M.C., Kuo A., Paredez A., Chapman J., Pham J., Shu S., Neupane R.,
RA Cipriano M., Mancuso J., Tu H., Salamov A., Lindquist E., Shapiro H.,
RA Lucas S., Grigoriev I.V., Cande W.Z., Fulton C., Rokhsar D.S., Dawson S.C.;
RT "The genome of Naegleria gruberi illuminates early eukaryotic
RT versatility.";
RL Cell 140:631-642(2010).
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DR EMBL; GG738884; EFC41620.1; -; Genomic_DNA.
DR RefSeq; XP_002674364.1; XM_002674318.1.
DR AlphaFoldDB; D2VNA8; -.
DR EnsemblProtists; EFC41620; EFC41620; NAEGRDRAFT_70430.
DR GeneID; 8851455; -.
DR VEuPathDB; AmoebaDB:NAEGRDRAFT_70430; -.
DR eggNOG; KOG4270; Eukaryota.
DR InParanoid; D2VNA8; -.
DR OrthoDB; 7959at2759; -.
DR Proteomes; UP000006671; Unassembled WGS sequence.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd00030; C2; 1.
DR CDD; cd00159; RhoGAP; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR PANTHER; PTHR45808:SF22; CRAL-TRIO DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR45808; RHO GTPASE-ACTIVATING PROTEIN 68F; 1.
DR Pfam; PF00168; C2; 2.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000006671}.
FT DOMAIN 146..297
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 322..533
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 118..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 549 AA; 61984 MW; F2B4F728FD9E7F9C CRC64;
MKLTVSIIEC KNLIVGDLIT NLADPYVICT INAPAQEIRE EEKVLPSPSA VISTHKTLAD
KEGGVIGSAY GSFASLQHLN TLQNPLLSNT VENINQSPTT PRKKSLCITS SLHQSNELAK
YYSPPTTITP TTPRSSRKFS SNDLAKKRAS TRTINSSSSG GNTSSISEDI HSGSNGIGHI
VNGHRSSSSS DSNDKNSAVT MDSPVYEYEN RRPCEFKNRK IIAQKKTEII YNNLNPIFTD
EHLVVEGIKD ESVVKNWIIT LEVFDYDYMK YDDYLGSVEI SFEKYQIQVL QPMVLTVPLE
GVPNGEITID INLGEESKVF GLELEKIMSR HREKIHGLGL PKCVHDMFVF LSDEISICEE
GIFRIPGKSD LITAIKKQYD QNEDKEIKNY ILDQEKVFLT DPEQKRSPAM VKITASLLKD
FIRSLPTPLL TYQLYDEFVD LKNDDKTILE LIQKLPPLHQ HLLYWLLALI SMIESKSQLN
KMSASSLASV IAINLLRKKD ENKSANSLES LRMETDRVIK CVELLINKYQ TVLKPYFEKT
YSFFKQQEL
//
