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Database: UniProt
Entry: A0A099YZI5_TINGU
LinkDB: A0A099YZI5_TINGU
Original site: A0A099YZI5_TINGU 
ID   A0A099YZI5_TINGU        Unreviewed;       791 AA.
AC   A0A099YZI5;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   SubName: Full=Ras GTPase-activating protein 2 {ECO:0000313|EMBL:KGL73925.1};
DE   Flags: Fragment;
GN   ORFNames=N309_03416 {ECO:0000313|EMBL:KGL73925.1};
OS   Tinamus guttatus (White-throated tinamou).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Palaeognathae; Tinamiformes; Tinamidae; Tinamus.
OX   NCBI_TaxID=94827 {ECO:0000313|EMBL:KGL73925.1, ECO:0000313|Proteomes:UP000053641};
RN   [1] {ECO:0000313|EMBL:KGL73925.1, ECO:0000313|Proteomes:UP000053641}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N309 {ECO:0000313|EMBL:KGL73925.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KL886535; KGL73925.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A099YZI5; -.
DR   STRING; 94827.A0A099YZI5; -.
DR   Proteomes; UP000053641; Unassembled WGS sequence.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0046580; P:negative regulation of Ras protein signal transduction; IEA:InterPro.
DR   CDD; cd08401; C2A_RasA2_RasA3; 1.
DR   CDD; cd04010; C2B_RasA3; 1.
DR   CDD; cd13370; PH_GAP1m_mammal-like; 1.
DR   CDD; cd05394; RasGAP_RASA2; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 2.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR039360; Ras_GTPase.
DR   InterPro; IPR037773; RASA2_PH.
DR   InterPro; IPR023152; RasGAP_CS.
DR   InterPro; IPR001936; RasGAP_dom.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR001562; Znf_Btk_motif.
DR   PANTHER; PTHR10194:SF21; RAS GTPASE-ACTIVATING PROTEIN 2; 1.
DR   PANTHER; PTHR10194; RAS GTPASE-ACTIVATING PROTEINS; 1.
DR   Pfam; PF00779; BTK; 1.
DR   Pfam; PF00168; C2; 2.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00616; RasGAP; 1.
DR   SMART; SM00107; BTK; 1.
DR   SMART; SM00239; C2; 2.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00323; RasGAP; 1.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 2.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   PROSITE; PS50004; C2; 2.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS00509; RAS_GTPASE_ACTIV_1; 1.
DR   PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
DR   PROSITE; PS51113; ZF_BTK; 1.
PE   4: Predicted;
KW   GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053641};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00432}.
FT   DOMAIN          1..89
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          100..240
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          306..500
FT                   /note="Ras-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50018"
FT   DOMAIN          555..656
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KGL73925.1"
FT   NON_TER         791
FT                   /evidence="ECO:0000313|EMBL:KGL73925.1"
SQ   SEQUENCE   791 AA;  91175 MW;  CC7F95A8081F2D55 CRC64;
     EAKHLVPNKM RDVFCTINLD QEEVFRTQVV EKSLSPYFGE EFYFEIPRTF QWLSFYIYDK
     SVLQKDLRIG KVSIKKDDLC NYTGKESWFL LQPIDSNSEV QGKVHLELKL NELITDNGSV
     CQQLVVHIKE CHGLPLINGQ NCDPYATVSL VGPSRNDQKK TKVKKKTSNP QFNETFYFEV
     TRSSSYTKKS QFQVEEEDIE KLEVRVDLWN NGNLVQDIFL GEIKVPVKVL RNDSFQAWYL
     LQPRENGNKS SKTDDLGSLR LNICYTEDYV LPSEYYASLR NLLLKSSDVQ PISASAAYIL
     SEVCRDKYDA VLPLVRLLLH HNKLVPFVTA VAELDLKDTQ EANTVFRGNT LATRCVDEMM
     KIVGRHYLKV TLKPVLDEIC ESPKPCEIDP IKLKEGDNVE IHMENLRYYV DKVFREIVRS
     SISCPTLMCD VFYSLRHLAA KRFPNDPHVQ YSAVSSFVFL RFFAVAVVSP HTFHLRPHHP
     DAQTSRTLTL ISKAIQTLGS WGSLTKSKLS SFKETFMYEF FKTFQEEKFT ESVKKFLDDV
     SSTESKEPSG LSEPVHLKEG EMYKRAQGRT RIGKKNFKKR WFCLTSREFT YHKQQDKEPI
     FTIPIKNILA VEKLDESSFN KKNMFQVLHG EKPLYIQANN CVEASEWIEA LCRVTRCNQK
     RLNFYHPSAF LNGNWLCCKA TIENTEGCAR CTADVPADTQ IEIDGDRETE RIYSLFTINI
     SKLQKLEEAC GSIAVYQGPQ KEPDDYSSFT IEDSVATFHT LKQIIDIVEK LNDSHEKYQK
     KRSSSAKYGS E
//
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