ID A0A162PS34_9CRUS Unreviewed; 1410 AA.
AC A0A162PS34;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Putative Ras GTPase-activating protein nGAP {ECO:0000313|EMBL:KZS19101.1};
GN ORFNames=APZ42_014597 {ECO:0000313|EMBL:KZS19101.1};
OS Daphnia magna.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia.
OX NCBI_TaxID=35525 {ECO:0000313|EMBL:KZS19101.1, ECO:0000313|Proteomes:UP000076858};
RN [1] {ECO:0000313|EMBL:KZS19101.1, ECO:0000313|Proteomes:UP000076858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xinb3 {ECO:0000313|EMBL:KZS19101.1,
RC ECO:0000313|Proteomes:UP000076858};
RC TISSUE=Complete organism {ECO:0000313|EMBL:KZS19101.1};
RA Gilbert D.G., Choi J.-H., Mockaitis K., Colbourne J., Pfrender M.;
RT "EvidentialGene: Evidence-directed Construction of Genes on Genomes.";
RL Submitted (MAR-2016) 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:KZS19101.1}.
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DR EMBL; LRGB01000446; KZS19101.1; -; Genomic_DNA.
DR STRING; 35525.A0A162PS34; -.
DR Proteomes; UP000076858; Unassembled WGS sequence.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR CDD; cd04013; C2_SynGAP_like; 1.
DR CDD; cd05136; RasGAP_DAB2IP; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR021887; DAB2P_C.
DR InterPro; IPR039360; Ras_GTPase.
DR InterPro; IPR023152; RasGAP_CS.
DR InterPro; IPR001936; RasGAP_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR PANTHER; PTHR10194:SF125; RAS GTPASE-ACTIVATING PROTEIN RASKOL; 1.
DR PANTHER; PTHR10194; RAS GTPASE-ACTIVATING PROTEINS; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF12004; DAB2P_C; 1.
DR Pfam; PF00616; RasGAP; 2.
DR SMART; SM00239; C2; 1.
DR SMART; SM00323; RasGAP; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS00509; RAS_GTPASE_ACTIV_1; 1.
DR PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW Reference proteome {ECO:0000313|Proteomes:UP000076858}.
FT DOMAIN 259..376
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 434..628
FT /note="Ras-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50018"
FT REGION 34..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 780..833
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 852..892
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 970..1017
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1081..1122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1147..1200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1263..1296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1221..1248
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1303..1330
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 37..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 780..828
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1081..1118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1168..1193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1410 AA; 155447 MW; E6B058720D393411 CRC64;
MAEGNSPQQQ YAKSRLSRMR NVRANAAGML RRAPSFLPES SNGNTNGGGG HVATNSVGRV
GGATKLKRSN SSSSTFYVQL PSTERKHSSA YFNRFDFRSS CHAQQRIEGE SGHDSDTSGC
ESGKLISSPS LLCTHLSAAF GVFSLPVTES IPFEELMSQV WAPKRDGVIF LLQYIERVGL
SRLRTSRSHE SLLCGPGGIG GSSPQNAVQT VDLSSSESGD IGVRQLHQSV LGEDHCLQIT
RPSGNVYIAC SNAEERDRWR NCLKKTIQPV QEHVRRTDNS LKIWILEAKG VANKKWYFCE
LCLDKSMHAR TAGKQKNDLC FWGQHFEFDD LPVVHNININ LYREADRKKK KDKTFVGTVT
IPVNTITSRF LIEKWYPVVS EKGSSKEPPS LRIKCKYQTV DILPLEVYEE FLEYLKTDYM
TVCDLLEPVI GVKAKEDIAT ALVAVMQREG YAQKFLADIV MADVDKIDDE HLTFRGNSLA
TKAMEAYMKL VGENYLQDTL AEVIGGIVDH AADRDCEVDP LKVTSPAMLA KQQAHLRAVV
ESSWRCILNS TPYFPAELQE CFYTYRQRLA GFGREEVADH LISASIFLRF LCPAILSPSL
FGITPEYPSD KAARNLTLIA KTLQTLANFT RFQGKENFME FMNDFLEKEA STMKQYLKEI
SSPLSKDQSY SKFDDYIDVC KNLSILHTLF SESLSKVAPL SQRMDKLQRI LDGISAHLSQ
PVTSMPPYSR QTSLPVPSAG VVTVNGQRNC NKMVDVERPG FQSLQRNVFR FNDPTVTSVT
VSGSANTNGH HLQHSGADGS TSPKASTLPR NAHLMTPPVT TGMNGNLSAP GRRTAIDLTT
SDDYVMFSAL NQSADQSGGP SSGLNTQQQQ QQQQQRQTNG HYGSNGATSF NVKNGSAKYE
RVLGLGPNKQ AVTASANANL DEFIDSLQYV DESPDAHSGG EGDNNTQGSQ VSISQLSTVA
SSGYQSFAYS QSSSPVDPTI SNGQDPASTN MNGHRSTSSG SFRKASAASP TSTAANNNVN
EHSAAIAFTN PVYNLRNKPT TPLARGYSSA YGYDNVLNRT PSCEDVHQTV MNAPRVTLIS
NGGGCGSSPN NNSLSSGTMS RTRISSSSSD STSCLTTPPH ERRLFISTAP RTNPRCIYPS
PVPAQHQVSP VEGNNSGDYV AIRRKGRKSS VTSIQNSRSR IYDSSSSDSD YDQLPSTRFR
ERNVKRGSRM ALDRFSNPKS LDEYEKEIMD LRNAMESLQS RLSRAEQLYL QGAMQAALAV
KERELEEKRR DNESRSSLSS SRYTPSPIME PQPLDEIKDN GQLKSMITRL VSLEEELHRE
KRKMADKQKV IEAQVQTIQA LDAANNRLLS ALAQLRNYQV VEPAEHDEVE RNIMSFARNP
LPEPDYGGSA SLSMARRILA DLGEVQSSSC
//
