ID A0A232FJM6_9HYME Unreviewed; 2468 AA.
AC A0A232FJM6;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Ras GTPase-activating protein 1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=TSAR_002549 {ECO:0000313|EMBL:OXU30668.1};
OS Trichomalopsis sarcophagae.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Proctotrupomorpha;
OC Chalcidoidea; Pteromalidae; Pteromalinae; Trichomalopsis.
OX NCBI_TaxID=543379 {ECO:0000313|EMBL:OXU30668.1, ECO:0000313|Proteomes:UP000215335};
RN [1] {ECO:0000313|EMBL:OXU30668.1, ECO:0000313|Proteomes:UP000215335}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Alberta {ECO:0000313|EMBL:OXU30668.1,
RC ECO:0000313|Proteomes:UP000215335};
RC TISSUE=Whole body {ECO:0000313|EMBL:OXU30668.1};
RX PubMed=28648823; DOI=10.1016/j.cub.2017.05.032;
RA Martinson E.O., Mrinalini, Kelkar Y.D., Chang C.H., Werren J.H.;
RT "The Evolution of Venom by Co-option of Single-Copy Genes.";
RL Curr. Biol. 27:2007-2013(2017).
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004406};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004406}. Membrane
CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}. Microsome membrane
CC {ECO:0000256|ARBA:ARBA00004174}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004174}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|ARBA:ARBA00010617}.
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:OXU30668.1}.
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DR EMBL; NNAY01000133; OXU30668.1; -; Genomic_DNA.
DR STRING; 543379.A0A232FJM6; -.
DR Proteomes; UP000215335; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0009887; P:animal organ morphogenesis; IEA:UniProt.
DR GO; GO:0048468; P:cell development; IEA:UniProt.
DR GO; GO:0060429; P:epithelium development; IEA:UniProt.
DR CDD; cd11056; CYP6-like; 1.
DR CDD; cd11788; SH3_RasGAP; 1.
DR CDD; cd14277; UBA_UBP2_like; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 3.30.505.10; SH2 domain; 2.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR023152; RasGAP_CS.
DR InterPro; IPR001936; RasGAP_dom.
DR InterPro; IPR035652; RasGAP_SH3.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR022166; UBAP2/Lig.
DR PANTHER; PTHR24292; CYTOCHROME P450; 1.
DR PANTHER; PTHR24292:SF105; CYTOCHROME P450 9AC1; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00067; p450; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00616; RasGAP; 1.
DR Pfam; PF00017; SH2; 2.
DR Pfam; PF00018; SH3_1; 1.
DR Pfam; PF12478; UBAP2-Lig; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR PRINTS; PR00401; SH2DOMAIN.
DR SMART; SM00239; C2; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00323; RasGAP; 1.
DR SMART; SM00252; SH2; 2.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF55550; SH2 domain; 2.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR SUPFAM; SSF46934; UBA-like; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS00509; RAS_GTPASE_ACTIV_1; 1.
DR PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
DR PROSITE; PS50001; SH2; 2.
DR PROSITE; PS50002; SH3; 1.
PE 3: Inferred from homology;
KW GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000215335};
KW SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW ProRule:PRU00191};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 77..167
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 174..236
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 246..334
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 372..564
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 451..564
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 620..793
FT /note="Ras-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50018"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 873..895
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 940..1049
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1195..1214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1247..1273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1310..1331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1521..1540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1570..1608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1708..1729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1803..1837
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1897..1922
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 994..1020
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2468 AA; 273588 MW; E3FC3042630AD8BF CRC64;
MAEFVRGGPS VSNNAKIENT KKGDSPSTGS EDGGNIEPIN DNDFDVFLEN IPDDIQDIEE
PDHTNNTTFS APPENQWYHG RLDRFTAEER LRDASRLGSY LVRESDRKPG SYVLSYLGRT
GINHFRITAV CGDYYIGGRQ FNSLMDLVAY YTHCSDLLKK ERLIHPTPPP EPVNDKKRIV
AILPYTKMPD TDELSFQKGD IFFVHNDMGD GWLWVTAHRT GEQGLIFREL VDDLDDSIDP
NTVFSWFHPN VTKSEAVDML VKAGPGSFLV RPSDNSPGDY SLFFHINNQI QRFRIEKKGV
RYLMGGRTFE CLDAVINRYR KEQIVEGHTL VQAMVTEPDG TVRVNKEVQH AEKIYATLRE
CREQSGAKKN KGIKMQGYLE KKSEKNKKWK ALYFVLVVDA SDTHLYLYDN PKRTKPKGLI
DLSCAYLYQV HETAPNSETA SDWINALKPL CVSQLTRAPK VARLRELRSL QLHIMDAHRL
PYKLVPNPFI IVALNNVKVA RTKMKTGPHP VWDEEFILED VPPDVMSFSL TLYNKGKRSK
DTEVAELIVE LSSLANGEEM DEWYPFAGVT PIGDWGALRL RLRYRHDLAM PPEEYSPLQQ
LLLDPELHVV KALADVCHLD RIPLANSLLR IFRHEKREAD LLKSLNQAEV DKEDETPTLF
RAASLTTTLM DLYMNKQSCE LNPSKMDSPE DACSNAEFLL QVLDEVTLSI FTSPDMCPKS
LRYICCCLQR AVVAKWPHER LVRTRVVSGF IFLRLLCPAI LNPKSFNLIA ESPSPAATRS
LVMVAKCLQN LANLVEFGGK EPYMEVVNPF ILKNKERMVV FLDQLSNVSD KPEPECISPR
GKCISDIAKD LATLHHICVS HLKELQILSK QQHKSDQLKH TQSDNRNNSK EDVALNERIK
QVMELTRRSE DEVIMALHDC DDDLNRAVND LLEGVSPEWE VKKKKARQTG GPKQNSEQSG
VPDSNADWGE DKRSLYTNDG SSRVRGGRGG NHNNRGWRRR ENKENEKNSE EGKSDAPHGG
SRRGRGVSGR SGRGGRGGGR GLGPRTFANR GKLDAWSGID ATEDWDNEEY TGSLADTKVF
TPSTLTTEAA AVPEQPKSEE LPSIKPIRSA GLLEHNELPK ISGATATAQE TVIQEQSHQD
IINMPSMHLP HSLDDVNRGS LSAAQSEYFT QLAQANDINL NVSTGQTTFL SVMNSQPQRQ
TKHRPRVPPP SKIPSTAVEM PGDALNSSIS FLDVQFGALE FGSDASITDG TNQEKFNSSR
SSPGTSSVES TSITTKTVVN SINSLNVEVA QASPSQKFST TTKMLRSDNQ CIPKEHSINS
QSGLTSRSAA TQPVDIQKQD LSAQTSLSNS STYNAATVTY QSPKPSYSTS VTSSNYSSYA
PSNQASFSCP TTSSHANSFS GIAPVTQSGY SSPYTQPITT YSQTSSSSST SGIYNQASTT
TQGYQQTTGF TTTPISQYQS QAVTTNASSN SSSYISPGYQ NPSTFQSTAQ TYQPSNTTFV
SSISQGSSVY SNTSQSVYSN TYPSYGSQNQ SGSQDHKLST NKDLQFDNNA TATSTSLATT
AVSTLGLTSS SVNTSQTKTT MSSTVPKSTV SGLVPSSSSS SSSISGSGTT GNIAPILSHQ
YIMGQSVPYA TFQQPHMYSY EDLQLMQQRM PHMPTTGYYD ATLGYQTTGP VTSLGNSRSD
ALSGVQGVQG VQAVQGQYTS INDARFTRTD SNASPVSSTM SQQSATQHQQ PLMNPIPPGY
AYFYGGGIMP AGGFQYGTPA IYPQIATAGS AGTTSGAYNT KPGSYGSGYG SGTNYDSLTN
SASSGDYKST ASGYTSSQTG KNGSSSANTN TAGTSTDINT TMYTKGHVTL NKVNSYDKQT
FHSATPPPFG LTNNQNANVI SGYGTHLFIP TLPHQLHQPL HQDSGNSSGQ RTNTNSQNKA
QVKPGYSTSY WAGDMNMMES LAPMLHTKLF WLTAVVTLIW VHFKFVIYTY WKRKGIPHDE
PVVPFGSTLP IFLGKSSMGN LVKQKYQKSK KYPLYGIYMF HQPMLLINDP DLVRIILIKE
FNKFRDRGLY FNEKVDPLSG HLFLLPGERW RKLRAKLTPT FTSGKLKQMF PLLMEIGDEL
IKVCEKIIQT DSVVEFKDLN ARYTVDTISS IAFGFNCKSL DNPNNEFKRY GSMVFDQSPI
RNALGTFAPV VLDTLRIPLI RRVIIDFFSQ TFKDMVDHRH SNKIVRKDFI NLLMQLMDKG
VLEEDETSQK SNDHAKAAES LGNMFEIAGL IDNEKISMVE AQAQAFVFFL AGFETTSSTI
TYCLYELALN PHIQEKLQAE IDEHLAKPGG MTYDRIMNEL EYLHMVFSET LRKHPSVPIL
NRLCIEDCDL PNTNFRIKKG TGVMISVSGM QRDPNIYPDP DKFDPLRFTK ENIASRSPYV
YLPFGDGPRV CIGTRFGILQ SKIALIALLA KYKFSVCDKT SIPINYSKRS FTQSPEGGVY
LRMEKRIK
//
