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Database: UniProt
Entry: A0A0M9A0H3_9HYME
LinkDB: A0A0M9A0H3_9HYME
Original site: A0A0M9A0H3_9HYME 
ID   A0A0M9A0H3_9HYME        Unreviewed;      1659 AA.
AC   A0A0M9A0H3;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Rho GTPase-activating protein 100F {ECO:0008006|Google:ProtNLM};
GN   ORFNames=WN51_14429 {ECO:0000313|EMBL:KOX73383.1};
OS   Melipona quadrifasciata.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC   Anthophila; Apidae; Melipona.
OX   NCBI_TaxID=166423 {ECO:0000313|EMBL:KOX73383.1, ECO:0000313|Proteomes:UP000053105};
RN   [1] {ECO:0000313|EMBL:KOX73383.1, ECO:0000313|Proteomes:UP000053105}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0111107301 {ECO:0000313|EMBL:KOX73383.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KOX73383.1};
RA   Pan H., Kapheim K.;
RT   "The genome of Melipona quadrifasciata.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KQ435798; KOX73383.1; -; Genomic_DNA.
DR   STRING; 166423.A0A0M9A0H3; -.
DR   OrthoDB; 2905108at2759; -.
DR   Proteomes; UP000053105; Unassembled WGS sequence.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd00030; C2; 1.
DR   CDD; cd00992; PDZ_signaling; 1.
DR   Gene3D; 2.30.42.10; -; 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; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   PANTHER; PTHR46150; RHO GTPASE-ACTIVATING PROTEIN 100F; 1.
DR   PANTHER; PTHR46150:SF3; RHO GTPASE-ACTIVATING PROTEIN 100F; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00228; PDZ; 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   SUPFAM; SSF50156; PDZ domain-like; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000053105}.
FT   DOMAIN          196..266
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          927..1065
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          1103..1289
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          64..83
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          303..353
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          602..641
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          659..739
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          829..893
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1307..1334
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1346..1384
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1402..1480
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1579..1618
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        303..331
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        338..353
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        602..622
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        659..711
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        829..870
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        879..893
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1432..1457
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1458..1480
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1592..1612
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1659 AA;  183608 MW;  9D49E4730FD9CB17 CRC64;
     MLYLDAPRSH KIFGSYVNND TETTQLNSEF TIYFSKGASH VLKLGIGNFD GMKLLEEGRG
     EVTDISASPG RQAPANQLRP KEPPPMVIQG DFRKKDESVE QFHEVLFILN ASVHDMAWLK
     WKDLSLQVSG ISTEIFKQIE TVENDHDAST AAALEAVERR GEMVVRVIEP RQMGRQASEA
     AKKFIAMQDP KHPIHFVEII KRPGQTLGLY IREGNGVDRN DGVFISRIAL ETAVYNSGCL
     KVGDEILAVN LVDVTHMSLD DVVIIMSIPR RLVLATRHGQ HQPVSHSRQT EHKAPPVVVI
     KRELNEDESD HATSNHVRDG NRRRGDGREM LPSRSRLGLS GLGSSQDLGS SNGDLYYNSR
     PEGHWSYQPP PPPVITHQPK PSATQHFQPY ERGYPKTLES LAEKVSPCDA LLVPRDFDAG
     RGFHKGKETT NSFLISRLML CSNPLHRAPP GQWTTRTSKN LSQKAQKSVT FMVSQFNLDV
     FVENSKKMLN ISPGVQVHSF YTGPVMPSNG GRRMSTGAGM QSVGSRLSSQ TQSSHYGYGQ
     HAGSGRIMPR SGSDQHLPRV DYTSITTPAR HTLLRSSLKS VYKTLDSYFT TGTSALRYNT
     RYGSQGDSTT ATQRQGQFGT LTRRHRPSLD YASDTEATCS SSPKSAYYYY RHNMNNPPQS
     SAVSHLATLS RSQIGQSSSG LRSNSLPRSG RTLPQQPGLR SGLSTVASGL IDQEDSDGAL
     SAPELPSIRR DRGRIPSSPS VFTSDEYRAW LSRTPSTSAL YEQIRASTTR PPRYTYSAEN
     IHAAANQGEY GSYGAYRPLS STLDRLSTRS ASAQQVNLAN LRASTAISST CHRGTANPRP
     ASVASSARTS LTSQKPSLSS SATQRATSVR RIRNLLDLES TRSIPTPTPT RTQDQRLLDI
     NPAGDIQVLE FLKYKIEKPP TVGTPSSTNS LLSSLGETSS GDLAGGVSGL LWVHLLAGRG
     LRSTTSSSAA TTPSTPSGQP NLASCGLRDL YCVLECDRVH KARTVMRTGD LMFDWDETFE
     LDLVGNRQLD LLVYSWDPQY RHKLCYKGSV HLATLLKESP VHQLAVKVEP RGTIYLRLRY
     TDAQQTFRRR GLPTGGVPGG VSTALAMGVP NVPIIVWRCV EEVERRGLDI IGLYRLCGSA
     TKKRILREAF ERNARSVNLS PDNVPDINVI TGVLKDYLRE LPEPLFTKCL YQMMVDALAV
     CLPDDPQGNA KLMFSILDCL PKVNRCTLIY LLDHLAMVVS QCNKMSPASL AVCFGPVLML
     HSEENGPPLD FQQPIAVLKY LLEIWPVKSV RKISSVASTL PRVTPAVEHN NSHQPLQQQQ
     QPQPQQQQVQ QQVQQQVQQQ LQGTLGRTGL PWQPPHSLHQ QPPTTAPAAL AASIRPPPPV
     KPRQEMTLFG TAFLFVQVIV SSPGSPSSEE SEASPEPINK SLLGGLGLEK SNEGATANST
     GPGTEQITPT SSVDTEEGNT THPEEGEKGV EGDAEASDDD RHQHMIWKDV FNKVLNKNKS
     QVSQRENKET KKKEEYSISK IDLQESTNIF GKLQKIRRTG LISSGGLSDW PSDLNYRKIQ
     KDQACIYWTL KTPTSRGIRG TEVRFSSQSK EKEEEEEEEE EEEEEEEEEE EEDITLHKSK
     KTYAYQGRSW LSWGQVIYSD SWCTVLKAVE RHESPRTEL
//
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