ID A0A137QSH5_9AGAR Unreviewed; 2087 AA.
AC A0A137QSH5;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Dedicator of cytokinesis protein 3 {ECO:0000313|EMBL:KXN90212.1};
GN ORFNames=AN958_04702 {ECO:0000313|EMBL:KXN90212.1};
OS Leucoagaricus sp. SymC.cos.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Agaricaceae; Leucoagaricus.
OX NCBI_TaxID=1714833 {ECO:0000313|EMBL:KXN90212.1, ECO:0000313|Proteomes:UP000070249};
RN [1] {ECO:0000313|EMBL:KXN90212.1, ECO:0000313|Proteomes:UP000070249}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SymC.cos {ECO:0000313|EMBL:KXN90212.1,
RC ECO:0000313|Proteomes:UP000070249};
RA Hu H.;
RT "Leucoagaricus sp. SymC.cos WGS genome.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the DOCK family. {ECO:0000256|PROSITE-
CC ProRule:PRU00983}.
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DR EMBL; KQ962070; KXN90212.1; -; Genomic_DNA.
DR STRING; 1714833.A0A137QSH5; -.
DR OrthoDB; 8258at2759; -.
DR Proteomes; UP000070249; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR CDD; cd08679; C2_DOCK180_related; 1.
DR CDD; cd11684; DHR2_DOCK; 1.
DR Gene3D; 1.20.58.740; -; 1.
DR Gene3D; 1.25.40.410; -; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 1.20.1270.350; Dedicator of cytokinesis N-terminal subdomain; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR027007; C2_DOCK-type_domain.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR026791; DOCK.
DR InterPro; IPR043161; DOCK_C_lobe_A.
DR InterPro; IPR043162; DOCK_C_lobe_C.
DR InterPro; IPR032376; DOCK_N.
DR InterPro; IPR042455; DOCK_N_sub1.
DR InterPro; IPR027357; DOCKER_dom.
DR InterPro; IPR046769; DOCKER_Lobe_A.
DR InterPro; IPR046773; DOCKER_Lobe_C.
DR InterPro; IPR006594; LisH.
DR PANTHER; PTHR45653; DEDICATOR OF CYTOKINESIS; 1.
DR PANTHER; PTHR45653:SF10; MYOBLAST CITY, ISOFORM B; 1.
DR Pfam; PF06920; DHR-2_Lobe_A; 1.
DR Pfam; PF20421; DHR-2_Lobe_C; 1.
DR Pfam; PF14429; DOCK-C2; 1.
DR Pfam; PF16172; DOCK_N; 1.
DR SMART; SM00667; LisH; 2.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR PROSITE; PS51650; C2_DOCK; 1.
DR PROSITE; PS51651; DOCKER; 1.
DR PROSITE; PS50896; LISH; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000070249}.
FT DOMAIN 648..845
FT /note="C2 DOCK-type"
FT /evidence="ECO:0000259|PROSITE:PS51650"
FT DOMAIN 1566..1977
FT /note="DOCKER"
FT /evidence="ECO:0000259|PROSITE:PS51651"
FT REGION 167..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..527
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2087 AA; 235098 MW; 8FCD186EDBF96EFF CRC64;
MWEPLPLIVY GYAIHPLTPY KREARQSLRN RLSTVTEASA DDHSIMLRDV VSLEVGDEVY
AFEKYTPSAK DFVEGPWYRG YVVCTARRPP ISWSESSTAR PAKLEEPQQV FIGIFPASHI
FVRDELPDAE GRLLELAHSL GGGAADGEYL ASGAWTRDKA MGVLQEVDEQ PASRAPIRSA
SVRSVSIRSS SPPLSHIDRP LPPRPSLKSG DDTASGVEQP IIDEIASALR EWHTLMFHYL
ARRDYKLFQV VREHIEALHS GRRQLLAQTL NAEETDYMLR ECVIRLVSGN LVQGLDVIVR
HPTWGGLVNV DIDTVPVPRS WISAVRMYAM QTSLAYINVR DDVEIKPYRI STDQLLTNTL
PTPANSAFPE LPHLHQRTRS QSSAGLIRSS TRHSTAKFFH VFLDLRAFVA SPCAPGETAE
LFFSLYKKQG TQFVTEEFCA ILNHNGVLAR DPSTKIRTLF TDLAYADIQD PIYLVCRIVR
SGSFKIGSGF SENGKRGSEV SYRNEQAWDS KQSPGANGTR NLSNGDSTSF VRRPFGCAVL
ELTQLSKMAA DQSDFTGLKE YTMPIYVPTN EASFSMIHQS IINNIAKEYD KSPRHVSSVI
LAEMLAVSIK IFRGDAPAVV RENPSLLHDI PHTLRLGFPD VVFPGDKRNE LYIKLWCGDF
GASNNTSGRL SLGRPPNGNV QITTEIKDQN GRMVENVISQ GSGEPLMSQF HSMVFHRTVE
PTFGELIKIK LPPNEVPNWH LFFTFRNRSG REKAGGKSGT DTLDRPFAFA FQPLFPDSSA
FVEDGSHTLV MYRADRISQL TPDIYLPSPS TLSAGQKADQ LAIPPELQKL APPLKDTLTI
RTSLCSTTLT QNPTLFQLLG WESISDKDTL SHLLTRFTFV GEGEIVKFLR DIFEALFGIL
VSQNNQSGEM DLLVFNALVT VLGIVQDRRF SNFQPVLEVY IEKHFTCAGA TSHIIHSMNR
LLINPTSEET AHHLRAALKV WHYIFKFIAR SRELQKAKEI GMGGGAIAEH FEATFKRELR
AHISEVTRMM SISSPAIVGT QTIALQHFTS ILPELEKIFT NVELVSIATT FANAVTANKG
KIVIWKLIMY LHMVKGFLFD HTQSRPLLVE AVVIWIKPHF GRYDEYLHTS THDSDAVRDA
ARLTWLESIR LCITIIAVML DKLQQNLVKP EIRVDNRKYR QEQENVDCLL SLLPRLLDSY
RELQSPASRK VMEQTRSQPN YRSSIPVTFP ESYPFSLLAS LPETPRSVGV TAAVPKDADN
LFSPALGETA VVILVLILAL PVKEILNFME NSLVIEGRDR FISLLSQLFK VATSILDNEV
FPRTWLNINI LAHKVLIKMM EPVATILEKE FIPPQEQESD FDSNVWRECF YMLLRLLSSD
QLVIEEFSPQ KRRAVWRLAG DIRGDGAAIL LNLWQALGTS VLGGGTELPI RYGGYQVYLH
SLVGHVVNLC LSHHDQLRNN AVQMLFSMIV TEYHQSEHFD GIENELVTRL DSLFMSDSKG
DDISRAFFIS QLRLLFTTSD VDEQLRERVS NFLDSVDLFL ELLLSVRDLP EGEEFQDDRV
MATVRLALVK QDEIYIKYVH QLVNMHLQSQ NYVEAALTLK LHSDLHEWDL NSFIGPMEDL
GLPQQSHFHR KETLCLLILN YLGQGKAWET AIEICKELAF QHAGVTFNYS RLSEILRHQA
TLLEHIVAEQ RYYPDYYRVT FYGNFPAAIR DKRFIYRGYE WEKFGAFCER MLNKHPGAQL
LKTPGDPPVD IRFGNDQYIQ CTAVTPEPDR TSPIFTNPDV PLAVRTHYEH SAINLFSSSR
QVKKTARDGS EEIWHEKTYF TTEETFPTVL RRSEVVAVEI VEISPLENAL NEVELKTKEL
SSLYQKYQAL AKTAQHVSTN ALAMALNSAV DAPLNTGISS YRQTFFNPDY VARNPERVEL
LEKLRIAIDE QVRVIDSCLK LHGHLCPPEF IPFHETLEKF FKRNFKEEIK RLAVEVSDSI
SPMPNSKQQT PLQRHLAHLA RHGITGVASA PGDMVGSDSM SVDSPRNSFI NVGNGNNAIQ
STSAPQVSGA SVAPSFMGSV GSFSLRTRLS RFGSITFGWP GRNATNT
//
