ID A0A0V0YEK1_TRIPS Unreviewed; 1949 AA.
AC A0A0V0YEK1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Dedicator of cytokinesis protein 1 {ECO:0000313|EMBL:KRX98671.1};
GN Name=F40A3.3 {ECO:0000313|EMBL:KRX98671.1};
GN ORFNames=T4E_9039 {ECO:0000313|EMBL:KRX98671.1};
OS Trichinella pseudospiralis (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6337 {ECO:0000313|EMBL:KRX98671.1, ECO:0000313|Proteomes:UP000054815};
RN [1] {ECO:0000313|EMBL:KRX98671.1, ECO:0000313|Proteomes:UP000054815}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS141 {ECO:0000313|EMBL:KRX98671.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the DOCK family. {ECO:0000256|PROSITE-
CC ProRule:PRU00983}.
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:KRX98671.1}.
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DR EMBL; JYDU01000019; KRX98671.1; -; Genomic_DNA.
DR Proteomes; UP000054815; 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 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 Gene3D; 2.30.30.40; SH3 Domains; 1.
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; IPR046770; DOCKER_Lobe_B.
DR InterPro; IPR046773; DOCKER_Lobe_C.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
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; PF20422; DHR-2_Lobe_B; 1.
DR Pfam; PF20421; DHR-2_Lobe_C; 1.
DR Pfam; PF14429; DOCK-C2; 1.
DR Pfam; PF16172; DOCK_N; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS51650; C2_DOCK; 1.
DR PROSITE; PS51651; DOCKER; 1.
DR PROSITE; PS50002; SH3; 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:UP000054815};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 7..69
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 444..632
FT /note="C2 DOCK-type"
FT /evidence="ECO:0000259|PROSITE:PS51650"
FT DOMAIN 1275..1703
FT /note="DOCKER"
FT /evidence="ECO:0000259|PROSITE:PS51651"
FT REGION 1783..1856
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1886..1949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1783..1805
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1806..1856
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1911..1929
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1949 AA; 223754 MW; 1D8D06980B35113A CRC64;
MWTKVNEDEK IVVAKHNFRP NVVGNYLPLL IGDVVRVLQF SGEWYYGCLD NDMTKVGVFP
ISFVEEKHAN FENNELGSIA QTAVYSVLTV LKEWRKMCRE SFEQRGSIDI GKIFPMMKDI
INWRSQIVSK KLSLEEVKKL NYKIALKIDL GNKMLGADVI VRDIHGNELQ TENCSVAELH
KHHLETAERI ATEIRHSSRA EKFMQTKRSQ SNWNLLLTFV EFHHPYMNNG ELSFMLFDGR
LWHGISEPAV VVVQQNSSTR FGVDPAPLQR FIITDLGTKD LDRDKFWIIF LATKTGPFEW
KDTLTYRKTH VSSTTVRQTF AVAALDLTEL LNQAFCTDAD AAGAGAGATA FSSTIDEQEE
RRIFVPLRLL VDDSVEGMLR KIVDNKIGYN SELEAKGDGF WLTLQPVFAS LDELKHSQPH
LFSNPLTLVR KMGFPEVISR DDVRNDLFVT LVSGDFTHCT GRSDKNIEVK VCLVDELTNS
VLPDSVVNVG VAKETFYTSS VFYHQDRPKW FETIKFSIPV EIYGNVHIRF SFKHRSSNES
KDRNDRPFSV SFIRLKQSNG TVIKDGFHDL VVYRVSSKIE ENDFSYHTLP ASKADLEMSG
MEGTSSKFHI QSPTGGFAIS PKDFFSISTT VCSTSLTQNV DLLGLLEWET KRVNLKSSLE
ALMKDEGDRA GEEIVKANYL YAVFVVSVVI KFLFFQFLQD ILDVLFTVLI SCNDHDQLVF
DALVYVIGLV GERRYHNFKA VLDSYLLLHF SAALAYQKLI PIFKDYIDKV EECSNKLLKT
LKSLEYLMKF IVRSRNLYVQ LKGSNAGKER FHELICSLFI SLTTLMLYQT DWSLLCQGAA
LKYIPHIVVD VLAVFDAREL AAMMANFLKN VPRDRLTKQK LMCLQDLVHS ELIKKSEPRA
VLLPVILESV RNQIDDNEEL ELCAQILTEI MNVLFDKHST SGAHSSTLLF IMRTILRQVV
QVVVRLIEAG ETLILGQYVA LLLAILEELD ACTYRCYIAE FATRTDLMDF LTELLMLFKD
LIRRPVFPSD WFQMIFVQNS IMLKILCYTA STVKARFLHE KFEFQVCNNF FQTVVTFITQ
KLLQLEQYNV KKRKAILERF RDMRLTCARE LVRSMWFSMN LLEKNQFIPS LVGFVLEVTL
IPVEEVRKLT IPIFFDMMVT EFYLRANNNS TTSSTPLLGN FSYNSSVMEF ETEFIKKLDS
LVENDYGDAK YVDTFVKIMM QLCSSHTEAL RDEGIRFTKT VEHLMFRLLE FRNVRLHHNN
VNNCMSCTVS LLNFYYEIGH TELYIRYLYK LYELHMQRDN FVEAGLTMAL HAECLKWCDS
SVHALLAHSL FPDCVLQREL KEKLFLKMID LFDRGELWEK AIVVCQELQH EYEHRTYEYD
KLANLLEKMS KMYRNILKHQ RAEPEYFRVL FCGLGFPIFL QNTTFIYRGD GYERLADFTS
RIQAQYPNAT VTFKLLLQTL HPPSEEIKKS NGQYLLINKV DPVYDDQIKT IPTPVKDSRI
LWYYKCNDVQ KFYFSRRISK KDCTLSKEWP VADEQENEFG LMWLEKTILV TSCRFPGILR
WFLVSSESQV ELSPLEVAVD SMKATISDLE KLIEEVERYS ERALKPLAAK LQGMLQPAVM
GGIKNYEKVF FTEEFMSKGS RKNLEVLELL KEQIASQVPL LEKGIFLHAK FCSSDQREFH
HLLIDCFKEY KTHVEQHYGK QASLLPENSS LEIPKSNVLV YKQNVMDGSN TFNDGRYPFS
SSIASRKSNS VREWQASTSA PWLLRTGVMT TLSGATVPRR LNSKEAAIRR KAAHSTEKEI
HQKRHSNSSM GSTQSAEMSC AGSTIVLTEK LTTLRPPRPD SSFSKGSFKQ QSNSSINRLT
SSVEKLSISA SHSLVHSDSD EILLTNDRAE DHTAVPPPLP PRRDSGQIVE IPDFNASNIT
FSPLSPQRLP SIISGPRREK PLPPLPTTE
//
