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Database: UniProt
Entry: A0A0V1BT31_TRISP
LinkDB: A0A0V1BT31_TRISP
Original site: A0A0V1BT31_TRISP 
ID   A0A0V1BT31_TRISP        Unreviewed;      2147 AA.
AC   A0A0V1BT31;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Dedicator of cytokinesis protein 1 {ECO:0000313|EMBL:KRY40095.1};
DE   Flags: Fragment;
GN   Name=DOCK1 {ECO:0000313|EMBL:KRY40095.1};
GN   ORFNames=T01_2419 {ECO:0000313|EMBL:KRY40095.1};
OS   Trichinella spiralis (Trichina worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=6334 {ECO:0000313|EMBL:KRY40095.1, ECO:0000313|Proteomes:UP000054776};
RN   [1] {ECO:0000313|EMBL:KRY40095.1, ECO:0000313|Proteomes:UP000054776}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS3 {ECO:0000313|EMBL:KRY40095.1};
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   -!- SIMILARITY: Belongs to the phosphatidylethanolamine-binding protein
CC       family. {ECO:0000256|ARBA:ARBA00007091}.
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:KRY40095.1}.
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DR   EMBL; JYDH01000014; KRY40095.1; -; Genomic_DNA.
DR   STRING; 6334.A0A0V1BT31; -.
DR   InParanoid; A0A0V1BT31; -.
DR   Proteomes; UP000054776; 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; cd00866; PEBP_euk; 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   Gene3D; 3.90.280.10; PEBP-like; 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; IPR046773; DOCKER_Lobe_C.
DR   InterPro; IPR008914; PEBP.
DR   InterPro; IPR036610; PEBP-like_sf.
DR   InterPro; IPR035810; PEBP_euk.
DR   InterPro; IPR001858; Phosphatidylethanolamine-bd_CS.
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; PF20421; DHR-2_Lobe_C; 1.
DR   Pfam; PF14429; DOCK-C2; 1.
DR   Pfam; PF16172; DOCK_N; 1.
DR   Pfam; PF01161; PBP; 1.
DR   SUPFAM; SSF49777; PEBP-like; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS51650; C2_DOCK; 1.
DR   PROSITE; PS51651; DOCKER; 1.
DR   PROSITE; PS01220; PBP; 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:UP000054776};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          198..260
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          670..848
FT                   /note="C2 DOCK-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51650"
FT   DOMAIN          1479..1902
FT                   /note="DOCKER"
FT                   /evidence="ECO:0000259|PROSITE:PS51651"
FT   REGION          1979..2055
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2087..2147
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1982..2004
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2005..2055
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2109..2127
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KRY40095.1"
SQ   SEQUENCE   2147 AA;  245748 MW;  4D8151B3960ADA34 CRC64;
     LSLNRHFSRS ILSKFCNSSM SSLKDKFEEH KIIPDVVDQA PTQHLQVKYK SGVQADLGNV
     LTPTQVKEPP SLNWVATPGA LYTMVMTDPD APSRQNPKFR EWHHWLVANI PGCEINKGEV
     LSDYIGSGPP QGTGLHRYVF LVYQQKSHLT DKEHGHLTNR SGNNRGGFSI RKFAAKHDLG
     APIAGNFYQA EWDDYVPKLY EQLSAKHNFR PNVVGNYLPL LIGDVVRVLQ FSGEWYYGCL
     DDDMTKAGVF PISFVEEKHA NFENNELGSI AQTAVYSVLT VLKEWKKMCR ESFERRGSID
     IEKIFPMMKD IINWRSQIVS KKLSLEEVKK LNYKIALKID LGNKMLGADV IVRDIHGNEL
     QTENCSVAEL HKHHLETAER IATEIEQSSW NTLSHLQRHS SRAEKFMQTK RSQSNWNLLL
     TFVEFHHPYM NNGELSFMLF DGRLWHGISE PAVVVVQQNN STRFGVDPAP LQRFIITVRM
     RIFIIVVVVD LQVGNLCFVV QDLGTKDLDR EKFWIIFLAT KTGPFEWKDT LTYRKTHVSS
     TTVRQTFAVA ALDLTELLNQ AFCTDPDAGT GAGAGAFSST IDEQEERRIF LPLRPLVDDS
     VEGMLRKIVD NKIGYNSELE TKGDGFWLTL QPMFASLDEL KHSQPHLFSN PFKLVRKMGF
     PEVISRDDVR NDLFVTLVSG DFTHCTGRSD KNIEVKVCLV DELTNSVLPD SVVNVGVAKE
     TFYTSSVFYH QDRPKWFETI KVNIFNLEKI FCTLLSKDRN DRPFSVSFIR LKQSNGTVIK
     DGFHDLVVYR VSSKIEENDF SYHTLPASKA DLEMSGMEGT SSKFHIQSPT GGFAISPKDF
     FTICTTVCST SLTQNVDLLG LLEWETKRVN LKSSLEALMK DEGDRAGEEI VKASLLHVGV
     FLQDILDVLF TVLISCNDHD QLVFDALVYV IGLVGERRYH NFKAVLDSYL LLHFSAALAY
     QKLIPIFKDY IDKVEECSNK LLKTLKSLEY LMKFIVRSRN LYVQLKGSNA GKERFHELIC
     SLFISLTTLM LYQTDWSLLC QGAALKYIPH IVVDVLAVFD ARELAAMMAN FLKNVPRDRL
     TKQKLMCLQD LVHSELIKKS EPRAVLLPVI LESVRNQIDD NEELELCAQI LTEIMNVLFD
     KHSTSGAHSS TLLFIMRTIL RQVVQVVVRL IEAGENLILG QYVALLLAIL EELDACTYRC
     YIAEFATRTD LMDFLTELLM LFKDLIRRPV FSSDWFQMIF VQNSIMLKIL CYAASTVKAR
     FLHEKFEFQV CNSFFQTVVT FITQKLLQLE QYNVKKRKAI LERFRDMRLT CARELVRSMW
     FSMNLLEKNQ FIPSLVGFVL EVTLIPVEEV RKLTIPIFFD MMVTEFYLRA NNNSATTSTP
     LLGNFSYNSS VMEFETEFIK KLDSLVENDY GDAKYVDTFV KIMMQLCSSH TEALRDEGIR
     FTKTVEHLMF RLLEFRNVRL YHNNVNNCMS CTVSLLNFYY EIGHTELYIR YLYKLYELHM
     QRDNFVEAGL TMALHAECLK WCDSSVHALL AHSLFPDCVS QRELKEKLFL KMIDLFDRGE
     LWEKAIVVCQ ELQHEYEHRT YEYDKLANLL EKMSKMYRNI LKHQRAEPEY FRVLFCGLGF
     PIFLQNTTFI YRGDGYERLA DFTGRIQAQY PNATLLQTLQ PPGEEIKRSN GQYLLINKVD
     PIYDDQIKTI PTPVKDSRIL WYYKCNDVQK FYFSRRISKK DCTLSKEWPV ADEQENEFGL
     MWLEKTILVT SCRFPGILRW FLVSSESQVE LSPLEVAVDS MKATISDLEK LIEEVERYSE
     RALKPLAAKL QGMLQPAVMG GIKNYEKVFF TEEFMSKGSR KNLEVLELLK EQIASQVPLL
     EKGIFLHAKF CSSDQREFHH LLIDCFKEYK SHVEQHYGKQ ASLLPENSSL EIPKSNVLVY
     KQNLIDGSAT SNDGRYPFSS SIASRKSNSV REWQASTSAP WLLRTGVMTT LSGATVPRRI
     NSKEAAIRRK AAHSTEKEIH QKRHSNSSMG STQSAEMSCA GSTIVLTEKL TTLRPPRPDS
     SFSKGSFKQQ SNSSINRLTS SVEKLSISAS HSLVHSDSDE ILLTNDRIDD HAAVPPPLPP
     RRDSGQIEIP DFNASSVTFS PLSPQRLPSI ISGPRREKPL PPLPTTE
//
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