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Database: UniProt
Entry: A0A0V0ZRK7_9BILA
LinkDB: A0A0V0ZRK7_9BILA
Original site: A0A0V0ZRK7_9BILA 
ID   A0A0V0ZRK7_9BILA        Unreviewed;      2214 AA.
AC   A0A0V0ZRK7;
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:KRY15334.1};
DE   Flags: Fragment;
GN   Name=DOCK1 {ECO:0000313|EMBL:KRY15334.1};
GN   ORFNames=T12_15202 {ECO:0000313|EMBL:KRY15334.1};
OS   Trichinella patagoniensis.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY15334.1, ECO:0000313|Proteomes:UP000054783};
RN   [1] {ECO:0000313|EMBL:KRY15334.1, ECO:0000313|Proteomes:UP000054783}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS2496 {ECO:0000313|EMBL:KRY15334.1};
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:KRY15334.1}.
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DR   EMBL; JYDQ01000097; KRY15334.1; -; Genomic_DNA.
DR   Proteomes; UP000054783; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; 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   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054783};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        18..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          228..290
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          700..888
FT                   /note="C2 DOCK-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51650"
FT   DOMAIN          1546..1969
FT                   /note="DOCKER"
FT                   /evidence="ECO:0000259|PROSITE:PS51651"
FT   REGION          2046..2122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2153..2214
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2049..2071
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2072..2122
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2176..2194
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KRY15334.1"
SQ   SEQUENCE   2214 AA;  253791 MW;  8386566D611C0E91 CRC64;
     LQSVVAQLSF FSQYIIEVFW FCNMLQMLII KFMKILFYVF LMCRFCYSSM SSLKDKFEEH
     KIIPDVVDQA PTQHLQVKYK SGVQADLGNV LTPTQVKEPP SLNWVATPGA LYTMVMTDPD
     APSRQNPKFR EWHHWLVANI PGCEINKGEV LSDYIGSGPP QGTGLHRYVF LVYQQKSHLT
     DKEHGHLTNR SGNNRGGFSI RKFAAKHDLG APIAGNFYQA EWDDYVPKLY EQLGAKHNFR
     PNVVGNYLPL LIGDVVRVLQ FSGEWYYGCL DDDMTKVGVF PISFVEEKHA NFENNELGSI
     AQTAVYSVLT VLKEWKKMCR ESFERRGSID IGKIFPMMKD IINWRSQIVS KKLSLEEVKK
     LNYKIALKID LGNKMLGADV IVRDIHGNEL QTENCSVAEL HKHHLETAER IATEIEQSSW
     NALSHLQRHS SRAEKFMQTK RSQSNWNLLL TFVEFHHPYM NNGELSFMLF DGRLWHGISE
     PAVVVVQQNN STRFGVDPAP LQRFIITVRM RIFIIIIVVD LQVGNLCFVV QDLGTKDLDR
     EKFWIIFLAT KTGPFEWKDT LTYRKTHVSS TTVRQTFAVA ALDLTELLNQ AFCTDPDAGT
     GAGAGAFSST IDEQEERRIF LPLRPLVDDS VEGMLRKIVD NKIGYNSELE TKGDGFWLTL
     QPVFASLDEL KHSQPHLFSN PFKLVRKMGF PEVISRDDVR NDLFVTLVSG DFTHCTGRSD
     KNIEVKVCLV DELTNSVLPD SVVNVGVAKE TFYTSSVFYH QDRPKWFETI KFSIPVEIYG
     NVHIRFSFKH RSSNESKDRN DRPFSVSFIR LKQSNGTVIK DGFHDLVVYR VSSKIEENDF
     SYHTLPASKA DLEMSGMEGT SSKFHIQSPT GGFAISPKDF FTICTTVCST SLTQNVDLLG
     LLEWETKRVN LKSSLEALMK DEGDRAGEEI VKASLLYVGV GVVVFLQDIL DVLFTVLISC
     NDHDQLVFDA LVYVIGLVGE RRYHNFKAVL DSYLLLHFSA ALAYQKLIPI FKDYIDKVEE
     CSNKLLKTLK SLEYLMKFIV RSRNLYVQLK GSNAGKERFH ELICSLFISL TTLMLYQTDW
     SLLCQGAALK YIPHIVVDVL AVFDARELAA MMANFLKNVP RDRLTKQKLM CLQDLVHSEL
     IKKSGAHCNS FARIIVFQYC VLYSMYSEPR AVLLPVILES VRNQIDDNEE LELCAQILTE
     IMNVLFDKHS TSGAHSSTLL FIMRTILRQV VQVVVRLIEA GENLILGQYV ALLLAILEEL
     DACTYRCYIA EFATRTDLMD FLTELLMLFK DLIRRPVFSS DWFQMIFVQN SIMLKILCYA
     ASTVKARFLH EKFEFQVCNS FFQTVVTFIT QKLLQLEQYN VKKRKAILER FRDMRLTCAR
     ELVRSMWFSM NLLEKNQFIP SLVGFVLEVT LIPVEEVRKL TIPIFFDMMV TEFYLRANNN
     STTTSTPLLG NFSYNSSVME FETEFIKKLD SLVENDYGDA KYVDTFVKIM MQLCSSHTEA
     LRDEGIRFTK TVEHLMFRLL EFRNVRLYHN NVNNCMSCTV SLLNFYYEIG HTELYIRYLY
     KLYELHMQRD NFVEAGLTMA LHAECLKWCD SSVHALLAHS LFPDCVSQRE LKEKLFLKMI
     DLFDRGELWE KAIVVCQELQ HEYEHRTYEY DKLANLLEKM SKMYRNILKH QRAEPEYFRV
     LFCGLGFPIF LQNTTFIYRG DGYERLADFT SRIQAQYPNA TLLQTLQPPG EEIKKSNGQY
     LLINKVDPIY DDQIKTIPTP VKDSRILWYY KCNDVQKFYF SRRISKKDCT LSKEWPVADE
     QENEFGLMWL EKTILVTSCR FPGILRWFLV SSESQIELSP LEVAVDSMKA TISDLEKLIE
     EVERYSERAL KPLAAKLQGM LQPAVMGGIK NYEKVFFTEE FMSKGSRKNL EMLELLKEQI
     ASQVPLLEKG IFLHAKFCSS DQREFHHLLI DCFKEYKSHV EQHYGKQASL LPENSSLEIP
     KSNVLVYKQN LIDGSATSND GRYPFSSSIA SRKSNSVREW QASTSAPWLL RTGVMTTLSG
     ATVPRRINSK EAAIRRKAAH STEKEIHQKR HSNSSMGSTQ SAEMSCAGST IVLTEKLTTL
     RPPRPDSSFS KGSFKQQSNS SINRLTSSVE KLSISASHSL VHSDSDEILL TNDRIDDHSA
     VPPPLPPRRD SGQIEIPDFN ASSVTFSPLS PQRLPSIISG PRREKPLPPL PTTE
//
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