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Database: UniProt
Entry: A0A3Q3CXQ8_HAPBU
LinkDB: A0A3Q3CXQ8_HAPBU
Original site: A0A3Q3CXQ8_HAPBU 
ID   A0A3Q3CXQ8_HAPBU        Unreviewed;      1869 AA.
AC   A0A3Q3CXQ8;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Dedicator of cytokinesis 1 {ECO:0000313|Ensembl:ENSHBUP00000033118.1};
OS   Haplochromis burtoni (Burton's mouthbrooder) (Chromis burtoni).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Haplochromis.
OX   NCBI_TaxID=8153 {ECO:0000313|Ensembl:ENSHBUP00000033118.1, ECO:0000313|Proteomes:UP000264840};
RN   [1] {ECO:0000313|Ensembl:ENSHBUP00000033118.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the DOCK family. {ECO:0000256|PROSITE-
CC       ProRule:PRU00983}.
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DR   RefSeq; XP_005919560.1; XM_005919498.1.
DR   Ensembl; ENSHBUT00000026643.1; ENSHBUP00000033118.1; ENSHBUG00000020126.1.
DR   GeneID; 102312690; -.
DR   CTD; 1793; -.
DR   GeneTree; ENSGT00940000154974; -.
DR   OrthoDB; 8258at2759; -.
DR   Proteomes; UP000264840; Unplaced.
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; cd08694; C2_Dock-A; 1.
DR   CDD; cd12051; SH3_DOCK1_5_A; 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; 2.30.30.40; SH3 Domains; 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; IPR047025; DOCK1_5_SH3.
DR   InterPro; IPR047026; DOCK1_C2.
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:SF1; DEDICATOR OF CYTOKINESIS PROTEIN 1; 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   Pfam; PF00018; SH3_1; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF48371; ARM repeat; 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   Coiled coil {ECO:0000256|SAM:Coils};
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:UP000264840};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          8..69
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          424..608
FT                   /note="C2 DOCK-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51650"
FT   DOMAIN          1204..1615
FT                   /note="DOCKER"
FT                   /evidence="ECO:0000259|PROSITE:PS51651"
FT   REGION          1610..1714
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1736..1869
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          711..738
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1610..1626
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1631..1658
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1673..1712
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1755..1787
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1826..1857
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1869 AA;  215734 MW;  E45053C20ED65996 CRC64;
     MSRWVPTKKE KYGVAIYNYD ARGEEELSLQ IGDTVHILET YEDWYRGYRL RRKSKKGIFP
     ACYIHLKEAT VEGSGQKETV IPTELPLVQE VTTTLREWAT IWRDLYVGDK REMFNCVRDM
     IYDLIEWRSQ ILSGTLPQDE LSELKQKVTS KIDYGNKYLD LDLVVRDKDG NILDPELTST
     ISLFRAHEAA SKQIEDRIQE EKSQKQNIDL TRQAKFASTP AFALFVTLKN VVCKIGEDAE
     VLMSLYDPVE SKFISENYLV KWSSCGLVKD IDQLHNLRAV FTDLGSEDLK REKISFVCQI
     VRVGRMELRD NNTKKLTSGL RRPFGVAVMD VTDIITGKMD DEDKQHFIPF QPVAGENDFL
     QTVINKVITA KEVNHKGQGL WVTLKLLPGD IHQIRKDFPH LVDRSTAVAR KMGFPEIIMP
     GDVRNDIYVT LVQGDFDKGS KTTPKNVEVT MSVYDEDGKK LENVIFPGAG DEGINEYKSV
     IYYQVKQPRW FETIKVAIPI EDVNRSHLRF TFRHRSSQDS KDKSEKIFAL SFVKLMRYDG
     TTLRDGEHDL IVYKAEVKKL EDSSLYLNLP STKLEMEEKG YSTTGKNTQT LGICTISKDS
     FQISTLVCST KLTQNVDLLG LLKWRSNTSL LQQNLRQLMK VEGGEVVKFL QDTLDALFNI
     MMENSDSDTF DTLVFDALVF IIGLIADRKF QHFNPVLETY IRKHFSATLA YTKLTKVLKN
     YVDNADKLTE QLLKAMKALE YIFKFIVRSR VLFNQLYENK GEADFMESLR NLFTSFNDMM
     NSNSENTGMV KGAALKYIPT IVNDVKLVFD PKELSKLFTE FILKVPVGRL VKQKLDCLID
     IVHSDLFNHH DCREILLPLM TDQLKFHLEK REDLKACCQL LSDILEVLYR KDVGPTQWHV
     QIIMEKLLRT VNRTIISMGR DSPHIGSFVA SMTGVLRQMD DYHYAHLIST FGKIRSDVVD
     FLMETFIMFK DLIGKNVYPS DWIIMNMMQN KVFLRAISQY AAVLNKKFLD QTNFELQLWN
     NYFHLAVAFL TQESLQLENF SSDKRAKIFH RYQDMRRQIG FEIRDMWYNL GPHKIKFIPE
     MVGPILEMTL VPEIELRKAT IPIFFDMMQC EFHFTMHFQR FENEIITKLD HEVEGGRGDE
     QYKVLFQKIL LEHCRKHKYL ARTGENFVTL VVRLLERLLD YRTIMHDENK ENRMSCTVNV
     LNFYKEIDRE EMYIRYLYKL CDLHKECDNY TEAAYTLLLH AKLLKWSDEA CAAHLTQRDG
     YQATTQGQLK DHLYQEIINY FDKGKMWEEA IILGKELAEQ YENEMFDFEQ LSASLRKQAQ
     FYENIVKVIR PKPDYFAVGY YGTGFPSFLR NKMFIYRGKE YERREDFEAR LLTQFPNAEK
     MKTTTPPSED TKSSSGQYIQ CFTVKPILDL PAKFQNKSVS EQILSFYTVN EVHKFQYSRP
     VRKGEKDPDN EFANMWIERT TYSTAYKLPG ILRWFEVKSV STEEISPLEN AIETMQQTNE
     KISSMVQRHL NDPNLPINPL SMLLNGIVDP AVMGGFTNYE KAFFNDKYIQ EHPEDLEKIE
     KLKDLIAWQI PHLAEGVRIH GEKVTEALRP FHDRMEACFK QLREKVEKQY GVKSLPPADE
     RRGPRPPSMV RSFTMPSSQR PLSVASVTSI SSDNAPSRPG SDGFALEPLL PKKLHTKSQD
     KLDRDEPEKD RKEKKKEKRN SKHQEVFDKE MKTADISLQP AEAVILSETI SPLRPQRPRS
     QVLNQIVGDR RLSVSPGPPT SSSSSSSQCP PPITPRSKVS YNLHAVSSLE LNGMGCSDKG
     ETPPPLPLKS NTADYGNLLD NQDLTSPSTP PPPPPHQRQF PPPLPSKTPP PPPPKTTRKQ
     ASIDSGIVQ
//
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