ID A0A3Q1FU79_9TELE Unreviewed; 1827 AA.
AC A0A3Q1FU79;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Dedicator of cytokinesis 5 {ECO:0000313|Ensembl:ENSAPOP00000019187.1};
OS Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000019187.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000019187.1}
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 STRING; 80966.ENSAPOP00000019187; -.
DR Ensembl; ENSAPOT00000028992.1; ENSAPOP00000019187.1; ENSAPOG00000022711.1.
DR GeneTree; ENSGT00940000157734; -.
DR InParanoid; A0A3Q1FU79; -.
DR Proteomes; UP000257200; Unplaced.
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 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; 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:SF3; DEDICATOR OF CYTOKINESIS PROTEIN 5; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000257200};
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 1737..1757
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 8..69
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 443..626
FT /note="C2 DOCK-type"
FT /evidence="ECO:0000259|PROSITE:PS51650"
FT DOMAIN 1228..1639
FT /note="DOCKER"
FT /evidence="ECO:0000259|PROSITE:PS51651"
FT COILED 191..218
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1827 AA; 210785 MW; 1A299D0BBFFCE752 CRC64;
ACPGLRVKKE KIGVTIYNYD PSGEQELCLQ VGDTVHILEK LEGWYRGYTL RKKSQKGIFP
ASYIHLKEAT VEGIGQQEII IPADLPLVQE LGATLREWAQ IWHKLFVANK STLFRSVQQM
AYSLIEYRSQ IVSGTLPKDD LVELKKKVTA KIDYGNRILG LDLVVRDEAG NTLDPDRTST
VSLFRAHETA SRSVDDRIQE EKTRLQNLEM RRQTLFSTVH TYSLLMNLKN FVCNIGEDAE
LLMSLYDPDQ SEFISENFLV RWDSMGMPKE IEKLNNLPAL FTDLSSSDLM RQRLFLVCQI
IRVGSMELKE GKKQTGGLRR PFGVAVMDIT DIAHGKTDDE DKQHFIPFQQ IAMETYIRQR
QLIMSPLIPS RVIGENEPLT AVFNKVIATR EVNHKGQGLF VTLKLLPGDL AQVRKDYPHF
VDRSTAIVRK MGFPEIILPG NVRNDIYVTL LQGEFDRGKK KTPKNVEVIL SVHDDEGNPM
EKAIFPGAGY DGITEYKSVI YYQVKQPCWN ETVKVTIPIE DVCRCHLRVM FRHRSSQDSR
DKSEKPFGMA FVRLMRGDGT TLKDGRHELI VYKVDVKKAE DAKVYLTLPA TWAEVGEKEK
QMGKQFHHSG AIPVTKDSFQ IATLTCSTKL TQNVDLLGLL NWRSNPEDLD QILQRLMEVE
GGEIVKFLQD TLDALFNIMM ETSEKDTYDT LVFNALVFII TLIGDIKFQH FNPVLETYIN
KHFSATLAYM KLTRVLNYYV GHAEEPQLTE RLYAALKALK YLFRFIVQSR VLYLRFYGNS
EDGDAFFNSI RTLFLSFNTL MDRPLDEGVK IKGAILKYLP SIINDIQTVF DPVELSVLLA
KFIESIPDSQ LVRQKLGCMC KMVESDLFRQ PDCRDVLLPL VTDQLSGQLD DHSSKPDYEA
CVQLLSTVLD NLDRKDVGPT RGHVQLIMER LLRRVNRTVI SMDRSSPLIG HYLACMTAIL
KQMDDMHYAH YISTFKTRQD IIDFLMETFI MFKDLMGNVF PADWMIMNLV QMQVFLRAIS
QYSDVLNMYF LDQAHFELQL WNNYFHLTVA YLTHKTLQLE SFSQEKRNKI LNKYGDMRKT
IGFKIRDMWY NLGPHKMRFI PAMVGSILEV TLVPEPELRK ATIPIFFDMM QCEHNFSPGR
TFETFENELI TKLDQEVEGG RGDEQYKVLL EKTLLEHCRR HRYLSQSGEE LALLLSSLLE
NLLAYRTITH DESPEHRMSC TVNVLNFYKE KKREDIYIRY LYKLRDLHLD CENYTEAAYT
LLLHAELLEW SDKPCAPHLI PRDGQHVWTQ QELKERLFQE IICYLDKGKM WEKAIELGKQ
LAKMHESHMF DFMELSQLLK KQAEFYENIM HAMRPQPEYF AVGYYGLGFP SFLRNKMFIY
RGKEYEWLED FSLKLLSQFP NAVRMTSTAP PEDNISNSSG QYIQCFTVKP VLTVPHQFKD
KGVPEQILNY YRTNEVDQFQ YSRPFRKGEK DPDNEFATMW IERTTYITAY RFPGILKWFE
VKSVSVEEIS PLENAIETME MANEKLSNLV QQQACDRSLS INPLSMMLSG IVDPAVMGGF
SNYEKAFFTD TYIQEHPDDH ERIEVLKHLI ALQIPVLADG IRIHGEKTTE QLKPLHNRLV
TCFQDLREKV EKHYGVITLP CSLTERKKSR VGSVVMPYIL SSTLRRMSTV STLSNASSGL
SSGSASSDGP SCISSQESVP ASSACLPNSS FSPCLLLDSL CLFQVHVFFF APKIAPFLFL
IVLHLFLCLW SFTYSSLLSH PSDRRVSVLS RSEEDNRIAR KNRKEWSVSK SQVLLERQSD
VDEVRFYVPE LFLYLCCFSF TSTQVFI
//
