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Database: UniProt
Entry: A0A2U9BR52_SCOMX
LinkDB: A0A2U9BR52_SCOMX
Original site: A0A2U9BR52_SCOMX 
ID   A0A2U9BR52_SCOMX        Unreviewed;      1861 AA.
AC   A0A2U9BR52;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   22-FEB-2023, entry version 24.
DE   SubName: Full=Putative dedicator of cytokinesis protein 5 {ECO:0000313|EMBL:AWP06688.1};
GN   ORFNames=SMAX5B_010986 {ECO:0000313|EMBL:AWP06688.1};
OS   Scophthalmus maximus (Turbot) (Psetta maxima).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC   Scophthalmus.
OX   NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP06688.1, ECO:0000313|Proteomes:UP000246464};
RN   [1] {ECO:0000313|EMBL:AWP06688.1, ECO:0000313|Proteomes:UP000246464}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Martinez P.;
RT   "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT   evaluation of genetic and physical mapping variation across individuals.";
RL   Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the DOCK family. {ECO:0000256|PROSITE-
CC       ProRule:PRU00983}.
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DR   EMBL; CP026251; AWP06688.1; -; Genomic_DNA.
DR   STRING; 52904.ENSSMAP00000002935; -.
DR   Proteomes; UP000246464; Chromosome 9.
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; 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   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000246464};
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          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   REGION          1671..1751
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1770..1861
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          191..218
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1671..1698
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1699..1719
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1728..1747
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1770..1802
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1835..1850
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1861 AA;  214327 MW;  8B14248A7BE431EF CRC64;
     MTRWIPTKKE KYGVAIYNYD PSGEQELCLQ VGDTVHILEK LEGWYRGYTL RKKSQKGIFP
     ASYIHLKEAT FEGIGQQEII IPADLPLVQE LGATLREWAQ IWHTLFVANK TTQFRSVQQM
     AYSLIEYRSQ IVSGTLPKDD LVELKKKVTA KIDYGNRILG LDLVVRDIAG NTLDPDRTST
     VSLYRAHETA SRSVDDRIQE EKTRLQNLER QRQTLFSTVH TYSLLMNLKN FVCNIGEDAE
     LLMSLYDPDQ SEFISENFLV RWDSMGMPKE IEKLNNLPAL FTDLSSSDLM RQRLFLVCQI
     IRVGSMELKE GKKHTGGLRR PFGVAVMDIT DVAHGKTDDE DKQHFIPFQQ IAMETYIRQR
     QLIMSPLIPS RVIGENEPLT AVFNKVIATR EVNHKGQGLF VTLKLLPGDL AQVRKDYPHF
     VDRSTAIVRK MGFPEIILPG NVRNDIYITL LQGEFDRGKK KTPKNVEVIL TVHDDEGNPM
     EKAIFPGAGY DGITEYKSVI YYQVKQPCWN ETVKVTIPIE DVCRCHLRVM FRHRSSQDSR
     DKSEKPFGMA FVRLMRGDGT TLKDGRHELI VYKVDVKKAE DAKVYLNLPA TWGEVEEKEK
     QTGKQFHHSG VIPVTKDSFQ IATLTCSTKL TQNVDLLGLL NWRSNPEALD QILQRLMEVE
     GGEIVKFLQD TLDALFNIMM ETSEKDTYDT LVFNALVFII TLIGDIKFQH FNPVLETYIN
     KHFSATLAYM KLTGVLNYYV GHAEEPILTE KLYVALKALK YLFRFIVQSR DLYLRFYGNS
     EDGDAFFNSI RTLFLSFNTL MDRPLDEGVK IKGAILKYLP SIINDIQTVF DPVELSVLLA
     KFIESIPDSQ LVRQKLGCMC KMVESDLFRQ PDCRDVLLPL VTDQLSGQLD DHSSKPDYEA
     CVQLLSTVLD NLDRKDVGPT RGHVQLIMER LLRRVNRTVI SMDRSSPLIG HYLACMTAIL
     KQMDDMHYAH YISTFKTRQD IIDFLMETFI MFKDLMGNIF PADWMIMNLV QMQVFLRAID
     EYSDVLNMYF LDQAHFELQL WNNYFHLTVA FLTHKTLQLE SFSQEKRNKI LNKYGDMRKI
     VGFKIRDMWY NLGPHKMRFI PAMVGPILEV TLVPEPELRK ATIPIFFDMM QCEHNFNPGR
     TFEMFENELI TKLDQEVEGG QGDEQYKVLL EKTLLEHCRR HRYLSQSGEE LALLLSSLLE
     NLLAYRTITH DESPEHRMSC TVNVLNFYKE KKREDIYIRY LYKLRDLHLD CENYTEASYT
     LLLHAELLEW SDKACAPHLI PRDGEHVWTQ QELKERLFQE IICYLDKGKM WEKAIELGKQ
     LAKMHEIHMF DFMELSQLLK KQAKFYENIM HAMRPQPEYF AVGYYGLGFP SFLRNKMFIY
     RGKEYEWLED FSLKLLSQFP SAVRMTSTAP PGDNISNSPG QHIQCFTVKP VLTVPQQFKD
     KGVPEQILNY YRTNEVDQFK YSRPFRKGEK DPDNEFATMW IERTTYITAY HFPGILKWFE
     VKSVSVEEIS PLENAVETME MANEKLSNLV QQQACDRSLS INPLSMMLSG IVDPAVMGGF
     SNYEKAFFTD SYIQEHPEDH ERIEVLKHLI ALQIPLLADG IHIHGEKTTE QLKPLHNRLV
     TCFQDLREKV EKQYGVITLP CSLTEKKKSR VGSVVMPYIL SSTLRRMSTV STHSTASSGL
     SSGSASSDGP SCISSQDDRR ASVMEEDNRI ARKNRKEWSV SKSQVLLERQ TDTEETPPEK
     QQRPKSLQLG DRRLTLSLFQ GGLSQLSLSN PLSPLPASPH TPHTLRSSSY SSLLSDNDAN
     IIDTPGTPPP MPPKKHPHEI DNPRFSSEFT PPLPVKIESK PPPPPPKTRK SMFPSYEHTP
     Q
//
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