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Database: UniProt
Entry: G0S212_CHATD
LinkDB: G0S212_CHATD
Original site: G0S212_CHATD 
ID   G0S212_CHATD            Unreviewed;      2104 AA.
AC   G0S212;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   RecName: Full=Dedicator of cytokinesis protein 1 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CTHT_0015580 {ECO:0000313|EMBL:EGS23072.1};
OS   Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
OS   (Thermochaetoides thermophila).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Thermochaetoides.
OX   NCBI_TaxID=759272 {ECO:0000313|Proteomes:UP000008066};
RN   [1] {ECO:0000313|EMBL:EGS23072.1, ECO:0000313|Proteomes:UP000008066}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1495 / CBS 144.50 / IMI 039719
RC   {ECO:0000313|Proteomes:UP000008066};
RX   PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA   Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA   Arumugam M., Bork P., Hurt E.;
RT   "Insight into structure and assembly of the nuclear pore complex by
RT   utilizing the genome of a eukaryotic thermophile.";
RL   Cell 146:277-289(2011).
CC   -!- SIMILARITY: Belongs to the DOCK family. {ECO:0000256|PROSITE-
CC       ProRule:PRU00983}.
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DR   EMBL; GL988039; EGS23072.1; -; Genomic_DNA.
DR   RefSeq; XP_006692064.1; XM_006692001.1.
DR   STRING; 759272.G0S212; -.
DR   GeneID; 18255596; -.
DR   KEGG; cthr:CTHT_0015580; -.
DR   eggNOG; KOG1998; Eukaryota.
DR   HOGENOM; CLU_000595_0_1_1; -.
DR   OMA; LWDNQAF; -.
DR   OrthoDB; 8258at2759; -.
DR   Proteomes; UP000008066; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   CDD; cd08679; C2_DOCK180_related; 1.
DR   CDD; cd11684; DHR2_DOCK; 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; IPR032376; DOCK_N.
DR   InterPro; IPR042455; DOCK_N_sub1.
DR   InterPro; IPR027357; DOCKER_dom.
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; 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   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008066};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          7..87
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          605..791
FT                   /note="C2 DOCK-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51650"
FT   DOMAIN          1412..1827
FT                   /note="DOCKER"
FT                   /evidence="ECO:0000259|PROSITE:PS51651"
FT   REGION          89..168
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          439..487
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1832..1876
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1894..1918
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1971..2007
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2047..2078
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        110..125
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        439..455
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1832..1875
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2047..2061
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2104 AA;  232055 MW;  8C927344F5FD99F7 CRC64;
     MPWQPLPRIA FAVAIYPFAA QGPQDLPLEL GDELYIIEET SDGNWLRGYL VAPPSLLAGL
     TSVKGQTLEA RVFSGIFPRS CVEIREVLGE SDESDESDAN SSSLTDEDGA APEPGERGVE
     NKRRKAGSRK GGRSTSPGLL SVPVRRDPNA PRPPAPVPML KIGDETPTSA SEPLIDEIAS
     CLREWHSTNL HELLLSRQYS KLDTLSHLIT SLNLARQQFL HDVLTSWEYE KLREKTVWDL
     VKVNKLCGGE VIVRDPNARG RVLTGDDSVI EVTKLQSIMS LLEEPPTQPV ELTALHHLLV
     DIKGFAGAST EATTLVLYLA IKPPGGTLKP LSECYIVEMP AGGQMGHLAR NAQMRTLFTD
     LTAAEIGDVP ANEPELFLIV KIRASQQVVA VKPSSRSGSI SQALPQFAKD HKPPLSAGAK
     SVRRSLMWAG KTTRSAFSRG NARLDSLSEQ PEETVGSPHT AGAESRDGMP PGTANSKSGG
     GGRTSVDGHV AQATADRTVG VGILKLNSVM KQADEVEHIV TIWSPSVRVP ERNEAGEEWD
     PIIRDLLESK TGHYEKSRRA ERVQVHLRAF NHPDADALIK ATPTMLAGVC KTNKMGFAGA
     PTKPRSDIYL TLDEAVLSRQ TLLSRAGGSP TSLPNAVHGT NLQLTLEVRR STGERVESCI
     YPSSNAEPAS AWKTVVTERG EKWRQTIRLS LSPSDVSQSH VVLHLADAPN PPFAIAFMPL
     WDRQAFIHDG AHSLLLYRLD ENTSNAQPGS QGRGGYLSLP FAAAEDKRHH HGPGSEGSGP
     LAMVRVDTYL CSTRFSQDRV VLGLLAWKES SREGIPHLLK QFIFVPEIEV VKLLNDVLDA
     LFGILVEYSG NDDYEDLVFT ALVRVLDIVH DRRFNLAPLV DQYAETRFNY PFATLCLVRS
     FIRLLSKPTE PETARKLRST FKVARHILKF ITHARSQQKA KEAGIGITGP NAGFTRHLRT
     IFKALDSMMR SSAPVLIGSQ TLAVQHFHTW LPELTGLLST EEILHIAIDF MDSCSKVKGK
     LILFKLVLII NYARLDIFSG AEQRSALSAN TVRWIAPHWG YTDEVTDQWR DQVRLCCSVL
     ASQMDHLGPE IPDYIPKIIG KPISEPAIFD EALIELSAIL SALSSSPSGM QLELAEDDLH
     VIVEKCLRVH MSILQGEAFP QNWLSVHIYH HKSAMRVLQY LASILLDSFL PHPDEAESFN
     TELWKLFFTT LLKLVGSPSL ALETFPEQKR RAVWKIAGDV REHGADLLRK TWEAIGWETT
     VEERARFGLS KLGGYQVQYV PTLVAPIVEL CLSVHEGLRR MAVEVLQTMI VSEWTLSEDL
     SVIQTEMIDC LDAYFKAKPL TESILQKLFI GELLERFEPL RKVDSEDPLY KSLRELTDTV
     DEFLDLLVAV HSGDGSGEAT HLIHRLRLME FLRDMQKEEI FIRYVHQLAN LQAQARNHTE
     AGLALRLHAD LYDWDPLKTT PALHEPEFPA QSHFERKERI YFDMIKHFED GEAWSSALAA
     YKELQTQYET NVFDFAKLAR TERAIASIYE HIVKSDKLVP KYFKVVFKGL GFPPSVRDKE
     FVFEGSPNER TASFTDRMQE MYPAARIVTT EHIDDLEGQF LVISMLSPHR DPSHQVYQRA
     RVPQIIRDYL LSANPQTFSV TVRRVTAGPV HEHFTDKLVY TTAEPFPTIL RRSEVVSVRE
     VRLSAGETAL ERIVRKTAEM SSLEKKIADG EAGEDAAQLL LDAVAISVNP GSESSVAAYR
     QLLPGAKERT SGSEQFDLED LEQAPELSPQ ENAIKMALVD HAIMLKRCLA TVAKFGSEQL
     SKRVEELQRY FETTYAPEIA LFTPAPAIMS SSTAGLTSGT LRSSPSMSYP QQFQQQPTQQ
     PKNGTSSSPT PEHKPAQSIS FLHGRAPRLS FLHSSRKKEH HHQRSATATN GADMKHPLYE
     TEGNDTVVSL GAAKSVTSSV TGASTAKEGA STGHHGNRRS FFKVTSVPNL TGSSSGQGNT
     NHNMNGDGSH HHRITAQPSS NVGSGVAAGM GVTNEWVTDA GTSSVAGTAS FEHHRNYGMA
     EKDGAVVTTS NPVSSSGEGQ THGHGHGHHH HGSSIGSVRK RLSLLRLGKK SSRGAGMLGG
     VDEE
//
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