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Database: UniProt
Entry: A0A194VDF1_9PEZI
LinkDB: A0A194VDF1_9PEZI
Original site: A0A194VDF1_9PEZI 
ID   A0A194VDF1_9PEZI        Unreviewed;      2083 AA.
AC   A0A194VDF1;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Dedicator of cytokinesis protein 1 {ECO:0000313|EMBL:KUI61796.1};
GN   ORFNames=VP1G_08938 {ECO:0000313|EMBL:KUI61796.1};
OS   Valsa mali var. pyri (nom. inval.).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX   NCBI_TaxID=694573 {ECO:0000313|EMBL:KUI61796.1, ECO:0000313|Proteomes:UP000078576};
RN   [1] {ECO:0000313|Proteomes:UP000078576}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SXYL134 {ECO:0000313|Proteomes:UP000078576};
RA   Yin Z., Liu H., Gao X., Li Z., Song N., Ke X., Dai Q., Wu Y., Sun Y.,
RA   Xu J.-R., Kang Z.K., Wang L., Huang L.;
RT   "Genome Sequence of Valsa Canker Pathogens Uncovers a Specific Adaption of
RT   Colonization on Woody Bark.";
RL   Submitted (DEC-2014) 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; KN714787; KUI61796.1; -; Genomic_DNA.
DR   STRING; 694573.A0A194VDF1; -.
DR   OrthoDB; 8258at2759; -.
DR   Proteomes; UP000078576; 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   CDD; cd00174; SH3; 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; 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; 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:UP000078576};
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          625..804
FT                   /note="C2 DOCK-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51650"
FT   DOMAIN          1452..1877
FT                   /note="DOCKER"
FT                   /evidence="ECO:0000259|PROSITE:PS51651"
FT   REGION          93..131
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          164..194
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          419..507
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1871..1970
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1989..2054
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2064..2083
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        470..484
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        486..507
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1872..1891
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1892..1915
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1934..1964
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1990..2034
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2083 AA;  231149 MW;  510965E7A438BB92 CRC64;
     MPWQPLPRIA FAIATYPFQS QEPEDLPLEI GDELYIIEET PDGNWLRGYL VAQPSLLAGL
     TSVKGQTLEA RIYNGIFPRS CVEVREVLGE TAEGSDGYLD NDGPEHTVGP AHLTASDSAK
     SGFAGQDKGR RTKDGELTLS LLGDGDGDRL QEWARGIADG TDGRLSVPVK RDPDGQRPQA
     PVPMLKIGDE TPTSASEPLI DEIASCLREW HSTNLHELLL SRQYPKLDSL GHLITALYFA
     RQQFLHNVLT AWEYKHLREK TVWDLVRVNK LCGGEVIVRD PNERGRVLTA DDSVVEVTKL
     QSVMSLLDEP PRPVVEPTSL HHLVVDIRSI AGSLNEPMTL VLYLVRKPLG GFLTQLSEPY
     IIEVPAGGSM GTLGKNAHAR MRTLFADLSP QDIGSAPSVE SEIYLIVKIY AAEHIATGES
     NSRSGSISRE AAPFPKDRPP LSTGNKAVRR SLMWAGKSTK TALSRGSPMA KVDERAEERP
     FSGGASDSRD GSQPPGTASS KASCTSSDGV TTLMADRLVG VGCLTLNAIM KQDEEIEQVV
     NIWSPSAKFV SEKESREEWD PLVREIVGSK SGQYEKPRNA ERLQLHLRAF DHPDSDVLIK
     ATPTLLSGIC KTRKMGFSGA PTKPRSDIYI TLDEASISKQ TLLSRYGASA TSMPINLPGN
     NLQATLEVRR SSGERIDACI YPSSNSDALD TWKSSAVEAG EPWRQTLRLL LDDDDVPAAH
     VVVYLSNMPN PPFAVAYLPL WDQQAFVRDG AHGLLLYKLD EYTSAAQPGP LGKGGYISLP
     SAAKGHSADV TGPLATLRLN TYLCSTRYSQ DRVVLALLKW RERPRTEIPS LLKELIFVDE
     IEIVKLLDDV LDALFDILVE WTGDDEYEDL VFTALVRVLA ITHDRRFNIA PLVDQYAETK
     FNCPFATPCL VRSFTRLLQK PTEPDTARKL RATFKVVRHI LKFITHGRGQ QKEKEVGIGI
     TGSTSKFTRH LRSIFKALDS MMRSTAPVLV GSQTLAVQHF HTWLPELSGL LTTEEILHIA
     IDFMDSCSLV KGKLILYKLV LIINYAKLDI FSHPEQRSAL SANTVRWIAP HWGHTEEVTD
     LWKDQVRLCC SILASQVNHL GPEIPDYIPK IIDSYLCIQT KPQQPKSGLS LLFPTSYPFP
     SKPTTEKIVA EEAIIELSAV LSALANSPNG MQLELTDDDL GLVLENTLHV HMSILQGEAF
     PPDWLSVHIY HHKSTMRTLQ YLSSILLETF LPHPDEAETF NTELWKMFFT TLLKLVGSPS
     LALETFPEQK RRAVWKIAGD VREHGAELLR RTWEAIGWDT SPDEKQRYGL SRMGGYQVQY
     VPTLVGPIVE LCLSVHEGLR GMAVEVLQTM MVSEWTLSED LSVIQTEIIE SLDAYFKSKP
     LTESILQKLF VGEVLERFEP LAELPDEPLC AAVRDLMATV DEFLDLLVAV HSGDGSGEAS
     NLINRLRLME FLRDMQKEDI FVRYVHQLAD LQAGARNFTE AGLALRLHAD LYDWDPIRTT
     RALSDPEYPA QSHFERKERI YFDMIKLFED GEAWSSALAA YKELEAQYES NVFDFAKLAR
     TQRAVATIYE TIAKGEKLVP KYYKVTLRGL GFPASVRDKE YMYEGWPNER ASGFTDRIQE
     QYPSAQIVTS ESMVDVEGQF LVISSVSPHR DLTHHVFQRA RVPQIIRDYI ISAHPQKFSI
     STKRSTSGPV QEHFAEKIVF TTVEAFPTIL RRSEIVRTEE VRLGAKEAAL ERIVRKTQEM
     TAVEKRISDG DKSDEVAQLL VDAISISVNP DSESSIVHYR QLVPGTQPVA ETASQAGDEE
     DVDALEEEML ESQVPELDAQ ENAIKMALID HALMIKRCLA MFSRSSNQIL LLHQGDLQRC
     FEATFAPEIE AFTPPQPAPV NPQPSPPSAT PMTPKHQHQF STVSANGTTE VSTVQPVPLR
     PGRGARLSFL GGRKKEGQQQ QQQQQANQVN GEQGHMSEMG RGENNSQVAE VHRRSAFPAQ
     SYENQRPGLE MLGSASNGTH SHGPVSRSGT EASEWVTDSG SHASHDTRIL AGTSVDSLEN
     KERESMGGVG TPILGGVKKR LSMLRLGKKP GKGNGDMGAL DEE
//
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