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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//