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Database: UniProt
Entry: A0A218ZAE1_9HELO
LinkDB: A0A218ZAE1_9HELO
Original site: A0A218ZAE1_9HELO 
ID   A0A218ZAE1_9HELO        Unreviewed;      2091 AA.
AC   A0A218ZAE1;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OWP04255.1};
GN   ORFNames=B2J93_9323 {ECO:0000313|EMBL:OWP04255.1};
OS   Marssonina coronariae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Dermateaceae; Marssonina.
OX   NCBI_TaxID=503106 {ECO:0000313|EMBL:OWP04255.1, ECO:0000313|Proteomes:UP000242519};
RN   [1] {ECO:0000313|EMBL:OWP04255.1, ECO:0000313|Proteomes:UP000242519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NL1 {ECO:0000313|EMBL:OWP04255.1,
RC   ECO:0000313|Proteomes:UP000242519};
RA   Cheng Q.;
RT   "Draft genome sequence of Marssonina coronaria NL1: causal agent of apple
RT   blotch.";
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the DOCK family. {ECO:0000256|PROSITE-
CC       ProRule:PRU00983}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OWP04255.1}.
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DR   EMBL; MZNU01000116; OWP04255.1; -; Genomic_DNA.
DR   STRING; 503106.A0A218ZAE1; -.
DR   InParanoid; A0A218ZAE1; -.
DR   OrthoDB; 8258at2759; -.
DR   Proteomes; UP000242519; 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; 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   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:UP000242519};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          7..88
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          625..810
FT                   /note="C2 DOCK-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51650"
FT   DOMAIN          1458..1864
FT                   /note="DOCKER"
FT                   /evidence="ECO:0000259|PROSITE:PS51651"
FT   REGION          90..203
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          420..459
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          481..510
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1857..1914
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1931..2091
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        90..106
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        144..158
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        420..457
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1871..1914
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1959..1989
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2026..2040
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2091 AA;  230711 MW;  F0C94AB782DB8B7A CRC64;
     MPWQPLPRIA FAVATFPFPA QDPADLPLEL GDELYIIEQG GRHGDWFRGY LVAPPSLLAG
     LTSTKGQTLE ARVFSGIFPR SCVEVREVLG EDEEDEVSDE EAEADAVLET PTTNGHGRNG
     SACASVGADG SPLASSRSTR TPKKALRQRS ESGETARTRK RRTRRLLNGD VLAVPVDRDP
     DAPKPPAPVP MLKIGDETPT STSEPLVDEI ASCLREWHST NLHELLLSRQ YPRLDDMSAL
     VQNLDLSRRK FLHNVLTTHE LSSLREKTVW DLVRGNKVFN GEVIVRDPAE RGRVLTGDDS
     AVEITKLQSL MSLLEEPPQP PANETLTLHH LLIDVRAFVG ASTEPTTLVF YLASKTPGRA
     AVALSESYVV EVPPGGAMTS LAQVGQMRTL FTELTSSDIG DSTAADRELY LVVKLRSKQQ
     VTGGKPSSRN GLSSRDGSQE TRNGEKPLSS AGSRTGRRSL MWGQKVKRNV YSRNASISKL
     GSLAEGQESR EGPPGTADLR GPAAERKSGT VSRVVNRTMG VGAIKINSIM KQEEEIEQVI
     PIWAAAAGLV QEQGSGDGWD EVIKDLMSSK TGNYAKSKKA ERLQVHLKAF QSPDADGLIS
     ATPTLLSGVA KTAKMGFSGA PTKGRSDIYL TIDEAFLPRN ALIARANGHA LPLPSSVAGM
     NLQVSMEVCR ATGERLENCI FPSSNAEGGL SSWESTAAEK GDAWNQTLRI CIPAADVAGC
     HVAMTLCDAP SQPFAICYLP LWDQSAFVRD GHHSLLLYRY DEHTTTAKGK GEGRTGYLDV
     PWNARGKDDV SKDEAVTGPT TTLRVQTYLC STLFSQDKVL LGLLRWKEQP PGDVQELLRR
     LVFVPEIEVV KLLSDVFDAI FGILVEHTGN DDYEDLIFSA LVTVLGIVHD RRFNLGPLVD
     HYAQEKFNYP FVTPCLVRSF TRLLQNPADP DTSRKLRATF KVVRHILKFI THARGQQKEK
     EAGIGITSSS PGFTRHLRSI FKALDGLMRN NAPILVGSQT LAVQHFHTWL PELTGLLSPE
     EILHIAIDFM DSCHAVKGKL VLYKLVLIIN YAKLELFAAP EQREALSANT VRWIAPHWGK
     TDEVTDQWIE QIRLCCSVLS TQIDKIGPEI PDYIPKIVDS YLSLRATPKS DKTRLSLLFP
     TTYPFPTRPI EGKVQFAEVL IELSAILAAV STLPAGLQLD LADDEMATLI ENLLHVHLSI
     LDFEAFPSNW LSVHIFHHKS AMKTLEYVSG ILLESFLPPP DDAEDYNTEL WKAFFTVLLK
     LVGSDALALE TFPEQKRRAV WKIAGDVREH GADLLRRTWE AIGWETSPDE RQQYGLAKTG
     GYQVQYVPVL VGPIVELCLS VHEGLRRVAV EVLQSMIVSE WTLGEDLSVI QTEMIDCLDR
     LFKSKPLTES ILQKLFIHEL FSLFDSLARA EDDSLFGTVR ELIATIDEFL DLLVAVHSTD
     VSGEASHMIH RLRLMEFLRD MQKEEIFIRY VHQLAQLQAD ARNPTEAGLA LRLHADMYDW
     DPTKVVPPLV DPDFPSQSQF ERKERIYFEI IKYFEEGESW CSALSVYQEL QSQYQENIFD
     FSKLARTQRA IATVYETIAK SDKLVPKYFR VTYRGMGFPP SLRDKEFVYE GSQTERTSAF
     TDRMLEQHPA AQIVAAGDVD DVEGQFLQIS PLTPHRDLGH SVFQRARVPQ VIRDYLPSAN
     PQVFSVTSKR NTAGPVHEHY AEKIICRTAE AFPTILRRSE IVAIDRVKLN PLQTAVERIL
     RKTAEMSLVE KRVADGEDDI APLLIDALQV SVNPGSDTTV ANYRELLPAA SEADDVREIE
     LGPLENALKT ALIDHAVMIR RCLAMLSSST SIGSVEREVV AQNFQATFAP ELASFAFPRH
     TKPPTPTPSW AVASPVQSDG SNNRRNSQAM GRLPNSATNG TLATMDTSIL DTPSARAGRN
     RLSFLKRHTP AALPDQPLQP PPMLNGLSLN GVTPKDLPAS LREHSRSNES SSARSRSRSH
     SRLRTEENRR SFFGSTAGLG SIGRVRGRAF GQKEEESDWV TQSDLAGMAR RSSSSHRPPT
     GKSGGGGGGP TSRDGSVGSK VGSVRKRLSR LALGKKTSRP SVLVGSVAEE G
//
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