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Database: UniProt
Entry: A0A2J6PXP5_9HELO
LinkDB: A0A2J6PXP5_9HELO
Original site: A0A2J6PXP5_9HELO 
ID   A0A2J6PXP5_9HELO        Unreviewed;       688 AA.
AC   A0A2J6PXP5;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   18-JUN-2025, entry version 25.
DE   RecName: Full=DBF4-type domain-containing protein {ECO:0000259|PROSITE:PS51265};
GN   ORFNames=NA56DRAFT_647682 {ECO:0000313|EMBL:PMD18805.1};
OS   Hyaloscypha hepaticicola.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Hyaloscyphaceae; Hyaloscypha.
OX   NCBI_TaxID=2082293 {ECO:0000313|EMBL:PMD18805.1, ECO:0000313|Proteomes:UP000235672};
RN   [1] {ECO:0000313|EMBL:PMD18805.1, ECO:0000313|Proteomes:UP000235672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 7357 {ECO:0000313|EMBL:PMD18805.1,
RC   ECO:0000313|Proteomes:UP000235672};
RG   DOE Joint Genome Institute;
RA   Martino E., Morin E., Grelet G., Kuo A., Kohler A., Daghino S., Barry K.,
RA   Choi C., Cichocki N., Clum A., Copeland A., Hainaut M., Haridas S.,
RA   Labutti K., Lindquist E., Lipzen A., Khouja H.-R., Murat C., Ohm R.,
RA   Olson A., Spatafora J., Veneault-Fourrey C., Henrissat B., Grigoriev I.,
RA   Martin F., Perotto S.;
RT   "A degradative enzymes factory behind the ericoid mycorrhizal symbiosis.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KZ613492; PMD18805.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2J6PXP5; -.
DR   STRING; 1745343.A0A2J6PXP5; -.
DR   OrthoDB; 21380at2759; -.
DR   Proteomes; UP000235672; Unassembled WGS sequence.
DR   GO; GO:0031431; C:Dbf4-dependent protein kinase complex; IEA:TreeGrafter.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0043539; F:protein serine/threonine kinase activator activity; IEA:TreeGrafter.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0010571; P:positive regulation of nuclear cell cycle DNA replication; IEA:TreeGrafter.
DR   GO; GO:1901987; P:regulation of cell cycle phase transition; IEA:TreeGrafter.
DR   FunFam; 6.10.250.3410:FF:000001; Protein DBF4 homolog A; 1.
DR   Gene3D; 3.40.50.10190; BRCT domain; 2.
DR   Gene3D; 6.10.250.3410; DBF zinc finger; 1.
DR   InterPro; IPR036420; BRCT_dom_sf.
DR   InterPro; IPR055116; DBF4_BRCT.
DR   InterPro; IPR013939; Regulatory_Dfp1/Him1.
DR   InterPro; IPR051590; Replication_Regulatory_Kinase.
DR   InterPro; IPR006572; Znf_DBF.
DR   InterPro; IPR038545; Znf_DBF_sf.
DR   PANTHER; PTHR15375; ACTIVATOR OF S-PHASE KINASE-RELATED; 1.
DR   PANTHER; PTHR15375:SF26; PROTEIN CHIFFON; 1.
DR   Pfam; PF22437; DBF4_BRCT; 1.
DR   Pfam; PF08630; Dfp1_Him1_M; 1.
DR   Pfam; PF07535; zf-DBF; 1.
DR   SMART; SM00586; ZnF_DBF; 1.
DR   PROSITE; PS51265; ZF_DBF4; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000235672};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00600}.
FT   DOMAIN          630..679
FT                   /note="DBF4-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51265"
FT   REGION          1..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          180..238
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          415..465
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          525..612
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        63..72
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        180..198
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        199..210
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        215..228
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        455..465
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        540..553
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        597..607
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   688 AA;  77217 MW;  6869F82D6A8B7EC8 CRC64;
     MSGRRVPLTS NPNAVNSPYR AVAAAASKQK RSYATTQREE AYGQPRPAKK QMLEAHQPLR
     TPPRQQSIQS SAEGRLFTRK SNAPQQSAFE RKCVAVREKP QQTVTKAEKP TGENLDTIRQ
     WQKHYRKIFP TFVFYFESFE SIPEDVRLKY TKQVIALGAR EEKFFSNAVT HVVTTRSIPP
     EISSSSTEIP ITSSTAESNS QNSQLQTINP SLLDRSSESA NGHHDHGQKG KLTTEAPTGR
     RLAAQGYDGE IKRQQARNAD VLHRARELGM KIWALEKLQR MMTTMFDTET GFQTSHGHNT
     RANSVQGSTV IPQATREADL SQLLRNERIN GPSDRDPRVA TKELTVFKGP FIYIHDIDEK
     QRPIMVREYA KVANKEDGDW PQFRSVANGK CPFVEEVDHS RREAEKEKEL VRLQRQQEKE
     KSMVPRTRSA AEAKMQPPRP VTGKRHLSEM EDGSNRSITV STEQANPFVA KKSIFSHRTA
     PDPEGSSRSN QNAFVSRAGA GRLFAGEPVA SGVQQSNITS AIRSQMISST AAQPGAKTGT
     SKEVRGLQRK VLEKNSGGPG SYSLASSHRM TDLAAAAREE APNRASKRRG QDKLGLIEED
     VDPSEAEEAA RKVEAARKAK AVQQRKLEKR DPKPGYCENC QDKFEDFDEH ILSRKHRKFA
     ERVENWRDLD ALLNQLARPL REEAEEGY
//
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