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Database: UniProt
Entry: M1VYV7_CLAP2
LinkDB: M1VYV7_CLAP2
Original site: M1VYV7_CLAP2 
ID   M1VYV7_CLAP2            Unreviewed;       675 AA.
AC   M1VYV7;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   28-JAN-2026, entry version 44.
DE   SubName: Full=Related to DBF4-regulatory subunit for Cdc7p protein kinase {ECO:0000313|EMBL:CCE34417.1};
GN   ORFNames=CPUR_08349 {ECO:0000313|EMBL:CCE34417.1};
OS   Claviceps purpurea (strain 20.1) (Ergot fungus) (Sphacelia segetum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Claviceps.
OX   NCBI_TaxID=1111077 {ECO:0000313|EMBL:CCE34417.1, ECO:0000313|Proteomes:UP000016801};
RN   [1] {ECO:0000313|EMBL:CCE34417.1, ECO:0000313|Proteomes:UP000016801}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=20.1 {ECO:0000313|EMBL:CCE34417.1,
RC   ECO:0000313|Proteomes:UP000016801};
RX   PubMed=23468653; DOI=10.1371/journal.pgen.1003323;
RA   Schardl C.L., Young C.A., Hesse U., Amyotte S.G., Andreeva K., Calie P.J.,
RA   Fleetwood D.J., Haws D.C., Moore N., Oeser B., Panaccione D.G.,
RA   Schweri K.K., Voisey C.R., Farman M.L., Jaromczyk J.W., Roe B.A.,
RA   O'Sullivan D.M., Scott B., Tudzynski P., An Z., Arnaoudova E.G.,
RA   Bullock C.T., Charlton N.D., Chen L., Cox M., Dinkins R.D., Florea S.,
RA   Glenn A.E., Gordon A., Gueldener U., Harris D.R., Hollin W., Jaromczyk J.,
RA   Johnson R.D., Khan A.K., Leistner E., Leuchtmann A., Li C., Liu J., Liu J.,
RA   Liu M., Mace W., Machado C., Nagabhyru P., Pan J., Schmid J., Sugawara K.,
RA   Steiner U., Takach J.E., Tanaka E., Webb J.S., Wilson E.V., Wiseman J.L.,
RA   Yoshida R., Zeng Z.;
RT   "Plant-symbiotic fungi as chemical engineers: Multi-genome analysis of the
RT   Clavicipitaceae reveals dynamics of alkaloid loci.";
RL   PLoS Genet. 9:E1003323-E1003323(2013).
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:CCE34417.1}.
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DR   EMBL; CAGA01000088; CCE34417.1; -; Genomic_DNA.
DR   AlphaFoldDB; M1VYV7; -.
DR   STRING; 1111077.M1VYV7; -.
DR   VEuPathDB; FungiDB:CPUR_08349; -.
DR   eggNOG; KOG4139; Eukaryota.
DR   HOGENOM; CLU_017715_0_0_1; -.
DR   OrthoDB; 21380at2759; -.
DR   PhylomeDB; M1VYV7; -.
DR   Proteomes; UP000016801; Unassembled WGS sequence.
DR   GO; GO:0031431; C:Dbf4-dependent protein kinase complex; IEA:TreeGrafter.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
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; 6.10.250.3410; DBF zinc finger; 1.
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   Kinase {ECO:0000313|EMBL:CCE34417.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016801};
KW   Transferase {ECO:0000313|EMBL:CCE34417.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00600}.
FT   TRANSMEM        144..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          612..661
FT                   /note="DBF4-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51265"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          192..226
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          563..614
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        597..608
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   675 AA;  76026 MW;  4A2DA1A0230D1126 CRC64;
     MSSRRVPLTN NPNVANSPLR GPTTLNGYAK QKQSYANVQR EEAYGQPPPA KKLAIDNASQ
     RVVRSPAKAS RAQVLLQRSA AARPALKDRA TRTAAQENAR NVQENEVEKE AWKKHYRVKF
     PKMVFYFESI PDDIRAKLTK RVTYLGAVSS FCFAFYLFDM SMAQLTYIFS ARQQRQEPFF
     SIDVTHVVTT RSIPVGKPGT GQEQHAEPEQ QEPQEQPQTI NPSLLDRNTV AARRRLLFDF
     RPTQAPSHQS DDPTRRTRGI RHNDVLHKAR DMGKKIWSLE KFQIMLSVLL EPDTKSGSQS
     TRTQSLRNHY GMAKGTHEPN LLQLLHNERI NGPSDRDPTA VSRELVHFKG PYIYVWDMDE
     KHKPMMVREY PKVVHKQDGE WPQFRSVGNG RCPFVEEVEA PEKEARRPRE REVARVVKRE
     EAVAVPKPAD IPVSKPAARK RSLMEMEDGH NHARPNVPVD VFNPAKAAIS KQTDMKLQNA
     FTSRAQGARL LAGEPVASGM QPSNITSAIQ SQMVSSTSGI NGGKAGTSKE VHGLQRKVLQ
     KVHPVSHDAS SRRLAEVSMD VASSRSANTG MGVRPPPKTV QPQEDECQGA DGKAKKAQPQ
     LPSQLQSLKS KRDLKPGYCE NCQDKFRDFD EHIVSRKHRK FAENDDNWTE LDLLLEQLRR
     VPKYAGADSD DDGGW
//
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