ID I2H7B0_HENB6 Unreviewed; 858 AA.
AC I2H7B0;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 08-OCT-2025, entry version 48.
DE RecName: Full=DBF4-type domain-containing protein {ECO:0000259|PROSITE:PS51265};
GN Name=TBLA0G03250 {ECO:0000313|EMBL:CCH62262.1};
GN ORFNames=TBLA_0G03250 {ECO:0000313|EMBL:CCH62262.1};
OS Henningerozyma blattae (strain ATCC 34711 / CBS 6284 / DSM 70876 / NBRC
OS 10599 / NRRL Y-10934 / UCD 77-7) (Yeast) (Tetrapisispora blattae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Henningerozyma.
OX NCBI_TaxID=1071380 {ECO:0000313|EMBL:CCH62262.1, ECO:0000313|Proteomes:UP000002866};
RN [1] {ECO:0000313|EMBL:CCH62262.1, ECO:0000313|Proteomes:UP000002866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 34711 / CBS 6284 / DSM 70876 / NBRC 10599 / NRRL Y-10934 /
RC UCD 77-7 {ECO:0000313|Proteomes:UP000002866};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., Oheigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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DR EMBL; HE806322; CCH62262.1; -; Genomic_DNA.
DR RefSeq; XP_004181781.1; XM_004181733.1.
DR AlphaFoldDB; I2H7B0; -.
DR FunCoup; I2H7B0; 223.
DR STRING; 1071380.I2H7B0; -.
DR GeneID; 14497394; -.
DR KEGG; tbl:TBLA_0G03250; -.
DR eggNOG; KOG4139; Eukaryota.
DR HOGENOM; CLU_023948_0_0_1; -.
DR InParanoid; I2H7B0; -.
DR OMA; IITLEWK; -.
DR OrthoDB; 21380at2759; -.
DR Proteomes; UP000002866; Chromosome 7.
DR GO; GO:0000785; C:chromatin; IEA:EnsemblFungi.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:EnsemblFungi.
DR GO; GO:0031431; C:Dbf4-dependent protein kinase complex; IEA:EnsemblFungi.
DR GO; GO:0003688; F:DNA replication origin binding; IEA:EnsemblFungi.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; IEA:EnsemblFungi.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006270; P:DNA replication initiation; IEA:EnsemblFungi.
DR GO; GO:0033314; P:mitotic DNA replication checkpoint signaling; IEA:EnsemblFungi.
DR GO; GO:0001100; P:negative regulation of exit from mitosis; IEA:EnsemblFungi.
DR GO; GO:1903468; P:positive regulation of DNA replication initiation; IEA:EnsemblFungi.
DR GO; GO:0060903; P:positive regulation of meiosis I; IEA:EnsemblFungi.
DR GO; GO:0006279; P:premeiotic DNA replication; IEA:EnsemblFungi.
DR FunFam; 6.10.250.3410:FF:000001; Protein DBF4 homolog A; 1.
DR Gene3D; 3.40.50.10190; BRCT domain; 1.
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:UP000002866};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00600}.
FT DOMAIN 783..832
FT /note="DBF4-type"
FT /evidence="ECO:0000259|PROSITE:PS51265"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 104..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 652..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 717..738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..159
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..507
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..685
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 727..736
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 858 AA; 97101 MW; 088D6BF181B0F394 CRC64;
MYPAMKIVNR SPLKETDANS KREKISLKQT NSVMSGITTI SSTAATTSNA TTSNNIYKNI
PLLQNKKRSI NASACGTTPV SKDLVSKKPK IERNRSIEGA IRINSNKNIP STTTSTLNPG
HASTTTTLHN SYSNTTQLTT TTNISTVTTT TNRSNTHSHS NSKKNETGAS RVTPNELLEW
QNNWKKIMKR ESVIYFDTTE DVEISKNNKL KLEKRENLLR KGFLFLDARI TEFFDTNVTI
VVTKRSTEKL SLYSPNDILI RAKKNYMKVW DYKKAQRFLK NLDVDIEKMS SFQNETSLSN
LLQNEKLYGP TDRDPKTRRD EIHYFKHSYI YMYDLWQFWA PIITLEWKHH ELQIQDNNSN
KKLPYPVLKY GTFGRCPFVG DVNCNELSQK RVFKRYHRDK LNRKYAFKLR KLYQYHASPS
LNEIITNNKN DNNDPTNAQN YGCIIIPHDA LDSTKLALEW QWRTNASNNT NNNNSNNNNN
NNNNNNNNNN NNNNNHNLTP NNTINNNDGI QLNDESNSGI PIELQLNKQI VSQQSNSLSR
IVPDYQKNNI TSEKQVFERI SPQDKMAPTL SAREISSLLK REETEDLQDD LCNNNENKSN
LRNNFDIKAS GVHQSNDIAT SFGNGLGPTK ASVTNKNLKT LTRMVVDRRL GVTKKPKPLK
KTETIKEEDS LDDQNKGSGN TTISKDSTVS VATTVSNAPG INTTNTNGEL IVIEDRSSNK
EDENEESNNT SASNKNVAAG TTTANALPID NNATTNLHND TKIANNNTIT EKRLPARANR
EPIVKNSGYC ENCRVKYDDL DNHILGERHQ SFANSDENFD LIDNLIKKLN NAQMSFEVDL
TDISSSDDEC SSTSQTVY
//
