ID G2QRA8_THETT Unreviewed; 642 AA.
AC G2QRA8;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 18-JUN-2025, entry version 51.
DE RecName: Full=DBF4-type domain-containing protein {ECO:0000259|PROSITE:PS51265};
GN ORFNames=THITE_2110023 {ECO:0000313|EMBL:AEO64160.1};
OS Thermothielavioides terrestris (strain ATCC 38088 / NRRL 8126) (Thielavia
OS terrestris).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Thermothielavioides;
OC Thermothielavioides terrestris.
OX NCBI_TaxID=578455 {ECO:0000313|EMBL:AEO64160.1, ECO:0000313|Proteomes:UP000008181};
RN [1] {ECO:0000313|EMBL:AEO64160.1, ECO:0000313|Proteomes:UP000008181}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 38088 / NRRL 8126 {ECO:0000313|Proteomes:UP000008181};
RX PubMed=21964414; DOI=10.1038/nbt.1976;
RA Berka R.M., Grigoriev I.V., Otillar R., Salamov A., Grimwood J., Reid I.,
RA Ishmael N., John T., Darmond C., Moisan M.-C., Henrissat B., Coutinho P.M.,
RA Lombard V., Natvig D.O., Lindquist E., Schmutz J., Lucas S., Harris P.,
RA Powlowski J., Bellemare A., Taylor D., Butler G., de Vries R.P.,
RA Allijn I.E., van den Brink J., Ushinsky S., Storms R., Powell A.J.,
RA Paulsen I.T., Elbourne L.D.H., Baker S.E., Magnuson J., LaBoissiere S.,
RA Clutterbuck A.J., Martinez D., Wogulis M., de Leon A.L., Rey M.W.,
RA Tsang A.;
RT "Comparative genomic analysis of the thermophilic biomass-degrading fungi
RT Myceliophthora thermophila and Thielavia terrestris.";
RL Nat. Biotechnol. 29:922-927(2011).
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DR EMBL; CP003009; AEO64160.1; -; Genomic_DNA.
DR RefSeq; XP_003650496.1; XM_003650448.1.
DR AlphaFoldDB; G2QRA8; -.
DR STRING; 578455.G2QRA8; -.
DR GeneID; 11516716; -.
DR KEGG; ttt:THITE_2110023; -.
DR eggNOG; KOG4139; Eukaryota.
DR HOGENOM; CLU_017715_0_0_1; -.
DR OrthoDB; 21380at2759; -.
DR Proteomes; UP000008181; Chromosome 1.
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; 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 SUPFAM; SSF52113; BRCT domain; 1.
DR PROSITE; PS51265; ZF_DBF4; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000008181};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00600}.
FT DOMAIN 590..639
FT /note="DBF4-type"
FT /evidence="ECO:0000259|PROSITE:PS51265"
FT REGION 1..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 163..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..33
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..187
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..237
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..407
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..541
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..555
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..572
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 642 AA; 70898 MW; D0770EB7BB0D67E8 CRC64;
MSTRRVPLST SNPNVANSPM RASAAAAAAF GAVKKARSHT ETMREESYAQ PPPAKRQMTD
RGIASPSRSR PARTMVHRSA SRATAGPGTT QRASHAAACK PTKEELINLR TWHTQIRSRF
PKMVFYFESI PDEQRSKLAK QVGRLGAREE KFFSIDITHV VTSRPVPPEK PKDEHPGAAD
AHADHDQPMT IDPALLNRTA DPTRRKPAAE TPSSRTPLVS AQEDAVKRPK TRSTDVLDRA
RDMGKKIWSL EKLHKILEMA LDPDPYTSAA LGLGRGGSQT ASRAANEESN LAQLLHNERV
HGPSDRDPTV SSKELHHFRG YYIYVYDVEE KTKPIMVREY NKVADPKDGD WPQFRSVSQG
RCPFVVDENY DLPDKENRDR ARAKARAAKT TAVDAAEPVA QQARASAAPP PKLVTGKRTL
SQMEDGHNRG AADVGATESF DRSRVSNPPS FDFRPQNAFI SHSKPGRFLA GEPVASGLQP
SGVTSAIRSQ MISSTTGGVL GAKAGTSKEI HGLQRKVVLQ KASTPALSQD LSSRRMAEMS
HDSTALVQSA SVNRATQRKL DTVDEEETTR QKERLRRSAS AAVSQPKPKR DPKPGYCENC
QDKFADFDEH IVSRKHRKFA ENDENWSQLD ALLAQLKRVP RY
//
