ID A0AAD5TKQ3_9FUNG Unreviewed; 1819 AA.
AC A0AAD5TKQ3;
DT 29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2024, sequence version 1.
DT 08-OCT-2025, entry version 7.
DE RecName: Full=DBF4-type domain-containing protein {ECO:0000259|PROSITE:PS51265};
GN ORFNames=HDU87_003589 {ECO:0000313|EMBL:KAJ3178514.1};
OS Geranomyces variabilis.
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Chytridiomycetes; Spizellomycetales;
OC Powellomycetaceae; Geranomyces.
OX NCBI_TaxID=109894 {ECO:0000313|EMBL:KAJ3178514.1, ECO:0000313|Proteomes:UP001212152};
RN [1] {ECO:0000313|EMBL:KAJ3178514.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JEL0379 {ECO:0000313|EMBL:KAJ3178514.1};
RA Stajich J.E., Amses K., Simmons R., Seto K., Myers J., Bonds A.,
RA Quandt C.A., Barry K., Liu P., Grigoriev I., Longcore J.E., James T.Y.;
RT "Phylogenomic resolution of chytrid fungi.";
RL Submitted (MAY-2020) to the EMBL/GenBank/DDBJ databases.
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:KAJ3178514.1}.
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DR EMBL; JADGJQ010000026; KAJ3178514.1; -; Genomic_DNA.
DR Proteomes; UP001212152; 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 CDD; cd00027; BRCT; 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; 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; 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:UP001212152};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00600}.
FT DOMAIN 616..664
FT /note="DBF4-type"
FT /evidence="ECO:0000259|PROSITE:PS51265"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 127..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 333..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 583..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 686..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 773..995
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1027..1062
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1103..1231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1323..1391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1432..1458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1532..1650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1664..1692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1723..1744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1769..1789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..42
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..344
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..538
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 786..798
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 799..809
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 810..829
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 845..873
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 885..895
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 909..923
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 978..992
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1103..1113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1141..1151
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1152..1163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1191..1214
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1449..1458
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1552..1574
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1601..1614
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1632..1644
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1677..1689
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1819 AA; 192138 MW; 93D0D2889612F992 CRC64;
MRGSDVDVEN RLYRQEDKDE NGGDDDEEEE EEDDDDDDDE VVKEEVAYAS RPAPPGIRGG
NATVLRSRTN TAAVFADSAA ATTPIGQTPR RFVDLQKTPS ASSFSRPFGF ASSASGRGSS
VRLFMSSVPP SAKGKTSSAG LQGGSPLNTP TRIPGGRPPN QPLSLLQTPG TTTRIPESSS
AKHQMLTVTP VSNRLDQLRE NGVATTAATT PKTPVPSPKT DMALRPHVFA TPRTPTSKRT
PAPPLRSTMP PVAPAAAVQS AGQRAAQTVD RAAMIAHTKT RIKACRFFFD CADQRVSAHM
SKQVKELGAT VELFMSNKVT HLITTKPIPA EPVTVNSKAK TPSRSPAAKK PADLVNKASP
VSVKNGLFLA GSRSKGIEDN ITSARKFGAH VWPLERLQTI LKAVNGVAAP RKLQDHLRDE
KLYGISTTRD AEHQKVKYRV FKERYLIIED IAEAYRPIMV KEYHEAENPA DPPWPVMSLK
DRPGGCPFLR YPATEPHNAP SSAALANGED CDMPPTIRLE DTVTGDHASE SDAAKDAPTE
QPSNPHHRVS AASGLVSMSA AVPQRLAAIK TAAVKQLDKR ELAVKPGRKA RPGSAKQEGL
KAEARRRDHR VVGKAFYTRS GYCENCNLKY ELFTEHVRSN AHKAWLAQAN FQDLDNLLAK
IARRPKKSAA TASDVSVKRV RVDSVSTTSA DSYPSARVQP DCASVTSLPA AKRPRLKTPT
PFIESACHDT PANELSAPLC RSAQTEAPCA KQPVTPAVSS ANPDTLSLSE TAALAAEPPQ
PSESAEEAHV RQRTKKTDPP PVQLPPSAPP TSESLPLPAA LSASASLSPV AEPNPAEPTV
RARRPPPVTK SAPLPPQFPR PKVPKPPGLP PCSPVASAPA AHINTARSSP AQSPHSMGIP
HSVGSPLQSE TSTPPDSPAA AATGRGILGR TKIAVPTNSP RGRSMYSSPH RRHPPPQRFG
MRNDPQNPFV EPQRGRGRAN GGGGGGGGGG AVRGPAVPVV ASNRAAPLPA WPRVGSDVKS
MPPALSLTLP DKTSSPVSEG RQDVSVPVTP CRPSPSLEMP VPPTLSHGVG NGRDASNSCT
LAVGLTTFQN PRLNLVYDMT ATSPLTTPVN SDPDTGLLGR APPTPTVLQP SSSSARRRRP
SLPLTPLLAA AQKREAGSVL DRRRPVKRVR LILGPKPQQD TSPARLHTDA DNYDDYDDDG
DDDDDDDNDD EEGGGDAAEM APDSPTTTDF VERDGADVFG VPPLAVTAPA TMTMAMPPGR
VGAGGRRGSC QLLLQPLRLK IKTRPRSMSA SAEAGESCAG GAVARETVGK LFDERSCRDG
LIREGPGNDS VTYALSRPRE EDDGLLAEAA PVKRAKHSMS TRGDHDEAVA DEPTTMEADD
GSAADVSSTL STETQLAADA PIANANDDSA ADVCPSHTEN NASVDVPTVH ASLHGGEADP
ADSSRVLAEE EEPDADEPAL CADDESVVDA STLKASASRL SLRADDDGSD AATATLRADD
DSAADVAISL ADDDELVANA LTPRAAPLEA RGGDLTLEAP SSPCLRLPAD SVDVKTEPDV
RDNGHPRVEL EMKESTPVAH DDDDAGRSTP PDGSECVEPQ DSCSDTAAES AASQTPSPPR
PPPTTEDANV VAPDADTTPR AAARFWRPTS DFMRVVLNSD DEEAEIGNGA NNDCGVSSPA
SSALSTHSSR TTRAKRASWA AALAAERQKR ADAWRRSRQR VLPFDGAGGA GMQRDWHGGT
GEEEEPDEFD ALMMTSSMSV PDHRACVGEV GGDRDGVDGT TATAQSESKP AILLSRDPAW
YYDLCVAVGS EPISSEGDH
//
