ID A0A9P6JFC4_MORAP Unreviewed; 1397 AA.
AC A0A9P6JFC4;
DT 13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 1.
DT 18-JUN-2025, entry version 10.
DE RecName: Full=DBF4-type domain-containing protein {ECO:0000259|PROSITE:PS51265};
GN ORFNames=BGZ70_000507 {ECO:0000313|EMBL:KAF9968662.1};
OS Mortierella alpina (Oleaginous fungus) (Mortierella renispora).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mortierellomycotina;
OC Mortierellomycetes; Mortierellales; Mortierellaceae; Mortierella.
OX NCBI_TaxID=64518 {ECO:0000313|EMBL:KAF9968662.1, ECO:0000313|Proteomes:UP000738359};
RN [1] {ECO:0000313|EMBL:KAF9968662.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CK1249 {ECO:0000313|EMBL:KAF9968662.1};
RX PubMed=33364917;
RA Vandepol N., Liber J., Desiro A., Na H., Kennedy M., Barry K.,
RA Grigoriev I.V., Miller A.N., O'Donnell K., Stajich J.E., Bonito G.;
RT "Resolving the Mortierellaceae phylogeny through synthesis of multi-gene
RT phylogenetics and phylogenomics.";
RL Fungal Divers. 104:267-289(2020).
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:KAF9968662.1}.
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DR EMBL; JAAAHY010000011; KAF9968662.1; -; Genomic_DNA.
DR OrthoDB; 21380at2759; -.
DR Proteomes; UP000738359; 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; 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:UP000738359};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00600}.
FT DOMAIN 629..678
FT /note="DBF4-type"
FT /evidence="ECO:0000259|PROSITE:PS51265"
FT REGION 158..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 278..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 684..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 820..870
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 944..970
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1040..1069
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1082..1272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1299..1383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 719..733
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 823..838
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 954..969
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1044..1058
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1082..1097
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1208..1224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1249..1269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1320..1337
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1397 AA; 153253 MW; CC450C01259F5FA7 CRC64;
MTDRAANTAS MRVPLQESHG QNINNHRRQN LSNITNHNVA NKFAPDGNMT KPMFVAPFSR
RGPSMNATIA EDRDMARPRI ALQQKPLNSN TANIRALQPL SNSAYKPKPT APAPSLAPLA
SKHSTLSYPT REAKFTQAPH HPNTHYGVRS AAPSYPARGD TIVQSQPSYS QHNVRHSVPS
HTVKTSTTFE PQAPEASVKD DAAAQDPLQI QASAPEYGSK EWIDGLVRIL PRCKFYFDCV
DQAMASRLTK ALHHYHAHVT MFFSLDVTHI VTTNYIPRSK TPSHHTPLQR PTTPMPSPSF
VPGKLPMKPL ALPPNSNTES NILVKALSHG IKIWSLERMV NLINPLVGGR IAKTGQQLEN
RNLQDFLQHE KVYGLTTTQN DDSPRAEYHV LKDHYLLVED VSGHYRTIIA QEFPKEVPKY
GGTPWPRLYV QSHSNRSPFV FAHDRSKSTK KPDETVNDKD ETLKDAEVAQ KGQEAPAGSN
TAAGDTRMMP SVPASGIINS VTSNAISTTS AMGKPVAVQG LQNTLDQLGK RVLNATKGEA
GIPPVVKTSE FVHPGSIFRA NRTTTDTDLN RLKRQPLGAV DLNTVAPEES KQPPAEPVQD
RLSATALDAH QPKERQAEEN ATQTAAPKDY RNKGYCENCR QLYDDFNAHT ATPEHRRYAH
DSSKFAQLDK LLMALQRKPK AVSAHTVAEA KGQEQAPGEN GSPPLVVGVG AQHAEPTLDT
VQPTSTSTAA HSETQNRSER CSKSRLPAVV RDTPPQNIEV ARTVVRKRVV EPVAKRAEIQ
RATKDDLEVV HETVEEQNNE DQAEDADDFD DQLSSEMSRL DVTEADDQDA ADAADAENDD
RLVQIPSILS TADDAPRSAR MSGDSSVPNK HHRLRVKPAF YDRLRLPYSD MGTASESQCL
SVADTDATQP DERFLECSGM NSMHTSQITD PVPQIELAIS LTDGPEASED PAADDFKLDE
TNESDKEGSD DAVALLKSPS AGRGAFAKAQ GAMLRQAMGL ALGQAAGGQD LMAPPERGVT
SGLFRGALKR KLENVLAEER GCEWSSQVAA TANSQTPGTP RPQQPSTRPI VYDDSLRSRL
LQQSTTPQRP VSWPNQRPFS TLPLPPAPPS FASPKQLSHH RRSQQPSPGY HHHHQRHVGT
DDTSDTIPIP SFAGSEADGS ALERYDSDVR SMGSSTGGYP TTPLAQHRAA YSHHQQHQQY
SSHRSHSNQH GIPQVLRSNP QYHSSPPVPR HTLPVHAQPS RRGVEITVND RNSTQSPRSA
VQTSPTSPLS YHDYDMPMQH LYHPATAMAT ATATATAKAT ASTPTAAHHP RSQSPADSTY
SGSGYSSPSR SPSQRSQFYR MQKIPTMSHA EQERERCYHH YRGNRLPESA GQKKVKSSSG
LEDEFEEYGE GCMVYIE
//
