ID A0AAD4D911_9FUNG Unreviewed; 1273 AA.
AC A0AAD4D911;
DT 29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2024, sequence version 1.
DT 28-JAN-2026, entry version 8.
DE RecName: Full=DBF4-type domain-containing protein {ECO:0000259|PROSITE:PS51265};
GN ORFNames=BGZ95_000276 {ECO:0000313|EMBL:KAG0271854.1};
OS Linnemannia exigua.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mortierellomycotina;
OC Mortierellomycetes; Mortierellales; Mortierellaceae; Linnemannia.
OX NCBI_TaxID=604196 {ECO:0000313|EMBL:KAG0271854.1, ECO:0000313|Proteomes:UP001194580};
RN [1] {ECO:0000313|EMBL:KAG0271854.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NRRL 28262 {ECO:0000313|EMBL:KAG0271854.1};
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:KAG0271854.1}.
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DR EMBL; JAAAIL010001045; KAG0271854.1; -; Genomic_DNA.
DR AlphaFoldDB; A0AAD4D911; -.
DR Proteomes; UP001194580; 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 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 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:UP001194580};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00600}.
FT DOMAIN 595..644
FT /note="DBF4-type"
FT /evidence="ECO:0000259|PROSITE:PS51265"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 383..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 510..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 855..892
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 909..940
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1164..1183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..411
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..523
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..543
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 865..878
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 929..938
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1170..1183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1273 AA; 139981 MW; 5934DB7042A0CCCD CRC64;
MADRPLYSAH QRAPLQESRG YNTNQPRQHL NGLTTFNAPS GTLNKPGQDV IFARSSSLVN
MPLKPVLASQ TDKDDTRPRI ALQQKPFNGN NANNLKAPPA TTLMPSNSMY KTKPVPFPGF
TQTTSSYTRS DVNIESRSRL LSQHVDLAQH LPQPQDTEPH TQPRHKTRPK PEYGTPEWAQ
QMAGVLPRCR FYFDSVDPAM IKKISDVVRS HRGTTTSFFS NEVTHVITTR SVPDDNTLKR
AKNQDDIDHL SSSQLQDPRK PNTKIFPNAE TSILVKALSL GIKIWTLDST LKLLNPLAPG
LVKQTGDRNL KDMLQYEKVH GVSTIHVDNS TKPDFYAFQG KYVLVDDTTG YYRTIMAYDF
TAKPSATGKH PWPRIYLQES DRSPFCYNEP ASKESERPPG IRDDKGDNTK VDKDLANAAQ
DAQPADDQKL SPSAMASGIV NSITSNIIST TTSTTAKSVV AIPQQDRRVE QLEKRALNAT
KVETGVSVDF NKKLEFARPL DMARRDTDAA TLGNARQDTT PNRGTLEDAG NKMQPPTLTP
KLNTGLVIST NNERVVTQGH EAADSARDGA TNAQPTHVIP EVPVDRAVMH KEVKDYRKQR
YCENCRGFFE NFEKHIESPA HRKYAHDASK FAQLDILLAK LQRKPKITSA LTEMPLIALA
PSEPEANGGC STNETCDDEP VTLAPEPLDM HHTQEAMDTN PRTQELPAAM NESMVHSEQN
PFQCQAVPVQ ETQQPAGRML DRRDDEEDEG IVEDIDEEVT HDQIEDQATL TLEPAREAVE
EGDITDVLSS ELSLLGLSER GVDRYSDQPD DVETETPLTI RKEDGKVAET PSELMGAIKA
HAPSSLQKVL RHEFRLPPSD RSGPSDGNIT SQLETDTTQP DDRFLDGSAS ASVDDGLSTP
IRLLCDLSST VGSPNASRAA GREYFSPEST HESDREGGSD DAVVMVKVSS SYSPTNDLTS
GLYKGALKRK LENVLAEERA ADQAQARIGN AIETPDTPRP DSLFASRQLP VDVGSSNASH
TSSQRPVAWF IDSPSHSSAQ SSPLSPNVPL ETLFQTTSPP PAFNPFHAPV DCSLQRQAQL
ASGYFHPSLS SQLGHESSPL SHRVARRQSL TINSQQTPSS LSRVQQRPLQ IGTPIVPFQD
YSQMKEPETS AKSAIPAPVV TARKGPEALP SQSSPLAYSS PGGSHSPMDA INFMGHSGYG
FMSPTQSPSR RAQVQRTQFP VMTHAEQEQE RFFHHYNGNH LPEPAGGAKK MRSSSSLAEA
YEEYGEGAMV FIE
//
