ID A0A9P3HB66_9FUNG Unreviewed; 1229 AA.
AC A0A9P3HB66;
DT 13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 1.
DT 28-JAN-2026, entry version 11.
DE SubName: Full=Regulatory subunit for Cdc7p protein kinase {ECO:0000313|EMBL:GJJ73127.1};
GN ORFNames=EMPS_05485 {ECO:0000313|EMBL:GJJ73127.1};
OS Entomortierella parvispora.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mortierellomycotina;
OC Mortierellomycetes; Mortierellales; Mortierellaceae; Entomortierella.
OX NCBI_TaxID=205924 {ECO:0000313|EMBL:GJJ73127.1, ECO:0000313|Proteomes:UP000827284};
RN [1] {ECO:0000313|EMBL:GJJ73127.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=E1425 {ECO:0000313|EMBL:GJJ73127.1};
RA Herlambang A., Guo Y., Takashima Y., Nishizawa T.;
RL Submitted (NOV-2021) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GJJ73127.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=E1425 {ECO:0000313|EMBL:GJJ73127.1};
RX PubMed=35023780; DOI=10.1128/mra.01101-21;
RA Herlambang A., Guo Y., Takashima Y., Narisawa K., Ohta H., Nishizawa T.;
RT "Whole-Genome Sequence of Entomortierella parvispora E1425, a Mucoromycotan
RT Fungus Associated with Burkholderiaceae-Related Endosymbiotic Bacteria.";
RL Microbiol. Resour. Announc. 11:0-0(2022).
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:GJJ73127.1}.
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DR EMBL; BQFW01000007; GJJ73127.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A9P3HB66; -.
DR OrthoDB; 21380at2759; -.
DR Proteomes; UP000827284; 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:UP000827284};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00600}.
FT DOMAIN 538..587
FT /note="DBF4-type"
FT /evidence="ECO:0000259|PROSITE:PS51265"
FT REGION 103..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 369..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 654..689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 878..897
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 987..1025
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1122..1170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..380
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..665
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1127..1137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1229 AA; 133466 MW; 33C3EBBF872B0C13 CRC64;
MAEIGMNPQP LRTPFQDVGN NLNAMRPGLT SQGNALQQKP AQKVSPTIII DEKEIQRSRL
ALQQRTISGL NIYNPKAQQP LGAKVRMPQG TYPEAKKLEG ALRTGDRDKN PSAGVPPQQI
GTVNNPAEVT RRWLQMLPSC RFYFDNVEPP VVAKISKVLA AHNSSVAMFF SNDVTHLITT
RAIPRKEDHA RIKLQAQEES QNAAQQQASI PVLKPSIKPA GPPAPTQEPS IIVKAIGLNI
KIWHMDRMKH LMEPLMGKSV AHAESRKLQD LLLHEKTYGL TTTQMDDSVR SDYHIFRGPY
VLIEDTTGRH RTILAHEYDS KKTSSSVKCP WPKIQLHMTE RSPFIHIEPR VPKQEAQAVP
ARQGIEPAAA AGEAPRVPEA QDVQPSPSAL ASGIVNSVTS HVVSTTSAMG KAHHAQGPEA
AHDEVLRQLG KRTLPAPKAD AIVSAAMVAT VPTQDSKKAE FARPAEIVRP GSAGVLLEAG
ASKFRLQKTE QQPQAVPQTK TVIATADATV PIPLGLPPVP DPARQEQLKA LAPAVPPEHR
KKGYCENCRG FFEDMNRHIA SQAHRIYAHD ASKFVHLDKF LLRLKRQPKT VTASTKLDDL
DLSKDQPAVV PSLEKSTNSD AAISPAASTA IKGDCAEAVE LGNNDPCMNL LAPSSKETTG
MQEPSLTIKE AVPESRSPPE GDDADIAGRN EPLESGVAQE VPLTSDNNVT IHTNETSAAN
DAGAAHDVET TNDADTVNNA NNANDANDAN DLLDADDADD LKDMATMAAS VPSMTCLESQ
DRLLVNPFLE DASEPARVPG FFAKRVFSNQ LRLPMSDNLT SQADTDATQP DDRFLDGSAA
YSQATEPVVQ IHLSMSMSTL TDGPEPVPAV SERERNYAHE NESLGSSDSD KEESDDAVAL
VKSPSAGRGL FARSQGTLLR SGLMNLSSAR QGDGELSRPA MSLKRKLDIA LSEEREAQRN
GTSLQTKTQT LKQKTVVYDD NLRSRLLSHT PAPSTRPAAW STLRNPFESH TPMPASSPIQ
LLPETSPLSH QFGATAVDTT SDTLPLDSIS GRDFGRPYMN SIADYGFDSQ LGYPDTPSTQ
KVARMSAHQG TPVTLPQPFV FNSHARQFAS PGADFGFAQT ADAAASGPTS RQTSPTSPVG
HESVLSRSPA RSAYMESTSP SPSRSPSHRQ MYRNHFPVMT RAEQEQERCF HHYRGHRLPE
AAAQKKMRSS ISLLEEFEEY GEGCMVFIE
//
