ID A0AAJ4XG10_9BASI Unreviewed; 784 AA.
AC A0AAJ4XG10;
DT 24-JUL-2024, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2024, sequence version 1.
DT 28-JAN-2026, entry version 7.
DE SubName: Full=Related to Hsk1-interacting molecule 1 {ECO:0000313|EMBL:SNX81709.1};
GN ORFNames=MEPE_00414 {ECO:0000313|EMBL:SNX81709.1};
OS Melanopsichium pennsylvanicum.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Melanopsichium.
OX NCBI_TaxID=63383 {ECO:0000313|EMBL:SNX81709.1, ECO:0000313|Proteomes:UP001294444};
RN [1] {ECO:0000313|EMBL:SNX81709.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Mp4 {ECO:0000313|EMBL:SNX81709.1};
RA Guldener U.;
RL Submitted (OCT-2023) 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:SNX81709.1}.
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DR EMBL; OAPG01000001; SNX81709.1; -; Genomic_DNA.
DR AlphaFoldDB; A0AAJ4XG10; -.
DR Proteomes; UP001294444; 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; IPR001357; BRCT_dom.
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; PF00533; BRCT; 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:UP001294444};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00600}.
FT DOMAIN 657..706
FT /note="DBF4-type"
FT /evidence="ECO:0000259|PROSITE:PS51265"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 71..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 143..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 299..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 634..660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 710..784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..179
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..656
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 733..743
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 784 AA; 86921 MW; 4E67CF7CFBB28C5A CRC64;
MSTKRDNTSS RIPLSVKNVP TQDVPSRDTS MLRKPTSQQL LRGSVATATS TSACPRATAS
RLPSFVSRSH LGFDRSNQEN IPLVPTTATP KKRAIPTDES HSRNIVVDSP SKRSRSSKTG
TDSSNTEQSI SVALASDLNG IRVNESRKLP STHVAASATA RSRRPQQAPN PVPAAATATS
VKTNRTLREP TEEFAMEARR RQSEQEIWRQ KSLRAFPNFI FHFDSVDDST ARKYTNLIQQ
LGGHVDQFFS RKVTHVVTTR RVPDGPTPEP VGATGGPSTT EKAGAHKLFR PSFLAARTSS
TKMGGNGARS RPIPLYSERN PLQDRPTRHY SPNDILVKAQ SFGIRLWQLE KLQNILTRLM
KLSLRDLDTP SKQEDLGQML EKEKVYGTSE RDPATARSTF YYFEKSARYV FVEDATLEHR
PIMCIEFQYT QEDRAQRIPP PWPVVYGQTP GRCPFTYYPP KKSSPTQDEG EPLSANKLNT
QQSLRRAVSL NNMVRSNLGP TFRPRVATIC TNDQRQQDYP MASGNSVSIT SNIASTTSNV
FTDQQAGATI GLPQDRRVAE LNRRMHMSNA PHRPLRTLNA SPASVLVGST ASGLGIRRES
GSPIVGSIAF QRGGPEQGAT VRRMLGLEDK ERRFETGTNG SGLQRSMSTS AINRPPSTKK
PGYCENCRVK YEHFIDHIND RKHRKFATTE SNFVDIDALI MRVQRPLRSV SEDEPSANYF
DLDAIPSSQP EENVPDQESE DESVSAGSPD GEDVHFGMAL THERGDSYDE QGFEASHEAV
PVAI
//
