ID   A0A6V8QNF2_TRIAP        Unreviewed;       632 AA.
AC   A0A6V8QNF2;
DT   02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT   02-DEC-2020, sequence version 1.
DT   08-OCT-2025, entry version 18.
DE   SubName: Full=Hsk1-interacting molecule 1 {ECO:0000313|EMBL:GFP53682.1};
GN   ORFNames=TASIC1_0003006000 {ECO:0000313|EMBL:GFP53682.1};
OS   Trichoderma asperellum (Filamentous fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=101201 {ECO:0000313|EMBL:GFP53682.1, ECO:0000313|Proteomes:UP000517252};
RN   [1] {ECO:0000313|EMBL:GFP53682.1, ECO:0000313|Proteomes:UP000517252}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IC-1 {ECO:0000313|EMBL:GFP53682.1,
RC   ECO:0000313|Proteomes:UP000517252};
RA   Kanamasa S., Takahashi H.;
RT   "Trichoderma asperellum IC-1 whole genome shotgun sequence.";
RL   Submitted (JUL-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:GFP53682.1}.
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DR   EMBL; BLZH01000003; GFP53682.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A6V8QNF2; -.
DR   OrthoDB; 21380at2759; -.
DR   Proteomes; UP000517252; 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; 2.
DR   Gene3D; 6.10.250.3410; DBF zinc finger; 1.
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; 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   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00600}.
FT   DOMAIN          568..617
FT                   /note="DBF4-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51265"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          84..108
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          170..207
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          513..567
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        97..108
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        180..196
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        532..542
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   632 AA;  71293 MW;  0149114986E50FD7 CRC64;
     MSSKRAPLAS NPNVANSPLR APSILTGYAK TKRSFATVQR EEPYGQPPPV KKQILENGAQ
     RAVRSPSKPV ARAPTHIVVP RNSSAVPRPV VRERSTRTAT TTSTARASQA VDTEKELWKK
     HHRAKFPKMV FYFESIPDDV RAKLTKRVTY LGARQEPFFS IDVTHVVTSR AIPPEKPETG
     DAEAEPEATE EQEPEEQPQT INPSLLDRNT AARRRLLYDF RQASSSQLDG LVKRNKTTRN
     NDVLHKAREM GKKIWSLDKF QSMLAVLLES ETQSYSSRSA SMRNHYGTKS SHEPNLYQLL
     HNERINGPSD RDPTVNTREL TYFKGPYLYI WDMDEKQKPI MVREYPKVAN KADGEWPQFR
     SVGNGRCPFV EEVDTAERDQ RKAREREKAY QAKKEESVQI LKAPEVPPMK PVTGKRTLTQ
     MEDAHNRVRA SMSMEKLQPI KVTFSRQPVA FTSRAEAGRM FAGEPVASGI QNTITSAIRS
     QMISSTSGIN GSKAGTSKEV HGLQRKVLQM ANPTSYDASS RRPAEVVADA ASSRSTLTRT
     TSKTIPAQDD DSQKVEKKAP AQRLKSKRDL KPGYCENCQD KFNDFDEHIL SRKHRKFAEN
     DDNWIELDAL LTQLKRMPKF SSAVSDDEGG EW
//