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Database: UniProt
Entry: A0A086SVR2_HAPC1
LinkDB: A0A086SVR2_HAPC1
Original site: A0A086SVR2_HAPC1 
ID   A0A086SVR2_HAPC1        Unreviewed;       654 AA.
AC   A0A086SVR2;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   18-JUN-2025, entry version 40.
DE   SubName: Full=Hsk1-interacting molecule-like protein {ECO:0000313|EMBL:KFH41194.1};
GN   ORFNames=ACRE_080960 {ECO:0000313|EMBL:KFH41194.1};
OS   Hapsidospora chrysogenum (strain ATCC 11550 / CBS 779.69 / DSM 880 / IAM
OS   14645 / JCM 23072 / IMI 49137) (Acremonium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Bionectriaceae; Hapsidospora.
OX   NCBI_TaxID=857340 {ECO:0000313|EMBL:KFH41194.1, ECO:0000313|Proteomes:UP000029964};
RN   [1] {ECO:0000313|Proteomes:UP000029964}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11550 / CBS 779.69 / DSM 880 / IAM 14645 / JCM 23072 / IMI
RC   49137 {ECO:0000313|Proteomes:UP000029964};
RX   PubMed=25291769; DOI=10.1128/genomea.00948-14;
RA   Terfehr D., Dahlmann T.A., Specht T., Zadra I., Kuernsteiner H., Kueck U.;
RT   "Genome sequence and annotation of Acremonium chrysogenum, producer of the
RT   beta-lactam antibiotic cephalosporin C.";
RL   Genome Announc. 2:E0094814-E0094814(2014).
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:KFH41194.1}.
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DR   EMBL; JPKY01000141; KFH41194.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A086SVR2; -.
DR   STRING; 857340.A0A086SVR2; -.
DR   HOGENOM; CLU_017715_0_0_1; -.
DR   OrthoDB; 21380at2759; -.
DR   Proteomes; UP000029964; 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   Reference proteome {ECO:0000313|Proteomes:UP000029964};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00600}.
FT   DOMAIN          593..642
FT                   /note="DBF4-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51265"
FT   REGION          1..106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          171..196
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          216..238
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          266..294
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          385..410
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          520..598
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        274..285
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        385..398
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        537..546
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        548..562
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        563..576
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   654 AA;  73174 MW;  FC45B72AB089A2FA CRC64;
     MSSRRGPLTN NPNVVNSPLR AAGATSLAAK QKRSHANVQR EEAYGQPPPK KQAVEATVSQ
     RAARSPSKLP RSQVLAQRGI SAPSTTRTAP KERVSKPPTV YKTSNQDEGV DKEVWKKHYR
     AKFPKMVFYF ESIPDEIRAK LTKRVQYLGA RQEPFFSIEV THVITTRNIP TGRTDTQAAE
     PEVQEREPEE QPQTINPSLL DRNTAARRKL LFEFRNVPSR PQHVNDPTKA NKGIRNNDVL
     HKAREMGKKI WSLEKFQTMV SVLLESETDS GQQSSRTTNS RATSRPQGQT RGGHENNLLQ
     LLQHERINGP TDRDLGVFNR EVSYFKGPYI YVFDMEERHK PMMVREYAKV ANKADGDWPQ
     FRSVGNGRCP FVDEEPQERE YRKLREQREQ RREQERARAA AAKPAEVTTV KARDAATAAA
     AAATRPVTGK RTLAEMEDGH NKVRAPAASG VLNPAKAALS KQTLQNAFTS RAAEGRVVHG
     EPVASGVQPS NVTSAIRSQM ISSQAGVSAI KAGTSKELHG LQRKVLQKTA PTSQEASSRR
     PVEHSLEGPS SRSTTLSRQA SKAAQTQEEG GRQAAEGQEK RGQAESQPMK SKKDMKPGYC
     ENCQDKFRDF DEHIVSRKHR KFAENTDNWG ELDALLSKLK RSPKDFYMDV DYDL
//
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