ID A0A9Q0BB29_9HYPO Unreviewed; 632 AA.
AC A0A9Q0BB29;
DT 13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 1.
DT 28-JAN-2026, entry version 12.
DE SubName: Full=Hsk1-interacting molecule-like protein {ECO:0000313|EMBL:KAI6778236.1};
GN ORFNames=J7T54_004131 {ECO:0000313|EMBL:KAI6778236.1};
OS Emericellopsis cladophorae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Bionectriaceae; Emericellopsis.
OX NCBI_TaxID=2686198 {ECO:0000313|EMBL:KAI6778236.1, ECO:0000313|Proteomes:UP001055219};
RN [1] {ECO:0000313|EMBL:KAI6778236.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MUM 19.33 {ECO:0000313|EMBL:KAI6778236.1};
RX PubMed=35049971;
RA Goncalves M.F.M., Hilario S., Van de Peer Y., Esteves A.C., Alves A.;
RT "Genomic and Metabolomic Analyses of the Marine Fungus Emericellopsis
RT cladophorae: Insights into Saltwater Adaptability Mechanisms and Its
RT Biosynthetic Potential.";
RL J Fungi (Basel) 8:0-0(2021).
RN [2] {ECO:0000313|EMBL:KAI6778236.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MUM 19.33 {ECO:0000313|EMBL:KAI6778236.1};
RA Goncalves M.F.M., Hilario S., Van De Peer Y., Esteves A.C., Alves A.;
RL Submitted (JUL-2022) 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:KAI6778236.1}.
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DR EMBL; JAGIXG020000077; KAI6778236.1; -; Genomic_DNA.
DR RefSeq; XP_051359092.1; XM_051509980.1.
DR AlphaFoldDB; A0A9Q0BB29; -.
DR GeneID; 75830620; -.
DR OrthoDB; 21380at2759; -.
DR Proteomes; UP001055219; 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; 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:UP001055219};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00600}.
FT DOMAIN 571..620
FT /note="DBF4-type"
FT /evidence="ECO:0000259|PROSITE:PS51265"
FT REGION 1..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 166..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 209..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 354..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 507..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..385
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..546
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..562
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 632 AA; 70749 MW; 90A67BDFFCE8EF4E CRC64;
MASRRGPLTN NPNVANSPLR PATAGFAKPK RPYAVLQREE PYGQAPPSKK QAVEQRAARS
PSKLPRAQAL PQRGSTTATT SRPVNKERMQ KPAASAKVSL QDEREKDAWK KHYRARFPKM
VFYFESIPED IRAKLTKRIT YLGARQEPFF SIDVTHVITT RAIPTEQPEA QPEPEAEPHH
EPSVAEQPQT INPSLLDRSS ARRKLLLEFR NAPSRSHASA DPSKPHKPTR NSDVLHKAKD
MGKKIWSLEK FQAMVSLLCE AEKPSHDYTA YVNSGPRATG ASAHASLNQM LRNERINGPS
DRDVSALSKD LTYFKGPHIY VFDMDERYKP IMVREYAKVS NKMDGDWPQF RSVGSGRCPF
VEEDPEEKER QKRREQRQLQ QEKDEARAAV AKQVEASKMQ AQAALPKPVT GKRMLGEMED
GHNKIRVPAT STINPAKAVL SKQGSQNAFV SRNEGGRLVH GEPVASGVQP SNITSAIRSQ
MISSQAGITG IKAGTSKELH GLQRQVLQKT GTVSQETSSR RPVDNSVEGT SSRSAPSLSR
KTSHNGSIPE AHKATDSRDK RSQCQTMKSK KDMKPGYCEN CQEKFRDFDE HILSRKHRRF
ADNPSNWVEL DDLLAELTRQ PKEFMSSPGY DL
//
