ID B6Q427_TALMQ Unreviewed; 662 AA.
AC B6Q427;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 08-OCT-2025, entry version 65.
DE SubName: Full=G1/S regulator NimO, putative {ECO:0000313|EMBL:EEA28199.1};
GN ORFNames=PMAA_030150 {ECO:0000313|EMBL:EEA28199.1};
OS Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS (Penicillium marneffei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441960 {ECO:0000313|EMBL:EEA28199.1, ECO:0000313|Proteomes:UP000001294};
RN [1] {ECO:0000313|Proteomes:UP000001294}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18224 / CBS 334.59 / QM 7333
RC {ECO:0000313|Proteomes:UP000001294};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
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DR EMBL; DS995899; EEA28199.1; -; Genomic_DNA.
DR RefSeq; XP_002144714.1; XM_002144678.1.
DR AlphaFoldDB; B6Q427; -.
DR STRING; 441960.B6Q427; -.
DR VEuPathDB; FungiDB:PMAA_030150; -.
DR HOGENOM; CLU_017715_0_0_1; -.
DR OrthoDB; 21380at2759; -.
DR PhylomeDB; B6Q427; -.
DR Proteomes; UP000001294; 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; 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 PROSITE; PS51265; ZF_DBF4; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000001294};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00600}.
FT DOMAIN 608..657
FT /note="DBF4-type"
FT /evidence="ECO:0000259|PROSITE:PS51265"
FT REGION 1..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..76
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..411
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..529
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..543
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 564..576
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..591
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..617
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 662 AA; 73916 MW; 4B47CDA648330115 CRC64;
MAAIFVPPSP QTSFAMSSRR PPLANVPNAA NSPHRSSNSA AVKRARTGSE MGSRIDLLFG
QPPAKKQFVD REDHHAAGTG PGSPSKARTM AAPQMSVESR MFSRRSHASQ LTPFEKKLMA
VREQKDSGAA QAPRNSRYDK VSAEKLDNIR QWQRHYRKAF PNFVFYFDSL PADVRNRSLR
EVLALGAREE RFFSRTVTHV VTSRPIPEVD VPSPTEATQN DQAAIENPPQ TVNPVLLERN
DNRRDHGNNT DVLYRARQMG MKIWAIEKLQ RMLTAIHEPD TSAPYTGGRA GSISAKGRGE
TELSQVLRNE RLHGPADRDP SQLMKDLVFF RGPFIYVHDM DEKTRPVMVR EYPKVPIKED
GLWPQFRSAP IGKCPFIEEP PSKKELAHMK EEKKRQRQEK VSVKDGAKDE NVPQAQNRAQ
PAKQEKEDAP VQVKLDEEED AAMLGPADNL KPLSVRPAPP RTKSENHPAK PIGKITAWPM
LREPAASGVQ PSNITSAIRS QMVSSTAAAP GAKAGLSKEV HELKRKVLEK SNGSMTTSAN
PSSHRPMDAP INARPASASA GSKRPREQMG HVHEEDTTQS EDNGSNNVSQ NTDRKGALQK
KAVKEKQRDP KPGYCENCRD KFDDFDEHIM TRKHRKFAMT LSNWTELDAL LSKLERPLKP
GY
//
