GenomeNet

Database: UniProt
Entry: A0A0K3C8N5_RHOTO
LinkDB: A0A0K3C8N5_RHOTO
Original site: A0A0K3C8N5_RHOTO 
ID   A0A0K3C8N5_RHOTO        Unreviewed;       719 AA.
AC   A0A0K3C8N5;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   18-JUN-2025, entry version 36.
DE   SubName: Full=BY PROTMAP: gi|472586719|gb|EMS24238.1| regulatory subunit for Cdc7p protein kinase [Rhodosporidium toruloides NP11] gi|647398132|emb|CDR41759.1| RHTO0S06e05710g1_1 [Rhodosporidium toruloides] {ECO:0000313|EMBL:CTR06099.1};
DE   SubName: Full=Dfp1/Him1, central region-domain containing protein {ECO:0000313|EMBL:PRQ76196.1};
GN   Name=FGENESH: predicted gene_3.411 {ECO:0000313|EMBL:CTR06099.1};
GN   ORFNames=AAT19DRAFT_13218 {ECO:0000313|EMBL:PRQ76196.1},
GN   BN2166_0019600 {ECO:0000313|EMBL:CTR06099.1};
OS   Rhodotorula toruloides (Yeast) (Rhodosporidium toruloides).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX   NCBI_TaxID=5286 {ECO:0000313|EMBL:CTR06099.1, ECO:0000313|Proteomes:UP000199069};
RN   [1] {ECO:0000313|EMBL:CTR06099.1, ECO:0000313|Proteomes:UP000199069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Single colony {ECO:0000313|EMBL:CTR06099.1};
RA   Cajimat M.N.B., Milazzo M.L., Fulhorst C.F.;
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:PRQ76196.1, ECO:0000313|Proteomes:UP000239560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 0880 {ECO:0000313|EMBL:PRQ76196.1,
RC   ECO:0000313|Proteomes:UP000239560};
RX   PubMed=29521624;
RA   Coradetti S.T., Pinel D., Geiselman G., Ito M., Mondo S., Reilly M.C.,
RA   Cheng Y.F., Bauer S., Grigoriev I., Gladden J.M., Simmons B.A., Brem R.,
RA   Arkin A.P., Skerker J.M.;
RT   "Functional genomics of lipid metabolism in the oleaginous yeast
RT   Rhodosporidium toruloides.";
RL   Elife 7:0-0(2018).
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CWKI01000003; CTR06099.1; -; Genomic_DNA.
DR   EMBL; LCTV02000003; PRQ76196.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0K3C8N5; -.
DR   STRING; 5286.A0A0K3C8N5; -.
DR   OMA; GMKIWAI; -.
DR   OrthoDB; 21380at2759; -.
DR   Proteomes; UP000199069; Unassembled WGS sequence.
DR   Proteomes; UP000239560; Unassembled WGS sequence.
DR   GO; GO:0031431; C:Dbf4-dependent protein kinase complex; IEA:TreeGrafter.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
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; 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; PS50172; BRCT; 1.
DR   PROSITE; PS51265; ZF_DBF4; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:CTR06099.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199069};
KW   Transferase {ECO:0000313|EMBL:CTR06099.1};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00600}.
FT   DOMAIN          165..213
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   DOMAIN          588..637
FT                   /note="DBF4-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51265"
FT   REGION          1..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          86..118
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          130..159
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          213..257
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          536..555
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          642..719
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        24..34
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        92..108
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        227..241
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        536..553
FT                   /note="Gly residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        656..666
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        676..703
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   719 AA;  77095 MW;  0E54F11BD2202846 CRC64;
     MATATTPNSH RQATQSHNSR THSVRTVSCA QLAQDSRPPA PPFVEQQLRF VQALGGGAND
     VGPTSVPMQT SRIDGRTAAA AAAAAAGSRK RAAVEQDDTR SPDAADKRQA KRSRGANPLA
     ALSVNVAAGG AEKGAADGTK RKSRKTYAGA EKEKLQHESQ QWRAKYRKAF PSFTFYFDAV
     DDSTKASLSA AVKKLGASVD NFFSKKVTHV VTSRPLPSTS GKENAGAAAS KASTSASAST
     SRSKKTSARS PKTYELPNGQ KLWPLANATD HDKNPFIDSQ DILSKALDFG LKVWASEKLQ
     LIIDRINHAS PNKDKASLQR DPSLPTLLRD EQLYGTRERD PLVARADMHY FPSTKSYLLV
     EDSTGEHRPI VVKEYERPKK NEVPSWPVLW GGIEGRTGFY YYDGPEITYE RRVPPRPAPA
     PAATNGKAGG FGSTAARAVA PNLRRAVSLQ NVARGQQATY GYAGYEPAGR RDSYIAASGN
     SQIITSNIQS ATSTAARSGT AQANRFGNPY VDKRLAVLSN RTVSVAGGSI LGSGSTAGGS
     GGVASGSAGG SGGRLAALKR SERPGALKRS LSVDGHLARV PNPPVRDEPK KAGYCENCRI
     KYDCFREHVR SSKHRRFALN PKNWADLDKL LQRIARKPLE AGEWERGEEG ASSELAADEG
     EYEDSGYFDA SVLAGDAEEC EGDSAQDDGD EDEVMDEEEE EEESSKPLEA QVLAQAVRA
//
DBGET integrated database retrieval system