ID R9AA69_WALI9 Unreviewed; 1106 AA.
AC R9AA69;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 08-OCT-2025, entry version 51.
DE SubName: Full=Hsk1-interacting molecule 1 {ECO:0000313|EMBL:EOQ98939.1};
GN ORFNames=J056_002705 {ECO:0000313|EMBL:EOQ98939.1};
OS Wallemia ichthyophaga (strain EXF-994 / CBS 113033).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Wallemiomycotina;
OC Wallemiomycetes; Wallemiales; Wallemiaceae; Wallemia.
OX NCBI_TaxID=1299270 {ECO:0000313|EMBL:EOQ98939.1, ECO:0000313|Proteomes:UP000014064};
RN [1] {ECO:0000313|Proteomes:UP000014064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-994 / CBS 113033 {ECO:0000313|Proteomes:UP000014064};
RX PubMed=24034603; DOI=10.1186/1471-2164-14-617;
RA Zajc J., Liu Y., Dai W., Yang Z., Hu J., Gostincar C., Gunde-Cimerman N.;
RT "Genome and transcriptome sequencing of the halophilic fungus Wallemia
RT ichthyophaga: haloadaptations present and absent.";
RL BMC Genomics 14:617-617(2013).
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; KE007247; EOQ98939.1; -; Genomic_DNA.
DR RefSeq; XP_009270245.1; XM_009271970.1.
DR AlphaFoldDB; R9AA69; -.
DR STRING; 1299270.R9AA69; -.
DR GeneID; 20375657; -.
DR KEGG; wic:J056_002705; -.
DR eggNOG; KOG4139; Eukaryota.
DR HOGENOM; CLU_306339_0_0_1; -.
DR OrthoDB; 21380at2759; -.
DR Proteomes; UP000014064; 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 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:UP000014064};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00600}.
FT DOMAIN 719..768
FT /note="DBF4-type"
FT /evidence="ECO:0000259|PROSITE:PS51265"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 102..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 356..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 423..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 627..686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 828..858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1079..1106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..434
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..456
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..471
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..518
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..672
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..686
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 828..853
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1089..1099
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1106 AA; 124369 MW; 8E8A714E7E697648 CRC64;
MDDQFKRPIN AKKRVLEPTA SNNREHEPER ERTKRVKVDR QGDQDYIRKW TRAFRNIVLY
FDKPPENGIK GDIVQMAVKL GASVDDFFSN KVTHVITSRE IPKAATDSTS STKENKPKVL
SRQATPTYGD EAVTGSAAYT VVDPLNHTQH SIVDTQPKNP FLGPIQQADD LLLRAQEFKI
KVWSYPKIYN ILRHLLANDT GGNPLSHSQT QAHAHVHSHS HSHATAREQS LKAMLKREKL
QGTTERDRSV RQIDQYYFPR NVRYVLVEDA SETHRPVLIQ EYAVPRANEE AAWPILFACR
DERNPFTKYY QNEAPFDGRV YASKGWGMQE HVNYVVEAQL ARLCKQGVIT MVGSGQHGEQ
EMELEQDMEV DQHHHQAQLQ MQMQLQEDVD KNQNLIQSHS HSRQKDKAED AYAAASGNSV
TITSTNATSQ AQAARVPGQR DKRVLQLDKR TTEHRPKTAQ ANAQTRANAN ARSREADANA
IANETAVAST STSTSASASA SANTTLSTPT TTNTTTRTTP RRVSDHSHAP AHTSFAQLLQ
HRRSSRGKAV VEDSSKPTNA AQALLRAREH NKFEESVAAL KNRGAHDVVD DNFDSANYSA
NESVISSAPT PPPKDILATK EARAAFKEVL PRRKVPTTKP PKEHTQSGKT TQTAQTNDLI
SPKTQHTQQK ETAPSKEENK QVDKQVDAQV SQETVDMYNH MEKLQAKQKH KEKLSKRQEN
FKPGYCEICR VKFEDFDRHI KTSTHQKKAT DPKIWSSLDS LLTQTVRPPA KDLPPIPVSP
PSPPKKVNML KRLEKNEDDV AHEELEEMIL NPHVPLNVES TYIQNSQPTT VATTQTMSQS
QSQTQSQTHS QSSKKSAENA AVSYLENVAE FTEQKDGNVA EPEQVDGGVI DCLYSHQVHQ
AHQQPPQVDT YKPNNYQQER DAGYYHGYDD LSEFSAEQYQ LQKQIADYDV EAEWNAIQDI
INPPTNTNNN TNNNTHAHAH ELDLPRTITH ESITRQDILS LIDDDGRTVQ VYDDGDGYVE
EDQLEDGHAH DDGKFKVASP EMAEAPRSFS VFEAPQPPPL TRSGGKIDFV HTLTEAFRQM
SDSNDHQQHS QSHQSSSHSL VEQPLY
//
