ID A0A0D2KBS0_9EURO Unreviewed; 475 AA.
AC A0A0D2KBS0;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=DNA repair protein rad9 {ECO:0000256|PIRNR:PIRNR009303};
GN ORFNames=Z520_03203 {ECO:0000313|EMBL:KIY00540.1};
OS Fonsecaea multimorphosa CBS 102226.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX NCBI_TaxID=1442371 {ECO:0000313|EMBL:KIY00540.1, ECO:0000313|Proteomes:UP000053411};
RN [1] {ECO:0000313|EMBL:KIY00540.1, ECO:0000313|Proteomes:UP000053411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 102226 {ECO:0000313|EMBL:KIY00540.1,
RC ECO:0000313|Proteomes:UP000053411};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Fonsecaea multimorphosa CBS 102226.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts in DNA repair and mutagenesis. Involved in promoting
CC resistance to ionizing radiation and UV light, as well as regulating
CC cell cycle progression after irradiation.
CC {ECO:0000256|PIRNR:PIRNR009303}.
CC -!- SIMILARITY: Belongs to the rad9 family. {ECO:0000256|ARBA:ARBA00008494,
CC ECO:0000256|PIRNR:PIRNR009303}.
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; KN848066; KIY00540.1; -; Genomic_DNA.
DR RefSeq; XP_016634662.1; XM_016773716.1.
DR AlphaFoldDB; A0A0D2KBS0; -.
DR STRING; 1442371.A0A0D2KBS0; -.
DR GeneID; 27708949; -.
DR VEuPathDB; FungiDB:Z520_03203; -.
DR OrthoDB; 1111055at2759; -.
DR Proteomes; UP000053411; Unassembled WGS sequence.
DR GO; GO:0030896; C:checkpoint clamp complex; IEA:UniProtKB-UniRule.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR Gene3D; 3.70.10.10; -; 1.
DR InterPro; IPR046938; DNA_clamp_sf.
DR InterPro; IPR026584; Rad9.
DR InterPro; IPR007268; Rad9/Ddc1.
DR PANTHER; PTHR15237:SF0; CELL CYCLE CHECKPOINT CONTROL PROTEIN; 1.
DR PANTHER; PTHR15237; DNA REPAIR PROTEIN RAD9; 1.
DR Pfam; PF04139; Rad9; 1.
DR PIRSF; PIRSF009303; Cell_cycle_RAD9; 1.
DR SUPFAM; SSF55979; DNA clamp; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|PIRNR:PIRNR009303};
KW Reference proteome {ECO:0000313|Proteomes:UP000053411}.
FT REGION 288..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 475 AA; 52906 MW; 674664E101F5D4CF CRC64;
MPTLLFTVAP SGAAYFHDLL TCLAKFDEDV SLEATPQFLR LSSLNISKTA HAAFTLSSSF
FNKYHFSPGP RTTSAPALPK QWSCKLQIRA LLSIFKRRLG DQRDKDTALE TCDCELQDNL
DQAECRLVFR LNCRHGVVKT YRLFYEAGEI LHAAFDKIGS TNYWSVSSRT LRDIVEYFGP
KTDQLDWFFQ NGKVTFTSYT EKIQAGREIL KQPMHTSVAL ERKDFSDFNV QEGLHIGTVV
KDFRAIVAHA ETMHSQVTAR YSRGNRPLQI SYGENGLQAE FTLMTRGSAN VPVSTSTRTT
PARDLSMRPA SRPPEAPTPT SQTSLRNPRP PQSADTGMPP PARSSLHNRD QPTQSTSARA
DAEDSAPSLA AAAAPTPSIN IDPHSLFFPA DDDDHQWDEP NFEAEPDIVT WDESADNAAS
ASNSTRRIRD SEFHSFASIS AQEQHDRRTA SLAKSRFPVE IAPTQRLSQV KGIFD
//
