DCR1C_DANRE
ID DCR1C_DANRE Reviewed; 639 AA.
AC Q5RGE5; Q1RLS6;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Protein artemis;
DE EC=3.1.-.-;
DE AltName: Full=DNA cross-link repair 1C protein;
GN Name=dclre1c; ORFNames=si:dkey-153k10.3, zgc:136877;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May have a role in the processing of DNA double strand breaks
CC (DSBs) prior to their repair by the non homologous end joining (NHEJ)
CC pathway. Probably exhibits both exonuclease and endonuclease activity
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DNA repair metallo-beta-lactamase (DRMBL)
CC family. {ECO:0000305}.
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DR EMBL; BX901962; CAI20677.1; -; Genomic_DNA.
DR EMBL; BC115304; AAI15305.1; -; mRNA.
DR RefSeq; NP_001038566.1; NM_001045101.1.
DR RefSeq; XP_017210553.1; XM_017355064.1.
DR AlphaFoldDB; Q5RGE5; -.
DR SMR; Q5RGE5; -.
DR STRING; 7955.ENSDARP00000067187; -.
DR PaxDb; Q5RGE5; -.
DR Ensembl; ENSDART00000067188; ENSDARP00000067187; ENSDARG00000045704.
DR Ensembl; ENSDART00000182748; ENSDARP00000151325; ENSDARG00000110444.
DR GeneID; 566285; -.
DR KEGG; dre:566285; -.
DR CTD; 64421; -.
DR ZFIN; ZDB-GENE-041210-72; dclre1c.
DR eggNOG; KOG1361; Eukaryota.
DR GeneTree; ENSGT00940000157779; -.
DR HOGENOM; CLU_029238_0_0_1; -.
DR InParanoid; Q5RGE5; -.
DR OMA; FLFEGCH; -.
DR OrthoDB; 1441774at2759; -.
DR PhylomeDB; Q5RGE5; -.
DR TreeFam; TF329572; -.
DR Reactome; R-DRE-5693571; Nonhomologous End-Joining (NHEJ).
DR PRO; PR:Q5RGE5; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 4.
DR Bgee; ENSDARG00000045704; Expressed in testis and 19 other tissues.
DR ExpressionAtlas; Q5RGE5; baseline.
DR GO; GO:0070419; C:nonhomologous end joining complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0035312; F:5'-3' exodeoxyribonuclease activity; IBA:GO_Central.
DR GO; GO:0003684; F:damaged DNA binding; IBA:GO_Central.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IBA:GO_Central.
DR GO; GO:0036297; P:interstrand cross-link repair; IBA:GO_Central.
DR GO; GO:0031848; P:protection from non-homologous end joining at telomere; IBA:GO_Central.
DR Gene3D; 3.60.15.10; -; 1.
DR InterPro; IPR011084; DRMBL.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR Pfam; PF07522; DRMBL; 1.
DR Pfam; PF12706; Lactamase_B_2; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
PE 2: Evidence at transcript level;
KW DNA damage; DNA recombination; DNA repair; Endonuclease; Exonuclease;
KW Hydrolase; Nuclease; Nucleus; Reference proteome.
FT CHAIN 1..639
FT /note="Protein artemis"
FT /id="PRO_0000209127"
FT REGION 450..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 515..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 590..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..467
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..537
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..570
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 92
FT /note="S -> N (in Ref. 2; AAI15305)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="N -> S (in Ref. 2; AAI15305)"
FT /evidence="ECO:0000305"
FT CONFLICT 592
FT /note="A -> V (in Ref. 2; AAI15305)"
FT /evidence="ECO:0000305"
FT CONFLICT 635
FT /note="A -> V (in Ref. 2; AAI15305)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 639 AA; 71711 MW; 33CD8B23AE326A2A CRC64;
MSSFAGRMKE YPSISLDRFD RENLHARAYF LSHCHKDHMK GLKGPLLKRK LKFSLTVKLY
CSYVTKELLL SNPRYAFWED HIVPLELDSP TSISLIDEST GETEDVVVTL LSAGHCPGSV
MFLFEGAKGT VLYTGDFRLA VGDAARMEYL HSGDRVKDIQ SVYIDTTFFD PKYYQIPSRE
ACLAGIQQLV QDWICQSPYH VVWLNCKAAY GYEYLFTNLG QEFNSQIHVN SLDMFKKMPE
ILCHVTTNRA TQIHACRHPK DEEFFRANRL PCGSTAPDGI PLNIISIKPS TIWFGERTRK
TSVVVKMGSS SYRACFSFHS SYLEVKDFLS YICPVNIYPN VIPLGKTVED LTELLKPLCR
KHCGREEIVY KPLGALKRTR KRSTSEGSDS DGDLFEEVST APRRRKITVS DLTTVAIRVR
PHSANADSHD NDQTYSLIKL CPSAHTSNYM DCTESNDDDD DEDDAAEQTP AAAPPPSSTE
KPCSKHTHSD SSLTSSTQPC WEKFFKAEVV LTDESELENS QNTQTLSTEN TASQSPELFQ
DEDEDSSVHM SSSQSTHISD AGTESLSQVD TIMVQEDHSK ACNLQHKTEE AAELKSDSQV
SSDFELPPTP GSKVPQPEDL KELYRKLAAG EDVVARQIF
