DCR1C_CHICK
ID DCR1C_CHICK Reviewed; 714 AA.
AC Q5QJC2;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Protein artemis;
DE EC=3.1.-.-;
DE AltName: Full=DNA cross-link repair 1C protein;
DE AltName: Full=SNM1 homolog C;
DE Short=chSNM1C;
DE AltName: Full=SNM1-like protein;
GN Name=DCLRE1C; Synonyms=SNM1C;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15572677; DOI=10.1128/mcb.24.24.10733-10741.2004;
RA Ishiai M., Kimura M., Namikoshi K., Yamazoe M., Yamamoto K., Arakawa H.,
RA Agematsu K., Matsushita N., Takeda S., Buerstedde J.-M., Takata M.;
RT "DNA cross-link repair protein SNM1A interacts with PIAS1 in nuclear focus
RT formation.";
RL Mol. Cell. Biol. 24:10733-10741(2004).
CC -!- FUNCTION: Required for V(D)J recombination, the process by which exons
CC encoding the antigen-binding domains of immunoglobulins and T-cell
CC receptor proteins are assembled from individual V, (D), and J gene
CC segments. V(D)J recombination is initiated by the lymphoid specific RAG
CC endonuclease complex, which generates site specific DNA double strand
CC breaks (DSBs). These DSBs present two types of DNA end structures:
CC hairpin sealed coding ends and phosphorylated blunt signal ends. These
CC ends are independently repaired by the non homologous end joining
CC (NHEJ) pathway to form coding and signal joints respectively. This
CC protein exhibits single-strand specific 5'-3' exonuclease activity in
CC isolation, and acquires endonucleolytic activity on 5' and 3' hairpins
CC and overhangs when in a complex with PRKDC. The latter activity is
CC required specifically for the resolution of closed hairpins prior to
CC the formation of the coding joint. May also be required for the repair
CC of complex DSBs induced by ionizing radiation, which require
CC substantial end-processing prior to religation by NHEJ (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PRKDC. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- PTM: Phosphorylation on undefined residues by PRKDC may stimulate
CC endonucleolytic activity on 5' and 3' hairpins and overhangs. PRKDC
CC must remain present, even after phosphorylation, for efficient hairpin
CC opening (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DNA repair metallo-beta-lactamase (DRMBL)
CC family. {ECO:0000305}.
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DR EMBL; AY376898; AAR27406.1; -; mRNA.
DR RefSeq; NP_001026765.1; NM_001031594.1.
DR AlphaFoldDB; Q5QJC2; -.
DR SMR; Q5QJC2; -.
DR STRING; 9031.ENSGALP00000022533; -.
DR PaxDb; Q5QJC2; -.
DR Ensembl; ENSGALT00000022573; ENSGALP00000022533; ENSGALG00000013926.
DR GeneID; 430764; -.
DR KEGG; gga:430764; -.
DR CTD; 64421; -.
DR VEuPathDB; HostDB:geneid_430764; -.
DR eggNOG; KOG1361; Eukaryota.
DR GeneTree; ENSGT00940000157779; -.
DR InParanoid; Q5QJC2; -.
DR OMA; FLFEGCH; -.
DR OrthoDB; 1441774at2759; -.
DR PhylomeDB; Q5QJC2; -.
DR PRO; PR:Q5QJC2; -.
DR Proteomes; UP000000539; Chromosome 1.
DR Bgee; ENSGALG00000013926; Expressed in spermatid and 13 other tissues.
DR ExpressionAtlas; Q5QJC2; baseline and differential.
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:0002250; P:adaptive immune response; 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 Adaptive immunity; DNA damage; DNA recombination; DNA repair; Endonuclease;
KW Exonuclease; Hydrolase; Immunity; Magnesium; Nuclease; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..714
FT /note="Protein artemis"
FT /id="PRO_0000209126"
FT REGION 391..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 516..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 598..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 638..683
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..407
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..439
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..467
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..500
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..577
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 670
FT /note="Phosphoserine; by ATM"
FT /evidence="ECO:0000250"
SQ SEQUENCE 714 AA; 80677 MW; 45AB9CB9FA305F6C CRC64;
MSRFGGRLRE YPQLSIDRFD YDNLRARAYF LSHCHKDHMK GLRAPALRRR LQSSLKVKLY
CSPVTKELLL TNSKYAFWEN HIVALEVETP TQISLVDETT GEKEDIEVTL LPAGHCPGSV
MFLFQGENGT VLYTGDFRLA KGEAARMELL HSGTSVKDIQ SVYLDTTFCD PRFYHIPSRE
ECLSGILELV RSWTTLSRYH VVWLNCKAAY GYEYLFINLS EELGIKVHVN KLDMFKNMPE
ILYHITTDRY TQIHACRHPK DDDYVRGNRL PCGITCQNGT PLHVISIKPS TMWFGERIKK
TNVIVRTGES TYRACFSFHS SYSEIMDFLS YIRPVNVYPN VLPVGGSEDK VMEILQPLCR
SYRRNTEPRY KPLGTLKRAC KRNLSDTDED ELFDTELSAR PKIAKYQGEE SKPSQTAQPE
NAERNINEST ESYRANTAYT SLKVDFVDCE ESNDDDDDDD DDDKEDDSEK NTAQVLSHEP
DANSIASCNG IPSNQQESNA DIPSWDMFFK CNKVDESSEN EDNFPSSADA GGSQSLFSDS
DGVSDSTHIS SQNSSQSTHI SEQGSQGWDS QMDTVLITSQ ERNAADFSCF SRGGSRTALL
SHDTPRDSQA DDSRWKLLGQ NPSCASDVIC DLKSEDCEKD AEAGTAPTQD LLVEISDSSR
TPDLELKRDS QSSSDFEIPL TPDAEIPQRD KLHYLYKKLA AGESIMRKNS PEKR
