DCR1B_CHICK
ID DCR1B_CHICK Reviewed; 457 AA.
AC Q5QJC3;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=5' exonuclease Apollo;
DE EC=3.1.-.-;
DE AltName: Full=Beta-lactamase MBLAC2;
DE EC=3.5.2.6 {ECO:0000250|UniProtKB:Q9H816};
DE AltName: Full=DNA cross-link repair 1B protein;
DE AltName: Full=SNM1 homolog B;
GN Name=DCLRE1B; Synonyms=SNM1B;
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], AND FUNCTION.
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: 5'-3' exonuclease that plays a central role in telomere
CC maintenance and protection during S-phase. Participates in the
CC protection of telomeres against non-homologous end-joining (NHEJ)-
CC mediated repair, thereby ensuring that telomeres do not fuse. Plays a
CC key role in telomeric loop (T loop) formation by being recruited by
CC TERF2 at the leading end telomeres and by processing leading-end
CC telomeres immediately after their replication via its exonuclease
CC activity: generates 3' single-stranded overhang at the leading end
CC telomeres avoiding blunt leading-end telomeres that are vulnerable to
CC end-joining reactions and expose the telomere end in a manner that
CC activates the DNA repair pathways (By similarity). May be required for
CC DNA interstrand cross-link repair (PubMed:15572677). Possesses beta-
CC lactamase activity, catalyzing the hydrolysis of penicillin G and
CC nitrocefin (By similarity). Exhibits no activity towards other beta-
CC lactam antibiotic classes including cephalosporins (cefotaxime) and
CC carbapenems (imipenem) (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:15572677}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-lactam + H2O = a substituted beta-amino acid;
CC Xref=Rhea:RHEA:20401, ChEBI:CHEBI:15377, ChEBI:CHEBI:35627,
CC ChEBI:CHEBI:140347; EC=3.5.2.6;
CC Evidence={ECO:0000250|UniProtKB:Q9H816};
CC -!- SUBUNIT: Interacts with TERF2; the interaction is direct.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Chromosome, telomere {ECO:0000250}. Nucleus
CC {ECO:0000250}.
CC -!- DOMAIN: The TBM domain mediates interaction with TERF2. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DNA repair metallo-beta-lactamase (DRMBL)
CC family. {ECO:0000305}.
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DR EMBL; AY376897; AAR27405.1; -; mRNA.
DR RefSeq; NP_001026671.3; NM_001031500.3.
DR AlphaFoldDB; Q5QJC3; -.
DR SMR; Q5QJC3; -.
DR STRING; 9031.ENSGALP00000041920; -.
DR PaxDb; Q5QJC3; -.
DR GeneID; 428269; -.
DR KEGG; gga:428269; -.
DR CTD; 64858; -.
DR VEuPathDB; HostDB:geneid_428269; -.
DR eggNOG; KOG1361; Eukaryota.
DR InParanoid; Q5QJC3; -.
DR OrthoDB; 1441774at2759; -.
DR PhylomeDB; Q5QJC3; -.
DR PRO; PR:Q5QJC3; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0000781; C:chromosome, telomeric region; 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:0008409; F:5'-3' exonuclease activity; ISS:UniProtKB.
DR GO; GO:0008800; F:beta-lactamase activity; ISS:UniProtKB.
DR GO; GO:0003684; F:damaged DNA binding; IBA:GO_Central.
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; ISS:UniProtKB.
DR GO; GO:0000723; P:telomere maintenance; ISS:UniProtKB.
DR GO; GO:0031860; P:telomeric 3' overhang formation; ISS:UniProtKB.
DR GO; GO:0031627; P:telomeric loop formation; ISS:UniProtKB.
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 SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
PE 2: Evidence at transcript level;
KW Chromosome; DNA damage; DNA repair; Exonuclease; Hydrolase; Nuclease;
KW Nucleus; Reference proteome; Telomere.
FT CHAIN 1..457
FT /note="5' exonuclease Apollo"
FT /id="PRO_0000209121"
FT MOTIF 425..437
FT /note="TBM"
SQ SEQUENCE 457 AA; 50830 MW; 27E27E2D25E2AB95 CRC64;
MNGTVIPGTP IAVDFWSVRR AGGARLFFLS HMHSDHTVGL SSTWSRPLYC SPLTARLLHH
RLKVPTRWIR PLEVGQSHAV GEEVTVTLLD ANHCPGSVMF LFEGAFGTIL YTGDFRYSPA
MQREPALSGR RIDRLYLDNT NCRPHGALPS RSRAALQAAQ LIRRHPQHRV VIGVYSLGKE
ELLVDLALEF GTWVVVSPSR LEQMRLLELP EVFTTEEGAG RIHAVDVAEI RWDTLVSWNV
LHPTIAILPT GRPVKVTHPQ IHLIPYSDHS SFSELCEFVK WLKPCSVIPI VKGDMCYASF
QKYLSPDHQA LPGLGIPKPL QVSVQWQSKT KKQKPVCLVK RAAQHSVPKG VVYEPLEEYI
EQSDGLGGVT APQQNSHESA FCSLEDGICF YDCKEEELSG EQPGGAMAAG TAGQSLVSDE
DFPSELPKQY LLTPLNALKQ SSFCKALKNL FIRWEPS
