DCR1B_DANRE
ID DCR1B_DANRE Reviewed; 571 AA.
AC B0V2S2; Q08BA3;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 80.
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; ORFNames=si:dkey-73i4.1, zgc:154089;
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 (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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). 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|UniProtKB:Q9H816}.
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}.
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; CT025875; CAQ15298.1; -; Genomic_DNA.
DR EMBL; BC124809; AAI24810.1; -; mRNA.
DR RefSeq; NP_001070751.1; NM_001077283.1.
DR AlphaFoldDB; B0V2S2; -.
DR SMR; B0V2S2; -.
DR STRING; 7955.ENSDARP00000090466; -.
DR PaxDb; B0V2S2; -.
DR Ensembl; ENSDART00000099692; ENSDARP00000090466; ENSDARG00000068833.
DR Ensembl; ENSDART00000186211; ENSDARP00000149606; ENSDARG00000068833.
DR GeneID; 768137; -.
DR KEGG; dre:768137; -.
DR CTD; 64858; -.
DR ZFIN; ZDB-GENE-061013-328; dclre1b.
DR eggNOG; KOG1361; Eukaryota.
DR GeneTree; ENSGT00940000158175; -.
DR HOGENOM; CLU_034741_0_0_1; -.
DR InParanoid; B0V2S2; -.
DR OMA; KMVTVLT; -.
DR OrthoDB; 1441774at2759; -.
DR PhylomeDB; B0V2S2; -.
DR TreeFam; TF329572; -.
DR Reactome; R-DRE-6783310; Fanconi Anemia Pathway.
DR PRO; PR:B0V2S2; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 8.
DR Bgee; ENSDARG00000068833; Expressed in mature ovarian follicle and 28 other tissues.
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 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..571
FT /note="5' exonuclease Apollo"
FT /id="PRO_0000398627"
FT REGION 346..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 431..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 501..532
FT /note="TBM"
FT COMPBIAS 363..386
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..487
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 165
FT /note="Q -> L (in Ref. 2; AAI24810)"
FT /evidence="ECO:0000305"
FT CONFLICT 239
FT /note="S -> N (in Ref. 2; AAI24810)"
FT /evidence="ECO:0000305"
FT CONFLICT 314
FT /note="K -> R (in Ref. 2; AAI24810)"
FT /evidence="ECO:0000305"
FT CONFLICT 336
FT /note="R -> Q (in Ref. 2; AAI24810)"
FT /evidence="ECO:0000305"
FT CONFLICT 339
FT /note="T -> A (in Ref. 2; AAI24810)"
FT /evidence="ECO:0000305"
FT CONFLICT 408
FT /note="G -> R (in Ref. 2; AAI24810)"
FT /evidence="ECO:0000305"
FT CONFLICT 415
FT /note="I -> M (in Ref. 2; AAI24810)"
FT /evidence="ECO:0000305"
FT CONFLICT 517
FT /note="Q -> H (in Ref. 2; AAI24810)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 571 AA; 64185 MW; 3EA154E026743F90 CRC64;
MNGKVLPDTP IAVDCWQLRK CLHVRLFFLS HMHSDHTCGL SSTWSHRPIY CSPLTAKLLR
LKLQIKQKWI RPLEIGQDHM LMLDDLGKER LTVNLIDANH CPGAVMFLFQ GYFGTRLYTG
DFRYTPSMLR VPCLQNHINI DVLYLDNTNC DPTRALPSRQ QATQQIKQII RDHPGYAVVI
GLYSLGKESL LVDLAMEFKT WVEVDRERLE TLRVLQLPDV FTTDSGAGRI RVVNQSMISA
SNLMAWNKLQ STIAILPTSR PMVSCHPNVY VVPYSDHSSY QELEDFVSAL SPISLVPIVG
NCLPYFSSLL SPRKKPKAVV IPESVKQYMM TNSNIRSSTN GMIQRTSRPE VRGVVFDSPE
TKLSQPNHDD MDSNDTEIDH DTTDRNSDSD CILLDMGTNS YHRDNDQGNK RLKLIRIESE
DVVTVTSSLT MDDNESVSTR KGIGSPDPSL IYECDHESPT KSSKEKSPEM GSTNSGEMCS
SMDSMHDQTS LTTAAALTLP NPQSVTSAIP ITLESEQFEH WLLENFTIPA EELKEGQVLR
GLCENYRLNP VDLPKPVGDP LEAAIKRLMS N
