DCR1B_AILME
ID DCR1B_AILME Reviewed; 529 AA.
AC D2H8V8;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 1.
DT 25-MAY-2022, entry version 51.
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=PANDA_006715;
OS Ailuropoda melanoleuca (Giant panda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX NCBI_TaxID=9646;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20010809; DOI=10.1038/nature08696;
RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA Wang J.;
RT "The sequence and de novo assembly of the giant panda genome.";
RL Nature 463:311-317(2010).
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. Together with TERF2, required to
CC protect telomeres from replicative damage during replication by
CC controlling the amount of DNA topoisomerase (TOP1, TOP2A and TOP2B)
CC needed for telomere replication during fork passage and prevent
CC aberrant telomere topology. Also involved in response to DNA damage:
CC plays a role in response to DNA interstrand cross-links (ICLs) by
CC facilitating double-strand break formation. In case of spindle stress,
CC involved in prophase checkpoint (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. Interacts
CC with MUS81, MRE11 and FANCD2. Interacts with HSPA2, HSPA8 and HSPA14.
CC Interacts with SPAG5 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Chromosome, telomere {ECO:0000250}. Nucleus
CC {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center,
CC centrosome {ECO:0000250}. Note=Mainly localizes to telomeres, recruited
CC via its interaction with TERF2. During mitosis, localizes to the
CC centrosome (By similarity). {ECO:0000250}.
CC -!- DOMAIN: The TBM domain mediates interaction with TERF2. {ECO:0000250}.
CC -!- PTM: Ubiquitinated, leading to its degradation. Interaction with TERF2
CC protects it from ubiquitination (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; GL192586; EFB15061.1; -; Genomic_DNA.
DR AlphaFoldDB; D2H8V8; -.
DR SMR; D2H8V8; -.
DR STRING; 9646.ENSAMEP00000003441; -.
DR eggNOG; KOG1361; Eukaryota.
DR HOGENOM; CLU_034741_0_0_1; -.
DR InParanoid; D2H8V8; -.
DR OMA; KMVTVLT; -.
DR Proteomes; UP000008912; Unassembled WGS sequence.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0000781; C:chromosome, telomeric region; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008409; F:5'-3' exonuclease activity; ISS:UniProtKB.
DR GO; GO:0008800; F:beta-lactamase activity; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
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 SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
PE 3: Inferred from homology;
KW Chromosome; Cytoplasm; Cytoskeleton; DNA damage; DNA repair; Exonuclease;
KW Hydrolase; Isopeptide bond; Nuclease; Nucleus; Reference proteome;
KW Telomere; Ubl conjugation.
FT CHAIN 1..529
FT /note="5' exonuclease Apollo"
FT /id="PRO_0000398625"
FT REGION 352..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 494..509
FT /note="TBM"
FT COMPBIAS 364..392
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 334
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H816"
SQ SEQUENCE 529 AA; 59809 MW; B23600F5EC8F08A2 CRC64;
MNGALIPHTP IAVDFWSLRR AGSARLFFLS HMHSDHTVGL SSTWARPLYC SPITAYLVHR
HLQVPKEWIR ALEVGESHVL PLDEIGRETM TVTLMDANHC PGSVMFLFEG YFGTILYTGD
FRYTPSMLKE PALKLGKQIH TLYLDNTNCN PAWVLPSRQE AARQIVELIR KHPQHNIKIG
LYSLGKESLL EQLALEFQTW VVLSPRRLEL VQLLGLADVF TLEEKAGRIH AVDHMEICHS
AMLHWNQTHP TIAILPTSRK IHRSHPDIHI IPYSDHSSYS ELRTFVAALK PCQVVPIVSR
QPCRDYFQDS LSPRLSVPLI PDSVQQYMNS SSRKPSFLWL LLERRLKRPR TRGVVFDSSQ
ETADQSQADR DSKKAKNENL SGDLEKQASR HPLQNKKQLF PDFCSKEWDG TAPSSESQKM
VTVRTAPLSF SVHVRSTDEN FLSLETGEET GVGPHLVPRG DHDGLAATGN QSACLGQDSP
LSHRSKAAPL QAPEFRGLAL KYLLTPVNFF QAQFSSRGFD QQVEKYHKP
