ID A0A9D3XBU6_9SAUR Unreviewed; 773 AA.
AC A0A9D3XBU6;
DT 03-MAY-2023, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2023, sequence version 1.
DT 02-APR-2025, entry version 11.
DE RecName: Full=Nibrin {ECO:0000256|ARBA:ARBA00020013, ECO:0000256|PIRNR:PIRNR011869};
GN ORFNames=KIL84_010443 {ECO:0000313|EMBL:KAH1176741.1};
OS Mauremys mutica (yellowpond turtle).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Geoemydidae; Geoemydinae; Mauremys.
OX NCBI_TaxID=74926 {ECO:0000313|EMBL:KAH1176741.1, ECO:0000313|Proteomes:UP000827986};
RN [1] {ECO:0000313|EMBL:KAH1176741.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MM-2020 {ECO:0000313|EMBL:KAH1176741.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:KAH1176741.1};
RA Gong S., Gao Y.;
RT "The genome of Mauremys mutica provides insights into the evolution of
RT semi-aquatic lifestyle.";
RL Submitted (SEP-2021) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the MRN complex, which plays a central role in
CC double-strand break (DSB) repair, DNA recombination, maintenance of
CC telomere integrity and meiosis. The MRN complex is involved in the
CC repair of DNA double-strand breaks (DSBs) via homologous recombination
CC (HR), an error-free mechanism which primarily occurs during S and G2
CC phases. The complex (1) mediates the end resection of damaged DNA,
CC which generates proper single-stranded DNA, a key initial steps in HR,
CC and is (2) required for the recruitment of other repair factors and
CC efficient activation of ATM and ATR upon DNA damage. The MRN complex
CC possesses single-strand endonuclease activity and double-strand-
CC specific 3'-5' exonuclease activity, which are provided by MRE11, to
CC initiate end resection, which is required for single-strand invasion
CC and recombination. Within the MRN complex, nbn acts as a protein-
CC protein adapter, which specifically recognizes and binds phosphorylated
CC proteins, promoting their recruitment to DNA damage sites. Recruits
CC mre11 and rad50 components of the MRN complex to DSBs in response to
CC DNA damage. Promotes the recruitment of PI3/PI4-kinase family members
CC atm, atr, and probably DNA-PKcs to the DNA damage sites, activating
CC their functions. Mediates the recruitment of phosphorylated rbbp8/CtIP
CC to DSBs, leading to cooperation between the MRN complex and rbbp8/CtIP
CC to initiate end resection. {ECO:0000256|PIRNR:PIRNR011869}.
CC -!- SUBUNIT: Component of the MRN complex. {ECO:0000256|PIRNR:PIRNR011869}.
CC -!- SUBCELLULAR LOCATION: Chromosome, telomere
CC {ECO:0000256|ARBA:ARBA00004574}. Nucleus, PML body
CC {ECO:0000256|ARBA:ARBA00004322}.
CC -!- SIMILARITY: Belongs to the Nibrin family.
CC {ECO:0000256|ARBA:ARBA00044757}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAH1176741.1}.
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DR EMBL; JAHDVG010000474; KAH1176741.1; -; Genomic_DNA.
DR OrthoDB; 552194at2759; -.
DR Proteomes; UP000827986; Unassembled WGS sequence.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0030870; C:Mre11 complex; IEA:InterPro.
DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR GO; GO:0003684; F:damaged DNA binding; IEA:TreeGrafter.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:TreeGrafter.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; IEA:InterPro.
DR GO; GO:0000723; P:telomere maintenance; IEA:InterPro.
DR CDD; cd17741; BRCT_nibrin; 1.
DR CDD; cd22667; FHA_NBN; 1.
DR FunFam; 2.60.200.20:FF:000017; Nibrin; 1.
DR FunFam; 3.40.50.10190:FF:000024; Nibrin; 1.
DR FunFam; 3.40.50.10980:FF:000001; Nibrin; 1.
DR Gene3D; 2.60.200.20; -; 1.
DR Gene3D; 3.40.50.10190; BRCT domain; 1.
DR Gene3D; 3.40.50.10980; Nibrin, BRCT2 domain; 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR040227; Nibrin-rel.
DR InterPro; IPR032429; Nibrin_BRCT2.
DR InterPro; IPR043014; Nibrin_BRCT2_sf.
DR InterPro; IPR013908; Nibrin_C.
DR InterPro; IPR016592; Nibrin_met.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR PANTHER; PTHR12162:SF0; NIBRIN; 1.
DR PANTHER; PTHR12162; NIBRIN-RELATED; 1.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF08599; Nbs1_C; 1.
DR Pfam; PF16508; NIBRIN_BRCT_II; 1.
DR PIRSF; PIRSF011869; Nibrin_animal; 1.
DR SMART; SM00292; BRCT; 1.
DR SMART; SM00240; FHA; 1.
DR SMART; SM01348; Nbs1_C; 1.
DR SUPFAM; SSF52113; BRCT domain; 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|PIRNR:PIRNR011869};
KW Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|PIRNR:PIRNR011869};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|PIRNR:PIRNR011869};
KW Meiosis {ECO:0000256|ARBA:ARBA00023254, ECO:0000256|PIRNR:PIRNR011869};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR011869};
KW Reference proteome {ECO:0000313|Proteomes:UP000827986};
KW Telomere {ECO:0000256|ARBA:ARBA00022895, ECO:0000256|PIRNR:PIRNR011869}.
FT DOMAIN 26..85
FT /note="FHA"
FT /evidence="ECO:0000259|PROSITE:PS50006"
FT DOMAIN 127..184
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 546..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 773 AA; 86518 MW; C575A1C4F342FA5E CRC64;
MWKLVSAAGP APAPGEPYRL LVGTEYVVGR KNCAILIQDD QSISRSHAIL TVTHPETNLS
QALSVPELII QDTSKYGTFV NGEKVLNGTS RTLKSGDRVN FGVFESKFRV EYEPLIVCSS
CLEVSGKTAL NQAILQLGGL VVNDWSEECT HLVMLSVKVT VKTICALICN RPIIKPEYFV
ECIRAIQSKQ QLPKLESFYP PVDEPAIGPE KLDLSMRHER KIIFRGKTFL FLSAKQHKKL
SPAIILGGGE AKLLPERIKE TSLLVAPEVC VIDAGLTNSQ VPVSDSVRNW IDSIITLLQS
KNLRAIPEAE IGLAVIFMSM ERYCNPQNQP GIAKQPVSPG SAILHPTLSQ SSTVHETIMP
VTTSDNRAYV ADTEPEELMD TCMEISGEER EKTPKMDRRD KMYSQNITTV KETPSTSGSV
NTGTVLPRMH RTLGVDQKSQ PLSPSKILGV NRNRERASQQ ESNSIKNYFQ AAPKKRERIE
EGETSVPKLA KMEEKSSQLS SQTQPITSLM WKSKVEQTQK EQYTLDLKTN LLPVDTRLKL
AIETSKSEKD KTVTKNVSSE KPASKKRKEL GDLVEDAATL ELVFGSKELD WEADMGDRGE
EPGTNMQKKR RLETKGERIE EENVIQEEAN RILQENELGA VPTTKKKIDI KQESSVLNTD
GLQDVSSNLP SRLLLTEFRS LVVSHPRPNS LVAPQINYKQ LNNFKKFKKV PYPGAGQLPH
IIGGSDLIGH HAKKNSQLEE WLRQEMEEQN RHAREESLAD DLFRYDPNVK RRR
//
