ID I3JG27_ORENI Unreviewed; 801 AA.
AC I3JG27;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Nibrin {ECO:0000256|ARBA:ARBA00020013, ECO:0000256|PIRNR:PIRNR011869};
GN Name=nbn {ECO:0000313|Ensembl:ENSONIP00000007818.2};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000007818.2, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000007818.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Component of the MRE11-RAD50-NBN (MRN complex) which plays a
CC critical role in the cellular response to DNA damage and the
CC maintenance of chromosome integrity. The complex is involved in double-
CC strand break (DSB) repair, DNA recombination, maintenance of telomere
CC integrity, cell cycle checkpoint control and meiosis.
CC {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
CC {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR011869}.
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DR AlphaFoldDB; I3JG27; -.
DR Ensembl; ENSONIT00000007823.2; ENSONIP00000007818.2; ENSONIG00000006204.2.
DR GeneTree; ENSGT00390000000521; -.
DR HOGENOM; CLU_023410_0_0_1; -.
DR Proteomes; UP000005207; Linkage group LG11.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0030870; C:Mre11 complex; IEA:InterPro.
DR GO; GO:0006302; P:double-strand break repair; IEA:InterPro.
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 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; SM00240; FHA; 1.
DR SMART; SM01348; Nbs1_C; 1.
DR SUPFAM; SSF52113; BRCT domain; 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
PE 4: Predicted;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|PIRNR:PIRNR011869};
KW Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW DNA damage {ECO:0000256|PIRNR:PIRNR011869};
KW DNA repair {ECO:0000256|PIRNR:PIRNR011869};
KW Meiosis {ECO:0000256|ARBA:ARBA00023254, ECO:0000256|PIRNR:PIRNR011869};
KW Nucleus {ECO:0000256|PIRNR:PIRNR011869};
KW Reference proteome {ECO:0000313|Proteomes:UP000005207};
KW Telomere {ECO:0000256|ARBA:ARBA00022895, ECO:0000256|PIRNR:PIRNR011869}.
FT DOMAIN 22..70
FT /note="FHA"
FT /evidence="ECO:0000259|PROSITE:PS50006"
FT REGION 412..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 773..801
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..480
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..527
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..618
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..646
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 773..795
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 801 AA; 87914 MW; C2974237D9F58429 CRC64;
MWILTPQQPG DEACYLLPGK EYVVGRKNCD ILLPSDQSIS RAHAHLSATE QTLTLKDTSK
YGTFVNNQQI TTPVNLKSGD LVTFGVFQSK FSVVHLQPVV CSSCLDNAGQ ASLSQAVLAL
GGKLVSSWSQ DCTHLVMSSI KVTIKTISAL LCCCPIVKPE FFSELSRAVQ QKLPPPKAES
FIPEIDEPSL NKDNVNLGAV PLRKQLFSGR TFIFLSAKQL KRLRAAVSFG GGRSQLLEEG
SLPRDLLESP LSCVVDFTTG ASQTLLSPSA TEWANSVKSI VERKGLRVIT ESEIGLAAIY
ASCEKYCNPS SSDSDSVPKV TPRIPSASLS QSVAVDETVL PAASQNITAY AANTETSQRM
RVCEVTGVTS VGETPEKKPH QYASQLRGSS LVAQKTTTQC VVDETVSSSF TAAANAESQK
KKSESKLAGE DGFDIRPQPS TPKTNSGTKT FPPKQSPQKP KISSQASPQK QSTLTTFFQP
ASKKRHLEDE PSAVTSDPKR PALESSVTAR SEEPRSRKRK EMEDVIQMEE LESIMSEDMD
CFDEQPSINK GQQAKHEHSS AKQKQVLNSA EFSSKRQRVH LEKNGITNQR PQAGAEKESS
LEKNSQRSEQ HTVRIKTEPA DPADYTTANH GSSKPEEMSS ASTSKDVIPF EEDDVSFIED
LELLNADIPQ PKEETKSPLK PVVIKQEVQE SKIDEDLPKK LLLVEFKSLT VAAPPKAKQN
QTQGNGLIKN FKCFRKNRVP GSEGFHHIIG GSDLLVHNRG KNSDLDEWLK DAAEEEQQSR
RDETIGDDLF RYNPTKLSKR R
//
