ID E5FGM8_MIOTA Unreviewed; 748 AA. AC E5FGM8; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 24-JAN-2024, entry version 38. DE RecName: Full=Nibrin {ECO:0000256|ARBA:ARBA00020013}; DE Flags: Fragment; GN Name=NBN {ECO:0000313|EMBL:ADQ01171.1}; OS Miopithecus talapoin (Angolan talapoin) (Cercopithecus talapoin). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; OC Cercopithecidae; Cercopithecinae; Miopithecus. OX NCBI_TaxID=36231 {ECO:0000313|EMBL:ADQ01171.1}; RN [1] {ECO:0000313|EMBL:ADQ01171.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=20975951; DOI=10.1371/journal.pgen.1001169; RA Demogines A., East A.M., Lee J.H., Grossman S.R., Sabeti P.C., Paull T.T., RA Sawyer S.L.; RT "Ancient and recent adaptive evolution of primate non-homologous end RT joining genes."; RL PLoS Genet. 6:E1001169-E1001169(2010). CC -!- SUBCELLULAR LOCATION: Chromosome, telomere CC {ECO:0000256|ARBA:ARBA00004574}. Nucleus CC {ECO:0000256|ARBA:ARBA00004123}. 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; HM486835; ADQ01171.1; -; mRNA. DR AlphaFoldDB; E5FGM8; -. 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 2: Evidence at transcript level; KW Cell cycle {ECO:0000256|ARBA:ARBA00023306}; KW Chromosome {ECO:0000256|ARBA:ARBA00022454}; KW Meiosis {ECO:0000256|ARBA:ARBA00023254}; KW Telomere {ECO:0000256|ARBA:ARBA00022895}. FT DOMAIN 24..83 FT /note="FHA" FT /evidence="ECO:0000259|PROSITE:PS50006" FT REGION 326..345 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 426..480 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 504..552 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 330..345 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 426..460 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 461..477 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 504..538 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT NON_TER 748 FT /evidence="ECO:0000313|EMBL:ADQ01171.1" SQ SEQUENCE 748 AA; 84305 MW; 7E600DE2205ACF74 CRC64; MWKLLPVAGP AGGEPYRLLT GVEYVVGRKN CALLIENDQS ISRNHAVLTA NFSVTNLSQT DEIPVLTLKD NSKYGTFVNE EKMQNGFSRT LKSGDGITFG VFESKFRVEY EPLVACSSCL DVSGKTALNQ AILQLGGFTV NNWTEECTHL VMVSVKVTIK TICALICGRP IVKPEYFTEF LKAVQSKKQP PQIESFYPPL DEPSIGSKNV DLSGRQERKQ IFKGKTFIFL SAKQHKKLSS AVVFGGGEAR LITEENEEEH NLFLAPETCV VDTGITNSQT LIPDSQKKWI QSIMDMLQRQ GLRPIPEAEI GLAVIFMTTK NYCDPRGHPS TGLKTTTPGP SLSQGLSVDE KLMPSTPVNA TTCVADTESE QADTWDLSER PKEIKVSKME QKIRMLSQDT PTIKESCKTS SNNNSMVSNT LAKMRIPNYQ LSPTKLPSIN KSKDRASQQQ QTNSIRNYFQ PSTKKRERDE ENQEVSSCKS ARIEMSCSVL EQTQPATPSL WKNKEQHLSQ NEPVDTNSDD NLFTDTDLKS SVKNSASKSH ASEKLRSNKK REMDDVAIED EVLEQLFKDT KPELETVVKV QKQEEDVNIR KRPRMDIETN DTFSDEAVPE SSKISQENEI GKKRELKEGS LWSTKEEISD DSEMLPRKLL LTEFRSLVIE NSTSRNPSGI NDYGQLNNFK KFKKVTYPGA GKLPHIIGGS DLIPHHARKN TELEEWLRQE MEVQNQHAKE ESLADDLFRY NPYLKRRR //