ID   SMC6_TAKRU              Reviewed;        1090 AA.
AC   Q802R8;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Structural maintenance of chromosomes protein 6;
DE            Short=SMC protein 6;
DE            Short=SMC-6;
GN   Name=smc6; Synonyms=smc6l1;
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=14660695; DOI=10.1093/molbev/msh023;
RA   Cobbe N., Heck M.M.S.;
RT   "The evolution of SMC proteins: phylogenetic analysis and structural
RT   implications.";
RL   Mol. Biol. Evol. 21:332-347(2004).
CC   -!- FUNCTION: Core component of the SMC5-SMC6 complex, a complex involved
CC       in repair of DNA double-strand breaks by homologous recombination. The
CC       complex may promote sister chromatid homologous recombination by
CC       recruiting the SMC1-SMC3 cohesin complex to double-strand breaks. The
CC       complex is required for telomere maintenance via recombination and
CC       mediates sumoylation of shelterin complex (telosome) components (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Forms a heterodimer with smc5. Component of the SMC5-SMC6
CC       complex which consists at least of smc5, smc6, nsmce2, nsmce1 and
CC       nsmce4a (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Chromosome {ECO:0000250}. Chromosome,
CC       telomere {ECO:0000250}. Note=Associates with chromatin. {ECO:0000250}.
CC   -!- DOMAIN: The flexible hinge domain, which separates the large
CC       intramolecular coiled coil regions, allows the heterotypic interaction
CC       with the corresponding domain of SMC5, forming a V-shaped heterodimer.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SMC family. SMC6 subfamily. {ECO:0000305}.
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DR   EMBL; AJ543330; CAD65851.1; -; mRNA.
DR   RefSeq; NP_001027868.1; NM_001032696.1.
DR   AlphaFoldDB; Q802R8; -.
DR   SMR; Q802R8; -.
DR   STRING; 31033.ENSTRUP00000038201; -.
DR   GeneID; 446077; -.
DR   KEGG; tru:446077; -.
DR   CTD; 79677; -.
DR   eggNOG; KOG0250; Eukaryota.
DR   InParanoid; Q802R8; -.
DR   OrthoDB; 263113at2759; -.
DR   Proteomes; UP000005226; Unplaced.
DR   GO; GO:0000781; C:chromosome, telomeric region; ISS:UniProtKB.
DR   GO; GO:0016605; C:PML body; ISS:UniProtKB.
DR   GO; GO:0030915; C:Smc5-Smc6 complex; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0090398; P:cellular senescence; ISS:UniProtKB.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0000722; P:telomere maintenance via recombination; ISS:UniProtKB.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR003395; RecF/RecN/SMC_N.
DR   Pfam; PF02463; SMC_N; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Chromosome; Coiled coil; DNA damage; DNA recombination;
KW   DNA repair; Nucleotide-binding; Nucleus; Reference proteome; Telomere.
FT   CHAIN           1..1090
FT                   /note="Structural maintenance of chromosomes protein 6"
FT                   /id="PRO_0000270958"
FT   REGION          1..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          480..667
FT                   /note="Flexible hinge"
FT   COILED          242..479
FT                   /evidence="ECO:0000255"
FT   COILED          668..858
FT                   /evidence="ECO:0000255"
FT   COILED          894..919
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..22
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         83..90
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1090 AA;  124809 MW;  E21DD7AC8A53C878 CRC64;
     MSKRKSISTH DKSTKRARPV EEEEDSEDAD DRDQDVERLS PQVLPSGDVS DVGIVKSITL
     NNFMCHANLG PFAFGSNVNF IVGKNGSGKS AILTGLIVAL GGNAQATNRG SSLKGFVKEG
     ESFAVVSITL NNIGKDAYKP EVYGQAIVID QKITREGIRT YKLKSQSGHI ISTKKEDLVT
     ILDYYNIQVN NPVTILTQEM SKYFLHSKGG AEKYKFFMKA TQLEQMKDDF VHIKSTKSVT
     VDKVEQHSEC LKDLKRDYLE KEDRYKSLAS VNEMYTKLEE LKKQMAWALV GEVEKEFEPM
     KEKLESDRCA TNKFNEKVDE WKKKVEVAEG KQKQSHEQLE EITQQVSELQ SKCTEFKTEV
     QRRNADLKSC EVTVHRHKAI LRDLEKDKAQ LSSKINDLSL SISQATGAES QARMERIAQI
     EAALEDLTHH TSTLGQQIEQ YQHSYRHAIE GQGKMKRELE GLQKSIDANR RQLQSMESSR
     SNRLQRFGDQ MPALLAAIDE AHKKGQFKHR PRGPLGYLIS LKDPELALSI EICLKNLVQA
     FTCDNYDDER VLKSLMTKVL QHGRRPAIIT SRFFPKVHDV SVRAVNHPDY PSVLQALEIE
     DPVVANCLID QRAIECILLI KNRTEARRVM QGRNPPQNCT SAFSVEGDQI FTNRSYTADQ
     TRANFLSKDV EEGIRHLKRE METQKVQAAH IQQQIRSTDK NISENQDLLR RTQTEQKTTE
     VKTMKLQLEL TDLKNVEEPQ SEDLAELKSA FENAEQEYKQ HKQLIDTAAE EADVKKVETK
     LTPLFTSLSC NILWVHCLFV LLQEELSKTD QEVMKCKHHE KHYEERRNAH LCSIKTLENN
     VASKEKELQE SIAKAKEICP EQLVVRRTAR SLDVEITRLK VKIATQREHQ GDREEIVREY
     HEALESYANK AQQIKNLNNF IKCLDRVMDQ RLYAYTVLRR FLSARCKYYF DSMLAQRGFT
     GNMTFDHKNE TLSISVQPGQ GNKADLNDMR CLSGGERSFS TVCFVLSLWP ITEAPFRCLD
     EFDVYMDMAN RRNTQRQSGL KMATSQKIRQ LIFLTPQSMS SLPECRRIHI VQLNDPVHGQ
     TQMEQEEEGP