SMC5_TAKRU
ID SMC5_TAKRU Reviewed; 1092 AA.
AC Q802R9;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Structural maintenance of chromosomes protein 5;
DE Short=SMC protein 5;
DE Short=SMC-5;
GN Name=smc5; Synonyms=smc5l1;
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.
CC Required for sister chromatid cohesion during prometaphase and mitotic
CC progression; the function seems to be independent of SMC6 (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Forms a heterodimer with smc6. 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 SMC6, forming a V-shaped heterodimer.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC5 subfamily. {ECO:0000305}.
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DR EMBL; AJ543329; CAD65850.1; -; mRNA.
DR RefSeq; NP_001027801.1; NM_001032629.1.
DR AlphaFoldDB; Q802R9; -.
DR SMR; Q802R9; -.
DR STRING; 31033.ENSTRUP00000041402; -.
DR PRIDE; Q802R9; -.
DR Ensembl; ENSTRUT00000041546; ENSTRUP00000041402; ENSTRUG00000016193.
DR GeneID; 445963; -.
DR KEGG; tru:445963; -.
DR CTD; 23137; -.
DR eggNOG; KOG0979; Eukaryota.
DR GeneTree; ENSGT00550000074816; -.
DR InParanoid; Q802R9; -.
DR OrthoDB; 100993at2759; -.
DR Proteomes; UP000005226; Chromosome 3.
DR GO; GO:0000781; C:chromosome, telomeric region; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; 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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0090398; P:cellular senescence; ISS:UniProtKB.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; ISS:UniProtKB.
DR GO; GO:0034184; P:positive regulation of maintenance of mitotic sister chromatid cohesion; ISS:UniProtKB.
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 InterPro; IPR027131; SMC5.
DR PANTHER; PTHR45916; PTHR45916; 1.
DR Pfam; PF02463; SMC_N; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell cycle; Cell division; Chromosome; Coiled coil;
KW DNA damage; DNA recombination; DNA repair; Mitosis; Nucleotide-binding;
KW Nucleus; Reference proteome; Telomere.
FT CHAIN 1..1092
FT /note="Structural maintenance of chromosomes protein 5"
FT /id="PRO_0000270954"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..635
FT /note="Flexible hinge"
FT COILED 146..449
FT /evidence="ECO:0000255"
FT COILED 636..806
FT /evidence="ECO:0000255"
FT COILED 878..921
FT /evidence="ECO:0000255"
FT BINDING 71..78
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1092 AA; 127653 MW; 2F02EA5DB29FCB49 CRC64;
MAEPEKKRRI SRVNSSQTSS NIGKILSGHR PCGAEVEGRM DGSILRITMR NFLTYDYTEV
YPGPNLNMIV GANGTGKSSI VCAICLGLAG KTAVLGRGDK VGLYVKRGCQ KGSIEIELYK
HGGNLVITRE IHVENNQSHW MINGKQRNQK AVEEEVKNLC IQVSNLCQFL PQEKVGEFAK
MSKTELLEAT EKSVGPPEMF EFHCELKNFR SKERELENTV TEKTKYIEKA KQRNERNKHD
VNRYYEKKRH LDMIELLEKK KPWVEYESTR KELESVKRER EEAKRNLSAL RHSQAPMIRK
IKEIEDRLQP FDDQIKSQTA AIKDAALKCK QKQDQLDRKQ KEIEDINQAF KLKEMEEDDH
QKRISNTRRI IEDLRTELAK VEDQPDVTPR INDVNSELRR NQIERARIDG EKCELCREKD
NAFAQCRSLQ KKLNDMNNLM KVKEEKLRGR HRDTHAALQW LRQNRNRFRG NVYEPMLLEI
NVKDHRFAKY VENHISFQDL RAFVFQRKED MEIFMSEVRD KMNLKVNSIS APEQSRSKAQ
PSQNIEDLRR FGFFTYLREM FDAPDEVMSY LCQQYNVHNV PVGTEQTKTM IRQVIEELNL
RVLFTLDERY MLKRSVYSKM ISTINSPVNP SQYLSIAVDA EEKRQLEQEL NACELRFREI
DERLKALQRE TAVLDRRDNE LLAEKKKLSE LKGKKRQLEQ KISTKQDSLR QMEQNVTDLK
KIEEETKEKV SAVNSQKVTI VKAFIASIKL KATLTMEKVY LSLEMMGLSA EKTKLEHDFR
EGASLLRSMD QRCSQLEQRK VQLTEQGKGQ MKRAKSICNM QPNDSLSEEL RNVRVYVIPP
YLCVPSPLMA FAKLPDTPDD IDSMLNEERS RSECFTGLSE NVVDEYNRSD QEIKELENEL
EEKKNALESY RQNISEAKER WLNPLKQLVE QINEKFTAFF RSMNCAGEVD LHSEKEEDYD
KYGIRIRVKF HSNTQLHELT PFHQSGGERS VSTMLYLMSL QELNRCPFRV VDEINQGMDP
INERRVFDIV VGTACKERTS QYFFITPKLL QNLKYAEEMT VLCVHNGAYM LPPNQWDDKA
FLRRCLQRKA KA
