SMC5_XENLA
ID SMC5_XENLA Reviewed; 1065 AA.
AC Q805A1;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Structural maintenance of chromosomes protein 5;
DE Short=SMC protein 5;
DE Short=SMC-5;
GN Name=smc5; Synonyms=smc5l1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RX PubMed=17094943; DOI=10.1016/j.bbrc.2006.10.133;
RA Tsuyama T., Inou K., Seki M., Seki T., Kumata Y., Kobayashi T., Kimura K.,
RA Hanaoka F., Enomoto T., Tada S.;
RT "Chromatin loading of Smc5/6 is induced by DNA replication but not by DNA
RT double-strand breaks.";
RL Biochem. Biophys. Res. Commun. 351:935-939(2006).
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 -!- DEVELOPMENTAL STAGE: Loaded onto chromatin during DNA replication in a
CC manner dependent on the initiation of DNA synthesis, and it dissociated
CC from chromatin during mitosis. Chromatin loading is not induced by DNA
CC double-strand breaks. {ECO:0000269|PubMed:17094943}.
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; AB103030; BAC56936.1; -; mRNA.
DR RefSeq; NP_001082472.1; NM_001089003.1.
DR BioGRID; 99824; 1.
DR IntAct; Q805A1; 1.
DR PRIDE; Q805A1; -.
DR GeneID; 398492; -.
DR KEGG; xla:398492; -.
DR CTD; 398492; -.
DR Xenbase; XB-GENE-953075; smc5.S.
DR OrthoDB; 100993at2759; -.
DR Proteomes; UP000186698; Chromosome 1S.
DR Bgee; 398492; Expressed in ovary and 19 other tissues.
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; IPR041685; AAA_15.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR027131; SMC5.
DR PANTHER; PTHR45916; PTHR45916; 1.
DR Pfam; PF13175; AAA_15; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
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..1065
FT /note="Structural maintenance of chromosomes protein 5"
FT /id="PRO_0000270955"
FT REGION 438..628
FT /note="Flexible hinge"
FT COILED 210..439
FT /evidence="ECO:0000255"
FT COILED 629..797
FT /evidence="ECO:0000255"
FT COILED 855..893
FT /evidence="ECO:0000255"
FT BINDING 58..65
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1065 AA; 124938 MW; 2663E7B1FF4265C9 CRC64;
MESAPVKRKA XGTKLLLGRQ EHHRNLVEGS IVRIKMENFL TYDQCEVFPG PYLNMIVGAN
GTGKSSIVCA ICLGLAGKTA FIGRADKVGF YVKRGCQKGF VELELYKTSG NVIIKREIQV
ANNQSVWYIN HKSATLKTVE EQVPALNIQV GNLCPIPATR TKFGEFANLS KIETSKKQLK
NHVGTPRNVQ VPLRIEELHG EKKELAGACK SKAEFLEKLN QRNERYKQDV ERYYQQKRHQ
DKIDMLERKR PWVEYENVRQ QYEDVKKSCG NFKDELKKLQ GLQAPLNQKI QQIEKRQRII
DEKIKDKAIE IKETSKNCKQ KQDELEQKDK QIEEVQQSLR VKRDAEQERQ KKIGNIRKMI
EDWEKELSAM TNQENIQPEM DSINTDFRRI QDDKANIESE MTDLRMEKDN LEREKKEKAN
RIKQFDNLMN LKEEKLKRMY SDTYNAVVWL KENKDRFKNR VCQPMMLEIN MKDQRHAKYV
ENHIPMNDMK AFVFESQEDM QVFLKEVRDK QNLRVNTVCA PQEPYAEQRP KRPITDLKQY
GFFSYLRELF DAPYPVMNYL CYQYKVHEVP VGTEQTRSMI EKVIKETDLR QMYTAEEKYV
TKKSVYSQKL ISSNVSLKGA QFLTVTVDAE ERQQVVDQLK EIERKCSTIE TSMEQLAERQ
RSLDRRDNEL RLRKKTILEM KTKKRQLEQK ISTKYDSLNR LEQDNLNLEE VQQQANNRIK
NLNVQKAKLV KDLLELMKEC TSLSIEKVEL ALQSTAISSE KNKIESDYKS ATSQLRELKN
QYDGIEAKKL HLLENCKGLL RKARQACNLG PNQAVPQDFQ TAFQSLPESL DEIDAMLNEE
RSRASCFTGL TASVVDDYNK RTKEIQEVTE ELNRKKLELE DYRKNISQVK EKWLNPLKQL
IEKINDQFSS FFSSMQCVGE VDLHTEKEEE YDKYGIRIRV KFRSSTQLHE LTPHHQSGGE
RSVSTMLYLM ALQELNRCPF RVVDEINQGM DPVNERRVFE MVVKTACKEN TSQYFFITPK
LLQNLTYAEK MTVLFVYNGP FMLEPTKWNL KAFHRRRRRV AAVDQ