SMC6_XENLA
ID SMC6_XENLA Reviewed; 1128 AA.
AC Q6P9I7; Q805A0;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, 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;
DE Short=xSMC6;
GN Name=smc6; Synonyms=smc6l1;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
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. Chromosome, telomere
CC {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 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; AB103031; BAC56937.1; -; mRNA.
DR EMBL; BC060747; AAH60747.1; -; mRNA.
DR RefSeq; NP_001083550.1; NM_001090081.1.
DR AlphaFoldDB; Q6P9I7; -.
DR SMR; Q6P9I7; -.
DR BioGRID; 100312; 2.
DR IntAct; Q6P9I7; 3.
DR DNASU; 398986; -.
DR GeneID; 398986; -.
DR KEGG; xla:398986; -.
DR CTD; 398986; -.
DR Xenbase; XB-GENE-6071335; smc6.1.L.
DR OrthoDB; 263113at2759; -.
DR Proteomes; UP000186698; Chromosome 5L.
DR Bgee; 398986; Expressed in testis and 19 other tissues.
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 InterPro; IPR036277; SMC_hinge_sf.
DR Pfam; PF02463; SMC_N; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF75553; SSF75553; 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..1128
FT /note="Structural maintenance of chromosomes protein 6"
FT /id="PRO_0000270959"
FT REGION 1..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 520..692
FT /note="Flexible hinge"
FT COILED 275..519
FT /evidence="ECO:0000255"
FT COILED 693..955
FT /evidence="ECO:0000255"
FT COMPBIAS 44..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 115..122
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 58
FT /note="T -> A (in Ref. 1; BAC56937)"
FT /evidence="ECO:0000305"
FT CONFLICT 62
FT /note="Y -> H (in Ref. 1; BAC56937)"
FT /evidence="ECO:0000305"
FT CONFLICT 68
FT /note="C -> F (in Ref. 1; BAC56937)"
FT /evidence="ECO:0000305"
FT CONFLICT 755
FT /note="L -> H (in Ref. 1; BAC56937)"
FT /evidence="ECO:0000305"
FT CONFLICT 1023..1024
FT /note="KC -> RS (in Ref. 1; BAC56937)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1128 AA; 130513 MW; 126806396112F088 CRC64;
MGKRKDGSPI APSSQRKKQR QEVDDPYDEE DYGQAGPSVS NDYGQRKKQR KEADNSHTDS
DYENSVSCAS SQRVSASQSG TGDVGIIESI FLRNFMCHSM LGPFRFGPNV NFVIGNNGSG
KSAVLTALIV GLGGKAAITN RGSSIKGFVK EGQTFAEISI TLRNRGQDAY KPDVFGNSIT
VQQRLTTDGS RTYKLKSATG AVVSNKKEEL TAILDHFNIQ VDNPVSVLTQ EMSKHFLQSK
NESDKYKFFM KATQLEQMKE DYSYIMETKS RTHDQVENGG ERLRDLRQEC IQKEERFKSI
ASLGEMKEKL EDLKNKMAWA LVTESEKQIK PFIEQISTEE GRTVKYEQKI EECQGKVINA
EEKFRAKQEE LDKITQEAVA LKPQGIGLKE DVQKKRKSYN ESEVLYNRHR MELKRLERDA
EQLHKRIEEL KKSADNDSES EKMARQKEIN QIRERMKALH DKDITTNQQI HQFQQAIEKY
KEERARIGNE ERNIKQRLEQ HKRQLKELHE SKTDRLKRFG QNMPALLAAI DEADKLGRFR
KKPVGPLGAC IHLKDQELAL AVESCLKGLM FAFCCDNHQD ERMLQNIMSR EYPRGRRPQI
IVNEFIDHVY DVRQRATFHP DHPTVLTALE IDHPVVTNCL IDMRGIETIL IIKGKDEARE
IMQKRAPPRN CREAFTGEGD QVYTNRYYSS DSRRATLLSR DVEAEISHLE KELRNFGSQM
ATFQQRAQSV DKDIKENEGI LRQYHNSKKQ IQIDLRPLLE RISELENVEE QPSIDIATLE
GEAEENLNKI ELVKQEVELA KEKMGNLKSF LTTAEINYEE IKKKISSVAE VAEPVKEDLH
RVDQEVENCK RHRKHYEEKL KEHLDRIQKR KEEVAAKEQE LEVKISQAKC ICPERIEVSR
TARSLDTEIN RLREKINSEE VLHGNREEII KQYHEAKERY QDVEGKVKHL KRFIKLLDEI
MAQRYKSYQQ FRRCLTFRCK IYFDSLLSQR AYSGKINFDH KNETLSITVQ PGEGNKAALS
DMKCLSGGER SFSTVCFILS LWSIAESPFR CLDEFDVYMD MVNRRISMDM MLSMADSQRF
RQFILLTPQN MSSLPSTSLV RILRMKDPER GQTTLPFQPL NQEAEDEE
