SMC5_ARATH
ID SMC5_ARATH Reviewed; 1053 AA.
AC Q9LFS8; Q9FV56;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Structural maintenance of chromosomes protein 5;
DE AltName: Full=Protein EMBRYO DEFECTIVE 2782;
GN Name=SMC5; Synonyms=EMB2782; OrderedLocusNames=At5g15920;
GN ORFNames=F1N13.60;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-284.
RC STRAIN=cv. Columbia;
RX PubMed=10929106; DOI=10.1046/j.1365-313x.2000.00809.x;
RA Kleinow T., Bhalerao R., Breuer F., Umeda M., Salchert K., Koncz C.;
RT "Functional identification of an Arabidopsis Snf4 ortholog by screening for
RT heterologous multicopy suppressors of snf4 deficiency in yeast.";
RL Plant J. 23:115-122(2000).
RN [4]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=19737979; DOI=10.1105/tpc.108.060525;
RA Watanabe K., Pacher M., Dukowic S., Schubert V., Puchta H., Schubert I.;
RT "The STRUCTURAL MAINTENANCE OF CHROMOSOMES 5/6 complex promotes sister
RT chromatid alignment and homologous recombination after DNA damage in
RT Arabidopsis thaliana.";
RL Plant Cell 21:2688-2699(2009).
CC -!- FUNCTION: Core component of the SMC5-SMC6 complex that promotes sister
CC chromatid alignment after DNA damage and facilitates double-stranded
CC DNA breaks (DSBs) repair via homologous recombination between sister
CC chromatids. {ECO:0000269|PubMed:19737979}.
CC -!- SUBUNIT: Forms a heterodimer with SMC6A or SMC6B. The SMC5-SMC6 complex
CC is composed of the SMC5 and SMC6 heterodimer attached via their hinge
CC domain and from the non-SMC subunit NSE4A or NSE4B (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
CC Note=Associates with chromatin. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, rosette leaves and floral
CC buds. {ECO:0000269|PubMed:19737979}.
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 -!- DISRUPTION PHENOTYPE: Lethal when homozygous.
CC {ECO:0000269|PubMed:19737979}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC5 subfamily. {ECO:0000305}.
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DR EMBL; AL391145; CAC01791.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92224.1; -; Genomic_DNA.
DR EMBL; AF250342; AAG10148.1; -; mRNA.
DR PIR; T51375; T51375.
DR RefSeq; NP_197096.1; NM_121597.3.
DR AlphaFoldDB; Q9LFS8; -.
DR SMR; Q9LFS8; -.
DR BioGRID; 16725; 3.
DR STRING; 3702.AT5G15920.1; -.
DR PaxDb; Q9LFS8; -.
DR PRIDE; Q9LFS8; -.
DR ProteomicsDB; 228203; -.
DR EnsemblPlants; AT5G15920.1; AT5G15920.1; AT5G15920.
DR GeneID; 831449; -.
DR Gramene; AT5G15920.1; AT5G15920.1; AT5G15920.
DR KEGG; ath:AT5G15920; -.
DR Araport; AT5G15920; -.
DR TAIR; locus:2146107; AT5G15920.
DR eggNOG; KOG0979; Eukaryota.
DR HOGENOM; CLU_004969_1_0_1; -.
DR InParanoid; Q9LFS8; -.
DR OMA; SAEFFPG; -.
DR OrthoDB; 100993at2759; -.
DR PhylomeDB; Q9LFS8; -.
DR PRO; PR:Q9LFS8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LFS8; baseline and differential.
DR Genevisible; Q9LFS8; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0030915; C:Smc5-Smc6 complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:0007062; P:sister chromatid cohesion; IMP:TAIR.
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; Chromosome; Coiled coil; DNA damage; DNA recombination;
KW DNA repair; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..1053
FT /note="Structural maintenance of chromosomes protein 5"
FT /id="PRO_0000424411"
FT DOMAIN 23..991
FT /note="Zinc-hook"
FT REGION 432..616
FT /note="Flexible hinge"
FT COILED 182..431
FT /evidence="ECO:0000255"
FT COILED 617..798
FT /evidence="ECO:0000255"
FT BINDING 50..57
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1053 AA; 121441 MW; 9BA3BB80D07C2A0E CRC64;
MSERRAKRPK ISRGEDDFLP GNIIEIELHN FMTFNHLVCK PGSRLNLVIG PNGSGKSSLV
CAIALCLGGE PQLLGRATSV GAYVKRGEDS GYVKISLRGN TREENLTIFR KIDTRNKSEW
MFNGSTVSKK DIVEIIQKFN IQVNNLTQFL PQDRVCEFAK LTPVQLLEET EKAVGDPQLP
VHHRALVEKS RDLKQLERAV AKNGETLNQL KALVDEQEKD VERVRQRELF LTKVDSMKKK
LPWLKYDMKK AEYMDAKKRM KEAEKKLDEA AKNLNSMKEP IEKQKKEKAE TDSKCKKVKN
LMDANGRNRC HLLEKEDEAD ARVVATYKEL EELKKQEEHR QERILKATED LVAAERELQN
LPVYERPVAK LEELSSQVTE LHHSINGKKN QKEDNEKLLS QKRYTLRQCV DKLKDMENAN
NKLLKALANS GADRIFDAYQ WVQQNRHEFK REVYGPVLVE VNVPNRENAC FLEGHVSFYI
WKSFITQDPE DRDLLVKNLK RFDVPVLNYV GNSGNQKAPF HISDQMRSLG IHARLDQIFD
APDAVKEVLN SQFGLEDSYI GSKITDQRAE EVYKLGIKDF WTPDNHYRWS SSRYGGHSSA
SVDSVYQSRL LLCGVDVGEL EKLRSRKEEL EDSILFMEET HKSLQTEQRR LEEEAAKLHK
EREEIVNVSY LEKKKRRELE SRYQQRKTKL ESLEQEEDMD ASVAKLIDQA SRANADRYTY
AINLKKLLVE AVAHKWSYAE KHMASIELER KIRESEINIK QYEKTAQQLS LAVEYCKKEV
EGKQQRLATA KRDAESVATI TPELKKEFME MPTTVEELEA AIQDNLSQAN SILFINENIL
QEYEHRQSQI YTISTKLETD KRDLSICMKE IDSLKEKWLP TLRQLVGQIN ETFSHNFQEM
AVAGEVSLDE RDTDFDQYGI HIKVKFRESG QLQVLSSHHQ SGGERSVSTI LYLVSLQDLT
NCPFRVVDEI NQGMDPINER KMFQQLVRAA SQPNTPQCFL LTPKLLPELE YSEACSILNI
MNGPYIAEPS KVWSLGDSWG SLNRRRTEAS QCS
