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Protein

Structural maintenance of chromosomes protein 3

Gene

SMC3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in chromosome cohesion during cell cycle and in DNA repair. Central component of cohesin complex. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi32 – 39ATPSequence analysis8

GO - Molecular functioni

  • ATPase activity Source: SGD
  • ATP binding Source: UniProtKB-KW
  • chromatin binding Source: InterPro

GO - Biological processi

  • ascospore formation Source: SGD
  • cell division Source: UniProtKB-KW
  • meiotic sister chromatid cohesion Source: SGD
  • mitotic sister chromatid cohesion Source: SGD
  • reciprocal meiotic recombination Source: SGD
  • replication-born double-strand break repair via sister chromatid exchange Source: SGD
  • synaptonemal complex assembly Source: SGD
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-31532-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Structural maintenance of chromosomes protein 3
Alternative name(s):
DA-box protein SMC3
Gene namesi
Name:SMC3
Ordered Locus Names:YJL074C
ORF Names:J1049
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome X

Organism-specific databases

EuPathDBiFungiDB:YJL074C.
SGDiS000003610. SMC3.

Subcellular locationi

  • Nucleus
  • Chromosome

  • Note: Associates with chromatin. Before prophase it is scattered along chromosome arms. At anaphase, the MCD1 subunit of the cohesin complex is cleaved, leading to the dissociation of the complex from chromosomes, allowing chromosome separation.

GO - Cellular componenti

  • cohesin core heterodimer Source: InterPro
  • nuclear mitotic cohesin complex Source: SGD
  • nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001190151 – 1230Structural maintenance of chromosomes protein 3Add BLAST1230

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei112N6-acetyllysine1 Publication1
Modified residuei113N6-acetyllysine1 Publication1

Post-translational modificationi

Acetylation at Lys-112 and Lys-113 by ECO1 is important for genome stability and S phase sister chromatid cohesion.1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP47037.
PRIDEiP47037.

Interactioni

Subunit structurei

Cohesin complexes are composed of the SMC1 and SMC3 heterodimer attached via their hinge domain, MCD1/SCC1 which link them, and IRR1/SCC3, which interacts with MCD1. The cohesin complex also interacts with SCC2, which is required for its association with chromosomes.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself5EBI-17423,EBI-17423
IRR1P405412EBI-17423,EBI-16667
MCD1Q1215813EBI-17423,EBI-16655
RAD61Q993599EBI-17423,EBI-2082336
SMC1P3290820EBI-17423,EBI-17402

Protein-protein interaction databases

BioGridi33681. 278 interactors.
DIPiDIP-2991N.
IntActiP47037. 55 interactors.
MINTiMINT-435389.

Structurei

Secondary structure

11230
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 11Combined sources6
Beta strandi14 – 17Combined sources4
Beta strandi25 – 33Combined sources9
Helixi38 – 49Combined sources12
Beta strandi53 – 55Combined sources3
Helixi58 – 64Combined sources7
Beta strandi68 – 72Combined sources5
Beta strandi77 – 80Combined sources4
Turni111 – 113Combined sources3
Turni118 – 121Combined sources4
Helixi125 – 133Combined sources9
Beta strandi142 – 146Combined sources5
Helixi152 – 154Combined sources3
Helixi159 – 167Combined sources9
Helixi172 – 237Combined sources66
Helixi239 – 244Combined sources6
Helixi976 – 980Combined sources5
Helixi982 – 988Combined sources7
Helixi998 – 1059Combined sources62
Beta strandi1065 – 1069Combined sources5
Beta strandi1109 – 1113Combined sources5
Beta strandi1121 – 1123Combined sources3
Helixi1128 – 1143Combined sources16
Beta strandi1149 – 1153Combined sources5
Turni1154 – 1159Combined sources6
Helixi1162 – 1176Combined sources15
Beta strandi1179 – 1184Combined sources6
Helixi1188 – 1190Combined sources3
Turni1191 – 1193Combined sources3
Beta strandi1198 – 1203Combined sources6
Beta strandi1206 – 1210Combined sources5
Helixi1214 – 1221Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4UX3X-ray3.30A2-261[»]
A970-1230[»]
ProteinModelPortaliP47037.
SMRiP47037.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni483 – 684Flexible hingeAdd BLAST202

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili172 – 482Sequence analysisAdd BLAST311
Coiled coili685 – 1041Sequence analysisAdd BLAST357

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1126 – 1161Ala/Asp-rich (DA-box)Add BLAST36

Domaini

The flexible hinge domain, which separates the large intramolecular coiled coil regions, allows the heterotypic interaction with the corresponding domain of SMC1, forming a V-shaped heterodimer. The two heads of the heterodimer are then connected by different ends of the cleavable MCD1 protein, forming a ring structure (By similarity).By similarity

Sequence similaritiesi

Belongs to the SMC family. SMC3 subfamily.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

GeneTreeiENSGT00580000081628.
HOGENOMiHOG000166512.
InParanoidiP47037.
KOiK06669.
OMAiRIVANDC.
OrthoDBiEOG092C0XGI.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR027417. P-loop_NTPase.
IPR003395. RecF/RecN/SMC_N.
IPR024704. SMC.
IPR029685. SMC3.
IPR010935. SMC_hinge.
[Graphical view]
PANTHERiPTHR18937:SF8. PTHR18937:SF8. 1 hit.
PfamiPF06470. SMC_hinge. 1 hit.
PF02463. SMC_N. 1 hit.
[Graphical view]
PIRSFiPIRSF005719. SMC. 1 hit.
SMARTiSM00968. SMC_hinge. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
SSF75553. SSF75553. 1 hit.

Sequencei

Sequence statusi: Complete.

P47037-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYIKRVIIKG FKTYRNETII DNFSPHQNVI IGSNGSGKSN FFAAIRFVLS
60 70 80 90 100
DDYSNLKREE RQGLIHQGSG GSVMSASVEI VFHDPDHSMI LPSGVLSRGD
110 120 130 140 150
DEVTIRRTVG LKKDDYQLND RNVTKGDIVR MLETAGFSMN NPYNIVPQGK
160 170 180 190 200
IVALTNAKDK ERLQLLEDVV GAKSFEVKLK ASLKKMEETE QKKIQINKEM
210 220 230 240 250
GELNSKLSEM EQERKELEKY NELERNRKIY QFTLYDRELN EVINQMERLD
260 270 280 290 300
GDYNNTVYSS EQYIQELDKR EDMIDQVSKK LSSIEASLKI KNATDLQQAK
310 320 330 340 350
LRESEISQKL TNVNVKIKDV QQQIESNEEQ RNLDSATLKE IKSIIEQRKQ
360 370 380 390 400
KLSKILPRYQ ELTKEEAMYK LQLASLQQKQ RDLILKKGEY ARFKSKDERD
410 420 430 440 450
TWIHSEIEEL KSSIQNLNEL ESQLQMDRTS LRKQYSAIDE EIEELIDSIN
460 470 480 490 500
GPDTKGQLED FDSELIHLKQ KLSESLDTRK ELWRKEQKLQ TVLETLLSDV
510 520 530 540 550
NQNQRNVNET MSRSLANGII NVKEITEKLK ISPESVFGTL GELIKVNDKY
560 570 580 590 600
KTCAEVIGGN SLFHIVVDTE ETATLIMNEL YRMKGGRVTF IPLNRLSLDS
610 620 630 640 650
DVKFPSNTTT QIQFTPLIKK IKYEPRFEKA VKHVFGKTIV VKDLGQGLKL
660 670 680 690 700
AKKHKLNAIT LDGDRADKRG VLTGGYLDQH KRTRLESLKN LNESRSQHKK
710 720 730 740 750
ILEELDFVRN ELNDIDTKID QVNGNIRKVS NDRESVLTNI EVYRTSLNTK
760 770 780 790 800
KNEKLILEES LNAIILKLEK LNTNRTFAQE KLNTFENDLL QEFDSELSKE
810 820 830 840 850
EKERLESLTK EISAAHNKLN ITSDALEGIT TTIDSLNAEL ESKLIPQEND
860 870 880 890 900
LESKMSEVGD AFIFGLQDEL KELQLEKESV EKQHENAVLE LGTVQREIES
910 920 930 940 950
LIAEETNNKK LLEKANNQQR LLLKKLDNFQ KSVEKTMIKK TTLVTRREEL
960 970 980 990 1000
QQRIREIGLL PEDALVNDFS DITSDQLLQR LNDMNTEISG LKNVNKRAFE
1010 1020 1030 1040 1050
NFKKFNERRK DLAERASELD ESKDSIQDLI VKLKQQKVNA VDSTFQKVSE
1060 1070 1080 1090 1100
NFEAVFERLV PRGTAKLIIH RKNDNANDHD ESIDVDMDAE SNESQNGKDS
1110 1120 1130 1140 1150
EIMYTGVSIS VSFNSKQNEQ LHVEQLSGGQ KTVCAIALIL AIQMVDPASF
1160 1170 1180 1190 1200
YLFDEIDAAL DKQYRTAVAT LLKELSKNAQ FICTTFRTDM LQVADKFFRV
1210 1220 1230
KYENKISTVI EVNREEAIGF IRGSNKFAEV
Length:1,230
Mass (Da):141,336
Last modified:February 1, 1996 - v1
Checksum:iB152D88F7780341F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y14278 Genomic DNA. Translation: CAA74655.1.
Z49349 Genomic DNA. Translation: CAA89366.1.
X88851 Genomic DNA. Translation: CAA61313.1.
BK006943 Genomic DNA. Translation: DAA08725.1.
PIRiS56850.
RefSeqiNP_012461.1. NM_001181507.1.

Genome annotation databases

EnsemblFungiiYJL074C; YJL074C; YJL074C.
GeneIDi853371.
KEGGisce:YJL074C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y14278 Genomic DNA. Translation: CAA74655.1.
Z49349 Genomic DNA. Translation: CAA89366.1.
X88851 Genomic DNA. Translation: CAA61313.1.
BK006943 Genomic DNA. Translation: DAA08725.1.
PIRiS56850.
RefSeqiNP_012461.1. NM_001181507.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4UX3X-ray3.30A2-261[»]
A970-1230[»]
ProteinModelPortaliP47037.
SMRiP47037.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33681. 278 interactors.
DIPiDIP-2991N.
IntActiP47037. 55 interactors.
MINTiMINT-435389.

Proteomic databases

MaxQBiP47037.
PRIDEiP47037.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYJL074C; YJL074C; YJL074C.
GeneIDi853371.
KEGGisce:YJL074C.

Organism-specific databases

EuPathDBiFungiDB:YJL074C.
SGDiS000003610. SMC3.

Phylogenomic databases

GeneTreeiENSGT00580000081628.
HOGENOMiHOG000166512.
InParanoidiP47037.
KOiK06669.
OMAiRIVANDC.
OrthoDBiEOG092C0XGI.

Enzyme and pathway databases

BioCyciYEAST:G3O-31532-MONOMER.

Miscellaneous databases

PROiP47037.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR027417. P-loop_NTPase.
IPR003395. RecF/RecN/SMC_N.
IPR024704. SMC.
IPR029685. SMC3.
IPR010935. SMC_hinge.
[Graphical view]
PANTHERiPTHR18937:SF8. PTHR18937:SF8. 1 hit.
PfamiPF06470. SMC_hinge. 1 hit.
PF02463. SMC_N. 1 hit.
[Graphical view]
PIRSFiPIRSF005719. SMC. 1 hit.
SMARTiSM00968. SMC_hinge. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
SSF75553. SSF75553. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiSMC3_YEAST
AccessioniPrimary (citable) accession number: P47037
Secondary accession number(s): D6VWA9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: November 2, 2016
This is version 155 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 2660 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome X
    Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.