Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P32908 (SMC1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Structural maintenance of chromosomes protein 1
Alternative name(s):
DA-box protein SMC1
Gene names
Name:SMC1
Synonyms:CHL10
Ordered Locus Names:YFL008W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1225 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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. Ref.4 Ref.5

Subcellular location

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.

Domain

The flexible hinge domain, which separates the large intramolecular coiled coil regions, allows the heterotypic interaction with the corresponding domain of SMC3, 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.

Miscellaneous

Present with 5710 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the SMC family. SMC1 subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12251225Structural maintenance of chromosomes protein 1
PRO_0000119011

Regions

Nucleotide binding33 – 408ATP Potential
Region490 – 678189Flexible hinge
Coiled coil173 – 489317 Potential
Coiled coil679 – 1063385 Potential
Motif1057 – 10615Nuclear localization signal Potential
Compositional bias1129 – 116436Ala/Asp-rich (DA-box)

Experimental info

Mutagenesis1731S → L in temperature-sensitive mutant SMC1-2.
Mutagenesis4581N → D in temperature-sensitive mutant SMC1-1.

Secondary structure

................................................... 1225
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P32908 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: B504017AA0ECCA8C

FASTA1,225141,280
        10         20         30         40         50         60 
MGRLVGLELS NFKSYRGVTK VGFGESNFTS IIGPNGSGKS NMMDAISFVL GVRSNHLRSN 

        70         80         90        100        110        120 
ILKDLIYRGV LNDENSDDYD NEGAASSNPQ SAYVKAFYQK GNKLVELMRI ISRNGDTSYK 

       130        140        150        160        170        180 
IDGKTVSYKD YSIFLENENI LIKAKNFLVF QGDVEQIAAQ SPVELSRMFE EVSGSIQYKK 

       190        200        210        220        230        240 
EYEELKEKIE KLSKSATESI KNRRRIHGEL KTYKEGINKN EEYRKQLDKK NELQKFQALW 

       250        260        270        280        290        300 
QLYHLEQQKE ELTDKLSALN SEISSLKGKI NNEMKSLQRS KSSFVKESAV ISKQKSKLDY 

       310        320        330        340        350        360 
IFKDKEKLVS DLRLIKVPQQ AAGKRISHIE KRIESLQKDL QRQKTYVERF ETQLKVVTRS 

       370        380        390        400        410        420 
KEAFEEEIKQ SARNYDKFKL NENDLKTYNC LHEKYLTEGG SILEEKIAVL NNDKREIQEE 

       430        440        450        460        470        480 
LERFNKRADI SKRRITEELS ITGEKLDTQL NDLRVSLNEK NALHTERLHE LKKLQSDIES 

       490        500        510        520        530        540 
ANNQEYDLNF KLRETLVKID DLSANQRETM KERKLRENIA MLKRFFPGVK GLVHDLCHPK 

       550        560        570        580        590        600 
KEKYGLAVST ILGKNFDSVI VENLTVAQEC IAFLKKQRAG TASFIPLDTI ETELPTLSLP 

       610        620        630        640        650        660 
DSQDYILSIN AIDYEPEYEK AMQYVCGDSI ICNTLNIAKD LKWKKGIRGK LVTIEGALIH 

       670        680        690        700        710        720 
KAGLMTGGIS GDANNRWDKE EYQSLMSLKD KLLIQIDELS NGQRSNSIRA REVENSVSLL 

       730        740        750        760        770        780 
NSDIANLRTQ VTQQKRSLDE NRLEIKYHND LIEKEIQPKI TELKKKLDDL ENTKDNLVKE 

       790        800        810        820        830        840 
KEALQNNIFK EFTSKIGFTI KEYENHSGEL MRQQSKELQQ LQKQILTVEN KLQFETDRLS 

       850        860        870        880        890        900 
TTQRRYEKAQ KDLENAQVEM KSLEEQEYAI EMKIGSIESK LEEHKNHLDE LQKKFVTKQS 

       910        920        930        940        950        960 
ELNSSEDILE DMNSNLQVLK RERDGIKEDI EKFDLERVTA LKNCKISNIN IPISSETTID 

       970        980        990       1000       1010       1020 
DLPISSTDNE AITISNSIDI NYKGLPKKYK ENNTDSARKE LEQKIHEVEE ILNELQPNAR 

      1030       1040       1050       1060       1070       1080 
ALERYDEAEG RFEVINNETE QLKAEEKKIL NQFLKIKKKR KELFEKTFDY VSDHLDAIYR 

      1090       1100       1110       1120       1130       1140 
ELTKNPNSNV ELAGGNASLT IEDEDEPFNA GIKYHATPPL KRFKDMEYLS GGEKTVAALA 

      1150       1160       1170       1180       1190       1200 
LLFAINSYQP SPFFVLDEVD AALDITNVQR IAAYIRRHRN PDLQFIVISL KNTMFEKSDA 

      1210       1220 
LVGVYRQQQE NSSKIITLDL SNYAE 

« Hide

References

« Hide 'large scale' references
[1]"SMC1: an essential yeast gene encoding a putative head-rod-tail protein is required for nuclear division and defines a new ubiquitous protein family."
Strunnikov A.V., Larionov V.L., Koshland D.
J. Cell Biol. 123:1635-1648(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE, MUTANTS SMC1-1 AND SMC1-2.
[2]"Analysis of the nucleotide sequence of chromosome VI from Saccharomyces cerevisiae."
Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S., Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H., Eki T.
Nat. Genet. 10:261-268(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Yeast cohesin complex requires a conserved protein, Eco1p(Ctf7), to establish cohesion between sister chromatids during DNA replication."
Toth A., Ciosk R., Uhlmann F., Galova M., Schleiffer A., Nasmyth K.
Genes Dev. 13:320-333(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COHESIN COMPLEX WITH SMC3; IRR1 AND MCD1, INTERACTION OF THE COHESIN COMPLEX WITH SCC2.
[5]"Molecular architecture of SMC proteins and the yeast cohesin complex."
Haering C.H., Loewe J., Hochwagen A., Nasmyth K.
Mol. Cell 9:773-788(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COHESIN COMPLEX WITH SMC3; MCD1 AND IRR1, STRUCTURE.
[6]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L00602 Unassigned DNA. Translation: AAA16595.1.
D50617 Genomic DNA. Translation: BAA09230.1.
BK006940 Genomic DNA. Translation: DAA12432.1.
PIRA49464.
RefSeqNP_116647.1. NM_001179958.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1W1WX-ray2.90A/B/C/D1-1225[»]
ProteinModelPortalP32908.
SMRP32908. Positions 2-205, 1048-1223.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31139. 159 interactions.
DIPDIP-2982N.
IntActP32908. 26 interactions.
MINTMINT-434606.
STRING4932.YFL008W.

Proteomic databases

PaxDbP32908.
PeptideAtlasP32908.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYFL008W; YFL008W; YFL008W.
GeneID850540.
KEGGsce:YFL008W.

Organism-specific databases

CYGDYFL008w.
SGDS000001886. SMC1.

Phylogenomic databases

eggNOGCOG1196.
GeneTreeENSGT00580000081569.
HOGENOMHOG000195481.
KOK06636.
OMAFKSYRGH.
OrthoDBEOG7M0P0T.

Enzyme and pathway databases

BioCycYEAST:G3O-30448-MONOMER.

Gene expression databases

GenevestigatorP32908.

Family and domain databases

Gene3D3.40.50.300. 5 hits.
InterProIPR027417. P-loop_NTPase.
IPR003395. RecF/RecN/SMC_N.
IPR024704. SMC.
IPR028468. Smc1.
IPR010935. SMC_hinge.
[Graphical view]
PANTHERPTHR18937:SF12. PTHR18937:SF12. 1 hit.
PfamPF06470. SMC_hinge. 1 hit.
PF02463. SMC_N. 1 hit.
[Graphical view]
PIRSFPIRSF005719. SMC. 1 hit.
SMARTSM00968. SMC_hinge. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 2 hits.
SSF75553. SSF75553. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP32908.
NextBio966301.
PROP32908.

Entry information

Entry nameSMC1_YEAST
AccessionPrimary (citable) accession number: P32908
Secondary accession number(s): D6VTM2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: April 16, 2014
This is version 136 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome VI

Yeast (Saccharomyces cerevisiae) chromosome VI: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references