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Protein

Structural maintenance of chromosomes protein 1

Gene

SMC1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -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.

Miscellaneous

Present with 5710 molecules/cell in log phase SD medium.1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi33 – 40ATPSequence analysis8

GO - Molecular functioni

  • AT DNA binding Source: SGD
  • ATPase activity Source: SGD
  • ATP binding Source: UniProtKB-KW
  • chromatin binding Source: InterPro
  • DNA secondary structure binding Source: SGD
  • double-stranded DNA binding Source: SGD
  • identical protein binding Source: IntAct
  • protein heterodimerization activity Source: InterPro

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • double-strand break repair Source: SGD
  • mitotic sister chromatid cohesion Source: SGD
  • mitotic sister chromatid segregation Source: SGD

Keywordsi

Biological processCell cycle, Cell division, Mitosis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-30448-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
Structural maintenance of chromosomes protein 1
Alternative name(s):
DA-box protein SMC1
Gene namesi
Name:SMC1
Synonyms:CHL10
Ordered Locus Names:YFL008W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VI

Organism-specific databases

EuPathDBiFungiDB:YFL008W
SGDiS000001886 SMC1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi173S → L in temperature-sensitive mutant SMC1-2. 1
Mutagenesisi458N → D in temperature-sensitive mutant SMC1-1. 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001190111 – 1225Structural maintenance of chromosomes protein 1Add BLAST1225

Proteomic databases

MaxQBiP32908
PaxDbiP32908
PRIDEiP32908

PTM databases

iPTMnetiP32908

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

Show more details

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • protein heterodimerization activity Source: InterPro

Protein-protein interaction databases

BioGridi31139, 358 interactors
ComplexPortaliCPX-1408 Nuclear meiotic cohesin complex
CPX-1867 Nuclear mitotic cohesin complex
DIPiDIP-2982N
IntActiP32908, 28 interactors
MINTiP32908
STRINGi4932.YFL008W

Structurei

Secondary structure

11225
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 11Combined sources8
Beta strandi17 – 22Combined sources6
Beta strandi27 – 32Combined sources6
Helixi39 – 49Combined sources11
Helixi63 – 65Combined sources3
Beta strandi91 – 100Combined sources10
Beta strandi103 – 112Combined sources10
Beta strandi117 – 121Combined sources5
Beta strandi124 – 126Combined sources3
Helixi128 – 137Combined sources10
Turni142 – 144Combined sources3
Helixi156 – 159Combined sources4
Helixi162 – 167Combined sources6
Helixi170 – 173Combined sources4
Turni175 – 178Combined sources4
Helixi179 – 188Combined sources10
Helixi240 – 259Combined sources20
Beta strandi269 – 272Combined sources4
Beta strandi274 – 279Combined sources6
Helixi280 – 282Combined sources3
Beta strandi287 – 290Combined sources4
Helixi298 – 300Combined sources3
Helixi304 – 319Combined sources16
Beta strandi325 – 331Combined sources7
Turni332 – 335Combined sources4
Helixi338 – 350Combined sources13
Beta strandi352 – 357Combined sources6
Helixi361 – 364Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1W1WX-ray2.90A/B/C/D1-214[»]
A/B/C/D1024-1225[»]
ProteinModelPortaliP32908
SMRiP32908
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP32908

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni490 – 678Flexible hingeAdd BLAST189

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili173 – 489Sequence analysisAdd BLAST317
Coiled coili679 – 1063Sequence analysisAdd BLAST385

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1057 – 1061Nuclear localization signalSequence analysis5

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1129 – 1164Ala/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 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.

Sequence similaritiesi

Belongs to the SMC family. SMC1 subfamily.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

GeneTreeiENSGT00580000081569
HOGENOMiHOG000195481
InParanoidiP32908
KOiK06636
OMAiFNFKSYK
OrthoDBiEOG092C0XGI

Family and domain databases

InterProiView protein in InterPro
IPR027417 P-loop_NTPase
IPR003395 RecF/RecN/SMC_N
IPR024704 SMC
IPR028468 Smc1
IPR010935 SMC_hinge
IPR036277 SMC_hinge_sf
PANTHERiPTHR18937:SF12 PTHR18937:SF12, 1 hit
PfamiView protein in Pfam
PF06470 SMC_hinge, 1 hit
PF02463 SMC_N, 1 hit
PIRSFiPIRSF005719 SMC, 1 hit
SMARTiView protein in SMART
SM00968 SMC_hinge, 1 hit
SUPFAMiSSF52540 SSF52540, 2 hits
SSF75553 SSF75553, 1 hit

Sequencei

Sequence statusi: Complete.

P32908-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGRLVGLELS NFKSYRGVTK VGFGESNFTS IIGPNGSGKS NMMDAISFVL
60 70 80 90 100
GVRSNHLRSN ILKDLIYRGV LNDENSDDYD NEGAASSNPQ SAYVKAFYQK
110 120 130 140 150
GNKLVELMRI ISRNGDTSYK IDGKTVSYKD YSIFLENENI LIKAKNFLVF
160 170 180 190 200
QGDVEQIAAQ SPVELSRMFE EVSGSIQYKK EYEELKEKIE KLSKSATESI
210 220 230 240 250
KNRRRIHGEL KTYKEGINKN EEYRKQLDKK NELQKFQALW QLYHLEQQKE
260 270 280 290 300
ELTDKLSALN SEISSLKGKI NNEMKSLQRS KSSFVKESAV ISKQKSKLDY
310 320 330 340 350
IFKDKEKLVS DLRLIKVPQQ AAGKRISHIE KRIESLQKDL QRQKTYVERF
360 370 380 390 400
ETQLKVVTRS KEAFEEEIKQ SARNYDKFKL NENDLKTYNC LHEKYLTEGG
410 420 430 440 450
SILEEKIAVL NNDKREIQEE LERFNKRADI SKRRITEELS ITGEKLDTQL
460 470 480 490 500
NDLRVSLNEK NALHTERLHE LKKLQSDIES ANNQEYDLNF KLRETLVKID
510 520 530 540 550
DLSANQRETM KERKLRENIA MLKRFFPGVK GLVHDLCHPK KEKYGLAVST
560 570 580 590 600
ILGKNFDSVI VENLTVAQEC IAFLKKQRAG TASFIPLDTI ETELPTLSLP
610 620 630 640 650
DSQDYILSIN AIDYEPEYEK AMQYVCGDSI ICNTLNIAKD LKWKKGIRGK
660 670 680 690 700
LVTIEGALIH KAGLMTGGIS GDANNRWDKE EYQSLMSLKD KLLIQIDELS
710 720 730 740 750
NGQRSNSIRA REVENSVSLL NSDIANLRTQ VTQQKRSLDE NRLEIKYHND
760 770 780 790 800
LIEKEIQPKI TELKKKLDDL ENTKDNLVKE KEALQNNIFK EFTSKIGFTI
810 820 830 840 850
KEYENHSGEL MRQQSKELQQ LQKQILTVEN KLQFETDRLS TTQRRYEKAQ
860 870 880 890 900
KDLENAQVEM KSLEEQEYAI EMKIGSIESK LEEHKNHLDE LQKKFVTKQS
910 920 930 940 950
ELNSSEDILE DMNSNLQVLK RERDGIKEDI EKFDLERVTA LKNCKISNIN
960 970 980 990 1000
IPISSETTID DLPISSTDNE AITISNSIDI NYKGLPKKYK ENNTDSARKE
1010 1020 1030 1040 1050
LEQKIHEVEE ILNELQPNAR ALERYDEAEG RFEVINNETE QLKAEEKKIL
1060 1070 1080 1090 1100
NQFLKIKKKR KELFEKTFDY VSDHLDAIYR ELTKNPNSNV ELAGGNASLT
1110 1120 1130 1140 1150
IEDEDEPFNA GIKYHATPPL KRFKDMEYLS GGEKTVAALA LLFAINSYQP
1160 1170 1180 1190 1200
SPFFVLDEVD AALDITNVQR IAAYIRRHRN PDLQFIVISL KNTMFEKSDA
1210 1220
LVGVYRQQQE NSSKIITLDL SNYAE
Length:1,225
Mass (Da):141,280
Last modified:October 1, 1993 - v1
Checksum:iB504017AA0ECCA8C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L00602 Unassigned DNA Translation: AAA16595.1
D50617 Genomic DNA Translation: BAA09230.1
BK006940 Genomic DNA Translation: DAA12432.1
PIRiA49464
RefSeqiNP_116647.1, NM_001179958.1

Genome annotation databases

EnsemblFungiiBAA09230; BAA09230; BAA09230
YFL008W; YFL008W; YFL008W
GeneIDi850540
KEGGisce:YFL008W

Similar proteinsi

Entry informationi

Entry nameiSMC1_YEAST
AccessioniPrimary (citable) accession number: P32908
Secondary accession number(s): D6VTM2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: June 20, 2018
This is version 176 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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

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