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Protein

Structural maintenance of chromosomes protein 3

Gene

psm3

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission 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.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi32 – 398ATPCurated

GO - Molecular functioni

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • DNA repair Source: InterPro
  • mitotic sister chromatid cohesion Source: UniProtKB
  • positive regulation of maintenance of mitotic sister chromatid cohesion, centromeric Source: PomBase
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-SPO-2500257. Resolution of Sister Chromatid Cohesion.

Names & Taxonomyi

Protein namesi
Recommended name:
Structural maintenance of chromosomes protein 3
Alternative name(s):
Cohesin complex Psm3 subunit
Gene namesi
Name:psm3
Synonyms:smc3
ORF Names:SPAC10F6.09c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC10F6.09c.
PomBaseiSPAC10F6.09c. psm3.

Subcellular locationi

GO - Cellular componenti

  • chromosome Source: UniProtKB
  • cohesin complex Source: UniProtKB
  • cohesin core heterodimer Source: InterPro
  • condensed nuclear chromosome Source: PomBase
  • cytosol Source: PomBase
  • nuclear chromatin Source: PomBase
  • nuclear mitotic cohesin complex Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11941194Structural maintenance of chromosomes protein 3PRO_0000119014Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei105 – 1051N6-acetyllysineBy similarity
Modified residuei106 – 1061N6-acetyllysineBy similarity

Post-translational modificationi

Acetylation at Lys-105 and Lys-106 by ECO1 is important for genome stability and S phase sister chromatid cohesion.By similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiO42649.

Interactioni

Subunit structurei

Cohesin complexes are composed of the psm1/smc1 and psm3/smc3 heterodimer attached via their hinge domain, rad21/scc1 which link them, and psc3/scc3, which interacts with rad21.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
psm1O943833EBI-1151879,EBI-1151900

Protein-protein interaction databases

BioGridi279448. 5 interactions.
DIPiDIP-35366N.
IntActiO42649. 2 interactions.
MINTiMINT-4673146.

Structurei

3D structure databases

ProteinModelPortaliO42649.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni498 – 667170Flexible hingeAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili176 – 497322Sequence analysisAdd
BLAST
Coiled coili668 – 908241Sequence analysisAdd
BLAST
Coiled coili970 – 100637Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1097 – 113236Ala/Asp-rich (DA-box)Add
BLAST

Domaini

The flexible hinge domain, which separates the large intramolecular coiled coil regions, allows the heterotypic interaction with the corresponding domain of psm1, forming a V-shaped heterodimer. The two heads of the heterodimer are then connected by different ends of the cleavable rad21 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

HOGENOMiHOG000166512.
InParanoidiO42649.
KOiK06669.
OMAiQKANRID.
OrthoDBiEOG7M0P0T.
PhylomeDBiO42649.

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. 2 hits.
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.

O42649-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYITKIVIQG FKSYKDYTVI EPLSPHHNVI VGRNGSGKSN FFAAIRFVLS
60 70 80 90 100
DAYTHLSREE RQALLHEGPG ATVMSAYVEV TFANADNRFP TGKSEVVLRR
110 120 130 140 150
TIGLKKDEYS LDKKTVSKTE VINLLESAGF SRSNPYYIVP QGRVTSLTNA
160 170 180 190 200
KDSERLELLK EVAGTQIYEN RRAESNKIMD ETIQKSEKID ELLQYIEERL
210 220 230 240 250
RELEEEKNDL AVYHKKDNER RCLEYAIYSR EHDEINSVLD ALEQDRIAAL
260 270 280 290 300
ERNDDDSGAF IQREERIERI KAEITELNHS LELLRVEKQQ NDEDYTNIMK
310 320 330 340 350
SKVALELQSS QLSRQIEFSK KDESSKLNIL SELESKISEK ENELSEILPK
360 370 380 390 400
YNAIVSEADD LNKRIMLLKN QKQSLLDKQS RTSQFTTKKE RDEWIRNQLL
410 420 430 440 450
QINRNINSTK ENSDYLKTEY DEMENELKAK LSRKKEIEIS LESQGDRMSQ
460 470 480 490 500
LLANITSINE RKENLTDKRK SLWREEAKLK SSIENVKDDL SRSEKALGTT
510 520 530 540 550
MDRNTSNGIR AVKDIAERLK LEGYYGPLCE LFKVDNRFKV AVEATAGNSL
560 570 580 590 600
FHIVVDNDET ATQILDVIYK ENAGRVTFMP LNKLRPKAVT YPDASDALPL
610 620 630 640 650
IQYLEFDPKF DAAIKQVFSK TIVCPSIETA SQYARSHQLN GITLSGDRSD
660 670 680 690 700
KKGALTAGYR DYRNSRLDAI KNVKTYQIKF SDLQESLEKC RSEIESFDQK
710 720 730 740 750
ITACLDDLQK AQLSLKQFER DHIPLKDELV TITGETTDLQ ESMHHKSRML
760 770 780 790 800
ELVVLELHTL EQQANDLKSE LSSEMDELDP KDVEALKSLS GQIENLSHEF
810 820 830 840 850
DAIIKERAHI EARKTALEYE LNTNLYLRRN PLKAEIGSDN RIDESELNSV
860 870 880 890 900
KRSLLKYENK LQIIKSSSSG LEEQMQRINS EISDKRNELE SLEELQHEVA
910 920 930 940 950
TRIEQDAKIN ERNAAKRSLL LARKKECNEK IKSLGVLPEE AFIKYVSTSS
960 970 980 990 1000
NAIVKKLHKI NEALKDYGSV NKKAYEQFNN FTKQRDSLLA RREELRRSQE
1010 1020 1030 1040 1050
SISELTTVLD QRKDEAIERT FKQVAKSFSE IFVKLVPAGR GELVMNRRSE
1060 1070 1080 1090 1100
LSQSIEQDIS MDIDTPSQKS SIDNYTGISI RVSFNSKDDE QLNINQLSGG
1110 1120 1130 1140 1150
QKSLCALTLI FAIQRCDPAP FNILDECDAN LDAQYRSAIA AMVKEMSKTS
1160 1170 1180 1190
QFICTTFRPE MVKVADNFYG VMFNHKVSTV ESISKEEAMA FVEG
Length:1,194
Mass (Da):136,850
Last modified:June 1, 1998 - v1
Checksum:iFD4D1E81A9E2E423
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAA15722.1.
PIRiT37503.
RefSeqiNP_593260.1. NM_001018657.2.

Genome annotation databases

EnsemblFungiiSPAC10F6.09c.1; SPAC10F6.09c.1:pep; SPAC10F6.09c.
GeneIDi2543010.
KEGGispo:SPAC10F6.09c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAA15722.1.
PIRiT37503.
RefSeqiNP_593260.1. NM_001018657.2.

3D structure databases

ProteinModelPortaliO42649.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi279448. 5 interactions.
DIPiDIP-35366N.
IntActiO42649. 2 interactions.
MINTiMINT-4673146.

Proteomic databases

MaxQBiO42649.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC10F6.09c.1; SPAC10F6.09c.1:pep; SPAC10F6.09c.
GeneIDi2543010.
KEGGispo:SPAC10F6.09c.

Organism-specific databases

EuPathDBiFungiDB:SPAC10F6.09c.
PomBaseiSPAC10F6.09c. psm3.

Phylogenomic databases

HOGENOMiHOG000166512.
InParanoidiO42649.
KOiK06669.
OMAiQKANRID.
OrthoDBiEOG7M0P0T.
PhylomeDBiO42649.

Enzyme and pathway databases

ReactomeiR-SPO-2500257. Resolution of Sister Chromatid Cohesion.

Miscellaneous databases

NextBioi20804043.
PROiO42649.

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. 2 hits.
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...

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. "Characterization of fission yeast cohesin: essential anaphase proteolysis of Rad21 phosphorylated in the S phase."
    Tomonaga T., Nagao K., Kawasaki Y., Furuya K., Murakami A., Morishita J., Yuasa T., Sutani T., Kearsey S.E., Uhlmann F., Nasmyth K., Yanagida M.
    Genes Dev. 14:2757-2770(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN A COHESIN COMPLEX WITH PSM1 AND RAD21.

Entry informationi

Entry nameiSMC3_SCHPO
AccessioniPrimary (citable) accession number: O42649
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 28, 2003
Last sequence update: June 1, 1998
Last modified: November 11, 2015
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

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.