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Protein

Structural maintenance of chromosomes protein 2-2

Gene

SMC2-2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Central component of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases. Also involved in chromosome segregation in meiosis.

Regions

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

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • transporter activity Source: TAIR

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • meiotic cell cycle Source: UniProtKB-KW
  • mitotic chromosome condensation Source: InterPro
  • transport Source: GOC
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, DNA condensation, Meiosis, Mitosis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-ATH-2299718. Condensation of Prophase Chromosomes.
R-ATH-2514853. Condensation of Prometaphase Chromosomes.

Names & Taxonomyi

Protein namesi
Recommended name:
Structural maintenance of chromosomes protein 2-2
Short name:
AtSMC2-2
Alternative name(s):
Chromosome-associated protein E-2
Short name:
AtCAP-E2
Gene namesi
Name:SMC2-2
Synonyms:CAP-E2
Ordered Locus Names:At3g47460
ORF Names:F1P2.10, T21L8.210
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 3

Organism-specific databases

TAIRiAT3G47460.

Subcellular locationi

  • Nucleus

  • Note: Associates with chromatin.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11711171Structural maintenance of chromosomes protein 2-2PRO_0000284895Add
BLAST

Proteomic databases

PaxDbiQ9SN90.
PRIDEiQ9SN90.

PTM databases

iPTMnetiQ9SN90.

Expressioni

Tissue specificityi

Highly expressed in roots and young floral buds.1 Publication

Gene expression databases

GenevisibleiQ9SN90. AT.

Interactioni

Subunit structurei

Forms a heterodimer with SMC4. Component of the condensin complex, which contains the SMC2 and SMC4 heterodimer, and three non SMC subunits that probably regulate the complex: CAPH, CAPD2 and CAPG.

Protein-protein interaction databases

STRINGi3702.AT3G47460.1.

Structurei

3D structure databases

ProteinModelPortaliQ9SN90.
SMRiQ9SN90. Positions 2-195, 413-715, 853-1163.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 11581157Zinc-hookAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni511 – 673163Flexible hingeAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili172 – 510339Sequence analysisAdd
BLAST
Coiled coili674 – 1026353Sequence analysisAdd
BLAST

Domaini

The hinge domain, which separates the large intramolecular coiled coil regions, allows the heterodimerization with SMC4, forming a V-shaped heterodimer.

Sequence similaritiesi

Belongs to the SMC family. SMC2 subfamily.Curated
Contains 1 zinc-hook domain.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG0933. Eukaryota.
COG1196. LUCA.
HOGENOMiHOG000163792.
InParanoidiQ9SN90.
KOiK06674.
OMAiTFICNDP.
PhylomeDBiQ9SN90.

Family and domain databases

Gene3Di3.40.50.300. 3 hits.
InterProiIPR027417. P-loop_NTPase.
IPR003395. RecF/RecN/SMC_N.
IPR024704. SMC.
IPR027120. Smc2.
IPR010935. SMC_hinge.
[Graphical view]
PANTHERiPTHR18937:SF9. PTHR18937:SF9. 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.

Q9SN90-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHIKEICLEG FKSYATRTVV PGFDPHFNAI TGLNGSGKSN ILDSICFVLG
60 70 80 90 100
ITNLQQVRAA NLQELVYKQG QAGITRATVS VTFDNSERNR SPLGHEDHSE
110 120 130 140 150
ITVTRQIVVG GKNKYLINGK LAQPNQVQNL FHSVQLNVNN PHFLIMQGRI
160 170 180 190 200
TKVLNMKPME ILSMLEEAAG TRMYENKKEA ALKTLEKKQT KVDEINKLLE
210 220 230 240 250
KDILPALEKL RREKSQYMQW ANGNAELDRL KRFCVAFEYV QAEKIRDNSI
260 270 280 290 300
HVVEEMKIKM TGIDEQTDKT QGEISELEKQ IKALTQAREA SMGGEVKALS
310 320 330 340 350
DKVDSLSNEV TRELSKLTNM EDTLQGEEKN AEKMVHNIED LKKSVEERAS
360 370 380 390 400
ALNKCDEGAA ELKQKFQEFS TTLEECEREH QGILAGKSSG DEEKCLEDQL
410 420 430 440 450
RDAKISVGTA ETELKQLNTK ISHCEKELKE KKSQLMSKQD EAVAVENELD
460 470 480 490 500
ARKNDVESVK RAFDSLPYKE GQMEALEKDR ESELEIGHRL KDKVHELSAQ
510 520 530 540 550
LANVQFTYRD PVKNFDRSKV KGVVAKLIKV NDRSSMTALE VTAGGKLFNV
560 570 580 590 600
IVDTEDTGKQ LLQKGDLRRR VTIIPLNKIQ SHLVPPRVQQ ATVGKGNAEL
610 620 630 640 650
ALSLVGYSEE LKNAMEYVFG STFVCKTTDA AKEVAFNREI RTPSVTLEGD
660 670 680 690 700
VFQPSGLLTG GSRKGGGDLL RQLHDLAEAE TKFRAHQKSL SEIEANIKEL
710 720 730 740 750
QPLQTKFTDM KAQLELKMYD MSLFLKRAEQ NEHHKLGDAV KKLEEEVEEM
760 770 780 790 800
RSQIKEKEGL YKSCADTVST LEKSIKDHDK NREGRLKDLE KNIKTLKARI
810 820 830 840 850
QASSKDLKGH ENVRERLVME QEAVTQEQSY LKSQLTSLRT QISTLASDVG
860 870 880 890 900
NQRAKVDAIQ KDHDQSLSEL KLIHAKMKEC DTQISGSIAE QEKCLQKISD
910 920 930 940 950
MKLDRKKLEN EVTRMEMEHK NCSVKVDKLV EKHTWITSEK RLFGNGGTDY
960 970 980 990 1000
DFESRDPHKA REELERLQTD QSSLEKRVNK KVTAMFEKAE DEYNALMTKK
1010 1020 1030 1040 1050
NIIETDKSKI KKVIEELDEK KKETLKVTWV KVNQDFGSIF STLLPGTMSK
1060 1070 1080 1090 1100
LEPPEGGTFL DGLEVRVAFG DVWKQSLSEL SGGQRSLLAL SLILALLLFK
1110 1120 1130 1140 1150
PAPIYILDEV DAALDLSHTQ NIGRMIKSHF PHSQFIVVSL KEGMFSNADV
1160 1170
LFRTKFVDGV STVQRTVTKQ S
Length:1,171
Mass (Da):132,315
Last modified:May 1, 2000 - v1
Checksum:i2FB6BFC4F00F4C95
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL096860 Genomic DNA. Translation: CAB51218.1.
AL132955 Genomic DNA. Translation: CAB61972.1.
CP002686 Genomic DNA. Translation: AEE78284.1.
PIRiT45706.
RefSeqiNP_190330.1. NM_114614.3.
UniGeneiAt.35803.
At.71101.

Genome annotation databases

EnsemblPlantsiAT3G47460.1; AT3G47460.1; AT3G47460.
GeneIDi823900.
GrameneiAT3G47460.1; AT3G47460.1; AT3G47460.
KEGGiath:AT3G47460.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL096860 Genomic DNA. Translation: CAB51218.1.
AL132955 Genomic DNA. Translation: CAB61972.1.
CP002686 Genomic DNA. Translation: AEE78284.1.
PIRiT45706.
RefSeqiNP_190330.1. NM_114614.3.
UniGeneiAt.35803.
At.71101.

3D structure databases

ProteinModelPortaliQ9SN90.
SMRiQ9SN90. Positions 2-195, 413-715, 853-1163.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT3G47460.1.

PTM databases

iPTMnetiQ9SN90.

Proteomic databases

PaxDbiQ9SN90.
PRIDEiQ9SN90.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G47460.1; AT3G47460.1; AT3G47460.
GeneIDi823900.
GrameneiAT3G47460.1; AT3G47460.1; AT3G47460.
KEGGiath:AT3G47460.

Organism-specific databases

TAIRiAT3G47460.

Phylogenomic databases

eggNOGiKOG0933. Eukaryota.
COG1196. LUCA.
HOGENOMiHOG000163792.
InParanoidiQ9SN90.
KOiK06674.
OMAiTFICNDP.
PhylomeDBiQ9SN90.

Enzyme and pathway databases

ReactomeiR-ATH-2299718. Condensation of Prophase Chromosomes.
R-ATH-2514853. Condensation of Prometaphase Chromosomes.

Miscellaneous databases

PROiQ9SN90.

Gene expression databases

GenevisibleiQ9SN90. AT.

Family and domain databases

Gene3Di3.40.50.300. 3 hits.
InterProiIPR027417. P-loop_NTPase.
IPR003395. RecF/RecN/SMC_N.
IPR024704. SMC.
IPR027120. Smc2.
IPR010935. SMC_hinge.
[Graphical view]
PANTHERiPTHR18937:SF9. PTHR18937:SF9. 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...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
    Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F.
    , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
    Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "Mutations in Arabidopsis condensin genes disrupt embryogenesis, meristem organization and segregation of homologous chromosomes during meiosis."
    Siddiqui N.U., Stronghill P.E., Dengler R.E., Hasenkampf C.A., Riggs C.D.
    Development 130:3283-3295(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
    Strain: cv. Landsberg erecta.

Entry informationi

Entry nameiSMC22_ARATH
AccessioniPrimary (citable) accession number: Q9SN90
Secondary accession number(s): Q9STX7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: May 1, 2000
Last modified: June 8, 2016
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: 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.