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Protein

Structural maintenance of chromosomes protein 4

Gene

smc4

Organism
Dictyostelium discoideum (Slime mold)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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 (By similarity).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi189 – 1968ATPSequence analysis

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, DNA condensation, Mitosis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Structural maintenance of chromosomes protein 4
Short name:
SMC protein 4
Short name:
SMC-4
Gene namesi
Name:smc4
ORF Names:DDB_G0286403
OrganismiDictyostelium discoideum (Slime mold)
Taxonomic identifieri44689 [NCBI]
Taxonomic lineageiEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium
Proteomesi
  • UP000002195 Componentsi: Chromosome 4, Unassembled WGS sequence

Organism-specific databases

dictyBaseiDDB_G0286403. smc4.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14151415Structural maintenance of chromosomes protein 4PRO_0000328140Add
BLAST

Proteomic databases

PaxDbiQ54LV0.

Interactioni

Subunit structurei

Forms a heterodimer with smc2. Component of the condensin complex, which contains the smc2-smc4 heterodimer (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi44689.DDB0219935.

Structurei

3D structure databases

ProteinModelPortaliQ54LV0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni683 – 852170Flexible hingeBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili361 – 479119Sequence analysisAdd
BLAST
Coiled coili533 – 675143Sequence analysisAdd
BLAST
Coiled coili855 – 1120266Sequence analysisAdd
BLAST
Coiled coili1162 – 123372Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi13 – 175Poly-Glu
Compositional biasi33 – 6028Poly-GluAdd
BLAST
Compositional biasi115 – 1184Poly-Gln
Compositional biasi1386 – 13916Poly-Thr
Compositional biasi1395 – 140915Poly-GlnAdd
BLAST

Domaini

The hinge domain, which separates the large intramolecular coiled coil regions, allows the heterodimerization with smc2 forming a V-shaped heterodimer.By similarity

Sequence similaritiesi

Belongs to the SMC family. SMC4 subfamily.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG0996. Eukaryota.
COG1196. LUCA.
InParanoidiQ54LV0.
KOiK06675.
OMAiCERERDS.
PhylomeDBiQ54LV0.

Family and domain databases

Gene3Di3.40.50.300. 3 hits.
InterProiIPR027417. P-loop_NTPase.
IPR003395. RecF/RecN/SMC_N.
IPR024704. SMC.
IPR010935. SMC_hinge.
[Graphical view]
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. 3 hits.
SSF75553. SSF75553. 1 hit.

Sequencei

Sequence statusi: Complete.

Q54LV0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVEDEEINDQ ISEEEEEKKK NNDSDEEMKD IDEEEEEEEE EEEEEEEEEK
60 70 80 90 100
EEEEEEEEEE TPKKPMPPPQ SKAKPSSQPP DIKKASQQSQ TQKNTPPPIQ
110 120 130 140 150
TSQSSQSSQS SQSSQQQQPK NISQTQQPKN TPPLQSSQTS QTSQKTPVSS
160 170 180 190 200
NNGIEKRLMI TKMVMENFKS YAGAQEVGPF HKCFSSVVGP NGSGKSNVID
210 220 230 240 250
AMLFVFGYRA KQIRLNKISE LIHNSENHKN LTNGRVSVHF QEIIDLPGED
260 270 280 290 300
NYEVVKGSEF VVTRTAQKTG NNKDGVSKYY LNDKVVKLDD LKTILKDKGI
310 320 330 340 350
DLDNNRFLIL QGEVEQIAMM KPKGVHPGEE GLLEYLEDII GSKKYLPDIE
360 370 380 390 400
ATSKLIEDIG DKRTSSNNRM KVVEKEKDAL QQERDNALEY IDKELKLIHC
410 420 430 440 450
KSIHYQIGRS KPEREKNEIA AKQEMVEKQL EQELVTQKAS NDKLLEFEKN
460 470 480 490 500
LKQQNKQLDE LNKQMAKCKN ELLTTEKKGV KYKEETKHLK TKVKKNNSVI
510 520 530 540 550
EEETKKQAEF ERSTIIHKQD IVRFEKEYVE LPKELIVEEK KLESMLNSLK
560 570 580 590 600
GEVTELQREM EEKQKQLLPW SKKHSEAKAV VDLKTSELAV LSKDFNGATQ
610 620 630 640 650
NLDDAIKALE DAKTISSTRK NNITKSKKEL ESVKAIIVDL EKRLASGKVT
660 670 680 690 700
EENLYRNTMD AKRQLEQIKT NLSENSSRNT ILDRLLKIKE SGQISGIHGR
710 720 730 740 750
LGDLGAIDQK YDVAISTAAF SQMDNIIVET TAAAEACVEL LRKENLGRAT
760 770 780 790 800
FMILENLEYQ RQNLGPVQTP NNTPRLFDLI KMKDEKKYAT AFFTAVGHTL
810 820 830 840 850
VADTLDEATK IAYGAKRHRV VTLDGSLIDT SGAMSGGGLK PRVGAMNSKL
860 870 880 890 900
KGDPKEDKKK LIELQDNLSQ LDSDLRQCRD ELVEIENQIQ QAQNRRSELE
910 920 930 940 950
LELPKMDMDI KAAITKCEEL TKVIPQLKNK AKLSTEKKEQ IDSIKESLIV
960 970 980 990 1000
DQKSLDKVQE KVNKLESEVQ EIQNSILNVG GPQLKMQKNK VESLQSRIDS
1010 1020 1030 1040 1050
NQTNTTKANV QIKSLAKSME KSIKILNENT KEKDENEAAL AEILEKYKSL
1060 1070 1080 1090 1100
EKENLKATEA MEAVSEQLRE KEEETKEIRK EHEKAKKVIE KIKVSNSKLE
1110 1120 1130 1140 1150
TQIEEFKTLI NEKQAEIADC LSKFANQAKK AKIYKDYVDE SLINQVSAIL
1160 1170 1180 1190 1200
TPEEIEQYME ATEQQNLIAK IHELTTQIQK ISKENNVNIE VVKDFQKKEQ
1210 1220 1230 1240 1250
EYHSRKAEFD EIEKERDNLS KRYESLRKNR LDEFMAGFTI ITMKLKEIYQ
1260 1270 1280 1290 1300
MITLGGDAEL EIIDREDPFQ EGISFSVRPP KKSWKNISNL SGGEKTLSSL
1310 1320 1330 1340 1350
ALVFALHHYK PNALYVMDEI DAALDFKNVS IIANYIKERT KNAQFIIISL
1360 1370 1380 1390 1400
RNYMFELADR LVGIYKTDNC TKSVTINPNS FTSLSTTTTT TNNSQQQQQQ
1410
KQQQKQQQQN STSQK
Length:1,415
Mass (Da):161,555
Last modified:May 24, 2005 - v1
Checksum:i75444BC92B3FD95D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAFI02000085 Genomic DNA. Translation: EAL64226.1.
RefSeqiXP_637730.1. XM_632638.1.

Genome annotation databases

EnsemblProtistsiDDB0219935; DDB0219935; DDB_G0286403.
GeneIDi8625595.
KEGGiddi:DDB_G0286403.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAFI02000085 Genomic DNA. Translation: EAL64226.1.
RefSeqiXP_637730.1. XM_632638.1.

3D structure databases

ProteinModelPortaliQ54LV0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi44689.DDB0219935.

Proteomic databases

PaxDbiQ54LV0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsiDDB0219935; DDB0219935; DDB_G0286403.
GeneIDi8625595.
KEGGiddi:DDB_G0286403.

Organism-specific databases

dictyBaseiDDB_G0286403. smc4.

Phylogenomic databases

eggNOGiKOG0996. Eukaryota.
COG1196. LUCA.
InParanoidiQ54LV0.
KOiK06675.
OMAiCERERDS.
PhylomeDBiQ54LV0.

Enzyme and pathway databases

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

Miscellaneous databases

PROiQ54LV0.

Family and domain databases

Gene3Di3.40.50.300. 3 hits.
InterProiIPR027417. P-loop_NTPase.
IPR003395. RecF/RecN/SMC_N.
IPR024704. SMC.
IPR010935. SMC_hinge.
[Graphical view]
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. 3 hits.
SSF75553. SSF75553. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "The genome of the social amoeba Dictyostelium discoideum."
    Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N.
    , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.
    Nature 435:43-57(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: AX4.

Entry informationi

Entry nameiSMC4_DICDI
AccessioniPrimary (citable) accession number: Q54LV0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: May 24, 2005
Last modified: December 9, 2015
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Dictyostelium discoideum
    Dictyostelium discoideum: entries, gene names and cross-references to dictyBase
  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.