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Q8TZY2 (SMC_PYRFU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Chromosome partition protein Smc
Gene names
Name:smc
Ordered Locus Names:PF1843
OrganismPyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) [Reference proteome] [HAMAP]
Taxonomic identifier186497 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus

Protein attributes

Sequence length1177 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for chromosome condensation and partitioning By similarity. Binds single-stranded but not double-stranded DNA. HAMAP-Rule MF_01894

Subunit structure

Homodimer. Ref.5

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_01894.

Domain

Contains large globular domains required for ATP hydrolysis at each terminus and a third globular domain forming a flexible hinge near the middle of the molecule. These domains are separated by coiled-coil structures. The N- and C-terminus interact to make up an ATP-binding cassette-type ATPase domain. The hinge domain mediates dimerization and binds DNA. Ref.3 Ref.5

Sequence similarities

Belongs to the SMC family.

Sequence caution

The sequence AAL81967.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11771177Chromosome partition protein Smc HAMAP-Rule MF_01894
PRO_0000409287

Regions

Nucleotide binding34 – 418ATP HAMAP-Rule MF_01894
Coiled coil167 – 506340 Potential
Coiled coil659 – 1012354 Potential

Secondary structure

............................................................................................. 1177
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8TZY2 [UniParc].

Last modified May 31, 2011. Version 2.
Checksum: EC12C4C060E5A1CB

FASTA1,177135,014
        10         20         30         40         50         60 
MPYIEKLELK GFKSYGNKKV VIPFSKGFTA IVGANGSGKS NIGDAILFVL GGLSAKAMRA 

        70         80         90        100        110        120 
SRISDLIFAG SKNEPPAKYA EVAIYFNNED RGFPIDEDEV VIRRRVYPDG RSSYWLNGRR 

       130        140        150        160        170        180 
ATRSEILDIL TAAMISPDGY NIVLQGDITK FIKMSPLERR LLIDDISGIA EYDSKKEKAL 

       190        200        210        220        230        240 
EELKQAEENL ARVDLLIKEV KKQLDKLEKE RNDALRYLDL KDKLEKAKVS LLLGEIKILE 

       250        260        270        280        290        300 
TQIKEGEKRR AEIEEEIQKI EKEIEKIGKE IVEKVKVLRE IEERIEKESG EEAIQITKKI 

       310        320        330        340        350        360 
GEVTSKIELT KRNIEVAKEE LEDAQRRLAK TKEELRKVLS EIEKSKGAIT RWKKRRDALI 

       370        380        390        400        410        420 
NEIKKKEEER NVLVVKLGEI DKTFGAAREE FDSVVKELEE TTRKMYEIEG NIRRLQEEKE 

       430        440        450        460        470        480 
KLHSRILFLR AKLPGIKEKI NEFKAVVEDK RAEISEIEGK LSTIQAKRIK VEKEIEAKSN 

       490        500        510        520        530        540 
ELEKVSKELE SSERELIAAE AQREVRGNRA AEELKRSGIG GIYGTLAELI KVKDEAYALA 

       550        560        570        580        590        600 
IEVALGNRAD NVVVEDELVA EKAIKYLKEH KLGRLTFLPL NKIKPKHVDS SVGLPAVDVI 

       610        620        630        640        650        660 
EYDQKIENAV KFALGDTVIV NSMEEARPHI GKVRMVTIEG ELYERSGAIT GGHFRARGLA 

       670        680        690        700        710        720 
VDTTKLREKV ESLRRRKEAL EGELNSLKIE LRSLENASFE LRIKLSDEKK ELELASKDLN 

       730        740        750        760        770        780 
RLLEEENAVK EEIEESERKI QEIEQKIENE KSELAKLRGR IQRLERKKEK LKKALENPEA 

       790        800        810        820        830        840 
RELMEKIRII DGEISSLKEE LSRIESRIES LESRLNEELL PRKASLEEEI EGLVNKINAL 

       850        860        870        880        890        900 
KNNISENEKA LELLNKELEK LKSIEENIKG EIRTLREKRK KLEEDISKLR EKKEVLQRKL 

       910        920        930        940        950        960 
QELEIEANTL KVRDAQLNAQ LEEKKYQLTH YDKNLIKSIK EIPLDLEKVK KEIEKMEEEI 

       970        980        990       1000       1010       1020 
RSLEPVNMKA IEDFEIVERR YLELKSKREK LEAEKESIIE FINEIEKEKK NVFMRTFEAI 

      1030       1040       1050       1060       1070       1080 
SRNFSEIFAK LSPGGSARLI LENPEDPFSG GLEIEAKPAG KDVKRIEAMS GGEKALTALA 

      1090       1100       1110       1120       1130       1140 
FVFAIQKFKP APFYLFDEID AHLDDANVKR VADLIKESSK ESQFIVITLR DVMMANADKI 

      1150       1160       1170 
IGVSMRDGVS KVVSLSLEKA MKILEEIRKK QGWEHGN 

« Hide

References

« Hide 'large scale' references
[1]"The evolution of SMC proteins: phylogenetic analysis and structural implications."
Cobbe N., Heck M.M.S.
Mol. Biol. Evol. 21:332-347(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences."
Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., DiRuggiero J., Robb F.T.
Genetics 152:1299-1305(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
[3]"Structural biochemistry of ATP-driven dimerization and DNA-stimulated activation of SMC ATPases."
Lammens A., Schele A., Hopfner K.P.
Curr. Biol. 14:1778-1782(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-182 AND 1006-1177 IN COMPLEX WITH ATP, DOMAIN.
[4]"Structural basis for adenylate kinase activity in ABC ATPases."
Lammens A., Hopfner K.P.
J. Mol. Biol. 401:265-273(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS) OF 1-182 AND 1006-1177.
[5]"Structure and DNA-binding activity of the Pyrococcus furiosus SMC protein hinge domain."
Griese J.J., Hopfner K.P.
Proteins 79:558-568(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 488-667, DNA-BINDING, SUBUNIT, DOMAIN.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ543649 Genomic DNA. Translation: CAD66602.1.
AE009950 Genomic DNA. Translation: AAL81967.1. Different initiation.
RefSeqNP_579572.1. NC_003413.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1XEWX-ray2.00X1-182[»]
Y1006-1177[»]
1XEXX-ray2.50A1-182[»]
3KTAX-ray1.63A/C1-182[»]
B/D1006-1177[»]
3NWCX-ray1.70A/B488-667[»]
4I99X-ray2.30A/B1-1172[»]
ProteinModelPortalQ8TZY2.
SMRQ8TZY2. Positions 2-167, 1012-1173.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-54374N.
IntActQ8TZY2. 2 interactions.
STRING186497.PF1843.

Proteomic databases

PRIDEQ8TZY2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL81967; AAL81967; PF1843.
GeneID1469722.
KEGGpfu:PF1843.

Phylogenomic databases

eggNOGCOG1196.
HOGENOMHOG000228754.
KOK03529.

Family and domain databases

Gene3D3.40.50.300. 4 hits.
HAMAPMF_01894. Smc_prok.
InterProIPR027417. P-loop_NTPase.
IPR003395. RecF/RecN/SMC_N.
IPR024704. SMC.
IPR010935. SMC_hinge.
IPR011890. SMC_prok.
[Graphical view]
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.
TIGRFAMsTIGR02169. SMC_prok_A. 1 hit.
TIGR02168. SMC_prok_B. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ8TZY2.

Entry information

Entry nameSMC_PYRFU
AccessionPrimary (citable) accession number: Q8TZY2
Secondary accession number(s): Q877I1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 31, 2011
Last sequence update: May 31, 2011
Last modified: July 9, 2014
This is version 81 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references