Chromosome partition protein Smc - Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)

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Q8TZY2 (SMC_PYRFU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 72. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Chromosome partition protein Smc

Gene names

Name:	smc
Ordered Locus Names:	PF1843

Organism

Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) [Reference proteome] [HAMAP]

Taxonomic identifier

186497 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus ›

Protein attributes

Sequence length	1177 AA.
Sequence status	Complete.
Protein existence	Evidence 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.
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.

Ontologies

Keywords
Cellular component	Cytoplasm
Domain	Coiled coil
Ligand	ATP-binding DNA-binding Nucleotide-binding
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA recombination Inferred from electronic annotation. Source: InterPro DNA repair Inferred from electronic annotation. Source: InterPro DNA replication Inferred from electronic annotation. Source: HAMAP chromosome condensation Inferred from electronic annotation. Source: InterPro sister chromatid cohesion Inferred from electronic annotation. Source: InterPro
Cellular_component	chromosome Inferred from electronic annotation. Source: InterPro cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: HAMAP DNA binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1177

1177

Chromosome partition protein Smc HAMAP-Rule MF_01894

PRO_0000409287

Regions

Nucleotide binding

34 – 41

ATP HAMAP-Rule MF_01894

Coiled coil

167 – 506

340

Potential

Coiled coil

659 – 1012

354

Potential

Secondary structure

1177

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q8TZY2 [UniParc].

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

1,177

135,014

        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' referencesShow '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.

RefSeq

NP_579572.1. NC_003413.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1XEW	X-ray	2.00	X	1-182	[»]
			Y	1006-1177	[»]
1XEX	X-ray	2.50	A	1-182	[»]
3KTA	X-ray	1.63	A/C	1-182	[»]
			B/D	1006-1177	[»]
3NWC	X-ray	1.70	A/B	488-667	[»]
4I99	X-ray	2.30	A/B	1-1177	[»]

ProteinModelPortal

Q8TZY2.

SMR

Q8TZY2. Positions 2-167, 1012-1173.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q8TZY2. 2 interactions.

STRING

186497.PF1843.

Proteomic databases

PRIDE

Q8TZY2.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAL81967; AAL81967; PF1843.

GeneID

1469722.

KEGG

pfu:PF1843.

Phylogenomic databases

eggNOG

COG1196.

HOGENOM

HOG000228754.

K03529.

ProtClustDB

CLSK254754.

Family and domain databases

HAMAP

MF_01894. Smc_prok.

InterPro

IPR003395. RecF/RecN/SMC.
IPR024704. SMC.
IPR010935. SMC_hinge.
IPR011890. SMC_prok.
[Graphical view]

Pfam

PF06470. SMC_hinge. 1 hit.
PF02463. SMC_N. 1 hit.
[Graphical view]

PIRSF

PIRSF005719. SMC. 1 hit.

SMART

SM00968. SMC_hinge. 1 hit.
[Graphical view]

SUPFAM

SSF75553. SMC_hinge. 1 hit.

TIGRFAMs

TIGR02169. SMC_prok_A. 1 hit.
TIGR02168. SMC_prok_B. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

Q8TZY2.

Entry information

Entry name

SMC_PYRFU

Accession

Primary (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:	May 1, 2013
This is version 72 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Family and domain databases

Other

Entry information

Relevant documents