Q8TZY2 (SMC_PYRFU) Reviewed, UniProtKB/Swiss-Prot

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)

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 MF_01894
Subunit structure	Homodimer. Ref.5
Subcellular location	Cytoplasm By similarity HAMAP 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.

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 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: UniProtKB-KW DNA binding Inferred from electronic annotation. Source: UniProtKB-KW
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 MF_01894

PRO_0000409287

Regions

Nucleotide binding

34 – 41

8

ATP HAMAP MF_01894

Coiled coil

167 – 506

340

Potential

Coiled coil

659 – 1012

354

Potential

Secondary structure

1

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1177

Helix Strand Turn

Details...

Beta strand

3 – 10

8

Beta strand

20 – 23

4

Beta strand

29 – 31

3

Helix

45 – 49

5

Helix

56 – 58

3

Helix

63 – 66

4

Beta strand

80 – 87

8

Beta strand

95 – 106

12

Beta strand

112 – 116

5

Helix

123 – 132

10

Helix

150 – 153

4

Helix

156 – 166

11

Sequences

	Sequence		Length	Mass (Da)
	Q8TZY2 [UniParc]. Last modified May 31, 2011. Version 2. Checksum: EC12C4C060E5A1CB	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

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: 14660695] [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: 10430560] [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: 15458651] [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: 20600125] [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: 21117236] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 488-667, DNA-BINDING, SUBUNIT, DOMAIN.
+	Additional computationally mapped references.

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	[»]

ProteinModelPortal

Q8TZY2.

SMR

Q8TZY2. Positions 2-167, 1012-1173.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q8TZY2. 2 interactions.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBPYRT00000005128; EBPYRP00000004989; EBPYRG00000005127.

GeneID

1469722.

GenomeReviews

Gene locus PF1843 in contig AE009950_GR.

KEGG

pfu:PF1843.

NMPDR

fig|186497.1.peg.1892.

Phylogenomic databases

GeneTree

EBGT00050000022195.

HOGENOM

HBG616483.

OMA

EPVNMRA.

ProtClustDB

CLSK254754.

Family and domain databases

HAMAP

MF_01894. Smc_prok.
[Tree]

InterPro

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

KO

K03529.

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...

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:	January 25, 2012
This is version 65 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program