Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q8TZY2

- SMC_PYRFU

UniProt

Q8TZY2 - SMC_PYRFU

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Chromosome partition protein Smc

Gene

smc

Organism
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Required for chromosome condensation and partitioning (By similarity). Binds single-stranded but not double-stranded DNA.UniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi34 – 418ATP1 PublicationUniRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-HAMAP
  2. DNA binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. chromosome condensation Source: InterPro
  2. DNA replication Source: UniProtKB-HAMAP
  3. sister chromatid cohesion Source: InterPro
Complete GO annotation...

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Chromosome partition protein SmcUniRule annotation
Gene namesi
Name:smcUniRule annotation
Ordered Locus Names:PF1843
OrganismiPyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Taxonomic identifieri186497 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
ProteomesiUP000001013: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. chromosome Source: InterPro
  2. cytoplasm Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11771177Chromosome partition protein SmcPRO_0000409287Add
BLAST

Proteomic databases

PRIDEiQ8TZY2.

Interactioni

Subunit structurei

Homodimer.2 PublicationsUniRule annotation

Protein-protein interaction databases

DIPiDIP-54374N.
IntActiQ8TZY2. 2 interactions.
STRINGi186497.PF1843.

Structurei

Secondary structure

1
1177
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 1210
Helixi13 – 153
Beta strandi20 – 234
Beta strandi26 – 338
Helixi39 – 4911
Helixi56 – 583
Helixi63 – 664
Beta strandi80 – 878
Beta strandi93 – 10614
Beta strandi112 – 1165
Beta strandi119 – 1213
Helixi123 – 13210
Helixi137 – 1393
Helixi150 – 1534
Helixi156 – 16712
Helixi490 – 50516
Helixi510 – 5145
Beta strandi521 – 5255
Helixi526 – 5294
Beta strandi531 – 5333
Helixi535 – 5373
Helixi538 – 5458
Helixi546 – 5505
Beta strandi552 – 5565
Helixi557 – 56913
Beta strandi577 – 5793
Turni580 – 5823
Beta strandi592 – 5954
Helixi596 – 5994
Helixi604 – 6063
Helixi607 – 6148
Beta strandi617 – 6215
Helixi624 – 6296
Turni630 – 6323
Beta strandi633 – 6375
Beta strandi659 – 6613
Helixi1008 – 103124
Beta strandi1036 – 10427
Beta strandi1044 – 10463
Helixi1047 – 10493
Beta strandi1052 – 10576
Beta strandi1060 – 10623
Helixi1066 – 10683
Helixi1071 – 108818
Beta strandi1092 – 10987
Turni1099 – 11024
Helixi1105 – 111814
Turni1119 – 11213
Beta strandi1122 – 11276
Helixi1131 – 11344
Beta strandi1138 – 11469
Beta strandi1149 – 11546
Helixi1157 – 116812

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliQ8TZY2.
SMRiQ8TZY2. Positions 2-167, 1012-1173.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8TZY2.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili167 – 506340UniRule annotationAdd
BLAST
Coiled coili659 – 1012354UniRule annotationAdd
BLAST

Domaini

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.2 PublicationsUniRule annotation

Sequence similaritiesi

Belongs to the SMC family.UniRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG1196.
HOGENOMiHOG000228754.
KOiK03529.

Family and domain databases

Gene3Di3.40.50.300. 4 hits.
HAMAPiMF_01894. Smc_prok.
InterProiIPR027417. P-loop_NTPase.
IPR003395. RecF/RecN/SMC_N.
IPR024704. SMC.
IPR010935. SMC_hinge.
IPR011890. SMC_prok.
[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. 2 hits.
SSF75553. SSF75553. 1 hit.
TIGRFAMsiTIGR02169. SMC_prok_A. 1 hit.
TIGR02168. SMC_prok_B. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8TZY2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPYIEKLELK GFKSYGNKKV VIPFSKGFTA IVGANGSGKS NIGDAILFVL
60 70 80 90 100
GGLSAKAMRA SRISDLIFAG SKNEPPAKYA EVAIYFNNED RGFPIDEDEV
110 120 130 140 150
VIRRRVYPDG RSSYWLNGRR ATRSEILDIL TAAMISPDGY NIVLQGDITK
160 170 180 190 200
FIKMSPLERR LLIDDISGIA EYDSKKEKAL EELKQAEENL ARVDLLIKEV
210 220 230 240 250
KKQLDKLEKE RNDALRYLDL KDKLEKAKVS LLLGEIKILE TQIKEGEKRR
260 270 280 290 300
AEIEEEIQKI EKEIEKIGKE IVEKVKVLRE IEERIEKESG EEAIQITKKI
310 320 330 340 350
GEVTSKIELT KRNIEVAKEE LEDAQRRLAK TKEELRKVLS EIEKSKGAIT
360 370 380 390 400
RWKKRRDALI NEIKKKEEER NVLVVKLGEI DKTFGAAREE FDSVVKELEE
410 420 430 440 450
TTRKMYEIEG NIRRLQEEKE KLHSRILFLR AKLPGIKEKI NEFKAVVEDK
460 470 480 490 500
RAEISEIEGK LSTIQAKRIK VEKEIEAKSN ELEKVSKELE SSERELIAAE
510 520 530 540 550
AQREVRGNRA AEELKRSGIG GIYGTLAELI KVKDEAYALA IEVALGNRAD
560 570 580 590 600
NVVVEDELVA EKAIKYLKEH KLGRLTFLPL NKIKPKHVDS SVGLPAVDVI
610 620 630 640 650
EYDQKIENAV KFALGDTVIV NSMEEARPHI GKVRMVTIEG ELYERSGAIT
660 670 680 690 700
GGHFRARGLA VDTTKLREKV ESLRRRKEAL EGELNSLKIE LRSLENASFE
710 720 730 740 750
LRIKLSDEKK ELELASKDLN RLLEEENAVK EEIEESERKI QEIEQKIENE
760 770 780 790 800
KSELAKLRGR IQRLERKKEK LKKALENPEA RELMEKIRII DGEISSLKEE
810 820 830 840 850
LSRIESRIES LESRLNEELL PRKASLEEEI EGLVNKINAL KNNISENEKA
860 870 880 890 900
LELLNKELEK LKSIEENIKG EIRTLREKRK KLEEDISKLR EKKEVLQRKL
910 920 930 940 950
QELEIEANTL KVRDAQLNAQ LEEKKYQLTH YDKNLIKSIK EIPLDLEKVK
960 970 980 990 1000
KEIEKMEEEI RSLEPVNMKA IEDFEIVERR YLELKSKREK LEAEKESIIE
1010 1020 1030 1040 1050
FINEIEKEKK NVFMRTFEAI SRNFSEIFAK LSPGGSARLI LENPEDPFSG
1060 1070 1080 1090 1100
GLEIEAKPAG KDVKRIEAMS GGEKALTALA FVFAIQKFKP APFYLFDEID
1110 1120 1130 1140 1150
AHLDDANVKR VADLIKESSK ESQFIVITLR DVMMANADKI IGVSMRDGVS
1160 1170
KVVSLSLEKA MKILEEIRKK QGWEHGN
Length:1,177
Mass (Da):135,014
Last modified:May 31, 2011 - v2
Checksum:iEC12C4C060E5A1CB
GO

Sequence cautioni

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ543649 Genomic DNA. Translation: CAD66602.1.
AE009950 Genomic DNA. Translation: AAL81967.1. Different initiation.
RefSeqiNP_579572.1. NC_003413.1.

Genome annotation databases

EnsemblBacteriaiAAL81967; AAL81967; PF1843.
GeneIDi1469722.
KEGGipfu:PF1843.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ543649 Genomic DNA. Translation: CAD66602.1 .
AE009950 Genomic DNA. Translation: AAL81967.1 . Different initiation.
RefSeqi NP_579572.1. NC_003413.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 1-1172 [» ]
ProteinModelPortali Q8TZY2.
SMRi Q8TZY2. Positions 2-167, 1012-1173.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-54374N.
IntActi Q8TZY2. 2 interactions.
STRINGi 186497.PF1843.

Proteomic databases

PRIDEi Q8TZY2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAL81967 ; AAL81967 ; PF1843 .
GeneIDi 1469722.
KEGGi pfu:PF1843.

Phylogenomic databases

eggNOGi COG1196.
HOGENOMi HOG000228754.
KOi K03529.

Miscellaneous databases

EvolutionaryTracei Q8TZY2.

Family and domain databases

Gene3Di 3.40.50.300. 4 hits.
HAMAPi MF_01894. Smc_prok.
InterProi IPR027417. P-loop_NTPase.
IPR003395. RecF/RecN/SMC_N.
IPR024704. SMC.
IPR010935. SMC_hinge.
IPR011890. SMC_prok.
[Graphical view ]
Pfami PF06470. SMC_hinge. 1 hit.
PF02463. SMC_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF005719. SMC. 1 hit.
SMARTi SM00968. SMC_hinge. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 2 hits.
SSF75553. SSF75553. 1 hit.
TIGRFAMsi TIGR02169. SMC_prok_A. 1 hit.
TIGR02168. SMC_prok_B. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiSMC_PYRFU
AccessioniPrimary (citable) accession number: Q8TZY2
Secondary accession number(s): Q877I1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 31, 2011
Last sequence update: May 31, 2011
Last modified: October 29, 2014
This is version 84 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3