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Q8TZY2

- SMC_PYRFU

UniProt

Q8TZY2 - SMC_PYRFU

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
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    • History
      Entry version 83 (01 Oct 2014)
      Sequence version 2 (31 May 2011)
      Previous versions | rss
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    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

    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-SubCell

    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

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    MPYIEKLELK GFKSYGNKKV VIPFSKGFTA IVGANGSGKS NIGDAILFVL     50
    GGLSAKAMRA SRISDLIFAG SKNEPPAKYA EVAIYFNNED RGFPIDEDEV 100
    VIRRRVYPDG RSSYWLNGRR ATRSEILDIL TAAMISPDGY NIVLQGDITK 150
    FIKMSPLERR LLIDDISGIA EYDSKKEKAL EELKQAEENL ARVDLLIKEV 200
    KKQLDKLEKE RNDALRYLDL KDKLEKAKVS LLLGEIKILE TQIKEGEKRR 250
    AEIEEEIQKI EKEIEKIGKE IVEKVKVLRE IEERIEKESG EEAIQITKKI 300
    GEVTSKIELT KRNIEVAKEE LEDAQRRLAK TKEELRKVLS EIEKSKGAIT 350
    RWKKRRDALI NEIKKKEEER NVLVVKLGEI DKTFGAAREE FDSVVKELEE 400
    TTRKMYEIEG NIRRLQEEKE KLHSRILFLR AKLPGIKEKI NEFKAVVEDK 450
    RAEISEIEGK LSTIQAKRIK VEKEIEAKSN ELEKVSKELE SSERELIAAE 500
    AQREVRGNRA AEELKRSGIG GIYGTLAELI KVKDEAYALA IEVALGNRAD 550
    NVVVEDELVA EKAIKYLKEH KLGRLTFLPL NKIKPKHVDS SVGLPAVDVI 600
    EYDQKIENAV KFALGDTVIV NSMEEARPHI GKVRMVTIEG ELYERSGAIT 650
    GGHFRARGLA VDTTKLREKV ESLRRRKEAL EGELNSLKIE LRSLENASFE 700
    LRIKLSDEKK ELELASKDLN RLLEEENAVK EEIEESERKI QEIEQKIENE 750
    KSELAKLRGR IQRLERKKEK LKKALENPEA RELMEKIRII DGEISSLKEE 800
    LSRIESRIES LESRLNEELL PRKASLEEEI EGLVNKINAL KNNISENEKA 850
    LELLNKELEK LKSIEENIKG EIRTLREKRK KLEEDISKLR EKKEVLQRKL 900
    QELEIEANTL KVRDAQLNAQ LEEKKYQLTH YDKNLIKSIK EIPLDLEKVK 950
    KEIEKMEEEI RSLEPVNMKA IEDFEIVERR YLELKSKREK LEAEKESIIE 1000
    FINEIEKEKK NVFMRTFEAI SRNFSEIFAK LSPGGSARLI LENPEDPFSG 1050
    GLEIEAKPAG KDVKRIEAMS GGEKALTALA FVFAIQKFKP APFYLFDEID 1100
    AHLDDANVKR VADLIKESSK ESQFIVITLR DVMMANADKI IGVSMRDGVS 1150
    KVVSLSLEKA MKILEEIRKK QGWEHGN 1177
    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

    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 1, 2014
    This is version 83 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