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Protein
Submitted name:

Metallophosphoesterase

Gene

Cthe_2768

Organism
Clostridium thermocellum (strain ATCC 27405 / DSM 1237 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Ruminiclostridium thermocellum)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei116 – 1161ADPCombined sources
Binding sitei116 – 1161ATPCombined sources
Binding sitei116 – 1161CTPCombined sources
Binding sitei116 – 1161GTPCombined sources
Binding sitei120 – 1201ADPCombined sources
Binding sitei162 – 1621GTPCombined sources
Metal bindingi187 – 1871ManganeseCombined sources
Metal bindingi189 – 1891Manganese; via tele nitrogenCombined sources
Metal bindingi233 – 2331ManganeseCombined sources
Binding sitei531 – 5311ATPCombined sources
Binding sitei536 – 5361ADPCombined sources
Binding sitei536 – 5361AMPCombined sources
Binding sitei536 – 5361ATPCombined sources
Binding sitei565 – 5651ADPCombined sources
Binding sitei565 – 5651ATPCombined sources
Binding sitei607 – 6071ADPCombined sources
Binding sitei607 – 6071AMPCombined sources
Binding sitei607 – 6071ATPCombined sources
Binding sitei687 – 6871AMPCombined sources
Binding sitei704 – 7041ADPCombined sources
Binding sitei704 – 7041AMPCombined sources
Binding sitei704 – 7041ATPCombined sources
Metal bindingi731 – 7311Magnesium; via carbonyl oxygenCombined sources
Metal bindingi734 – 7341Magnesium; via carbonyl oxygenCombined sources
Metal bindingi737 – 7371Magnesium; via carbonyl oxygenCombined sources
Binding sitei769 – 7691AMPCombined sources
Binding sitei774 – 7741ADPCombined sources
Binding sitei774 – 7741AMPCombined sources
Binding sitei774 – 7741ATPCombined sources
Binding sitei792 – 7921ADPCombined sources
Binding sitei792 – 7921AMPCombined sources
Binding sitei792 – 7921ATPCombined sources
Binding sitei824 – 8241ADPCombined sources

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi17 – 237ATPCombined sources
Nucleotide bindingi17 – 237CTPCombined sources
Nucleotide bindingi17 – 237GTPCombined sources
Nucleotide bindingi18 – 236ADPCombined sources
Nucleotide bindingi120 – 1234ATPCombined sources
Nucleotide bindingi120 – 1234CTPCombined sources
Nucleotide bindingi120 – 1234GTPCombined sources
Nucleotide bindingi495 – 4962ADPCombined sources
Nucleotide bindingi529 – 5324AMPCombined sources

GO - Molecular functioni

Complete GO annotation...

Keywords - Ligandi

ATP-bindingCombined sources, GTP-bindingCombined sources, MagnesiumCombined sources, ManganeseCombined sources, Metal-bindingCombined sources, Nucleotide-binding

Enzyme and pathway databases

BioCyciCTHE203119:GIW8-2869-MONOMER.
BRENDAi2.7.1.78. 1530.

Names & Taxonomyi

Protein namesi
Submitted name:
MetallophosphoesteraseImported
Gene namesi
Ordered Locus Names:Cthe_2768Imported
OrganismiClostridium thermocellum (strain ATCC 27405 / DSM 1237 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Ruminiclostridium thermocellum)Imported
Taxonomic identifieri203119 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesRuminococcaceaeRuminiclostridium
ProteomesiUP000002145 Componenti: Chromosome

Interactioni

Protein-protein interaction databases

DIPiDIP-60067N.
STRINGi203119.Cthe_2768.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3TY5X-ray2.40A/B479-870[»]
3TY8X-ray2.60A/B479-870[»]
3TY9X-ray3.12A/B/C/D479-870[»]
4DRFX-ray2.60A/C445-870[»]
4E6NX-ray2.39A/C445-870[»]
4GP6X-ray2.10A/B1-170[»]
4GP7X-ray2.00A/B1-170[»]
4J6OX-ray1.60A/B171-424[»]
4JSTX-ray2.03A/B1-170[»]
4JSYX-ray2.14A/B1-170[»]
4JT2X-ray2.49A/B1-170[»]
4JT4X-ray2.01A/B1-170[»]
4MDEX-ray1.80A/B1-170[»]
4MDFX-ray1.73A/B1-170[»]
4QM6X-ray1.50A/B1-170[»]
4QM7X-ray1.80A/B1-170[»]
ProteinModelPortaliA3DJ38.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

eggNOGiCOG0639.
HOGENOMiHOG000245786.
KOiK01090.
OMAiVCEEKHM.
OrthoDBiEOG6WX4P8.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
3.60.21.10. 1 hit.
InterProiIPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR027417. P-loop_NTPase.
IPR024028. PNKP_bac.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamiPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSiPR00114. STPHPHTASE.
SMARTiSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
SSF56300. SSF56300. 1 hit.
TIGRFAMsiTIGR04075. bacter_Pnkp. 1 hit.

Sequencei

Sequence statusi: Complete.

A3DJ38-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLTIPELSL VVLIGSSGSG KSTFAKKHFK PTEVISSDFC RGLVSDDEND
60 70 80 90 100
QTVTGAAFDV LHYIVSKRLQ LGKLTVVDAT NVQESARKPL IEIAKDYHCF
110 120 130 140 150
PVAVVFNLPE KVCQERNKNR TDRQVEEYVI RKHTQQLKKS IKGLQREGFR
160 170 180 190 200
YVYILNSPEE VEEVVFERQP LWNNKKDEHG PFDIIGDIHG CYDELKMLLE
210 220 230 240 250
KLGYLIEEVE GGVGSGKYRV THPEGRKVLF LGDLVDRGPK ITEVLKLVMG
260 270 280 290 300
MVKSGIALCV PGNHDVKLLR KLNGRDVQIT HGLDRTLEQL AKEPQEFIEE
310 320 330 340 350
VKAFIDGLVS HYVLDDGKLV VAHAGMKEEF QGRGSGKVRE FALYGETTGE
360 370 380 390 400
TDEYGLPVRY DWASDYRGKA LVVYGHTPQA EVLKVNNTIN IDTGCVFGGK
410 420 430 440 450
LTAYRYPERE IVDVKALKTY YEPAKPFLPK EDMAERFEAR TDNDILDIND
460 470 480 490 500
VLGKKIITTR LMSSITIHEE NSIAALEVMS RFAADPHWLI YLPPTMSPCE
510 520 530 540 550
TSKKEGMLEH PIEAFEYFRT RGVGKVVCEQ KHMGSRAVVI VCKDSQVAEK
560 570 580 590 600
RFGVLDGTAG ICYTRTGRHF FDDMQLEAEL IDRVRKVLDK SGFWGDFNTD
610 620 630 640 650
WVCLDCELMP WSAKAQKLLE EQYSAVGISG RVVLDEAVKL LKQASLNKTV
660 670 680 690 700
SFDVSRQTSG KNADINELLQ RFTERSEMMQ KYVEAYRKYC WPVNSIDDLK
710 720 730 740 750
LAPFHILATE GKVHSDKNHI WHMDTIAKYC TQDDSLIMAT NHILVDVTDA
760 770 780 790 800
ESVDKGIKWW EDLTASGGEG MVVKPYDFIV KNGRELLQPA VKCRGREYLR
810 820 830 840 850
IIYGPEYTMD ENIERLRNRA VGKKRSLALR EFSLGMEALE RFVRNEPLYR
860 870
VHECVFGVLA LESEPVDPRL
Length:870
Mass (Da):98,776
Last modified:March 20, 2007 - v1
Checksum:i11CA5878DD2919E9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000568 Genomic DNA. Translation: ABN53967.1.
RefSeqiWP_020457916.1. NC_009012.1.
YP_001039160.1. NC_009012.1.

Genome annotation databases

EnsemblBacteriaiABN53967; ABN53967; Cthe_2768.
KEGGicth:Cthe_2768.
PATRICi19519588. VBICloThe47081_2947.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000568 Genomic DNA. Translation: ABN53967.1.
RefSeqiWP_020457916.1. NC_009012.1.
YP_001039160.1. NC_009012.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3TY5X-ray2.40A/B479-870[»]
3TY8X-ray2.60A/B479-870[»]
3TY9X-ray3.12A/B/C/D479-870[»]
4DRFX-ray2.60A/C445-870[»]
4E6NX-ray2.39A/C445-870[»]
4GP6X-ray2.10A/B1-170[»]
4GP7X-ray2.00A/B1-170[»]
4J6OX-ray1.60A/B171-424[»]
4JSTX-ray2.03A/B1-170[»]
4JSYX-ray2.14A/B1-170[»]
4JT2X-ray2.49A/B1-170[»]
4JT4X-ray2.01A/B1-170[»]
4MDEX-ray1.80A/B1-170[»]
4MDFX-ray1.73A/B1-170[»]
4QM6X-ray1.50A/B1-170[»]
4QM7X-ray1.80A/B1-170[»]
ProteinModelPortaliA3DJ38.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-60067N.
STRINGi203119.Cthe_2768.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABN53967; ABN53967; Cthe_2768.
KEGGicth:Cthe_2768.
PATRICi19519588. VBICloThe47081_2947.

Phylogenomic databases

eggNOGiCOG0639.
HOGENOMiHOG000245786.
KOiK01090.
OMAiVCEEKHM.
OrthoDBiEOG6WX4P8.

Enzyme and pathway databases

BioCyciCTHE203119:GIW8-2869-MONOMER.
BRENDAi2.7.1.78. 1530.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
3.60.21.10. 1 hit.
InterProiIPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR027417. P-loop_NTPase.
IPR024028. PNKP_bac.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamiPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSiPR00114. STPHPHTASE.
SMARTiSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
SSF56300. SSF56300. 1 hit.
TIGRFAMsiTIGR04075. bacter_Pnkp. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 27405 / DSM 1237 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372Imported.
  2. "The adenylyltransferase domain of bacterial Pnkp defines a unique RNA ligase family."
    Smith P., Wang L.K., Nair P.A., Shuman S.
    Proc. Natl. Acad. Sci. U.S.A. 109:2296-2301(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 479-870 IN COMPLEX WITH ADP; AMP; ATP AND MAGNESIUM.
  3. "Molecular basis of bacterial protein Hen1 activating the ligase activity of bacterial protein Pnkp for RNA repair."
    Wang P., Chan C.M., Christensen D., Zhang C., Selvadurai K., Huang R.H.
    Proc. Natl. Acad. Sci. U.S.A. 109:13248-13253(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.39 ANGSTROMS) OF 445-870 IN COMPLEX WITH AMP.
  4. "Structure and mechanism of the polynucleotide kinase component of the bacterial Pnkp-Hen1 RNA repair system."
    Wang L.K., Das U., Smith P., Shuman S.
    RNA 18:2277-2286(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-170 IN COMPLEX WITH ADP AND ATP.
  5. "Structural and biochemical analysis of the phosphate donor specificity of the polynucleotide kinase component of the bacterial pnkphen1 RNA repair system."
    Das U., Wang L.K., Smith P., Shuman S.
    Biochemistry 52:4734-4743(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) OF 1-170 IN COMPLEX WITH CTP AND GTP.
  6. "Structure and mechanism of the 2',3' phosphatase component of the bacterial Pnkp-Hen1 RNA repair system."
    Wang L.K., Smith P., Shuman S.
    Nucleic Acids Res. 41:5864-5873(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 171-424 IN COMPLEX WITH MANGANESE.
  7. "Structures of bacterial polynucleotide kinase in a michaelis complex with nucleoside triphosphate (NTP)-Mg2+ and 5'-OH RNA and a mixed substrate-product complex with NTP-Mg2+ and a 5'-phosphorylated oligonucleotide."
    Das U., Wang L.K., Smith P., Munir A., Shuman S.
    J. Bacteriol. 196:4285-4292(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 1-170 IN COMPLEX WITH GTP.
  8. "Structures of bacterial polynucleotide kinase in a Michaelis complex with GTPMg2+ and 5'-OH oligonucleotide and a product complex with GDPMg2+ and 5'-PO4 oligonucleotide reveal a mechanism of general acid-base catalysis and the determinants of phosphoacceptor recognition."
    Das U., Wang L.K., Smith P., Jacewicz A., Shuman S.
    Nucleic Acids Res. 42:1152-1161(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF 1-170 IN COMPLEX WITH GTP.

Entry informationi

Entry nameiA3DJ38_CLOTH
AccessioniPrimary (citable) accession number: A3DJ38
Entry historyi
Integrated into UniProtKB/TrEMBL: March 20, 2007
Last sequence update: March 20, 2007
Last modified: May 27, 2015
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteome, Reference proteomeImported

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.