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A3DJ38

- A3DJ38_CLOTH

UniProt

A3DJ38 - A3DJ38_CLOTH

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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: 1 out of 5- Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. GTP binding Source: UniProtKB-KW
  3. hydrolase activity Source: InterPro
  4. metal ion binding Source: UniProtKB-KW
Complete GO annotation...

Keywords - Ligandi

ATP-bindingImported, GTP-bindingImported, MagnesiumImported, ManganeseImported, Metal-bindingImported, Nucleotide-binding

Enzyme and pathway databases

BioCyciCTHE203119:GIW8-2869-MONOMER.

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: 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.
OMAiHGCRSEL.
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.
GeneIDi4810085.
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 .
RefSeqi WP_020457916.1. NC_009012.1.
YP_001039160.1. NC_009012.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3TY5 X-ray 2.40 A/B 479-870 [» ]
3TY8 X-ray 2.60 A/B 479-870 [» ]
3TY9 X-ray 3.12 A/B/C/D 479-870 [» ]
4DRF X-ray 2.60 A/C 445-870 [» ]
4E6N X-ray 2.39 A/C 445-870 [» ]
4GP6 X-ray 2.10 A/B 1-170 [» ]
4GP7 X-ray 2.00 A/B 1-170 [» ]
4J6O X-ray 1.60 A/B 171-424 [» ]
4JST X-ray 2.03 A/B 1-170 [» ]
4JSY X-ray 2.14 A/B 1-170 [» ]
4JT2 X-ray 2.49 A/B 1-170 [» ]
4JT4 X-ray 2.01 A/B 1-170 [» ]
4MDE X-ray 1.80 A/B 1-170 [» ]
4MDF X-ray 1.73 A/B 1-170 [» ]
4QM6 X-ray 1.50 A/B 1-170 [» ]
4QM7 X-ray 1.80 A/B 1-170 [» ]
ProteinModelPortali A3DJ38.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-60067N.
STRINGi 203119.Cthe_2768.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABN53967 ; ABN53967 ; Cthe_2768 .
GeneIDi 4810085.
KEGGi cth:Cthe_2768.
PATRICi 19519588. VBICloThe47081_2947.

Phylogenomic databases

eggNOGi COG0639.
HOGENOMi HOG000245786.
KOi K01090.
OMAi HGCRSEL.
OrthoDBi EOG6WX4P8.

Enzyme and pathway databases

BioCyci CTHE203119:GIW8-2869-MONOMER.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
3.60.21.10. 1 hit.
InterProi IPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR027417. P-loop_NTPase.
IPR024028. PNKP_bac.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view ]
Pfami PF00149. Metallophos. 1 hit.
[Graphical view ]
PRINTSi PR00114. STPHPHTASE.
SMARTi SM00156. PP2Ac. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
SSF56300. SSF56300. 1 hit.
TIGRFAMsi TIGR04075. bacter_Pnkp. 1 hit.
ProtoNeti Search...

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 pnkp.hen1 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 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. 0:0-0(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 1-170.
  8. "Structures of bacterial polynucleotide kinase in a Michaelis complex with GTP.Mg2+ and 5'-OH oligonucleotide and a product complex with GDP.Mg2+ 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: November 26, 2014
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureImported, Complete proteome, Reference proteomeImported

External Data

Dasty 3