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CAZyme Information: MGYG000002224_02154

You are here: Home > Sequence: MGYG000002224_02154

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Faecalibacterium sp900540455
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Faecalibacterium; Faecalibacterium sp900540455
CAZyme ID MGYG000002224_02154
CAZy Family CBM50
CAZyme Description Trifunctional nucleotide phosphoesterase protein YfkN
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
602 MGYG000002224_32|CGC1 65237.97 4.8823
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002224 2335657 MAG United States North America
Gene Location Start: 1942;  End: 3750  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002224_02154.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK09419 PRK09419 5.47e-147 42 594 42 644
multifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase/5'-nucleotidase.
COG0737 UshA 3.82e-85 39 499 24 499
2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or 3'-nucleotidase, 5'-nucleotidase family [Nucleotide transport and metabolism, Defense mechanisms].
cd07410 MPP_CpdB_N 9.45e-85 42 305 1 279
Escherichia coli CpdB and related proteins, N-terminal metallophosphatase domain. CpdB is a bacterial periplasmic protein with an N-terminal metallophosphatase domain and a C-terminal 3'-nucleotidase domain. This alignment model represents the N-terminal metallophosphatase domain, which has 2',3'-cyclic phosphodiesterase activity, hydrolyzing the 2',3'-cyclic phosphates of adenosine, guanosine, cytosine and uridine to yield nucleoside and phosphate. CpdB also hydrolyzes the chromogenic substrates p-nitrophenyl phosphate (PNPP), bis(PNPP) and p-nitrophenyl phosphorylcholine (NPPC). CpdB is thought to play a scavenging role during RNA hydrolysis by converting the non-transportable nucleotides produced by RNaseI to nucleosides which can easily enter a cell for use as a carbon source. This family also includes YfkN, a Bacillus subtilis nucleotide phosphoesterase with two copies of each of the metallophosphatase and 3'-nucleotidase domains. The N-terminal metallophosphatase domain belongs to a large superfamily of distantly related metallophosphatases (MPPs) that includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.
PRK09418 PRK09418 7.60e-61 40 583 38 641
bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase.
PRK09420 cpdB 1.01e-59 39 556 23 598
bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AAO36497.1 6.48e-188 40 598 36 605
CDI50173.1 1.30e-187 40 598 36 605
AVP54978.1 3.68e-187 40 598 36 605
QBD85406.1 7.37e-187 40 598 36 605
SNV84369.1 5.57e-181 40 598 36 605

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3GVE_A 9.29e-31 39 306 9 313
Crystalstructure of calcineurin-like phosphoesterase YfkN from Bacillus subtilis [Bacillus subtilis subsp. subtilis str. 168],3GVE_B Crystal structure of calcineurin-like phosphoesterase YfkN from Bacillus subtilis [Bacillus subtilis subsp. subtilis str. 168]
4Q7F_A 6.15e-26 41 497 19 479
ChainA, 5' nucleotidase family protein [Staphylococcus aureus subsp. aureus COL]
3QFK_A 6.15e-26 41 497 19 479
ChainA, Uncharacterized protein [Staphylococcus aureus subsp. aureus NCTC 8325]
5EQV_A 1.18e-24 40 318 8 319
1.45Angstrom Crystal Structure of Bifunctional 2',3'-cyclic Nucleotide 2'-phosphodiesterase/3'-Nucleotidase Periplasmic Precursor Protein from Yersinia pestis with Phosphate bound to the Active site [Yersinia pestis CO92]
3JYF_A 2.13e-24 40 329 7 329
ChainA, 2',3'-cyclic nucleotide 2'-phosphodiesterase/3'-nucleotidase bifunctional periplasmic protein [Klebsiella pneumoniae subsp. pneumoniae MGH 78578],3JYF_B Chain B, 2',3'-cyclic nucleotide 2'-phosphodiesterase/3'-nucleotidase bifunctional periplasmic protein [Klebsiella pneumoniae subsp. pneumoniae MGH 78578]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
O34313 1.02e-44 39 559 42 616
Trifunctional nucleotide phosphoesterase protein YfkN OS=Bacillus subtilis (strain 168) OX=224308 GN=yfkN PE=1 SV=1
P08331 2.01e-41 40 555 22 595
2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase OS=Escherichia coli (strain K12) OX=83333 GN=cpdB PE=1 SV=2
P53052 2.82e-39 40 559 27 604
2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase OS=Yersinia enterocolitica OX=630 GN=cpdB PE=3 SV=1
P44764 2.94e-39 40 598 32 655
2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=cpdB PE=3 SV=1
P26265 2.27e-38 40 563 22 603
2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=cpdB PE=3 SV=2

SignalP and Lipop Annotations help

This protein is predicted as TAT

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000000 0.000000 0.000000 0.999985 0.000001 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002224_02154.