dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000001592_01812

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Basic Information help

Species

Intestinimonas sp900540545

Lineage

Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Oscillospiraceae; Intestinimonas; Intestinimonas sp900540545

CAZyme ID

MGYG000001592_01812

CAZy Family

CBM50

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
708	MGYG000001592_24\|CGC1	75712.01	4.2749

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001592	3584489	MAG	China	Asia

Gene Location

Start: 32056; End: 34182 Strand: +

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000001592_01812.

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK09419	PRK09419	8.65e-115	2	567	4	631	multifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase/5'-nucleotidase.
COG0737	UshA	3.87e-79	31	499	24	502	2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or 3'-nucleotidase, 5'-nucleotidase family [Nucleotide transport and metabolism, Defense mechanisms].
cd07410	MPP_CpdB_N	1.24e-70	34	290	1	265	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	3.76e-67	1	542	1	610	bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase.
PRK09420	cpdB	3.57e-58	3	547	2	605	bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AGB41602.1	1.15e-134	2	545	5	547
BAL01252.1	2.04e-106	5	597	4	593
AAO36497.1	5.65e-95	5	569	8	590
SNV84369.1	6.06e-95	4	569	7	590
QUI23903.1	2.90e-94	27	569	78	629

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4Q7F_A	6.61e-42	40	496	26	481	ChainA, 5' nucleotidase family protein [Staphylococcus aureus subsp. aureus COL]
3QFK_A	6.61e-42	40	496	26	481	ChainA, Uncharacterized protein [Staphylococcus aureus subsp. aureus NCTC 8325]
3GVE_A	9.66e-36	25	257	3	251	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]
3JYF_A	1.44e-25	32	264	7	251	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]
5EQV_A	3.61e-25	27	264	3	252	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]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O34313	3.56e-53	3	542	9	612	Trifunctional nucleotide phosphoesterase protein YfkN OS=Bacillus subtilis (strain 168) OX=224308 GN=yfkN PE=1 SV=1
P08331	2.09e-47	6	542	3	598	2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase OS=Escherichia coli (strain K12) OX=83333 GN=cpdB PE=1 SV=2
P53052	1.22e-45	18	545	15	606	2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase OS=Yersinia enterocolitica OX=630 GN=cpdB PE=3 SV=1
P26265	2.45e-44	6	542	3	598	2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=cpdB PE=3 SV=2
P44764	2.17e-41	1	543	1	612	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

SignalP and Lipop Annotations help

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000279	0.998950	0.000204	0.000196	0.000190	0.000166

TMHMM Annotations download full data without filtering help

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