CAZyme Information: MGYG000001663_01557

Basic Information

• Species: Alistipes sp900760675
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes; Alistipes sp900760675
• CAZyme ID: MGYG000001663_01557
• CAZy Family: PL0
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
528	MGYG000001663_21|CGC1	59415.39	5.1088

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001663	3090424	MAG	United States	North America

• Gene Location: Start: 4970; End: 6556 Strand: -

Full Sequence      

MKRFIFCIAACTALLFTGCSSDDERPVKTPIDPATDIYGVVVDNNGRRLQGVVVSDGYTC
ALTDENGVYQLTASEFAYHVNISLPEAYEVPSDKGLPYFWQKLTEGRKRYDFTLTPLAGG
VENEFNLFCVADPQCQNTTNVARFSNETVPDIAAQVAASTLPCYGITLGDIGWNTANTDY
TNDIFPLMKVAMQQSKVGLPLFQVMGNHDNKVISVTKANYTVEHDIAAQRNFELAFGPVN
YSFNRGSVHVVAMDNIIFPNHNDYSLGFRDDQVEWLKQDLSYVSKDKMVILCTHIPMRNG
TSQNVNEVIALLKSFAEVHIMTGHTHYAENNVYADHYEHVHGAACGAWWNSTINTDGTPN
GYAIYKIKGATIDSWSYKATGLENDFQIRLYRADETFMRDYAKSYKFYYNGGDQIIANIW
NADKDWTIEVYENGVKSGEMTRFEHTGAEKDKSWDAWALGYHIGVVGKNEMVDGKPTDYY
QRNVRHLYYYTLKSASASVEIRATDRFGKTYTQTQFTTGLPEDFPAGE

Enzyme Prediction     

No EC number prediction in MGYG000001663_01557.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam16370	MetallophosC	1.28e-45	340	510	1	156	C terminal of Calcineurin-like phosphoesterase. This is the C-terminal of Calcineurin-like phosphoesterases. It is around 150 residues in length from various Bacteroides species. The function of this family is unknown.
pfam16371	MetallophosN	2.95e-23	45	114	1	73	N terminal of Calcineurin-like phosphoesterase. This is the N-terminal of Calcineurin-like phosphoesterases. It is around 150 residues in length from various Bacteroides species. The function of this family is unknown.
COG1409	CpdA	1.65e-06	195	402	62	268	3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms].
cd00839	MPP_PAPs	2.11e-05	199	297	69	165	purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain. Purple acid phosphatases (PAPs) belong to a diverse family of binuclear metallohydrolases that have been identified and characterized in plants, animals, and fungi. PAPs contain a binuclear metal center and their characteristic pink or purple color derives from a charge-transfer transition between a tyrosine residue and a chromophoric ferric ion within the binuclear center. PAPs catalyze the hydrolysis of a wide range of activated phosphoric acid mono- and di-esters and anhydrides. PAPs are distinguished from the other phosphatases by their insensitivity to L-(+) tartrate inhibition and are therefore also known as tartrate resistant acid phosphatases (TRAPs). While only a few copies of PAP-like genes are present in mammalian and fungal genomes, multiple copies are present in plant genomes. PAPs belong to the metallophosphatase (MPP) superfamily. 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 MPP superfamily 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). 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.
cd07402	MPP_GpdQ	4.54e-04	200	334	71	200	Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain. GpdQ (glycerophosphodiesterase Q, also known as Rv0805 in Mycobacterium tuberculosis) is a binuclear metallophosphoesterase from Enterobacter aerogenes that catalyzes the hydrolysis of mono-, di-, and triester substrates, including some organophosphate pesticides and products of the degradation of nerve agents. The GpdQ homolog, Rv0805, has 2',3'-cyclic nucleotide phosphodiesterase activity. GpdQ and Rv0805 belong to the metallophosphatase (MPP) superfamily. 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 MPP superfamily 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). 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AWI10123.1	1.73e-117	26	526	880	1365
AWI09078.1	2.11e-108	22	526	939	1435

PDB Hits     

has no PDB hit.

Swiss-Prot Hits     

has no Swissprot hit.

SignalP and Lipop Annotations

This protein is predicted as LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000000	0.000000	1.000069	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001663_01557.