CAZyme Information: MGYG000003327_02100

Basic Information

• Species: Lawsonibacter sp900764755
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Oscillospiraceae; Lawsonibacter; Lawsonibacter sp900764755
• CAZyme ID: MGYG000003327_02100
• CAZy Family: CBM50
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
758		83612.15	4.318

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003327	2549294	MAG	United States	North America

• Gene Location: Start: 32983; End: 35259 Strand: -

Full Sequence      

MKVTRTHQWTSLLLSGALVAGMMITPSLAAGGAELEFQYPSDVKAEDVTITVYEGVPADS
GEDAVKALPEVEKNAEGDYLVNEPGTYSYWVRGDGYYNVCKIFNVTQKDLDAGSLKLEVE
TGKMAYTGYEPTSPNLANVPENYDQGARDSLLILWSDEVLDKYFSTDTLKNFKEYDTPFF
TKDRADHQFTTQDEMMSYLTAKDKAEEDMYLYSLGKTPAYQYDMPIAVFTETDLSSAKSL
EEAGELVSANGKLTVWIQSQIHPNEPAAGEGALVMVSDLCGSYGEEVLDDVNVIVIPRIN
PDGSYLFTRATYQGFDMNRDHMALKAPELAYLHTAYRYFMPEVVMDGHEFTFYGVTKDGY
MKNADDMQSTPASSLNNDPLVNQLAEEAVDGLHKNAADSGLRIYHYGTTVNNPIGRAYYG
LYNSISILVETRGIGAGSTNFARRVYSQQNAAHSIIDYAVANDDAINKAVADARAQVTAD
GKVFDAEDTVILQQVASGKTQSPTALTTYQYSMDGSDVKSSSATLSMNDTVVRSRIRPTA
YVIPKDIPNAEKILYILQNQGAEYYELEPGSTAQLKQYYYVGEYTYKEKKAGFTADLRDA
ANVTFEKGAYVIPMDQVSGNVIAMIMEPDINDSNGYDGTLVQYGVVSYDETTKNFPIYRY
EGNDPRTTLVSNAAEKPVEPETPEKPAEPEKPAEPEKPAEPQQPSGSYTVKAGDSLWSIA
QKHLGTGTKWEVIYKANQKLIQNPNQIQIGQVLTIPAA

Enzyme Prediction     

No EC number prediction in MGYG000003327_02100.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CBM50	708	756	7.7e-17	0.975

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06242	M14-like	8.22e-73	252	459	1	220	Peptidase M14-like domain; uncharacterized subgroup. Peptidase M14-like domain of a functionally uncharacterized subgroup of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Two major subfamilies of the M14 family, defined based on sequence and structural homology, are the A/B and N/E subfamilies. Enzymes belonging to the A/B subfamily are normally synthesized as inactive precursors containing preceding signal peptide, followed by an N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The A/B enzymes can be further divided based on their substrate specificity; Carboxypeptidase A-like (CPA-like) enzymes favor hydrophobic residues while carboxypeptidase B-like (CPB-like) enzymes only cleave the basic residues lysine or arginine. The A forms have slightly different specificities, with Carboxypeptidase A1 (CPA1) preferring aliphatic and small aromatic residues, and CPA2 preferring the bulky aromatic side chains. Enzymes belonging to the N/E subfamily enzymes are not produced as inactive precursors and instead rely on their substrate specificity and subcellular compartmentalization to prevent inappropriate cleavages. They contain an extra C-terminal transthyretin-like domain, thought to be involved in folding or formation of oligomers. MCPs can also be classified based on their involvement in specific physiological processes; the pancreatic MCPs participate only in alimentary digestion and include carboxypeptidase A and B (A/B subfamily), while others, namely regulatory MCPs or the N/E subfamily, are involved in more selective reactions, mainly in non-digestive tissues and fluids, acting on blood coagulation/fibrinolysis, inflammation and local anaphylaxis, pro-hormone and neuropeptide processing, cellular response and others. Another MCP subfamily, is that of succinylglutamate desuccinylase /aspartoacylase, which hydrolyzes N-acetyl-L-aspartate (NAA), and deficiency in which is the established cause of Canavan disease. Another subfamily (referred to as subfamily C) includes an exceptional type of activity in the MCP family, that of dipeptidyl-peptidase activity of gamma-glutamyl-(L)-meso-diaminopimelate peptidase I which is involved in bacterial cell wall metabolism.
cd03857	M14-like	1.34e-29	254	446	1	202	Peptidase M14-like domain; uncharacterized subfamily. Peptidase M14-like domain of a functionally uncharacterized subgroup of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Two major subfamilies of the M14 family, defined based on sequence and structural homology, are the A/B and N/E subfamilies. Enzymes belonging to the A/B subfamily are normally synthesized as inactive precursors containing preceding signal peptide, followed by an N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The A/B enzymes can be further divided based on their substrate specificity; Carboxypeptidase A-like (CPA-like) enzymes favor hydrophobic residues while carboxypeptidase B-like (CPB-like) enzymes only cleave the basic residues lysine or arginine. The A forms have slightly different specificities, with Carboxypeptidase A1 (CPA1) preferring aliphatic and small aromatic residues, and CPA2 preferring the bulky aromatic side chains. Enzymes belonging to the N/E subfamily enzymes are not produced as inactive precursors and instead rely on their substrate specificity and subcellular compartmentalization to prevent inappropriate cleavage. They contain an extra C-terminal transthyretin-like domain, thought to be involved in folding or formation of oligomers. MCPs can also be classified based on their involvement in specific physiological processes; the pancreatic MCPs participate only in alimentary digestion and include carboxypeptidase A and B (A/B subfamily), while others, namely regulatory MCPs or the N/E subfamily, are involved in more selective reactions, mainly in non-digestive tissues and fluids, acting on blood coagulation/fibrinolysis, inflammation and local anaphylaxis, pro-hormone and neuropeptide processing, cellular response and others. Another MCP subfamily, is that of succinylglutamate desuccinylase /aspartoacylase, which hydrolyzes N-acetyl-L-aspartate (NAA), and deficiency in which is the established cause of Canavan disease. Another subfamily (referred to as subfamily C) includes an exceptional type of activity in the MCP family, that of dipeptidyl-peptidase activity of gamma-glutamyl-(L)-meso-diaminopimelate peptidase I which is involved in bacterial cell wall metabolism.
PRK11198	PRK11198	2.41e-13	696	757	86	147	LysM domain/BON superfamily protein; Provisional
cd00118	LysM	4.58e-13	707	755	2	45	Lysin Motif is a small domain involved in binding peptidoglycan. LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.
cd00596	Peptidase_M14_like	2.35e-12	255	440	1	202	M14 family of metallocarboxypeptidases and related proteins. The M14 family of metallocarboxypeptidases (MCPs), also known as funnelins, are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Two major subfamilies of the M14 family, defined based on sequence and structural homology, are the A/B and N/E subfamilies. Enzymes belonging to the A/B subfamily are normally synthesized as inactive precursors containing preceding signal peptide, followed by an N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The A/B enzymes can be further divided based on their substrate specificity; Carboxypeptidase A-like (CPA-like) enzymes favor hydrophobic residues while carboxypeptidase B-like (CPB-like) enzymes only cleave the basic residues lysine or arginine. The A forms have slightly different specificities, with Carboxypeptidase A1 (CPA1) preferring aliphatic and small aromatic residues, and CPA2 preferring the bulky aromatic side chains. Enzymes belonging to the N/E subfamily enzymes are not produced as inactive precursors and instead rely on their substrate specificity and subcellular compartmentalization to prevent inappropriate cleavage. They contain an extra C-terminal transthyretin-like domain, thought to be involved in folding or formation of oligomers. MCPs can also be classified based on their involvement in specific physiological processes; the pancreatic MCPs participate only in alimentary digestion and include carboxypeptidase A and B (A/B subfamily), while others, namely regulatory MCPs or the N/E subfamily, are involved in more selective reactions, mainly in non-digestive tissues and fluids, acting on blood coagulation/fibrinolysis, inflammation and local anaphylaxis, pro-hormone and neuropeptide processing, cellular response and others. Another MCP subfamily, is that of succinylglutamate desuccinylase /aspartoacylase, which hydrolyzes N-acetyl-L-aspartate (NAA), and deficiency in which is the established cause of Canavan disease. Another subfamily (referred to as subfamily C) includes an exceptional type of activity in the MCP family, that of dipeptidyl-peptidase activity of gamma-glutamyl-(L)-meso-diaminopimelate peptidase I which is involved in bacterial cell wall metabolism.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QQL05891.1	1.34e-13	707	758	43	94
BAL01252.1	1.67e-13	706	758	623	675
QEY33737.1	4.45e-10	705	756	168	219
BCQ23212.1	6.82e-10	708	758	111	161
ALP92894.1	7.47e-10	705	756	162	214

PDB Hits     

has no PDB hit.

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
B6V866	8.69e-28	196	661	92	538	Carboxypeptidase 2 OS=Trichophyton tonsurans OX=34387 GN=MCPB PE=3 SV=1
B8XGR2	1.16e-27	196	659	92	536	Carboxypeptidase 2 OS=Trichophyton equinum OX=63418 GN=MCPB PE=3 SV=1
A6XHF7	3.73e-26	252	659	126	536	Carboxypeptidase 2 OS=Trichophyton rubrum OX=5551 GN=MCPB PE=2 SV=1
C5FYJ7	2.82e-25	239	659	118	537	Carboxypeptidase 2 OS=Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) OX=554155 GN=MCPB PE=3 SV=1
D4D4Z1	7.62e-25	252	610	126	470	Probable carboxypeptidase 2 OS=Trichophyton verrucosum (strain HKI 0517) OX=663202 GN=MCPB PE=3 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000484	0.998655	0.000221	0.000246	0.000187	0.000160

TMHMM  Annotations     

start	end
9	31