dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000001416_01683

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Basic Information help

Species

Cellulomonas massiliensis

Lineage

Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Cellulomonadaceae; Cellulomonas; Cellulomonas massiliensis

CAZyme ID

MGYG000001416_01683

CAZy Family

CBM12

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
497	MGYG000001416_1\|CGC25	49855.93	5.7468

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001416	3245988	Isolate	not provided	not provided

Gene Location

Start: 1804985; End: 1806478 Strand: +

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000001416_01683.

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd21112	alphaLP-like	4.16e-66	204	377	1	188	alpha-lytic protease (alpha-LP), a bacterial serine protease of the chymotrypsin family, and similar proteins. This family represents the catalytic domain of alpha-lytic protease (alpha-LP) and its closely-related homologs. Alpha-lytic protease (EC 3.4.21.12; also called alpha-lytic endopeptidase), originally isolated from the myxobacterium Lysobacter enzymogenes, belongs to the MEROPS peptidase family S1, subfamily S1E (streptogrisin A subfamily). It is synthesized as a pro-enzyme, thus having two domains; the N-terminal pro-domain acts as a foldase, required transiently for the correct folding of the protease domain, and also acts as a potent inhibitor of the mature enzyme, while the C-terminal domain catalyzes the cleavage of peptide bonds. Members of the alpha-lytic protease subfamily include Nocardiopsis alba protease (NAPase), a secreted chymotrypsin from the alkaliphile Cellulomonas bogoriensis, streptogrisins (SPG-A, SPG-B, SPG-C, and SPG-D), and Thermobifida fusca protease A (TFPA). These serine proteases have characteristic kinetic stability, exhibited by their extremely slow unfolding kinetics. The active site, characteristic of serine proteases, contains the catalytic triad consisting of serine acting as a nucleophile, aspartate as an electrophile, and histidine as a base, all required for activity. This model represents the C-terminal catalytic domain of alpha-lytic proteases.
pfam00089	Trypsin	1.43e-11	204	374	1	217	Trypsin.
pfam02983	Pro_Al_protease	4.05e-05	131	165	2	36	Alpha-lytic protease prodomain.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCJ76543.1	7.80e-134	5	383	3	371
ADB33067.1	4.57e-127	8	383	1	371
CCH28016.1	2.86e-126	50	442	39	423
AUI59717.1	1.48e-125	35	383	26	375
QFZ16630.1	9.80e-125	3	437	2	419

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2EA3_A	4.98e-90	203	383	2	183	CrystalStructure Of Cellulomonas Bogoriensis Chymotrypsin [Cellulomonas bogoriensis]
2PFE_A	3.67e-70	204	382	3	185	ChainA, Alkaline serine protease [Thermobifida fusca YX],2PFE_B Chain B, Alkaline serine protease [Thermobifida fusca YX]
2OUA_A	2.41e-56	203	382	2	188	CrystalStructure of Nocardiopsis Protease (NAPase) [Nocardiopsis alba],2OUA_B Crystal Structure of Nocardiopsis Protease (NAPase) [Nocardiopsis alba]
2SFA_A	1.67e-47	204	381	1	191	SerineProteinase From Streptomyces Fradiae Atcc 14544 [Streptomyces fradiae]
1SGD_E	1.52e-45	204	380	1	184	ChainE, Streptogrisin B [Streptomyces griseus],1SGE_E Chain E, Streptogrisin B [Streptomyces griseus],1SGN_E Chain E, Streptogrisin B [Streptomyces griseus],1SGY_E Chain E, Streptogrisin B [Streptomyces griseus],2GKV_E Chain E, Streptogrisin B [Streptomyces griseus],2NU0_E Chain E, Streptogrisin B, Protease B [Streptomyces griseus],2NU1_E Chain E, Streptogrisin B [Streptomyces griseus],2NU2_E Chain E, Streptogrisin B, Protease B [Streptomyces griseus],2NU3_E Chain E, Streptogrisin B, Proteinase B [Streptomyces griseus],2NU4_E Chain E, Streptogrisin B, Proteinase B [Streptomyces griseus],2QA9_E Crystal structure of the second tetrahedral intermediates of SGPB at pH 4.2 [Streptomyces griseus],2QAA_A Crystal structure of the second tetrahedral intermediates of SGPB at pH 7.3 [Streptomyces griseus],2QAA_B Crystal structure of the second tetrahedral intermediates of SGPB at pH 7.3 [Streptomyces griseus],2SGD_E ASP 18 VARIANT OF TURKEY OVOMUCOID INHIBITOR THIRD DOMAIN COMPLEXED WITH STREPTOMYCES GRISEUS PROTEINASE B AT PH 10.7 [Streptomyces griseus],2SGE_E GLU 18 VARIANT OF TURKEY OVOMUCOID INHIBITOR THIRD DOMAIN COMPLEXED WITH STREPTOMYCES GRISEUS PROTEINASE B AT PH 10.7 [Streptomyces griseus],2SGF_E PHE 18 VARIANT OF TURKEY OVOMUCOID INHIBITOR THIRD DOMAIN COMPLEXED WITH STREPTOMYCES GRISEUS PROTEINASE B [Streptomyces griseus],2SGP_E Chain E, PROTEINASE B [Streptomyces griseus],2SGQ_E GLN 18 VARIANT OF TURKEY OVOMUCOID INHIBITOR THIRD DOMAIN COMPLEXED WITH STREPTOMYCES GRISEUS PROTEINASE B AT PH 6.5 [Streptomyces griseus],3SGQ_E Chain E, Streptogrisin B [Streptomyces griseus]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P52320	2.27e-106	1	437	6	440	Streptogrisin-C OS=Streptomyces griseus OX=1911 GN=sprC PE=3 SV=1
P52321	1.27e-49	83	377	88	388	Streptogrisin-D OS=Streptomyces griseus OX=1911 GN=sprD PE=1 SV=1
P00778	7.62e-48	54	382	44	396	Alpha-lytic protease OS=Lysobacter enzymogenes OX=69 GN=alpha-LP PE=1 SV=3
P00777	5.09e-47	150	380	62	298	Streptogrisin-B OS=Streptomyces griseus OX=1911 GN=sprB PE=1 SV=2
Q05308	1.84e-46	51	383	63	397	Serine protease 1 OS=Rarobacter faecitabidus OX=13243 PE=1 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
0.335130	0.601841	0.059026	0.002281	0.000951	0.000762

TMHMM Annotations download full data without filtering help

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