dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000001443_06134

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Basic Information help

Species

Streptomyces albus

Lineage

Bacteria; Actinobacteriota; Actinomycetia; Streptomycetales; Streptomycetaceae; Streptomyces; Streptomyces albus

CAZyme ID

MGYG000001443_06134

CAZy Family

CBM12

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
467		47667.56	8.362

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001443	7820353	Isolate	not provided	not provided

Gene Location

Start: 208962; End: 210365 Strand: -

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000001443_06134.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
CBM12	423	455	9e-16	0.9411764705882353

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd21112	alphaLP-like	8.33e-66	218	400	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.
cd12214	ChiA1_BD	2.62e-17	423	467	1	45	chitin-binding domain of Chi A1-like proteins. This group contains proteins related to the chitin binding domain of chitinase A1 (ChiA1) of Bacillus circulans WL-12. Glycosidase ChiA1 hydrolyzes chitin and is comprised of several domains: the C-terminal chitin binding domain, an N-terminal and catalytic domain, and 2 fibronectin type III-like domains. Chitinases function in invertebrates in the degradation of old exoskeletons, in fungi to utilize chitin in cell walls, and in bacteria which use chitin as an energy source. Bacillus circulans WL-12 ChiA1 facilitates invasion of fungal cell walls. The ChiAi chitin binding domain is required for the specific recognition of insoluble chitin. although topologically and structurally related, ChiA1 lacks the characteristic aromatic residues of Erwinia chrysanthemi endoglucanase Z (CBD(EGZ)).
pfam00089	Trypsin	5.78e-14	220	396	3	216	Trypsin.
pfam02983	Pro_Al_protease	3.78e-06	145	200	1	57	Alpha-lytic protease prodomain.
smart00495	ChtBD3	4.75e-05	423	464	3	41	Chitin-binding domain type 3.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QID37532.1	5.21e-310	1	467	1	467
QHF92780.1	2.88e-210	15	467	16	471
QNQ35710.1	1.07e-199	16	467	3	457
BAG20889.1	1.23e-198	18	467	5	457
APS20807.1	1.63e-198	18	467	5	455

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2EA3_A	9.50e-74	217	409	2	186	CrystalStructure Of Cellulomonas Bogoriensis Chymotrypsin [Cellulomonas bogoriensis]
2PFE_A	5.03e-66	216	405	1	185	ChainA, Alkaline serine protease [Thermobifida fusca YX],2PFE_B Chain B, Alkaline serine protease [Thermobifida fusca YX]
2OUA_A	6.54e-64	216	405	1	188	CrystalStructure of Nocardiopsis Protease (NAPase) [Nocardiopsis alba],2OUA_B Crystal Structure of Nocardiopsis Protease (NAPase) [Nocardiopsis alba]
3M7T_A	3.70e-44	216	405	1	197	ChainA, Alpha-lytic protease [Lysobacter enzymogenes]
1GBJ_A	1.98e-43	216	405	1	197	ChainA, ALPHA-LYTIC PROTEASE [Lysobacter enzymogenes],1GBK_A Alpha-lytic Protease With Met 190 Replaced By Ala Complex With Methoxysuccinyl-ala-ala-pro-alanine Boronic Acid [Lysobacter enzymogenes],1GBL_A Chain A, ALPHA-LYTIC PROTEASE [Lysobacter enzymogenes],1GBM_A Chain A, ALPHA-LYTIC PROTEASE [Lysobacter enzymogenes],2LPR_A Structural Basis For Broad Specificity In Alpha-Lytic Protease Mutants [Lysobacter enzymogenes],3LPR_A Structural Basis For Broad Specificity In Alpha-Lytic Protease Mutants [Lysobacter enzymogenes]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P52320	2.33e-197	18	467	5	457	Streptogrisin-C OS=Streptomyces griseus OX=1911 GN=sprC PE=3 SV=1
P00778	8.13e-56	63	405	39	396	Alpha-lytic protease OS=Lysobacter enzymogenes OX=69 GN=alpha-LP PE=1 SV=3
P52321	5.43e-44	80	403	73	391	Streptogrisin-D OS=Streptomyces griseus OX=1911 GN=sprD PE=1 SV=1
P00777	2.31e-43	150	403	42	298	Streptogrisin-B OS=Streptomyces griseus OX=1911 GN=sprB PE=1 SV=2
Q05308	7.85e-41	65	406	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
0.049339	0.508985	0.005239	0.406088	0.029669	0.000664

TMHMM Annotations help

There is no transmembrane helices in MGYG000001443_06134.