dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000001341_00316

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Basic Information help

Species

Leuconostoc mesenteroides

Lineage

Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Leuconostoc; Leuconostoc mesenteroides

CAZyme ID

MGYG000001341_00316

CAZy Family

CBM50

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
435		43802.01	4.0982

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001341	1638558	Isolate	not provided	not provided

Gene Location

Start: 101408; End: 102715 Strand: -

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000001341_00316.

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd00118	LysM	4.70e-11	30	73	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.
pfam00188	CAP	2.81e-10	337	428	5	105	Cysteine-rich secretory protein family. This is a large family of cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins (CAP) that are found in a wide range of organisms, including prokaryotes and non-vertebrate eukaryotes, The nine subfamilies of the mammalian CAP 'super'family include: the human glioma pathogenesis-related 1 (GLIPR1), Golgi associated pathogenesis related-1 (GAPR1) proteins, peptidase inhibitor 15 (PI15), peptidase inhibitor 16 (PI16), cysteine-rich secretory proteins (CRISPs), CRISP LCCL domain containing 1 (CRISPLD1), CRISP LCCL domain containing 2 (CRISPLD2), mannose receptor like and the R3H domain containing like proteins. Members are most often secreted and have an extracellular endocrine or paracrine function and are involved in processes including the regulation of extracellular matrix and branching morphogenesis, potentially as either proteases or protease inhibitors; in ion channel regulation in fertility; as tumor suppressor or pro-oncogenic genes in tissues including the prostate; and in cell-cell adhesion during fertilisation. The overall protein structural conservation within the CAP 'super'family results in fundamentally similar functions for the CAP domain in all members, yet the diversity outside of this core region dramatically alters the target specificity and, thus, the biological consequences. The Ca++-chelating function would fit with the various signalling processes (e.g. the CRISP proteins) that members of this family are involved in, and also the sequence and structural evidence of a conserved pocket containing two histidines and a glutamate. It also may explain how the cysteine-rich venom protein helothermine blocks the Ca++ transporting ryanodine receptors.
smart00257	LysM	2.34e-09	30	73	1	44	Lysin motif.
cd05379	CAP_bacterial	6.47e-09	329	428	1	108	Bacterial CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain proteins. Little is known about bacterial and archaeal members of the CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain family. The wider family of CAP domain containing proteins includes plant pathogenesis-related protein 1 (PR-1), cysteine-rich secretory proteins (CRISPs), and allergen 5 from vespid venom, among others. Studies of eukaryotic proteins show that CAP domains have several functions, including the binding of cholesterol, lipids and heparan sulfate. This group includes Borrelia burgdorferi outer surface protein BB0689, which does not bind to cholesterol, lipids, or heparan sulfate, and whose function is unknown.
pfam01476	LysM	1.82e-08	33	73	3	42	LysM domain. The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AKP36344.1	3.44e-206	1	435	1	435
QUY15570.1	3.44e-206	1	435	1	435
ARR88781.1	1.06e-204	1	435	1	433
QXC54283.1	6.43e-202	1	435	1	436
AET29735.1	1.22e-199	1	435	1	436

PDB Hits help

has no PDB hit.

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O34669	1.50e-07	6	138	2	128	Cell wall-binding protein YocH OS=Bacillus subtilis (strain 168) OX=224308 GN=yocH PE=1 SV=1
P37710	2.08e-07	33	132	365	473	Autolysin OS=Enterococcus faecalis (strain ATCC 700802 / V583) OX=226185 GN=EF_0799 PE=1 SV=2
O31852	3.39e-07	24	138	22	138	D-gamma-glutamyl-meso-diaminopimelic acid endopeptidase CwlS OS=Bacillus subtilis (strain 168) OX=224308 GN=cwlS PE=1 SV=1
P54421	3.49e-07	25	135	22	133	Probable peptidoglycan endopeptidase LytE OS=Bacillus subtilis (strain 168) OX=224308 GN=lytE PE=1 SV=1
Q49UX4	1.07e-06	30	135	87	199	N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41) OX=342451 GN=sle1 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
0.000244	0.999071	0.000173	0.000179	0.000167	0.000144

TMHMM Annotations help

There is no transmembrane helices in MGYG000001341_00316.