CAZyme Information: MGYG000002408_03336

Basic Information

• Species: Bacillus_BD tuaregi
• Lineage: Bacteria; Firmicutes; Bacilli; Bacillales_B; DSM-18226; Bacillus_BD; Bacillus_BD tuaregi
• CAZyme ID: MGYG000002408_03336
• CAZy Family: CBM50
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
209	MGYG000002408_16|CGC26	23565.04	9.9934

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002408	4862251	Isolate	not provided	not provided

• Gene Location: Start: 2919879; End: 2920508 Strand: -

Full Sequence      

MKKLVPFLLTILISLSIIPTATNAQSITMFKEPPFEFYKISKGDTFWFIAKRYGLDYKRL
MELNPDTNPYNMQVGGVIRLKESAASVSSFEEEVVRLVNAERAKQGLRSLQHRADVKNVA
EKKAMDMINSNYFSHTSPNYGSPFDMLKTFGISYRSAGENIAKGQKSPQEVMNAWMNSSG
HRANILNPSYNAIGVGFYNGAWVQLFIQS

Enzyme Prediction     

No EC number prediction in MGYG000002408_03336.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
TIGR02909	spore_YkwD	5.56e-65	87	208	1	127	uncharacterized protein, YkwD family. Members of this protein family represent a subset of those belonging to pfam00188 (SCP-like extracellular protein). Based on currently cuttoffs for this model, all member proteins are found in Bacteria capable of endospore formation. Members include a named but uncharacterized protein, YkwD of Bacillus subtilis. Only the C-terminal region is well-conserved and is included in the seed alignment for this model. Three members of this family have an N-terminal domain homologous to the spore coat assembly protein SafA.
COG2340	YkwD	4.52e-43	82	207	72	205	Uncharacterized conserved protein YkwD, contains CAP (CSP/antigen 5/PR1) domain [Function unknown].
cd05379	CAP_bacterial	6.48e-41	91	207	1	120	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.
pfam00188	CAP	1.32e-19	95	206	1	117	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.
cd00118	LysM	2.94e-11	37	80	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QCR31002.1	4.38e-113	1	209	1	209
QOR64956.1	4.00e-106	10	209	9	205
QGQ46532.1	4.14e-106	1	209	2	206
AGK53354.1	1.90e-105	2	209	37	240
QNF30498.1	9.71e-105	1	209	2	206

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4IFA_A	8.07e-17	92	208	222	338	1.5Angstrom resolution crystal structure of an extracellular protein containing a SCP domain from Bacillus anthracis str. Ames [Bacillus anthracis str. Ames]
5K2L_A	1.46e-06	38	80	5	47	Crystalstructure of LysM domain from Volvox carteri chitinase [Volvox carteri f. nagariensis],5YZK_A Solution structure of LysM domain from a chitinase derived from Volvox carteri [Volvox carteri f. nagariensis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O31398	1.21e-45	85	207	131	255	Uncharacterized protein YkwD OS=Bacillus subtilis (strain 168) OX=224308 GN=ykwD PE=3 SV=1
O34586	1.93e-17	91	208	227	344	Uncharacterized membrane protein YlbC OS=Bacillus subtilis (strain 168) OX=224308 GN=ylbC PE=4 SV=1

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
0.000245	0.999082	0.000200	0.000156	0.000152	0.000143

TMHMM  Annotations     

start	end
7	29