CAZyme Information: MGYG000004712_01328

Basic Information

• Species: Marvinbryantia sp014385005
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Marvinbryantia; Marvinbryantia sp014385005
• CAZyme ID: MGYG000004712_01328
• CAZy Family: GH0
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
199	MGYG000004712_41|CGC1	22290.14	4.7482

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004712	1922596	MAG	China	Asia

• Gene Location: Start: 12287; End: 12886 Strand: +

Full Sequence      

MTAAYRNKGFDFTITSSTAFDHKWIYGRNIFESISEIVDEIFENYLSRPNVKQPILTQYC
DGSRVTCPQWMSQWGSKALGDQGYSAIEILRYYYGDSMYINQAEQVAGIPASWPGYVLAL
GSTGDAVLQIQEQLNAISNNYPLIPRVAVDGIYGPATAEAVRSFQGIFGLTQDGIVGRRT
WYKIQEIYVGVTRIAELNP

Enzyme Prediction     

No EC number prediction in MGYG000004712_01328.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam01471	PG_binding_1	4.43e-15	123	184	1	57	Putative peptidoglycan binding domain. This domain is composed of three alpha helices. This domain is found at the N or C-terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally.
COG3409	PGRP	7.81e-11	117	186	38	104	Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope biogenesis].
COG3409	PGRP	1.14e-09	100	184	103	183	Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope biogenesis].
TIGR02669	SpoIID_LytB	9.97e-06	71	94	237	260	SpoIID/LytB domain. This model describes a domain found typically in two or three proteins per genome in Cyanobacteria and Firmicutes, and sporadically in other genomes. One member is SpoIID of Bacillus subtilis. Another in B. subtilis is the C-terminal half of LytB, encoded immediately upstream of an amidase, the autolysin LytC, to which its N-terminus is homologous. Gene neighborhoods are not well conserved for members of this family, as many, such as SpoIID, are monocistronic. One early modelling-based study suggests a DNA-binding role for SpoIID, but the function of this domain is unknown. [Unknown function, General]
PRK10594	PRK10594	0.001	145	180	301	336	murein L,D-transpeptidase; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AWY98201.1	1.13e-103	2	197	225	420
QEI32542.1	8.49e-103	2	198	234	430
QHB25032.1	8.49e-103	2	198	234	430
QRT31086.1	9.02e-103	2	198	236	432
QCU03784.1	2.01e-102	2	198	226	424

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1LBU_A	2.90e-09	112	187	5	76	HydrolaseMetallo (zn) Dd-peptidase [Streptomyces albus G]
7RUM_A	1.43e-07	117	186	24	87	ChainA, Endolysin [Salmonella phage GEC_vB_GOT],7RUM_B Chain B, Endolysin [Salmonella phage GEC_vB_GOT]
5NM7_A	3.32e-07	118	181	5	62	Crystalstructure of Burkholderia AP3 phage endolysin [Burkholderia],5NM7_G Crystal structure of Burkholderia AP3 phage endolysin [Burkholderia]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P00733	2.29e-08	112	187	47	118	Zinc D-Ala-D-Ala carboxypeptidase OS=Streptomyces albus G OX=1962 PE=1 SV=2
P49320	1.73e-06	101	184	28	105	Uncharacterized protein in bpoA1 3'region (Fragment) OS=Kitasatospora aureofaciens OX=1894 PE=4 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000058	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004712_01328.