CAZyme Information: MGYG000002132_01084

Basic Information

• Species: Monoglobus sp900542675
• Lineage: Bacteria; Firmicutes_A; Clostridia; Monoglobales; Monoglobaceae; Monoglobus; Monoglobus sp900542675
• CAZyme ID: MGYG000002132_01084
• CAZy Family: PL11
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1323	MGYG000002132_36|CGC1	143043.71	4.2575

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002132	1988610	MAG	United States	North America

• Gene Location: Start: 1422; End: 5393 Strand: +

Full Sequence      

MGRKLVSLVLAVLMVLTAAPVFSAAEPEQAAIVSDTSRQMENLNRGGFAATNPTGGVYLS
WRLLGTEPMDTVFNVYKNGVLFSENLNNTNILDSTGTKDDVYTVAPVIGGTEGEISSAFP
MLTGYANSRNASAPYAYFDIPVQIPEAGTDYTYNTADVGHGESGGPNDASVGDVDGDGEY
EVILKWDPSNSKDSAASGITGLVYLDCYEMDGTLLWRINLGRNIRAGAHYTQFQVFDYDG
DGKAEVAVKTAPGSVDGKGNYVSDAGNTNEIKNTDNTKSYLGSNGHVTGGPEYLTIFNGE
TGAAMQTIDYGAPLGNVRDWGDNSYNRSDRFLAGTAYLDGVHPSILMCRGYYGKSVIMAY
DWDGENLTQRWKLDSTSSSSNKFYGQGNHNLSIADLDNDGKDEIIYGSCAVDDNGTLLWS
TGLGHGDALHVSDFDGDGKQEIYKVLEDKPHWGETYIEGDGTVVWHITSQTADKDGDRDD
GRGIMGNFSPKYGVLAWDARNGICTIDGAVSGKGGNISKKTSQDNSWSSANFNIYWDGDL
YEEHFDGNRISKWNDYEEANADGDLGGFGRFWDIPGIAYNNTTKRNPCLQADLFGDWREE
LILRTNDNSSLRVFTSLATTDYKFTTFMHDSQYRCAVAWQNTGYNQPPHQSYYIGYDKSE
KEVTEYTQPDIAVRPLDPETAVTVKNADGTPAVGVKVNLGGIEKPTNSEGVVYYRLAAGT
YSYSINQAGYYDVTGSVNVSADSANLEEVEITELPDSTITVKSGDKTVAGAAVTIGGFTA
VTGTDGKATLKIKPGENDITVECKKYETYTGKVTAPADKGADVSIELTAINYAYDSVNDA
DGKQFEYTGGAGTELTFGGGSWTFNQNSTDGGRSFGSTFKASENGNAEFELKYSTGAVKD
ASDAWNWSGRPYTHYVKLVDIYGSTIIGISQEYTESDGAQETKYFTSDESAKKNVNSGEM
FGGPNITKRSSSKWMLNFKLNLKDKKATLTLSDEAGENGYVVSDIPIDSTSFCQVKIGSE
ASGNVTWSPVIKDVLYWSDCLTDAVPTSPTPAPKPTPEPPLDEANAVVWNLSEEPFVKNG
AVNTSMFPEGTHKTEDNVVDRFNITSTSIVNVNGLTYVTANTDENQFQGSNVTFDDGTAC
NWSLKTSKAGSDTDRVFTYTPAKAGVIRVYAKSGSSSNASGVNVKQGGKTIGSAEYNIGA
AAQMDEFKVQAGSEVKIVTTGNTQYYVLKFVPYCEPLSDVIGYSSAPDLSSKHVTAEIFN
NSTDGTKAIFIAAAYENEVLAEAQTVIAEAGTTPVSIDFEKEYTDVKYFLWNAETYEPYT
YSE

Enzyme Prediction     

No EC number prediction in MGYG000002132_01084.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
PL11	38	664	6.3e-216	0.9914236706689536

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd10318	RGL11	0.0	40	652	1	564	Rhamnogalacturonan lyase of the polysaccharide lyase family 11. The rhamnogalacturonan lyase of the polysaccharide lyase family 11 (RGL11) cleaves glycoside bonds in polygalacturonan as well as RG (rhamnogalacturonan) type-I through a beta-elimination reaction. Functionally characterized members of this family, YesW and YesX from Bacillus subtilis, cleave glycoside bonds between rhamnose and galacturonic acid residues in the RG-I region of plant cell wall pectin. YesW and YesX work synergistically, with YesW cleaving the glycoside bond of the RG chain endolytically, and YesX converting the resultant oligosaccharides through an exotype reaction. This domain is sometimes found in architectures with non-catalytic carbohydrate-binding modules (CBMs). There are two types of RG lyases, which both cleave the alpha-1,4 bonds of the RG-I main chain through a beta-elimination reaction, but belong to two structurally unrelated polysaccharide lyase (PL) families, 4 and 11.
pfam18370	RGI_lyase	6.43e-24	38	119	1	83	Rhamnogalacturonan I lyases beta-sheet domain. This is the beta-sheet domain found in rhamnogalacturonan (RG) lyases, which are responsible for an initial cleavage of the RG type I (RG-I) region of plant cell wall pectin. Polysaccharide lyase family 11 carrying this domain, such as YesW (EC:4.2.2.23) and YesX (EC:4.2.2.24), cleave glycoside bonds between rhamnose and galacturonic acid residues in RG-I through a beta-elimination reaction. Other family members carrying this domain are hemagglutinin A, lysine gingipain (Kgp) and Chitinase C (EC:3.2.1.14).
pfam13715	CarbopepD_reg_2	2.96e-04	758	827	4	76	CarboxypepD_reg-like domain. This domain family is found in bacteria, archaea and eukaryotes, and is approximately 90 amino acids in length. The family is found in association with pfam07715 and pfam00593.
pfam13517	VCBS	0.001	395	443	1	60	Repeat domain in Vibrio, Colwellia, Bradyrhizobium and Shewanella. This domain of about 100 residues is found in multiple (up to 35) copies in long proteins from several species of Vibrio, Colwellia, Bradyrhizobium, and Shewanella (hence the name VCBS) and in smaller copy numbers in proteins from several other bacteria. The large protein size and repeat copy numbers, species distribution, and suggested activities of several member proteins suggests a role for this domain in adhesion (TIGR).
cd11308	Peptidase_M14NE-CP-C_like	0.007	684	739	6	63	Peptidase associated domain: C-terminal domain of M14 N/E carboxypeptidase; putative folding, regulation, or interaction domain. This domain is found C-terminal to the M14 carboxypeptidase (CP) N/E subfamily containing zinc-binding enzymes that hydrolyze single C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. The N/E subfamily includes enzymatically active members (carboxypeptidase N, E, M, D, and Z), as well as non-active members (carboxypeptidase-like protein 1, -2, aortic CP-like protein, and adipocyte enhancer binding protein-1) which lack the critical active site and substrate-binding residues considered necessary for activity. The active N/E enzymes fulfill a variety of cellular functions, including prohormone processing, regulation of peptide hormone activity, alteration of protein-protein or protein-cell interactions and transcriptional regulation. For M14 CPs, it has been suggested that this domain may assist in folding of the CP domain, regulate enzyme activity, or be involved in interactions with other proteins or with membranes; for carboxypeptidase M, it may interact with the bradykinin 1 receptor at the cell surface. This domain may also be found in other peptidase families.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AUO19809.1	0.0	1	1046	1	952
AIQ75296.1	3.02e-181	37	655	6	574
AWV36810.1	3.94e-181	23	655	10	592
QLG37185.1	6.24e-178	37	655	41	608
APO48084.1	1.94e-177	37	655	24	591

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2ZUY_A	3.34e-172	38	655	6	590	Crystalstructure of exotype rhamnogalacturonan lyase YesX [Bacillus subtilis]
2Z8R_A	1.48e-170	37	661	2	575	Crystalstructure of rhamnogalacturonan lyase YesW at 1.40 A resolution [Bacillus subtilis],2Z8R_B Crystal structure of rhamnogalacturonan lyase YesW at 1.40 A resolution [Bacillus subtilis],2Z8S_A Crystal structure of rhamnogalacturonan lyase YesW complexed with digalacturonic acid [Bacillus subtilis],2Z8S_B Crystal structure of rhamnogalacturonan lyase YesW complexed with digalacturonic acid [Bacillus subtilis],2ZUX_A Crystal structure of rhamnogalacturonan lyase YesW complexed with rhamnose [Bacillus subtilis],2ZUX_B Crystal structure of rhamnogalacturonan lyase YesW complexed with rhamnose [Bacillus subtilis]
4CAG_A	1.52e-167	37	655	8	576	Bacilluslicheniformis Rhamnogalacturonan Lyase PL11 [Bacillus licheniformis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O31527	1.41e-171	38	655	6	590	Rhamnogalacturonan exolyase YesX OS=Bacillus subtilis (strain 168) OX=224308 GN=yesX PE=1 SV=1
O31526	2.10e-169	37	661	39	612	Rhamnogalacturonan endolyase YesW OS=Bacillus subtilis (strain 168) OX=224308 GN=yesW PE=1 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
0.000315	0.999024	0.000184	0.000170	0.000153	0.000150

TMHMM  Annotations     

start	end
5	24