CAZyme Information: MGYG000000104_01044

Basic Information

• Species: Clostridium cuniculi
• Lineage: Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium; Clostridium cuniculi
• CAZyme ID: MGYG000000104_01044
• CAZy Family: GH85
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1800	MGYG000000104_5|CGC3	200542.89	4.0675

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000104	3679160	Isolate	Canada	North America

• Gene Location: Start: 127022; End: 132424 Strand: -

Full Sequence      

MIRRNENIKRLVAMAMAATVTTGLLASFPQVAYAGDTLPYEGESAKGENQPYAHGYRVYD
IKEWSPETDVFGPYMRAQVPLQERNEAFAATQANPELDPSTEFFSLSGDYGNAFFDSYQS
TNEFSQYLFNFWQYTDYYGSWHGTPTAEVPEELYDANASWEYRYFEFGILNLPNPAYTNA
AHKNGALSLGCIFLPREGQYHSPMLEKDENGNFPVADKLAEMCEYYGFDGYFINQEESIE
LEEVDLYKEFMVYLREKGVYVQWYDSIVDTTGALAYENEFNEDNDSFIKDKNFGNEEDNY
RIADSIFLNYWWNHDMLKSSKETAEDLGVDPKTTVFAGIEGGGDRFNQKYDLRDNLDENG
QPMNSIAMIGGEFVHDGLDEDLGDWTQLRRQDDDYQWMTVDRERMWYSGVNQDPTEVVRD
SSYEREEIGVTETTKWDGVSAYITERSVINGTNFITNFNTGHGLDYMINGEKSNDEEWSN
INIQDILPTWQWWIDTDGSRLGVEFDYGTEYTKDTEDTYTQIGAYNGGSSLVINGKLDSE
NLLRLYKTDLDVNKDSKASITFQKISEDTTSKMKLALIFKDDAENVVYLDIDNSTNKSNG
WITSKVDLSEFAGRQIATIGLAFESSETVNDYQINIGQLSVTDGTAAKPEAPTGFKITSA
ISDTKELFVEWDLDDYDTVKQYNLYAVDKDGNDMYLGGSYDSAYYIKNIPTDTVTLKLTA
VGADGTESEAATTNYDFTSKVSNIKTEENMGYIDVTWDNPDVDFESIKLEVNFVYSDKTE
SFETTVNKGETSARIIVPVGDGSRYTLSISTVNYDGTVNQSVDYNSRVADGYSKPYDGEA
ILLPESKVKLTTPSSIDWWHMYIYEDGKAITQTTNGTEYDYYIRGKNSIKSIPVSGSGKL
TIVLEDYRGNMSEPIEVVYGKDSVKAGEITSEHFADDILLNFVKENIGTTVDEVKNYTGK
LDLSNLDITNISGLALFENVEEIDLSNTNIRTIEKQSFSGAVKKISLKDCSELVKVEKNA
FTHAVNLKELDITGCNALEILSANNTTLEKLTYGDVETFKNLISLDLSSSRFDMSEGTLE
RVLADAIDAQNVDSEDIVEKANEKSNLAIGSEIVSTTNPDAYRLVDGVQDVSGYWVIMKA
GDEVVIDLGKEEVIYNWEFVNYNSRSYGVKDLEILVSNDGENFETLSRVNESTKYHRAEV
ENPTAYRYYKLIAHELGTSNGHSYEFKLFGYGDVIYKAGSKYNNQRPVAYQNEIPNNVTI
DMVREVEKLSNKLDITSYLTSYSTINGADFLSLVGEDFVDPNYDLYKETALSDSLYITIT
DRDGNTEITNMIDISKVNTYTANIVEFNTPDYNGKTIATITVNVVNPADTNHLEIALEMI
KSLNEEHYTVDSWNNLQKAVAVAEGVLSNEMATQEEIDSAFTGLIEAKDNLEYAVDKTAL
SLMIDVARELDLTDLTPSSVEALQVAISNAEKVLANENATQEEVNKASQELVDAINNLVE
IIDNSRLVQLVEAAEGLTESKYTASTWANLQLALEDAKEVVANKDATAVDVKEAFDKLSN
SMVKLTLKSNKVALERIISIGNSILNNSDKYVPSTIEGLDKLIKDAEVILNNNEATQNEV
DEIVKELTEKIGNTREKADKTKLITTVTAAKEYDLSLYTEESTAPLKELLGKAEAVLSDD
EVEQATIDALQKGIESALMNLVKVDNIEDVIPDEDGNEGDNENNNDSGSGSNTGNGSDNS
NVNNGSGSAGGNNSSNNGQNNSNKGQNDKLPQTGGVSMSIPLIGGLMAILGGVKLRKKSR

Enzyme Prediction     

No EC number prediction in MGYG000000104_01044.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH85	111	466	2.8e-84	0.9777777777777777

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG4724	COG4724	1.21e-99	20	643	12	551	Endo-beta-N-acetylglucosaminidase D [Carbohydrate transport and metabolism].
cd06547	GH85_ENGase	1.70e-78	106	498	2	339	Endo-beta-N-acetylglucosaminidase (ENGase) hydrolyzes the N-N'-diacetylchitobiosyl core of N-glycosylproteins. The beta-1,4-glycosyl bond located between two N-acetylglucosamine residues is hydrolyzed such that N-acetylglucosamine 1 remains with the protein and N-acetylglucosamine 2 forms the reducing end of the released glycan. ENGase is a key enzyme in the processing of free oligosaccharides in the cytosol of eukaryotes. Oligosaccharides formed in the lumen of the endoplasmic reticulum are transported into the cytosol where they are catabolized by cytosolic ENGases and other enzymes, possibly to maximize the reutilization of the component sugars. ENGases have an eight-stranded alpha/beta barrel topology and are classified as a family 85 glycosyl hydrolase (GH85) domain. The GH85 ENGases are sequence-similar to the family 18 glycosyl hydrolases, also known as GH18 chitinases. An ENGase-like protein is also found in bacteria and is included in this alignment model.
pfam03644	Glyco_hydro_85	3.35e-76	121	463	2	291	Glycosyl hydrolase family 85. Family of endo-beta-N-acetylglucosaminidases. These enzymes work on a broad spectrum of substrates.
sd00033	LRR_RI	1.56e-08	960	1069	3	128	leucine-rich repeats, ribonuclease inhibitor (RI)-like subfamily. A leucine-rich repeat (LRR) is a structural protein motif of 20-30 amino acids that is unusually rich in the hydrophobic amino acid leucine. The conserved eleven-residue sequence motif (LxxLxLxxN/CxL) within the LRRs corresponds to the beta-strand and adjacent loop regions, whereas the remaining parts of the repeats are variable. LRRs fold together to form a solenoid protein domain, termed leucine-rich repeat domain. Leucine-rich repeats are usually involved in protein-protein interactions.
sd00031	LRR_1	4.01e-08	961	1069	4	104	leucine-rich repeats. A leucine-rich repeat (LRR) is a structural protein motif of 20-30 amino acids that is unusually rich in the hydrophobic amino acid leucine. The conserved eleven-residue sequence motif (LxxLxLxxN/CxL) within the LRRs corresponds to the beta-strand and adjacent loop regions, whereas the remaining parts of the repeats are variable. LRRs fold together to form a solenoid protein domain, termed leucine-rich repeat domain. Leucine-rich repeats are usually involved in protein-protein interactions.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AUS27834.1	2.08e-314	13	912	10	910
AHM67228.1	2.08e-314	13	912	10	910
AIY08018.1	2.08e-314	13	912	10	910
APB70257.1	5.84e-314	13	912	10	910
QDA28322.1	4.59e-313	13	912	10	910

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2W91_A	2.35e-62	60	737	19	634	Structureof a Streptococcus pneumoniae family 85 glycoside hydrolase, Endo-D. [Streptococcus pneumoniae TIGR4],2W92_A Structure of a Streptococcus pneumoniae family 85 glycoside hydrolase, Endo-D, in complex with NAG-thiazoline. [Streptococcus pneumoniae TIGR4]
3FHA_A	3.08e-62	49	709	4	586	ChainA, Endo-beta-N-acetylglucosaminidase [Glutamicibacter protophormiae],3FHA_B Chain B, Endo-beta-N-acetylglucosaminidase [Glutamicibacter protophormiae],3FHA_C Chain C, Endo-beta-N-acetylglucosaminidase [Glutamicibacter protophormiae],3FHA_D Chain D, Endo-beta-N-acetylglucosaminidase [Glutamicibacter protophormiae]
3FHQ_A	4.16e-62	49	709	4	586	ChainA, Endo-beta-N-acetylglucosaminidase [Glutamicibacter protophormiae],3FHQ_B Chain B, Endo-beta-N-acetylglucosaminidase [Glutamicibacter protophormiae],3FHQ_D Chain D, Endo-beta-N-acetylglucosaminidase [Glutamicibacter protophormiae],3FHQ_F Chain F, Endo-beta-N-acetylglucosaminidase [Glutamicibacter protophormiae]
2VTF_A	1.52e-61	49	709	9	591	X-raycrystal structure of the Endo-beta-N-acetylglucosaminidase from Arthrobacter protophormiae E173Q mutant reveals a TIM barrel catalytic domain and two ancillary domains [Glutamicibacter protophormiae],2VTF_B X-ray crystal structure of the Endo-beta-N-acetylglucosaminidase from Arthrobacter protophormiae E173Q mutant reveals a TIM barrel catalytic domain and two ancillary domains [Glutamicibacter protophormiae]
3GDB_A	1.44e-60	60	737	170	785	Crystalstructure of Spr0440 glycoside hydrolase domain, Endo-D from Streptococcus pneumoniae R6 [Streptococcus pneumoniae R6]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9SRL4	5.69e-20	164	579	108	479	Cytosolic endo-beta-N-acetylglucosaminidase 2 OS=Arabidopsis thaliana OX=3702 GN=ENGASE2 PE=1 SV=1
F4JZC2	4.01e-17	164	584	103	458	Cytosolic endo-beta-N-acetylglucosaminidase 1 OS=Arabidopsis thaliana OX=3702 GN=ENGASE1 PE=1 SV=1
A1L251	1.50e-15	147	648	124	540	Cytosolic endo-beta-N-acetylglucosaminidase OS=Danio rerio OX=7955 GN=engase PE=2 SV=1
Q8NFI3	2.41e-14	147	540	146	474	Cytosolic endo-beta-N-acetylglucosaminidase OS=Homo sapiens OX=9606 GN=ENGASE PE=1 SV=1
E8MGH9	2.47e-13	1502	1697	1666	1871	Beta-L-arabinobiosidase OS=Bifidobacterium longum subsp. longum (strain ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b) OX=565042 GN=hypBA2 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
0.000590	0.998180	0.000441	0.000371	0.000208	0.000163

TMHMM  Annotations     

start	end
12	34
1773	1795