CAZyme Information: MGYG000000134_01072

Basic Information

• Species: Longibaculum muris
• Lineage: Bacteria; Firmicutes; Bacilli; Erysipelotrichales; Erysipelatoclostridiaceae; Longibaculum; Longibaculum muris
• CAZyme ID: MGYG000000134_01072
• CAZy Family: GH136
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1809		203646.93	4.9823

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000134	3162983	Isolate	Canada	North America

• Gene Location: Start: 106278; End: 111707 Strand: -

Full Sequence      

MKWKKGVLKVWTCVLTISLLSNPVYAQGNRQAIKTAVGHTYYVDSVNGSDKNSGMSENEA
FKTLSKINHIELSAGDIVYLKNGSEFNEQLKPKGKGTPANPITITNYGNEKNGMPVINGG
GQIYEGAVNKTSSAVLIENMEYVNVSHLEVTNDDVFNMTDSANDKNNMKGNNQRRIGIHI
TINEDAPTFTANQRAWKGITVENCYVHDVDGDEQRSANKVNGGIGVEVFFRNANKVYPYF
DGVTIASNTIEKVDRTGIKGIRLTELSLADNDGGDSVRYQAVRAEASKNQAGRNFVVRNN
DLKNIGGDGILIDSTIKTVVERNTLFDHTKRSTLANAGIWCWNTQDVLFQYNESYGGPTY
NQDGCSYDCDYNSAGTIFQYNYSHDTPMGFMLLMGGNEMDIVRYNISQNDGVAWRHFSGD
STTKSYIHNNVFYYDGAKWKWSESDNLKNNYEFINNIFYNTNTTTPTTWGKSMDWSKAVF
KTNAVYEASQKNGINEIPDVIHVDPKFKNAGGGETKNWNTLQGYQLKEDSPLINKGSYVY
LDLSGARLLDNRDYYRATQDFFGHPLYVGAPDIGVHEVNSKVSSDLKLEENGTYRLITGD
GCQYLDYSNQKVTLNENKTDEQEYVFIKSTNGYKLKLLNSGLDVLYLSVENGQLKLSEKA
TIWQIEDLKNGLVKIKNGNQALSYDGKNVFISNDKQQDWYLELEENSKSFNCGGSSVEGY
SLDQQWNEEKHISGRYGDVTSIGQGNRDVFSTAIVGQKFGYKFPVTKGSYNVKLSFNEIE
DVKNRTFDILVNGEIYKEQFKIKQKNIVEEIGNVYPKNGVIDIQLVAAYNDDGVKTNGLL
NGISLQKAMSAHTTLNMNCGSSAVDGLSSDAPFPTMGSGYYGDSSSIDFGNAGRPTYDGG
MPTAMQTAREGSEFGYKFKLQPGNYRLKCLFNDGNAKAKEGERVFDIYVNGQLLVSHFDI
VKEAKGNRKGVDLTRFVKSENGILDVKFVGKNGTKALVNVIMVDNLTKEENRENILLNKK
ATCSSKEGSLDANYVVDGSQTTRWGSDFKDNQWIQVDMGQSYLLDTVSIDWTYGAYAKKY
RVEISEDGQKWTSVQNVTDAQPGLNFISFEPTEGRYLRIFGETRNDVWGMSITELGAYGT
KILGTPCVESQVDSNENLYTTTLGIKNIYKRYTTMTVTLDYNVKELEYIGREKYLNPNLK
FIDKNIEDGKIKYNFELMRQNAFDDVSDFMKFDFKAKGVRSPITVHTVLSDAAAHLTALP
EIKVFLPNVIHHSELETLLKQAKEVMDCAEEGRLPGQYRKEDIASFNEVIQEVQKILDQN
LDKEYEKAYTKLESAISDFKNSVLKYQYNHYYKNYSVDKDIDFEFNNASANLKDDKLHIQ
LNGANSTATDLLAPKLNSGTFIVKFDIDSLKDQIRFDLKNTGKSSIQVGYENGRWFWGGA
NNGAWGYFPNIENDLLFTDKTNEVSISFEKQDNGETVLTLIVNGYKVGSVKNTFSNEAGN
YRLWTRYTQKNLYIHEVTYTNAPIYHIDVVGTDNGAISENGKVKVFGETDKTFIFTPNDG
YEVDKVYVDGKEVHSYDKYTFQYIESDHTLKVTFRKVANKNELKDFYDDCLDLLKDNYTS
GSWNQFMNALDKTKDIISANRVTQKEVDESLETLKDAKNSLVLKEADYHKVDEWLAKVPQ
DLSQYTQESVEVLNIALAKVERGLKITEQEKVDFMAEAIENAIKQLEVRKEDKPDIDFKP
DVPIEPSIPDHQGENGDTNNPDNSNTTEIETNNQKEDTTNTGDTTLVTTFVGLGLMSLAG
LLFMRRKED

Enzyme Prediction     

No EC number prediction in MGYG000000134_01072.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH136	38	577	3.4e-149	0.9959266802443992
CBM32	1021	1135	2.4e-24	0.9274193548387096
CBM57	906	1000	7e-19	0.6462585034013606

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam00754	F5_F8_type_C	1.74e-18	1020	1135	1	127	F5/8 type C domain. This domain is also known as the discoidin (DS) domain family.
pfam11721	Malectin	2.99e-13	858	999	6	151	Di-glucose binding within endoplasmic reticulum. Malectin is a membrane-anchored protein of the endoplasmic reticulum that recognizes and binds Glc2-N-glycan. It carries a signal peptide from residues 1-26, a C-terminal transmembrane helix from residues 255-274, and a highly conserved central part of approximately 190 residues followed by an acidic, glutamate-rich region. Carbohydrate-binding is mediated by the four aromatic residues, Y67, Y89, Y116, and F117 and the aspartate at D186. NMR-based ligand-screening studies has shown binding of the protein to maltose and related oligosaccharides, on the basis of which the protein has been designated "malectin", and its endogenous ligand is found to be Glc2-high-mannose N-glycan.
pfam11721	Malectin	2.04e-08	709	843	4	164	Di-glucose binding within endoplasmic reticulum. Malectin is a membrane-anchored protein of the endoplasmic reticulum that recognizes and binds Glc2-N-glycan. It carries a signal peptide from residues 1-26, a C-terminal transmembrane helix from residues 255-274, and a highly conserved central part of approximately 190 residues followed by an acidic, glutamate-rich region. Carbohydrate-binding is mediated by the four aromatic residues, Y67, Y89, Y116, and F117 and the aspartate at D186. NMR-based ligand-screening studies has shown binding of the protein to maltose and related oligosaccharides, on the basis of which the protein has been designated "malectin", and its endogenous ligand is found to be Glc2-high-mannose N-glycan.
cd00057	FA58C	2.30e-08	1013	1119	6	126	Substituted updates: Jan 31, 2002
pfam17132	Glyco_hydro_106	3.29e-06	1017	1119	172	282	alpha-L-rhamnosidase.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AQM59543.1	0.0	37	1598	53	1629
AIY85170.1	0.0	27	1598	43	1629
QIB55408.1	0.0	2	1662	6	1747
QBE95432.1	0.0	2	1662	6	1747
QMW76729.1	0.0	2	1662	6	1747

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5GQC_A	6.43e-50	27	577	6	596	Crystalstructure of lacto-N-biosidase LnbX from Bifidobacterium longum subsp. longum, ligand-free form [Bifidobacterium longum subsp. longum],5GQC_B Crystal structure of lacto-N-biosidase LnbX from Bifidobacterium longum subsp. longum, ligand-free form [Bifidobacterium longum subsp. longum],5GQC_C Crystal structure of lacto-N-biosidase LnbX from Bifidobacterium longum subsp. longum, ligand-free form [Bifidobacterium longum subsp. longum],5GQC_D Crystal structure of lacto-N-biosidase LnbX from Bifidobacterium longum subsp. longum, ligand-free form [Bifidobacterium longum subsp. longum],5GQC_E Crystal structure of lacto-N-biosidase LnbX from Bifidobacterium longum subsp. longum, ligand-free form [Bifidobacterium longum subsp. longum],5GQC_F Crystal structure of lacto-N-biosidase LnbX from Bifidobacterium longum subsp. longum, ligand-free form [Bifidobacterium longum subsp. longum],5GQC_G Crystal structure of lacto-N-biosidase LnbX from Bifidobacterium longum subsp. longum, ligand-free form [Bifidobacterium longum subsp. longum],5GQC_H Crystal structure of lacto-N-biosidase LnbX from Bifidobacterium longum subsp. longum, ligand-free form [Bifidobacterium longum subsp. longum],5GQF_A Crystal structure of lacto-N-biosidase LnbX from Bifidobacterium longum subsp. longum, lacto-N-biose complex [Bifidobacterium longum subsp. longum],5GQF_B Crystal structure of lacto-N-biosidase LnbX from Bifidobacterium longum subsp. longum, lacto-N-biose complex [Bifidobacterium longum subsp. longum],5GQG_A Crystal structure of lacto-N-biosidase LnbX from Bifidobacterium longum subsp. longum, galacto-N-biose complex [Bifidobacterium longum subsp. longum],5GQG_B Crystal structure of lacto-N-biosidase LnbX from Bifidobacterium longum subsp. longum, galacto-N-biose complex [Bifidobacterium longum subsp. longum]
7V6M_A	6.15e-46	34	577	4	576	ChainA, Fibronectin type III domain-containing protein [Tyzzerella nexilis]
7V6I_A	4.47e-45	38	577	13	608	ChainA, Lacto-N-biosidase [Bifidobacterium saguini DSM 23967]
6KQT_A	4.54e-31	38	433	244	638	CrystalStructure of GH136 lacto-N-biosidase from Eubacterium ramulus - native protein [Eubacterium ramulus ATCC 29099]
6KQS_A	6.03e-31	38	433	244	638	CrystalStructure of GH136 lacto-N-biosidase from Eubacterium ramulus - selenomethionine derivative [Eubacterium ramulus ATCC 29099]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9ASQ6	1.75e-06	896	994	471	578	Probable LRR receptor-like serine/threonine-protein kinase At1g29720 OS=Arabidopsis thaliana OX=3702 GN=RFK1 PE=2 SV=3

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
0.000288	0.998977	0.000193	0.000184	0.000171	0.000154

TMHMM  Annotations     

start	end
1784	1803