CAZyme Information: MGYG000000119_02513

Basic Information

• Species: Blautia sp000432195
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Blautia; Blautia sp000432195
• CAZyme ID: MGYG000000119_02513
• CAZy Family: GH136
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1494	MGYG000000119_17|CGC2	163018.14	4.5139

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000119	3510293	Isolate	Canada	North America

• Gene Location: Start: 55255; End: 59739 Strand: +

Full Sequence      

MKHIAKKISCIALTAALLAGGMPVQVLADSPKTQQEQLGEVLPQEVLPEEIQPETPEQEG
TGSVLPDGESQMQEETHKPQEPPQEVPQEQPQEQPQEQTEEAPQEPAEEETAEPEEPGRQ
VPQAGTRVLLEDDFQDAGGWKVNKPDAVKIGGGQAVIKGAGPNNAMISNGMIAAQNFLIQ
TDLVIGSGNTNCNAKIGFKAEDGFEGQRLQLRFDFPHNKVFLERVTGNTVNTGYGEAEVT
VSEGTHKLTVEVQDNTITAWLDEQEIITATHDEIGKMEKGKLLFAGQYPAQDFAVANLRV
TTNEQPSGKECKVTLETYTDGVLDAEHKGGTLTADKLSGYSGDYVTLTPKANHGYVFEKY
ETSTDNLVPIENNRFQLNEKFPNITVRAYFKTRVPGKDELFFEDFGGDLGTQPDGIRTQD
GELVVEVADGSSSNAYKPEVDWTKISGNKGYRISADARRMTGESGTIQIAFRGGESFDSR
YVVAINSQGSAMLRKLHNGKNEELKKSGFQMTDKFAHVVIEVKGSEMKLFIDNKEMFSYT
DNGNWSEMQPAVQLINMTAGAPAAFDNLLVEQICEKKPVGVVSIFEGKEDKEHKTGTATS
DVTEAEEGQKVTLTATAKAGYRLKEYQIENVEVKDGTFVMPAGDFEKLVVKAVFETDKVR
EGKTFYVDSENGDNDAEGTSEKTAWKTLDKVKEYGTFVPGDKILLKRGSVFTGQQLAFQG
MGAKGNPIEVSAYGKGALPRLEGNGEVENVVSLYNQEYVEIRNLEITNLDTQYNTKFGLN
ESNNTKKALRAVNVSIRNFGTASGIAIEDCYIHDINGNINLKWNGGVFFDVKADIQNGQL
TGVPSKYDNISISGCTFERVDRSAIKLVSSQWCNQWEKNDPGVPVHWYPSTNVVVEGNYM
EYIGGDGITVRDTDGALIEHNLAKDCRFQNTGYNVGIWPFEAANTVLQYNEAYETHGTTD
GQGLDCDHASSNSVMQYNYSHNNEGGFMLIMGGYPHTGATVRYNISQNDRDKTFEFAQGL
PKGTMIYNNTIYSDQVLDKGVFFLSNTGAGVGVNDGFAFNNVFSYPQGQKAYGGDAKGAG
LVQEHMKIYNNAYTGGMSAFEADAKPLQADDLGIADLGSAPEAHEGKDAVTGSSGLLDGY
KLQEDSVLIDKGLTVDEAWKHFGGNKLVDGRNHSPRELFEEAKAQNYASIDCIMGNNFPQ
VAGVTYDQDFFGGSLAKGKPDIGAAEYQSKEPEKPEPPQTVLLEGISIQKAPEKTTYTEG
ETFNPKGMEVEAKFSDGTTKDVTGEISYSEEPLKAGDKEIIISYTYEGITKEAAQGITVK
TKEEPQPPTPEEPEKPQQPENPDASGWEIEAVEIVPEKAEVKAGESKQFTVEVKGKGEFS
KEVSWELVGKHHEDTYIDEKGTLYVSKAETAGEVKVKVVSKADAKKSDEAVVKIKKAQTQ
VPGTNVNNNGNNTTTGKPAGNQGVQTGDESHVVMLLGLLAVSGGVLLICKRKRQ

Enzyme Prediction     

No EC number prediction in MGYG000000119_02513.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH136	662	1226	2.2e-155	0.9959266802443992

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam13229	Beta_helix	5.22e-10	848	1005	9	133	Right handed beta helix region. This region contains a parallel beta helix region that shares some similarity with Pectate lyases.
pfam18998	Flg_new_2	7.11e-05	596	655	11	71	Divergent InlB B-repeat domain. This family of domains are found in bacterial cell surface proteins. They are often found in tandem array. This domain is closely related to pfam09479.
pfam13229	Beta_helix	7.60e-05	798	983	4	156	Right handed beta helix region. This region contains a parallel beta helix region that shares some similarity with Pectate lyases.
pfam07523	Big_3	2.34e-04	1252	1311	2	61	Bacterial Ig-like domain (group 3). This family consists of bacterial domains with an Ig-like fold. Members of this family are found in a variety of bacterial surface proteins.
cd05865	IgI_1_NCAM-1	0.003	1352	1438	3	97	First immunoglobulin (Ig)-like domain of neural cell adhesion molecule (NCAM-1); member of the I-set of Ig superfamily (IgSF) domains. The members here are composed of the first immunoglobulin (Ig)-like domain of neural cell adhesion molecule (NCAM-1). NCAM-1 plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-nonNCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves the Ig1, Ig2, and Ig3 domains. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AIY03209.1	4.03e-280	124	1233	29	1169
SDS97815.1	4.93e-270	124	1232	48	1190
QLL50162.1	7.16e-198	313	1228	47	979
QLL52630.1	7.16e-198	313	1228	47	979
ALA27928.1	7.16e-198	313	1228	47	979

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7V6M_A	1.29e-58	661	1167	7	566	ChainA, Fibronectin type III domain-containing protein [Tyzzerella nexilis]
5GQC_A	4.21e-52	662	1157	17	571	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]
7V6I_A	5.74e-51	662	1226	13	608	ChainA, Lacto-N-biosidase [Bifidobacterium saguini DSM 23967]
6KQT_A	1.20e-41	662	1009	244	617	CrystalStructure of GH136 lacto-N-biosidase from Eubacterium ramulus - native protein [Eubacterium ramulus ATCC 29099]
6KQS_A	2.85e-41	662	1009	244	617	CrystalStructure of GH136 lacto-N-biosidase from Eubacterium ramulus - selenomethionine derivative [Eubacterium ramulus ATCC 29099]

Swiss-Prot Hits     

has no Swissprot hit.

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
0.000291	0.998959	0.000252	0.000172	0.000170	0.000145

TMHMM  Annotations     

start	end
1472	1489