CAZyme Information: MGYG000000720_01068

Basic Information

• Lineage: Bacteria; Verrucomicrobiota; Lentisphaeria; Victivallales; Victivallaceae; Victivallis
• CAZyme ID: MGYG000000720_01068
• CAZy Family: GH50
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
905		101518.18	7.0545

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000720	3759035	MAG	Kazakhstan	Asia

• Gene Location: Start: 17820; End: 20537 Strand: -

Full Sequence      

MKSLLLFLVACLFCVTAPAAVKLTASGIEVDGGAMGKLTFRYPKFTPQGGKDVKPEVKFV
DDARVEISYLTEAAPAIVLTRDGDTVTGILTTKSAGKLYWEMHIPITFAGAGFFSFGANG
EKKPFPKNLPEKPHLLQANGNALQLFDGNSDCSISIRIDPGAYWQLQDNRAWKWKIFQLS
LLQDVYENRREQKISFNFGAEQPKVAKVRVDRFGQPTDLDFPGKVHSEQELKNDVAADKA
YFDSLKPPARTAWGGMPGSREKFNLKATGFFRTDKVAGRDILVTPEGDVFFQLGVCSVSP
CDDYTYTGGREQIYAWLPKYESEFKTAYRGHWATEFSYYLANRIRKTGKPFVLDEWKAEQ
IDRLRKWGFNSDGAFTAYSKVNRGKKFGRVPGLYKSKGLIGDICDPFDPAIREDLDRNFS
KLADSKDDPTIIGYFIANEQPYPEVARMVPGFDGKVAAKRELVRMLQKKYRSIETFNAAW
NLKASSFEELNDLPLPVQTREAWTDMEAYAAHFFDAYFKLIGETFRKYDPNHLLIGARFL
VANANVESAVAACGKYCDIFSYNYYTRAIDPALLDRIHRLSGEPIILSEWSYGTGEQGLS
GGVVDVRNQIERGKAYRSYVEEAASLPYVVGSQWFAYIDQALTGRFFQHYNGECMNIGLV
NVADRPFKEFLALAMETNYRIYDVLFGKVEPFVWRAEGSVGERAAKSVQIPHAVAGHKLD
GIRQPWPGRPSERIDGSCLVDGAEDGGVSADFWLCWDKENLYLFAEVRDPSPARNSRKEK
HLWQSDCIELFIGAEELEKGGPLLFSDRQILISAEPSKGGAWVMNQPSQPKIPVVVTPNS
QGYAMEAAVPWSALGIKPESGRKIRFDIGLDDGDDGPRRLRQFMWSGRSGNSAERTHWGT
ATLVD

Enzyme Prediction     

No EC number prediction in MGYG000000720_01068.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH50	210	682	1.9e-98	0.7718223583460949
CBM9	738	903	6e-27	0.8846153846153846

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd09619	CBM9_like_4	2.03e-19	711	866	1	153	DOMON-like type 9 carbohydrate binding module. Family 9 carbohydrate-binding modules (CBM9) play a role in the microbial degradation of cellulose and hemicellulose (materials found in plants). The domain has previously been called cellulose-binding domain. The polysaccharide binding sites of CBMs with available 3D structure have been found to be either flat surfaces with interactions formed by predominantly aromatic residues (tryptophan and tyrosine), or extended shallow grooves. CBM9 domains found in this uncharacterized heterogeneous subfamily are often located at the C-terminus of longer proteins and may co-occur with various other domains.
cd09621	CBM9_like_5	6.21e-12	742	866	24	152	DOMON-like type 9 carbohydrate binding module. Family 9 carbohydrate-binding modules (CBM9) play a role in the microbial degradation of cellulose and hemicellulose (materials found in plants). The domain has previously been called cellulose-binding domain. The polysaccharide binding sites of CBMs with available 3D structure have been found to be either flat surfaces with interactions formed by predominantly aromatic residues (tryptophan and tyrosine), or extended shallow grooves. CBM9 domains found in this uncharacterized heterogeneous subfamily are often located at the C-terminus of longer proteins and may co-occur with various other functional domains such as glycosyl hydrolases. The CBM9 module in these architectures may be involved in binding to carbohydrates.
cd00005	CBM9_like_1	3.86e-11	746	904	35	185	DOMON-like type 9 carbohydrate binding module of xylanases. Family 9 carbohydrate-binding modules (CBM9) play a role in the microbial degradation of cellulose and hemicellulose (materials found in plants). The domain has previously been called cellulose-binding domain. The polysaccharide binding sites of CBMs with available 3D structure have been found to be either flat surfaces with interactions formed by predominantly aromatic residues (tryptophan and tyrosine), or extended shallow grooves. The CBM9 domain frequently occurs in tandem repeats; members found in this subfamily typically co-occur with glycosyl hydrolase family 10 domains and are annotated as endo-1,4-beta-xylanases. CBM9 from Thermotoga maritima xylanase 10A is reported to have specificity for polysaccharide reducing ends.
cd09620	CBM9_like_3	2.09e-08	754	866	36	166	DOMON-like type 9 carbohydrate binding module. Family 9 carbohydrate-binding modules (CBM9) play a role in the microbial degradation of cellulose and hemicellulose (materials found in plants). The domain has previously been called cellulose-binding domain. The polysaccharide binding sites of CBMs with available 3D structure have been found to be either flat surfaces with interactions formed by predominantly aromatic residues (tryptophan and tyrosine), or extended shallow grooves. CBM9 domains found in this uncharacterized heterogeneous subfamily may co-occur with various other domains.
cd00241	DOMON_like	4.72e-08	742	859	12	132	Domon-like ligand-binding domains. DOMON-like domains can be found in all three kindgoms of life and are a diverse group of ligand binding domains that have been shown to interact with sugars and hemes. DOMON domains were initially thought to confer protein-protein interactions. They were subsequently found as a heme-binding motif in cellobiose dehydrogenase, an extracellular fungal oxidoreductase that degrades both lignin and cellulose, and in ethylbenzene dehydrogenase, an enzyme that aids in the anaerobic degradation of hydrocarbons. The domain interacts with sugars in the type 9 carbohydrate binding modules (CBM9), which are present in a variety of glycosyl hydrolases, and it can also be found at the N-terminus of sensor histidine kinases.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AVM47142.1	0.0	1	905	1	906
SDU06021.1	1.85e-222	27	903	46	937
SDU02961.1	9.55e-211	18	905	23	940
AHF90550.1	3.38e-192	210	904	1	717
SDT95096.1	2.16e-182	206	904	34	756

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4BQ2_A	1.71e-57	210	687	204	748	Structuralanalysis of an exo-beta-agarase [Saccharophagus degradans 2-40],4BQ2_B Structural analysis of an exo-beta-agarase [Saccharophagus degradans 2-40],4BQ2_C Structural analysis of an exo-beta-agarase [Saccharophagus degradans 2-40],4BQ2_D Structural analysis of an exo-beta-agarase [Saccharophagus degradans 2-40],4BQ3_A Structural analysis of an exo-beta-agarase [Saccharophagus degradans 2-40],4BQ3_B Structural analysis of an exo-beta-agarase [Saccharophagus degradans 2-40],4BQ3_C Structural analysis of an exo-beta-agarase [Saccharophagus degradans 2-40],4BQ3_D Structural analysis of an exo-beta-agarase [Saccharophagus degradans 2-40]
4BQ4_A	4.27e-57	210	687	204	748	Structuralanalysis of an exo-beta-agarase [Saccharophagus degradans 2-40],4BQ4_B Structural analysis of an exo-beta-agarase [Saccharophagus degradans 2-40],4BQ5_A Structural analysis of an exo-beta-agarase [Saccharophagus degradans 2-40],4BQ5_B Structural analysis of an exo-beta-agarase [Saccharophagus degradans 2-40]
6XJ9_A	2.20e-54	210	688	223	765	Structureof PfGH50B [Pseudoalteromonas fuliginea],6XJ9_B Structure of PfGH50B [Pseudoalteromonas fuliginea]
5Z6P_A	8.65e-48	200	686	213	763	Thecrystal structure of an agarase, AgWH50C [Agarivorans gilvus],5Z6P_B The crystal structure of an agarase, AgWH50C [Agarivorans gilvus]
5T3B_A	5.85e-09	266	685	96	476	ChainA, Glycoside Hydrolase [Phocaeicola plebeius],5T3B_B Chain B, Glycoside Hydrolase [Phocaeicola plebeius]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P48840	3.62e-49	177	688	397	955	Beta-agarase B OS=Vibrio sp. (strain JT0107) OX=47913 GN=agaB PE=3 SV=1
P48839	5.09e-28	211	682	400	913	Beta-agarase A OS=Vibrio sp. (strain JT0107) OX=47913 GN=agaA PE=3 SV=1
Q60042	3.27e-09	719	904	878	1054	Endo-1,4-beta-xylanase A OS=Thermotoga neapolitana OX=2337 GN=xynA 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
0.000318	0.999046	0.000171	0.000150	0.000139	0.000142

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000720_01068.