CAZyme Information: MGYG000004304_00892

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; UBA1394
• CAZyme ID: MGYG000004304_00892
• CAZy Family: GH26
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
285		32665.36	3.8933

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004304	1366914	MAG	Israel	Asia

• Gene Location: Start: 2150; End: 3007 Strand: -

Full Sequence      

MLTIDCLAQELLKVQEAGVPILFRPYHEAEGNPGDAWFWWGQDGPEAYKNLWKLLYTTLT
EKYDLHNLIWIYNSYTYASSPEWYPGDEWVDIVGYDKYNCVYNRNDGLSNCPNEDAISGT
FYNLVDLTNNKKLVAMTENDTVPSLKNMEVEKANWLWFCIWYDNGSDNFLTGEDKNNYDT
LKEIYTSDYCITLDELPDWKNYEYQGSAEPAIIPGDLNNDKTVNVFDSILMKKLLMNTEE
ASDVLAASPEDVDGDGVCTVADLTLLNEYLLGKNVNLTTYKPENV

Enzyme Prediction     

No EC number prediction in MGYG000004304_00892.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH26	3	195	2.8e-58	0.5610561056105611

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam02156	Glyco_hydro_26	5.26e-36	4	195	136	311	Glycosyl hydrolase family 26.
COG4124	ManB2	1.92e-10	17	98	178	256	Beta-mannanase [Carbohydrate transport and metabolism].
cd14256	Dockerin_I	7.41e-10	214	271	1	57	Type I dockerin repeat domain. Bacterial cohesin domains bind to a complementary protein domain named dockerin, and this interaction is required for the formation of the cellulosome, a cellulose-degrading complex. The cellulosome consists of scaffoldin, a noncatalytic scaffolding polypeptide, that comprises repeating cohesion modules and a single carbohydrate-binding module (CBM). Specific calcium-dependent interactions between cohesins and dockerins appear to be essential for cellulosome assembly. This subfamily represents type I dockerins, which are responsible for anchoring a variety of enzymatic domains to the complex.
pfam00404	Dockerin_1	2.51e-06	215	271	1	56	Dockerin type I repeat. The dockerin repeat is the binding partner of the cohesin domain pfam00963. The cohesin-dockerin interaction is the crucial interaction for complex formation in the cellulosome. The dockerin repeats, each bearing homology to the EF-hand calcium-binding loop bind calcium.
cd14254	Dockerin_II	3.07e-05	215	271	1	54	Type II dockerin repeat domain. Bacterial cohesin domains bind to a complementary protein domain named dockerin, and this interaction is required for the formation of the cellulosome, a cellulose-degrading complex. The cellulosome consists of scaffoldin, a noncatalytic scaffolding polypeptide, that comprises repeating cohesion modules and a single carbohydrate-binding module (CBM). Specific calcium-dependent interactions between cohesins and dockerins appear to be essential for cellulosome assembly. This subfamily represents type II dockerins, which are responsible for mediating attachment of the cellulosome complex to the bacterial cell wall.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AZK49093.1	1.80e-83	1	274	312	587
QKS59949.1	2.48e-83	2	270	326	592
APO46210.1	2.59e-83	1	279	312	581
QLG42866.1	1.38e-82	1	275	312	584
ABX42494.1	1.86e-82	1	238	312	556

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3ZM8_A	2.05e-44	4	219	279	466	ChainA, Gh26 Endo-beta-1,4-mannanase [Podospora anserina S mat+]
6HPF_A	1.51e-33	4	196	141	310	Structureof Inactive E165Q mutant of fungal non-CBM carrying GH26 endo-b-mannanase from Yunnania penicillata in complex with alpha-62-61-di-galactosyl-mannotriose [Yunnania penicillata]
3WDQ_A	1.89e-28	7	199	181	355	Crystalstructure of beta-mannanase from a symbiotic protist of the termite Reticulitermes speratus [Symbiotic protist of Reticulitermes speratus],3WDR_A Crystal structure of beta-mannanase from a symbiotic protist of the termite Reticulitermes speratus complexed with gluco-manno-oligosaccharide [Symbiotic protist of Reticulitermes speratus]
6HF2_A	6.13e-28	7	163	180	316	Thestructure of BoMan26B, a GH26 beta-mannanase from Bacteroides ovatus [Bacteroides ovatus ATCC 8483],6HF4_A The structure of BoMan26B, a GH26 beta-mannanase from Bacteroides ovatus, complexed with G1M4 [Bacteroides ovatus ATCC 8483]
6D2X_A	1.40e-26	8	196	149	334	Crystalstructure of the GH26 domain from PbGH26-GH5A endo-beta-mannanase/endo-beta-glucanase from Prevotella bryantii [Prevotella bryantii B14]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
G2Q4H7	4.77e-43	4	201	308	481	Mannan endo-1,4-beta-mannosidase OS=Myceliophthora thermophila (strain ATCC 42464 / BCRC 31852 / DSM 1799) OX=573729 GN=Man26A PE=1 SV=1
P49425	5.28e-42	4	217	289	476	Mannan endo-1,4-beta-mannosidase OS=Rhodothermus marinus (strain ATCC 43812 / DSM 4252 / R-10) OX=518766 GN=manA PE=1 SV=3
Q5AWB7	1.24e-35	4	199	181	353	Probable mannan endo-1,4-beta-mannosidase E OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=manE PE=3 SV=1
A2R6F5	1.35e-31	4	193	163	330	Mannan endo-1,4-beta-mannosidase man26A OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=man26A PE=1 SV=1
P55298	7.70e-25	4	205	293	470	Mannan endo-1,4-beta-mannosidase C OS=Piromyces sp. OX=45796 GN=MANC PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000065	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004304_00892.