CAZyme Information: MGYG000000403_00394

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; Monoglobales_A; UBA1381; UBA4716
• CAZyme ID: MGYG000000403_00394
• CAZy Family: CBM9
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1320	MGYG000000403_63|CGC1	146508.41	4.6395

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000403	2138464	MAG	Sweden	Europe

• Gene Location: Start: 1222; End: 5184 Strand: +

Full Sequence      

MKKIIAAAAVAVISFSVCAAAFAQQYKAEGSRYSVQREFTEERYSSYIDDSLILRTGNNR
ALADGYRRNMDTEYQYVMPCRLAEETYIPIKFSLEHLGCEVKKRDDNSLEINAITAEANK
PFNGGKNVVSRYGVLYAAAEDIAKFTGFNIYDDGVLVILSPNKTINNPDEKIINELKAAL
EWRASKMYFGDEGFILGIQIHPKNPDIMYARTDVGGCYRWQPETQTWTQLLNVIPRADHE
LISVLSLMPDPNDTEVVYALVGWGYTNPKTGLLKSYDRGNSWENVLSVPVHGNVATRVSG
ERVAIDPNNSDIVYVGTQNDGLLVSRDGGKTWMQNTAVAKGYNGHGVNIIMFDGRYKNDE
GNTSLIYASVAGKGLYVSEDAGETFKLIKDTPQYPTRIKLVGNTLYVAANARKAIGTPAD
GGGLWKYNSGRWTDITPPLNNIKEGRQGIGAFLVDYTNHDFILASGESWTNNDYERYRSY
DGGKTWECIRTDMGWNLAELVQDPKNPKRALMADGAGLIAIKDIYKKLNGSGDMLECEYQ
ERGMEELVCLKVMSVPHKDAPKLLLSCYDRGFMIAEDPYHRGISQSAEQNMDIGWATDMD
YCNQDPSFVARLGRNSTGNNIALSDDYGRMAKISDAWDRGNACISIALSATVQKNGYPVI
IAGGAKQNGVQGSLYRSKDWGKTWEELDGVKSDASSETWSRYWEYILVSDTVDGKTFYYC
ENSDFYVTKDAGETWSKTVSFKTLDNSFGNPSMAAVPGHEGEVFVRGGGKLWRSTDFGKT
WSKIEGVSFDGRSHFAFGKGKQGSNYPALYVTALINGTRGVYISDDMGKSFRRIDDDSQS
YTIGQEDGIAGDMNVYGRVYVSTANTGVTYYQLAELDDIPPVIEVDNKSTSNDYGIDYAV
IDNKLTIKGNVNEISEVRINNEPVALSENLSFQKEVTLSEGENIYRIEAADEAGNKAKPK
EIKVRYIPDFIELELDNKSETVTKEDSITISGTASTDAEIFVNETTVKTGENNKFSVDYA
LTGDETDIKVYAKRSDGKVSAEKSVRVAVDKTAPAVSVTNLPSEPVIKKNFKLEGKINEP
GYVRINDKDVAVNDDLTFSSYVMVTDAETSFKIQSRDIAGNVSKPEYVTIKRDMSKALDK
SKLNLKYKTDDFVYDGDISEWTLDYETDELYWGETDNMAQFGFMWDEEYLYVAVKVSDNV
IFTGHPDNTRCDAVEVYIDGNNTKGKSYDAHCKQYVFVAGKETANSISKTTGDGYVTEIA
IPWSSVGVTAEQGKEIGVDVNVIDNDNNRSDSGRCGIIGFNGTQNNWLDPSPWSTLTLVK

Enzyme Prediction     

No EC number prediction in MGYG000000403_00394.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CBM9	1167	1318	4.3e-29	0.9065934065934066

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam06452	CBM9_1	7.56e-24	1179	1319	33	182	Carbohydrate family 9 binding domain-like. CBM9_1 is a C-terminal domain on bacterial xylanase proteins, and it is tandemly repeated in a number of family-members. The CBM9 module binds to amorphous and crystalline cellulose and a range of soluble di- and monosaccharides as well as to cello- and xylo- oligomers of different degrees of polymerization. Comparison of the glucose and cellobiose complexes during crystallisation reveals surprising differences in binding of these two substrates by CBM9-2. Cellobiose was found to bind in a distinct orientation from glucose, while still maintaining optimal stacking and electrostatic interactions with the reducing end sugar.
cd09619	CBM9_like_4	2.99e-22	1155	1313	5	186	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.
cd00005	CBM9_like_1	5.35e-20	1179	1319	39	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.
cd00241	DOMON_like	1.13e-11	1162	1290	2	152	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.
pfam15902	Sortilin-Vps10	3.86e-11	672	846	1	176	Sortilin, neurotensin receptor 3,. Sortilin, also known in mammals as neurotensin receptor-3, is the archetypical member of a Vps10-domain (Vps10-D) that binds neurotrophic factors and neuropeptides. This domain constitutes the entire luminal part of Sortilin and is activated in the trans-Golgi network by enzymatic propeptide cleavage. The structure of the domain has been determined as a ten-bladed propeller, with up to 9 BNR or beta-hairpin turns in it. The mature receptor binds various ligands, including its own propeptide (Sort-pro), neurotensin, the pro-forms of nerve growth factor-beta (NGF)6 and brain-derived neurotrophic factor (BDNF)7, lipoprotein lipase (LpL), apo lipoprotein AV14 and the receptor-associated protein (RAP)1.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ANE48490.1	2.83e-143	181	1318	39	1181
ANE48489.1	5.15e-95	190	1318	46	1112
QJC51548.1	1.77e-81	181	1318	41	1353
QGH20147.1	2.10e-78	193	875	53	775
QGH24182.1	2.10e-78	193	875	53	775

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6P2M_A	5.67e-68	174	870	2	690	ChainA, Type 3a cellulose-binding domain protein [Caldicellulosiruptor lactoaceticus 6A]
4LGN_A	1.19e-66	185	874	10	736	Thestructure of Acidothermus cellulolyticus family 74 glycoside hydrolase [Acidothermus cellulolyticus 11B]
2CN2_A	5.85e-66	190	870	20	728	ChainA, BETA-1,4-XYLOGLUCAN HYDROLASE [Acetivibrio thermocellus],2CN2_B Chain B, BETA-1,4-XYLOGLUCAN HYDROLASE [Acetivibrio thermocellus],2CN2_C Chain C, BETA-1,4-XYLOGLUCAN HYDROLASE [Acetivibrio thermocellus],2CN2_D Chain D, BETA-1,4-XYLOGLUCAN HYDROLASE [Acetivibrio thermocellus]
2CN3_A	5.85e-66	190	870	20	728	ChainA, BETA-1,4-XYLOGLUCAN HYDROLASE [Acetivibrio thermocellus],2CN3_B Chain B, BETA-1,4-XYLOGLUCAN HYDROLASE [Acetivibrio thermocellus]
6P2N_A	1.39e-64	193	870	18	744	Crystalstructure of Paenibacillus graminis GH74 (PgGH74) [Paenibacillus graminis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q70DK5	4.31e-67	190	886	47	771	Xyloglucanase Xgh74A OS=Acetivibrio thermocellus OX=1515 GN=xghA PE=1 SV=1
A3DFA0	7.80e-67	190	886	47	771	Xyloglucanase Xgh74A OS=Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) OX=203119 GN=xghA PE=3 SV=1
Q3MUH7	3.67e-61	193	910	50	809	Xyloglucanase OS=Paenibacillus sp. OX=58172 GN=xeg74 PE=1 SV=1
Q5BD38	1.65e-48	193	875	46	810	Oligoxyloglucan-reducing end-specific xyloglucanase OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=xgcA PE=1 SV=1
Q7Z9M8	2.64e-45	178	872	19	744	Xyloglucanase OS=Hypocrea jecorina (strain QM6a) OX=431241 GN=cel74a 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
0.000630	0.668469	0.330141	0.000278	0.000236	0.000213

TMHMM  Annotations     

start	end
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