CAZyme Information: MGYG000000129_01302

Basic Information

• Species: Marseille-P4683 sp900232885
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; Marseille-P4683; Marseille-P4683 sp900232885
• CAZyme ID: MGYG000000129_01302
• CAZy Family: CBM9
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1643		179280.56	4.122

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000129	2720267	Isolate	Canada	North America

• Gene Location: Start: 75823; End: 80754 Strand: +

Full Sequence      

MKLGKTLKRALSCVLAAAMICVSGVMPTGLAAETDNPLIPSAKPQGSTIKVIDHNVYTGM
TNFDQRSEGAVQLFEKYMPDSIGLQEANVSWMNALKEGLSDHYDCVGVGRENGTNDENSG
EATPIFYLKDKYNLVDSGTFWLSETPDVPSIGWDAMYNRICTWAILENKETGETYAHVNT
HFDHVGSTARIKSMRMIIDFLNTLDMPVVCTGDFNVSEGSDVYNLMLSSGFMQDTKNMAE
KKVNEGGTMSNFGQNDVSGQLPIDFTFVSKDDFKVSLYQVLDEKSNGTYISDHLGIYSEM
TLMAPADTYRAVYGTAQLDGQMDDAYSRAQEVPVNLDSSGDDAAGATGNARTIYDENYIY
SFVQVKDSTPNVNVTDPTNSNYGVDGVQFFYDFKNVDGSAWTTDHSGYFITDLTSSGHWT
SPDGTPGQDIARWAGGFSGFKGDTSKMDFRGVKTDDGYTMEIRVALPDTIRARYAAGEDN
IQIGVGFQINDDQNDDGTRDAMCFDNPSLESAWKGPDYMSNMILAGSPESATDPSVTEKG
YYMAVPGTPTVDGYLDDAYLYAPTIAVNKDGNNAVSTNGAATSTSRVLYDDNYIYVFNDI
KDAAVNDPSTSQPEDNYTNYGIDNVQLFFDFANTDTPLDMADTYTYSSNDGTQKHESGYM
MLYNNEKTPFLTYGFTDYKGDADKLTYKTQRTATGYTVELRLALSDSLKDKLADGQHPKI
GIGFQVNDDTNDDGVRNNTTFSSNRLGDAWTSPIYFEDIVLGEMGGRPSENGDPSSLKNG
ELISTSATEWRYLDNNTDPAAGSDSRTSWTLASFDDSQWKTAKGSFGAKNGQQKDLGDGF
YPNTLLNQYINGKDGDDIPAFFFRSTFEIEDLESLVALDGELLYDDAAIVYINGHKVASF
YEPDGGFDSNLSYGGSNKSDPLTGTFTVTDKSLLNEGVNTIAVELHQGRASSSDIYFDFV
SLKQRGDLDGTAQVKSVSLNVGGDETTRNVTWYSNSTKDGVVQLAEKADMTGDSFPETYQ
EFTATSQAANDSGFNSFFATVEVQPGKEYVYRVGNQQGWSEIYSFETQNISDGFNFLLAG
DPQIGSSGNVGNDTTGWNNTLTQAVKQFPDTSFVLSAGDQVEHASNENEYAGFLSPEILK
SLPLATNVGNHDVGSTSYNQHFNMPNVSSSLGVSGQVGGDYWFRYGNTLIMSINSNQLST
AQHVQFMEDVLKEQGDATWKVVTFHHSIYSTASHSTESDIIGRRNELAPEFSRLGIDVVL
MGHDHVYTRSYMMDGVTPVVPEDGKPASSVTNPEDGQVLYITANSASGSKYYEILSNQAF
PYAAVKEQGHTPSFSNIQVTDSSFTVTTYRSNDLSVIDTFTINKTTDTTAPVITLPEDNE
IQVGDTFDAMEGVTATDDVDGDLTDAIQVEGEVDTQVAGSYDLIYRVSDKAGNEATATRT
VVVKETVSIEASTDKQNYEVGETITLTVVTGSDVRAIGLRNEIGKGLGLTSIKSSNDGLQ
KVWTVQFSVGTKGDRTISIRTRTDSGWQDTGITFNIQVGIPPVSQAEPEIYRADIAADSA
HVNEKFPVIVETSTSVIDVKVRNELGRAMGVQVVGYYDQGDRRIWTLNMEVGTAGSRLFS
FYPVGRDGTMLNASVEDMITIVS

Enzyme Prediction     

No EC number prediction in MGYG000000129_01302.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CBM9	319	524	3.2e-20	0.989010989010989
CBM9	551	761	1.9e-19	0.9945054945054945

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd09083	EEP-1	9.65e-81	50	299	1	251	Exonuclease-Endonuclease-Phosphatase domain; uncharacterized family 1. This family of uncharacterized proteins belongs to a superfamily that includes the catalytic domain (exonuclease/endonuclease/phosphatase, EEP, domain) of a diverse set of proteins including the ExoIII family of apurinic/apyrimidinic (AP) endonucleases, inositol polyphosphate 5-phosphatases (INPP5), neutral sphingomyelinases (nSMases), deadenylases (such as the vertebrate circadian-clock regulated nocturnin), bacterial cytolethal distending toxin B (CdtB), deoxyribonuclease 1 (DNase1), the endonuclease domain of the non-LTR retrotransposon LINE-1, and related domains. These diverse enzymes share a common catalytic mechanism of cleaving phosphodiester bonds. Their substrates range from nucleic acids to phospholipids and perhaps, proteins.
cd00005	CBM9_like_1	9.96e-24	544	761	4	184	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.
cd00005	CBM9_like_1	2.75e-18	311	502	4	162	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.
pfam16403	DUF5011	3.11e-17	1373	1443	1	71	Domain of unknown function (DUF5011). This small family of proteins is functionally uncharacterized. This family is found in Bacteroides, Prevotella, and Parabateroides. Proteins in this family are around 230 amino acids in length.
pfam06452	CBM9_1	5.34e-17	551	761	1	181	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCI59828.1	0.0	1	1643	1	1643
QNL45026.1	1.85e-159	783	1389	1570	2177
BCI61176.1	1.48e-38	1445	1641	1047	1240
BCI61555.1	1.35e-36	1454	1641	1221	1411
BCI61304.1	4.71e-33	1410	1641	2031	2270

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3G6S_A	3.77e-39	47	269	7	229	ChainA, Putative endonuclease/exonuclease/phosphatase family protein [Phocaeicola vulgatus ATCC 8482]
4C1R_A	9.49e-39	65	283	25	241	Bacteroidesthetaiotaomicron VPI-5482 mannosyl-6-phosphatase Bt3783 [Bacteroides thetaiotaomicron VPI-5482],4C1R_B Bacteroides thetaiotaomicron VPI-5482 mannosyl-6-phosphatase Bt3783 [Bacteroides thetaiotaomicron VPI-5482],4C1R_C Bacteroides thetaiotaomicron VPI-5482 mannosyl-6-phosphatase Bt3783 [Bacteroides thetaiotaomicron VPI-5482],4C1R_D Bacteroides thetaiotaomicron VPI-5482 mannosyl-6-phosphatase Bt3783 [Bacteroides thetaiotaomicron VPI-5482]
3MPR_A	2.49e-37	45	283	3	246	CrystalStructure of endonuclease/exonuclease/phosphatase family protein from Bacteroides thetaiotaomicron, Northeast Structural Genomics Consortium Target BtR318A [Bacteroides thetaiotaomicron],3MPR_B Crystal Structure of endonuclease/exonuclease/phosphatase family protein from Bacteroides thetaiotaomicron, Northeast Structural Genomics Consortium Target BtR318A [Bacteroides thetaiotaomicron],3MPR_C Crystal Structure of endonuclease/exonuclease/phosphatase family protein from Bacteroides thetaiotaomicron, Northeast Structural Genomics Consortium Target BtR318A [Bacteroides thetaiotaomicron],3MPR_D Crystal Structure of endonuclease/exonuclease/phosphatase family protein from Bacteroides thetaiotaomicron, Northeast Structural Genomics Consortium Target BtR318A [Bacteroides thetaiotaomicron]
3L1W_A	5.47e-22	50	300	2	249	Thecrystal structure of a functionally unknown conserved protein from Enterococcus faecalis V583 [Enterococcus faecalis],3L1W_B The crystal structure of a functionally unknown conserved protein from Enterococcus faecalis V583 [Enterococcus faecalis],3L1W_C The crystal structure of a functionally unknown conserved protein from Enterococcus faecalis V583 [Enterococcus faecalis],3L1W_D The crystal structure of a functionally unknown conserved protein from Enterococcus faecalis V583 [Enterococcus faecalis],3L1W_E The crystal structure of a functionally unknown conserved protein from Enterococcus faecalis V583 [Enterococcus faecalis],3L1W_F The crystal structure of a functionally unknown conserved protein from Enterococcus faecalis V583 [Enterococcus faecalis]
2KPN_A	2.63e-14	1371	1459	11	97	SolutionNMR structure of a Bacterial Ig-like (Big_3) domain from Bacillus cereus. Northeast Structural Genomics Consortium target BcR147A [Bacillus cereus ATCC 14579]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P36917	1.43e-21	310	790	686	1063	Endo-1,4-beta-xylanase A OS=Thermoanaerobacterium saccharolyticum OX=28896 GN=xynA PE=1 SV=1
P38535	4.67e-20	310	769	538	899	Exoglucanase XynX OS=Acetivibrio thermocellus OX=1515 GN=xynX PE=3 SV=1
Q8BX37	9.17e-10	975	1331	33	398	Acid phosphatase type 7 OS=Mus musculus OX=10090 GN=Acp7 PE=2 SV=2
O69230	4.72e-08	547	761	905	1083	Endo-1,4-beta-xylanase C OS=Paenibacillus barcinonensis OX=198119 GN=xynC PE=1 SV=1
Q5UQW5	6.77e-08	49	296	1	263	Uncharacterized protein L388 OS=Acanthamoeba polyphaga mimivirus OX=212035 GN=MIMI_L388 PE=4 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
0.000228	0.999047	0.000208	0.000179	0.000164	0.000145

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000129_01302.