CAZyme Information: MGYG000001542_04781

Basic Information

• Species: Paenibacillus_A sp900069005
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_A; Paenibacillus_A sp900069005
• CAZyme ID: MGYG000001542_04781
• CAZy Family: GH39
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1649	MGYG000001542_44|CGC11	181172.02	4.6057

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001542	5846629	Isolate	not provided	not provided

• Gene Location: Start: 538705; End: 543654 Strand: -

Full Sequence      

MAIKKWMLSSMLVLLLLTWPMNGLLFNSKLAAYADESLQSIVIGNFESDEEVWNLSLGTE
FPGAKGEYIRDSTVSQSGVYAGKLHGDFSGGGKYVAIGRNFTPLDMQKLEFWVKSADATA
IVLRVTDSTGQVHQQKISIPLAAVWQKIEITNFNGGASYLHFNGANDGVWHGPAQGIGIL
LEKAGLSSNQSSGDVWIDAVSAIAPQQAPLWENKIGTFEDGFDIWKLGLGTDFPGASGRY
VRDALEPKSGLYAAKLQGDFTAGGKYITLGKSLSPLSIQKIAFWIKTADASSISLRLKDA
TGQVHQQKLSLKPTINWQKIEIYKFDSGQNYLHFGGANDGKWHGPIQQIEFLLEKSGLNS
GKSSGEILLDNVVLTAPYPDLSIQQSRMGNIFLENEPVAFQITTQGDAVSWRMYDHLDHK
VLEGIEGVQGGQLNLSIPLQQLGYFKLSIDAVKNGQMIKSSEISLARLSNTDPTVTDSSP
FGMSTHLAWETPQGWTPELSELLTRAGVKNFRDEIPWDAVEYEKGKYRKPANRDAYMQRT
QQDGLKPFIILDYTHPFYDQNSTPYTDQGRQGFADYGKALLNLYGDQIPWVEVYNEFNGG
FGDRGNGPADSRPDYYFQLLKKTYETVKAARPDVTVVGMATAGTPLSWMEEVFKLGGLQY
MDAVSIHPYQSQRSPDGIVDNVRSTQDLIRQYNQGQLKPIWFTEVGWPTSIGGIGISENT
QADYLVRTHVQALAEGVEKVFWYDLMNDGMDSGYHEDNFGILRNANDPKGAFTPKPAYAA
YAAMTRELIGAQFVDRESFDANISSYKFNKDGQNLRVIWANTPVQTVINTNSQIQIMDIM
GNTETYTPMEGKVYLTLTEEPIYIKSDIDDIAMDTTFNLTGDEAVVGEPIALKMEMNNAS
SKALSVSFTVEGESYPLSAEAGQKASQTFTLPGWREEGTRYLKVDLTANGRKIGHLKHII
QAAPSYSVRVTPTITEVSSKNEGLKVQINNHSKAQGLSVQQIDWKFGNQSGNQAIDLVIP
PDTIDTIDIPLHGFDFGASYPVQVTIYLDGKEPFVYEGNFDFNPIIRGTVEVDGTVDPGV
IAQTPIVELSKGTVKMQNYTGPADLDGSIWANWDSDSFYLTAKIKDDVHSAPASGEEIWK
NDSIQFAMMAGIPGENRGYYELGISDTPQGPQIFRWLSPDSGAKGLVTNGSLQVIRDEVQ
KLTIYEMALPWSEISQVKPSTNEALSISFLVNDNDGPGRKGYIEWGSGIGEVKDSKKFRT
AQWIHDAASPIITVQGVAEGESYADEVIPVVTVETEEGQALEARILLDGEPWTSGTPITA
KGEHLLVVQAGDPAGIITEQKLTFKLYHSTILETSDVEGGANDTVLLQAKLHDKNGQAIS
GENVSFAVYGGEPIGEAVTDADGIAMLNYKIQIQADPNQETIYPLQAFYSQNDAAYLLGS
EGTGQLKVNPSPRPDPKGIPGKPVLSDNQGYNTGIKDGTYAIAMNMWWGNNGTTYKLYEN
DVLIDTQSLTDHSPNAQTAVTSNLLRKNGTYRYYAELTNTSGTTRSDVHTVTVTEAAPAV
PILSHDNWDGNGNFKVSMNMWWGTNGTTYRLYENGILIDTQVLNDRTPNAQTTITVIHDK
PVGTYEYRCELANDSGATSSEKMIVVVTK

Enzyme Prediction     

No EC number prediction in MGYG000001542_04781.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH39	534	826	4.1e-28	0.7146171693735499

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd09621	CBM9_like_5	2.27e-50	1097	1262	20	187	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.
cd00241	DOMON_like	3.77e-12	1100	1245	13	158	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.
cd09619	CBM9_like_4	1.19e-11	1072	1241	4	167	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.
cd02848	E_set_Chitinase_N	1.68e-07	1573	1646	37	105	N-terminal Early set domain associated with the catalytic domain of chitinase. E or "early" set domains are associated with the catalytic domain of chitinase at the N-terminal end. Chitinases hydrolyze the abundant natural biopolymer chitin, producing smaller chito-oligosaccharides. Chitin consists of multiple N-acetyl-D-glucosamine (NAG) residues connected via beta-1,4-glycosidic linkages and is an important structural element of fungal cell wall and arthropod exoskeletons. On the basis of the mode of chitin hydrolysis, chitinases are classified as random, endo-, and exo-chitinases and belong to families 18 and 19 of glycosyl hydrolases based on sequence criteria. The N-terminal domain of chitinase may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family include members of the alpha amylase family, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase, among others.
cd02848	E_set_Chitinase_N	2.99e-07	1479	1552	37	105	N-terminal Early set domain associated with the catalytic domain of chitinase. E or "early" set domains are associated with the catalytic domain of chitinase at the N-terminal end. Chitinases hydrolyze the abundant natural biopolymer chitin, producing smaller chito-oligosaccharides. Chitin consists of multiple N-acetyl-D-glucosamine (NAG) residues connected via beta-1,4-glycosidic linkages and is an important structural element of fungal cell wall and arthropod exoskeletons. On the basis of the mode of chitin hydrolysis, chitinases are classified as random, endo-, and exo-chitinases and belong to families 18 and 19 of glycosyl hydrolases based on sequence criteria. The N-terminal domain of chitinase may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family include members of the alpha amylase family, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase, among others.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AZS14129.1	0.0	1	1649	1	1649
QTH40658.1	0.0	1	1306	1	1304
SMF84368.1	0.0	358	1647	290	1550
AZS14136.1	0.0	370	1647	316	1566
SMF73229.1	0.0	8	1419	75	1508

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5JVK_A	8.52e-36	427	864	53	496	Structuralinsights into a family 39 glycoside hydrolase from the gut symbiont Bacteroides cellulosilyticus WH2. [Bacteroides cellulosilyticus],5JVK_B Structural insights into a family 39 glycoside hydrolase from the gut symbiont Bacteroides cellulosilyticus WH2. [Bacteroides cellulosilyticus],5JVK_C Structural insights into a family 39 glycoside hydrolase from the gut symbiont Bacteroides cellulosilyticus WH2. [Bacteroides cellulosilyticus]

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
0.328650	0.659403	0.010426	0.000792	0.000337	0.000370

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001542_04781.