CAZyme Information: MGYG000001542_04771

Basic Information

• Species: Paenibacillus_A sp900069005
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_A; Paenibacillus_A sp900069005
• CAZyme ID: MGYG000001542_04771
• CAZy Family: GH39
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1567	MGYG000001542_44|CGC11	171371.96	4.403

Genome Property

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

• Gene Location: Start: 522532; End: 527235 Strand: -

Full Sequence      

MPANKMIGVRRVLKIKRAKAPIRLMSVFLAVVILQGSLLTWHGATPGLAAAAAEAALAST
GGSLPVQLEPVEDTYVNAGGNAGKNFGSSNLLIVKNFEADVNLNRQAYMKFDLSSITGEI
GSVKLKAYAVDNENSTIAVQAYGMEDSSWQEDMVTWNNKPEIDHYLSSENVGKIAGWHEW
DVTSFVKQQLAKGDIVSIALIQQAAKGHSVSLNSKEHTDNHPYLEISVDRAEESAPSWSA
GASLQATNITENGLQLDWDAASDTVGVTGYAVYQNGVLLGKVSGGITSYTVTGLTVGQKY
TFKVEAGNAQNSWSSDGPFVTVRTPTTELIQLRPGNIYTNGEAVRFKVQTARPAVSWAVY
DYQGALAQEGTAATVQNEAAWTVPHLKHGYFTLQVRADLDGSDPVLLKTPFAVLAPRDEP
TNEASPFGVSTHLHRLPQNLTSNIVDLIKAAGIRTVRGGYEWRGIEKQQGSYTFTPQPDY
YMNMLNKDDFDFLFVSGYTNPFYDNDSTPYTDAGREGFANFMKAYVDHYQDQLDVVEVYN
EFYGSFGDRGNGPADSKPEYYYPLLKKTYETLKASHPDLPVLGTSTVGDLKWIEAVFKLG
GMQYMDGFSIHPYLYPGAPEGYEDLILNLKDLIREYNNGNLKPIWINETGWPTERDARGV
DEKTQANYLIRANVVALANGVEKIVWYDMINDGIQNINEDNFGLLRNPDDKLGSLTPKPA
YTAYATMTQMLNAAMFASRDATDSDIRSYVFQKTGGNVRVIWSTADSSIPAAIHTSTPIQ
ITDMMGNTSTYTPYNGNVFVTLSNEPFFVVGEVNGIERDSTFVLSGEEARIGDSLVFTLE
TNNTDSDDFAFQLAVEDQIHPVVTPSGQQAVQTIEVASGIEPGSRLVTAVLLKGNDRVGL
LRSGTSTLPPYTVQIRPMMEEPDLNQTLRVAVNNESKSKAMQLQKVDWRFGTQSGTEIMN
EEIAAGSSAIVDIPLASMSIGITSSLKVTVYIDGLEPYTYEGTAEFNPVPARSVTVDGTL
DPETLNSASTIDLSKGTVKMSGYQGAGDLSGQVWLSYDADHLYLSARIKDDTHTASMAGA
DIWNNDSLQFAISDGLPGEKAYWHEIGISQTPEGPQSYRWMAPPGVDKGPLIDSQLAITR
DEELKYTIYELALPWSEIEPVRAENHGVISFSMLVNDNDGAGRKGFIEWGGGIGDGKLSS
KFRSMQWMALAEDMVPPETSLNMEGTERNGWYISEVRAVLKAADETSGVAETVYSLDNGK
TWLSYKEPLTFTEDGTYTLTYRSMDRAGNIEETQEVIFRIDRTAPTASIRYSTTEPTREP
VTATMIPSEPVTITNNDGNDSYTFSQNGSFTFEFIDAAGHEGSATAVAGNIIAAATGVPG
QPKLSSDNGYDTGIMDGSYRISMNLWWGNNGTDYILYENGVPIDRQALKDDSPNAQSAVT
AVFNKPNGTYEYVAELTNAFGTTRSDVLVVTVNEATPGQPVLSHDHWDGDGSYKVSMNMW
WGTNGSTYRLYENDVLIDTQTLINKTPQAQSAITEIREKSAGTYVYWCELINDAGTVSSG
KITVIVK

Enzyme Prediction     

No EC number prediction in MGYG000001542_04771.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH39	516	766	5.6e-23	0.605568445475638
CBM9	1016	1191	2.3e-18	0.9010989010989011

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd09621	CBM9_like_5	1.47e-49	1042	1202	21	183	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.
NF033679	DNRLRE_dom	8.28e-27	72	226	1	163	DNRLRE domain. The DNRLRE domain, with a length of about 160 amino acids, appears typically in large, repetitive surface proteins of bacteria and archaea, sometimes repeated several times. It occurs, notably, three times in the C-terminal region of the enzyme disaggregatase from the archaeal species Methanosarcina mazei, each time with the motif DNRLRE, for which the domain is named. Archaeal proteins within this family are described particularly well by the currently more narrowly defined Pfam model, PF06848. Note that the catalytic region of disaggregatase, in the N-terminal portion of the protein, is modeled by a different HMM, PF08480.
cd00241	DOMON_like	1.71e-13	1036	1189	5	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	5.67e-13	1014	1185	2	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.
pfam06452	CBM9_1	1.50e-09	1016	1189	1	162	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
AZS14136.1	0.0	1	1567	1	1567
SMF84368.1	0.0	14	1567	3	1551
AZS16815.1	0.0	64	1208	43	1183
AZS14129.1	0.0	298	1566	347	1647
QNK56522.1	0.0	66	1248	331	1514

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5JVK_A	1.34e-25	389	816	69	505	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]
1K85_A	3.16e-09	239	324	5	88	ChainA, CHITINASE A1 [Niallia circulans]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
A0P8X0	1.06e-09	185	325	756	900	Alpha-amylase OS=Niallia circulans OX=1397 GN=igtZ PE=1 SV=1
P27050	1.92e-09	242	326	97	179	Chitinase D OS=Niallia circulans OX=1397 GN=chiD PE=1 SV=4
P20533	3.19e-09	228	324	457	549	Chitinase A1 OS=Niallia circulans OX=1397 GN=chiA1 PE=1 SV=1
O82833	1.36e-08	50	237	25	213	Gellan lyase OS=Bacillus sp. OX=1409 PE=1 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
0.695804	0.285522	0.007273	0.001232	0.000819	0.009358

TMHMM  Annotations     

start	end
20	42