CAZyme Information: MGYG000001525_00542

Basic Information

• Species: Paenibacillus_A rubinfantis
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_A; Paenibacillus_A rubinfantis
• CAZyme ID: MGYG000001525_00542
• CAZy Family: GH36
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2182	MGYG000001525_15|CGC2	239854.95	4.3158

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001525	5369528	Isolate	not provided	not provided

• Gene Location: Start: 36522; End: 43070 Strand: +

Full Sequence      

MQLSKCKIKVINRWFLIAVMLFSSLMPQLATAHAAGEDSMDAGERLSSALIAGDNPTSSG
DAYVRYDENESGKVWTIGTSQIEKVIRLKDGRFQMISLVNKLAEGGAGKEYVNPNDGSDE
FAIKAVIEGDPNGLVLSGSDDIWSLENYSTELGSQQELILSVSLTSPTMRVTRNYQILPD
TGVIEEWTNFTNLEETAATYAEPSFVRGSIMPDATADNVIVYRMIGDKVSSSPKHTLTQN
PVNMNGLSTIDGSGADISHPFVALQYKDTQEGVFFTWDYTGKWQTKVGNNSGMTFIQTAA
YNQSDGEKWTFSLKPDETVSMPLSRVGVFVGDTDDMGNAITDYQYKYKWDATNEEFMNLI
RFGGYGSDPELIFQKVNSNRYIGGDMIWIDDGWQTNLGDWEWKEGMPIEKYQEYIARNSQ
VLGLWMPPWGAEQQAQLMNDHPDWYIEYTTGMDARKTGLDTSKPEVVDYIRSKVNEVQTA
LDGFMLKTDFNQYKDGFSRAQGVMQVMKNFKLDHPDQGLHICSDGAGVLNPGSAALSELI
LLQDGTPAYSDGYYASMLYPIDKILTSRGRGDIGSYSKSNRAMLSYAMTVAGKTNGTMEE
LEPIRQDMDLYRYLKDQGVMGRYVKVYRPSHTLEADRYYFVQKMNKDGDKGYITVRFDNS
YAGVNVTLTPKGLDPASTYTISTLESGMATATKSGAEWMSEGIPLTPLQVGEVIFLNLEN
RPGSGNDQIEPASPVNVSASNARYMDRSGVELTWDEGSDNNWISYYEVFKNGEAYDKVSK
GTYYFDVNGTLNDQYSIRTVDGDNNVSGQVEAVQNAPSIKPGVAEFDKAPNRQADVISEI
TWNNATQVTDIKLNGATIGSDAYVVGQTHDGQATLTIKKELLALQEVGSLEVTVEFDQGY
KQLLIVNIVDKSGTTSGDAYVRFEDLGNEKIWTMGTDQIEKVVRIQNSKFLMTSLVNKLA
PGGGKEYSTHTQTVSDEFAIKPVIPGNTSAPIVTGNDRVWTYETHSVTKGDQGELILSVS
VTGKSMRVTRHYRMLPDTGVIEEWTDYTNLKQAEAIFAEPRLVRYRVMSDAADKVDLYHV
NVNKTDGVTEQVLVKQPVNKTSLTTIESSDTEINHPFFAMQYRDDQDGLFFTWDYSGKWT
TKVGNNSGMTFVQVAVYNKLDTENWTFTAAPDATFSTPVSRVGVFLGDIDDMGNAITDYQ
YKYKWSDTNEAYLNMIQYNGAGADPDSVFERISNNRYIGGDLVWLEEGWQTHVGDWGWKA
EMPIDQYQQYADMSGQSLGLWLPPWGAEQDSQLKQQHPDWFIEYKAGMDQSKAGLDTSKP
EVIQYIQSKISSLQAELGGFALKTDHNLYKDGFSRAQGVLKVVENYKRDYPDKGLQISSN
GSDLLHPGSAAYSEFIIPQEGAVGPSDGYYTSLLYPIDKLVTNYGRGDLGSYTKANRALL
SYQMTVAGAADSTEDLEPIRQDADFYRYLKTQGVMGRYVKVYRPVADTNEPYYFVQKVSQ
DESKSYITVRFDASLEGSNVTVYPKGLNEEQAYTVSTLEGGMGTATRTGAQWMSEGIPLT
PLKTGEVIFLNLEGRPGSGQDHTAPLAPELISVSSAVYMDHNGMEIVWEAGSDDNWISYY
EIEKNGAPYDKVSKGTRYFDEGGLSSDTYRIRTVDGDGNVSEYVSNAAAPAEPSISPSSA
SFDKNPEKQTDVLIDVTWNSASEVVAIKHDGVSVTEDVYYSLTGNLITLKKEYLAMQETG
DISLSVSFDTGHEAELTIAILDTSVDPVDPPAVDFSNLHTALVTAQSKVDGAEIGDQPGE
YPEAAVDALKAAMAIAMEIMNQAATQEAVDVATMELYRAISDFEAAKVPAETPTDETVPA
WPADKAIRATHVGKTSLTLSWTSATDNIAVSNYKVFLNGSEIVTVTGDVYSYTVRGLTPK
TRYTFKTEAGDTAGNWSADGPSVVVTTQAEASSDGGSKPKPNPVPVSPSQPEQEEEPEIT
DPAEPTEPAEPTEPPAPAEPAPPEVTLTDIEGHWAKASIEQSVELGFVTGYGDGSFRPNA
NVTRAEIAAMLARALKLEINDSELSFADKNAVPIWAQPFIQAIAKAGIVSGYEDGTFRAN
KEITRTELVVIIVRSLGLEVTSGANIAFDDAGQVPVWARPYVATAVEKGLIKGDGNGRFN
PNDPSTRAEAITMTLAMLNNMG

Enzyme Prediction     

No EC number prediction in MGYG000001525_00542.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH36	154	703	6.2e-30	0.8401162790697675
GH36	1001	1348	2.9e-24	0.5406976744186046

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam03442	CBM_X2	6.82e-21	1675	1758	1	83	Carbohydrate binding domain X2. This domain binds to cellulose and to bacterial cell walls. It is found in glycosyl hydrolases and in scaffolding proteins of cellulosomes (multiprotein glycosyl hydrolase complexes). In the cellulosome it may aid cellulose degradation by anchoring the cellulosome to the bacterial cell wall and by binding it to its substrate. This domain has an Ig-like fold.
NF033190	inl_like_NEAT_1	1.14e-19	2011	2169	587	743	NEAT domain-containing leucine-rich repeat protein. Members of this family have an N-terminal NEAT (near transporter) domain often associated with iron transport, followed by a leucine-rich repeat region with significant sequence similarity to the internalins of Listeria monocytogenes. However, since Bacillus cereus (from which this protein was described, in PMID:16978259) is not considered an intracellular pathogen, and the function may be iron transport rather than internalization, applying the name "internalin" to this family probably would be misleading.
cd14791	GH36	4.87e-17	382	602	31	261	glycosyl hydrolase family 36 (GH36). GH36 enzymes occur in prokaryotes, eukaryotes, and archaea with a wide range of hydrolytic activities, including alpha-galactosidase, alpha-N-acetylgalactosaminidase, stachyose synthase, and raffinose synthase. All GH36 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. GH36 members are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively.
pfam03442	CBM_X2	5.39e-12	819	906	1	83	Carbohydrate binding domain X2. This domain binds to cellulose and to bacterial cell walls. It is found in glycosyl hydrolases and in scaffolding proteins of cellulosomes (multiprotein glycosyl hydrolase complexes). In the cellulosome it may aid cellulose degradation by anchoring the cellulosome to the bacterial cell wall and by binding it to its substrate. This domain has an Ig-like fold.
cd14791	GH36	1.17e-11	1238	1392	31	211	glycosyl hydrolase family 36 (GH36). GH36 enzymes occur in prokaryotes, eukaryotes, and archaea with a wide range of hydrolytic activities, including alpha-galactosidase, alpha-N-acetylgalactosaminidase, stachyose synthase, and raffinose synthase. All GH36 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. GH36 members are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QGU28165.1	4.73e-189	53	807	32	760
QTH40290.1	3.80e-118	58	822	37	794
QNK59398.1	9.16e-111	916	1667	39	788
QNA93536.1	1.06e-97	55	829	43	822
QYM63786.1	1.31e-97	75	829	12	772

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6BT4_A	1.99e-16	2013	2170	33	188	Crystalstructure of the SLH domain of Sap from Bacillus anthracis in complex with a pyruvylated SCWP unit [Bacillus anthracis]
3PYW_A	2.04e-16	2013	2170	12	167	Thestructure of the SLH domain from B. anthracis surface array protein at 1.8A [Bacillus anthracis]
3MI6_A	1.47e-13	992	1536	110	696	ChainA, Alpha-galactosidase [Levilactobacillus brevis ATCC 367],3MI6_B Chain B, Alpha-galactosidase [Levilactobacillus brevis ATCC 367],3MI6_C Chain C, Alpha-galactosidase [Levilactobacillus brevis ATCC 367],3MI6_D Chain D, Alpha-galactosidase [Levilactobacillus brevis ATCC 367]
2YFN_A	3.76e-12	1226	1561	346	705	galactosidasedomain of alpha-galactosidase-sucrose kinase, AgaSK [[Ruminococcus] gnavus E1],2YFO_A GALACTOSIDASE DOMAIN OF ALPHA-GALACTOSIDASE-SUCROSE KINASE, AGASK, in complex with galactose [[Ruminococcus] gnavus E1]
1K85_A	4.43e-09	1876	1947	19	88	ChainA, CHITINASE A1 [Niallia circulans]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
C6CRV0	2.30e-17	2014	2173	1291	1454	Endo-1,4-beta-xylanase A OS=Paenibacillus sp. (strain JDR-2) OX=324057 GN=xynA1 PE=1 SV=1
Q06853	5.16e-17	2005	2158	523	679	Cell surface glycoprotein 2 OS=Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) OX=203119 GN=Cthe_3079 PE=1 SV=1
P38537	1.39e-16	2014	2181	42	209	Surface-layer 125 kDa protein OS=Lysinibacillus sphaericus OX=1421 PE=3 SV=1
Q9ZES5	1.11e-14	2013	2170	41	197	S-layer protein OS=Bacillus thuringiensis subsp. finitimus OX=29337 GN=ctc PE=1 SV=1
Q06848	5.36e-14	2005	2158	283	439	Cellulosome-anchoring protein OS=Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) OX=203119 GN=ancA 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
0.000556	0.998548	0.000271	0.000224	0.000200	0.000187

TMHMM  Annotations     

start	end
13	35