CAZyme Information: APA07677.1

Basic Information

• Species: Sclerotinia sclerotiorum
• Lineage: Ascomycota; Leotiomycetes; ; Sclerotiniaceae; Sclerotinia; Sclerotinia sclerotiorum
• CAZyme ID: APA07677.1
• CAZy Family: CE9
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1170		126858.53	4.1830

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Ssclerotiorum1980UF-70	11368	665079	238	11130

• Gene Location: location=CP017816:798681-802621(-)

Full Sequence      

MKAITVLVGLSWLRWALADDIYCDANVPCAIGCCGVKSNVCGLGPNYCSAENCINSCDAK
AECNPGGWASEYVNSTTCPLNVCCSEYGFCGTGESFCGTKTPTIPSCDVDSQSITRVIGY
YASGGATRACDAMLPESFPQGIYSHIYFAFGSINPDTFEVIPGADGDEALYTKLSALQTR
DATQKFWLSIGGWTFTDSDQATATTFSDLAAADITHQNVFFSSLTLFMTTWGFSGVDIDW
EYPAASDRSGRTEDYANYPKFLANLKSALDEYSYGLSITLPTSYWYLQHFDLISIEPSVD
WFNYMAYDLHGTWDIGNEWTGAILDAHTNLTEIESSMNLLWWNNITSSKVNLGLAFYGRS
FTIASSNCDTPGCAYLSAGDEGVCSASAGILLSSEIEQIMSDNDLTPVFYKDAAVKAITW
DNDQWVSFDDQETFKIKSDFAKSQCLGGVLVWSVDYDDSNNTLSRGLAAALGNEINIDTS
TGLALTESETSDTTTTSKGGQDAYCRFTNCGETCPAGFTTVVRGDKKSQLMLDGSQCWPG
SGLTQTLCCPTSTDVPTCQWRGFHNNGKCKGGCNSGEAEVGTNSAGCKSGYQSACCTTTS
STKPYSECAWTSSCESDDTCPSGYSNFIVGSRAGWGGRKKSCSGKKKYNYCCADSVPDAF
TNCAWAGFEVAFKNEKYCSDTCPSGTIRIAEQDDFGQTPNVENCIWGKEAYCCGGTVTTS
TVSPRAPTYQDTTAKEFDAYLKKYLAAPICPGGFEAEYSASFSSDPLGWKRSISLEKRAT
DQGITLEVLIPILSTWITSQYPRTDLMEIWNDDTSEAGFGSMNYTVLRDTLYPNAWTGDP
EYATDTLLTDMLCNMAEAANGLENLQTDSSILCVSPDDDAGTWDDLVTTKREISARRLDE
MVSTARTADGLQPSVSQAIRGVLNGDLSLHYLRWLNPSGAQVILELAFWIGPTAGVAPTA
AQRAAYADTTHTAAADRWIVFHLHIPLDRYTFRQEITNDDTFWHLGVGTITVYHGQTVNR
SPPRSGDDTLEPRVEFRYSSTYVGGVNNGNMANYNARTQALSCPIGDDIQTRMYLGLDLN
AAVQASIRPSVGATLVNSFNLWMYEQGITSLTNLQYLWPSLPGDQGGFELVGGFNGNSNL
NPEYGAFQQNWLPDGGPAPDINSAPTGTSG

Enzyme Prediction     

EC	3.2.1.14:2

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	115	464	6.1e-59	0.9594594594594594

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
214753	Glyco_18	4.42e-69	116	457	1	334	Glyco_18 domain.
395573	Glyco_hydro_18	3.08e-65	116	457	1	307	Glycosyl hydrolases family 18.
119357	GH18_zymocin_alpha	6.90e-65	118	457	3	345	Zymocin, alpha subunit. Zymocin is a heterotrimeric enzyme that inhibits yeast cell cycle progression. The zymocin alpha subunit has a chitinase activity that is essential for holoenzyme action from the cell exterior while the gamma subunit contains the intracellular toxin responsible for G1 phase cell cycle arrest. The zymocin alpha and beta subunits are thought to act from the cell's exterior by docking to the cell wall-associated chitin, thus mediating gamma-toxin translocation. The alpha subunit has an eight-stranded TIM barrel fold similar to that of family 18 glycosyl hydrolases such as hevamine, chitolectin, and chitobiase.
119351	GH18_chitolectin_chitotriosidase	6.30e-60	117	462	1	346	This conserved domain family includes a large number of catalytically inactive chitinase-like lectins (chitolectins) including YKL-39, YKL-40 (HCGP39), YM1, oviductin, and AMCase (acidic mammalian chitinase), as well as catalytically active chitotriosidases. The conserved domain is an eight-stranded alpha/beta barrel fold belonging to the family 18 glycosyl hydrolases. The fold has a pronounced active-site cleft at the C-terminal end of the beta-barrel. The chitolectins lack a key active site glutamate (the proton donor required for hydrolytic activity) but retain highly conserved residues involved in oligosaccharide binding. Chitotriosidase is a chitinolytic enzyme expressed in maturing macrophages, which suggests that it plays a part in antimicrobial defense. Chitotriosidase hydrolyzes chitotriose, as well as colloidal chitin to yield chitobiose and is therefore considered an exochitinase. Chitotriosidase occurs in two major forms, the large form being converted to the small form by either RNA or post-translational processing. Although the small form, containing the chitinase domain alone, is sufficient for the chitinolytic activity, the additional C-terminal chitin-binding domain of the large form plays a role in processing colloidal chitin. The chitotriosidase gene is nonessential in humans, as about 35% of the population are heterozygous and 6% homozygous for an inactivated form of the gene. HCGP39 is a 39-kDa human cartilage glycoprotein thought to play a role in connective tissue remodeling and defense against pathogens.
119365	GH18_chitinase	4.37e-47	117	457	1	322	The GH18 (glycosyl hydrolases, family 18) type II chitinases hydrolyze chitin, an abundant polymer of N-acetylglucosamine and have been identified in bacteria, fungi, insects, plants, viruses, and protozoan parasites. The structure of this domain is an eight-stranded alpha/beta barrel with a pronounced active-site cleft at the C-terminal end of the beta-barrel.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
APA07677.1|CBM18|GH18	0.0	1	1170	1	1170
QKD59080.1|CBM18|GH18	0.0	10	1164	14	1171
QKD61252.1|CBM18|GH18	0.0	10	1164	14	1171
CEF84382.1|CBM18|GH18	0.0	5	1164	7	1157
CZS74851.1|CBM18|GH18	0.0	5	1164	35	1175

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6LE8_A	6.06e-32	134	460	22	351	Chain A, Probable endochitinase [Caenorhabditis elegans]
6LE7_A	2.05e-31	134	460	21	350	Chain A, Probable endochitinase [Caenorhabditis elegans]
6LDU_A	2.13e-31	134	460	22	351	Chain A, Probable endochitinase [Caenorhabditis elegans]
1LG1_A	3.73e-31	116	458	2	343	Crystal Structure Of Human Chitotriosidase In Complex With Chitobiose [Homo sapiens],1LG2_A Crystal Structure Of Human Chitotriosidase In Complex With Ethylene Glycol [Homo sapiens],1LQ0_A Crystal Structure Of Human Chitotriosidase At 2.2 Angstrom Resolution [Homo sapiens],6ZE8_A Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_B Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_C Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_D Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_E Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_F Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens]
1GUV_A	3.80e-31	116	458	2	343	Structure of human chitotriosidase [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P09805|KTXA_KLULA	1.86e-43	61	456	317	711	Killer toxin subunits alpha/beta OS=Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) OX=284590 PE=1 SV=1
sp|Q9D7Q1|CHIT1_MOUSE	3.09e-30	135	481	43	389	Chitotriosidase-1 OS=Mus musculus OX=10090 GN=Chit1 PE=1 SV=2
sp|Q13231|CHIT1_HUMAN	4.27e-30	113	458	20	364	Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1
sp|Q11174|CHIT_CAEEL	2.11e-29	134	460	73	402	Probable endochitinase OS=Caenorhabditis elegans OX=6239 GN=cht-1 PE=1 SV=1
sp|Q6TMG6|CH3L1_SHEEP	1.46e-26	116	462	2	340	Chitinase-3-like protein 1 OS=Ovis aries OX=9940 GN=CHI3L1 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000194	0.999788	CS pos: 18-19. Pr: 0.9797

TMHMM  Annotations     

There is no transmembrane helices in APA07677.1.