CAZyme Information: KFA56363.1

Basic Information

• Species: Stachybotrys chartarum
• Lineage: Ascomycota; Sordariomycetes; ; Stachybotryaceae; Stachybotrys; Stachybotrys chartarum
• CAZyme ID: KFA56363.1
• CAZy Family: GT66
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1276		139101.86	4.5139

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_SchartarumIBT40293	11453	1280524	0	11453

• Gene Location: location=KL650210:4830-8972(+)

Full Sequence      

MLLLSSKLVHHAVLAALSLSALLDTGAGVEAQLTVSSQGTSTWTMYGATTVSQAPHGIPK
LVYNCAKMPAICQNVHVTYPLNTINQGTGLNGHGTLQGQSHLLLHFDRGGNAATRRGIAC
SGNFAAGHLGNPCPTVADTAADVLGTVPFGAMSGRGSYPAARFNPTNIAPGNPGYNTIAG
AAGQHSGMMWTCHEFPPASTVEGGSGARTICAPQNGRCDSNNYNGPLGGVNSEQNFQSWA
HMALRNNVFDPPGRHGVYRFYFVTRFNTDIDGDAAEVHWYGEDATFAVGFGQPEKRYLDG
TPAVHRAVESFYGNGTSIITRQLLQEEEYKVLRRHWIDNLHGNSSSISQGPLDSVADALL
ETRQAPEDTWASVDGNGTSPVRQAFEILPQAPPLPIIEITRDFMAEEEGVEEHESYVARV
LDAVDADLSNTNAGSRDSIEEEFARAVAASRRSDPDGDSGWMQRRQSQRQCDSVAPCPDG
SCCNRTGRCGYGNETCAPNVCISNCNATALCGRDSLNGEVVCPLNVCCSHYGYCGVEDDF
CLGAGPHAPCQEGFGSCNVVSPPSCGGNSAFAQSIGYYQLANVRERQCNRIRPDQIRTEG
FTHLFAAFATINPSTFAVEPWHPDDVAMYEELIALRSSSMQIWIAIGGWTFNDAGPTRTT
LSDLAMNPTRRRRFINSLVTFLQEHGFDGVELDWEYPGAPDRGGRPEDTANYVSLIREMR
EVFGTRFGISMAIPTSYWYLRWFRPIEIEPYIDFFGVMSFDLHGPWDEDVRHIGRVVLGH
TNVPEIANWTLPLYYDGLDPAKLNLGLPYYARGYTVAVSDCNAIGCDWVSTSRPAPCTNF
CGVMSLEEIERMVSEQNISPRLLASDVMMQLTFGNQWIGYDNLDTIRMKKRWASQRCFGG
TMDWSVDMYSGSGSGDVPDGGGSENPGDPGGGQGEGSGMVYIDPEVWEEDTPEVNCWPPC
TFVMPPLLLDEPVTISLPPYETSLDVAWAGTDGWHSTIQTTTLTIPVMTITTIDAWHITV
RETRTGTGTRTGARATYYITLSIRLPTFIITNNLPETSNDGVTQPPGTRTITPPPYPWTF
TPPDPEATTTRSNTPEDIPEFPIVTWRPGNPGPRCRSGCGRRCRLFCSFPCLLDCPDPGL
DFPDPSNPRPPTRPVPQPTPGPPPPPPGSEPENEDHEEEERACAIEWGQPIPTFRSDDSS
TSSIPSPTRPPPSPSPTPDPEPPSPNPDTEEVDCYNNGQFINRALAIEALDYFCDAFEGQ
VLDATRPGTQRTLTWP

Enzyme Prediction     

No EC number prediction in KFA56363.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	573	912	1.8e-50	0.9425675675675675

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
214753	Glyco_18	5.47e-67	575	908	3	333	Glyco_18 domain.
395573	Glyco_hydro_18	5.40e-63	592	908	14	306	Glycosyl hydrolases family 18.
119351	GH18_chitolectin_chitotriosidase	8.82e-62	602	908	29	340	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.
119357	GH18_zymocin_alpha	2.74e-57	574	909	2	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.
119365	GH18_chitinase	2.43e-50	593	908	18	321	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
QKD48531.1|GH18	0.0	29	1273	66	1299
CEI63226.1|CBM18|GH18	0.0	51	1273	24	1142
CEI60137.1|CBM18|GH18	2.25e-138	462	1018	58	593
CDP30264.1|CBM18|GH18	1.52e-133	477	986	120	615
CAP65874.1|CBM18|GH18	1.52e-133	477	986	120	615

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5WUS_A	3.06e-37	573	918	3	354	Crystal structure of a insect group III chitinase (CAD2) from Ostrinia furnacalis [Ostrinia furnacalis],5WVH_A Crystal structure of an insect group III chitinase complex with (GlcNAc)6 (CAD2-(GlcNAc)6) from Ostrinia furnacalis [Ostrinia furnacalis]
5WVF_A	3.33e-36	573	918	3	354	Crystal structure of a mutant insect group III chitinase (CAD2-E647L) from Ostrinia furnacalis [Ostrinia furnacalis],5WVG_A Crystal structure of a mutant insect group III chitinase complex with (GlcNAc)5 (CAD1-E647L-(GlcNAc)5) from Ostrinia furnacalis [Ostrinia furnacalis]
1HKK_A	1.05e-35	590	908	19	341	High resoultion crystal structure of human chitinase in complex with allosamidin [Homo sapiens]
1HKI_A	1.08e-35	590	908	19	341	Crystal structure of human chitinase in complex with glucoallosamidin B [Homo sapiens],1HKJ_A Crystal structure of human chitinase in complex with methylallosamidin [Homo sapiens],1HKM_A High resolution crystal structure of human chitinase in complex with demethylallosamidin [Homo sapiens]
1LG1_A	1.08e-35	590	908	19	341	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q6RY07|CHIA_RAT	2.45e-37	592	914	42	370	Acidic mammalian chitinase OS=Rattus norvegicus OX=10116 GN=Chia PE=2 SV=1
sp|Q91XA9|CHIA_MOUSE	3.58e-36	592	914	42	370	Acidic mammalian chitinase OS=Mus musculus OX=10090 GN=Chia PE=1 SV=2
sp|Q95M17|CHIA_BOVIN	6.88e-35	592	908	42	364	Acidic mammalian chitinase OS=Bos taurus OX=9913 GN=CHIA PE=1 SV=1
sp|Q13231|CHIT1_HUMAN	3.71e-34	590	908	40	362	Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1
sp|Q9W5U2|CHI10_DROME	7.76e-34	559	908	1898	2252	Probable chitinase 10 OS=Drosophila melanogaster OX=7227 GN=Cht10 PE=2 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000364	0.999604	CS pos: 28-29. Pr: 0.9224

TMHMM  Annotations     

There is no transmembrane helices in KFA56363.1.