CAZyme Information: RHZ56572.1

Basic Information

• Species: Aspergillus thermomutatus
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus thermomutatus
• CAZyme ID: RHZ56572.1
• CAZy Family: GH3
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1137	NKHU02000087|CGC1	123629.81	4.3011

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AthermomutatusHMRAF39	9702	N/A	0	9702

• Gene Location: location=NKHU02000087:1528-5128(-)

Full Sequence      

MNEGMIGNNYGLYRGTSSDFCSKLKPKQHVCCSEGDLPDFSPKPNEDGSCYTYQVKEDDN
CDNLAAEYSLTRDALEDFNKNTWGWNGCQLLYKDTIMCLSKGTPPFPAPIANAVCGPQKP
GSQPPTDGSDIAEMNPCPLNACCNIWGQCGITKDFCVDTNTGAPGTAEPGTYGCISNCGM
DVVKGDGTGAIKIAYYEGYCLSRECLFQDASQIDTSAYTHVHFGFGTLTADYDVETDLVV
WWVGLSTSADTYQIFRNGVKPANRLTMATKIANFIKENDLDGVDIDWEYPGAPDLPDFDP
GTEEDGPNYLAFLVVLKNLLPGKSISIAAPASYWYLKQFPIEKISKIVDYIVYMTYDLHG
QWDAHNSNAQEGCDTGNCLRSQVNLTETKQSLAMITKAGVPGKKVVVGVTSYGRSFKMAE
AGCWGPDCVYTGDRLNSNAKKGKCTGTAGYIADAEIAEILNEPDRVVKHFVDSSSNSDVL
VYDDTEWVGYMSASTKKTRTALYSAWGLGGTSDWASDLQKYHDVPAPAKSWGMFKQLALA
GDDPKADHTRNGNWTEMDCTHEMIVDSTYHLGSERWSTLNADAAWADVVRIWQDTDQPRA
GISFMQSVSTTLHMGAEANCGSLTADSCVTKDCPAGANGDTSGPAAQLIWNSLVKIHMLH
KDYHDTLFEVAALTSTALKDLENKFAPIPPEEDNTWLLLLIDLLTLGALGTAGPFFNTAL
RKLPYFLEKGITVDNIKDTSMTLIGQGTTIAKDVLPSKDAPWTPEAQDEFSNYMGQVVWG
WANVTTIALKEIFNGSEHSLQILGDTMSGGKLIEGAFEQQPPEEDEDTDKNELRANIQKC
FFGYSIPALWQVSKTYAFIIDAGHGCDEGKQLTDYLKDDTMDATGACVDGQQYYLVYPDG
DAVECHCEFYDGGPCQRVCVDNKFSVPPGLDSLGNGNFGGITKDDLVKGSVRTWKQNGKE
NSGGFADPTNKGTIDNLMDVDVTTPGFMRIPVFSPERAFQSWDTAEAGSSQFYPCDIPPG
KDECGDSSFENQTSDGSPSVEDCQQIIKNIEGDAGTDWTTQVVGKNQREIASHGSCAFGV
EATKVDGNVNFVVGGQDVIDIINEAIRRFGGGGRVGAKGNMDCNGNVKSQPVLWGIY

Enzyme Prediction     

EC	3.2.1.14:3	3.2.1.14:3

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	193	520	1.4e-42	0.9290540540540541

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
119357	GH18_zymocin_alpha	5.86e-161	192	519	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.
214753	Glyco_18	7.17e-34	192	518	2	333	Glyco_18 domain.
395573	Glyco_hydro_18	2.36e-29	193	517	3	305	Glycosyl hydrolases family 18.
405536	Hce2	4.93e-28	1024	1123	2	103	Pathogen effector; putative necrosis-inducing factor. The domain corresponds to the mature part of the Ecp2 effector protein from the tomato pathogen Cladopsorium fulvum. Effectors are low molecular weight proteins that are secreted by bacteria, oomycetes and fungi to manipulate their hosts and adapt to their environment. Ecp2 is a 165 amino acid secreted protein that was originally identified as a virulence factor in C. fulvum, since disruption reduces virulence of the fungus on tomato plants. We have recently determined that Ecp2 is a member of a novel, widely distributed and highly diversified within the fungal kingdom multigene superfamily, which we have designated Hce2, for Homologs of C. fulvum Ecp2 effector. Although Ecp2 is present in most organisms as a small secreted protein, the mature part of this protein can be found fused to other protein domains, including the fungal Glycoside Hydrolase family 18, Glyco_hydro_18 pfam00704 and other, unknown, protein domains. The intrinsic function of Ecp2 remains unknown but it is postulated by that it is a necrosis-inducing factor in plants that serves pathogenicity on the host.
119365	GH18_chitinase	6.87e-26	261	368	107	224	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
BCS24215.1|CBM18|GH18	0.0	19	1137	324	1477
BCS04716.1|CBM18|GH18	0.0	4	1137	314	1462
BCS16285.1|CBM18|GH18	0.0	4	1137	314	1462
EAA32694.1|CBM18|GH18	0.0	18	1137	337	1484
CAP94173.1|CBM18|CBM50|GH18	0.0	18	1137	329	1442

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5WUS_A	2.39e-20	213	566	26	396	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]
1HKK_A	1.19e-19	253	521	83	344	High resoultion crystal structure of human chitinase in complex with allosamidin [Homo sapiens]
1HKI_A	1.20e-19	253	521	83	344	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	1.20e-19	253	521	83	344	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	1.22e-19	253	521	83	344	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	2.79e-91	22	523	225	716	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|Q13231|CHIT1_HUMAN	1.71e-18	253	521	104	365	Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1
sp|P20533|CHIA1_NIACI	2.47e-18	262	646	178	562	Chitinase A1 OS=Niallia circulans OX=1397 GN=chiA1 PE=1 SV=1
sp|Q9W5U2|CHI10_DROME	2.78e-16	213	521	989	1312	Probable chitinase 10 OS=Drosophila melanogaster OX=7227 GN=Cht10 PE=2 SV=2
sp|P36362|CHIT_MANSE	1.32e-15	260	524	118	380	Endochitinase OS=Manduca sexta OX=7130 PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000067	0.000001

TMHMM  Annotations     

There is no transmembrane helices in RHZ56572.1.