CAZyme Information: AO090103000180-T-p1

Basic Information

• Species: Aspergillus oryzae
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus oryzae
• CAZyme ID: AO090103000180-T-p1
• CAZy Family: GH89
• CAZyme Description: Putative chitin-binding protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1330	Chr8_A_oryzae_RIB40|CGC31	144733.04	4.3795

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AoryzaeRIB40	12364	510516	274	12090

• Gene Location: location=Chr8_A_oryzae_RIB40:802893-807338(+)

Full Sequence      

MLPIKSLFLVTHFLSFATTTPSPTRFRDYDPKDPCPRQCGLVGTDPQDWAVYYSPDALDG
CNRPLLLDFKLDSELDNPNTSVPGLNSSAQNVTLQRIEYDGASGDSLVAAGAVFHIQRYL
EQNVEQDNNVIMFSTSGNATVGFFGGALMDTQRMATSLLPELIRHITHDGFSNGVLEQIC
GTRRNAHEVWGIMVSFSASMSTVQETVRTWSQGKCVTPISPMAGVTSFHSAMIPTTAFNR
RPRVLNARTPTLQRRAECSTIKVLEGDSCGTLANRCGVSGADFEKYNTQSNLCSSLQPGQ
HVCCSAGTLPDFRPKPNPDGSCATYTVLVDESCKSIATANSITLGDLEEFNKKTWGKFSL
LLKQCPVQRSCGLVGWNGCGTLWQGAKICISSGDPPMPNSVANAICGPQVPGTEAPTDGQ
DLASLNPCPLNACCDIWGQCGTTAEFCTYSSSESGAPGTAAPGENGCISNCNANVVSSGP
PEEYLRIGYFEGYNLGRACLNMDAGQIDTEKYTHIHFGFGTLTEDFNVKVGDALSQFEFE
QFKQLTGVKRILSIGGWDFSTSPDTYTTFREGVKSANRMTMAENIANFVEEHDLDGVDID
WEYPGAPDIPGIPPGSADEGVEYAIFLILLKGLLRDKSLSIAAPASYWYLRPYQIAALAD
VLDYLVFMTYDLHGQWDHSNHWAAPGCEEGNCLRSHVNLTETYSALSMVTKAGMPSNKVI
TGIASFGRAFKMTTPGCTGPDCHFTGATSGARAGRCTATQGYLSVAEIDEILSTNPSADT
WTDDSLSNVLVYNETEWVAYMDDANKADRDILYKGLNFGGTVEWATSMHSFHEVPSDALV
PGGSLSDIIKEWPVFVETVINGKSPFIHGDRNGHWADGSITCTDDAVVGVLDIPPKKRWE
DLDCSTAWQDALDKYRQFDLPRNWDFTKSISDTFHGRENMNCGILSAQADCSMSFQCEQS
KGEGSGPAGYEVMNSLMFESLYKGIVGAAGVVASKNLEFVNKFAPIPDYTMTFNLFMDTL
GLVVPAGMAPVFNNVLSRTAYFSANPAMLDNAKDVVYTMVGSWVNIAKDSNPADYGWDEE
DQWEFMGFMTDVWHTWQNETENTSRYLFSGTEDAIRDLSKIIRDGQLIQGSFEGATPPTE
MSATEIQALIERAFYGYLIPRIWQSSGTKAFVIDTNHACDGSNPIPDYLDDTNAETTAVC
FEDKLYYLAYPDGNAGDTCQLPGSTPVCVPLKFKVPPGLDELTGAVKDYGGMKPVDIVAS
TVRSYQANGNKNGWTLKSMGDVQSVDDLNLDALITYQIGAAGFSTLPLCSAEEAHLNWGI
GKDTDNYPCN

Enzyme Prediction     

EC	3.2.1.14:3	3.2.1.14:3	3.2.1.14:3

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	486	828	2.3e-46	0.9256756756756757

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
119357	GH18_zymocin_alpha	0.0	486	829	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	2.12e-53	487	828	3	333	Glyco_18 domain.
395573	Glyco_hydro_18	1.18e-47	487	828	3	306	Glycosyl hydrolases family 18.
119351	GH18_chitolectin_chitotriosidase	8.62e-42	513	832	29	344	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	8.86e-39	507	731	21	267	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
BAE65642.1|CBM18|CBM50|GH18	0.0	1	1330	1	1330
QMW48046.1|CBM18|CBM50|GH18	0.0	1	1330	1	1335
QRD93063.1|CBM18|CBM50|GH18	0.0	1	1330	1	1335
QMW35984.1|CBM18|CBM50|GH18	0.0	1	1330	1	1335
UDD65190.1|CBM18|CBM50|GH18	0.0	1	1330	1	1333

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5WUS_A	1.54e-25	507	831	26	344	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	1.59e-24	507	831	26	344	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]
6JM7_A	7.08e-24	488	841	11	362	Crystal structure of Ostrinia furnacalis Group IV chitinase [Ostrinia furnacalis],6JMB_A Chain A, ofchtiv-allosamidin [Ostrinia furnacalis]
5Y29_A	7.52e-24	507	831	31	353	Crystal structure of Ostrinia furnacalis Group II chitinase catalytic domain 1 [Ostrinia furnacalis],5Y2B_A Crystal structure of Ostrinia furnacalis Group II chitinase catalytic domain 1 in complex with HEPTA-N-ACETYLCHITOOCTAOSE (NAG)7 [Ostrinia furnacalis]
6JAV_A	8.98e-24	507	831	31	353	Crystal structure of Ostrinia furnacalis Group II chitinase catalytic domain 1 in complex with a piperidine-thienopyridine derivative [Ostrinia furnacalis],6JAW_A Crystal structure of Ostrinia furnacalis Group II chitinase catalytic domain 1 in complex with a napthalimide derivative [Ostrinia furnacalis],6JAX_A Crystal structure of Ostrinia furnacalis Group II chitinase catalytic domain 1 in complex with chitooctaose [(GlcN)8] [Ostrinia furnacalis],6JAY_A Crystal structure of Ostrinia furnacalis Group II chitinase catalytic domain 1 in complex with a dipyrido-pyrimidine derivative [Ostrinia furnacalis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P09805|KTXA_KLULA	4.41e-100	133	837	79	720	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|Q6RY07|CHIA_RAT	9.60e-22	548	831	90	367	Acidic mammalian chitinase OS=Rattus norvegicus OX=10116 GN=Chia PE=2 SV=1
sp|Q95M17|CHIA_BOVIN	3.01e-21	484	831	22	367	Acidic mammalian chitinase OS=Bos taurus OX=9913 GN=CHIA PE=1 SV=1
sp|Q9W5U2|CHI10_DROME	4.13e-21	507	857	989	1339	Probable chitinase 10 OS=Drosophila melanogaster OX=7227 GN=Cht10 PE=2 SV=2
sp|Q91XA9|CHIA_MOUSE	7.21e-21	513	831	52	367	Acidic mammalian chitinase OS=Mus musculus OX=10090 GN=Chia PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000583	0.999380	CS pos: 19-20. Pr: 0.9378

TMHMM  Annotations     

There is no transmembrane helices in AO090103000180-T-p1.