CAZyme Information: ASPTUDRAFT_167444-t33_1-p1

Basic Information

• Species: Aspergillus tubingensis
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus tubingensis
• CAZyme ID: ASPTUDRAFT_167444-t33_1-p1
• CAZy Family: GH12
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1482		156825.71	3.8983

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AtubingensisCBS134.48	12592	767770	274	12318

• Gene Location: location=KV878187:4124957-4129633(+)

Full Sequence      

MRLISQLAGGLLASSLLVHPALASTEREIQARARVQKPKPCPAPCSSTDPADWFVYSDLE
RLAQCNESMLLNFNIYNTVTDPQHHSTIYTCTTPGDLASWGPASTNLSDSGSSSPVTYEV
GIWKASSPPGSSQLLALLRDMHSYLTANPHKGELFGYSNRVSVGVYLGGSLQLTPNVDFA
LNEMISLSQNFTYDRAILQYCGSNANNTLGVAVSTNGDITTVQQYIQSWSKADCISDYDS
HSSGTTTLWTSQTGLRNSTGAFDTIASNTSTSSRSSCSYIQVVSGDSCATLVSECGITAA
EFYQYNTASDLCSTLEVGQYVCCSSGGLPDFSPSAYSNGTCYTYTVQSGDTCSALAQTYS
LTVAEIDSYNNDTWGWYGCDDLQAGTNICLSTGNAPYPAAITNAVCGPQVPGTNFTDAPT
SFYWAQLNPCPLNACCDVWGQCGTTPLYCNDTRASTGAPGTAAAGSNGCIYNCGTNITNY
AEEPSGYDVIGYLEASSVNRTCLRWEASDVNTTKYTHVNFGFGNIASDFSINVDGMESDF
NLFLKLVGTKRILSFGGWDFSTSSSTYMIFREGTAAANRETFATNVANFVTEKGLDGVDF
DWEYPGEPDISGIPAGGSDEGENYLEFLKVLRALVANDTIISVTAPSSYWYLKAFPIAEM
AEVVDYINYMTYDLHGIWDLGNEYSQWGCSDGDCLFSHVNMTETMWALAMITKAGVATKD
IRVGVSSYGRSFHMTTAGCYESWCTYDTAGAAGPCTDTAGYIAEAEMDEILASDTTTQTY
STYDTDILVYNETQWVGYMNSTTRASRMAYYEQFNFGGTAEWAIDLETNPLGDSDDDDDD
GTSPLTTTTSTTTVTIDPTVWMEPSPVVTCVPPCLMIMPPKPLETTTTITFSEWDTHITW
ASTATKTTTLANGNVVTYKSMQNSAIPTRLSIAPVTTNYVNVWNQAITPGQTRVYQTSSI
LPTPFPVVYTPTVGGVTNVYGGTTSTIAGVSWSFGNATYTSPAWTGVFGGTTSVTGGTTL
SPSTTIVTPHPYPTDTSTTDPVLNTRTTRMSTGSPAGPTPTSSGEHTGHHCVIFCACAAC
PPDLDLDGSFGGEDDSGGGGSSGSSGSSNDSGDDSDDESSSTSSTSTSTETADVTMGGAG
TTIYYEFVPTAASTNSALQSSIDQYLGSVFRSLYGSEVAAITATETGTAAEASITSSSPL
CVEAQDPDSGSDDTVCSCSGGSGSYPTLTVGTNPCGYTALPTKTTIDAYPYTFTQADGWI
VGCASTGIIDDVSYCTGSRTTVGVDRTIDPYPYTFTQADGDIVACATTGIIDHVSYCSGS
RTTVSTASATATETSQAFAIWRTKTVEKSCVNSNCITVTDGNKVIASSADTTDGDFCEDL
AYEATNSNTGKALTTKLVADFTFSDWSVCGVSGGYSCTETSSTSGVWECADADGGNTARC
VKSTDSSSPLVTCEETRTGNGEDVYSYLLANCTAEWSCAVDF

Enzyme Prediction     

EC	3.2.1.14:3	3.2.1.14:3

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	487	826	4e-47	0.9324324324324325

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
119357	GH18_zymocin_alpha	6.63e-165	490	827	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.
214753	Glyco_18	3.12e-54	489	826	2	333	Glyco_18 domain.
395573	Glyco_hydro_18	1.57e-47	489	825	2	305	Glycosyl hydrolases family 18.
119349	GH18_chitinase-like	7.43e-39	489	674	1	178	The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant polymer of beta-1,4-linked N-acetylglucosamine (GlcNAc) which is a major component of the cell wall of fungi and the exoskeleton of arthropods. Chitinases have been identified in viruses, bacteria, fungi, protozoan parasites, insects, and plants. The structure of the GH18 domain is an eight-stranded beta/alpha barrel with a pronounced active-site cleft at the C-terminal end of the beta-barrel. The GH18 family includes chitotriosidase, chitobiase, hevamine, zymocin-alpha, narbonin, SI-CLP (stabilin-1 interacting chitinase-like protein), IDGF (imaginal disc growth factor), CFLE (cortical fragment-lytic enzyme) spore hydrolase, the type III and type V plant chitinases, the endo-beta-N-acetylglucosaminidases, and the chitolectins. The GH85 (glycosyl hydrolase, family 85) ENGases (endo-beta-N-acetylglucosaminidases) are closely related to the GH18 chitinases and are included in this alignment model.
119365	GH18_chitinase	4.73e-38	509	733	20	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
UKZ53593.1|CBM18|CBM50|GH18	7.85e-253	45	1089	86	1139
UKZ79393.1|CBM18|CBM50|GH18	4.50e-251	45	1071	86	1123
BCS25711.1|CBM18|CBM50|GH18	6.80e-229	45	948	44	952
QQK44152.1|CBM18|CBM50|GH18	2.79e-221	46	827	64	874
QMW24763.1|CBM18|CBM50|GH18	6.93e-220	50	948	46	952

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5WUS_A	5.32e-27	489	827	4	342	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	5.53e-26	489	827	4	342	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]
5WUP_A	7.35e-24	482	827	88	438	Crystal structure of a insect group III chitinase (CAD1) from Ostrinia furnacalis [Ostrinia furnacalis],5WV9_A Crystal structure of a insect group III chitinase complex with (GlcNAc)6 (CAD1-(GlcNAc)6) from Ostrinia furnacalis [Ostrinia furnacalis]
6JM7_A	1.46e-23	489	827	6	350	Crystal structure of Ostrinia furnacalis Group IV chitinase [Ostrinia furnacalis],6JMB_A Chain A, ofchtiv-allosamidin [Ostrinia furnacalis]
2YBT_A	1.65e-23	483	827	1	348	Crystal structure of human acidic chitinase in complex with bisdionin C [Homo sapiens],2YBT_B Crystal structure of human acidic chitinase in complex with bisdionin C [Homo sapiens],2YBT_C Crystal structure of human acidic chitinase in complex with bisdionin C [Homo sapiens],2YBT_D Crystal structure of human acidic chitinase in complex with bisdionin C [Homo sapiens],2YBT_E Crystal structure of human acidic chitinase in complex with bisdionin C [Homo sapiens],2YBT_F Crystal structure of human acidic chitinase in complex with bisdionin C [Homo sapiens],2YBU_A Crystal structure of human acidic chitinase in complex with bisdionin F [Homo sapiens],2YBU_B Crystal structure of human acidic chitinase in complex with bisdionin F [Homo sapiens],2YBU_C Crystal structure of human acidic chitinase in complex with bisdionin F [Homo sapiens],2YBU_D Crystal structure of human acidic chitinase in complex with bisdionin F [Homo sapiens],2YBU_E Crystal structure of human acidic chitinase in complex with bisdionin F [Homo sapiens],2YBU_F Crystal structure of human acidic chitinase in complex with bisdionin F [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P09805|KTXA_KLULA	1.24e-102	277	825	193	710	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|Q95M17|CHIA_BOVIN	2.37e-26	470	827	5	365	Acidic mammalian chitinase OS=Bos taurus OX=9913 GN=CHIA PE=1 SV=1
sp|Q91XA9|CHIA_MOUSE	1.03e-25	481	827	16	365	Acidic mammalian chitinase OS=Mus musculus OX=10090 GN=Chia PE=1 SV=2
sp|Q6RY07|CHIA_RAT	1.38e-25	485	827	20	365	Acidic mammalian chitinase OS=Rattus norvegicus OX=10116 GN=Chia PE=2 SV=1
sp|Q9BZP6|CHIA_HUMAN	8.53e-21	550	827	91	365	Acidic mammalian chitinase OS=Homo sapiens OX=9606 GN=CHIA PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000766	0.999203	CS pos: 23-24. Pr: 0.9708

TMHMM  Annotations     

There is no transmembrane helices in ASPTUDRAFT_167444-t33_1-p1.