CAZyme Information: ATEG_06214-t26_1-p1

Basic Information

• Species: Aspergillus terreus
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus terreus
• CAZyme ID: ATEG_06214-t26_1-p1
• CAZy Family: GH32
• CAZyme Description: conserved hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1301		141792.98	4.9900

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AterreusNIH2624	10551	341663	150	10401

• Gene Location: location=CH476601:1624648-1628803(+)

Full Sequence      

MKPNIKTLSISYLTFLSLSTFPTPTDASASGALGLVAPMGDLRTEDPIASALVHGCPQSC
TTLGSDPAKWTQIHDLNILERCKGSTLFAFNIQNELDVNTPMVSCSFLEEYPKRVLPKVA
QATWEKINTEDIDAVSEHIMGSGSCGATVSPMEVVLQSGNVGDLGSGSNFTNNAVAAVKN
LASYMADASSCGTTILFSKKEDSVAALYAGADVLHTDVGDTLDHFGLVRPHEINFHPSFL
FIALRYIPTNEVEQGARAVQVCDANSERARTIGLFVARSVDGLGDAQRALQTWASGECIS
LANLKTSETSIRSLEATNKTKRSSPFSLFSSLLTLRAECRAIQVASGDSCGALASRCGIT
SADFNKYNRKRNLCATLKPKQYVCCSLGSLPDIKPKPQADGTCATYTVQDNDNCKDIAAQ
YGLTTKDIETFNKATWGWAGCSRLQRDQVICTSKGNTPMPAAISNAVCGLQTPGTKKPKG
DFTGFNLTKLNPCPLNACCSGWGFCGTTMEFCTESPADTGAPGAFKSGMNGCISNCGTNI
MNNNEKPKFFRRVTYYEAYNMDRDCLNMDVREINDDDLTHVHFAFAGLTSNIEIMFDDSY
KDQFGAFIEMHAPWKKILSFGGWAESTDAATFQRYKDVVKPENRERFANNVVAFVNKHKL
DGIDFDWEYPGATDIPGVPGGQGETDHYLNFLKLMREKLGDKSLSIALPASYWYLKPFPV
EKMAKYLDYFIYMTYDLHGQWDFGNKNASPGCANGNCLRSHVNKTETHDALAMITKAGVP
ANQVVVGVSSYGRSFGMADPNCTGPMCKFTGSFNCTNTSGYISNAELMLLSDNALLGYDG
YHARSWHDDDSDSDIMVYGEDEHAHSWVAYMSEDTKAGRIEWVKGLNFGGVSDWAIDLGD
WYDGVDPDDHSSSALLAGGRTFDGCPSNNWPDTLDELNDNLDKIAVDCGSQAVVHVLLMQ
VNDAVSNYKAISSGDYDEKFKYYAKWIRDGINDSLDKFMRQNGSKHMDCEWKDAGVSGSG
PCTEMKRGSLNGNQYVTWKMRDEDGFYKDLLADYGIQKDWIQWKGSVQKVLPCNCPQVGE
NCLMCSPGVQYGEIYYNYPCRKDNDDDIAVPNPKTIIDSSIPNITSLSSVMLSSYFDMRT
FTLDADYGDVATSFSMPVFMLQDATEQMKTIKKIGAEVEAAEKKQLIMGILTIVFMVIPF
AGDAAAALGGAAAIARMALVIGEAGNAALSIADMIDDPSSAPFAIVGLLLGAGTAGRPTR
SAFKQAADARRALSADKLMLFSDTFRRKDSIVQNIVKRCAG

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	552	897	6.9e-56	0.9222972972972973

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
119357	GH18_zymocin_alpha	0.0	551	899	1	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	3.49e-61	551	898	1	333	Glyco_18 domain.
395573	Glyco_hydro_18	2.99e-54	551	897	1	305	Glycosyl hydrolases family 18.
119365	GH18_chitinase	1.90e-44	573	795	21	266	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.
119351	GH18_chitolectin_chitotriosidase	4.13e-39	579	900	29	342	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCS24971.1|CBM18|GH18	0.0	185	1300	1	1108
CZS82985.1|CBM18|CBM50|GH18	0.0	36	1299	52	1321
CEI63358.1|CBM18|CBM50|GH18	0.0	36	1299	52	1315
ALI93563.1|CBM18|CBM50|GH18	0.0	41	1299	57	1308
ANH56471.1|CBM18|CBM50|GH18	0.0	41	1299	57	1308

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JM7_A	3.23e-30	553	921	7	376	Crystal structure of Ostrinia furnacalis Group IV chitinase [Ostrinia furnacalis],6JMB_A Chain A, ofchtiv-allosamidin [Ostrinia furnacalis]
6JM8_A	3.53e-29	553	921	7	376	Crystal structure of Ostrinia furnacalis Group IV chitinase [Ostrinia furnacalis]
1HKK_A	1.03e-27	579	901	31	344	High resoultion crystal structure of human chitinase in complex with allosamidin [Homo sapiens]
1HKI_A	1.05e-27	579	901	31	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	1.05e-27	579	901	31	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P09805|KTXA_KLULA	1.89e-101	354	998	205	808	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	2.48e-26	579	901	52	365	Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1
sp|Q95M17|CHIA_BOVIN	1.18e-24	579	901	52	367	Acidic mammalian chitinase OS=Bos taurus OX=9913 GN=CHIA PE=1 SV=1
sp|Q9BZP6|CHIA_HUMAN	2.24e-23	579	901	52	367	Acidic mammalian chitinase OS=Homo sapiens OX=9606 GN=CHIA PE=1 SV=1
sp|P36362|CHIT_MANSE	2.42e-23	570	901	44	377	Endochitinase OS=Manduca sexta OX=7130 PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000432	0.999547	CS pos: 27-28. Pr: 0.9667

TMHMM  Annotations     

There is no transmembrane helices in ATEG_06214-t26_1-p1.