CAZyme Information: PMAA_014150-t26_1-p1

Basic Information

• Species: Talaromyces marneffei
• Lineage: Ascomycota; Eurotiomycetes; ; Trichocomaceae; Talaromyces; Talaromyces marneffei
• CAZyme ID: PMAA_014150-t26_1-p1
• CAZy Family: AA7
• CAZyme Description: bacteriodes thetaiotaomicron symbiotic chitinase, putative

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1618	DS995906|CGC8	176915.02	4.2264

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_TmarneffeiATCC18224	10194	441960	145	10049

• Gene Location: location=DS995906:1537095-1543159(+)

Full Sequence      

MADSKANRPWRILLLVVLFVSVTKSQTIYCNTTSPCVNDACCQWKDNQGICGYGSFCQTD
CISNCNATAECGKDAKDPSASCPLNVCCSQWGFCGTGDLFCGNGCQGDNCGDPTVPSCSS
NNVLNRVVGYYESWSSGRACDAWRPSDMAVFAEAVLKTLQQYGFDGVDLDWEYPAASDRA
GKTADTVNYVYLVNQLRKTFDESGQTYGITFTIPTSYWYMQHFDIPAMLEGGADWANLMA
YDLHGVWDGKDPNIGSVIASHTNLTEIKASLDLLWRAGVNPTQIVMGMGFYGRSFTLSDY
SCTEPGCPFSGPGTAGSCSNSSGILSYKEITEIMDEEGSELIWNEEAAVNYLVWGGNQWI
SFDNAQTFQQKVDYANSVCLGGAMIWAVDQDTYDWKALSGLLGQAVDGNDLLNGGSLLES
QKKSLVSELSAYTGADCYISDCVDINTGQCKSGYSVLDYVHSASGNGAALQNPDSKQCHS
GSETDHNSQYRMICCPAHAMPEGCVWEGANEFGLCSGNSSTCGDNKYELVADTYNDRTGT
IRCLINQRSLCCNTNSLLNECHWSGCADSCPTNWTTNEWGSIFGGNNLNPDEGEACPYLY
SFCCPSTDTYKNCEWHYCDYCPSDKVLITRRMEIDFFLNEGYYSRCGDTSTGALYNSFCC
DPPSASENRPVDPADLFEYPDEDHVMYSYEVEKTSNDDVVADNTSATNNENSDPFAFVMI
DGDPEAYDESLVDQWSFLVDEEQLTKRSLKMHERRSIFEYRDDTFDNEVEVYHIQCSTTF
INGTSGCMSIFQGGANNTIVKMPKDIGAGPFARVISLVPVGSTGKSGRSNILPRSSTNTY
ELTVDYDLAGASAERSGDVNFRVDYTNLLEYWKDITDTPSKRRKRWFGGFSAWLSKMTSI
TKKDQGYLPMEYDETIKLFHAQGYCPDLNITATVDLDANIHLALRAQYGYYFEGAILPTP
SLIAAYGYFSVAPEASILFTLRGEAVWQSTTGTQSIISGITFPGLSIKGLISIGPELELT
GKMDASLSISGELNAGVVASWPRAEVYFPQDDGGSDATIMPKDIVGDDPQTFSVDPIFDA
SLTAEGNMALTLTPQVKFGISVLGGSLMSGYVTAGVDNTVSLGINASASVSYDGTTSAGF
CYWADYIYSFFVSADVSFLNDLAYWGSSYEAASPDDPIVLVENTCITYSSNDPLSKRSSV
ESLVANSTGSGCFGGLVECSTTVSAGNSSCTLTSGDEGSGTTTSKRAPQCYNLPALFYNC
DLFGATAVTNRNQNTMQNFGSKSFIGICDNVRNYLQKNPGKIKGNGMELTYFSSNEQQKT
GGNRHDACSAKYKECVQEKTALWPTEVQSMYNWQTTQTINGVRTIVPAPTDYALMQGYDD
SLSCDEFPFNASEEGGTGAEVACVSAHQNDYQGTINSLISNIYDARTGTTMPWSGWTFAK
PWTGQTRKYRINLTSGTHNGYDLSYAGEITYAPYDMAYILGGLNLWGNPELYLSPTTRNA
VCLLGSWYNPLLGINEGRAYGCDVTFAAQTTLFKRAQDPDDPSTWVVEKVQVSAEDLKNP
IPLFTEDGKGYLDNAARNLEGMMEKLNLEADQEKEPMITATPHASHLRSDKESHHYRH

Enzyme Prediction     

No EC number prediction in PMAA_014150-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	147	396	2.7e-51	0.6993243243243243

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
214753	Glyco_18	2.01e-60	146	391	83	334	Glyco_18 domain.
119351	GH18_chitolectin_chitotriosidase	5.74e-59	145	391	94	341	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	6.32e-52	141	389	85	343	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.
395573	Glyco_hydro_18	2.07e-49	129	391	74	307	Glycosyl hydrolases family 18.
119365	GH18_chitinase	1.14e-45	146	391	101	322	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
QGA22188.1|CBM18|GH18	0.0	1	1618	36	1700
EGX48302.1|CBM18|GH18	4.61e-308	12	1550	16	1681
EGX53198.1|CBM18|GH18	1.08e-233	12	1503	11	1684
CAE7022350.1|CBM18|GH18	4.28e-199	12	1452	13	1606
EAA66640.1|GH18	5.48e-186	90	1450	3	1494

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JM7_A	3.82e-37	127	393	81	352	Crystal structure of Ostrinia furnacalis Group IV chitinase [Ostrinia furnacalis],6JMB_A Chain A, ofchtiv-allosamidin [Ostrinia furnacalis]
6JM8_A	4.27e-36	127	393	81	352	Crystal structure of Ostrinia furnacalis Group IV chitinase [Ostrinia furnacalis]
1HKK_A	1.78e-33	151	393	98	344	High resoultion crystal structure of human chitinase in complex with allosamidin [Homo sapiens]
1HKI_A	1.82e-33	151	393	98	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]
5WUP_A	1.84e-33	151	400	196	447	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q13231|CHIT1_HUMAN	7.89e-32	151	393	119	365	Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1
sp|O35744|CHIL3_MOUSE	2.39e-29	145	393	113	367	Chitinase-like protein 3 OS=Mus musculus OX=10090 GN=Chil3 PE=1 SV=2
sp|Q9W5U2|CHI10_DROME	3.46e-29	123	400	1981	2260	Probable chitinase 10 OS=Drosophila melanogaster OX=7227 GN=Cht10 PE=2 SV=2
sp|P36362|CHIT_MANSE	4.66e-29	127	400	101	382	Endochitinase OS=Manduca sexta OX=7130 PE=2 SV=1
sp|Q9BZP6|CHIA_HUMAN	8.02e-29	145	393	113	367	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
0.000306	0.999684	CS pos: 25-26. Pr: 0.9799

TMHMM  Annotations     

There is no transmembrane helices in PMAA_014150-t26_1-p1.