CAZyme Information: CPSG_07745-t26_1-p1

Basic Information

• Species: Coccidioides posadasii
• Lineage: Ascomycota; Eurotiomycetes; ; Onygenaceae; Coccidioides; Coccidioides posadasii
• CAZyme ID: CPSG_07745-t26_1-p1
• CAZy Family: GT2
• CAZyme Description: conserved hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1777		197876.90	6.3391

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CposadasiiSilveira	10379	443226	154	10225

• Gene Location: location=GL636501:183280-189774(-)

Full Sequence      

MRSLAFLILHAGLAILASAFPHSHNHGHRHLHHSLKPRDESPNTCRNPASIFDYSAKSRG
DDALPICPAAQENVKFLLATDFNIAEDYSCAPDRPCSNGACCPKKTLSCNYGEEYCGTNN
ISPNEVCWSNCDAKAECGKNADPPGKECPLNVCCSKWGFCGMTKEFCEKGTDDEPGCQSN
CDQPRPGKKASEQNIIIGYYEAWRHDSNCQGMGLKDIPVNSLTHLFFSFGYITPGDFKIA
GMDGLPDKLFSDFTSLKKKNPGLKTVIALGGWTFNDPGPTQKVFSNMVSTKENRAKFIDN
LFSFMRQYAFDGVDFDWEYPGADDRGGIPGDGKNFVKFLKELNDVNKKQPMHYSVSFTAP
SSYWYLRHFDLKAVDYVDFVNMMTYDLHGVWDRDNPIGSHIYGHSNITEMRLALDLLWRN
DVPAHKVNMGLGFYGRSFQLQDPACDKPGCVFKGGAAKGACSGESGILTYREIMAMIKTD
KLKPFHDKTAGVKYITYSGDQWVSYDHTVSLLGLEGANCSQDDAETFKQKKELAKELGLG
GYLIWAIDQDDDDLSALQAVIAPKRLGDFKDNAKDKSLYDDAYIPDCYVTGCDGNCKAGF
IKITEQKCGKDDKKSKLCCPLAGAPNPDDCTWRGTAPLCNGHCNDDEVLLQLNKWGSGHH
CNDGHKAYCCKSPLAQENKCYWQGIGKKCNSGDKAMTFSGTFLSDLVDIAQKIFDIIGRR
TPIGLLFGDELSEVLDAIELDLMKLYCCPEEDAKKWKNCKWHGEPGSCFDNHCDANSEVQ
LTDSYYGAGDTCGVKLERARVFCCQPVKGEHLFLPVPLENLFKDPPTGDNIDTDFDLNLD
DEDDNPSDTAFQFVVLTSPEELQVSIDKRDGSHWEVFGCKDAVTEGEHTIQMVCTDFSET
SNCYKIGLGHGVPGTILQMPKGCGPGKYAVAKSMEPAKRQMVPRHLAHLGSRGVVYDLTF
DYDFSRVPRDLGNTQMRVDFSNQDNYWDEVVAATPSKKRKRSLEDVGGNHVRWLEEEFRD
DYHFGGLDKRELQERWFGSTVLEWLKKMVKPEIKRDFTHDVDETFTAVIVDETWECERNN
VKYDGHISAKALTNMRVSTSFGFTMIVTSLIAPLDLSKSYLTFYNEGEITATLTLDAVAS
ISYSKEKTILTLPFPGTSFRIPGIATIGPQIHISGGLDAQLSVAAKFETKISIAKWEIRQ
TLPDGGMDEYKPKEIGPGDPDLDRTGDFSGIQRPEFYAGVAVEGDITAKLSAAAEFGVRF
DDRWKVGGATVGVVGEGSILVKMAAGISTEATCPFTYGMQVGAKLYARADASILKWPETT
YDIVGWEKDIIKGGTCPNLGGLPTVQGSMPLGLPWSTEGNMTSKAHLKHSENASHHSLQK
RAAVYGPKFHIPVGDLFCPKDEAGPDFPENRNDCLQIPGIWDNDKYLTDGDDYYSLTSGA
RASLDTRGELEKRSNTKESLLCGKLLMKSTYPTGGELPKAPIYGFEKIDCDDYSFGTPLT
SRVKGIQYDTEHILEFQLPGKFLAYLNKTKGLVYDHPDPNWKNGQGKRVKVSFCTYFEAL
WDIDPINIGGSKSTPVAHLGDCYPTKTRYSNELVVLEHRINIPSKGKAWGSDSQIVASKT
LKDGVEKQPDQAVKTLRELVGSVLYHKDPTIAAHLKRQKERVGKMFGLIDKELSKHPRVV
NNVKYTPWKPQGLEKEWNKYMRRQHILAFTKTTKPVIDWTPKLKDLWASKAARDAAEPDP
NDNQMQQDEKKKKRALIKKIDALDKARSAFSQWKNPF

Enzyme Prediction     

No EC number prediction in CPSG_07745-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	195	555	2.4e-67	0.9493243243243243

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
214753	Glyco_18	9.32e-90	196	550	2	334	Glyco_18 domain.
119357	GH18_zymocin_alpha	8.29e-83	197	548	3	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.
119351	GH18_chitolectin_chitotriosidase	1.81e-76	215	551	21	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.
395573	Glyco_hydro_18	7.02e-76	196	550	2	307	Glycosyl hydrolases family 18.
119365	GH18_chitinase	3.59e-67	196	550	1	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
QVM13519.1|CBM18|GH18	0.0	1	1777	1	1761
ATY59023.1|CBM18|GH18	0.0	40	1776	32	1839
QPG94581.1|CBM18|GH18	0.0	40	1776	39	1842
CBX95390.1|CBM18|GH18	0.0	32	1777	28	1779
UQC79223.1|CBM18|GH18	0.0	44	1760	48	1757

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1HKK_A	1.09e-45	196	551	3	343	High resoultion crystal structure of human chitinase in complex with allosamidin [Homo sapiens]
1HKI_A	1.12e-45	196	551	3	343	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	1.12e-45	196	551	3	343	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]
4WJX_A	1.51e-45	196	551	3	343	Crystal structure of human chitotriosidase-1 catalytic domain at 1.0 A resolution [Homo sapiens],4WK9_A Crystal structure of human chitotriosidase-1 catalytic domain in complex with chitobiose (0.3mM) at 1.10 A resolution [Homo sapiens],4WKA_A Crystal structure of human chitotriosidase-1 catalytic domain at 0.95 A resolution [Homo sapiens],4WKF_A Crystal structure of human chitotriosidase-1 catalytic domain in complex with chitobiose (2.5mM) at 1.10 A resolution [Homo sapiens],4WKH_A Crystal structure of human chitotriosidase-1 catalytic domain in complex with chitobiose (1mM) at 1.05 A resolution [Homo sapiens],5NR8_A Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound 7a [Homo sapiens],5NRA_A Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound 7g [Homo sapiens],5NRF_A Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound 7i [Homo sapiens]
1GUV_A	1.56e-45	196	551	3	343	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	1.25e-49	110	587	286	744	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	5.75e-44	196	551	24	364	Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1
sp|Q95M17|CHIA_BOVIN	5.25e-40	196	551	24	366	Acidic mammalian chitinase OS=Bos taurus OX=9913 GN=CHIA PE=1 SV=1
sp|Q91XA9|CHIA_MOUSE	5.85e-39	196	551	24	366	Acidic mammalian chitinase OS=Mus musculus OX=10090 GN=Chia PE=1 SV=2
sp|Q6RY07|CHIA_RAT	5.85e-39	196	551	24	366	Acidic mammalian chitinase OS=Rattus norvegicus OX=10116 GN=Chia PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000228	0.999758	CS pos: 19-20. Pr: 0.9808

TMHMM  Annotations     

There is no transmembrane helices in CPSG_07745-t26_1-p1.