CAZyme Information: SPSK_02915-t39_1-p1

Basic Information

• Species: Sporothrix schenckii
• Lineage: Ascomycota; Sordariomycetes; ; Ophiostomataceae; Sporothrix; Sporothrix schenckii
• CAZyme ID: SPSK_02915-t39_1-p1
• CAZy Family: CE9
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1669	AXCR01000010|CGC24	183745.31	5.4811

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Sschenckii1099-18	10434	1397361	141	10293

• Gene Location: location=AXCR01000010:382438-388656(+)

Full Sequence      

MPKAVGGNSASGRKIGYWQSSNVRKRQYKDGKFKCPPVRPGDIPLDTNIPSVAVGRIYTM
LLAPLYTEFTALKYRPNGPQTWIAVGGFDFSDPGVDPDAETDTAPDVSTHSTWSDMAMTT
DRRTAFIQLLITFMDKYGFQGIDLDWEYPVSEDRGGRPEDTKNFVSLVREMRQAFGTKYG
ISVALAPDFWYLRYFDAVAMQPYVDWFGFMAYDLHGVWASDSKSKLVRGHTDAEEIYKDI
IPLSFDGLDFRKINFGMAIYGRGFTLADPKCRAMDGTCSWTGGNEAGICTDFSGVLSYDE
IQQKILDAQRQNRAGPTLDPTTMMKYLTWGDKQQNWIGYYDQETWQLKKTNLADKYGFGG
TLFWSVDFMGQGMNISDVYIDPSLVCQDGNNGNRIASCHQPCRLIMPQCAIPTTTVTATY
TITFEVYQGPSSTLTETMITEVTVTTASISFSPVYVGGGRNGGDTFTPVPIIPMPSMILS
VTPTAGGTVTTRTVTLPNWPTTGQWPPPGGVTNQDPWQAPTHSDASSSTSTQEPFAPLPP
LYPITGPTDPPVPKETDFRTTETTETTSTTTAAVVIMTWPPGVIEPTDNDDDDIIPCHAW
FLTGFKLNFPIPPGLYIFPPPDPPSIKPPPGMNINLKPEPHIILTRGKDNKWTTSQRSDQ
TSSCAHSTTVFDTATSVTATVTISGKSTWTSTATVRSTQIPRTGCHLQATATTGQTFVTN
TNCPHARGIVAFERKNEEDDSDSDGSDADGSDSDSSEWADHQLHSAQRHANNKSLGHDDN
LSQSRPGKNTRKSTSRRHPSAPQSPHRREENNDIDIDCWFGHYGILLPADPLNVVDIDRL
LDDYKANRNLQFTKIWAPSHRGFTAGYFLEDATIRLENELIALRNSGILRPFFYIDHFHF
SDSSDGSLGGSLRRRTRPVMSFNITETKAQNREQEVRRSTNVVAKSSSWSASQVSVPRGV
RWPNDQSRIGNDYHYYYHPSAGQGQNIHVCEADDIPWHAHTVSIDVIAATLCSRQVHSDH
VGQEFSNFQSRNLPVRAYSVRGGPVFTGDGYHEPLVHKGRHASQVAAMAVGQHLGIAKRA
NLWTSTAGAESFIESDVFEVAFWLNDALVEILESIASQNNAHTAVLSISFDSELSENPAM
IGLDLMGTIFCWFRPSLTAAILFEFYKLNIPIIMSSGNIYNKDPAILWPPILAYETYRGY
NSIPGTPNRNELRNFANSIMLVGATTKNGPKADFSQFSSLVQLHAPAKALWEVQAPKHGN
GLIETNDADAQGTSYAAPQVAGLIAYFRALPNTDLQKRLSDVRTLKYFLGKLARVLNVMP
GLPMPPKYKARFPETLMVRTIWNGQLPEDLSCLVQEDIDKMTEAQRNVCPDIKNDKFWND
AKYWNAISTTEDNDKGQTIEWQPGEPGPLCSAAAPSTTPSKGSGRATLPPELNGRAPQIV
LGPGQCGTGCNSDWYCDDSPDGVPPFYRDPKDPNKSNPYLGILPVPIPIPTPLPSTAPQV
RHCHFHITKIFTYTTSIAPTSPTLSRLACTSYDPNNANTVLGTKNIGTASGNKLVWSASQ
SRLPADIHFALSSCLVPRSMNFRRGVDGTDDTDSTDSVDEVDSADGTDGADSMDGSDDSP
LESDNCVITFTTSGHTWSTDDRDSAKAAYCNVGKYSGHLTQDMDCFYTC

Enzyme Prediction     

No EC number prediction in SPSK_02915-t39_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	13	369	1.3e-46	0.9324324324324325

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
214753	Glyco_18	9.56e-54	13	367	1	332	Glyco_18 domain.
119351	GH18_chitolectin_chitotriosidase	1.28e-48	65	368	57	340	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	1.87e-46	69	367	56	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	5.43e-42	66	368	50	306	Glycosyl hydrolases family 18.
119365	GH18_chitinase	3.27e-35	83	367	89	320	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
CEI60137.1|CBM18|GH18	2.83e-98	4	1411	162	1412
CAE7012155.1|CBM18|GH18	5.78e-90	5	368	61	405
CEI67947.1|CBM18|GH18	7.23e-88	4	395	221	592
QPC78129.1|CBM18|GH18	1.87e-86	4	368	210	557
CZS83249.1|CBM18|GH18	2.22e-86	4	368	221	568

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5WUP_A	2.02e-24	65	367	153	436	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]
3FXY_A	5.35e-24	65	412	55	387	Acidic Mammalian Chinase, Catalytic Domain [Homo sapiens],3FXY_B Acidic Mammalian Chinase, Catalytic Domain [Homo sapiens],3FXY_C Acidic Mammalian Chinase, Catalytic Domain [Homo sapiens],3FXY_D Acidic Mammalian Chinase, Catalytic Domain [Homo sapiens],3FY1_A The Acidic Mammalian Chitinase catalytic domain in complex with methylallosamidin [Homo sapiens],3FY1_B The Acidic Mammalian Chitinase catalytic domain in complex with methylallosamidin [Homo sapiens],3RM4_A AMCase in complex with Compound 1 [Homo sapiens],3RM4_B AMCase in complex with Compound 1 [Homo sapiens],3RM8_A AMCase in complex with Compound 2 [Homo sapiens],3RM8_B AMCase in complex with Compound 2 [Homo sapiens],3RM9_A AMCase in complex with Compound 3 [Homo sapiens],3RM9_B AMCase in complex with Compound 3 [Homo sapiens],3RME_A AMCase in complex with Compound 5 [Homo sapiens],3RME_B AMCase in complex with Compound 5 [Homo sapiens]
3WL1_A	2.34e-23	66	367	67	357	Crystal structure of Ostrinia furnacalis Group I chitinase catalytic domain in complex with reaction products (GlcNAc)2,3 [Ostrinia furnacalis],3WQV_A Crystal structure of Ostrinia furnacalis Group I chitinase catalytic domain in complex with a(GlcN)5 [Ostrinia furnacalis],3WQW_A Crystal structure of Ostrinia furnacalis Group I chitinase catalytic domain in complex with a(GlcN)6 [Ostrinia furnacalis]
2YBT_A	3.45e-23	65	367	59	346	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]
3WKZ_A	5.67e-23	66	367	67	357	Crystal Structure of the Ostrinia furnacalis Group I Chitinase catalytic domain E148Q mutant [Ostrinia furnacalis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P09805|KTXA_KLULA	9.43e-27	16	368	371	711	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|Q9BZP6|CHIA_HUMAN	9.88e-23	65	412	76	408	Acidic mammalian chitinase OS=Homo sapiens OX=9606 GN=CHIA PE=1 SV=1
sp|Q6RY07|CHIA_RAT	1.71e-22	65	367	76	363	Acidic mammalian chitinase OS=Rattus norvegicus OX=10116 GN=Chia PE=2 SV=1
sp|Q91XA9|CHIA_MOUSE	1.71e-22	65	367	76	363	Acidic mammalian chitinase OS=Mus musculus OX=10090 GN=Chia PE=1 SV=2
sp|Q9W5U2|CHI10_DROME	3.79e-20	72	367	1972	2251	Probable chitinase 10 OS=Drosophila melanogaster OX=7227 GN=Cht10 PE=2 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000035	0.000007

TMHMM  Annotations     

There is no transmembrane helices in SPSK_02915-t39_1-p1.