CAZyme Information: SPBR_02181-t41_1-p1

Basic Information

• Species: Sporothrix brasiliensis
• Lineage: Ascomycota; Sordariomycetes; ; Ophiostomataceae; Sporothrix; Sporothrix brasiliensis
• CAZyme ID: SPBR_02181-t41_1-p1
• CAZy Family: CE15
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1556	AWTV01000006|CGC20	167320.10	5.2505

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Sbrasiliensis5110	9231	1398154	140	9091

• Gene Location: location=AWTV01000006:3983892-3988963(+)

Full Sequence      

MPPTNRTSPKPLLTGVAAFVGRVLLPLLCLTGQCHGEATSTNAADSSLASLDHLLDGLDT
PPLNGGFTYLPDFHECPLPCSDYANVFSWVRYWTPDQLQRCNEPLLLQFSVEQPVASSAS
SSFGAGVPIYACSLSPTAAGSSTASPPPIDNPKTSNDLNKDQLSRAVACAAPSSPSSSPR
GNITAVQKLVVSSGASWNGSGDGSDVSAMMKGLQSFFEAQGNCDETLVFARHKQTTMGMY
VGASLGKAATTDAVLTSLSSRLQTAGAASQPLVAQLCGNSGSNNRTTEQTLGIAMDATGD
LSIVQQAVAAWSKGNCVSSLGSSLQQDASPVEAHVVDLSPTPPRINNTLAVSRRFLGSRY
LRGRSADDAAVSAATPTPPVKNSDGTCASYVIQKTDTCSKLATQYGINVTDIEKWNANKT
WAWTDCAGMMYGNNMCLSEGRPPLPPPQQGVECGPTLPGTTLPTNKSVSMADLNPCPLNA
CCSNWGFCGVFPQHCDIHKAPGSDSPGAKDKKFQNTCISNCNRDIKQNSGPPDTQMRVGY
YEAFGMDRPCLNLKAKNANVGGVYTHIHWAFAAIDPTTLKPVINDTDKQWADFKALQDVK
RIVSFGGWSFSTDAATFEVMRKAILENRDTFAANVLRFVNDEGLDGADFDWEYPAAPDIF
AGGQPIGQKGDGLGYLKFLITMKQKLGKDKSLSIAAPASFWYLKPFPIDRISSAIDYIVY
MTYDLHGQWDYGNANSFDSCTSGKCIRSHVNLTETKNSLSIITKAGVANNKVVVGEASYG
RSFHMAEPLCWGPLCEFTGSRNQSDATPGRCTQTAGYIANAEINELIRQGAQSIYDGSSD
TDVVLYNGDYVAYMTPTTQDRRRDTWKGLNFAGTVNWAVDLQAFTADDMDNASGDRGKPG
SEGCIAGDDLTVDTGDLCQFTCDLGFCPESLCYCTERGILDPLPAVKNGSANDVVIAWNE
QGIDINKMCKFACTYGYCPDDVCTTPLETMVEDDSDDTPPEANPDDDPRVANANKCLIYE
NGDHDDSVAPCKIYCKPQLDAAAAAGRTSNYGCIGCYLIMSTLKLVVDIGSNIFTGGALS
AGLNAVTTAAQIVNYVYPNDQDPQGAFDWWLSPCGNTDLVPDDIKKAFGILSDVADTVTG
FKGPKNIPKGSGRHGDDGNPEDQSKPRPTSNEPKPTSKPTDKPTGKPTDKPTGKPTDKPT
ACPVPTKKVRRGMGIGAGHGGVPQTTTRPDGAVETLWPRGEAGIMTADQHGEYESYDSEY
YVDEVDSINASCKNNKAKKCKIPKGKDVQRLGAGKNTLRKLSCVNNVVKTQEMIVTSLVY
AAAATSSVVARKCEAAWTQACYHYRSVIRENPQYATLTCPQEAASTKHRQDAEATKVWSD
QHKGKGWLDSQHRQWPKCDRDEYPPAYLLNDADPAFVNSGHNRNGQLVRFVPGTQNQRAG
GMWKGVCFNGPVKELSDREFQDRVARSPHTNVIHDTNLVQTEAAITVDQRPEFTINSWGP
PSSPDDGLGSNPCWPSAIAPQDPGFALLTYDKYYDTHPMPYNYLAAYVPPAAPQPT

Enzyme Prediction     

EC	3.2.1.14:3	-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	538	882	1.6e-43	0.9256756756756757
CBM24	904	983	8e-17	0.9736842105263158

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
119357	GH18_zymocin_alpha	8.35e-166	536	882	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	3.39e-43	538	881	3	333	Glyco_18 domain.
395573	Glyco_hydro_18	8.14e-42	538	880	3	305	Glycosyl hydrolases family 18.
119365	GH18_chitinase	4.26e-33	538	784	2	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.
119351	GH18_chitolectin_chitotriosidase	9.08e-31	565	891	29	345	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
QYT05739.1|CBM18|CBM24|CBM50|GH18	0.0	59	1548	38	1514
UKZ57771.1|CBM18|CBM24|GH18	0.0	59	1547	38	1493
QPH01779.1|CBM18|CBM24|CBM50|GH18	0.0	25	1548	4	1513
AIT18865.1|CBM18|CBM50|GH18	0.0	59	1538	35	1520
CZS72048.1|CBM18|CBM24|CBM50|GH18	0.0	59	1537	34	1530

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1E9L_A	7.27e-23	540	885	6	347	The crystal structure of novel mammalian lectin Ym1 suggests a saccharide binding site [Mus musculus],1VF8_A The Crystal Structure of Ym1 at 1.31 A Resolution [Mus musculus]
3FXY_A	9.87e-22	565	885	31	347	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]
2YBT_A	1.10e-21	565	885	35	351	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]
6JM7_A	2.59e-18	565	884	34	352	Crystal structure of Ostrinia furnacalis Group IV chitinase [Ostrinia furnacalis],6JMB_A Chain A, ofchtiv-allosamidin [Ostrinia furnacalis]
5GZU_A	6.51e-18	564	877	50	372	Crystal Structure of Chitinase ChiW from Paenibacillus sp. str. FPU-7 Reveals a Novel Type of Bacterial Cell-Surface-Expressed Multi-Modular Enzyme Machinery [Paenibacillus sp. FPU-7],5GZU_B Crystal Structure of Chitinase ChiW from Paenibacillus sp. str. FPU-7 Reveals a Novel Type of Bacterial Cell-Surface-Expressed Multi-Modular Enzyme Machinery [Paenibacillus sp. FPU-7],5GZV_A Crystal Structure of Chitinase ChiW from Paenibacillus sp. str. FPU-7 Reveals a Novel Type of Bacterial Cell-Surface-Expressed Multi-Modular Enzyme Machinery [Paenibacillus sp. FPU-7],5GZV_B Crystal Structure of Chitinase ChiW from Paenibacillus sp. str. FPU-7 Reveals a Novel Type of Bacterial Cell-Surface-Expressed Multi-Modular Enzyme Machinery [Paenibacillus sp. FPU-7]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P09805|KTXA_KLULA	3.28e-79	289	896	133	724	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|Q91XA9|CHIA_MOUSE	2.06e-23	565	890	52	373	Acidic mammalian chitinase OS=Mus musculus OX=10090 GN=Chia PE=1 SV=2
sp|Q6RY07|CHIA_RAT	2.75e-23	565	890	52	373	Acidic mammalian chitinase OS=Rattus norvegicus OX=10116 GN=Chia PE=2 SV=1
sp|Q95M17|CHIA_BOVIN	1.55e-22	538	885	25	368	Acidic mammalian chitinase OS=Bos taurus OX=9913 GN=CHIA PE=1 SV=1
sp|O35744|CHIL3_MOUSE	5.03e-22	540	885	27	368	Chitinase-like protein 3 OS=Mus musculus OX=10090 GN=Chil3 PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.003381	0.996572	CS pos: 36-37. Pr: 0.9587

TMHMM  Annotations     

There is no transmembrane helices in SPBR_02181-t41_1-p1.