CAZyme Information: RL4_JR_03763-RA-p1

Basic Information

• Species: Raffaelea lauricola
• Lineage: Ascomycota; Sordariomycetes; ; Ophiostomataceae; Raffaelea; Raffaelea lauricola
• CAZyme ID: RL4_JR_03763-RA-p1
• CAZy Family: GH13
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
470		51500.58	4.8131

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_RlauricolaRL4	10461	N/A	146	10315

• Gene Location: location=JACBXF010000149:2883417-2885141(+)

Full Sequence      

MKSFVTHLTLLWIFFHTVLAVPSPERRIPPLDPFPPLFRRALPTGTCNSNTPCENAACCG
TNGLCGYSPTECGAGNCTSNCDAKAECGQYGKEGQKECPLSVCCSQFGFCGSTSDFCDKD
KGCQADYGGCGDVKRPSCGGTSANKRTPEDLNLNGFTHINFAFAFFDPTTFAIAPMDSNS
GALYERFTGLKDKHTGLETWISVGGWSFTDPGPTRSAFSDMSSSAANRKKFINELTNFME
HYGFDGVDLDWEYPQADDRGGVTADKANYVSLVKEMKAAFGGKYGITLTLPTSYWYLQHF
DLEAIQPNVNWFNLMAYDLHGVWDTQSKFVGPYLVSEIDLGMDLLWRAGVKPENVVLGMG
WYGRSFTLTDSSCNTPNGVCQFSGGAKAGECSKASGILDLQEIKNIIKDKSLSPHWDETA
AVKWITWDSDQWVSYDDDDTFDQKRKFANSRCLGGTMASKDDPSSLSTSS

Enzyme Prediction     

No EC number prediction in RL4_JR_03763-RA-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	148	458	7.8e-62	0.8513513513513513

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
214753	Glyco_18	1.80e-83	140	458	10	328	Glyco_18 domain.
119351	GH18_chitolectin_chitotriosidase	8.52e-77	145	458	17	335	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	5.43e-74	143	458	10	301	Glycosyl hydrolases family 18.
119357	GH18_zymocin_alpha	1.85e-64	151	456	23	337	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.
119365	GH18_chitinase	8.44e-58	148	457	18	315	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
UQC85767.1|CBM18|GH18	4.03e-223	8	457	192	672
AEO62990.1|CBM18|GH18	6.58e-221	14	457	16	481
QRD01729.1|CBM18|GH18	4.41e-217	41	457	55	494
QIX02022.1|CBM18|GH18	2.60e-205	37	457	34	476
UKZ69007.1|CBM18|GH18	1.68e-169	42	469	85	537

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5Y2A_A	4.81e-44	145	458	21	342	Crystal structure of Ostrinia furnacalis Group II chitinase catalytic domain 2 [Ostrinia furnacalis],5Y2A_B Crystal structure of Ostrinia furnacalis Group II chitinase catalytic domain 2 [Ostrinia furnacalis]
5Y2C_A	6.70e-43	145	458	21	342	Crystal structure of Ostrinia furnacalis Group II chitinase catalytic domain 2 E2180L mutant in complex with PENTA-N-ACETYLCHITOOCTAOSE (NAG)5 [Ostrinia furnacalis],5Y2C_B Crystal structure of Ostrinia furnacalis Group II chitinase catalytic domain 2 E2180L mutant in complex with PENTA-N-ACETYLCHITOOCTAOSE (NAG)5 [Ostrinia furnacalis]
1HKK_A	6.15e-41	148	457	22	335	High resoultion crystal structure of human chitinase in complex with allosamidin [Homo sapiens]
1HKI_A	6.29e-41	148	457	22	335	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	6.29e-41	148	457	22	335	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-41	85	419	317	668	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	2.21e-39	148	457	43	356	Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1
sp|Q9D7Q1|CHIT1_MOUSE	1.02e-37	141	457	36	354	Chitotriosidase-1 OS=Mus musculus OX=10090 GN=Chit1 PE=1 SV=2
sp|Q11174|CHIT_CAEEL	4.80e-35	145	457	71	392	Probable endochitinase OS=Caenorhabditis elegans OX=6239 GN=cht-1 PE=1 SV=1
sp|Q9BZP6|CHIA_HUMAN	4.36e-33	148	457	43	358	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
0.000193	0.999799	CS pos: 20-21. Pr: 0.9832

TMHMM  Annotations     

There is no transmembrane helices in RL4_JR_03763-RA-p1.