CAZyme Information: P170DRAFT_407094-t37_1-p1

Basic Information

• Species: Aspergillus steynii
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus steynii
• CAZyme ID: P170DRAFT_407094-t37_1-p1
• CAZy Family: GH16
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
590		65349.25	5.1118

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AsteyniiIBT23096	13430	1392250	235	13195

• Gene Location: location=MSFO01000003:4272489-4274440(-)

Full Sequence      

MAQLLRLVAVATIASAAALSRHMNTDCSGDDLSSGNLPRFLPDGSGSTEVPWANFDPAGE
PPDTGVTRHYEFTVSRDFASPDGFNKSVILINGQFPGPMIEANWGDMIEVKVTNDIDSPD
EGITLHWHGLTQKKTPWYDGVPGVSQCPIAPRGGKLTYRFQADRYGSGWYHSHYSAQYDD
GLFGPVIIHGPVQPEAEYDFDLGPVMISDYYHVGYYEIMERSLAKPPGIIPLDNNLINGK
GSYNCNRTSSASKCLLGAGYEKFRFHSGKRHRLRLINSGALANEKFSIDNHEMTVIANDF
VPVKPHKTKVVTLSPGQRTDVIVHATSAPNDIVWMRADMDMVCLQNTATFQTARAAIYYE
SADTKKLPHTKGTTWESNDCRNDPLELTVPYYPLTPPAPTTTQTVTVTAGLNGTGFMVMF
MDNSSFRANYNQAALLEVNQGRAEFPADRNVYDFGSNSSVRLVIENAFETLHPMHLHGHD
FWVLSEGPGPWDGTVVNPENPLRRDTHLMQPGTPENPSHLVLQWNQDNPGVWPLHCHISI
HSSAGMVILVMERPDDIVNEMAIPPAMDQTCEIWDNIDKSDYAEQIDSGV

Enzyme Prediction     

EC	1.10.3.2:2	-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	60	380	1.5e-113	0.9775641025641025

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	1.97e-73	67	552	1	523	L-ascorbate oxidase, plant type. Members of this protein family are the copper-containing enzyme L-ascorbate oxidase (EC 1.10.3.3), also called ascorbase. This family is found in flowering plants, and shows greater sequence similarity to a family of laccases (EC 1.10.3.2) from plants than to other known ascorbate oxidases.
259923	CuRO_1_MaLCC_like	1.71e-69	65	189	1	122	The first cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus albomyces. The subfamily of fungal laccases includes Ma-LCC and similar proteins. Ma-LCC is a multicopper oxidase (MCO) from Melanocarpus albomyces. Its crystal structure contains all four coppers at the mono- and trinuclear copper centers. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi and plants. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.
215324	PLN02604	1.02e-64	67	552	24	546	oxidoreductase
177843	PLN02191	2.33e-62	64	557	20	551	L-ascorbate oxidase
259968	CuRO_3_MaLCC_like	3.00e-57	410	551	17	157	The third cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus albomyces. The subfamily of fungal laccases includes Ma-LCC and similar proteins. Ma-LCC is a multicopper oxidase (MCO) from Melanocarpus albomyces. Its crystal structure contains all four coppers at the mono- and trinuclear copper centers. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi and plants. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QKX63435.1|AA1_3	3.69e-295	1	589	1	583
CAK48652.1|AA1_3	5.29e-287	50	590	104	648
BCS07898.1|AA1_3	8.30e-246	51	590	62	602
BCR95349.1|AA1_3	1.94e-245	51	590	86	626
QGA18227.1|AA1_3	2.91e-232	62	590	59	585

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3V9E_A	9.58e-105	44	590	50	580	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	2.67e-104	44	590	50	580	Crystal structure of laccase from Botrytis aclada at 1.67 A resolution [Botrytis aclada],4X4K_A Structure of laccase from Botrytis aclada with full copper content [Botrytis aclada]
5LWX_A	1.88e-95	37	579	16	558	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]
5LM8_A	2.45e-95	62	579	18	530	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	2.52e-95	62	579	19	531	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|A0A067XMP2|PTAK_PESFW	3.98e-163	37	590	39	585	Oxydoreductase ptaK OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=ptaK PE=2 SV=2
sp|J5JH35|OPS5_BEAB2	7.87e-113	62	590	68	590	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|Q96WM9|LAC2_BOTFU	2.13e-106	62	590	63	581	Laccase-2 OS=Botryotinia fuckeliana OX=40559 GN=lcc2 PE=2 SV=1
sp|Q12570|LAC1_BOTFU	6.88e-102	47	590	42	561	Laccase-1 OS=Botryotinia fuckeliana OX=40559 GN=lcc1 PE=2 SV=3
sp|A0A067XMP0|PTAE_PESFW	4.83e-93	65	590	55	610	Oxidoreductase ptaE OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=ptaE PE=2 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000755	0.999229	CS pos: 18-19. Pr: 0.8007

TMHMM  Annotations     

There is no transmembrane helices in P170DRAFT_407094-t37_1-p1.