CAZyme Information: P175DRAFT_0444000-t39_1-p1

Basic Information

• Species: Aspergillus ochraceoroseus
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus ochraceoroseus
• CAZyme ID: P175DRAFT_0444000-t39_1-p1
• CAZy Family: CE4
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
593		66487.90	5.5331

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AochraceoroseusIBT24754	9070	1392256	153	8917

• Gene Location: location=MSFN02000008:83245-85079(+)

Full Sequence      

MKGGYRHEISPLDSNAGYNYTCSADPHSHHPEKSCKKGDRHCINHNTTSITNTTIPTSTP
CPGNTREDRSRWCDFSIDTDYYTDAPNTNVIREYWLEVDDVIVAPDGYPRRAMAINGSIP
GPTIYADWGDTVVVHVTNNLHESKNGTSIHWHGLRQNYTNQNDGVVSITQCPIAPGSSTT
YKWRATQYGTTWYHSHIGLQAWEGVAGAIVINGPATANYDEDKGTILLSDWTHQTVDELY
LVAQTTGPPKLPNGLINGTNVYGSGCNATGSRFTMKVNEGTSYRLRLINGAINSHFKFMI
DNHTLTVIAMDLVPIQPYTTDSISIAMGQRYDVIVTANQASTASSFWLRAIPQEACSANE
SVDNIKGIFYYGDEPTIPETNPWPFNNSCADEPMSSLIPHLDMIVHSPDWEAVTDLTVGR
NKANLFRWYLNSTTMEVFWDNPTLLQIANNETVFQKSNAVISLPNENEWVYLIINTNHKD
PHPIHLHGHDFFVLAQGANHWNGSLVTQNPPRRDTAVLPAYGYLVIAFETNNPGAWLMHC
HIGWHLSEGLALQFVESYHKIEHLIDYDILKETCDAWTNYDEKYHVKEEDSGI

Enzyme Prediction     

EC	-	-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	79	389	2.1e-132	0.9935897435897436

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	2.81e-74	91	564	1	531	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.
259968	CuRO_3_MaLCC_like	1.71e-69	415	555	13	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.
274556	laccase	3.46e-66	110	555	22	518	laccase, plant. Members of this protein family include the copper-containing enzyme laccase (EC 1.10.3.2), often several from a single plant species, and additional, uncharacterized, closely related plant proteins termed laccase-like multicopper oxidases. This protein family shows considerable sequence similarity to the L-ascorbate oxidase (EC 1.10.3.3) family. Laccases are enzymes of rather broad specificity, and classification of all proteins scoring about the trusted cutoff of this model as laccases may be appropriate.
215324	PLN02604	5.22e-66	91	564	24	554	oxidoreductase
259947	CuRO_2_MaLCC_like	5.72e-64	224	391	2	167	The second 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. Laccase is composed of three cupredoxin domains 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 2 of 3-domain MCOs has lost the ability to bind copper.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QQK45664.1|AA1_3	8.50e-280	47	593	43	591
CAP98129.1|AA1_3	2.36e-276	47	592	59	606
BCS27040.1|AA1_3	1.43e-272	56	593	35	577
EAA62557.1|AA1_3	5.81e-267	59	593	122	664
QKX58305.1|AA1_3	6.73e-257	61	593	33	569

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3SQR_A	1.36e-177	64	593	41	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]
3V9E_A	2.73e-177	64	593	41	580	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
5LWX_A	2.16e-170	58	580	13	556	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]
5LM8_A	3.44e-170	72	580	4	528	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	3.56e-170	72	580	5	529	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|Q96WM9|LAC2_BOTFU	8.57e-181	64	593	41	581	Laccase-2 OS=Botryotinia fuckeliana OX=40559 GN=lcc2 PE=2 SV=1
sp|J5JH35|OPS5_BEAB2	7.09e-166	69	593	51	590	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|Q12570|LAC1_BOTFU	1.42e-152	64	593	39	561	Laccase-1 OS=Botryotinia fuckeliana OX=40559 GN=lcc1 PE=2 SV=3
sp|Q96UM2|LAC3_BOTFU	1.15e-131	120	554	1	452	Laccase-3 (Fragment) OS=Botryotinia fuckeliana OX=40559 GN=lcc3 PE=3 SV=1
sp|P06811|LAC1_NEUCR	6.57e-124	75	593	68	606	Laccase OS=Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) OX=367110 GN=lacc PE=1 SV=3

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000031	0.000012

TMHMM  Annotations     

There is no transmembrane helices in P175DRAFT_0444000-t39_1-p1.