CAZyme Information: ATY60613.1

Basic Information

• Species: Cordyceps militaris
• Lineage: Ascomycota; Sordariomycetes; ; Cordycipitaceae; Cordyceps; Cordyceps militaris
• CAZyme ID: ATY60613.1
• CAZy Family: GH1
• CAZyme Description: L-ascorbate oxidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
685		76621.81	5.2214

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CmilitarisATCC34164	9362	N/A	75	9287

• Gene Location: location=CP023323:4722078-4724135(-)

Full Sequence      

MSDVPRPPPPRPDGLPSSWNHHGRPRRALWSCWQMAFFFLVFVITILGLTLIPFGISSNA
VAPPSSHGDSEQHQTPPEPVDDTHPEPQPTAAPEPETRPGPRLRDPAEYILDMAWDFAVA
PTTREYNWTITNAHLNPDGVYRPMYLINDQFPGPLVECNDGDTIIVHVNNQAVNATALHF
HGLFQNGSNFMDGTVGVTQCPIAPRSSFTYNFTVSGQSGTYWYHAHHSAQASDGLLGPVV
IHARDERTVFQELDYASDRIVMVQDHYHNLTSELLMDYLQPDMENDEPVPDNALINGRGV
RDCADFPGWPCDAANTSRPVFDLAANQRHRLRVINVGAMAEFQIQFDEHPFYVTEVDGTD
VHPEPFHRLNILPAQRYSVILETNVTTADAFWMRARIVTQCFTTENKRLVPELHAVIRYQ
SDDAPLPAAEPTSKDWPEAAEVICRDLNVSALHPVVAQSPPPADEFVLVRANFMIGDWAL
ARGFFNGSTWHANATHPSLHRYLDGIRAADAGSSSSAKPDAAAMAVSDKVFDPARDYVLE
TTGARTIDLAINNFDDGSHPFHLHGHKFFVLVQGETGYPPEAHQMPAYLAEHEHLLVNPV
RRDTVTVEGYGWVIVRVVLDNPGLWAFHCHNTWHAESGMVMQFLVGSDAMRRWTVDERQR
ELCARDGVLTGMRPSDDLWFGQITK

Enzyme Prediction     

No EC number prediction in ATY60613.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	134	639	1.2e-107	0.9804469273743017

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	2.66e-70	123	652	1	530	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.
259926	CuRO_1_Diphenol_Ox	1.48e-69	124	242	1	119	The first cupredoxin domain of fungal laccase, diphenol oxidase. Diphenol oxidase belongs to the laccase family. It catalyzes the initial steps in melanin biosynthesis from diphenols. Melanin is one of the virulence factors of infectious fungi. In the pathogenesis of C. neoformans, melanin pigments have been shown to protect the fungal cells from oxidative and microbicidal activities of host defense systems. Laccase is a blue multicopper oxidase (MCO) which 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. 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.
177843	PLN02191	1.05e-63	124	648	24	549	L-ascorbate oxidase
215324	PLN02604	1.52e-62	123	648	24	549	oxidoreductase
259953	CuRO_2_MCO_like_1	5.13e-61	259	419	1	162	The second cupredoxin domain of uncharacterized multicopper oxidase. Multicopper Oxidases (MCOs) are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs oxidise their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre which binds a dioxygen. The dioxygen, following the transfer of four electrons, is reduced to two molecules of water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. This family of MCOs 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
ATY60613.1|AA1	0.0	1	685	1	685
UKZ88109.1|AA1	0.0	31	685	88	745
UPL00458.1|AA1	0.0	101	683	138	711
QYS98033.1|AA1	7.94e-318	17	685	38	719
UKZ77569.1|AA1	8.00e-318	20	683	41	712

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3V9E_A	4.29e-68	108	644	51	541	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	1.15e-67	108	644	51	541	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]
5LM8_A	3.79e-60	124	644	24	503	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	3.86e-60	124	644	25	504	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
5Z1X_A	4.35e-60	118	646	1	466	Crystal Structure of Laccase from Cerrena sp. RSD1 [Cerrena],5Z1X_B Crystal Structure of Laccase from Cerrena sp. RSD1 [Cerrena],5Z22_A Crystal Structure of Laccase from Cerrena sp. RSD1 [Cerrena]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q55P57|LAC1_CRYNB	2.41e-96	105	664	43	579	Laccase-1 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=LAC1 PE=1 SV=1
sp|J9VY90|LAC1_CRYNH	1.04e-93	105	664	43	579	Laccase-1 OS=Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) OX=235443 GN=LAC1 PE=1 SV=1
sp|J9VQZ4|LAC2_CRYNH	3.26e-89	105	664	43	579	Laccase-2 OS=Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) OX=235443 GN=LAC2 PE=3 SV=2
sp|E9R598|FETC_ASPFU	7.64e-71	123	670	22	518	Iron transport multicopper oxidase fetC OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=fetC PE=2 SV=1
sp|K7NCS2|FETC_EPIFE	5.36e-68	120	644	19	494	Iron transport multicopper oxidase fetC OS=Epichloe festucae (strain E2368) OX=696363 GN=fetC PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999968	0.000033

TMHMM  Annotations     

Start	End
36	58