CAZyme Information: sr16427-t26_1-p1

Basic Information

• Species: Sporisorium reilianum
• Lineage: Basidiomycota; Ustilaginomycetes; ; Ustilaginaceae; Sporisorium; Sporisorium reilianum
• CAZyme ID: sr16427-t26_1-p1
• CAZy Family: GT2|GT2
• CAZyme Description: related to cell surface ferroxidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
707		77076.37	5.2005

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_SreilianumSRZ2	6791	999809	118	6673

• Gene Location: location=FQ311442:12330-14453(-)

Full Sequence      

METGAVMNETSQQQTQMEKNDNQSSSKSLATSEHEAQNSETRAVDLPQRKRRRSAALVAV
FVALVCVVALALGLGLGLGLKHKHKSQSDAASSSNKTVPGATASNLAFIPREKLADPSQL
ALDATWDRFAPPQDRVYNWTLTQVLSNPAGTTKQMRLVNGLFPGPKVEGNIGDRIIVHIQ
NEMPVPTTIHWHGQFQRGSNQMDGSAGITECGIAPGTSFTYNWTVQQSGTYWWHSHYGPT
YADGLFGPLILHGDDEKFRMINSNNATTAQTNGTSTTTTNGTAVRTDYDRDLIFVVNDAY
QADSFSVAAIARSKSGPPGGDQGSEPVPDYGMINGLGFSNCALAPNGTTCISDAPAGKTA
YNFTVPANKRIRMRVINAGSLATFRFSVDGHNMTVIEADGTEVEPVVVQSLNVMVSQRYS
VIIETDRPVGAYAVRAEVLDDMFAYENPFLVMDQYAIMRYEGVAASTPPISNPVNTTLVN
VTESLSTSQLVPITRIDAPASNMTTKLVVNFGLDAYSNWHAFFNQTTFTSEMAPQASLMK
AYTFEKTQHASSNSTVGAYYNDPDEMIVTNTEVVVMDVIVNNLDEGEHPFHLHGFTPFLI
GAGAGNFQGPANFSEARVNPMRRDVFSVPPFSWIAFRFVADNTGVWPFHCHLMPHMAIGL
LMQFQVLPDQISTLPVSDQFYSQCSAVNSWVQQNQNLLTSVGDPDDM

Enzyme Prediction     

No EC number prediction in sr16427-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	151	660	3.4e-105	0.9776536312849162

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	6.17e-73	135	677	2	534	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	1.14e-66	135	252	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.
259953	CuRO_2_MCO_like_1	1.67e-66	292	461	1	163	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.
177843	PLN02191	2.46e-62	135	675	24	555	L-ascorbate oxidase
215324	PLN02604	2.60e-62	135	677	25	557	oxidoreductase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CBQ70849.1|AA1	0.0	1	707	1	707
SJX65875.1|AA1	0.0	1	707	1	707
CDU22906.1|AA1	0.0	91	707	91	709
CDI56230.1|AA1	0.0	92	707	83	701
SAM65069.1|AA1	0.0	91	704	84	700

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3KW7_A	3.69e-59	136	684	5	491	Crystal structure of LacB from Trametes sp. AH28-2 [Trametes sp. AH28-2],3KW7_B Crystal structure of LacB from Trametes sp. AH28-2 [Trametes sp. AH28-2]
1HFU_A	5.05e-58	140	664	10	466	Chain A, LACCASE 1 [Coprinopsis cinerea]
1A65_A	5.16e-58	140	664	10	466	Chain A, Laccase [Coprinopsis cinerea]
5MEJ_A	4.46e-57	141	699	11	499	Structural study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi. First structure of the series with 3 min total X-ray exposition time. [Steccherinum murashkinskyi],5MHU_A The study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi.The third structure of the series with total exposition time 63 min. [Steccherinum murashkinskyi],5MHV_A The study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi.The fourth structure of the series with total exposition time 93 min. [Steccherinum murashkinskyi]
5E9N_A	5.83e-57	141	700	11	500	Steccherinum murashkinskyi laccase at 0.95 resolution [Steccherinum murashkinskyi]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q55P57|LAC1_CRYNB	1.68e-75	93	685	19	579	Laccase-1 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=LAC1 PE=1 SV=1
sp|J9VQZ4|LAC2_CRYNH	1.20e-74	94	685	31	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|J9VY90|LAC1_CRYNH	6.33e-74	93	685	19	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|J5JH35|OPS5_BEAB2	7.34e-63	135	698	74	584	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|I1RMG9|FET3_GIBZE	1.90e-62	119	688	9	519	Iron transport multicopper oxidase FET3 OS=Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) OX=229533 GN=FET3 PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999817	0.000200

TMHMM  Annotations     

Start	End
56	78