CAZyme Information: EGD87607.1

Basic Information

• Species: Trichophyton rubrum
• Lineage: Ascomycota; Eurotiomycetes; ; Arthrodermataceae; Trichophyton; Trichophyton rubrum
• CAZyme ID: EGD87607.1
• CAZy Family: GH18
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
678		74985.54	6.6913

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_TrubrumCBS118892	8713	559305	97	8616

• Gene Location: location=GG700650:2911944-2914424(+)

Full Sequence      

MDRPASRRRHNSQRRLQQQPEDESVVAADTLIIPVQREDEKRPAGPSTGSQTGETKPEDH
RRSLSGCPWLLVGFVCCISTLLLVLGLAARWQQGAIPNIFDIGNLRPSSSPASSSSSTAG
PWSSRLHPEDHLFRPETTITLEWSVTTGYRRLDGVKKRVYLINGLFPGPTIEARSGDSLQ
VQVTNNIQDEGLVIHWHGLHMRGANHMDGVTGVTQCPIVPGDSMLYNFTISQSQSGTFWY
HAHSALQRAEGLYGGFVVHKPSTPSMRIARDPAIHADAVKYQYEKEHLLLIGDWYHRPAE
DVLKWFKSLEANGQEPVPDSFLINGAGRFNCSMALPTRPIDCVDEGYPTPELLLDSSTSY
RMRVINVGSLAGVSLGFEHGTVTPIQVDGGTEVELPSVSPNARSMGIVYPGQRTDFVLRN
PLGETGQSSITVELDPECFSLPNPALTRVQTFPISGSAKKPSHPLSDNPIGEAGTHVDLT
ELTSTASTISHIPAKADETFLVYTLLSKLSSNNYVPFAFFNHTSWRPQADPPLPLISLQR
KDWDKNQFTIKTSSRASWVDLIVNNLDEGPHPFHIHGHDFYVMSLHEADTGMGSYNPWDP
SNKAPAYDHSQAILRDTVHIPARGHAVLRFRADNPGIWLFHCHILWHLASGMAMLVDVMD
SASRPLHGILNQTCRYLT

Enzyme Prediction     

No EC number prediction in EGD87607.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	155	653	7.5e-93	0.9804469273743017

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	1.41e-75	141	652	4	517	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.
177843	PLN02191	1.31e-68	143	655	28	543	L-ascorbate oxidase
215324	PLN02604	2.27e-62	142	652	28	540	oxidoreductase
259977	CuRO_3_MCO_like_4	5.77e-61	500	658	1	166	The third 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 oxidize 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 subfamily of MCOs is composed of three cupredoxin domains. 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.
225043	SufI	9.02e-55	142	660	37	450	Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and spore coat protein CotA) [Cell cycle control, cell division, chromosome partitioning, Inorganic ion transport and metabolism, Cell wall/membrane/envelope biogenesis].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QGA16928.1|AA1	1.63e-212	126	675	108	689
QSS75251.1|AA1	3.75e-207	207	677	1	483
QKX62088.1|AA1	1.08e-206	126	667	97	661
QMW37919.1|AA1	7.18e-197	126	658	80	598
QRD88142.1|AA1	1.27e-196	126	658	97	615

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1ZPU_A	1.35e-65	138	678	2	507	Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_B Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_C Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_D Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_E Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_F Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae]
3V9E_A	1.10e-57	137	654	64	538	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	2.89e-57	137	654	64	538	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]
1AOZ_A	5.28e-54	162	655	27	520	Refined Crystal Structure Of Ascorbate Oxidase At 1.9 Angstroms Resolution [Cucurbita pepo var. melopepo],1AOZ_B Refined Crystal Structure Of Ascorbate Oxidase At 1.9 Angstroms Resolution [Cucurbita pepo var. melopepo],1ASO_A X-Ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-Forms [Cucurbita pepo var. melopepo],1ASO_B X-Ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-Forms [Cucurbita pepo var. melopepo],1ASP_A X-ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-forms [Cucurbita pepo var. melopepo],1ASP_B X-ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-forms [Cucurbita pepo var. melopepo],1ASQ_A X-Ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-Forms [Cucurbita pepo var. melopepo],1ASQ_B X-Ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-Forms [Cucurbita pepo var. melopepo]
5LM8_A	8.90e-53	135	674	18	522	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|I1RMG9|FET3_GIBZE	3.38e-69	153	652	40	490	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
sp|Q6CII3|FET3_KLULA	4.03e-68	138	674	27	526	Iron transport multicopper oxidase FET3 OS=Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) OX=284590 GN=FET3 PE=3 SV=1
sp|Q96WT3|FET3_CANGA	3.11e-67	138	674	19	521	Iron transport multicopper oxidase FET3 OS=Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) OX=284593 GN=FET3 PE=3 SV=1
sp|K7NCS2|FETC_EPIFE	2.33e-65	138	652	22	489	Iron transport multicopper oxidase fetC OS=Epichloe festucae (strain E2368) OX=696363 GN=fetC PE=2 SV=1
sp|Q55P57|LAC1_CRYNB	6.45e-65	137	662	60	564	Laccase-1 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=LAC1 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999778	0.000247

TMHMM  Annotations     

Start	End
69	91