CAZyme Information: SSD61244.1

Basic Information

• Species: Saccharomycodes ludwigii
• Lineage: Ascomycota; Saccharomycetes; ; Saccharomycodaceae; Saccharomycodes; Saccharomycodes ludwigii
• CAZyme ID: SSD61244.1
• CAZy Family: GT2|GT2
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
666		76692.86	4.3895

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_SludwigiiUTAD17	4017	N/A	2	4015

• Gene Location: location=UFAJ01000620:1034-3034(-)

Full Sequence      

MADSSNPFINLNEFDISDSVTDNNIDNIVEEKPTSSSKKVLKSLIIFTVFLAFLISTIMF
LTLQYHDTSKNGADRAKNTFFSKKHYFYDSDANFDDYANVTNEWRLDTGTNYTMNLTYWR
NDYGTSKERHYYFNITQLTVQMDNIENDEDLTSSAKTRNLTLVNGQYPAPLIEANSGDTI
YLHVVNKLPDKQPVSIHCHGLFYPNNPFDDGAVGINSCPIPSGYNYTYKIPVGKKQWGTY
WYHSHWSTQYADGIFGPLVIHSKDEDNLLDDYDEDRIILGNDFYQNFTDTYLTEYLESGN
ENTEPTPDDGFINGIYTQTDSQQDRFESLLYFDPEKVYRLRLVNAGFFLPFTFSIDAHKL
TLVEADGTNIVPHEVDNFDISVGQRYSVFLNYTKTKDQNYWMHTRYNAYCVTESNPNFNT
DVHAIVSYTNKYEEPEDMQSWSYYGGDPLCGDLDQNLLSTLVYETIPLNANGSARPDVKV
ELDIAFIIGGYQLDRGYFNDMTWVSWDKNTSTMHQLMFNSEEYKCDGVENKLNEHTYVLN
FDKRGQIVDLVLNNYDDGAHPFHLHGFKFWVIASSATGSWKDSYYDDLSLGKIKLDNPVL
RDNLNVGPYGYAVIRFVVDNPGVFPLHCHIGWHIEAGLLLQINALQSEYSQLEYDPEWKN
MCALDN

Enzyme Prediction     

No EC number prediction in SSD61244.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	155	638	1.9e-106	0.9804469273743017

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259953	CuRO_2_MCO_like_1	6.61e-58	276	429	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.
225043	SufI	2.76e-56	163	642	57	446	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].
177843	PLN02191	6.19e-56	163	638	47	540	L-ascorbate oxidase
274555	ascorbase	4.42e-55	163	638	25	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.
259977	CuRO_3_MCO_like_4	5.69e-53	482	644	3	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QOU22891.1|AA1	2.03e-238	64	665	78	656
AMD21008.1|AA1	2.50e-197	104	662	69	638
QEU59470.1|AA1	3.10e-192	95	662	86	673
QLG75039.1|AA1	4.45e-189	104	663	105	679
QGN15754.1|AA1	1.00e-188	104	663	99	677

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5LM8_A	3.78e-60	112	662	7	522	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	3.86e-60	112	662	8	523	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
5LWX_A	1.27e-59	112	662	35	550	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]
5Z1X_A	2.04e-55	148	666	12	488	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]
1ZPU_A	1.64e-54	156	638	20	473	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q55P57|LAC1_CRYNB	1.40e-66	129	663	62	579	Laccase-1 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=LAC1 PE=1 SV=1
sp|Q4PIF8|FER1_USTMA	7.96e-66	158	638	52	528	Iron multicopper oxidase fer1 OS=Ustilago maydis (strain 521 / FGSC 9021) OX=237631 GN=fer1 PE=2 SV=1
sp|J9VY90|LAC1_CRYNH	1.36e-64	129	663	62	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|Q09920|FIO1_SCHPO	3.49e-64	126	665	22	518	Iron transport multicopper oxidase fio1 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=fio1 PE=3 SV=1
sp|J9VQZ4|LAC2_CRYNH	2.68e-62	129	663	62	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

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000013	0.000022

TMHMM  Annotations     

Start	End
43	65