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CAZyme Information: SPSK_06412-t39_1-p1

You are here: Home > Sequence: SPSK_06412-t39_1-p1

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Sporothrix schenckii
Lineage Ascomycota; Sordariomycetes; ; Ophiostomataceae; Sporothrix; Sporothrix schenckii
CAZyme ID SPSK_06412-t39_1-p1
CAZy Family GH43
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
376 41581.72 4.8628
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_Sschenckii1099-18 10434 1397361 141 10293
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 1.10.3.2:1

CAZyme Signature Domains help

Family Start End Evalue family coverage
AA1 2 211 3.7e-42 0.5964391691394659

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
259966 CuRO_3_Fet3p 6.56e-61 171 326 5 160
The third Cupredoxin domain of multicopper oxidase Fet3p. Fet3p catalyzes the ferroxidase reaction, which couples the oxidation of Fe(II) to Fe(III) with the four-electron reduction of molecular oxygen to water. Fet3p is a type I membrane protein with the amino-terminal oxidase domain in the extracellular space and the carboxyl terminus in the cytoplasm. The periplasmic produced Fe(III) is transferred to the permease Ftr1p for import into the cytosol. The four copper ions are inserted post-translationally and are essential for catalytic activity, thus linking copper and iron homeostasis. Like other related multicopper oxidases (MCOs), Fet3p 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 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.
259945 CuRO_2_Fet3p_like 1.07e-36 1 136 22 148
The second Cupredoxin domain of multicopper oxidase Fet3P. Fet3p catalyzes the ferroxidase reaction, which couples the oxidation of Fe(II) to Fe(III) with the four-electron reduction of molecular oxygen to water. Fet3p is a type I membrane protein with the amino-terminal oxidase domain in the extracellular space and the carboxyl terminus in the cytoplasm. The periplasmic produced Fe(III) is transferred to the permease Ftr1p for import into the cytosol. The four copper ions are inserted post-translationally and are essential for catalytic activity, thus linking copper and iron homeostasis. Like other related multicopper oxidases (MCOs), Fet3p 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.
259977 CuRO_3_MCO_like_4 1.78e-32 180 322 10 164
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.
400194 Cu-oxidase_2 2.14e-32 195 327 1 137
Multicopper oxidase. This entry contains many divergent copper oxidase-like domains that are not recognized by the pfam00394 model.
225043 SufI 5.99e-31 15 323 190 447
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      help

Hit ID E-Value Query Start Query End Hit Start Hit End
6.88e-163 1 376 171 541
2.98e-154 1 376 48 418
1.01e-151 1 376 174 541
1.64e-146 1 376 174 549
2.32e-146 1 376 174 549

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.48e-50 12 367 165 525
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]
1.24e-26 11 324 163 472
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]
2.20e-25 6 346 183 512
Chain A, Laccase [Rigidoporus microporus]
3.45e-20 33 324 194 469
Crystal structure of laccase from Coriolus zonatus at 2.6 A resolution [Trametes ochracea]
7.38e-20 11 340 192 535
Near-atomic resolution structure of a Melanocarpus albomyces laccase [Melanocarpus albomyces],2Q9O_B Near-atomic resolution structure of a Melanocarpus albomyces laccase [Melanocarpus albomyces],3FU7_A Melanocarpus albomyces laccase crystal soaked (4 sec) with 2,6-dimethoxyphenol [Melanocarpus albomyces],3FU8_A Melanocarpus albomyces laccase crystal soaked (10 sec) with 2,6-dimethoxyphenol [Melanocarpus albomyces],3FU8_B Melanocarpus albomyces laccase crystal soaked (10 sec) with 2,6-dimethoxyphenol [Melanocarpus albomyces]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3.75e-131 1 376 174 541
Multicopper oxidase PfmaD OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=PfmaD PE=2 SV=1
2.79e-77 2 370 176 542
Iron transport multicopper oxidase fetC OS=Epichloe festucae (strain E2368) OX=696363 GN=fetC PE=2 SV=1
1.18e-75 2 370 176 539
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
3.62e-73 12 371 188 548
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
2.91e-57 12 367 191 551
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

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000028 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in SPSK_06412-t39_1-p1.