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CAZyme Information: MGYG000001639_00068

You are here: Home > Sequence: MGYG000001639_00068

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 Haloferax massiliensis
Lineage Archaea; Halobacteriota; Halobacteria; Halobacteriales; Haloferacaceae; Haloferax; Haloferax massiliensis
CAZyme ID MGYG000001639_00068
CAZy Family AA1
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
384 MGYG000001639_1|CGC1 42053.97 5.8309
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001639 3991467 Isolate not provided not provided
Gene Location Start: 69657;  End: 70811  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001639_00068.

CAZyme Signature Domains help

Family Start End Evalue family coverage
AA1 111 347 2.2e-34 0.6564245810055865

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd04202 CuRO_D2_2dMcoN_like 1.18e-47 213 365 1 138
The second cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar proteins. This family includes bacterial two domain multicopper oxidases (2dMCOs) represented by the McoN from Nitrosomonas europaea. McoN is a trimeric type C blue copper oxidase. Each subunit houses a type 1 copper site in domain 1 and a type 2/type 3 trinuclear copper cluster at the subunit-subunit interface. The 2dMCO is proposed to be a key intermediate in the evolution of three domain MCOs. The biological function of McoN has not been characterized. Multicopper oxidases couple oxidation of substrates with reduction of dioxygen to water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals.
cd11024 CuRO_1_2DMCO_NIR_like 1.89e-42 85 206 6 118
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase. The two-domain laccase (small laccase) in this family differs significantly from all laccases. It resembles the two domain nitrite reductase in both sequence and structure. It consists of two cupredoxin domains and forms trimers and hence resembles the quaternary structure of nitrite reductases more than that of large laccases. There are three trinuclear copper clusters in the enzyme localized between domains 1 and 2 of each pair of neighbor chains. Three copper ions of type 1 lie close to one another near the surface of the central part of the trimer, and, effectively, a trimeric substrate binding site is formed in their vicinity. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety of organic substrates coupled to the reduction of molecular oxygen to water. It displays broad substrate specificity, catalyzing the oxidation of a wide variety of aromatic, notably phenolic, and inorganic substances. Laccase has been implicated in a wide spectrum of biological activities.
COG2132 SufI 8.79e-42 69 358 149 448
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].
COG2132 SufI 4.06e-25 14 359 1 292
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].
cd13859 CuRO_D1_2dMcoN_like 8.31e-22 102 205 22 122
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar proteins. This family includes bacterial two domain multicopper oxidases (2dMCOs) represented by the McoN from Nitrosomonas europaea. McoN is a trimeric type C blue copper oxidase. Each subunit houses a type 1 copper site in domain 1 and a type 2/type 3 trinuclear copper cluster at the subunit-subunit interface. The 2dMCO is proposed to be a key intermediate in the evolution of three domain MCOs. Its biological function has not been characterized. Multicopper oxidases couple oxidation of substrates with reduction of dioxygen to water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QZY04861.1 3.86e-224 1 382 1 382
QWC19486.1 8.22e-179 13 383 13 382
QWC20514.1 2.90e-169 13 384 13 401
CAD7247108.1 4.33e-15 111 365 62 333
CAE7213185.1 5.88e-12 115 335 50 266

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3G5W_A 8.86e-43 111 367 28 277
Crystalstructure of Blue Copper Oxidase from Nitrosomonas europaea [Nitrosomonas europaea],3G5W_B Crystal structure of Blue Copper Oxidase from Nitrosomonas europaea [Nitrosomonas europaea],3G5W_C Crystal structure of Blue Copper Oxidase from Nitrosomonas europaea [Nitrosomonas europaea],3G5W_D Crystal structure of Blue Copper Oxidase from Nitrosomonas europaea [Nitrosomonas europaea],3G5W_E Crystal structure of Blue Copper Oxidase from Nitrosomonas europaea [Nitrosomonas europaea],3G5W_F Crystal structure of Blue Copper Oxidase from Nitrosomonas europaea [Nitrosomonas europaea]
4E9V_A 3.97e-42 111 371 29 282
MulticopperOxidase mgLAC (data1) [uncultured bacterium],4E9V_B Multicopper Oxidase mgLAC (data1) [uncultured bacterium],4E9V_C Multicopper Oxidase mgLAC (data1) [uncultured bacterium],4E9W_A Multicopper Oxidase mgLAC (data2) [uncultured bacterium],4E9W_B Multicopper Oxidase mgLAC (data2) [uncultured bacterium],4E9W_C Multicopper Oxidase mgLAC (data2) [uncultured bacterium],4E9X_A Multicopper Oxidase mgLAC (data3) [uncultured bacterium],4E9X_B Multicopper Oxidase mgLAC (data3) [uncultured bacterium],4E9X_C Multicopper Oxidase mgLAC (data3) [uncultured bacterium],4E9Y_A Multicopper Oxidase mgLAC (data4) [uncultured bacterium],4E9Y_B Multicopper Oxidase mgLAC (data4) [uncultured bacterium],4E9Y_C Multicopper Oxidase mgLAC (data4) [uncultured bacterium]
3GDC_A 5.70e-22 111 344 60 272
Crystalstructure of multicopper oxidase [Arthrobacter sp. FB24],3GDC_B Crystal structure of multicopper oxidase [Arthrobacter sp. FB24],3GDC_C Crystal structure of multicopper oxidase [Arthrobacter sp. FB24]
3WIA_A 1.45e-21 101 351 25 266
Crystalstructure of the N-terminal 1-37 residues deleted mutant of Geobacillus copper nitrite reductase [Geobacillus kaustophilus HTA426],3WIA_B Crystal structure of the N-terminal 1-37 residues deleted mutant of Geobacillus copper nitrite reductase [Geobacillus kaustophilus HTA426],3WIA_C Crystal structure of the N-terminal 1-37 residues deleted mutant of Geobacillus copper nitrite reductase [Geobacillus kaustophilus HTA426],3WIA_D Crystal structure of the N-terminal 1-37 residues deleted mutant of Geobacillus copper nitrite reductase [Geobacillus kaustophilus HTA426],3WIA_E Crystal structure of the N-terminal 1-37 residues deleted mutant of Geobacillus copper nitrite reductase [Geobacillus kaustophilus HTA426],3WIA_F Crystal structure of the N-terminal 1-37 residues deleted mutant of Geobacillus copper nitrite reductase [Geobacillus kaustophilus HTA426],3WIA_G Crystal structure of the N-terminal 1-37 residues deleted mutant of Geobacillus copper nitrite reductase [Geobacillus kaustophilus HTA426],3WIA_H Crystal structure of the N-terminal 1-37 residues deleted mutant of Geobacillus copper nitrite reductase [Geobacillus kaustophilus HTA426],3WIA_I Crystal structure of the N-terminal 1-37 residues deleted mutant of Geobacillus copper nitrite reductase [Geobacillus kaustophilus HTA426]
3WKQ_A 2.51e-21 101 351 61 302
Copper-containingnitrite reductase from Geobacillus thermodenitrificans in complex with formate [Geobacillus thermodenitrificans NG80-2],3WNI_A 1.50 A resolution crystal structure of dioxygen bound copper-containing nitrite reductase from Geobacillus thermodenitrificans [Geobacillus thermodenitrificans NG80-2],3WNJ_A 1.20 A resolution crystal structure of dioxygen bound copper-containing nitrite reductase from Geobacillus thermodenitrificans [Geobacillus thermodenitrificans NG80-2],4YSA_A Completely oxidized structure of copper nitrite reductase from Geobacillus thermodenitrificans [Geobacillus thermodenitrificans NG80-2],4YSD_A Room temperature structure of copper nitrite reductase from Geobacillus thermodenitrificans [Geobacillus thermodenitrificans NG80-2],4YSO_A Copper nitrite reductase from Geobacillus thermodenitrificans - 0.064 MGy [Geobacillus thermodenitrificans NG80-2],4YSP_A Structure of copper nitrite reductase from Geobacillus thermodenitrificans - 8.32 MGy [Geobacillus thermodenitrificans NG80-2],4YSQ_A Structure of copper nitrite reductase from Geobacillus thermodenitrificans - 8.38 MGy [Geobacillus thermodenitrificans NG80-2],4YSR_A Structure of copper nitrite reductase from Geobacillus thermodenitrificans - 16.6 MGy [Geobacillus thermodenitrificans NG80-2],4YSS_A Structure of copper nitrite reductase from Geobacillus thermodenitrificans - 16.7 MGy [Geobacillus thermodenitrificans NG80-2],4YST_A Structure of copper nitrite reductase from Geobacillus thermodenitrificans - 24.9 MGy [Geobacillus thermodenitrificans NG80-2],4YSU_A Structure of copper nitrite reductase from Geobacillus thermodenitrificans - 25.0 MGy [Geobacillus thermodenitrificans NG80-2],4ZK8_A Copper-containing nitrite reductase from thermophilic bacterium Geobacillus thermodenitrificans (Re-refined) [Geobacillus thermodenitrificans NG80-2],5YTL_A Crystal structure of Geobacillus thermodenitrificans copper-containing nitrite reductase determined with an anaerobically manipulated crystal [Geobacillus thermodenitrificans],6L46_A High-resolution neutron and X-ray joint refined structure of copper-containing nitrite reductase from Geobacillus thermodenitrificans [Geobacillus thermodenitrificans]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
I6WZK7 7.99e-11 13 331 17 325
Multicopper oxidase MmcO OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=mmcO PE=1 SV=1
Q96UM2 1.72e-10 115 381 1 266
Laccase-3 (Fragment) OS=Botryotinia fuckeliana OX=40559 GN=lcc3 PE=3 SV=1
E9F648 1.53e-08 111 240 47 169
Laccase 1 OS=Metarhizium robertsii (strain ARSEF 23 / ATCC MYA-3075) OX=655844 GN=Mlac1 PE=2 SV=2
A0A0B4F5S2 1.53e-08 111 240 47 169
Laccase 1 OS=Metarhizium brunneum (strain ARSEF 3297) OX=1276141 GN=Mlac1 PE=3 SV=1
A0A0B4F1I0 1.53e-08 111 240 47 169
Laccase 1 OS=Metarhizium anisopliae (strain ARSEF 549) OX=1276135 GN=Mlac1 PE=2 SV=1

SignalP and Lipop Annotations help

This protein is predicted as TATLIPO

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000000 0.000000 0.000038 0.000276 0.999671 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001639_00068.