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Protein
Submitted name:

Multicopper oxidase

Gene

mco

Organism
uncultured bacterium
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi90 – 901Copper 1; via pros nitrogenCombined sources
Metal bindingi93 – 931Copper 4; via tele nitrogenCombined sources
Metal bindingi95 – 951Copper 2; via pros nitrogenCombined sources
Metal bindingi95 – 951Copper 3; via pros nitrogenCombined sources
Metal bindingi137 – 1371Copper 2; via tele nitrogenCombined sources
Metal bindingi137 – 1371Copper 3; via tele nitrogenCombined sources
Metal bindingi138 – 1381Copper 1Combined sources
Metal bindingi139 – 1391Copper 2; via tele nitrogenCombined sources
Metal bindingi139 – 1391Copper 3; via tele nitrogenCombined sources
Metal bindingi145 – 1451Copper 1; via pros nitrogenCombined sources
Metal bindingi151 – 1511Copper 1Combined sources
Metal bindingi237 – 2371Copper 4; via tele nitrogenCombined sources
Metal bindingi239 – 2391Copper 3; via tele nitrogenCombined sources
Metal bindingi239 – 2391Copper 4; via tele nitrogenCombined sources
Metal bindingi239 – 2391Copper 5; via tele nitrogenCombined sources
Metal bindingi285 – 2851Copper 3; via tele nitrogenCombined sources
Metal bindingi285 – 2851Copper 5; via tele nitrogenCombined sources
Metal bindingi287 – 2871Copper 3; via tele nitrogenCombined sources
Metal bindingi287 – 2871Copper 5; via tele nitrogenCombined sources

GO - Molecular functioni

  1. copper ion binding Source: InterPro
  2. oxidoreductase activity Source: InterPro
Complete GO annotation...

Keywords - Ligandi

CopperCombined sources, Metal-bindingCombined sources

Names & Taxonomyi

Protein namesi
Submitted name:
Multicopper oxidaseImported
Gene namesi
Name:mcoImported
Organismiuncultured bacteriumImported
Taxonomic identifieri77133 [NCBI]
Taxonomic lineageiBacteriaenvironmental samples

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ZWNX-ray1.70A/B/C35-359[»]
4E9VX-ray1.80A/B/C35-359[»]
4E9WX-ray1.45A/B/C35-359[»]
4E9XX-ray1.14A/B/C35-359[»]
4E9YX-ray1.50A/B/C35-359[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Family and domain databases

Gene3Di2.60.40.420. 2 hits.
InterProiIPR011706. Cu-oxidase_2.
IPR011707. Cu-oxidase_3.
IPR008972. Cupredoxin.
IPR003599. Ig_sub.
[Graphical view]
PfamiPF07731. Cu-oxidase_2. 1 hit.
PF07732. Cu-oxidase_3. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 1 hit.
[Graphical view]
SUPFAMiSSF49503. SSF49503. 2 hits.

Sequencei

Sequence statusi: Complete.

C0STU6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRRSLRNERG FGFVKVFLFV FCSGLSLVVS HSWAAEREFD MTIEEVTIKV
60 70 80 90 100
APGLDYKVFG FNGQVPGPLI HVQEGDDVIV NVTNNTSLPH TIHWHGVHQK
110 120 130 140 150
GTWRSDGVPG VTQQPIEAGD SYTYKFKADR IGTLWYHCHV NVNEHVGVRG
160 170 180 190 200
MWGPLIVDPK QPLPIEKRVT KDVIMMMSTW ESAVADKYGE GGTPMNVADY
210 220 230 240 250
FSVNAKSFPL TQPLRVKKGD VVKIRFFGAG GGIHAMHSHG HDMLVTHKDG
260 270 280 290 300
LPLDSPYYAD TVLVSPGERY DVIIEADNPG RFIFHDHVDT HVTAGGKHPG
310 320 330 340 350
GPITVIEYDG VPVDDWYVWK DKDYDPNFFY SESLKQGYGM FDHDGFKGEF

EQRQRRPGR
Length:359
Mass (Da):40,403
Last modified:May 26, 2009 - v1
Checksum:i3586C4F1A57AEDFE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB469330 Genomic DNA. Translation: BAH47712.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB469330 Genomic DNA. Translation: BAH47712.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ZWNX-ray1.70A/B/C35-359[»]
4E9VX-ray1.80A/B/C35-359[»]
4E9WX-ray1.45A/B/C35-359[»]
4E9XX-ray1.14A/B/C35-359[»]
4E9YX-ray1.50A/B/C35-359[»]
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di2.60.40.420. 2 hits.
InterProiIPR011706. Cu-oxidase_2.
IPR011707. Cu-oxidase_3.
IPR008972. Cupredoxin.
IPR003599. Ig_sub.
[Graphical view]
PfamiPF07731. Cu-oxidase_2. 1 hit.
PF07732. Cu-oxidase_3. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 1 hit.
[Graphical view]
SUPFAMiSSF49503. SSF49503. 2 hits.
ProtoNetiSearch...

Publicationsi

  1. "X-ray structure of a two-domain type laccase: a missing link in the evolution of multi-copper proteins."
    Komori H., Miyazaki K., Higuchi Y.
    FEBS Lett. 583:1189-1195(2009)
    Cited for: NUCLEOTIDE SEQUENCE.

Entry informationi

Entry nameiC0STU6_9BACT
AccessioniPrimary (citable) accession number: C0STU6
Entry historyi
Integrated into UniProtKB/TrEMBL: May 26, 2009
Last sequence update: May 26, 2009
Last modified: January 7, 2015
This is version 21 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.