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Protein
Submitted name:

Alr2278 protein

Gene

alr2278

Organism
Nostoc sp. (strain PCC 7120 / UTEX 2576)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi105 – 1051Iron (heme axial ligand); via tele nitrogenCombined sources

GO - Molecular functioni

  1. heme binding Source: InterPro
  2. metal ion binding Source: UniProtKB-KW
Complete GO annotation...

Keywords - Ligandi

HemeCombined sources, Iron, Metal-binding

Names & Taxonomyi

Protein namesi
Submitted name:
Alr2278 proteinImported
Gene namesi
Ordered Locus Names:alr2278Imported
OrganismiNostoc sp. (strain PCC 7120 / UTEX 2576)Imported
Taxonomic identifieri103690 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaNostocalesNostocaceaeNostoc
ProteomesiUP000002483: Chromosome

Interactioni

Protein-protein interaction databases

STRINGi103690.alr2278.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2O09X-ray2.10A/B1-189[»]
2O0CX-ray2.60A/B1-189[»]
2O0GX-ray2.51A/B1-189[»]
3L6JX-ray2.30A/B1-189[»]
3TF8X-ray2.13A/B1-189[»]
3TF9X-ray2.59A/B1-189[»]
3TFAX-ray2.27A/B1-189[»]
3TFDX-ray1.96A/B1-189[»]
3TFEX-ray1.99A/B1-189[»]
3TFFX-ray1.94A/B1-189[»]
3TFGX-ray1.90A/B1-189[»]
4IAEX-ray2.05A/B1-189[»]
4IAHX-ray2.80A/B1-182[»]
4IAMX-ray1.99A/B1-182[»]
4JQHX-ray2.30A/B1-189[»]
SMRiQ8YUQ7. Positions 1-182.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8YUQ7.

Family & Domainsi

Phylogenomic databases

eggNOGiNOG261245.
HOGENOMiHOG000290574.
OMAiECFLRDT.
OrthoDBiEOG6384JV.

Family and domain databases

InterProiIPR011644. Heme_NO-bd.
IPR024096. NO_sig/Golgi_transp_ligand-bd.
[Graphical view]
PfamiPF07700. HNOB. 1 hit.
[Graphical view]
SUPFAMiSSF111126. SSF111126. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8YUQ7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYGLVNKAIQ DMISKHHGED TWEAIKQKAG LEDIDFFVGM EAYSDDVTYH
60 70 80 90 100
LVGAASEVLG KPAEELLIAF GEYWVTYTSE EGYGELLASA GDSLPEFMEN
110 120 130 140 150
LDNLHARVGL SFPQLRPPAF ECQHTSSKSM ELHYQSTRCG LAPMVLGLLH
160 170 180
GLGKRFQTKV EVTQTAFRET GEDHDIFSIK YEDSNLYDD
Length:189
Mass (Da):21,192
Last modified:March 1, 2002 - v1
Checksum:i34C54119F22AACC4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000019 Genomic DNA. Translation: BAB73977.1.
PIRiAG2090.
RefSeqiNP_486318.1. NC_003272.1.
WP_010996435.1. NC_003272.1.

Genome annotation databases

EnsemblBacteriaiBAB73977; BAB73977; BAB73977.
GeneIDi1105875.
KEGGiana:alr2278.
PATRICi22774726. VBINosSp37423_2830.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000019 Genomic DNA. Translation: BAB73977.1.
PIRiAG2090.
RefSeqiNP_486318.1. NC_003272.1.
WP_010996435.1. NC_003272.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2O09X-ray2.10A/B1-189[»]
2O0CX-ray2.60A/B1-189[»]
2O0GX-ray2.51A/B1-189[»]
3L6JX-ray2.30A/B1-189[»]
3TF8X-ray2.13A/B1-189[»]
3TF9X-ray2.59A/B1-189[»]
3TFAX-ray2.27A/B1-189[»]
3TFDX-ray1.96A/B1-189[»]
3TFEX-ray1.99A/B1-189[»]
3TFFX-ray1.94A/B1-189[»]
3TFGX-ray1.90A/B1-189[»]
4IAEX-ray2.05A/B1-189[»]
4IAHX-ray2.80A/B1-182[»]
4IAMX-ray1.99A/B1-182[»]
4JQHX-ray2.30A/B1-189[»]
SMRiQ8YUQ7. Positions 1-182.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi103690.alr2278.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB73977; BAB73977; BAB73977.
GeneIDi1105875.
KEGGiana:alr2278.
PATRICi22774726. VBINosSp37423_2830.

Phylogenomic databases

eggNOGiNOG261245.
HOGENOMiHOG000290574.
OMAiECFLRDT.
OrthoDBiEOG6384JV.

Miscellaneous databases

EvolutionaryTraceiQ8YUQ7.

Family and domain databases

InterProiIPR011644. Heme_NO-bd.
IPR024096. NO_sig/Golgi_transp_ligand-bd.
[Graphical view]
PfamiPF07700. HNOB. 1 hit.
[Graphical view]
SUPFAMiSSF111126. SSF111126. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: PCC 7120 / UTEX 2576Imported.
  2. "NO and CO differentially activate soluble guanylyl cyclase via a heme pivot-bend mechanism."
    Ma X., Sayed N., Beuve A., van den Akker F.
    EMBO J. 26:578-588(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH HEME.
  3. "Structure of cinaciguat (BAY 58-2667) bound to Nostoc H-NOX domain reveals insights into heme-mimetic activation of the soluble guanylyl cyclase."
    Martin F., Baskaran P., Ma X., Dunten P.W., Schaefer M., Stasch J.P., Beuve A., van den Akker F.
    J. Biol. Chem. 285:22651-22657(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS).
  4. "Tunnels modulate ligand flux in a heme nitric oxide/oxygen binding (H-NOX) domain."
    Winter M.B., Herzik M.A., Kuriyan J., Marletta M.A.
    Proc. Natl. Acad. Sci. U.S.A. 108:E881-E889(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH HEME.
  5. "Insights into BAY 60-2770 activation and S-nitrosylation-dependent desensitization of soluble guanylyl cyclase via crystal structures of homologous nostoc H-NOX domain complexes."
    Kumar V., Martin F., Hahn M.G., Schaefer M., Stamler J.S., Stasch J.P., van den Akker F.
    Biochemistry 52:3601-3608(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) OF 1-182.
  6. "Insights into soluble guanylyl cyclase activation derived from improved heme-mimetics."
    von Wantoch Rekowski M., Kumar V., Zhou Z., Moschner J., Marazioti A., Bantzi M., Spyroulias G.A., van den Akker F., Giannis A., Papapetropoulos A.
    J. Med. Chem. 56:8948-8952(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS).

Entry informationi

Entry nameiQ8YUQ7_NOSS1
AccessioniPrimary (citable) accession number: Q8YUQ7
Entry historyi
Integrated into UniProtKB/TrEMBL: March 1, 2002
Last sequence update: March 1, 2002
Last modified: March 4, 2015
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteome, Reference proteomeImported

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.