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Protein
Submitted name:

Uncharacterized protein

Gene

MA_2883

Organism
Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi120 – 1201Iron (heme axial ligand); via tele nitrogenCombined sources

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

HemeCombined sources, Iron, Metal-binding

Enzyme and pathway databases

BioCyciMACE188937:GI2O-2918-MONOMER.

Names & Taxonomyi

Protein namesi
Submitted name:
Uncharacterized proteinImported
Gene namesi
Ordered Locus Names:MA_2883Imported
OrganismiMethanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)Imported
Taxonomic identifieri188937 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina
ProteomesiUP000002487 Componenti: Chromosome

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VEBX-ray1.30A1-195[»]
2VEEX-ray2.60A/B/C/D/E/F/G/H1-195[»]
3QZXX-ray1.30A1-195[»]
3QZZX-ray2.40A1-195[»]
3R0GX-ray2.20A/B1-195[»]
3ZH0X-ray2.00A/B/C/D21-195[»]
3ZJHX-ray1.70A/B1-195[»]
3ZJIX-ray1.50A/B1-195[»]
3ZJJX-ray2.00A/B/C1-195[»]
3ZJLX-ray1.50A/B1-195[»]
3ZJMX-ray1.50A/B/C1-195[»]
3ZJNX-ray1.60A/B1-195[»]
3ZJOX-ray1.80A/B1-195[»]
3ZJPX-ray1.38A1-195[»]
3ZJQX-ray1.90A/B1-195[»]
3ZJRX-ray3.00A1-195[»]
3ZJSX-ray2.30A/B1-195[»]
3ZOLX-ray1.60A/B1-195[»]
3ZOMX-ray2.20A/B1-195[»]
ProteinModelPortaliQ8TLY9.
SMRiQ8TLY9. Positions 6-195.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8TLY9.

Family & Domainsi

Phylogenomic databases

eggNOGiNOG11581.
InParanoidiQ8TLY9.
OMAiDVWYGFV.

Family and domain databases

Gene3Di1.10.490.10. 1 hit.
InterProiIPR009050. Globin-like.
IPR012292. Globin/Proto.
IPR012102. Protoglobin.
[Graphical view]
PIRSFiPIRSF014300. Protoglobin. 1 hit.
SUPFAMiSSF46458. SSF46458. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8TLY9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVEKIPGYT YGETENRAPF NLEDLKLLKE AVMFTAEDEE YIQKAGEVLE
60 70 80 90 100
DQVEEILDTW YGFVGSHPHL LYYFTSPDGT PNEKYLAAVR KRFSRWILDT
110 120 130 140 150
CNRSYDQAWL DYQYEIGLRH HRTKKNQTDN VESVPNIGYR YLVAFIYPIT
160 170 180 190
ATMKPFLARK GHTPEEVEKM YQAWFKATTL QVALWSYPYV KYGDF
Length:195
Mass (Da):23,000
Last modified:June 1, 2002 - v1
Checksum:iEA883DAAB7AB138F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE010299 Genomic DNA. Translation: AAM06260.1.
RefSeqiNP_617780.1. NC_003552.1.
WP_011022833.1. NC_003552.1.

Genome annotation databases

EnsemblBacteriaiAAM06260; AAM06260; MA_2883.
GeneIDi1474779.
KEGGimac:MA2883.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE010299 Genomic DNA. Translation: AAM06260.1.
RefSeqiNP_617780.1. NC_003552.1.
WP_011022833.1. NC_003552.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VEBX-ray1.30A1-195[»]
2VEEX-ray2.60A/B/C/D/E/F/G/H1-195[»]
3QZXX-ray1.30A1-195[»]
3QZZX-ray2.40A1-195[»]
3R0GX-ray2.20A/B1-195[»]
3ZH0X-ray2.00A/B/C/D21-195[»]
3ZJHX-ray1.70A/B1-195[»]
3ZJIX-ray1.50A/B1-195[»]
3ZJJX-ray2.00A/B/C1-195[»]
3ZJLX-ray1.50A/B1-195[»]
3ZJMX-ray1.50A/B/C1-195[»]
3ZJNX-ray1.60A/B1-195[»]
3ZJOX-ray1.80A/B1-195[»]
3ZJPX-ray1.38A1-195[»]
3ZJQX-ray1.90A/B1-195[»]
3ZJRX-ray3.00A1-195[»]
3ZJSX-ray2.30A/B1-195[»]
3ZOLX-ray1.60A/B1-195[»]
3ZOMX-ray2.20A/B1-195[»]
ProteinModelPortaliQ8TLY9.
SMRiQ8TLY9. Positions 6-195.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAM06260; AAM06260; MA_2883.
GeneIDi1474779.
KEGGimac:MA2883.

Phylogenomic databases

eggNOGiNOG11581.
InParanoidiQ8TLY9.
OMAiDVWYGFV.

Enzyme and pathway databases

BioCyciMACE188937:GI2O-2918-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ8TLY9.

Family and domain databases

Gene3Di1.10.490.10. 1 hit.
InterProiIPR009050. Globin-like.
IPR012292. Globin/Proto.
IPR012102. Protoglobin.
[Graphical view]
PIRSFiPIRSF014300. Protoglobin. 1 hit.
SUPFAMiSSF46458. SSF46458. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity."
    Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W., Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J., Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.
    , McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D., Cann I., Graham D.E., Grahame D.A., Guss A., Hedderich R., Ingram-Smith C., Kuettner C.H., Krzycki J.A., Leigh J.A., Li W., Liu J., Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A., White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H., Macario A.J.L., Paulsen I., Pritchett M., Sowers K.R., Swanson R.V., Zinder S.H., Lander E., Metcalf W.W., Birren B.
    Genome Res. 12:532-542(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 35395 / DSM 2834 / JCM 12185 / C2AImported.
  2. "Archaeal protoglobin structure indicates new ligand diffusion paths and modulation of haem-reactivity."
    Nardini M., Pesce A., Thijs L., Saito J.A., Dewilde S., Alam M., Ascenzi P., Coletta M., Ciaccio C., Moens L., Bolognesi M.
    EMBO Rep. 9:157-163(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) IN COMPLEX WITH HEME.
  3. "Structural heterogeneity and ligand gating in ferric Methanosarcina acetivorans protoglobin mutants."
    Pesce A., Tilleman L., Dewilde S., Ascenzi P., Coletta M., Ciaccio C., Bruno S., Moens L., Bolognesi M., Nardini M.
    IUBMB Life 63:287-294(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) IN COMPLEX WITH HEME.
  4. "Functional and structural roles of the N-terminal extension in Methanosarcina acetivorans protoglobin."
    Ciaccio C., Pesce A., Tundo G.R., Tilleman L., Bertolacci L., Dewilde S., Moens L., Ascenzi P., Bolognesi M., Nardini M., Coletta M.
    Biochim. Biophys. Acta 1834:1813-1823(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 21-195 IN COMPLEX WITH HEME.
  5. "Structure and haem-distal site plasticity in Methanosarcina acetivorans protoglobin."
    Pesce A., Tilleman L., Donne J., Aste E., Ascenzi P., Ciaccio C., Coletta M., Moens L., Viappiani C., Dewilde S., Bolognesi M., Nardini M.
    PLoS ONE 8:e66144-e66144(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.38 ANGSTROMS) IN COMPLEX WITH HEME.
  6. "Structural Bases for the Regulation of Co Binding in the Archaeal Protoglobin from Methanosarcina Acetivorans."
    Tilleman L., Abbruzzetti S., Ciaccio C., De Sanctis G., Nardini M., Pesce A., Desmet F., Moens L., Van Doorslaer S., Bruno S., Bolognesi M., Ascenzi P., Coletta M., Viappiani C., Dewilde S.
    Submitted (FEB-2013) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH HEME.

Entry informationi

Entry nameiQ8TLY9_METAC
AccessioniPrimary (citable) accession number: Q8TLY9
Entry historyi
Integrated into UniProtKB/TrEMBL: June 1, 2002
Last sequence update: June 1, 2002
Last modified: July 22, 2015
This is version 83 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.