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Protein

Myohemerythrin

Gene
N/A
Organism
Themiste hennahi (Peanut worm) (Themiste zostericola)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Myohemerythrin is an oxygen-binding protein found in the retractor muscles of certain worms. The oxygen-binding site contains two iron atoms.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi25 – 251Iron 1Combined sources1 Publication
Metal bindingi54 – 541Iron 1Combined sources1 Publication
Metal bindingi58 – 581Iron 1Combined sources1 Publication
Metal bindingi58 – 581Iron 2Combined sources1 Publication
Metal bindingi73 – 731Iron 2Combined sources1 Publication
Metal bindingi77 – 771Iron 2Combined sources1 Publication
Metal bindingi106 – 1061Iron 2Combined sources1 Publication
Metal bindingi111 – 1111Iron 1Combined sources1 Publication
Metal bindingi111 – 1111Iron 2Combined sources1 Publication

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Muscle protein

Keywords - Biological processi

Oxygen transport, Transport

Keywords - Ligandi

Iron, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Myohemerythrin
Short name:
MHr
OrganismiThemiste hennahi (Peanut worm) (Themiste zostericola)
Taxonomic identifieri360549 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaAnnelidaPolychaetaSipunculaSipunculideaGolfingiidaThemistidaeThemiste

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 118118MyohemerythrinPRO_0000191842Add
BLAST

Expressioni

Tissue specificityi

Muscle.

Interactioni

Subunit structurei

Monomer.By similarity

Structurei

Secondary structure

1
118
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi12 – 143Combined sources
Helixi19 – 3719Combined sources
Helixi41 – 6424Combined sources
Helixi70 – 8516Combined sources
Helixi93 – 10917Combined sources
Helixi111 – 1144Combined sources
Turni115 – 1173Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A7DX-ray1.80A1-118[»]
1A7EX-ray1.80A1-118[»]
2IGFX-ray2.80P69-87[»]
2MHRX-ray1.30A1-118[»]
ProteinModelPortaliP02247.
SMRiP02247. Positions 1-118.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02247.

Family & Domainsi

Sequence similaritiesi

Belongs to the hemerythrin family.Curated

Family and domain databases

Gene3Di1.20.120.50. 1 hit.
InterProiIPR002063. Haemerythrin.
IPR012312. Haemerythrin-like.
IPR016131. Haemerythrin_Fe_BS.
IPR012827. Haemerythrin_metal-bd.
[Graphical view]
PfamiPF01814. Hemerythrin. 1 hit.
[Graphical view]
PIRSFiPIRSF002033. Hemerythrin. 1 hit.
PRINTSiPR00186. HEMERYTHRIN.
SUPFAMiSSF47188. SSF47188. 1 hit.
TIGRFAMsiTIGR02481. hemeryth_dom. 1 hit.
TIGR00058. Hemerythrin. 1 hit.
PROSITEiPS00550. HEMERYTHRINS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P02247-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
GWEIPEPYVW DESFRVFYEQ LDEEHKKIFK GIFDCIRDNS APNLATLVKV
60 70 80 90 100
TTNHFTHEEA MMDAAKYSEV VPHKKMHKDF LEKIGGLSAP VDAKNVDYCK
110
EWLVNHIKGT DFKYKGKL
Length:118
Mass (Da):13,778
Last modified:October 1, 1993 - v2
Checksum:i3591FEEC56EE90B4
GO

Sequence databases

PIRiA37369. HRTHM.

Cross-referencesi

Sequence databases

PIRiA37369. HRTHM.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A7DX-ray1.80A1-118[»]
1A7EX-ray1.80A1-118[»]
2IGFX-ray2.80P69-87[»]
2MHRX-ray1.30A1-118[»]
ProteinModelPortaliP02247.
SMRiP02247. Positions 1-118.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP02247.

Family and domain databases

Gene3Di1.20.120.50. 1 hit.
InterProiIPR002063. Haemerythrin.
IPR012312. Haemerythrin-like.
IPR016131. Haemerythrin_Fe_BS.
IPR012827. Haemerythrin_metal-bd.
[Graphical view]
PfamiPF01814. Hemerythrin. 1 hit.
[Graphical view]
PIRSFiPIRSF002033. Hemerythrin. 1 hit.
PRINTSiPR00186. HEMERYTHRIN.
SUPFAMiSSF47188. SSF47188. 1 hit.
TIGRFAMsiTIGR02481. hemeryth_dom. 1 hit.
TIGR00058. Hemerythrin. 1 hit.
PROSITEiPS00550. HEMERYTHRINS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: PROTEIN SEQUENCE.
  2. Cited for: X-RAY CRYSTALLOGRAPHY (5.5 ANGSTROMS).
  3. "Pseudosymmetry in the structure of myohemerythrin."
    Hendrickson W.A., Ward K.B.
    J. Biol. Chem. 252:3012-3018(1977) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (5.0 ANGSTROMS).
  4. "Structure of myohemerythrin in the azidomet state at 1.7/1.3-A resolution."
    Sheriff S., Hendrickson W.A., Smith J.L.
    J. Mol. Biol. 197:273-296(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) IN COMPLEX WITH IRON, SEQUENCE REVISION TO 34-35.
  5. "Structures of wild-type chloromet and L103N hydroxomet Themiste zostericola myohemerythrins at 1.8-A resolution."
    Martins L.J., Hill C.P., Ellis W.R. Jr.
    Biochemistry 36:7044-7049(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).

Entry informationi

Entry nameiHEMTM_THEHE
AccessioniPrimary (citable) accession number: P02247
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 1, 1993
Last modified: January 20, 2016
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.