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Entry version 100 (29 Sep 2021)
Sequence version 1 (24 May 2005)
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Protein

Methionine synthase

Gene

mtr

Organism
Dictyostelium discoideum (Slime mold)
Status
Reviewed-Annotation score:

Annotation score:3 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Protein inferred from homologyi <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Catalyzes the transfer of a methyl group from methyl-cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate (By similarity).

By similarity

Miscellaneous

L-homocysteine is bound via the zinc atom.By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: L-methionine biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes L-methionine from L-homocysteine (MetH route). This subpathway is part of the pathway L-methionine biosynthesis via de novo pathway, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-methionine from L-homocysteine (MetH route), the pathway L-methionine biosynthesis via de novo pathway and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi255ZincPROSITE-ProRule annotation1
Metal bindingi318ZincPROSITE-ProRule annotation1
Metal bindingi319ZincPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei699Methylcob(III)alaminBy similarity1
Metal bindingi778Cobalt (methylcob(III)alamin axial ligand)By similarity1
Binding sitei823Methylcob(III)alaminBy similarity1
Binding sitei827Methylcob(III)alaminBy similarity1
Binding sitei879Methylcob(III)alamin; via amide nitrogenBy similarity1
Binding sitei966S-adenosyl-L-methionineBy similarity1
Binding sitei1163S-adenosyl-L-methionine; via carbonyl oxygenBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionMethyltransferase, Transferase
Biological processAmino-acid biosynthesis, Methionine biosynthesis
LigandCobalamin, Cobalt, Metal-binding, S-adenosyl-L-methionine, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-DDI-156581, Methylation
R-DDI-1614635, Sulfur amino acid metabolism
R-DDI-196741, Cobalamin (Cbl, vitamin B12) transport and metabolism
R-DDI-9013407, RHOH GTPase cycle

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00051;UER00081

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Methionine synthase (EC:2.1.1.13)
Alternative name(s):
5-methyltetrahydrofolate--homocysteine methyltransferase
Vitamin-B12 dependent methionine synthase
Short name:
MS
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:mtr
ORF Names:DDB_G0284699
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiDictyostelium discoideum (Slime mold)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri44689 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaAmoebozoaEvoseaEumycetozoaDictyosteliaDictyostelialesDictyosteliaceaeDictyostelium
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002195 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componentsi: Chromosome 4, Unassembled WGS sequence

Organism-specific databases

Dictyostelium discoideum online informatics resource

More...
dictyBasei
DDB_G0284699, mtr

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00003277991 – 1260Methionine synthaseAdd BLAST1260

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q54P92

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
44689.DDB0230138

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q54P92

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini13 – 333Hcy-bindingPROSITE-ProRule annotationAdd BLAST321
Domaini364 – 625Pterin-bindingPROSITE-ProRule annotationAdd BLAST262
Domaini655 – 749B12-binding N-terminalPROSITE-ProRule annotationAdd BLAST95
Domaini766 – 883B12-bindingPROSITE-ProRule annotationAdd BLAST118
Domaini916 – 1256AdoMet activationPROSITE-ProRule annotationAdd BLAST341

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni775 – 779Methylcob(III)alamin bindingBy similarity5
Regioni1218 – 1219S-adenosyl-L-methionine bindingBy similarity2

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Modular enzyme with four functionally distinct domains. The isolated Hcy-binding domain catalyzes methyl transfer from free methylcobalamin to homocysteine. The Hcy-binding domain in association with the pterin-binding domain catalyzes the methylation of cob(I)alamin by methyltetrahydrofolate and the methylation of homocysteine. The B12-binding domain binds the cofactor. The AdoMet activation domain binds S-adenosyl-L-methionine. Under aerobic conditions cob(I)alamin can be converted to inactive cob(II)alamin. Reductive methylation by S-adenosyl-L-methionine and flavodoxin regenerates methylcobalamin (By similarity).By similarity

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1579, Eukaryota

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_004914_2_0_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q54P92

Identification of Orthologs from Complete Genome Data

More...
OMAi
ADCIAMS

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q54P92

Family and domain databases

Conserved Domains Database

More...
CDDi
cd02069, methionine_synthase_B12_BD, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.1240.10, 1 hit
3.10.196.10, 1 hit
3.20.20.20, 1 hit
3.20.20.330, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR003759, Cbl-bd_cap
IPR006158, Cobalamin-bd
IPR036724, Cobalamin-bd_sf
IPR011005, Dihydropteroate_synth-like
IPR003726, HCY_dom
IPR036589, HCY_dom_sf
IPR033706, Met_synthase_B12-bd
IPR011822, MetH
IPR036594, Meth_synthase_dom
IPR000489, Pterin-binding_dom
IPR004223, VitB12-dep_Met_synth_activ_dom
IPR037010, VitB12-dep_Met_synth_activ_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF02310, B12-binding, 1 hit
PF02607, B12-binding_2, 1 hit
PF02965, Met_synt_B12, 1 hit
PF00809, Pterin_bind, 1 hit
PF02574, S-methyl_trans, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000381, MetH, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM01018, B12-binding_2, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF47644, SSF47644, 1 hit
SSF51717, SSF51717, 1 hit
SSF52242, SSF52242, 1 hit
SSF56507, SSF56507, 1 hit
SSF82282, SSF82282, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR02082, metH, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50974, ADOMET_ACTIVATION, 1 hit
PS51332, B12_BINDING, 1 hit
PS51337, B12_BINDING_NTER, 1 hit
PS50970, HCY, 1 hit
PS50972, PTERIN_BINDING, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

Q54P92-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MINSNDKNES DTFGIIRKIL SERIMVLDGA MGTEIQKFKL KDNDYRGEEF
60 70 80 90 100
KDFPHELGGN NDLLSLTQPH IIREIHCKYL EAGADFIETN TFNGNIFSQA
110 120 130 140 150
DYKMEHLVKR INIESARLAK SACEEYTKKD PSRPRFVCGA VGPTNKTASI
160 170 180 190 200
SPSVERPEAR NVLFDELVSG YLEQVEALVE GGIDVILVET VFDSLNCKAA
210 220 230 240 250
LFAIEEFFKT YSPRLPVFVS GTIVDKSGRT LSGQTGEAFY TSVASANLMV
260 270 280 290 300
FGLNCALGAQ EMRPFLQNIS KCSECYVSCY PNAGLPNTFG GYDETPEMMA
310 320 330 340 350
EQIKEFAESG LLNIVGGCCG TSPDHIRAFC NAIEGIAPRA IPTLVPNTTL
360 370 380 390 400
SGLEPLVFTK ELNFVNVGER CNVSGSRRFA NLIKANKYEE ALSVARQQVE
410 420 430 440 450
AGAQIIDINM DEGMIDAVAA IQKFLFFIGS EPEISKVPIM LDSSNFDVVE
460 470 480 490 500
AGLKCVQGKC IVNSISLKVG EELFIKQAKI VKQYGASVVV MAFDENGQAT
510 520 530 540 550
SKEEKVRICY RSYKILTEQV GFYPQDIIFD PNILTIATGL EEHNNYGVEF
560 570 580 590 600
IEATREIKAL MPLTRVSGGV SNLSFSFRGN EPLREAMHSA FLYYAIAAGM
610 620 630 640 650
DMGIVNAGAL PIYDDIPKDL LKLVEDAILN RTNDATEKLL EYAQANNKSE
660 670 680 690 700
KANVEVEEWR NKPVSERIAH ALVKGITTYI IEDTEEARNT LPSSLSVIEG
710 720 730 740 750
PLMGGMNVVG DLFGAGKMFL PQVIKSARVM KKAVAHLIPF MEEEKRLKRL
760 770 780 790 800
EKGNDEAAED EPDNAGVVVL ATVKGDVHDI GKNIVGVVLG CNNYKVIDIG
810 820 830 840 850
VMTPCEKIVE AIIANKADVV GLSGLITPSL DEMIYVASEL ERLKFKIPLM
860 870 880 890 900
IGGATTSQIH TAVKISPHYS QPTVHVLDAS RSVTVVQSLL DPNNKEVFAE
910 920 930 940 950
DVSQQYAELR EKHYASLKDR KYTSLEKARQ HCVKVNWKTI QPVKPTFLGT
960 970 980 990 1000
QVFKEYSLEK LVTKIDWNPF FVTWQLRGKY PNRGYPRIFN DETVGAEAKK
1010 1020 1030 1040 1050
LFDDAQTMLK EIVDKKLLNA RGVIGFYPAN SIDEDIIIYD HNDDETRSKP
1060 1070 1080 1090 1100
IATLFGLRQQ NEKETDEPYI AIGDYIAPVS SGVKDYIGLF AVSSGFGLED
1110 1120 1130 1140 1150
MVEKYKKEND DYSSIMAKAL ADRLAEALAE AVHEDVRREH WAYEKDQALS
1160 1170 1180 1190 1200
NEDLFKIKYK GIRPAPGYPA QPDHTEMKTI WSLMNVNENT SIELTDHMAM
1210 1220 1230 1240 1250
LPGAAVCGVY FSHEHAKYFS VGKITKEQIE SYASRKQITK EEAERWLSSI
1260
LSYDRLPLVK
Length:1,260
Mass (Da):140,122
Last modified:May 24, 2005 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i095402C1F5889CF0
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AAFI02000070 Genomic DNA Translation: EAL65119.1

NCBI Reference Sequences

More...
RefSeqi
XP_638483.1, XM_633391.1

Genome annotation databases

Ensembl protists genome annotation project

More...
EnsemblProtistsi
EAL65119; EAL65119; DDB_G0284699

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
8624734

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ddi:DDB_G0284699

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAFI02000070 Genomic DNA Translation: EAL65119.1
RefSeqiXP_638483.1, XM_633391.1

3D structure databases

SMRiQ54P92
ModBaseiSearch...

Protein-protein interaction databases

STRINGi44689.DDB0230138

Proteomic databases

PaxDbiQ54P92

Genome annotation databases

EnsemblProtistsiEAL65119; EAL65119; DDB_G0284699
GeneIDi8624734
KEGGiddi:DDB_G0284699

Organism-specific databases

dictyBaseiDDB_G0284699, mtr

Phylogenomic databases

eggNOGiKOG1579, Eukaryota
HOGENOMiCLU_004914_2_0_1
InParanoidiQ54P92
OMAiADCIAMS
PhylomeDBiQ54P92

Enzyme and pathway databases

UniPathwayiUPA00051;UER00081
ReactomeiR-DDI-156581, Methylation
R-DDI-1614635, Sulfur amino acid metabolism
R-DDI-196741, Cobalamin (Cbl, vitamin B12) transport and metabolism
R-DDI-9013407, RHOH GTPase cycle

Miscellaneous databases

Protein Ontology

More...
PROi
PR:Q54P92

Family and domain databases

CDDicd02069, methionine_synthase_B12_BD, 1 hit
Gene3Di1.10.1240.10, 1 hit
3.10.196.10, 1 hit
3.20.20.20, 1 hit
3.20.20.330, 1 hit
InterProiView protein in InterPro
IPR003759, Cbl-bd_cap
IPR006158, Cobalamin-bd
IPR036724, Cobalamin-bd_sf
IPR011005, Dihydropteroate_synth-like
IPR003726, HCY_dom
IPR036589, HCY_dom_sf
IPR033706, Met_synthase_B12-bd
IPR011822, MetH
IPR036594, Meth_synthase_dom
IPR000489, Pterin-binding_dom
IPR004223, VitB12-dep_Met_synth_activ_dom
IPR037010, VitB12-dep_Met_synth_activ_sf
PfamiView protein in Pfam
PF02310, B12-binding, 1 hit
PF02607, B12-binding_2, 1 hit
PF02965, Met_synt_B12, 1 hit
PF00809, Pterin_bind, 1 hit
PF02574, S-methyl_trans, 1 hit
PIRSFiPIRSF000381, MetH, 1 hit
SMARTiView protein in SMART
SM01018, B12-binding_2, 1 hit
SUPFAMiSSF47644, SSF47644, 1 hit
SSF51717, SSF51717, 1 hit
SSF52242, SSF52242, 1 hit
SSF56507, SSF56507, 1 hit
SSF82282, SSF82282, 1 hit
TIGRFAMsiTIGR02082, metH, 1 hit
PROSITEiView protein in PROSITE
PS50974, ADOMET_ACTIVATION, 1 hit
PS51332, B12_BINDING, 1 hit
PS51337, B12_BINDING_NTER, 1 hit
PS50970, HCY, 1 hit
PS50972, PTERIN_BINDING, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiMETH_DICDI
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q54P92
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: May 24, 2005
Last modified: September 29, 2021
This is version 100 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Reference proteome

Documents

  1. Dictyostelium discoideum
    Dictyostelium discoideum: entries, gene names and cross-references to dictyBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families
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