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Entry version 40 (16 Oct 2019)
Sequence version 1 (19 Feb 2014)
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Protein

Magnetosome protein MamM

Gene

mamM

Organism
Magnetospirillum gryphiswaldense (strain DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1)
Status
Reviewed-Annotation score:

Annotation score:5 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>
-Experimental evidence at protein leveli <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

Essential for magnetosome formation; required for stable accumulation of MamB (PubMed:22007638). May nucleate iron crystal formation (Probable). Probably binds and transports iron. Binds divalent cations, possibly up to 3 Zn2+ per dimer in vitro, probably iron in vivo (Probable) (PubMed:30811856). One of 7 genes (mamLQBIEMO) able to induce magnetosome membrane biogenesis; coexpression of mamLQRBIEMO in a deletion of the 17 gene mamAB operon restores magnetosome vesicle formation but not magnetite biosynthesis (PubMed:27286560).3 Publications3 Publications

Miscellaneous

This bacteria makes up to 60 cubo-octahedral magnetosomes of about 45 nm in diameter which contain membrane-bound crystals of magnetite (Fe3O4).1 Publication
Expression of just the minimal mamAB gene cluster (MGMSRv2__2365 to MGMSRv2__2381), including this gene, is sufficient to form a minimal magnetosome chain with small magnetite particles.1 Publication
Cation diffusion facilitator (CDF) transporters all have similar domain structure. By recreating in MamM mutations known in paralogous human zinc transporters (Znt-8, SLC30A8 and ZnT-10, SLC30A10), information about the effects of these mutations can be learned.2 Publications

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 bindingi249Metal cation 11 Publication1
Metal bindingi264Metal cation 21 Publication1
Metal bindingi285Metal cation 11 Publication1
Metal bindingi289Metal cation 31 Publication1

<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

Biological processBiomineralization, Ion transport, Iron transport, Transport
LigandIron, Metal-binding

Protein family/group databases

Transport Classification Database

More...
TCDBi
2.A.4.7.4 the cation diffusion facilitator (cdf) family

<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:
Magnetosome protein MamMCurated
Alternative name(s):
Probable iron transporter MamMCurated
<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:mamM1 Publication
Ordered Locus Names:MGMSRv2__2375
ORF Names:mgI491, MGR_4095
<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>OrganismiMagnetospirillum gryphiswaldense (strain DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1)
<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 identifieri431944 [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 lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesRhodospirillaceaeMagnetospirillum
<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
  • UP000018922 <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> Componenti: Chromosome

<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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei13 – 33HelicalSequence analysisAdd BLAST21
Transmembranei39 – 59HelicalSequence analysisAdd BLAST21
Transmembranei81 – 101HelicalSequence analysisAdd BLAST21
Transmembranei117 – 137HelicalSequence analysisAdd BLAST21

GO - Cellular componenti

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Magnetosome, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Single gene disruption has no growth defects, no accumulation of magnetite, forms empty intracellular magnetosome vesicles, decreased levels of MamB, mislocation of MamC in 1-3 foci or rarely in a shortened chain (PubMed:22007638). Magnetosome vesicles are fewer and smaller, aligned in a chain with the filament, only a few have very small crystals. Other, possibly precursor magnetosome vesicles are visible. MamI mislocalized to cell inner membrane or in 1 to a few patches (PubMed:27286560). Deletion of approximately 80 kb of DNA, including this operon, leads to cells that are non-magnetic, lack internal membrane systems, grow poorly, have reduced mobility and take-up and accumulate iron poorly (PubMed:13129949).3 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi6 – 9CAVC → SAVS: Wild-type magnetic response. 1 Publication4
Mutagenesisi9C → S: Wild-type magnetic response. 1 Publication1
Mutagenesisi46Y → D: Loss of magnetic response. 1 Publication1
Mutagenesisi46Y → H: About 90% magnetic response. 1 Publication1
Mutagenesisi50D → A: About 50% magnetic response, fewer cells have iron crystals which are smaller, in addition to magnetite (Fe(3)O(4)) crystals of hematite (Fe(2)O(3)) also form. 1 Publication1
Mutagenesisi139C → A: Wild-type magnetic response. 1 Publication1
Mutagenesisi155H → A: About 65% magnetic response, fewer cells have iron crystals which are larger. 1 Publication1
Mutagenesisi159D → A: About 55% magnetic response, fewer cells have iron crystals which have altered morphology. 1 Publication1
Mutagenesisi249 – 285DMIIG…IESLH → AMIIGVDPENTVEQAHEICE AVQAAVCGKIRRIESLA: CTD binds only 2 cations. 1 PublicationAdd BLAST37
Mutagenesisi249D → A: Slightly decreased wild-type magnetic response, fewer, slightly smaller magnetite crystals. Significantly decreased magnetic response, many fewer, smaller crystals in vivo, isolated CTD does not bind cations; when associated with A-264. 1 Publication1
Mutagenesisi250M → L: CTD behaves like wild-type. 1 Publication1
Mutagenesisi250M → P: Severely impaired magnetic response, cells make very few, small magnetite particles, less MamB and MamM protein accumulate. CTD no longer dimerizes, CTD has cannot fold properly and is unstable. 1 Publication1
Mutagenesisi259 – 318Missing : Loss of magnetic response, reduces MamB expression. 1 PublicationAdd BLAST60
Mutagenesisi260V → G: Nearly wild-type magnetic response. 1 Publication1
Mutagenesisi260V → P: CTD dimerizes, binds fewer cations. Loss of magnetic response, still stabilizes MamB. 2 Publications1
Mutagenesisi260V → R: Loss of magnetic response, still stabilizes MamB, CTD dimerizes, binds cations, dimer interface is tighter and twisted. 1 Publication1
Mutagenesisi260V → W: Significantly reduced magnetic response, many fewer, much smaller magnetite crystals formed, still stabilizes MamB, CTD dimerizes, binds fewer cations. 1 Publication1
Mutagenesisi264 – 289HEICE…HVSAE → AEICEAVQAAVCGKIRRIES LHVSAA: CTD binds only 1 cation. 1 PublicationAdd BLAST26
Mutagenesisi264H → A: Wild-type magnetic response, no change in magnetite crystal size, number or shape. Significantly decreased magnetic response, many fewer, smaller crystals in vivo, isolated CTD does not bind cations; when associated with A-249. 1 Publication1
Mutagenesisi285H → A: Wild-type magnetic response, no change in magnetite crystal size, number or shape. 1 Publication1
Mutagenesisi289 – 318Missing : Wild-type magnetic response. 1 PublicationAdd BLAST30
Mutagenesisi289E → A: Nearly wild-type magnetic response, fewer magnetite crystals of normal size and shape. 1 Publication1
Mutagenesisi309 – 318Missing : Wild-type magnetic response. 1 Publication10

<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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004477391 – 318Magnetosome protein MamMAdd BLAST318

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Part of the probable 17 gene mamAB operon.1 Publication

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Forms homodimers via its C-terminal domain (CTD) in the presence of metal cations (Probable).

Interacts with MamB via their CTD (PubMed:22007638, PubMed:29243866) (Probable). Isolated CTD forms homodimers (PubMed:24658343, PubMed:24819161, PubMed:27550551, PubMed:30811856).

3 Publications6 Publications

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
1430440.MGMSRv2_2375

<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
V6F235

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
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

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>Regioni1 – 210Transmembrane domain (TMD)1 PublicationAdd BLAST210
Regioni211 – 318C-terminal domain (CTD)1 PublicationAdd BLAST108

<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

The C-terminal domain (CTD) is probably responsible for hetero- and homodimerization; it assumes a V-shaped, dimeric metallo-chaperone-like fold that can open and close. Val-260 forms the hinge between the dimers. Binds up to 3 divalent metal cations (probably iron in vivo); upon binding there is a conformational shift to a tighter dimer (PubMed:24658343, PubMed:30811856) (Probable). If the CTD cannot fold correctly the function of the whole protein is decreased, suggesting the CTD confers functionality on the transmembrane domain (TMD), perhaps activated by ligand binding to the CTD (Probable).3 Publications2 Publications

<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

Belongs to the cation diffusion facilitator (CDF) transporter (TC 2.A.4) family. [View classification]1 Publication

Keywords - Domaini

Transmembrane, Transmembrane helix

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.20.1510.10, 1 hit
3.30.70.1350, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR002524 Cation_efflux
IPR027470 Cation_efflux_CTD
IPR036837 Cation_efflux_CTD_sf
IPR027469 Cation_efflux_TMD_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01545 Cation_efflux, 1 hit
PF16916 ZT_dimer, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF160240 SSF160240, 1 hit
SSF161111 SSF161111, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01297 CDF, 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.

V6F235-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRKSGCAVCS RSIGWVGLAV STVLMVMKAF VGLIGGSQAM LADAMYSLKD
60 70 80 90 100
MLNALMVIIG TTISSKPLDA EHPYGHGKVE FILSMVVSVV FIVLTGYLLV
110 120 130 140 150
HAVQILLDES LHRTPHLIVL WAALVSIGVN VGMYFYSRCV AIETNSPLIK
160 170 180 190 200
TMAKHHHGDA TASGAVALGI IGAHYLNMPW IDPAVALWET IDLLLLGKVV
210 220 230 240 250
FMDAYRGLMD HTAGEAVQNR IVEAAERVPG VRGVIHLRAR YVGQDIWADM
260 270 280 290 300
IIGVDPENTV EQAHEICEAV QAAVCGKIRR IESLHVSAEA REIGDTTKPS
310
FSDQPLSFDE VMLSKVDN
Length:318
Mass (Da):34,485
Last modified:February 19, 2014 - 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:i76939A4A3FBCE291
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
BX571797 Genomic DNA Translation: CAE12036.1
CU459003 Genomic DNA Translation: CAM78027.1
AM085146 Genomic DNA Translation: CAJ30120.1
HG794546 Genomic DNA Translation: CDK99590.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
CDK99590; CDK99590; MGMSRv2__2375

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mgry:MSR1_03400
mgy:MGMSRv2__2375

<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
BX571797 Genomic DNA Translation: CAE12036.1
CU459003 Genomic DNA Translation: CAM78027.1
AM085146 Genomic DNA Translation: CAJ30120.1
HG794546 Genomic DNA Translation: CDK99590.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3W5XX-ray1.60A215-318[»]
3W5YX-ray1.95A/B215-318[»]
3W5ZX-ray1.66A215-318[»]
3W60X-ray1.82A215-318[»]
3W61X-ray1.59A215-318[»]
3W62X-ray1.64A215-318[»]
3W63X-ray1.90A215-293[»]
3W64X-ray2.85A/B/C/D215-293[»]
3W65X-ray2.37A215-318[»]
3W66X-ray2.05A215-318[»]
3W8GX-ray2.05A/B215-318[»]
3W8PX-ray1.80A/B215-318[»]
5HSPX-ray1.79A/D215-318[»]
6G55X-ray1.65A/D215-318[»]
6G5EX-ray1.60A215-318[»]
6G64X-ray1.90A215-318[»]
6G6IX-ray2.40A/B215-318[»]
6GMTX-ray1.59A215-318[»]
6GMVX-ray1.59A215-318[»]
6GP6X-ray2.15A/B215-318[»]
6H5KX-ray1.54A215-318[»]
6H5MX-ray1.60A215-318[»]
6H5UX-ray2.00A/B/C/H215-318[»]
6H5VX-ray1.49A215-318[»]
6H81X-ray1.50A215-318[»]
6H83X-ray1.50A215-318[»]
6H84X-ray2.04A215-318[»]
6H85X-ray2.00A215-318[»]
6H87X-ray1.50A215-318[»]
6H88X-ray1.50A215-318[»]
6H89X-ray1.70A215-318[»]
6H8AX-ray1.80A215-318[»]
6H8DX-ray1.62A215-318[»]
6H8GX-ray1.35A215-318[»]
6H8IX-ray1.40A215-318[»]
6H9PX-ray2.10A/B/C215-318[»]
6H9QX-ray1.50A215-318[»]
6H9TX-ray1.70A215-318[»]
6HA2X-ray1.50A215-318[»]
6HANX-ray2.60A/B/C/D215-318[»]
6HAOX-ray2.40A215-318[»]
SMRiV6F235
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi1430440.MGMSRv2_2375

Protein family/group databases

TCDBi2.A.4.7.4 the cation diffusion facilitator (cdf) family

Genome annotation databases

EnsemblBacteriaiCDK99590; CDK99590; MGMSRv2__2375
KEGGimgry:MSR1_03400
mgy:MGMSRv2__2375

Family and domain databases

Gene3Di1.20.1510.10, 1 hit
3.30.70.1350, 1 hit
InterProiView protein in InterPro
IPR002524 Cation_efflux
IPR027470 Cation_efflux_CTD
IPR036837 Cation_efflux_CTD_sf
IPR027469 Cation_efflux_TMD_sf
PfamiView protein in Pfam
PF01545 Cation_efflux, 1 hit
PF16916 ZT_dimer, 1 hit
SUPFAMiSSF160240 SSF160240, 1 hit
SSF161111 SSF161111, 1 hit
TIGRFAMsiTIGR01297 CDF, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

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 nameiMAMM_MAGGM
<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: V6F235
Secondary accession number(s): Q6NE57
<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: September 18, 2019
Last sequence update: February 19, 2014
Last modified: October 16, 2019
This is version 40 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)
Annotation programProkaryotic Protein Annotation Program

<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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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