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Entry version 145 (02 Jun 2021)
Sequence version 2 (01 Feb 1996)
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Protein

DDE-recombinase A

Gene

A

Organism
Escherichia phage Mu (Bacteriophage Mu)
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

Responsible for viral genome integration into the host chromosome. During integration of the incoming virus, DDE-recombinase A cleaves both viral DNA ends and the resulting 3'-OH perform a nucleophilic attack of the host DNA. The 5' flanking DNA attached to the ends of the viral genome (flaps) are resected by the DDE-recombinase A endonuclease activity, with the help of host chaperone ClpX. The gaps created in the host chromosome by the viral genome insertion are repaired by the host primary machinery for double-strand break repair.

Responsible for replication of the viral genome by replicative transposition. During replicative transposition, DDE-recombinase A is part of the transpososome complex. DDE-recombinase A cleaves the viral DNA and the resulting 3'-OH performs a nucleophilic attack of the host DNA. The 5' flanking DNA is not resected and an intermediary structure is formed. This structure is resolved by target-primed replication leading to two copies of the viral genome (the original one and the copied one). Host ClpX and translation initiation factor IF2 play an essential transpososome-remodeling role by releasing the block between transposition and DNA replication. Successive rounds of replicative transposition can lead up to 100 copies of the viral genome.

Promotes replication and thereby lytic development by competing with repressor c (Repc) for binding to the internal activation sequence (IAS) in the enhancer/operator region. The outcome of this competition determines if the virus enters latency or starts replication.

Miscellaneous

This enzyme is structurally similar to and performs the same endonucleotidic reaction as retroviral integrases, RNase H, RuvC holliday resolvases and RAG proteins.

<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

Mg2+2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi269Magnesium; catalytic1
Metal bindingi336Magnesium; catalyticCurated1
Metal bindingi392Magnesium; catalytic1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section specifies the position and type of each DNA-binding domain present within the protein.<p><a href='/help/dna_bind' target='_top'>More...</a></p>DNA bindingi176 – 196H-T-H motif; viral genome ends bindingPROSITE-ProRule annotationAdd BLAST21

<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 functionDNA-binding, Hydrolase, Ligase, Nuclease
Biological processDNA excision, DNA integration, DNA recombination, DNA replication, Latency-replication decision, Transposition, Viral DNA replication
LigandMagnesium, Metal-binding

<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%5Fand%5Ftaxonomy%5Fsection">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:
DDE-recombinase A (EC:3.1.22.-, EC:6.5.1.-)
Alternative name(s):
DDE-transposase A
Gene product 03
Short name:
gp03
Gene product A
Short name:
gpA
MuA
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:A
Ordered Locus Names:Mup03
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiEscherichia phage Mu (Bacteriophage Mu)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri10677 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiVirusesDuplodnaviriaHeunggongviraeUroviricotaCaudoviricetesCaudoviralesMyoviridaeMuvirus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section only exists in viral entries and indicates the host(s) either as a specific organism or taxonomic group of organisms that are susceptible to be infected by a virus.<p><a href='/help/virus_host' target='_top'>More...</a></p>Virus hostiEnterobacteriaceae [TaxID: 543]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
  • UP000002611 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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: Genome

<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

Keywords - Cellular componenti

Host cytoplasm

<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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi269D → N: Complete loss of both the DNA cleavage and joining activities without bloing tetramer assembly. 2 Publications1
Mutagenesisi269D → V: Loss of DNA-protein assembly. 2 Publications1
Mutagenesisi294D → N: Almost complete loss of both the DNA cleavage and joining activities without bloing tetramer assembly. 2 Publications1
Mutagenesisi348G → D: Loss of DNA-protein assembly. 1 Publication1
Mutagenesisi392E → A: Complete loss of both the DNA cleavage and joining activities without bloing tetramer assembly. 2 Publications1
Mutagenesisi392E → Q: Complete loss of both the DNA cleavage and joining activities without bloing tetramer assembly. 2 Publications1
Mutagenesisi550D → N: Almost no effect on both the DNA cleavage and joining activities without bloing tetramer assembly. 1 Publication1
Mutagenesisi556E → Q: Almost no effect on both the DNA cleavage and joining activities without bloing tetramer assembly. 1 Publication1
Mutagenesisi558E → Q: Almost no effect on both the DNA cleavage and joining activities without bloing tetramer assembly. 1 Publication1
Mutagenesisi567D → N: Almost no effect on both the DNA cleavage and joining activities without bloing tetramer assembly. 1 Publication1
Mutagenesisi573E → Q: Almost no effect on both the DNA cleavage and joining activities without bloing tetramer assembly. 1 Publication1
Mutagenesisi575 – 579RRRQK → KKKQR: No effect on DNA-binding and flaps endonuclease activity. 1 Publication5
Mutagenesisi575 – 579RRRQK → LQLQQ: Almost complete loss of flaps endonuclease activity, DNA-binding and transpososome assembly. 1 Publication5
Mutagenesisi576 – 579RRQK → QRQQ: Partial loss of flaps endonuclease activity resulting in delayed flaps removal. Complete loss of DNA-binding. 4
Mutagenesisi596D → N: Almost no effect on both the DNA cleavage and joining activities without bloing tetramer assembly. 1 Publication1
Mutagenesisi599E → Q: Almost no effect on both the DNA cleavage and joining activities without bloing tetramer assembly. 1 Publication1
Mutagenesisi602E → Q: Almost no effect on both the DNA cleavage and joining activities without bloing tetramer assembly. 1 Publication1

<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_00000775841 – 663DDE-recombinase AAdd BLAST663

<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

Expressed in the early phase of the viral replicative cycle. Expression of early genes is repressed by viral Repc (latency) and favored by viral Ner protein.1 Publication

Keywords - Developmental stagei

Early protein

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homotetramer. Part of the transpososome complex composed of a DDE-recombinase A tetramer synapsing the ends of the viral genome and the enhancer element.

Interacts with target DNA activator B; this interaction brings DDE-recombinase A to the transposition target site.

Interacts with host ClpX; this interaction remodels the transpososome for replication and is required for the flaps endonuclease activity of DDE-recombinase A. Binds (via N-terminus) three distinct recognition sites in the AttR and AttL regions of the viral genome ends: R1, R2, and R3 on the right end and L1, L2, and L3 on the left, not all of which are essential for transposition. The active transpososome is formed by three DDE-recombinase A subunits tightly bound to R1, R2, L1 plus a fourth subunit tightly bound in the complex but weakly bound to the L2 recognition site. Only two subunits out of the four involved are responsible for catalysis. Each subunit performs the cleavage and joining reactions for one DNA end and acts in trans, ensuring the reaction is only initiated when both viral genome ends are paired.

4 Publications

Protein-protein interaction databases

Database of interacting proteins

More...
DIPi
DIP-59984N

<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

Secondary structure

1663
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Biological Magnetic Resonance Data Bank

More...
BMRBi
P07636

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

More...
SMRi
P07636

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P07636

<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%5Fand%5Fdomains%5Fsection">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>Domaini1 – 69HTH Mu-type; 1-alpha, viral IAS bindingPROSITE-ProRule annotationAdd BLAST69

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>Regioni77 – 1741-beta, viral genome ends bindingAdd BLAST98
Regioni175 – 2471-gamma, viral genome ends bindingAdd BLAST73
Regioni249 – 490CatalyticAdd BLAST242
Regioni491 – 605Target DNA capture and bendingAdd BLAST115
Regioni575 – 579Involved in flaps endonuclease activity5
Regioni605 – 663Interaction with MuBAdd BLAST59
Regioni656 – 663Interaction with and host ClpX8

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi269 – 392DDEAdd BLAST124

<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 catalytic domain contains two distinct activities, the cleavage and strand transfer activity and the flaps endonuclease activity. The N-terminal HTH Mu-type domain 1-alpha is responsible for sequence-specific DNA binding to the IAS. Two adjacent regions 1-beta and 1-gamma bind to the ends of the viral genome.
Contains a D-x(n)-D-x(35)-E motif, named for the conserved glutamic acid and aspartic acid residues and the invariant 35 amino acid spacing between the second and third acidic residues. These residues coordinate the metal ions required for nucleophile activation. Each acidic residue of the D,D(35)E motif is independently essential for the 3'-processing and strand transfer activities (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

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.10.10, 1 hit
2.30.30.130, 1 hit
3.30.420.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR009061, DNA-bd_dom_put_sf
IPR009057, Homeobox-like_sf
IPR003314, Mu-type_HTH
IPR015126, Mu_I-gamma
IPR004189, Phage_Mu_transposase
IPR012337, RNaseH-like_sf
IPR036397, RNaseH_sf
IPR015378, Transposase-like_Mu_C
IPR009004, Transposase_Mu_C
IPR036388, WH-like_DNA-bd_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF02914, DDE_2, 1 hit
PF02316, HTH_Tnp_Mu_1, 1 hit
PF09039, HTH_Tnp_Mu_2, 1 hit
PF09299, Mu-transpos_C, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF46689, SSF46689, 2 hits
SSF46955, SSF46955, 1 hit
SSF50610, SSF50610, 1 hit
SSF53098, SSF53098, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51702, HTH_MU, 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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

P07636-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MELWVSPKEC ANLPGLPKTS AGVIYVAKKQ GWQNRTRAGV KGGKAIEYNA
60 70 80 90 100
NSLPVEAKAA LLLRQGEIET SLGYFEIARP TLEAHDYDRE ALWSKWDNAS
110 120 130 140 150
DSQRRLAEKW LPAVQAADEM LNQGISTKTA FATVAGHYQV SASTLRDKYY
160 170 180 190 200
QVQKFAKPDW AAALVDGRGA SRRNVHKSEF DEDAWQFLIA DYLRPEKPAF
210 220 230 240 250
RKCYERLELA AREHGWSIPS RATAFRRIQQ LDEAMVVACR EGEHALMHLI
260 270 280 290 300
PAQQRTVEHL DAMQWINGDG YLHNVFVRWF NGDVIRPKTW FWQDVKTRKI
310 320 330 340 350
LGWRCDVSEN IDSIRLSFMD VVTRYGIPED FHITIDNTRG AANKWLTGGA
360 370 380 390 400
PNRYRFKVKE DDPKGLFLLM GAKMHWTSVV AGKGWGQAKP VERAFGVGGL
410 420 430 440 450
EEYVDKHPAL AGAYTGPNPQ AKPDNYGDRA VDAELFLKTL AEGVAMFNAR
460 470 480 490 500
TGRETEMCGG KLSFDDVFER EYARTIVRKP TEEQKRMLLL PAEAVNVSRK
510 520 530 540 550
GEFTLKVGGS LKGAKNVYYN MALMNAGVKK VVVRFDPQQL HSTVYCYTLD
560 570 580 590 600
GRFICEAECL APVAFNDAAA GREYRRRQKQ LKSATKAAIK AQKQMDALEV
610 620 630 640 650
AELLPQIAEP AAPESRIVGI FRPSGNTERV KNQERDDEYE TERDEYLNHS
660
LDILEQNRRK KAI
Length:663
Mass (Da):75,003
Last modified:February 1, 1996 - v2
<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:iB882CFDCBFC0B2E3
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti66G → R in CAA24236 (PubMed:6222246).Curated1
Sequence conflicti408P → S in AAA32379 (Ref. 2) Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M11195 Genomic DNA Translation: AAA32369.1
M64097 Genomic DNA Translation: AAA32379.1
AF083977 Genomic DNA Translation: AAF01083.1
V01464 Genomic DNA Translation: CAA24713.1
V00868 Genomic DNA Translation: CAA24236.1

Protein sequence database of the Protein Information Resource

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PIRi
A24746, TQBPU

NCBI Reference Sequences

More...
RefSeqi
NP_050607.1, NC_000929.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

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GeneIDi
2636292

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
vg:2636292

<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
M11195 Genomic DNA Translation: AAA32369.1
M64097 Genomic DNA Translation: AAA32379.1
AF083977 Genomic DNA Translation: AAF01083.1
V01464 Genomic DNA Translation: CAA24713.1
V00868 Genomic DNA Translation: CAA24236.1
PIRiA24746, TQBPU
RefSeqiNP_050607.1, NC_000929.1

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
1BCMX-ray2.80A/B248-574[»]
1BCOX-ray2.40A248-574[»]
1TNSNMR-A1-76[»]
1TNTNMR-A1-76[»]
2EZHNMR-A174-247[»]
2EZINMR-A174-247[»]
2EZKNMR-A77-174[»]
2EZLNMR-A77-174[»]
4FCYX-ray3.71A/B77-605[»]
BMRBiP07636
SMRiP07636
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

DIPiDIP-59984N

Genome annotation databases

GeneIDi2636292
KEGGivg:2636292

Miscellaneous databases

EvolutionaryTraceiP07636

Family and domain databases

Gene3Di1.10.10.10, 1 hit
2.30.30.130, 1 hit
3.30.420.10, 1 hit
InterProiView protein in InterPro
IPR009061, DNA-bd_dom_put_sf
IPR009057, Homeobox-like_sf
IPR003314, Mu-type_HTH
IPR015126, Mu_I-gamma
IPR004189, Phage_Mu_transposase
IPR012337, RNaseH-like_sf
IPR036397, RNaseH_sf
IPR015378, Transposase-like_Mu_C
IPR009004, Transposase_Mu_C
IPR036388, WH-like_DNA-bd_sf
PfamiView protein in Pfam
PF02914, DDE_2, 1 hit
PF02316, HTH_Tnp_Mu_1, 1 hit
PF09039, HTH_Tnp_Mu_2, 1 hit
PF09299, Mu-transpos_C, 1 hit
SUPFAMiSSF46689, SSF46689, 2 hits
SSF46955, SSF46955, 1 hit
SSF50610, SSF50610, 1 hit
SSF53098, SSF53098, 1 hit
PROSITEiView protein in PROSITE
PS51702, HTH_MU, 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 nameiTNPA_BPMU
<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: P07636
Secondary accession number(s): P06021
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: February 1, 1996
Last modified: June 2, 2021
This is version 145 of the entry and version 2 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 programViral 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, Reference proteome, Transposable element

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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