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UniProtKB - Q8SWV6 (FICD_DROME)

Entry version 143 (12 Aug 2020)
Sequence version 1 (01 Jun 2002)
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Protein

Protein adenylyltransferase Fic

Gene

Fic

Organism
Drosophila melanogaster (Fruit fly)
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

Protein that can both mediate the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins (AMPylation), and the removal of the same modification from target proteins (de-AMPylation), depending on the context (PubMed:29089387). The side chain of Glu-247 determines which of the two opposing activities (AMPylase or de-AMPylase) will take place (By similarity). Acts as a key regulator of the unfolded protein response (UPR) by mediating AMPylation or de-AMPylation of Hsc70-3/BiP (PubMed:25395623, PubMed:29089387). In unstressed cells, acts as an adenylyltransferase by mediating AMPylation of Hsc70-3/BiP at 'Thr-518', thereby inactivating it (PubMed:29089387). In response to endoplasmic reticulum stress, acts as a phosphodiesterase by mediating removal of ATP (de-AMPylation) from Hsc70-3/BiP at 'Thr-518', leading to restore HSPA5/BiP activity (PubMed:29089387).By similarity3 Publications

Caution

Was initially thought to mediate AMPylation of Hsc70-3/BiP at 'Thr-366' (PubMed:25395623). However, it was later shown that it catalyzes AMPylation of Hsc70-3/BiP at 'Thr-518'.2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

The side chain of Glu-247 determines which of the two opposing activities (AMPylase or de-AMPylase) will take place. In response to endoplasmic reticulum stress, mediates de-AMPylase activity (By similarity). Adenylyltransferase activity is inhibited by the inhibitory helix present at the N-terminus: Glu-247 binds ATP and competes with ATP-binding at Arg-386, thereby preventing adenylyltransferase activity (By similarity). In unstressed cells, disengagement of Glu-247 promotes adenylyltransferase activity (By similarity). Activation dissociates ATP-binding from Glu-247, allowing ordered binding of the entire ATP moiety with the alpha-phosphate in an orientation that is productive for accepting an incoming target hydroxyl side chain (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei247ATP; via amide nitrogenBy similarity1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei247Important for autoinhibition of adenylyltransferase activityBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei3751 Publication1
Binding sitei419ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi328 – 331ATPBy similarity4
Nucleotide bindingi379 – 386ATPBy similarity8
Nucleotide bindingi411 – 412ATPBy similarity2

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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 functionHydrolase, Nucleotidyltransferase, Transferase
LigandATP-binding, Nucleotide-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:
Protein adenylyltransferase Fic (EC:2.7.7.n12 Publications)
Short name:
dFic1 Publication
Alternative name(s):
De-AMPylase FicCurated (EC:3.1.4.-1 Publication)
<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:Fic1 PublicationImported
ORF Names:CG9523
<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>OrganismiDrosophila melanogaster (Fruit fly)
<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 identifieri7227 [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 lineageiEukaryota › Metazoa › Ecdysozoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Holometabola › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora ›
<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
  • UP000000803 <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: Chromosome 2L

Organism-specific databases

Drosophila genome database

More...FlyBasei		FBgn0263278, Fic

<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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'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>Transmembranei33 – 55HelicalSequence analysisAdd BLAST23

Keywords - Cellular componenti

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

No visible phenotype. Flies are viable.1 Publication

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>Mutagenesisi247E → G: Promotes adenylyltransferase activity. Overexpression is lethal in a Fic null background. 2 Publications1
Mutagenesisi271I → D: Disrupts homodimerization, leading to increased adenylyltransferase activity and reduced phosphodiesterase activity. 1 Publication1
Mutagenesisi375H → A: Abolishes adenylyltransferase and phosphodiesterase activities. 2 Publications1

<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_00003817851 – 492Protein adenylyltransferase FicAdd BLAST492

Proteomic databases

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

More...PaxDbi		Q8SWV6

PRoteomics IDEntifications database

More...PRIDEi		Q8SWV6

<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

Up-regulated in response to endoplasmic reticulum stress.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		FBgn0263278, Expressed in spermathecum and 38 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q8SWV6, DM

<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

Homodimer; homodimerization may regulate adenylyltransferase and phosphodiesterase activities.

1 Publication

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		60054, 4 interactors

Protein interaction database and analysis system

More...IntActi		Q8SWV6, 4 interactors

STRING: functional protein association networks

More...STRINGi		7227.FBpp0078887

<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		Q8SWV6

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 'Family and Domains' section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati118 – 151TPR 1Add BLAST34
Repeati152 – 186TPR 2Add BLAST35
<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>Domaini297 – 432FidoPROSITE-ProRule annotationAdd BLAST136

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>Motifi243 – 248Inhibitory (S/T)XXXE(G/N) motif6

<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 fido domain mediates the adenylyltransferase activity.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

Belongs to the fic family.Curated

Keywords - Domaini

Repeat, TPR repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG3824, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00390000008873

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_040460_0_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q8SWV6

Identification of Orthologs from Complete Genome Data

More...OMAi		DHLYTKA

Database of Orthologous Groups

More...OrthoDBi		1057856at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q8SWV6

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.3290.10, 1 hit
1.25.40.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR003812, Fido
IPR036597, Fido-like_dom_sf
IPR040198, Fido_containing
IPR013026, TPR-contain_dom
IPR011990, TPR-like_helical_dom_sf

The PANTHER Classification System

More...PANTHERi		PTHR13504, PTHR13504, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF02661, Fic, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF140931, SSF140931, 1 hit
SSF48452, SSF48452, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51459, FIDO, 1 hit
PS50293, TPR_REGION, 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.

Q8SWV6-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGTEAEQPSP PAQQQDQENP PLCKAQNPKP ARLYRFVLIF VAGSLAAWTF 
        60         70         80         90        100
HALSSTNLVW KLRQLHHLPT AHYLQTRDEF ALYSVEELNA FKEFYDKSVS 
       110        120        130        140        150
DSVGASYTEA EQTNIKEALG ALRMAQDLYL AGKDDKAARL FEHALALAPR 
       160        170        180        190        200
HPEVLLRYGE FLEHNQRNIV LADQYYFQAL TISPSNSEAL ANRQRTADVV 
       210        220        230        240        250
QSLDERRLES LDSKRDALSA IHESNGALRR AKKEAYFQHI YHSVGIEGNT 
       260        270        280        290        300
MTLAQTRSIL ETRMAVDGKS IDEHNEILGM DLAMKYINAS LVQKIDITIK 
       310        320        330        340        350
DILELHRRVL GHVDPIEGGE FRRNQVYVGG HIPPGPGDLA LLMQRFERWL 
       360        370        380        390        400
NSEHSSTLHP VNYAALAHYK LVHIHPFVDG NGRTSRLLMN TLLMRAGYPP 
       410        420        430        440        450
VIIPKQQRSK YYHFLKLANE GDIRPFVRFI ADCTEKTLDL YLWATSDLPQ 
       460        470        480        490 
QIPMLIQTES EAGERLAQMQ SPNVAQRSSI LEFYESGSGD LP
Length:492
Mass (Da):55,725
Last modified:June 1, 2002 - 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:i452412D2865FED3A
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
AE014134 Genomic DNA Translation: AAF52381.2
AY095059 mRNA Translation: AAM11387.1

NCBI Reference Sequences

More...RefSeqi		NP_609026.1, NM_135182.2

Genome annotation databases

Ensembl metazoan genome annotation project

More...EnsemblMetazoai		FBtr0079257; FBpp0078887; FBgn0263278

Database of genes from NCBI RefSeq genomes

More...GeneIDi		33897

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		dme:Dmel_CG9523

UCSC genome browser

More...UCSCi		CG9523-RA, d. melanogaster

<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
AE014134 Genomic DNA Translation: AAF52381.2
AY095059 mRNA Translation: AAM11387.1
RefSeqiNP_609026.1, NM_135182.2

3D structure databases

SMRiQ8SWV6
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi60054, 4 interactors
IntActiQ8SWV6, 4 interactors
STRINGi7227.FBpp0078887

Proteomic databases

PaxDbiQ8SWV6
PRIDEiQ8SWV6

Genome annotation databases

EnsemblMetazoaiFBtr0079257; FBpp0078887; FBgn0263278
GeneIDi33897
KEGGidme:Dmel_CG9523
UCSCiCG9523-RA, d. melanogaster

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		33897
FlyBaseiFBgn0263278, Fic

Phylogenomic databases

eggNOGiKOG3824, Eukaryota
GeneTreeiENSGT00390000008873
HOGENOMiCLU_040460_0_0_1
InParanoidiQ8SWV6
OMAiDHLYTKA
OrthoDBi1057856at2759
PhylomeDBiQ8SWV6

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		33897, 0 hits in 1 CRISPR screen

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		Btk29A, fly

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		33897

Protein Ontology

More...PROi		PR:Q8SWV6

Gene expression databases

BgeeiFBgn0263278, Expressed in spermathecum and 38 other tissues
GenevisibleiQ8SWV6, DM

Family and domain databases

Gene3Di1.10.3290.10, 1 hit
1.25.40.10, 1 hit
InterProiView protein in InterPro
IPR003812, Fido
IPR036597, Fido-like_dom_sf
IPR040198, Fido_containing
IPR013026, TPR-contain_dom
IPR011990, TPR-like_helical_dom_sf
PANTHERiPTHR13504, PTHR13504, 1 hit
PfamiView protein in Pfam
PF02661, Fic, 1 hit
SUPFAMiSSF140931, SSF140931, 1 hit
SSF48452, SSF48452, 1 hit
PROSITEiView protein in PROSITE
PS51459, FIDO, 1 hit
PS50293, TPR_REGION, 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 nameiFICD_DROME
<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: Q8SWV6
Secondary accession number(s): Q9VMD8
<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: September 1, 2009
Last sequence update: June 1, 2002
Last modified: August 12, 2020
This is version 143 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 programDrosophila annotation project

<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. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
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