UniProtKB - P04993 (RECD_ECOLI)

BLAST

>sp|P04993|RECD_ECOLI RecBCD enzyme subunit RecD OS=Escherichia coli (strain K12) OX=83333 GN=recD PE=1 SV=2
MKLQKQLLEAVEHKQLRPLDVQFALTVAGDEHPAVTLAAALLSHDAGEGHVCLPLSRLEN
NEASHPLLATCVSEIGELQNWEECLLASQAVSRGDEPTPMILCGDRLYLNRMWCNERTVA
RFFNEVNHAIEVDEALLAQTLDKLFPVSDEINWQKVAAAVALTRRISVISGGPGTGKTTT
VAKLLAALIQMADGERCRIRLAAPTGKAAARLTESLGKALRQLPLTDEQKKRIPEDASTL
HRLLGAQPGSQRLRHHAGNPLHLDVLVVDEASMIDLPMMSRLIDALPDHARVIFLGDRDQ
LASVEAGAVLGDICAYANAGFTAERARQLSRLTGTHVPAGTGTEAASLRDSLCLLQKSYR
FGSDSGIGQLAAAINRGDKTAVKTVFQQDFTDIEKRLLQSGEDYIAMLEEALAGYGRYLD
LLQARAEPDLIIQAFNEYQLLCALREGPFGVAGLNERIEQFMQQKRKIHRHPHSRWYEGR
PVMIARNDSALGLFNGDIGIALDRGQGTRVWFAMPDGNIKSVQPSRLPEHETTWAMTVHK
SQGSEFDHAALILPSQRTPVVTRELVYTAVTRARRRLSLYADERILSAAIATRTERRSGL
AALFSSRE

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History
Entry version 161 (07 Nov 2018)
Sequence version 2 (01 Nov 1997)
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Protein

RecBCD enzyme subunit RecD

Gene

recD

Organism

Escherichia coli (strain K12)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

A helicase/nuclease that prepares dsDNA breaks (DSB) for recombinational DNA repair. Binds to DSBs and unwinds DNA via a rapid (>1 kb/second) and highly processive (>30 kb) ATP-dependent bidirectional helicase. Unwinds dsDNA until it encounters a Chi (crossover hotspot instigator, 5'-GCTGGTGG-3') sequence from the 3' direction. Cuts ssDNA a few nucleotides 3' to Chi site, by nicking one strand or switching the strand degraded (depending on the reaction conditions). The properties and activities of the enzyme are changed at Chi. The Chi-altered holoenzyme produces a long 3'-ssDNA overhang which facilitates RecA-binding to the ssDNA for homologous DNA recombination and repair. In the holoenzyme this subunit contributes ssDNA-dependent ATPase and fast 5'-3' helicase activity. When added to pre-assembled RecBC greatly stimulates nuclease activity and augments holoenzyme processivity. Negatively regulates the RecA-loading ability of RecBCD.14 Publications

Catalytic activityⁱ

Exonucleolytic cleavage (in the presence of ATP) in either 5'- to 3'- or 3'- to 5'-direction to yield 5'-phosphooligonucleotides.UniRule annotation

Activity regulationⁱ

In isolated subunit ATPase and 5'-3' helicase activity are inhibited by non-hydrolyzable ATP analogs and EDTA (PubMed:12815438). After reacting with DNA bearing a Chi site the holoenzyme is disassembled and loses exonuclease activity, DNA unwinding and Chi-directed DNA cleavage; RecB remains complexed with ssDNA, which may prevent holoenzyme reassembly (PubMed:10197988). High levels of Mg²⁺ (13 mM MgCl²⁺) or incubation with DNase allow holoenyzme reassembly, suggesting it is DNA bound to RecB that prevents reassembly (PubMed:10197988).3 Publications

Regions

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Nucleotide bindingⁱ	171 – 178	ATPCurated		8
DNA bindingⁱ	247	Curated		1

GO - Molecular functionⁱ

ATP binding
Source: EcoliWiki
Inferred from direct assayⁱ
- 3298248
ATP-dependent DNA helicase activity Source: UniProtKB-UniRule
DNA binding Source: UniProtKB-UniRule
exodeoxyribonuclease V activity
Source: EcoCyc
Inferred from direct assayⁱ
- 1618858
helicase activity
Source: EcoCyc
Inferred from direct assayⁱ
- 12815438
single-stranded DNA-dependent ATPase activity
Source: EcoCyc
Inferred from direct assayⁱ
- 9092551

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

cellular response to DNA damage stimulus
Source: EcoliWiki
Inferred from direct assayⁱ
- 1618858
DNA recombination
Source: EcoliWiki
Inferred from direct assayⁱ
- 1618858
double-strand break repair via homologous recombination
Source: EcoCyc
Traceable author statementⁱ
- 19052323

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	DNA-binding, Exonuclease, Helicase, Hydrolase, Nuclease
Biological process	DNA damage, DNA repair
Ligand	ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCycⁱ	EcoCyc:EG10826-MONOMER MetaCyc:EG10826-MONOMER
BRENDAⁱ	3.1.11.5 2026

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: RecBCD enzyme subunit RecDUniRule annotation (EC:3.1.11.5UniRule annotation) Alternative name(s): Exodeoxyribonuclease V 67 kDa polypeptide Exodeoxyribonuclease V alpha chain Exonuclease V subunit RecDUniRule annotation Short name: ExoV subunit RecDUniRule annotation Helicase/nuclease RecBCD subunit RecDUniRule annotation
Gene namesⁱ	Name:recDUniRule annotation Synonyms:hopE Ordered Locus Names:b2819, JW2787
Organismⁱ	Escherichia coli (strain K12)
Taxonomic identifierⁱ	83333 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › Escherichia coli
Proteomesⁱ	UP000000318 Componentⁱ: Chromosome UP000000625 Componentⁱ: Chromosome

Organism-specific databases

EcoGeneⁱ	EG10826 recD

EcoGeneⁱ

EG10826 recD

Subcellular locationⁱ

GO - Cellular componentⁱ

exodeoxyribonuclease V complex
Source: EcoCyc
Inferred from direct assayⁱ
- 15538360

View the complete GO annotation on QuickGO ...

Pathology & Biotechⁱ

Disruption phenotypeⁱ

Loss of RecBCD enzyme exonuclease activity, no effect on recombination proficiency or resistance to DNA-damaging agents.2 Publications

Mutagenesis

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Mutagenesisⁱ	177	K → Q: Loss of ATP-dependent exonuclease activity in holoenzyme. Subunit loses ATPase and has ~5% 5'-3' helicase activity, holoenzyme has 2-4 fold less helicase activity, 5-fold less processivity. 6 Publications		1

Chemistry databases

ChEMBLⁱ	CHEMBL2095232

ChEMBLⁱ

CHEMBL2095232

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000087115	1 – 608	RecBCD enzyme subunit RecDAdd BLAST		608

Proteomic databases

PaxDbⁱ	P04993
PRIDEⁱ	P04993

Interactionⁱ

Subunit structureⁱ

Heterotrimer of RecB, RecC and RecD. All subunits contribute to DNA-binding.UniRule annotation4 Publications

Protein-protein interaction databases

BioGridⁱ	4260684, 132 interactors
ComplexPortalⁱ	CPX-2197 Exodeoxyribonuclease V complex
Database of interacting proteins More...DIPⁱ	DIP-10651N
IntActⁱ	P04993, 13 interactors
Molecular INTeraction database More...MINTⁱ	P04993
STRINGⁱ	316385.ECDH10B_2989

Chemistry databases

BindingDBⁱ

P04993

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	4 – 12	Combined sources	9
Helixⁱ	18 – 27	Combined sources	10
Beta strandⁱ	28 – 31	Combined sources	4
Helixⁱ	33 – 47	Combined sources	15
Beta strandⁱ	51 – 54	Combined sources	4
Turnⁱ	55 – 60	Combined sources	6
Helixⁱ	61 – 64	Combined sources	4
Beta strandⁱ	65 – 67	Combined sources	3
Helixⁱ	81 – 87	Combined sources	7
Beta strandⁱ	91 – 96	Combined sources	6
Beta strandⁱ	99 – 102	Combined sources	4
Beta strandⁱ	104 – 109	Combined sources	6
Helixⁱ	110 – 123	Combined sources	14
Helixⁱ	134 – 142	Combined sources	9
Helixⁱ	153 – 162	Combined sources	10
Beta strandⁱ	164 – 170	Combined sources	7
Helixⁱ	177 – 190	Combined sources	14
Beta strandⁱ	199 – 205	Combined sources	7
Helixⁱ	206 – 216	Combined sources	11
Helixⁱ	218 – 222	Combined sources	5
Turnⁱ	239 – 241	Combined sources	3
Beta strandⁱ	264 – 268	Combined sources	5
Helixⁱ	271 – 273	Combined sources	3
Helixⁱ	276 – 284	Combined sources	9
Beta strandⁱ	291 – 296	Combined sources	6
Helixⁱ	301 – 303	Combined sources	3
Helixⁱ	310 – 313	Combined sources	4
Helixⁱ	314 – 317	Combined sources	4
Helixⁱ	323 – 332	Combined sources	10
Beta strandⁱ	333 – 335	Combined sources	3
Helixⁱ	346 – 349	Combined sources	4
Beta strandⁱ	352 – 354	Combined sources	3
Helixⁱ	367 – 374	Combined sources	8
Helixⁱ	378 – 382	Combined sources	5
Turnⁱ	383 – 385	Combined sources	3
Helixⁱ	387 – 389	Combined sources	3
Beta strandⁱ	392 – 394	Combined sources	3
Turnⁱ	401 – 403	Combined sources	3
Helixⁱ	404 – 414	Combined sources	11
Helixⁱ	416 – 423	Combined sources	8
Helixⁱ	432 – 435	Combined sources	4
Beta strandⁱ	438 – 443	Combined sources	6
Beta strandⁱ	445 – 450	Combined sources	6
Helixⁱ	451 – 459	Combined sources	9
Helixⁱ	460 – 462	Combined sources	3
Beta strandⁱ	534 – 537	Combined sources	4
Turnⁱ	538 – 543	Combined sources	6
Beta strandⁱ	546 – 552	Combined sources	7
Beta strandⁱ	559 – 561	Combined sources	3
Helixⁱ	563 – 570	Combined sources	8
Beta strandⁱ	573 – 575	Combined sources	3
Beta strandⁱ	577 – 580	Combined sources	4
Helixⁱ	585 – 591	Combined sources	7
Helixⁱ	600 – 603	Combined sources	4

Show more details

3D structure databases

ProteinModelPortalⁱ	P04993
SMRⁱ	P04993
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P04993

Family & Domainsⁱ

Domainⁱ

The holoenzyme may undergo conformational shifts upon DNA binding: the nuclease domain of RecB may swing away from the DNA exit tunnel in RecC. When Chi DNA binds to the RecC tunnel the nuclease domain may then swing back to its original position (that seen in crystal structures), allowing it to nick the DNA 3' of the Chi site and then rotate to load RecA. At high Mg²⁺ the nuclease domain may swing back more frequently, explaining differences seen in assays performed at high Mg²⁺.1 Publication

Sequence similaritiesⁱ

Belongs to the RecD family.UniRule annotation

Phylogenomic databases

eggNOGⁱ	ENOG4107QYX Bacteria COG0507 LUCA
HOGENOMⁱ	HOG000258341
InParanoidⁱ	P04993
KEGG Orthology (KO) More...KOⁱ	K03581
PhylomeDBⁱ	P04993

Family and domain databases

HAMAPⁱ	MF_01487 RecD, 1 hit
InterProⁱ	View protein in InterPro IPR003593 AAA+_ATPase IPR027417 P-loop_NTPase IPR006344 RecD IPR027785 UvrD-like_helicase_C
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF13538 UvrD_C_2, 1 hit
SMARTⁱ	View protein in SMART SM00382 AAA, 1 hit
SUPFAMⁱ	SSF52540 SSF52540, 2 hits
TIGRFAMsⁱ	TIGR01447 recD, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

P04993-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MKLQKQLLEA VEHKQLRPLD VQFALTVAGD EHPAVTLAAA LLSHDAGEGH 
        60         70         80         90        100
VCLPLSRLEN NEASHPLLAT CVSEIGELQN WEECLLASQA VSRGDEPTPM 
       110        120        130        140        150
ILCGDRLYLN RMWCNERTVA RFFNEVNHAI EVDEALLAQT LDKLFPVSDE 
       160        170        180        190        200
INWQKVAAAV ALTRRISVIS GGPGTGKTTT VAKLLAALIQ MADGERCRIR 
       210        220        230        240        250
LAAPTGKAAA RLTESLGKAL RQLPLTDEQK KRIPEDASTL HRLLGAQPGS 
       260        270        280        290        300
QRLRHHAGNP LHLDVLVVDE ASMIDLPMMS RLIDALPDHA RVIFLGDRDQ 
       310        320        330        340        350
LASVEAGAVL GDICAYANAG FTAERARQLS RLTGTHVPAG TGTEAASLRD 
       360        370        380        390        400
SLCLLQKSYR FGSDSGIGQL AAAINRGDKT AVKTVFQQDF TDIEKRLLQS 
       410        420        430        440        450
GEDYIAMLEE ALAGYGRYLD LLQARAEPDL IIQAFNEYQL LCALREGPFG 
       460        470        480        490        500
VAGLNERIEQ FMQQKRKIHR HPHSRWYEGR PVMIARNDSA LGLFNGDIGI 
       510        520        530        540        550
ALDRGQGTRV WFAMPDGNIK SVQPSRLPEH ETTWAMTVHK SQGSEFDHAA 
       560        570        580        590        600
LILPSQRTPV VTRELVYTAV TRARRRLSLY ADERILSAAI ATRTERRSGL 

AALFSSRE

Length:608

Mass (Da):66,902

Last modified:November 1, 1997 - v2

Checksum:ⁱC37C62E17D41AA82

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	247 – 248	QP → HR in CAA28253 (PubMed:3537961).Curated	2
Sequence conflictⁱ	306	A → V in CAA28253 (PubMed:3537961).Curated	1
Sequence conflictⁱ	390	F → L in CAA28253 (PubMed:3537961).Curated	1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X04582 Genomic DNA Translation: CAA28253.1 U29581 Genomic DNA Translation: AAB40466.1 U00096 Genomic DNA Translation: AAC75858.1 AP009048 Genomic DNA Translation: BAE76888.1 X04581 Genomic DNA Translation: CAA28251.1
PIRⁱ	D65064 NCECXF
NCBI Reference Sequences More...RefSeqⁱ	NP_417296.1, NC_000913.3 WP_000775955.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaⁱ	AAC75858; AAC75858; b2819 BAE76888; BAE76888; BAE76888
GeneIDⁱ	947287
KEGGⁱ	ecj:JW2787 eco:b2819
PATRICⁱ	fig\|1411691.4.peg.3917

Protein	Similar proteins		Species	Score	Length	Source
P04993	RecBCD enzyme subunit RecD		Shigella sp.		608	UniRef100_P04993
RecBCD enzyme subunit RecD		SHIBO		608
RecBCD enzyme subunit RecD		ECOLX		608
RecBCD enzyme subunit RecD		SHISO		608
RecBCD enzyme subunit RecD		SHIFL		608
+36

Protein	Similar proteins		Species	Score	Length	Source
P04993	RecBCD enzyme subunit RecD		Shigella sp.		608	UniRef90_P04993
RecBCD enzyme subunit RecD		SHIBO		608
RecBCD enzyme subunit RecD		ECOLX		608
RecBCD enzyme subunit RecD		SHISO		608
RecBCD enzyme subunit RecD		SHIFL		608
+811

Protein	Similar proteins		Species	Score	Length	Source
P04993	RecBCD enzyme subunit RecD		Shigella sp.		608	UniRef50_P04993
RecBCD enzyme subunit RecD		SHIBO		608
RecBCD enzyme subunit RecD		ECOLX		608
RecBCD enzyme subunit RecD		SHISO		608
RecBCD enzyme subunit RecD		SHIFL		608
+3038

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X04582 Genomic DNA Translation: CAA28253.1 U29581 Genomic DNA Translation: AAB40466.1 U00096 Genomic DNA Translation: AAC75858.1 AP009048 Genomic DNA Translation: BAE76888.1 X04581 Genomic DNA Translation: CAA28251.1
PIRⁱ	D65064 NCECXF
RefSeqⁱ	NP_417296.1, NC_000913.3 WP_000775955.1, NZ_LN832404.1

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 entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1W36	X-ray	3.10	D/G	1-608	[»]
	3K70	X-ray	3.59	D/G	1-608	[»]
	5LD2	electron microscopy	3.83	D	2-608	[»]
	5MBV	electron microscopy	3.80	D	2-608	[»]
ProteinModelPortalⁱ	P04993
SMRⁱ	P04993
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	4260684, 132 interactors
ComplexPortalⁱ	CPX-2197 Exodeoxyribonuclease V complex
DIPⁱ	DIP-10651N
IntActⁱ	P04993, 13 interactors
MINTⁱ	P04993
STRINGⁱ	316385.ECDH10B_2989

Chemistry databases

BindingDBⁱ	P04993
ChEMBLⁱ	CHEMBL2095232

Proteomic databases

PaxDbⁱ	P04993
PRIDEⁱ	P04993

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	AAC75858; AAC75858; b2819 BAE76888; BAE76888; BAE76888
GeneIDⁱ	947287
KEGGⁱ	ecj:JW2787 eco:b2819
PATRICⁱ	fig\|1411691.4.peg.3917

Organism-specific databases

EchoBASEⁱ	EB0819
EcoGeneⁱ	EG10826 recD

Phylogenomic databases

eggNOGⁱ	ENOG4107QYX Bacteria COG0507 LUCA
HOGENOMⁱ	HOG000258341
InParanoidⁱ	P04993
KOⁱ	K03581
PhylomeDBⁱ	P04993

Enzyme and pathway databases

BioCycⁱ	EcoCyc:EG10826-MONOMER MetaCyc:EG10826-MONOMER
BRENDAⁱ	3.1.11.5 2026

Miscellaneous databases

EvolutionaryTraceⁱ	P04993
Protein Ontology More...PROⁱ	PR:P04993

Family and domain databases

HAMAPⁱ	MF_01487 RecD, 1 hit
InterProⁱ	View protein in InterPro IPR003593 AAA+_ATPase IPR027417 P-loop_NTPase IPR006344 RecD IPR027785 UvrD-like_helicase_C
Pfamⁱ	View protein in Pfam PF13538 UvrD_C_2, 1 hit
SMARTⁱ	View protein in SMART SM00382 AAA, 1 hit
SUPFAMⁱ	SSF52540 SSF52540, 2 hits
TIGRFAMsⁱ	TIGR01447 recD, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	RECD_ECOLI
Accessionⁱ	P04993Primary (citable) accession number: P04993 Secondary accession number(s): Q2MA18, Q59378
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
	Last sequence update:	November 1, 1997
	Last modified:	November 7, 2018
	This is version 161 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

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

Documents

SIMILARITY comments
Index of protein domains and families
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
Escherichia coli
Escherichia coli (strain K12): entries and cross-references to EcoGene

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UniProtKB - P04993 (RECD_ECOLI)

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RecBCD enzyme subunit RecD

recD

Select a section on the left to see content.

<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

Regions

<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

Enzyme and pathway databases

<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

Organism-specific databases

<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

GO - Cellular componenti

<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

Chemistry databases

<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

Proteomic databases

<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

Chemistry databases

<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

3D structure databases

Miscellaneous databases

<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

<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

Phylogenomic databases

Family and domain databases

Experimental Info

Sequence databases

Genome annotation databases

<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

3D structure databases

Protein-protein interaction databases

Chemistry databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<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 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

Documents

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ