rpoA

Functionⁱ

DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. This subunit plays an important role in subunit assembly since its dimerization is the first step in the sequential assembly of subunits to form the holoenzyme.2 Publications

Keywordsⁱ

Molecular function	Nucleotidyltransferase, Transferase
Biological process	Transcription

Enzyme and pathway databases

BioCycⁱ	EcoCyc:EG10893-MONOMER ECOL316407:JW3257-MONOMER MetaCyc:EG10893-MONOMER

BioCycⁱ

EcoCyc:EG10893-MONOMER
ECOL316407:JW3257-MONOMER
MetaCyc:EG10893-MONOMER

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: DNA-directed RNA polymerase subunit alpha (EC:2.7.7.6) Short name: RNAP subunit alpha Alternative name(s): RNA polymerase subunit alpha Transcriptase subunit alpha
Gene namesⁱ	Name:rpoA Synonyms:pez, phs, sez Ordered Locus Names:b3295, JW3257
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	EG10893 rpoA

EcoGeneⁱ

EG10893 rpoA

Subcellular locationⁱ

GO - Cellular componentⁱ

Complete GO annotation on QuickGO ...

Keywords - Cellular componentⁱ

DNA-directed RNA polymerase

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	45	R → C in rpoA112; temperature-sensitive, blocks RNA polymerase assembly. 1 Publication	1
Mutagenesisⁱ	162 – 165	EEDE → AAAA: 5-fold decrease in CRP-class II promoter-dependent transcription. 1 Publication	4
Mutagenesisⁱ	165	E → K: 5-fold decrease in CRP-class II promoter-dependent transcription. 1 Publication	1
Mutagenesisⁱ	191	R → C in rpoA101; temperature-sensitive. 1 Publication	1

Chemistry databases

ChEMBLⁱ	CHEMBL2364672
Drug and drug target database More...DrugBankⁱ	DB00615 Rifabutin DB11753 Rifamycin

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000175304	1 – 329	DNA-directed RNA polymerase subunit alphaAdd BLAST		329

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	265	ADP-ribosylarginine1 Publication	1
Modified residueⁱ	297	N6-acetyllysine1 Publication	1
Modified residueⁱ	298	N6-acetyllysine; by PatZ1 Publication	1

Post-translational modificationⁱ

Acetylated on Lys-297 and Lys-298 in the presence of glucose. PatZ controls acetylation of Lys-298 but not of Lys-297.1 Publication

(Microbial infection) ADP-ribosylated on both alpha subunits by the phage T4 protein ModA (PubMed:10634320, PubMed:15489438). ADP-ribosylated on only one of the alpha subunits by the phage T4 protein Alt (PubMed:15489438).2 Publications

Keywords - PTMⁱ

Acetylation, ADP-ribosylation

Proteomic databases

EPDⁱ	P0A7Z4
jPOSTⁱ	P0A7Z4
PaxDbⁱ	P0A7Z4
PRIDEⁱ	P0A7Z4

2D gel databases

SWISS-2DPAGEⁱ	P0A7Z4

SWISS-2DPAGEⁱ

P0A7Z4

PTM databases

iPTMnetⁱ	P0A7Z4

iPTMnetⁱ

P0A7Z4

Interactionⁱ

Subunit structureⁱ

Homodimer. The RNAP catalytic core consists of 2 alpha, 1 beta, 1 beta' and 1 omega subunit. When a sigma factor is associated with the core the holoenzyme is formed, which can initiate transcription. Both the N- and C-terminus interact with different regions of transcriptional regulator CRP.

5 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct
coaBC	P0ABQ0	2	EBI-544985,EBI-548929
nusA	P0AFF6	7	EBI-544985,EBI-551571
rplB	P60422	6	EBI-544985,EBI-543515

GO - Molecular functionⁱ

protein dimerization activity Source: InterPro

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	4263398, 114 interactors 852106, 1 interactor
Database of interacting proteins More...DIPⁱ	DIP-35879N
IntActⁱ	P0A7Z4, 91 interactors
Molecular INTeraction database More...MINTⁱ	P0A7Z4
STRINGⁱ	511145.b3295

Chemistry databases

BindingDBⁱ

P0A7Z4

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	13 – 32	Combined sources	20
Helixⁱ	35 – 47	Combined sources	13
Beta strandⁱ	54 – 61	Combined sources	8
Beta strandⁱ	65 – 68	Combined sources	4
Beta strandⁱ	74 – 76	Combined sources	3
Helixⁱ	78 – 86	Combined sources	9
Beta strandⁱ	90 – 92	Combined sources	3
Beta strandⁱ	96 – 111	Combined sources	16
Helixⁱ	112 – 114	Combined sources	3
Beta strandⁱ	122 – 124	Combined sources	3
Beta strandⁱ	129 – 133	Combined sources	5
Beta strandⁱ	139 – 148	Combined sources	10
Beta strandⁱ	151 – 153	Combined sources	3
Helixⁱ	155 – 157	Combined sources	3
Helixⁱ	158 – 161	Combined sources	4
Beta strandⁱ	170 – 172	Combined sources	3
Beta strandⁱ	175 – 177	Combined sources	3
Beta strandⁱ	179 – 186	Combined sources	8
Beta strandⁱ	196 – 207	Combined sources	12
Beta strandⁱ	209 – 211	Combined sources	3
Helixⁱ	213 – 227	Combined sources	15
Helixⁱ	228 – 231	Combined sources	4
Helixⁱ	251 – 254	Combined sources	4
Helixⁱ	257 – 260	Combined sources	4
Helixⁱ	264 – 270	Combined sources	7
Turnⁱ	271 – 274	Combined sources	4
Helixⁱ	278 – 283	Combined sources	6
Helixⁱ	286 – 290	Combined sources	5
Beta strandⁱ	292 – 294	Combined sources	3
Helixⁱ	297 – 299	Combined sources	3
Helixⁱ	300 – 303	Combined sources	4
Helixⁱ	308 – 310	Combined sources	3
Beta strandⁱ	318 – 322	Combined sources	5

Show more details

3D structure databases

SMRⁱ	P0A7Z4
ModBaseⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P0A7Z4

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	1 – 235	Alpha N-terminal domain (alpha-NTD)Add BLAST	235
Regionⁱ	162 – 165	Required for interaction with Crp at class II promoters	4
Regionⁱ	249 – 329	Alpha C-terminal domain (alpha-CTD); not required for RNAP assembly or functionAdd BLAST	81

Domainⁱ

The N-terminal domain is essential for RNAP assembly and basal transcription, whereas the C-terminal domain is involved in interaction with transcriptional regulators (such as CRP) and with upstream promoter elements.2 Publications

Sequence similaritiesⁱ

Belongs to the RNA polymerase alpha chain family.Curated

Phylogenomic databases

eggNOGⁱ	COG0202 LUCA
HOGENOMⁱ	HOG000218481
InParanoidⁱ	P0A7Z4
KEGG Orthology (KO) More...KOⁱ	K03040
PhylomeDBⁱ	P0A7Z4

Family and domain databases

Gene3Dⁱ	2.170.120.12, 1 hit 3.30.1360.10, 1 hit
HAMAPⁱ	MF_00059 RNApol_bact_RpoA, 1 hit
InterProⁱ	View protein in InterPro IPR011262 DNA-dir_RNA_pol_insert IPR011263 DNA-dir_RNA_pol_RpoA/D/Rpb3 IPR011773 DNA-dir_RpoA IPR036603 RBP11-like IPR011260 RNAP_asu_C IPR036643 RNApol_insert_sf
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF01000 RNA_pol_A_bac, 1 hit PF03118 RNA_pol_A_CTD, 1 hit PF01193 RNA_pol_L, 1 hit
SMARTⁱ	View protein in SMART SM00662 RPOLD, 1 hit
SUPFAMⁱ	SSF55257 SSF55257, 1 hit SSF56553 SSF56553, 1 hit
TIGRFAMsⁱ	TIGR02027 rpoA, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

P0A7Z4-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MQGSVTEFLK PRLVDIEQVS STHAKVTLEP LERGFGHTLG NALRRILLSS 
        60         70         80         90        100
MPGCAVTEVE IDGVLHEYST KEGVQEDILE ILLNLKGLAV RVQGKDEVIL 
       110        120        130        140        150
TLNKSGIGPV TAADITHDGD VEIVKPQHVI CHLTDENASI SMRIKVQRGR 
       160        170        180        190        200
GYVPASTRIH SEEDERPIGR LLVDACYSPV ERIAYNVEAA RVEQRTDLDK 
       210        220        230        240        250
LVIEMETNGT IDPEEAIRRA ATILAEQLEA FVDLRDVRQP EVKEEKPEFD 
       260        270        280        290        300
PILLRPVDDL ELTVRSANCL KAEAIHYIGD LVQRTEVELL KTPNLGKKSL 
       310        320 
TEIKDVLASR GLSLGMRLEN WPPASIADE

Length:329

Mass (Da):36,512

Last modified:July 21, 1986 - v1

Checksum:ⁱ12A14B75A3CAEA19

GO

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	4	S → N AA sequence (PubMed:1095419).Curated		1
Sequence conflictⁱ	208	N → T in CAA26395 (PubMed:2989779).Curated		1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	J01685 Genomic DNA Translation: AAA24577.1 X00766 Genomic DNA Translation: CAA25337.1 X02543 Genomic DNA Translation: CAA26395.1 U18997 Genomic DNA Translation: AAA58092.1 X53843 Genomic DNA Translation: CAA37838.1 X53844 Genomic DNA Translation: CAA37839.1 U00096 Genomic DNA Translation: AAC76320.1 AP009048 Genomic DNA Translation: BAE77996.1 V00353 Genomic DNA Translation: CAA23646.1 M29822 Genomic DNA Translation: AAA24590.1 M29823 Genomic DNA Translation: AAA24592.1 M29824 Genomic DNA Translation: AAA24594.1
PIRⁱ	A22884 RNECA
NCBI Reference Sequences More...RefSeqⁱ	NP_417754.1, NC_000913.3 WP_001162094.1, NZ_STEB01000038.1

Genome annotation databases

EnsemblBacteriaⁱ	AAC76320; AAC76320; b3295 BAE77996; BAE77996; BAE77996
GeneIDⁱ	947794
KEGGⁱ	ecj:JW3257 eco:b3295
PATRICⁱ	fig\|1411691.4.peg.3436

Protein	Similar proteins		Species	Score	Length	Source
P0A7Z4	DNA-directed RNA polymerase subunit alpha		CITK8		329	UniRef100_A8AQJ0
DNA-directed RNA polymerase subunit alpha	)	ECO24		329
DNA-directed RNA polymerase subunit alpha	)	ECO57		329
DNA-directed RNA polymerase subunit alpha		ECOHS		329
DNA-directed RNA polymerase subunit alpha		ECOK1		329
+371

Protein	Similar proteins		Species	Score	Length	Source
P0A7Z4	DNA-directed RNA polymerase subunit alpha		YERE8		330	UniRef90_A1JS01
DNA-directed RNA polymerase subunit alpha		ENT38		329
DNA-directed RNA polymerase subunit alpha		KLEP7		329
DNA-directed RNA polymerase subunit alpha		SERP5		329
DNA-directed RNA polymerase subunit alpha		MANSM		329
+1884

Protein	Similar proteins		Species	Score	Length	Source
P0A7Z4	DNA-directed RNA polymerase subunit alpha		YERE8		330	UniRef50_A1JS01
DNA-directed RNA polymerase subunit alpha		SODGM		329
DNA-directed RNA polymerase subunit alpha		ALISL		329
DNA-directed RNA polymerase subunit alpha		ACTSZ		329
DNA-directed RNA polymerase subunit alpha		ACTP2		329
+2770

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	J01685 Genomic DNA Translation: AAA24577.1 X00766 Genomic DNA Translation: CAA25337.1 X02543 Genomic DNA Translation: CAA26395.1 U18997 Genomic DNA Translation: AAA58092.1 X53843 Genomic DNA Translation: CAA37838.1 X53844 Genomic DNA Translation: CAA37839.1 U00096 Genomic DNA Translation: AAC76320.1 AP009048 Genomic DNA Translation: BAE77996.1 V00353 Genomic DNA Translation: CAA23646.1 M29822 Genomic DNA Translation: AAA24590.1 M29823 Genomic DNA Translation: AAA24592.1 M29824 Genomic DNA Translation: AAA24594.1
PIRⁱ	A22884 RNECA
RefSeqⁱ	NP_417754.1, NC_000913.3 WP_001162094.1, NZ_STEB01000038.1

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
	1BDF	X-ray	2.50	A/B/C/D	1-235	[»]
	1COO	NMR	-	A	233-329	[»]
	1LB2	X-ray	3.10	B/E	246-329	[»]
	1XS9	NMR	-	D	249-329	[»]
	3IYD	electron microscopy	-	A/B	1-329	[»]
	3K4G	X-ray	2.05	A/B/C/D/E/F/G/H	245-329	[»]
	3LU0	electron microscopy	-	A/B	1-329	[»]
	3N4M	X-ray	2.99	B/C	246-329	[»]
	3N97	X-ray	3.25	B/C	246-329	[»]
	4JK1	X-ray	3.90	A/B/F/G	1-329	[»]
	4JK2	X-ray	4.20	A/B/F/G	1-329	[»]
	4KMU	X-ray	3.85	A/B/F/G	1-329	[»]
	4KN4	X-ray	3.96	A/B/F/G	1-329	[»]
	4KN7	X-ray	3.69	A/B/F/G	1-329	[»]
	4MEX	X-ray	3.90	A/B/G/H	1-329	[»]
	4MEY	X-ray	3.95	A/B/G/H	1-329	[»]
	4S20	X-ray	4.70	A/B/F/G	1-329	[»]
	4XSX	X-ray	3.71	A/B/G/H	1-234	[»]
	4XSY	X-ray	4.01	A/B/G/H	1-234	[»]
	4XSZ	X-ray	3.68	A/B/G/H	1-234	[»]
	4YG2	X-ray	3.70	A/B/G/H	1-329	[»]
	4YLN	X-ray	5.50	A/B/G/H/M/N	1-235	[»]
	4YLO	X-ray	6.00	A/B/G/H/M/N	1-235	[»]
	4YLP	X-ray	5.50	A/B/G/H/M/N	1-235	[»]
	4ZH2	X-ray	4.20	A/B/G/H	2-329	[»]
	4ZH3	X-ray	4.08	A/B/G/H	2-329	[»]
	4ZH4	X-ray	3.99	A/B/G/H	2-329	[»]
	5BYH	X-ray	3.76	A/B	1-329	[»]
	5CIZ	X-ray	5.01	B	246-329	[»]
	5EZK	X-ray	8.50	A/B	1-329	[»]
	5IPL	X-ray	3.60	A/B	1-235	[»]
	5IPM	X-ray	4.20	A/B	1-235	[»]
	5IPN	X-ray	4.61	A/B	1-235	[»]
	5MS0	electron microscopy	9.80	A/B	1-329	[»]
	5MY1	electron microscopy	7.60	V/W	1-329	[»]
	5NSR	electron microscopy	3.80	A/B	1-329	[»]
	5NSS	electron microscopy	5.80	A/B	1-329	[»]
	5NWT	X-ray	3.76	A/B	1-329	[»]
	5UAC	X-ray	3.80	A/B/G/H	1-329	[»]
	5UAG	X-ray	3.40	A/B/G/H	1-320	[»]
	5UAH	X-ray	4.10	A/B/G/H	1-329	[»]
	5UAJ	X-ray	3.92	A/B/G/H	1-329	[»]
	5UAL	X-ray	3.89	A/B/G/H	1-329	[»]
	5UAQ	X-ray	3.60	A/B/G/H	1-329	[»]
	5VSW	X-ray	4.29	A/B/G/H	1-329	[»]
	5VT0	electron microscopy	3.78	G/H	1-234	[»]
	5W1S	X-ray	3.81	A/B/G/H	1-329	[»]
	5W1T	X-ray	4.50	A/B/G/H	1-329	[»]
	6ALF	electron microscopy	4.10	G/H	1-234	[»]
	6ALG	electron microscopy	3.70	G/H	1-234	[»]
	6ALH	electron microscopy	4.40	G/H	1-234	[»]
	6ASX	electron microscopy	3.80	G/H	1-234	[»]
	6BJS	electron microscopy	5.50	G/H	1-234	[»]
	6BYU	X-ray	3.60	A/B/G/H	1-329	[»]
	6C6S	electron microscopy	3.70	G/H	1-234	[»]
	6C6T	electron microscopy	3.50	G/H	1-234	[»]
	6C6U	electron microscopy	3.70	G/H	1-234	[»]
	6C9Y	electron microscopy	4.25	A/B	1-329	[»]
	6CA0	electron microscopy	5.75	A/B	1-329	[»]
	6CUX	X-ray	4.10	A/B/G/H	1-329	[»]
	6FLP	electron microscopy	4.10	A/B	1-329	[»]
	6FLQ	electron microscopy	4.10	A/B	1-329	[»]
	6GFW	electron microscopy	3.70	A/B	1-329	[»]
6GH5	electron microscopy	3.40	A/B	1-329	[»]
6GH6	electron microscopy	4.10	A/B	1-329	[»]
6JBQ	electron microscopy	4.02	A/B	1-329	[»]
6JNX	electron microscopy	4.08	A/B	1-329	[»]
6N60	X-ray	3.68	A/B	1-234	[»]
6N61	X-ray	3.25	A/B	1-234	[»]
6P18	electron microscopy	3.50	A/B	1-329	[»]
6P19	electron microscopy	3.80	A/B	1-329	[»]
6RH3	electron microscopy	3.60	A/B	1-329	[»]
6RI7	electron microscopy	3.90	A/B	1-329	[»]
6RI9	electron microscopy	3.70	A/B	1-329	[»]
6RIN	electron microscopy	3.70	A/B	1-329	[»]
6RIP	electron microscopy	3.40	A/B	1-329	[»]
SMRⁱ	P0A7Z4
ModBaseⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	4263398, 114 interactors 852106, 1 interactor
DIPⁱ	DIP-35879N
IntActⁱ	P0A7Z4, 91 interactors
MINTⁱ	P0A7Z4
STRINGⁱ	511145.b3295

Chemistry databases

BindingDBⁱ	P0A7Z4
ChEMBLⁱ	CHEMBL2364672
DrugBankⁱ	DB00615 Rifabutin DB11753 Rifamycin
DrugCentral More...DrugCentralⁱ	P0A7Z4

PTM databases

iPTMnetⁱ	P0A7Z4

iPTMnetⁱ

P0A7Z4

2D gel databases

SWISS-2DPAGEⁱ	P0A7Z4

SWISS-2DPAGEⁱ

P0A7Z4

Proteomic databases

EPDⁱ	P0A7Z4
jPOSTⁱ	P0A7Z4
PaxDbⁱ	P0A7Z4
PRIDEⁱ	P0A7Z4

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	AAC76320; AAC76320; b3295 BAE77996; BAE77996; BAE77996
GeneIDⁱ	947794
KEGGⁱ	ecj:JW3257 eco:b3295
PATRICⁱ	fig\|1411691.4.peg.3436

Organism-specific databases

EchoBASEⁱ	EB0886
EcoGeneⁱ	EG10893 rpoA

Phylogenomic databases

eggNOGⁱ	COG0202 LUCA
HOGENOMⁱ	HOG000218481
InParanoidⁱ	P0A7Z4
KOⁱ	K03040
PhylomeDBⁱ	P0A7Z4

Enzyme and pathway databases

BioCycⁱ	EcoCyc:EG10893-MONOMER ECOL316407:JW3257-MONOMER MetaCyc:EG10893-MONOMER

BioCycⁱ

EcoCyc:EG10893-MONOMER
ECOL316407:JW3257-MONOMER
MetaCyc:EG10893-MONOMER

Miscellaneous databases

EvolutionaryTraceⁱ	P0A7Z4
Protein Ontology More...PROⁱ	PR:P0A7Z4

Family and domain databases

Gene3Dⁱ	2.170.120.12, 1 hit 3.30.1360.10, 1 hit
HAMAPⁱ	MF_00059 RNApol_bact_RpoA, 1 hit
InterProⁱ	View protein in InterPro IPR011262 DNA-dir_RNA_pol_insert IPR011263 DNA-dir_RNA_pol_RpoA/D/Rpb3 IPR011773 DNA-dir_RpoA IPR036603 RBP11-like IPR011260 RNAP_asu_C IPR036643 RNApol_insert_sf
Pfamⁱ	View protein in Pfam PF01000 RNA_pol_A_bac, 1 hit PF03118 RNA_pol_A_CTD, 1 hit PF01193 RNA_pol_L, 1 hit
SMARTⁱ	View protein in SMART SM00662 RPOLD, 1 hit
SUPFAMⁱ	SSF55257 SSF55257, 1 hit SSF56553 SSF56553, 1 hit
TIGRFAMsⁱ	TIGR02027 rpoA, 1 hit
ProtoNetⁱ	Search...
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	RPOA_ECOLI
Accessionⁱ	P0A7Z4Primary (citable) accession number: P0A7Z4 Secondary accession number(s): P00574, Q2M6W0
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
	Last sequence update:	July 21, 1986
	Last modified:	September 18, 2019
	This is version 144 of the entry and version 1 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

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

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P0A7Z4 (RPOA_ECOLI)

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DNA-directed RNA polymerase subunit alpha

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

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

<p>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

Keywords - 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

Amino acid modifications

Keywords - PTMi

Proteomic databases

2D gel databases

PTM 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

GO - Molecular functioni

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

Region

<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

PTM databases

2D gel 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

Catalytic activityⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ