UniProtKB - P25745 (MNMA_ECOLI)

>sp|P25745|MNMA_ECOLI tRNA-specific 2-thiouridylase MnmA OS=Escherichia coli (strain K12) OX=83333 GN=mnmA PE=1 SV=4
MSETAKKVIVGMSGGVDSSVSAWLLQQQGYQVEGLFMKNWEEDDGEEYCTAAADLADAQA
VCDKLGIELHTVNFAAEYWDNVFELFLAEYKAGRTPNPDILCNKEIKFKAFLEFAAEDLG
ADYIATGHYVRRADVDGKSRLLRGLDSNKDQSYFLYTLSHEQIAQSLFPVGELEKPQVRK
IAEDLGLVTAKKKDSTGICFIGERKFREFLGRYLPAQPGKIITVDGDEIGEHQGLMYHTL
GQRKGLGIGGTKEGTEEPWYVVDKDVENNILVVAQGHEHPRLMSVGLIAQQLHWVDREPF
TGTMRCTVKTRYRQTDIPCTVKALDDDRIEVIFDEPVAAVTPGQSAVFYNGEVCLGGGII
EQRLPLPV

Entry version 160 (11 Dec 2019)
Sequence version 4 (30 May 2000)
Previous versions | rss

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Protein

tRNA-specific 2-thiouridylase MnmA

Gene

mnmA

Organism

Escherichia coli (strain K12)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA(Lys), tRNA(Glu) and tRNA(Gln), leading to the formation of s₂U34, the first step of tRNA-mnm₅s₂U34 synthesis. Sulfur is provided by IscS, via a sulfur-relay system. Binds ATP and its substrate tRNAs.1 Publication

Miscellaneous

During the reaction, ATP is used to activate the C2 atom of U34 by adenylation. After this, the persulfide sulfur on the catalytic cysteine is transferred to the C2 atom of U34. The reaction probably involves hydrogen sulfide that is generated from the persulfide intermediate and that acts as nucleophile towards the activated C2 atom on U34. Subsequently, Cys-102 acts as nucleophile towards Cys-199, and a transient disulfide bond is formed.

Caution

Was originally thought to be a 5-methylaminomethyl-2-methyltransferase involved in tRNA modification.Curated

Catalytic activityⁱ

AH₂
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ATP
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+
S-sulfanyl-L-cysteinyl-[protein]
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+
uridine³⁴ in tRNA
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=
2-thiouridine³⁴ in tRNA
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+
A
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See the description of this molecule in ChEBI.
+
AMP
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+
diphosphate
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+
H⁺
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+
L-cysteinyl-[protein]
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2 Publications
Manual assertion based on experiment inⁱ
- Ref.7
  "MnmA and IscS are required for in vitro 2-thiouridine biosynthesis in Escherichia coli."
  Kambampati R., Lauhon C.T.
  Biochemistry 42:1109-1117(2003) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, ATP-BINDING, TRNA-BINDING.
- Ref.8
  "Mechanistic insights into sulfur relay by multiple sulfur mediators involved in thiouridine biosynthesis at tRNA wobble positions."
  Ikeuchi Y., Shigi N., Kato J., Nishimura A., Suzuki T.
  Mol. Cell 21:97-108(2006) [PubMed] [Europe PMC] [Abstract]
  Cited for: CATALYTIC ACTIVITY, INTERACTION WITH TUSE.
EC:
2.8.1.13
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
2 Publications
Manual assertion based on experiment inⁱ
- Ref.7
  "MnmA and IscS are required for in vitro 2-thiouridine biosynthesis in Escherichia coli."
  Kambampati R., Lauhon C.T.
  Biochemistry 42:1109-1117(2003) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, ATP-BINDING, TRNA-BINDING.
- Ref.8
  "Mechanistic insights into sulfur relay by multiple sulfur mediators involved in thiouridine biosynthesis at tRNA wobble positions."
  Ikeuchi Y., Shigi N., Kato J., Nishimura A., Suzuki T.
  Mol. Cell 21:97-108(2006) [PubMed] [Europe PMC] [Abstract]
  Cited for: CATALYTIC ACTIVITY, INTERACTION WITH TUSE.
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
. Show »« Hide
AH₂
No structure available
+
ATP
+
S-sulfanyl-L-cysteinyl-[protein]
S-sulfanyl-L-cysteine residue
zoom
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uridine³⁴ in tRNA
UMP residue
zoom
=
2-thiouridine³⁴ in tRNA
2-thiouridine 5'-phosphate residue
zoom
+
A
No structure available
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AMP
+
diphosphate
zoom
+
H⁺
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L-cysteinyl-[protein]
L-cysteine residue
zoom

Sites

Feature key	Position(s)	DescriptionActions	Length
Binding siteⁱ	37	ATP; via amide nitrogen and carbonyl oxygen	1
Active siteⁱ	102	Nucleophile	1
Binding siteⁱ	127	ATP; via amide nitrogen	1
Active siteⁱ	199	Cysteine persulfide intermediate	1

Regions

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Nucleotide bindingⁱ	11 – 18	ATP		8

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

tRNA wobble position uridine thiolation
Source: EcoCyc
Inferred from direct assayⁱ
- Ref.7
  "MnmA and IscS are required for in vitro 2-thiouridine biosynthesis in Escherichia coli."
  Kambampati R., Lauhon C.T.
  Biochemistry 42:1109-1117(2003) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, ATP-BINDING, TRNA-BINDING.

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	RNA-binding, Transferase, tRNA-binding
Biological process	tRNA processing
Ligand	ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCycⁱ	EcoCyc:EG11344-MONOMER ECOL316407:JW1119-MONOMER MetaCyc:EG11344-MONOMER
BRENDAⁱ	2.8.1.4 2026 2.8.1.7 2026 2.8.1.B1 2026

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: tRNA-specific 2-thiouridylase MnmA (EC:2.8.1.132 Publications)
Gene namesⁱ	Name:mnmA Synonyms:asuE, trmU, ycfB Ordered Locus Names:b1133, JW1119
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

Subcellular locationⁱ

Cytoplasm

GO - Cellular componentⁱ

cytosol
Source: EcoCyc
Inferred from direct assayⁱ
- "Protein abundance profiling of the Escherichia coli cytosol."
  Ishihama Y., Schmidt T., Rappsilber J., Mann M., Hartl F.U., Kerner M.J., Frishman D.
  BMC Genomics 9:102-102(2008) [PubMed] [Europe PMC] [Abstract]

Complete GO annotation on QuickGO ...

Keywords - Cellular componentⁱ

Cytoplasm

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	17	D → A: Loss of activity. 1 Publication	1
Mutagenesisⁱ	37	M → A: Reduces activity by 60%. 1 Publication	1
Mutagenesisⁱ	97	N → A: Loss of activity. 1 Publication	1
Mutagenesisⁱ	99	D → A: Loss of activity. 1 Publication	1
Mutagenesisⁱ	102	C → A: Loss of activity. 1 Publication	1
Mutagenesisⁱ	107	K → M: Reduces activity by 75%. 1 Publication	1
Mutagenesisⁱ	128	H → A: Reduces activity by 90%. 1 Publication	1
Mutagenesisⁱ	149	K → A: Loss of activity. 1 Publication	1
Mutagenesisⁱ	151	Q → E: Loss of activity. 1 Publication	1
Mutagenesisⁱ	199	C → A: Abolishes the incorporation of sulfur from the sulfur-relay system; loss of activity. 1 Publication	1
Mutagenesisⁱ	200	F → A: Reduces activity by 60%. 1 Publication	1
Mutagenesisⁱ	239	T → A: Reduces activity by 50%. 1 Publication	1
Mutagenesisⁱ	311	R → A: Reduces activity by 75%. 1 Publication	1
Mutagenesisⁱ	344	Q → A: Loss of activity. 1 Publication	1

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000121588	1 – 368	tRNA-specific 2-thiouridylase MnmAAdd BLAST		368

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Disulfide bondⁱ	102 ↔ 199	Alternate

Keywords - PTMⁱ

Disulfide bond

Proteomic databases

EPDⁱ	P25745
jPOSTⁱ	P25745
PaxDbⁱ	P25745
PRIDEⁱ	P25745

Interactionⁱ

Subunit structureⁱ

Interacts with TusE.

1 Publication

Sites

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Siteⁱ	128	Interaction with tRNA		1
Siteⁱ	344	Interaction with tRNA		1

Protein-protein interaction databases

BioGridⁱ	4263129, 67 interactors 850062, 1 interactor
ComplexPortalⁱ	CPX-2145 TusE-MnmA complex
Database of interacting proteins More...DIPⁱ	DIP-11035N
IntActⁱ	P25745, 8 interactors
STRINGⁱ	511145.b1133

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	7 – 11	Combined sources	5
Helixⁱ	19 – 26	Combined sources	8
Beta strandⁱ	31 – 38	Combined sources	8
Helixⁱ	45 – 65	Combined sources	21
Beta strandⁱ	69 – 73	Combined sources	5
Helixⁱ	75 – 81	Combined sources	7
Helixⁱ	83 – 91	Combined sources	9
Helixⁱ	98 – 105	Combined sources	8
Turnⁱ	106 – 109	Combined sources	4
Helixⁱ	110 – 117	Combined sources	8
Beta strandⁱ	122 – 125	Combined sources	4
Beta strandⁱ	131 – 135	Combined sources	5
Beta strandⁱ	138 – 142	Combined sources	5
Turnⁱ	147 – 149	Combined sources	3
Helixⁱ	152 – 155	Combined sources	4
Helixⁱ	160 – 165	Combined sources	6
Helixⁱ	170 – 172	Combined sources	3
Helixⁱ	175 – 184	Combined sources	10
Helixⁱ	198 – 204	Combined sources	7
Helixⁱ	206 – 211	Combined sources	6
Beta strandⁱ	220 – 223	Combined sources	4
Beta strandⁱ	224 – 226	Combined sources	3
Beta strandⁱ	228 – 231	Combined sources	4
Beta strandⁱ	252 – 254	Combined sources	3
Beta strandⁱ	259 – 265	Combined sources	7
Turnⁱ	266 – 269	Combined sources	4
Beta strandⁱ	270 – 276	Combined sources	7
Turnⁱ	280 – 282	Combined sources	3
Beta strandⁱ	284 – 294	Combined sources	11
Beta strandⁱ	302 – 311	Combined sources	10
Beta strandⁱ	317 – 322	Combined sources	6
Beta strandⁱ	325 – 327	Combined sources	3
Beta strandⁱ	329 – 338	Combined sources	10
Beta strandⁱ	344 – 350	Combined sources	7
Beta strandⁱ	353 – 365	Combined sources	13

Show more details

3D structure databases

SMRⁱ	P25745
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P25745

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	97 – 99	Interaction with target base in tRNA	3
Regionⁱ	149 – 151	Interaction with tRNA	3
Regionⁱ	243 – 252	Interaction with tRNA	10
Regionⁱ	311 – 312	Interaction with tRNA	2

Sequence similaritiesⁱ

Belongs to the MnmA/TRMU family.Curated

Phylogenomic databases

eggNOGⁱ	ENOG4105CCJ Bacteria COG0482 LUCA
HOGENOMⁱ	HOG000218046
InParanoidⁱ	P25745
KEGG Orthology (KO) More...KOⁱ	K00566
PhylomeDBⁱ	P25745

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd01998 tRNA_Me_trans, 1 hit
Gene3Dⁱ	2.30.30.280, 1 hit 3.40.50.620, 1 hit
HAMAPⁱ	MF_00144 tRNA_thiouridyl_MnmA, 1 hit
InterProⁱ	View protein in InterPro IPR023382 Adenine_a_hdrlase_dom IPR014729 Rossmann-like_a/b/a_fold IPR004506 tRNA-specific_2-thiouridylase
TIGRFAMsⁱ	TIGR00420 trmU, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

P25745-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MSETAKKVIV GMSGGVDSSV SAWLLQQQGY QVEGLFMKNW EEDDGEEYCT 
        60         70         80         90        100
AAADLADAQA VCDKLGIELH TVNFAAEYWD NVFELFLAEY KAGRTPNPDI 
       110        120        130        140        150
LCNKEIKFKA FLEFAAEDLG ADYIATGHYV RRADVDGKSR LLRGLDSNKD 
       160        170        180        190        200
QSYFLYTLSH EQIAQSLFPV GELEKPQVRK IAEDLGLVTA KKKDSTGICF 
       210        220        230        240        250
IGERKFREFL GRYLPAQPGK IITVDGDEIG EHQGLMYHTL GQRKGLGIGG 
       260        270        280        290        300
TKEGTEEPWY VVDKDVENNI LVVAQGHEHP RLMSVGLIAQ QLHWVDREPF 
       310        320        330        340        350
TGTMRCTVKT RYRQTDIPCT VKALDDDRIE VIFDEPVAAV TPGQSAVFYN 
       360 
GEVCLGGGII EQRLPLPV

Length:368

Mass (Da):40,959

Last modified:May 30, 2000 - v4

Checksum:ⁱ22CA92676D0805CC

Sequence cautionⁱ

The sequence CAA41994 differs from that shown. Reason: Frameshift.Curated

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U00096 Genomic DNA Translation: AAC74217.2 AP009048 Genomic DNA Translation: BAA35955.1 X59307 Genomic DNA Translation: CAA41994.1 Frameshift. M74924 Genomic DNA No translation available.
PIRⁱ	B64858
NCBI Reference Sequences More...RefSeqⁱ	NP_415651.4, NC_000913.3 WP_001297484.1, NZ_STEB01000016.1

Genome annotation databases

EnsemblBacteriaⁱ	AAC74217; AAC74217; b1133 BAA35955; BAA35955; BAA35955
GeneIDⁱ	945690
KEGGⁱ	ecj:JW1119 eco:b1133
PATRICⁱ	fig\|1411691.4.peg.1133

Protein	Similar proteins		Species	Score	Length	Source
P25745	tRNA-specific 2-thiouridylase MnmA		ECO24		368	UniRef100_A7ZKS3
tRNA-specific 2-thiouridylase MnmA		ECODH		368
tRNA-specific 2-thiouridylase MnmA		ECOHS		368
tRNA-specific 2-thiouridylase MnmA		ECOLC		368
tRNA-specific 2-thiouridylase MnmA		ECOLX		383
+100

Protein	Similar proteins		Species	Score	Length	Source
P25745	tRNA-specific 2-thiouridylase MnmA		SALTY		368	UniRef90_Q8ZPZ4
tRNA-specific 2-thiouridylase MnmA		ECO57		368
tRNA-specific 2-thiouridylase MnmA		SHIF8		368
tRNA-specific 2-thiouridylase MnmA		SHIFL		368
tRNA-specific 2-thiouridylase MnmA		SALAR		368
+569

Protein	Similar proteins		Species	Score	Length	Source
P25745	tRNA-specific 2-thiouridylase MnmA		SALTY		368	UniRef50_Q8ZPZ4
tRNA-specific 2-thiouridylase MnmA		CITK8		368
tRNA-specific 2-thiouridylase MnmA		SHIDS		368
tRNA-specific 2-thiouridylase MnmA		SHIF8		368
tRNA-specific 2-thiouridylase MnmA		SHIFL		368
+4020

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U00096 Genomic DNA Translation: AAC74217.2 AP009048 Genomic DNA Translation: BAA35955.1 X59307 Genomic DNA Translation: CAA41994.1 Frameshift. M74924 Genomic DNA No translation available.
PIRⁱ	B64858
RefSeqⁱ	NP_415651.4, NC_000913.3 WP_001297484.1, NZ_STEB01000016.1

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
	2DER	X-ray	3.10	A/B	1-368	[»]
	2DET	X-ray	3.40	A	1-368	[»]
	2DEU	X-ray	3.40	A/B	1-368	[»]
SMRⁱ	P25745
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	4263129, 67 interactors 850062, 1 interactor
ComplexPortalⁱ	CPX-2145 TusE-MnmA complex
DIPⁱ	DIP-11035N
IntActⁱ	P25745, 8 interactors
STRINGⁱ	511145.b1133

Proteomic databases

EPDⁱ	P25745
jPOSTⁱ	P25745
PaxDbⁱ	P25745
PRIDEⁱ	P25745

Genome annotation databases

EnsemblBacteriaⁱ	AAC74217; AAC74217; b1133 BAA35955; BAA35955; BAA35955
GeneIDⁱ	945690
KEGGⁱ	ecj:JW1119 eco:b1133
PATRICⁱ	fig\|1411691.4.peg.1133

Organism-specific databases

EchoBASEⁱ	EB1320

EchoBASEⁱ

EB1320

Phylogenomic databases

eggNOGⁱ	ENOG4105CCJ Bacteria COG0482 LUCA
HOGENOMⁱ	HOG000218046
InParanoidⁱ	P25745
KOⁱ	K00566
PhylomeDBⁱ	P25745

Enzyme and pathway databases

BioCycⁱ	EcoCyc:EG11344-MONOMER ECOL316407:JW1119-MONOMER MetaCyc:EG11344-MONOMER
BRENDAⁱ	2.8.1.4 2026 2.8.1.7 2026 2.8.1.B1 2026

Miscellaneous databases

EvolutionaryTraceⁱ	P25745
Protein Ontology More...PROⁱ	PR:P25745

Family and domain databases

CDDⁱ	cd01998 tRNA_Me_trans, 1 hit
Gene3Dⁱ	2.30.30.280, 1 hit 3.40.50.620, 1 hit
HAMAPⁱ	MF_00144 tRNA_thiouridyl_MnmA, 1 hit
InterProⁱ	View protein in InterPro IPR023382 Adenine_a_hdrlase_dom IPR014729 Rossmann-like_a/b/a_fold IPR004506 tRNA-specific_2-thiouridylase
TIGRFAMsⁱ	TIGR00420 trmU, 1 hit
ProtoNetⁱ	Search...
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	MNMA_ECOLI
Accessionⁱ	P25745Primary (citable) accession number: P25745 Secondary accession number(s): P75964
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
	Last sequence update:	May 30, 2000
	Last modified:	December 11, 2019
	This is version 160 of the entry and version 4 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

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UniProtKB - P25745 (MNMA_ECOLI)

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tRNA-specific 2-thiouridylase MnmA

mnmA

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

Miscellaneous

Caution

<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

Sites

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

<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

<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

<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

Sites

Protein-protein interaction 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

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

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

Proteomic 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

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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

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequence cautionⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ