UniProtKB - P05618 (CDGT_BACS0)

BLAST

>sp|P05618|CDGT_BACS0 Cyclomaltodextrin glucanotransferase OS=Bacillus sp. (strain 1011) OX=1410 GN=cgt PE=1 SV=1
MKRFMKLTAVWTLWLSLTLGLLSPVHAAPDTSVSNKQNFSTDVIYQIFTDRFSDGNPANN
PTGAAFDGSCTNLRLYCGGDWQGIINKINDGYLTGMGITAIWISQPVENIYSVINYSGVN
NTAYHGYWARDFKKTNPAYGTMQDFKNLIDTAHAHNIKVIIDFAPNHTSPASSDDPSFAE
NGRLYDNGNLLGGYTNDTQNLFHHYGGTDFSTIENGIYKNLYDLADLNHNNSSVDVYLKD
AIKMWLDLGVDGIRVDAVKHMPFGWQKSFMATINNYKPVFTFGEWFLGVNEISPEYHQFA
NESGMSLLDFRFAQKARQVFRDNTDNMYGLKAMLEGSEVDYAQVNDQVTFIDNHDMERFH
TSNGDRRKLEQALAFTLTSRGVPAIYYGSEQYMSGGNDPDNRARLPSFSTTTTAYQVIQK
LAPLRKSNPAIAYGSTHERWINNDVIIYERKFGNNVAVVAINRNMNTPASITGLVTSLRR
ASYNDVLGGILNGNTLTVGAGGAASNFTLAPGGTAVWQYTTDATTPIIGNVGPMMAKPGV
TITIDGRGFGSGKGTVYFGTTAVTGADIVAWEDTQIQVKIPAVPGGIYDIRVANAAGAAS
NIYDNFEVLTGDQVTVRFVINNATTALGQNVFLTGNVSELGNWDPNNAIGPMYNQVVYQY
PTWYYDVSVPAGQTIEFKFLKKQGSTVTWEGGANRTFTTPTSGTATVNVNWQP

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History
Entry version 127 (23 May 2018)
Sequence version 1 (01 Nov 1988)
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Protein

Cyclomaltodextrin glucanotransferase

Gene

cgt

Organism

Bacillus sp. (strain 1011)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

Catalytic activityⁱ

Cyclizes part of a (1->4)-alpha-D-glucan chain by formation of a (1->4)-alpha-D-glucosidic bond.

Cofactorⁱ

Ca²⁺Note: Binds 2 calcium ions per subunit.

Sites

Feature key	Position(s)	DescriptionActions	Length
Metal bindingⁱ	54	Calcium 1	1
Metal bindingⁱ	56	Calcium 1; via carbonyl oxygen	1
Metal bindingⁱ	59	Calcium 1	1
Metal bindingⁱ	60	Calcium 1	1
Metal bindingⁱ	78	Calcium 1; via carbonyl oxygen	1
Metal bindingⁱ	80	Calcium 1	1
Metal bindingⁱ	166	Calcium 2	1
Binding siteⁱ	167	SubstrateBy similarity	1
Metal bindingⁱ	217	Calcium 2; via carbonyl oxygen	1
Metal bindingⁱ	226	Calcium 2	1
Binding siteⁱ	254	SubstrateBy similarity	1
Active siteⁱ	256	Nucleophile	1
Metal bindingⁱ	260	Calcium 2; via carbonyl oxygen	1
Active siteⁱ	284	Proton donor	1
Binding siteⁱ	354	SubstrateBy similarity	1
Siteⁱ	355	Transition state stabilizerBy similarity	1
Binding siteⁱ	398	Substrate	1
Binding siteⁱ	402	Substrate	1

GO - Molecular functionⁱ

cyclomaltodextrin glucanotransferase activity Source: UniProtKB-EC
metal ion binding Source: UniProtKB-KW
starch binding Source: InterPro

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

carbohydrate metabolic process Source: InterPro

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Glycosyltransferase, Transferase
Ligand	Calcium, Metal-binding

Enzyme and pathway databases

BRENDAⁱ	2.4.1.19 691

BRENDAⁱ

2.4.1.19 691

Protein family/group databases

Carbohydrate-Active enZymes More...CAZyⁱ	CBM20 Carbohydrate-Binding Module Family 20 GH13 Glycoside Hydrolase Family 13

CAZyⁱ

CBM20 Carbohydrate-Binding Module Family 20
GH13 Glycoside Hydrolase Family 13

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Cyclomaltodextrin glucanotransferase (EC:2.4.1.19) Alternative name(s): Cyclodextrin-glycosyltransferase Short name: CGTase
Gene namesⁱ	Name:cgt
Organismⁱ	Bacillus sp. (strain 1011)
Taxonomic identifierⁱ	1410 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Terrabacteria group › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus

Subcellular locationⁱ

Secreted By similarity

GO - Cellular componentⁱ

extracellular region Source: UniProtKB-SubCell

View the complete GO annotation on QuickGO ...

Keywords - Cellular componentⁱ

Secreted

Pathology & Biotechⁱ

Chemistry databases

Drug and drug target database More...DrugBankⁱ	DB02379 Beta-D-Glucose DB03206 Duvoglustat

DrugBankⁱ

DB02379 Beta-D-Glucose
DB03206 Duvoglustat

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Signal peptideⁱ	1 – 27	Add BLAST		27
ChainⁱPRO_0000001437	28 – 713	Cyclomaltodextrin glucanotransferaseAdd BLAST		686

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Disulfide bondⁱ	70 ↔ 77

Keywords - PTMⁱ

Disulfide bond

Proteomic databases

PRIDEⁱ	P05618

PRIDEⁱ

P05618

Interactionⁱ

Subunit structureⁱ

Monomer.

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	44 – 46	Combined sources	3
Helixⁱ	49 – 51	Combined sources	3
Helixⁱ	57 – 59	Combined sources	3
Helixⁱ	63 – 65	Combined sources	3
Helixⁱ	81 – 89	Combined sources	9
Turnⁱ	90 – 93	Combined sources	4
Helixⁱ	94 – 96	Combined sources	3
Beta strandⁱ	100 – 103	Combined sources	4
Beta strandⁱ	107 – 109	Combined sources	3
Beta strandⁱ	114 – 116	Combined sources	3
Beta strandⁱ	119 – 121	Combined sources	3
Beta strandⁱ	128 – 135	Combined sources	8
Turnⁱ	137 – 139	Combined sources	3
Helixⁱ	142 – 154	Combined sources	13
Beta strandⁱ	158 – 163	Combined sources	6
Beta strandⁱ	167 – 170	Combined sources	4
Turnⁱ	179 – 182	Combined sources	4
Beta strandⁱ	184 – 186	Combined sources	3
Beta strandⁱ	189 – 192	Combined sources	4
Beta strandⁱ	194 – 196	Combined sources	3
Beta strandⁱ	210 – 212	Combined sources	3
Helixⁱ	213 – 218	Combined sources	6
Beta strandⁱ	219 – 221	Combined sources	3
Beta strandⁱ	224 – 227	Combined sources	4
Helixⁱ	232 – 247	Combined sources	16
Beta strandⁱ	252 – 255	Combined sources	4
Helixⁱ	258 – 260	Combined sources	3
Helixⁱ	263 – 276	Combined sources	14
Beta strandⁱ	280 – 283	Combined sources	4
Helixⁱ	294 – 302	Combined sources	9
Beta strandⁱ	303 – 308	Combined sources	6
Helixⁱ	310 – 320	Combined sources	11
Helixⁱ	327 – 340	Combined sources	14
Beta strandⁱ	341 – 343	Combined sources	3
Helixⁱ	344 – 346	Combined sources	3
Beta strandⁱ	347 – 349	Combined sources	3
Beta strandⁱ	362 – 364	Combined sources	3
Helixⁱ	366 – 378	Combined sources	13
Beta strandⁱ	379 – 386	Combined sources	8
Helixⁱ	389 – 391	Combined sources	3
Helixⁱ	400 – 402	Combined sources	3
Helixⁱ	413 – 421	Combined sources	9
Helixⁱ	424 – 427	Combined sources	4
Helixⁱ	429 – 433	Combined sources	5
Beta strandⁱ	435 – 441	Combined sources	7
Beta strandⁱ	443 – 452	Combined sources	10
Beta strandⁱ	455 – 462	Combined sources	8
Beta strandⁱ	465 – 467	Combined sources	3
Beta strandⁱ	469 – 471	Combined sources	3
Beta strandⁱ	473 – 475	Combined sources	3
Beta strandⁱ	480 – 483	Combined sources	4
Turnⁱ	486 – 491	Combined sources	6
Beta strandⁱ	496 – 498	Combined sources	3
Helixⁱ	500 – 502	Combined sources	3
Beta strandⁱ	507 – 509	Combined sources	3
Beta strandⁱ	514 – 519	Combined sources	6
Beta strandⁱ	527 – 532	Combined sources	6
Beta strandⁱ	534 – 536	Combined sources	3
Beta strandⁱ	541 – 547	Combined sources	7
Beta strandⁱ	555 – 558	Combined sources	4
Beta strandⁱ	561 – 563	Combined sources	3
Helixⁱ	565 – 567	Combined sources	3
Beta strandⁱ	568 – 571	Combined sources	4
Beta strandⁱ	573 – 579	Combined sources	7
Beta strandⁱ	585 – 593	Combined sources	9
Beta strandⁱ	603 – 608	Combined sources	6
Beta strandⁱ	610 – 622	Combined sources	13
Beta strandⁱ	630 – 637	Combined sources	8
Helixⁱ	638 – 640	Combined sources	3
Turnⁱ	641 – 643	Combined sources	3
Helixⁱ	645 – 647	Combined sources	3
Beta strandⁱ	655 – 658	Combined sources	4
Beta strandⁱ	663 – 670	Combined sources	8
Beta strandⁱ	673 – 683	Combined sources	11
Beta strandⁱ	686 – 689	Combined sources	4
Beta strandⁱ	695 – 698	Combined sources	4
Beta strandⁱ	701 – 710	Combined sources	10

Show more details

3D structure databases

ProteinModelPortalⁱ	P05618
SMRⁱ	P05618
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P05618

EvolutionaryTraceⁱ

P05618

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	526 – 607	IPT/TIGAdd BLAST		82
Domainⁱ	608 – 713	CBM20PROSITE-ProRule annotationAdd BLAST		106

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	28 – 165	A1Add BLAST	138
Regionⁱ	127 – 128	Substrate binding	2
Regionⁱ	166 – 229	BAdd BLAST	64
Regionⁱ	220 – 223	Substrate binding	4
Regionⁱ	230 – 433	A2Add BLAST	204
Regionⁱ	259 – 260	Substrate bindingBy similarity	2
Regionⁱ	434 – 522	CAdd BLAST	89
Regionⁱ	523 – 609	DAdd BLAST	87
Regionⁱ	610 – 713	EAdd BLAST	104

Domainⁱ

May consist of two protein domains: the one in the N-terminal side cleaves the alpha-1,4-glucosidic bond in starch, and the other in the C-terminal side catalyzes other activities, including the reconstitution of an alpha-1,4-glucosidic linkage for cyclizing the maltooligosaccharide produced.

Sequence similaritiesⁱ

Belongs to the glycosyl hydrolase 13 family.Curated

Keywords - Domainⁱ

Signal

Family and domain databases

Gene3Dⁱ	2.60.40.10, 2 hits 2.60.40.1180, 1 hit
InterProⁱ	View protein in InterPro IPR006048 A-amylase/branching_C IPR031319 A-amylase_C IPR006046 Alpha_amylase IPR013784 Carb-bd-like_fold IPR002044 CBM_fam20 IPR006047 Glyco_hydro_13_cat_dom IPR013780 Glyco_hydro_b IPR017853 Glycoside_hydrolase_SF IPR013783 Ig-like_fold IPR014756 Ig_E-set IPR002909 IPT_dom
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00128 Alpha-amylase, 1 hit PF02806 Alpha-amylase_C, 1 hit PF00686 CBM_20, 1 hit PF01833 TIG, 1 hit
PRINTSⁱ	PR00110 ALPHAAMYLASE
SMARTⁱ	View protein in SMART SM00642 Aamy, 1 hit SM00632 Aamy_C, 1 hit SM01065 CBM_2, 1 hit
SUPFAMⁱ	SSF49452 SSF49452, 1 hit SSF51445 SSF51445, 1 hit SSF81296 SSF81296, 1 hit
PROSITEⁱ	View protein in PROSITE PS51166 CBM20, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

P05618-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MKRFMKLTAV WTLWLSLTLG LLSPVHAAPD TSVSNKQNFS TDVIYQIFTD 
        60         70         80         90        100
RFSDGNPANN PTGAAFDGSC TNLRLYCGGD WQGIINKIND GYLTGMGITA 
       110        120        130        140        150
IWISQPVENI YSVINYSGVN NTAYHGYWAR DFKKTNPAYG TMQDFKNLID 
       160        170        180        190        200
TAHAHNIKVI IDFAPNHTSP ASSDDPSFAE NGRLYDNGNL LGGYTNDTQN 
       210        220        230        240        250
LFHHYGGTDF STIENGIYKN LYDLADLNHN NSSVDVYLKD AIKMWLDLGV 
       260        270        280        290        300
DGIRVDAVKH MPFGWQKSFM ATINNYKPVF TFGEWFLGVN EISPEYHQFA 
       310        320        330        340        350
NESGMSLLDF RFAQKARQVF RDNTDNMYGL KAMLEGSEVD YAQVNDQVTF 
       360        370        380        390        400
IDNHDMERFH TSNGDRRKLE QALAFTLTSR GVPAIYYGSE QYMSGGNDPD 
       410        420        430        440        450
NRARLPSFST TTTAYQVIQK LAPLRKSNPA IAYGSTHERW INNDVIIYER 
       460        470        480        490        500
KFGNNVAVVA INRNMNTPAS ITGLVTSLRR ASYNDVLGGI LNGNTLTVGA 
       510        520        530        540        550
GGAASNFTLA PGGTAVWQYT TDATTPIIGN VGPMMAKPGV TITIDGRGFG 
       560        570        580        590        600
SGKGTVYFGT TAVTGADIVA WEDTQIQVKI PAVPGGIYDI RVANAAGAAS 
       610        620        630        640        650
NIYDNFEVLT GDQVTVRFVI NNATTALGQN VFLTGNVSEL GNWDPNNAIG 
       660        670        680        690        700
PMYNQVVYQY PTWYYDVSVP AGQTIEFKFL KKQGSTVTWE GGANRTFTTP 
       710 
TSGTATVNVN WQP

Length:713

Mass (Da):78,340

Last modified:November 1, 1988 - v1

Checksum:ⁱ524B259526B56C52

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M17366 Genomic DNA Translation: AAA22308.1
PIRⁱ	A26678 ALBSG1

Protein	Similar proteins		Species	Score	Length	Source
P05618	Cyclomaltodextrin glucanotransferase		BACS3		712	UniRef90_P05618
Cyclodextrin glucanotransferase		Paenibacillus sp. JB-13		713
Cyclodextrin glucanotransferase		BACCI		713
Beta-cyclodextrin glycosyltransferase		Bacillus sp. N-227		713
Beta-cyclodextrin glycosyltransferase		Paenibacillus sp. xw-6-66		713
+9

Protein	Similar proteins		Species	Score	Length	Source
P05618	Cyclomaltodextrin glucanotransferase	)	BACCI		713	UniRef50_P43379
Cyclomaltodextrin glucanotransferase		BAC11		713
Cyclomaltodextrin glucanotransferase		BACS8		713
Cyclomaltodextrin glucanotransferase		BACSS		718
Cyclomaltodextrin glucanotransferase		BACLI		718
+361

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M17366 Genomic DNA Translation: AAA22308.1
PIRⁱ	A26678 ALBSG1

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
	1D7F	X-ray	1.90	A/B	28-713	[»]
	1DED	X-ray	2.00	A/B	28-713	[»]
	1I75	X-ray	2.00	A/B	28-713	[»]
	1PAM	X-ray	1.80	A/B	28-713	[»]
	1UKQ	X-ray	2.00	A/B	28-713	[»]
	1UKS	X-ray	1.90	A/B	28-713	[»]
	1UKT	X-ray	2.20	A/B	28-713	[»]
	1V3J	X-ray	2.00	A/B	28-713	[»]
	1V3K	X-ray	2.00	A/B	28-713	[»]
	1V3L	X-ray	2.10	A/B	28-713	[»]
	1V3M	X-ray	2.00	A/B	28-713	[»]
ProteinModelPortalⁱ	P05618
SMRⁱ	P05618
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Chemistry databases

DrugBankⁱ	DB02379 Beta-D-Glucose DB03206 Duvoglustat

DrugBankⁱ

DB02379 Beta-D-Glucose
DB03206 Duvoglustat

Protein family/group databases

CAZyⁱ	CBM20 Carbohydrate-Binding Module Family 20 GH13 Glycoside Hydrolase Family 13

CAZyⁱ

CBM20 Carbohydrate-Binding Module Family 20
GH13 Glycoside Hydrolase Family 13

Proteomic databases

PRIDEⁱ	P05618

PRIDEⁱ

P05618

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Enzyme and pathway databases

BRENDAⁱ	2.4.1.19 691

BRENDAⁱ

2.4.1.19 691

Miscellaneous databases

EvolutionaryTraceⁱ	P05618

EvolutionaryTraceⁱ

P05618

Family and domain databases

Gene3Dⁱ	2.60.40.10, 2 hits 2.60.40.1180, 1 hit
InterProⁱ	View protein in InterPro IPR006048 A-amylase/branching_C IPR031319 A-amylase_C IPR006046 Alpha_amylase IPR013784 Carb-bd-like_fold IPR002044 CBM_fam20 IPR006047 Glyco_hydro_13_cat_dom IPR013780 Glyco_hydro_b IPR017853 Glycoside_hydrolase_SF IPR013783 Ig-like_fold IPR014756 Ig_E-set IPR002909 IPT_dom
Pfamⁱ	View protein in Pfam PF00128 Alpha-amylase, 1 hit PF02806 Alpha-amylase_C, 1 hit PF00686 CBM_20, 1 hit PF01833 TIG, 1 hit
PRINTSⁱ	PR00110 ALPHAAMYLASE
SMARTⁱ	View protein in SMART SM00642 Aamy, 1 hit SM00632 Aamy_C, 1 hit SM01065 CBM_2, 1 hit
SUPFAMⁱ	SSF49452 SSF49452, 1 hit SSF51445 SSF51445, 1 hit SSF81296 SSF81296, 1 hit
PROSITEⁱ	View protein in PROSITE PS51166 CBM20, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	CDGT_BACS0
Accessionⁱ	P05618Primary (citable) accession number: P05618
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
	Last sequence update:	November 1, 1988
	Last modified:	May 23, 2018
	This is version 127 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

Documents

SIMILARITY comments
Index of protein domains and families
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
Glycosyl hydrolases
Classification of glycosyl hydrolase families and list of entries

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P05618 (CDGT_BACS0)

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Cyclomaltodextrin glucanotransferase

cgt

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

Sites

<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

Protein family/group 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

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

<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 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

Domains and Repeats

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

Keywords - Domaini

Family and domain databases

Sequence 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

Chemistry databases

Protein family/group databases

Proteomic databases

Protocols and materials 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

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ