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Entry version 17 (02 Dec 2020)
Sequence version 1 (13 Apr 2016)
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Protein

Highly reducing polyketide synthase cla2

Gene

cla2

Organism
Cladosporium cladosporioides
Status
Reviewed-Annotation score:

Annotation score:3 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

Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of cladosporin, a tricyclic octaketide that acts as an antimalarial agent though inhibition of the Plasmodium falciparum lysyl-tRNA synthetase (PubMed:26783060). The highly reducing polyketide synthase cla2 is responsible for biosynthesis up to the pentaketide stage, including of the tetrahydropyran (THP) ring, whereas the three subsequent ketide extensions with no reduction are catalyzed by the non-reducing polyketide synthase cla3 (PubMed:26783060).1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: Secondary metabolite biosynthesis

This protein is involved in Secondary metabolite biosynthesis.1 Publication
View all proteins of this organism that are known to be involved in Secondary metabolite biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 sitei182PROSITE-ProRule annotation1
Active sitei182For beta-ketoacyl synthase activityPROSITE-ProRule annotation1
Active sitei638For malonyltransferase activityPROSITE-ProRule annotation1
Active sitei968For beta-hydroxyacyl dehydratase activityPROSITE-ProRule annotation1

<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

<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 functionMultifunctional enzyme, Transferase

<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:
Highly reducing polyketide synthase cla21 Publication (EC:2.3.1.-1 Publication)
Alternative name(s):
Cladosporin biosynthesis cluster protein 21 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:cla21 Publication
<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>OrganismiCladosporium cladosporioides
<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 identifieri29917 [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 lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaDothideomycetesDothideomycetidaeCladosporialesCladosporiaceaeCladosporium

<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 use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei

Cladosporin has been intensely studied for its antimalarial activity though inhibition of the Plasmodium falciparum lysyl-tRNA synthetase (PubMed:22704625, PubMed:24935905, PubMed:26074468). Cladosporin has also antifungal activity against dermatophytes, as well as Penicillium and Aspergillus species (PubMed:5169000).4 Publications

<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_00004370511 – 2368Highly reducing polyketide synthase cla2Add BLAST2368

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2320O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

<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
A0A0Y0M151

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 <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>Domaini2283 – 2360CarrierPROSITE-ProRule annotationAdd BLAST78

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni13 – 437Ketosynthase (KS) domainSequence analysisAdd BLAST425
Regioni548 – 877Malonyl-CoA:ACP transacylase (MAT) domainSequence analysisAdd BLAST330
Regioni936 – 1175Dehydratase (DH) domainSequence analysisAdd BLAST240
Regioni1655 – 1967Enoylreductase (ER) domainSequence analysisAdd BLAST313
Regioni1991 – 2170Catalytic ketoreductase (KRc) domainSequence analysisAdd BLAST180

<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

Multidomain protein; including a starter unit:ACP transacylase (SAT) that selects the starter unit; a ketosynthase (KS) that catalyzes repeated decarboxylative condensation to elongate the polyketide backbone; a malonyl-CoA:ACP transacylase (MAT) that selects and transfers the extender unit malonyl-CoA; a product template (PT) domain that controls the immediate cyclization regioselectivity of the reactive polyketide backbone; and an acyl-carrier protein (ACP) that serves as the tether of the growing and completed polyketide via its phosphopantetheinyl arm (By similarity).By similarity

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.1200.10, 1 hit
3.10.129.110, 1 hit
3.40.366.10, 1 hit
3.40.47.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001227, Ac_transferase_dom_sf
IPR036736, ACP-like_sf
IPR014043, Acyl_transferase
IPR016035, Acyl_Trfase/lysoPLipase
IPR013154, ADH_N
IPR011032, GroES-like_sf
IPR014031, Ketoacyl_synth_C
IPR014030, Ketoacyl_synth_N
IPR016036, Malonyl_transacylase_ACP-bd
IPR036291, NAD(P)-bd_dom_sf
IPR032821, PKS_assoc
IPR020841, PKS_Beta-ketoAc_synthase_dom
IPR020807, PKS_dehydratase
IPR042104, PKS_dehydratase_sf
IPR020843, PKS_ER
IPR013968, PKS_KR
IPR020806, PKS_PP-bd
IPR009081, PP-bd_ACP
IPR006162, Ppantetheine_attach_site
IPR002364, Quin_OxRdtase/zeta-crystal_CS
IPR016039, Thiolase-like

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00698, Acyl_transf_1, 1 hit
PF08240, ADH_N, 1 hit
PF16197, KAsynt_C_assoc, 1 hit
PF00109, ketoacyl-synt, 1 hit
PF02801, Ketoacyl-synt_C, 1 hit
PF08659, KR, 1 hit
PF00550, PP-binding, 1 hit
PF14765, PS-DH, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00827, PKS_AT, 1 hit
SM00826, PKS_DH, 1 hit
SM00829, PKS_ER, 1 hit
SM00825, PKS_KS, 1 hit
SM00823, PKS_PP, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF47336, SSF47336, 1 hit
SSF50129, SSF50129, 1 hit
SSF51735, SSF51735, 2 hits
SSF52151, SSF52151, 1 hit
SSF53901, SSF53901, 1 hit
SSF55048, SSF55048, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50075, CARRIER, 1 hit
PS00012, PHOSPHOPANTETHEINE, 1 hit
PS01162, QOR_ZETA_CRYSTAL, 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.

A0A0Y0M151-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTSSGDSSPQ IPIAIVGLGC RFPGDADSPK KFWDILKEGR DAYSPRTDRW
60 70 80 90 100
NPDAFYHPNK DRANTQPTKG GHFLKQDPYV FDPSFFNITA TEAIALDPKQ
110 120 130 140 150
RLALEVAYEA LENAGFPLQK VAGSQTACYM GSAMADYRDS ISRDFGHAPK
160 170 180 190 200
YFVLGTCEEM ISNRISHFFD MHGPSATVHT ACSSSLVATH VACQSLRSGE
210 220 230 240 250
ADMALAGGVG IMLTPDSSLQ LNNMSFLNPE GHSRSFDADA GGYARGEGCG
260 270 280 290 300
ILVMKRLDDA VRDGDNIRAV IRGSGVNSDG WTQGVTMPSP EAQAALIKQV
310 320 330 340 350
FGKNKLDYDT IQYVEAHGTG TKAGDPVETK AIYDTIGRGI NKSRKLWIGS
360 370 380 390 400
VKPNIGHLEA AAGVAGIIKG VLSLENSAIP PNIYFSKPNP AIKLDEWNMA
410 420 430 440 450
VPTKLVNWPV AQTKRMTVSG FGMGGTNGLV VLEAYVPERL LNGATKVTTA
460 470 480 490 500
KDTAHSGKRL FVCSSQDQAG FKRIGEAFVD HLDNLGPIAS SSGYLANLAH
510 520 530 540 550
TLSTARAGLS WRTTFVADSK AELREHLTTT LGQDATRVSD TQAQRIGFVF
560 570 580 590 600
TGQGAQWAGM GVEMLERPVF GASVAESAKL LRSFGCTWDP ATELQKAAKE
610 620 630 640 650
SRLAVPEISQ PICTIIQIAL VDELKSWGVS PAKVVGHSSG EIAAAYTIGA
660 670 680 690 700
LSHRDAMAVA YFRGMASTAL KTSAPHLEGG MMAVGTSAEA AQTIIAETKN
710 720 730 740 750
SISGDITIAC VNSPSSVTLS GDAKALEELR KILDARSVFA RRLKVDVAYH
760 770 780 790 800
SSHMNVAAPE YQQSIADIEP RLCSDEVEEG SLPVMVSSVT TEQVSPELLG
810 820 830 840 850
TYYWIRNLVS PVQFSDALRE LVAPGGSDKN DVDLLIEIGP HSALGGPIEQ
860 870 880 890 900
ILSFHNVQKV DYKSVLTRGQ NALDTSLSLA SDLFVRGIQL DMEKVNGDSD
910 920 930 940 950
CHLLNDLPSY PWNHSKAFRA DSRIQRELLQ SKHPRHSMIG LKQPMLDESQ
960 970 980 990 1000
HVWRNYVRLT DEPWLRGHVV GGTALVPGAG MLSMIFEAVQ QLVDPGKPAH
1010 1020 1030 1040 1050
SLRVRDVKFS AALTLPEDTS IEVVTTLRPH LVSTSGSTPA SWWEFTISSC
1060 1070 1080 1090 1100
PGTDQIQDNC RGLVAIEYTN KRSEQMIYED VNEENSRIAD FHRVRDESPL
1110 1120 1130 1140 1150
MIRREKFYEH MQKSGYNYGE TFQGMETVHL GDGETAFHVK LIDIGETFSK
1160 1170 1180 1190 1200
GQLDRPFLIP GSSLDAIFQS IFGSTFKNGA FEVEKPNFLA YIGELEISLD
1210 1220 1230 1240 1250
IPGEVGYVMP GVCFSRKHGF NQQSADIFTF DKSLSRMHLA VRDFRMTEPE
1260 1270 1280 1290 1300
VGDDASDGFE PWAFTSAPHW NYAFSLLKTE ELRSVLSKVT TQDAPVELLR
1310 1320 1330 1340 1350
TILHENPSAS VLELIPEIGD LAIASSYQLP KGAIQPSQLR YAVAKDIPDS
1360 1370 1380 1390 1400
FIDENLVGEV FALDGVGEDD RKISADVLIV PSSLDLLEDR DAILARFLKL
1410 1420 1430 1440 1450
AGPAALMITA SGLHSARSVF EAHGFQAFPG LNGIASLPGL YSHAEEPSLR
1460 1470 1480 1490 1500
QTNRGTRDTS DTDITILEPS SPSFNTTEFS KTLSSRLEDQ NYSVTIRKWA
1510 1520 1530 1540 1550
GGETEEFQNT TYISLLELEQ PFLDNLSDPD FQGIKNLVLG SNRLIWLTLG
1560 1570 1580 1590 1600
DDPSFGAVDG LSRVMRSELG TPKFQVMHLS GEAGLLSGPE LTVRVLKSPT
1610 1620 1630 1640 1650
EDTEFRERDG LLQVIRIFES PDVNQSLRGH LENSTRILPI KQLDYPVRLT
1660 1670 1680 1690 1700
VGKPGFLDSL QFIKDRRTEA PLPENEIEID VHASGVNFRD VMASMGLIST
1710 1720 1730 1740 1750
PILGFEASGV VTKCGSQVSQ FRTGARVSFV GEHTHSTRIR ADPRLVAPIP
1760 1770 1780 1790 1800
DDVSFEEAAS LPIVGATAYH TLTNLARLRK GQTILIHAAA GGVGQAMIQL
1810 1820 1830 1840 1850
ASHFGLVIYA TVGTEDKRKL LGEKYNIPPE NILNSRDASF AKGIKRLTGG
1860 1870 1880 1890 1900
RGVDCVINSL SGELLRASWG CVAPFGIFIE LGLRDITDNM RLDMRPFSNV
1910 1920 1930 1940 1950
TSFTFCNILA LMQQDPDAMG LVLKETFKLV SQGILTSPFP TTVFPVEQTQ
1960 1970 1980 1990 2000
EAFRLMQQGK HRGKLVLSFA GDPQAPVHCE AKESLRLDGN ATYLIIGGLG
2010 2020 2030 2040 2050
GLGRSMALEL VASGARHLAF ISRSGDSTPQ AKATLAELEQ RNLDFRVYRG
2060 2070 2080 2090 2100
DVSNEESFLD AMKLCSSDLP PIKGVIQMAM VLKDIIFEKM THEQWTIPLR
2110 2120 2130 2140 2150
PKIQGTWNIH QYFDESRPLD FMVFCSSTSG IHGYPSQSQY AAGNTYQDTL
2160 2170 2180 2190 2200
AAYRRAHGLK AVAVNLTIIR EVGILAEQGT TGNIAVWEEA LGIKEPAFHA
2210 2220 2230 2240 2250
LMKTLIAGQQ GPAGSEFLPP QVSTGLGTAD IMSSYNLALP DYFQDPRFGP
2260 2270 2280 2290 2300
LAVSTFSTNV AGESQSAAVS LSSKLIEATN VDQASEIITE GLVTKVADML
2310 2320 2330 2340 2350
QIPVSEVDAS RPMYRYGVDS LVALEVRNWI VKEMKATIAL LEILAAVPMN
2360
VLAKTIASRS KHLAATLD
Length:2,368
Mass (Da):257,782
Last modified:April 13, 2016 - 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:i78CFB5EDCD2BC244
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
KT037691 mRNA Translation: AMB51799.1

<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
KT037691 mRNA Translation: AMB51799.1

3D structure databases

SMRiA0A0Y0M151
ModBaseiSearch...

Family and domain databases

Gene3Di1.10.1200.10, 1 hit
3.10.129.110, 1 hit
3.40.366.10, 1 hit
3.40.47.10, 1 hit
InterProiView protein in InterPro
IPR001227, Ac_transferase_dom_sf
IPR036736, ACP-like_sf
IPR014043, Acyl_transferase
IPR016035, Acyl_Trfase/lysoPLipase
IPR013154, ADH_N
IPR011032, GroES-like_sf
IPR014031, Ketoacyl_synth_C
IPR014030, Ketoacyl_synth_N
IPR016036, Malonyl_transacylase_ACP-bd
IPR036291, NAD(P)-bd_dom_sf
IPR032821, PKS_assoc
IPR020841, PKS_Beta-ketoAc_synthase_dom
IPR020807, PKS_dehydratase
IPR042104, PKS_dehydratase_sf
IPR020843, PKS_ER
IPR013968, PKS_KR
IPR020806, PKS_PP-bd
IPR009081, PP-bd_ACP
IPR006162, Ppantetheine_attach_site
IPR002364, Quin_OxRdtase/zeta-crystal_CS
IPR016039, Thiolase-like
PfamiView protein in Pfam
PF00698, Acyl_transf_1, 1 hit
PF08240, ADH_N, 1 hit
PF16197, KAsynt_C_assoc, 1 hit
PF00109, ketoacyl-synt, 1 hit
PF02801, Ketoacyl-synt_C, 1 hit
PF08659, KR, 1 hit
PF00550, PP-binding, 1 hit
PF14765, PS-DH, 1 hit
SMARTiView protein in SMART
SM00827, PKS_AT, 1 hit
SM00826, PKS_DH, 1 hit
SM00829, PKS_ER, 1 hit
SM00825, PKS_KS, 1 hit
SM00823, PKS_PP, 1 hit
SUPFAMiSSF47336, SSF47336, 1 hit
SSF50129, SSF50129, 1 hit
SSF51735, SSF51735, 2 hits
SSF52151, SSF52151, 1 hit
SSF53901, SSF53901, 1 hit
SSF55048, SSF55048, 1 hit
PROSITEiView protein in PROSITE
PS50075, CARRIER, 1 hit
PS00012, PHOSPHOPANTETHEINE, 1 hit
PS01162, QOR_ZETA_CRYSTAL, 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 nameiCLA2_CLACD
<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: A0A0Y0M151
<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 7, 2016
Last sequence update: April 13, 2016
Last modified: December 2, 2020
This is version 17 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 programFungal Protein Annotation Program

<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

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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