Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 91 (02 Jun 2021)
Sequence version 1 (11 Oct 2005)
Previous versions | rss
Add a publicationFeedback
Protein

Lovastatin nonaketide synthase mokA

Gene

mokA

Organism
Monascus pilosus (Red mold)
Status
Reviewed-Annotation score:

Annotation score:4 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

Nonaketide synthase; part of the gene cluster that mediates the biosynthesis of monakolin K, also known as lovastatin, and which acts as a potent competitive inhibitor of HMG-CoA reductase (PubMed:18578535).

Monakolin K biosynthesis is performed in two stages (PubMed:19693441).

The first stage is catalyzed by the nonaketide synthase mokA, which belongs to type I polyketide synthases and catalyzes the iterative nine-step formation of the polyketide (PubMed:18578535, PubMed:19693441).

This PKS stage is completed by the action of dehydrogenase mokE, which catalyzes the NADPH-dependent reduction of the unsaturated tetra-, penta- and heptaketide intermediates that arise during the mokA-mediated biosynthesis of the nonaketide chain and leads to dihydromonacolin L (PubMed:19693441).

Covalently bound dihydromonacolin L is released from mokA by the mokD esterase (By similarity).

Conversion of dihydromonacolin L into monacolin L and then monacolin J is subsequently performed with the participation of molecular oxygen and P450 monoogygenase mokC (PubMed:19693441).

Finally, mokF performs the conversion of monacoline J to monacoline K through the addition of the side-chain diketide moiety (2R)-2-methylbutanoate produced by the diketide synthase mokB (PubMed:19693441).

1 PublicationBy similarity1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

pantetheine 4'-phosphateBy similarityNote: Binds 1 phosphopantetheine covalently.By similarity

<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: lovastatin biosynthesis

This protein is involved in the pathway lovastatin biosynthesis, which is part of Polyketide biosynthesis.1 Publication
View all proteins of this organism that are known to be involved in the pathway lovastatin biosynthesis and in Polyketide 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 sitei222For beta-ketoacyl synthase activityPROSITE-ProRule annotation1
Active sitei697For malonyltransferase activityPROSITE-ProRule annotation1
Active sitei1029For 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

GO - Biological processi

<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 functionAcyltransferase, Methyltransferase, Multifunctional enzyme, Oxidoreductase, Transferase
LigandNADP, S-adenosyl-L-methionine

Enzyme and pathway databases

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00875

<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:
Lovastatin nonaketide synthase mokA1 Publication (EC:2.3.1.161By similarity)
Alternative name(s):
Monacolin K biosynthesis protein A1 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:mokA1 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>OrganismiMonascus pilosus (Red mold)
<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 identifieri89488 [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 lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeMonascus

<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

Monacoline K acts as an inhibitor of HMG-CoA reductase involved in cholesterogenesis (PubMed:21821946). Its hypocholesterolemic activity might be useful for lowering cholesterol levels in the blood and reduce artherosclerosis and coronary heart disease (PubMed:21821946).1 Publication

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Impairs the production of monacoline K (PubMed:18578535).1 Publication

<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_00004362791 – 3075Lovastatin nonaketide synthase mokAAdd BLAST3075

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 residuei2531O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
Q3S2T9

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Expression is controlled by the monacolin K cluster transcription regulator mokH (PubMed:19968298).1 Publication

<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

13075
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q3S2T9

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
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>Domaini2492 – 2571CarrierPROSITE-ProRule annotationAdd BLAST80

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>Regioni42 – 490Beta-ketoacyl synthaseBy similarityAdd BLAST449
Regioni603 – 945Acyl and malonyl transferaseBy similarityAdd BLAST343
Regioni1029 – 1041Dehydratase-likeBy similarityAdd BLAST13
Regioni1556 – 1594MethyltransferaseBy similarityAdd BLAST39
Regioni2176 – 2470Beta-ketoacyl reductaseBy similarityAdd BLAST295
Regioni2582 – 2624DisorderedSequence analysisAdd BLAST43
Regioni2633 – 2989Peptide synthetase elongationBy similarityAdd BLAST357

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi2586 – 2610Polar residuesSequence analysisAdd BLAST25

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.10.129.110, 1 hit
3.30.559.10, 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
IPR023213, CAT-like_dom_sf
IPR001242, Condensatn
IPR018201, Ketoacyl_synth_AS
IPR014031, Ketoacyl_synth_C
IPR014030, Ketoacyl_synth_N
IPR016036, Malonyl_transacylase_ACP-bd
IPR013217, Methyltransf_12
IPR036291, NAD(P)-bd_dom_sf
IPR032821, PKS_assoc
IPR020841, PKS_Beta-ketoAc_synthase_dom
IPR020807, PKS_dehydratase
IPR042104, PKS_dehydratase_sf
IPR013968, PKS_KR
IPR020806, PKS_PP-bd
IPR009081, PP-bd_ACP
IPR029063, SAM-dependent_MTases
IPR016039, Thiolase-like

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00698, Acyl_transf_1, 1 hit
PF00668, Condensation, 1 hit
PF16197, KAsynt_C_assoc, 1 hit
PF00109, ketoacyl-synt, 1 hit
PF02801, Ketoacyl-synt_C, 1 hit
PF08659, KR, 1 hit
PF08242, Methyltransf_12, 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
SM00825, PKS_KS, 1 hit
SM00823, PKS_PP, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF47336, SSF47336, 1 hit
SSF51735, SSF51735, 2 hits
SSF52151, SSF52151, 1 hit
SSF53335, SSF53335, 1 hit
SSF53901, SSF53901, 1 hit
SSF55048, SSF55048, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00606, B_KETOACYL_SYNTHASE, 1 hit
PS50075, CARRIER, 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.

Q3S2T9-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MYVGRIGATT YISRPADSRA TPKVIKTQGS ITTSNLTSLT TMAQSTYPNE
60 70 80 90 100
PIVVVGSGCR FPGGANTPSK LWELLREPRD VRSKIPKERF DVDAFYHPDG
110 120 130 140 150
KHHGRTNAPY AYMLQEDLRA FDGPFFNIQA GEAESMDPQQ RLLLETVYEA
160 170 180 190 200
VSDAGMRIQD LQGSSTAVYV GMMTHDYETV STRDLESIPT YSATGVAVSV
210 220 230 240 250
ASNRISYFFD WHGPSMTIDT ACSSSLVAVH LAVQQLRSGQ SSMAIAAGAN
260 270 280 290 300
MILGPMTFVL ESKLNMLSPS GRSRMWDAGA DGYARGEAVC SVVLKTLSQA
310 320 330 340 350
LRDGDSIECV IRETGVNQDG RTTGITMPNH SAQEALIRAT YSKAGLDITN
360 370 380 390 400
PEDRCQFFEA HGTGTPAGDP QEAEAIATAF FGHKKEASDA ENAETPLFVG
410 420 430 440 450
SVKTVVGHTE GTAGLAGLMK ASFAVQHGVI PPNLLFENIS PRVAPFYSNL
460 470 480 490 500
KIATETTPWP TIKPGQPRRV SVNSFGFGGT NAHAIIEEYI KSDQKVPASR
510 520 530 540 550
QPVEYSDSPS TLNLPLVLSA KSQRSMKTTL ESMVQFLQSN PEVNLRDLSW
560 570 580 590 600
TLLRKRSILP FRRAIVGHSH EAIRAALEAA IEDGIVVSDF SADVKGKPSV
610 620 630 640 650
LGVFTGQGAQ WPGMLKELIV GSSYVRSIAE ELDHSLQTLP EKYRPSWTIL
660 670 680 690 700
EQLMLEDEAS NVRHASFSQP LCCAVQIVLV RLLKAAGIQF AAVVGHSSGE
710 720 730 740 750
IACAFATGLI SASLAIRIAH LRGVVSAEHA ASASGGRGSM LAAGMSYEEA
760 770 780 790 800
KELCELDAFE SRICVAASNS PDSVTFSGDA DAIEHLQGVL EDEATFARLL
810 820 830 840 850
RVDTAYHSHH MLPCAAPYMQ ALEECGCAVA DGDGQVEEGS WYSSVKDSNE
860 870 880 890 900
PMGLADVTAE YWKDNLVSPV LFSQAVQRAA IMHRPLDVGI EVGCHPALKG
910 920 930 940 950
PCLATIKDAL SDVDLAYTGC LERGKNDMNA FSQALAYLWE QFGIPSLDAD
960 970 980 990 1000
RFISTIAPER SCVSLSKQLP TYSWDHSRSY WTESRATRQH LRGPKPHLLL
1010 1020 1030 1040 1050
GKLSEYSTPL TFQWLNFVRP RDIEWLDGHA LQGQVVFPAA GYIVMAMEAA
1060 1070 1080 1090 1100
MEIANSHQVQ VQLLEILDMS IDKAVVFDDE DSLVELNLTA EVTSGIGKGD
1110 1120 1130 1140 1150
RMILSFIIDS CLSREGDLST SAKGQLVVTL DEGHLQVTPD NEKQLLPPPE
1160 1170 1180 1190 1200
EEHPHMNRVN INSFYHELDL MGYDYSKDFR RLHSMRRADA RASGILEFIP
1210 1220 1230 1240 1250
LNDEVHGRPL LLHPAPLDIA FQTVIGAYSS PGDRRLRCLY VPTHIDRIAL
1260 1270 1280 1290 1300
VPSLCLATAA SGCDKIAFNT INTYDKGDFL SGDIVAFDAE QTSLFHVENI
1310 1320 1330 1340 1350
VFKPFSPPTA STDHPIFAKW SWGPLTPETL LDNPNHWATA QDKEAIPIIE
1360 1370 1380 1390 1400
RIVYFYIKLF LQQLTREDRE QAAFHLQRQI VWCEQVVADA HEGRHQWYDA
1410 1420 1430 1440 1450
AWENDTEAQI EQLCARSSYH PHVRLVQRVG QNLLATIRSN GNPFDLMDHD
1460 1470 1480 1490 1500
GLLTEFYTNT LSFGPALHYA QDLVGQIAHR YQSMDILEIG AGTGGATKYV
1510 1520 1530 1540 1550
LATPQLGFNS YTYTDISTGF FEKAREQFAA FEDRMEFEPL DIRRSPAEQG
1560 1570 1580 1590 1600
FTEHVYDLII ASNVLHATPD LEKTMAHARS LLKPGGQMVI LEITHRNHTR
1610 1620 1630 1640 1650
LGFIFGLFAD WWAGIDDGRT MEPFVSFDRW DEILKHVGFS GIDSRTKDRD
1660 1670 1680 1690 1700
ADLFPTSVFS THAVNSTIDY LHKPLDAPVK DSYPPLVVVG GQTPKTQRIL
1710 1720 1730 1740 1750
DEIKAVMPNR QIQLHQRLVD LLDAEDMQAK FTFVVLTELD EELFAGLTED
1760 1770 1780 1790 1800
SFEAVKLLLM YAGNMLWLTE NAWVKRPHQA STIGMLRSIR REHPDIGVHI
1810 1820 1830 1840 1850
MDVDSAENLD AHFLVEQVLR LEEDIDELAA TTTWTQEPEV FWCNGRAWIP
1860 1870 1880 1890 1900
RLKHDKSRNN RMNSSRRQIF ETLNPSKIPV ALKKAAASSS YYLESAETWP
1910 1920 1930 1940 1950
VPGAVTAGDR KTVHVRLSHP HALRVGHLGF FYLVQGHVLK GDQALPVVAL
1960 1970 1980 1990 2000
AERNASIVHV RSDYVHVLED TAVSANNGSF ILAAAAAVLA ETVIHSAKSL
2010 2020 2030 2040 2050
GADASVLVLN APGFCAQTLL RAARDSGLRV HLATTSSSTD PSPGADRCVR
2060 2070 2080 2090 2100
LHPRDTDRRL KQLLPRGTQA FFDLSTDPSS EGLTQRLPNV LIPSCVRHST
2110 2120 2130 2140 2150
EYLLRDTASA GGKATLPAAY WERVASLANH SLSTHFKEND NASNGCQVLS
2160 2170 2180 2190 2200
CTDIVARNNK SRLNASTVIS WPDDAALPAR IRPIDTETLF AAEKTYLLVG
2210 2220 2230 2240 2250
LTGDLGRSLG RWMVLHGARR IVLTSRNPQV SPNWVAHVEE LGGQVTVLSM
2260 2270 2280 2290 2300
DVTSEDSVDS GLAKLQDLKL PPIGGIAFGP LVLQDVMLKN MDLQMMEMVL
2310 2320 2330 2340 2350
KPKVEGARIL HEKFSDPASS NPLDFFVMFS SIVAVMGNPG QANYSAANCY
2360 2370 2380 2390 2400
LQALAQRRCA SGLAASTIDI GAVYGVGFVT RAELEEDFNA IRFMFDSVEE
2410 2420 2430 2440 2450
HELHSLFAEA VVSGRRAMHQ QQQFKTVLDM ADIELTTGIP PLDPTLKDRI
2460 2470 2480 2490 2500
TFFDDARVGN FKIPERRGKA GDNAAGSKGS VKEQLLQATS LDQVRQIVID
2510 2520 2530 2540 2550
GLSEKLRVTL QIPDGESVHP TIPLIDQGVD SLGAVTVGTW FSKQLYLDLP
2560 2570 2580 2590 2600
LLRVLGGASV ADLADDAAAR LPPSSIPLVA ASEGGAETSD NDTSGPEGTD
2610 2620 2630 2640 2650
LSASTTITEP SSADEEDEKQ EDDNDNSVLA LHPLSLGQEY AWRLQKAADD
2660 2670 2680 2690 2700
STIFNNTIGM FMTGSIDAKR LSKALRAVLR RHEIFRTGFA AVGNNADATS
2710 2720 2730 2740 2750
LAQIVFGRTK NKVQVIQVAD RAGAEEGYRQ LVQTQYDITA GDTLRLVDFF
2760 2770 2780 2790 2800
WGKDEHLFVV AYHRFVGDGS TTENIFVEAS QLYGGVTLDK HVPQFADLAT
2810 2820 2830 2840 2850
RQREALESGQ MDADLAYWES MHHQPTGVVS PVLPRMLLGE DGLNSPNHAR
2860 2870 2880 2890 2900
QPNSWKQHEA IARLDPMVAF RIRERSRKHK ATPMQFYLAA YHVLLARLTG
2910 2920 2930 2940 2950
SSDFSIGLAD TNRTNVDELA GMGFFANLLP LRFRNFVPHI TFGEHLVATK
2960 2970 2980 2990 3000
DKVREAMQHA RVPYGVLLER LGFEVPGATA ETAEPAPLFQ AVFDYKQGQA
3010 3020 3030 3040 3050
ESGSIGSAKM TEVIATRERT PYDVVLEMSD DPTKDPLLTV KLQSSVYEVH
3060 3070
HPRAFLESYI SILSMFSMNP ALKLA
Length:3,075
Mass (Da):338,037
Last modified:October 11, 2005 - 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:i6BDE751D492E9813
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
DQ176595 Genomic DNA Translation: ABA02239.1

<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
DQ176595 Genomic DNA Translation: ABA02239.1

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 entryMethodResolution (Å)ChainPositionsPDBsum
6AD3X-ray1.79A2578-3075[»]
SMRiQ3S2T9
ModBaseiSearch...
PDBe-KBiSearch...

Proteomic databases

PRIDEiQ3S2T9

Enzyme and pathway databases

UniPathwayiUPA00875

Family and domain databases

Gene3Di3.10.129.110, 1 hit
3.30.559.10, 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
IPR023213, CAT-like_dom_sf
IPR001242, Condensatn
IPR018201, Ketoacyl_synth_AS
IPR014031, Ketoacyl_synth_C
IPR014030, Ketoacyl_synth_N
IPR016036, Malonyl_transacylase_ACP-bd
IPR013217, Methyltransf_12
IPR036291, NAD(P)-bd_dom_sf
IPR032821, PKS_assoc
IPR020841, PKS_Beta-ketoAc_synthase_dom
IPR020807, PKS_dehydratase
IPR042104, PKS_dehydratase_sf
IPR013968, PKS_KR
IPR020806, PKS_PP-bd
IPR009081, PP-bd_ACP
IPR029063, SAM-dependent_MTases
IPR016039, Thiolase-like
PfamiView protein in Pfam
PF00698, Acyl_transf_1, 1 hit
PF00668, Condensation, 1 hit
PF16197, KAsynt_C_assoc, 1 hit
PF00109, ketoacyl-synt, 1 hit
PF02801, Ketoacyl-synt_C, 1 hit
PF08659, KR, 1 hit
PF08242, Methyltransf_12, 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
SM00825, PKS_KS, 1 hit
SM00823, PKS_PP, 1 hit
SUPFAMiSSF47336, SSF47336, 1 hit
SSF51735, SSF51735, 2 hits
SSF52151, SSF52151, 1 hit
SSF53335, SSF53335, 1 hit
SSF53901, SSF53901, 1 hit
SSF55048, SSF55048, 1 hit
PROSITEiView protein in PROSITE
PS00606, B_KETOACYL_SYNTHASE, 1 hit
PS50075, CARRIER, 1 hit

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 nameiMOKA_MONPI
<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: Q3S2T9
<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: May 11, 2016
Last sequence update: October 11, 2005
Last modified: June 2, 2021
This is version 91 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

Keywords - Technical termi

3D-structure

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again