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Entry version 18 (11 Dec 2019)
Sequence version 1 (02 Nov 2016)
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Protein

Highly reducing polyketide synthase sdnO

Gene

sdnO

Organism
Sordaria araneosa (Pleurage araneosa)
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>
-Protein inferred from homologyi <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 sordarin and hypoxysordarin, glycoside antibiotics with a unique tetracyclic diterpene aglycone structure (PubMed:27072286). First, the geranylgeranyl diphosphate synthase sdnC constructs GGDP from farnesyl diphosphate and isopentenyl diphosphate (PubMed:27072286). The diterpene cyclase sdnA then catalyzes the cyclization of GGDP to afford cycloaraneosene (PubMed:27072286). Cycloaraneosene is then hydroxylated four times by the putative cytochrome P450 monooxygenases sdnB, sdnE, sdnF and sdnH to give a hydroxylated cycloaraneosene derivative such as cycloaraneosene-8,9,13,19-tetraol (PubMed:27072286). Although the order of the hydroxylations is unclear, at least C8, C9 and C13 of the cycloaraneosene skeleton are hydroxylated before the sordaricin formation (PubMed:27072286). Dehydration of the 13-hydroxy group of the hydroxylated cycloaraneosene derivative might be catalyzed by an unassigned hypothetical protein such as sdnG and sdnP to construct the cyclopentadiene moiety (PubMed:27072286). The FAD-dependent oxidoreductase sdnN is proposed to catalyze the oxidation at C9 of the hydroxylated cycloaraneosene derivative and also catalyze the Baeyer-Villiger oxidation to give the lactone intermediate (PubMed:27072286). The presumed lactone intermediate would be hydrolyzed to give an acrolein moiety and a carboxylate moiety (PubMed:27072286). Then, [4+2]cycloaddition would occur between the acrolein moiety and the cyclopentadiene moiety to give sordaricin (PubMed:27072286). SdnN might also be involved in the [4+2]cycloaddition after the hypothesized oxidation to accommodate the oxidized product and prompt the [4+2]cycloaddition (PubMed:27072286). GDP-6-deoxy-D-altrose may be biosynthesized from GDP-D-mannose by the putative GDP-mannose-4,6-dehydratase sdnI and the short-chain dehydrogenase sdnK (PubMed:27072286). The glycosyltransferase sdnJ catalyzes the attachment of 6-deoxy-D-altrose onto the 19-hydroxy group of sordaricin to give 4'-O-demethylsordarin (PubMed:27072286). The methyltransferase sdnD would complete the biosynthesis of sordarin (PubMed:27072286). Sordarin can be further modified into hypoxysordarin (PubMed:27072286). The unique acyl chain at the 3'-hydroxy group of hypoxysordarin would be constructed by an iterative type I PKS sdnO and the trans-acting polyketide methyltransferase sdnL. SdnL would be responsible for the introduction of an alpha-methyl group of the polyketide chain (PubMed:27072286). Alternatively, the putative beta-lactamase-like sdnR might be responsible for the cleavage and transfer of the polyketide chain from the PKS sdnO to sordarin (PubMed:27072286). Two putative cytochrome P450 monooxygenases, sdnQ and sdnT, might catalyze the epoxidations of the polyketide chain to complete the biosynthesis of hypoxysordarin (PubMed:27072286). Transcriptional regulators sdnM and sdnS are presumably encoded for the transcriptional regulation of the expression of the sdn gene cluster (PubMed:27072286).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: Antibiotic biosynthesis

This protein is involved in Antibiotic biosynthesis.1 Publication
View all proteins of this organism that are known to be involved in Antibiotic 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 sitei178For beta-ketoacyl synthase activityBy similarity1
Active sitei632For malonyltransferase activityBy similarity1
Active sitei963For beta-hydroxyacyl dehydratase activityBy similarity1

<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 functionMultifunctional enzyme, Oxidoreductase, Transferase
Biological processAntibiotic biosynthesis

<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 sdnO1 Publication (EC:2.3.1.-1 Publication)
Alternative name(s):
Sordarin/hypoxysordarin biosynthesis cluster protein O1 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:sdnO1 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>OrganismiSordaria araneosa (Pleurage araneosa)
<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 identifieri573841 [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 lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeSordaria

<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_00004410651 – 3084Highly reducing polyketide synthase sdnOAdd BLAST3084

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 residuei2400O-(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
A0A1B4XBH3

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>Domaini2363 – 2440CarrierPROSITE-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>Regioni7 – 433Ketosynthase (KS) domainSequence analysisAdd BLAST427
Regioni541 – 841Malonyl-CoA:ACP transacylase (MAT) domainSequence analysis1 PublicationAdd BLAST301
Regioni931 – 1243Dehydratase (DH) domainSequence analysis1 PublicationAdd BLAST313
Regioni1733 – 2045Enoylreductase (ER) domainSequence analysis1 PublicationAdd BLAST313
Regioni2069 – 2252Catalytic ketoreductase (KRc) domainSequence analysis1 PublicationAdd BLAST184
Regioni2864 – 3084Choline/carnitine acyltransferase domainSequence analysis1 PublicationAdd BLAST221

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 amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi860 – 897Ser-richPROSITE-ProRule annotationAdd BLAST38

<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

SdnO consists of a ketosynthase domain, acyltransferase domain, dehydratase domain, unassigned region, enoylreductase domain, beta-ketoreductase domain, acyl carrier protein (ACP) and a choline/carnitine acyltransferase domain (PubMed:27072286). The polyketide chain might be transferred to the 3'-hydroxy group of sordarin by the putative choline/carnitine acyltransferase domain of SdnO because there is no obvious acyltransferase of the polyketide chain in the sdn cluster (PubMed:27072286).1 Publication

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
3.30.559.40, 1 hit
3.30.559.70, 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
IPR039551, Cho/carn_acyl_trans
IPR042232, Cho/carn_acyl_trans_1
IPR042231, Cho/carn_acyl_trans_2
IPR011032, GroES-like_sf
IPR032821, KAsynt_C_assoc
IPR014031, Ketoacyl_synth_C
IPR014030, Ketoacyl_synth_N
IPR016036, Malonyl_transacylase_ACP-bd
IPR036291, NAD(P)-bd_dom_sf
IPR020801, PKS_acyl_transferase
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
IPR016039, Thiolase-like

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00698, Acyl_transf_1, 1 hit
PF00755, Carn_acyltransf, 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

<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.

A0A1B4XBH3-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MASPIPLAVV GIACRFPGDA TNPEKLWDLL AEGKSAWSRV PSDRWNEEAF
60 70 80 90 100
LHPSPDDMNG SHNHLGGHFL RQDVGEFDAG FFNVLPGEAA AMDPQQRLLL
110 120 130 140 150
ETTYEAIESA GIPKESLAGS KTAVYMAMFT RDYDRNVYKD MMSIPKYHVT
160 170 180 190 200
GTGDAILANR ISYLFDLRGP SMTIDTGCSG GMAAVAHACQ ALRSGVSDVA
210 220 230 240 250
LAGAANLILS PDHMVGMSNL HMLNAEGKSY AFDDRGAGYG RGEGIATLVI
260 270 280 290 300
KRLDDAIKAN DPIRAIIRDA AVNQDGHTAG ITLPSGQAQE ALERQVWSNI
310 320 330 340 350
GLDPREVGYV EAHGTGTQAG DSAELEGISR VFCRGRTDSE SLTVGSIKSN
360 370 380 390 400
IGHTECVSGL AALIKSILVL EKGAIPPNVN YQTAKPGLDL DKRKLRVPTT
410 420 430 440 450
LQKWSQPGVP RVSVNSFGYG GTNAHAVLEK APETQRDSAS DSQEDVPRLF
460 470 480 490 500
TLSAASQSSL QDMAASIAGW VSQERDSQPL PTSRLQDIAY TLSERRSLMA
510 520 530 540 550
WRFWSVASNE HELVDSLYEA SRSTENISKI SSSEPPPKIS FIFTGQGAQW
560 570 580 590 600
PGMGRELLQS NAVFAESISR SNKILAGLGA AWGLVDEILR DKGPSRLREA
610 620 630 640 650
ELAQPATTAI QIALVDLARH WGIVPDSVVG HSSGEIAAAY AAGYLSPQQA
660 670 680 690 700
ITAAYYRGFS SAVARSKGLG KGGMLAVGLG EDEVAPYLAR ISPENGEAVV
710 720 730 740 750
ACQNSPKSVT ISGDDAAIAE LSELLTKDDV FNRRLLVDTA YHSHHMEAAA
760 770 780 790 800
DEYRSSLGDM EPRNSTGTIN MFSSVTGSLK TDDKFDANYW VSNLVGKVRF
810 820 830 840 850
RDALQALCQH DQTSSSPQTH RVFIEIGPHA ALAGPLRQSV ADMPTPLPHS
860 870 880 890 900
YTSALVRGTS ASQSALSMAG SLFSRGYPLN ISALNSASSL SSSSSPSVIP
910 920 930 940 950
NLPTYAWDHT KRHWHESRLS RDYRMRKHAY HDLLGLRMTD TTPLRPAWRH
960 970 980 990 1000
MVGVEGLPWL RDHVVDGLIV FPGAGYMCMA LQAAEQLALD LPSHSKVKRM
1010 1020 1030 1040 1050
RLQNVAFLKG LVIPDSTRER VEVQLVLTPL TGDNGPDNKL GYSFLVTAYT
1060 1070 1080 1090 1100
ADDDKWTEHC RGSVLIDLVS SSAASSQSTV GFESQHQITY AEAVSSLNLQ
1110 1120 1130 1140 1150
PGEDIPPSEL YQTLRKGGNA YGPTFSGIQV FRLLPDNASE DTSSANVALS
1160 1170 1180 1190 1200
TIAIPDIQSI MPAKHMQPHI IHPSTLDVLL HTTLPLVSRR LGVVGSVMPV
1210 1220 1230 1240 1250
RIDDLVIDLG EQQLETKTDA QLRAITTLTG SGFRSAEADM LVFPAPSSEV
1260 1270 1280 1290 1300
DQGQLMPVIS VMGMELRSLA ALDGAAAGDP ATENLSVEES RDICYEMKWV
1310 1320 1330 1340 1350
VDESFLSAEH LVNAVQQRDS SFDTPLERCL GALDKYLGIK ALKEFMADLK
1360 1370 1380 1390 1400
VLEIAAAGDS NGECTLAFLD ALQTRGALPA EYDLTAQPHG DALWQDKYPG
1410 1420 1430 1440 1450
VVTVRPLLDS MNHGLDGHYD IVFAAGSLNG SDGVTVQTSL SNIRSLMKPG
1460 1470 1480 1490 1500
AVLVAIHDTN SSLSADVFSQ TGFNTQLSIP FDELSLTIAR AVGSASTTTP
1510 1520 1530 1540 1550
VKLQFIAEPG FSTSTSIRTI IDNLPSTLTA KGVQIITAPE PCILNWTKGN
1560 1570 1580 1590 1600
LYDQDSDSEP VTLNIVLDNG ASPILPTVTN GTPTFSNIVS LLQKQHSKVL
1610 1620 1630 1640 1650
WVSLSDDEQH KLNPQKHLIT GVARTAHAEN ELLELVTVDV QQPISESTTS
1660 1670 1680 1690 1700
GLVNFLGDIA ASFPGLDGAA GETGTKKERE YIYIGENHIL VPRVMSSPSL
1710 1720 1730 1740 1750
NRQIKKSKET VTSTENFVMT PLKLDIAGKD GPGTAHAATF VEDESHRQPL
1760 1770 1780 1790 1800
GEDCVEIQAK AFGVGSSSWA SKGRPSSASS IAEYAGVITA IGSGVLISSG
1810 1820 1830 1840 1850
LKIGDRVVAW AETSLSFASR PRIPASQVRV LPDHVSLSTG AGLPVSLMTA
1860 1870 1880 1890 1900
CHALREISNV QPGQVVFIDG AASDIGQAAL LVARYLGAKV IVAVSTSDEA
1910 1920 1930 1940 1950
SFLQDKFGLP LANILPRASP FLRHQLRKLL ASGGAIDAIL SCAGSAVPGE
1960 1970 1980 1990 2000
IIKTQKPFGT LVQVGGTTGA MTASAVNSTV VSLDLGSFLT QTHPSKATRL
2010 2020 2030 2040 2050
FDMAMETVHR GLDLEPIRIA YLPMTNLNEA LKSARRHENM TKYVVEVGQE
2060 2070 2080 2090 2100
AMVKVARPSY ILPKLDEHAT YVVAGGLGDL GQRFLRLMAK AGARYLVTLS
2110 2120 2130 2140 2150
RSGAREGQQS ALERELNSLS PLSSLNLLCL KCDVSKEAKI QNSLAEIKAA
2160 2170 2180 2190 2200
GFPSVRGVIQ ASLVLGDSTL DNMTAQDFDR VLQAKAFGTL HLQRVFVPEG
2210 2220 2230 2240 2250
LAFFISLSSA VNMIGSAGQA NYNAANSLQD ALAQFDKSSD CFYMALNIGL
2260 2270 2280 2290 2300
IEDATVNSDV IIQSVQRQGL TTIYHDELDA YFEYSLSAEA RQAGCHQAVI
2310 2320 2330 2340 2350
GFTPESIAKT SIVNGTAKTL MFTHVRRQIS KQGQTEDDDA GGASGAVKTF
2360 2370 2380 2390 2400
AEFVAQGTHE QDDIEAFAAR AIANKLADLM LIEPEDVELD ESLNDFGLDS
2410 2420 2430 2440 2450
LIAIELRNWI MRELGSPIQT SEVLGSENIW ALARKVTLRS VHVTGGAGGD
2460 2470 2480 2490 2500
ASSTGNSESM ARTPSDSSTV PTSIPATPSR SPSREPPAKE TLTKSQQHLP
2510 2520 2530 2540 2550
IPDLTETLNM LVESRTAIGS LEEKAEIERV IQDFLTTDGP ELVEILRSNN
2560 2570 2580 2590 2600
DSSSDARLDF YNNHLHLERR EPLQDHALFF IGHLAEGEAG AAPPPKHTQA
2610 2620 2630 2640 2650
ERAAIITGAA MHFKQRLESG SLEQHKLNDI VLCMDTLQWL FHTIQEPGVA
2660 2670 2680 2690 2700
TDLAQKYPSN NKVVAMRKGH IFEIDVHPED DYAALHQIFS DIIASSDSSS
2710 2720 2730 2740 2750
DSIPKVSVLT TKPRHEWAVL RSQIQSLSPT NAETIDAIES CAFIVSLDHS
2760 2770 2780 2790 2800
SPETTSERST SILLNDLHLS NRWLDKMLTF TVASNGVSSL LGENTMLDGL
2810 2820 2830 2840 2850
SARQLSEYMT NEIFTNPKLS PPTSPPASTI RPLLFTLTPH VVETISQQIQ
2860 2870 2880 2890 2900
HNLSTYHPIS SSRHFYSQLN RAFLGSRGMR SKGTVLVAIA MATRLFFGHY
2910 2920 2930 2940 2950
EPLWETVTLA KYKQGRIDWL QTLTPDMVAF VDSLIAIHSH SLTSSSEVDW
2960 2970 2980 2990 3000
KGMNKLLKEV SISHVQNLQR VADGRGYVEA LYSLMGTAIS QGHDLPELFK
3010 3020 3030 3040 3050
SEAWKQTDRH LSPKRAKTDC LGSGGYLRMQ EGGFLMPNPG SLFIHYEVHH
3060 3070 3080
RDPLVNVSGR EEDVARFEGI LGACLGVVRR VVEG
Length:3,084
Mass (Da):332,855
Last modified:November 2, 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:i58126617F0154E48
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
LC079035 Genomic DNA Translation: BAV32159.1

<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
LC079035 Genomic DNA Translation: BAV32159.1

3D structure databases

SMRiA0A1B4XBH3
ModBaseiSearch...

Family and domain databases

Gene3Di1.10.1200.10, 1 hit
3.10.129.110, 1 hit
3.30.559.40, 1 hit
3.30.559.70, 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
IPR039551, Cho/carn_acyl_trans
IPR042232, Cho/carn_acyl_trans_1
IPR042231, Cho/carn_acyl_trans_2
IPR011032, GroES-like_sf
IPR032821, KAsynt_C_assoc
IPR014031, Ketoacyl_synth_C
IPR014030, Ketoacyl_synth_N
IPR016036, Malonyl_transacylase_ACP-bd
IPR036291, NAD(P)-bd_dom_sf
IPR020801, PKS_acyl_transferase
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
IPR016039, Thiolase-like
PfamiView protein in Pfam
PF00698, Acyl_transf_1, 1 hit
PF00755, Carn_acyltransf, 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

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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 nameiSDNO_SORAA
<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: A0A1B4XBH3
<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: August 30, 2017
Last sequence update: November 2, 2016
Last modified: December 11, 2019
This is version 18 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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