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Entry version 94 (23 Feb 2022)
Sequence version 1 (23 Jan 2007)
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Protein

Polyketide synthase-nonribosomal peptide synthetase

Gene

ccsA

Organism
Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107)
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>
-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

Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of the mycotoxins cytochalasins E and K (PubMed:21983160).

The hybrid PKS-NRPS synthetase ccsA and the enoyl reductase ccsC are responsible for fusion of phenylalanine with an octaketide backbone and subsequent release of the stable tetramic acid precursor (PubMed:21983160, PubMed:27551732).

The polyketide synthase module (PKS) of the PKS-NRPS ccsA is responsible for the synthesis of the octaketide backbone (PubMed:21983160).

The downstream nonribosomal peptide synthetase (NRPS) amidates the carboxyl end of the octaketide with a phenylalanine (PubMed:21983160).

A reductase-like domain (R) at the C-terminus catalyzes the reductive release of the polyketide-amino acid intermediate (PubMed:21983160).

Because ccsA lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase ccsC (PubMed:21983160, PubMed:27551732).

Upon formation of the 11-membered carbocycle-fused perhydroisoindolone intermediate, a number of oxidative steps are required to afford the final cytochalasin E and K, including two hydroxylations at C17 and C18, one alcohol oxidation at C17, one epoxidation at C6 and C7 and two Baeyer-Villiger oxidations (PubMed:21983160).

The oxidative modification at C17, C18 and the C6-C7 epoxidation are likely to be catalyzed by the two cytochrome P450 oxygenases ccsD and ccsG (PubMed:21983160).

CcsD may be responsible for the epoxidation of the C6-C7 double bond (PubMed:21983160).

CcsG may be responsible for the successive oxidative modifications at C17 and C18 (PubMed:21983160).

The double Baeyer-Villiger oxidations of ketocytochalasin to precytochalasin and cytochalasin Z(16) are among the final steps leading to cytochalasin E and K and are catalyzed by ccsB (PubMed:21983160, PubMed:24838010).

The first oxygen insertion step follows that of the classic BVMO mechanism, generating the ester precytochalasin (PubMed:24838010).

Release of precytochalasin into an aqueous environment can generate the shunt product iso-precytochalasin through spontaneous isomerization (PubMed:24838010).

Alternatively, precytochalasin can undergo further oxidation by ccsB to yield the in-line carbonate-containing cytochalasin Z(16) (PubMed:24838010).

Cytochalasin Z(16) is a precursor to cytochalasin E and cytochalasin K, whereas iso-precytochalasin is a precursor to cytochalasin Z(17) and rosellichalasin (PubMed:21983160, PubMed:24838010).

The hydrolyase ccsE may catalyze hydrolysis of epoxide bond in cytochalasin E to afford cytochalasin K (PubMed:21983160).

The function of ccsF has not been assigned but it may play a role in post-PKS-NRPS biosynthetic step, resistance or transport of cytochalasins and related PKS-NRPS products (PubMed:21983160).

3 Publications

<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: Mycotoxin biosynthesis

This protein is involved in Mycotoxin biosynthesis.1 Publication
View all proteins of this organism that are known to be involved in Mycotoxin 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 sitei181For ketoacyl synthase 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, Isomerase, Ligase, Methyltransferase, Multifunctional enzyme, Oxidoreductase, Transferase
LigandNADP, S-adenosyl-L-methionine

<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:
Polyketide synthase-nonribosomal peptide synthetase1 Publication (EC:2.3.1.-2 Publications, EC:6.3.2.-2 Publications)
Short name:
PKS-NRPS1 Publication
Alternative name(s):
Cytochalasin 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:ccsA1 Publication
ORF Names:ACLA_078660
<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>OrganismiAspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107)
<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 identifieri344612 [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 lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillusAspergillus subgen. Fumigati
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000006701 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unassembled WGS sequence

Organism-specific databases

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
FungiDB:ACLA_078660

<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 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

Loss of cytochalasin E and cytochalasin K production.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_00004314791 – 4043Polyketide synthase-nonribosomal peptide synthetaseAdd BLAST4043

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 residuei2435O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1
Modified residuei3657O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
A1CLY8

<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

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
5057.CADACLAP00007112

<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
A1CLY8

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>Domaini2394 – 2475Carrier 1PROSITE-ProRule annotationAdd BLAST82
Domaini3617 – 3697Carrier 2PROSITE-ProRule annotationAdd BLAST81

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>Regioni11 – 449Ketoacyl synthase (KS) domainSequence analysis1 PublicationAdd BLAST439
Regioni557 – 877Acyl transferaseSequence analysis1 PublicationAdd BLAST321
Regioni945 – 1243Dehydratase (DH) domainSequence analysis1 PublicationAdd BLAST299
Regioni1400 – 1585Methyltransferase (MT) domainSequence analysis1 PublicationAdd BLAST186
Regioni2115 – 2288Ketoreductase (KR)domainSequence analysis1 PublicationAdd BLAST174
Regioni2395 – 2472Peptidyl carrier proteinSequence analysis1 PublicationAdd BLAST78
Regioni2476 – 2575DisorderedSequence analysisAdd BLAST100
Regioni2587 – 2630DisorderedSequence analysisAdd BLAST44
Regioni2640 – 3069CondensationSequence analysis1 PublicationAdd BLAST430
Regioni3102 – 3502AdenylationSequence analysis1 PublicationAdd BLAST401
Regioni3622 – 3694ThiolationSequence analysis1 PublicationAdd BLAST73
Regioni3735 – 3954Reductase-likeSequence analysis1 PublicationAdd BLAST220

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 biasi2492 – 2534Polar residuesSequence analysisAdd BLAST43
Compositional biasi2559 – 2573Polar residuesSequence analysisAdd BLAST15
Compositional biasi2594 – 2608Polar residuesSequence analysisAdd BLAST15
Compositional biasi2615 – 2630Polar residuesSequence analysisAdd BLAST16

<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

NRP synthetases are composed of discrete domains (adenylation (A), thiolation (T) or peptidyl carrier protein (PCP) and condensation (C) domains) which when grouped together are referred to as a single module. Each module is responsible for the recognition (via the A domain) and incorporation of a single amino acid into the growing peptide product. Thus, an NRP synthetase is generally composed of one or more modules and can terminate in a thioesterase domain (TE) that releases the newly synthesized peptide from the enzyme. Occasionally, epimerase (E) domains (responsible for l- to d- amino acid conversion) are present within the NRP synthetase (By similarity). CcsA contains also a polyketide synthase module (PKS) consisting of several catalytic domains including a ketoacyl synthase domain (KS), an acyl transferase domain (AT), a dehydratase domain (DH), a methyltransferase domain (MT), and a ketoreductase domain (KR). Instead of a thioesterase domain (TE), CcsA finishes with a reductase-like domain (R) for peptide release. CcsA has the following architecture: KS-AT-DH-KR-PCP-C-A-T-R (PubMed:21983160).By similarity1 Publication

<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

In the C-terminal section; belongs to the NRP synthetase family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1178, Eukaryota
KOG1202, Eukaryota

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_000022_37_5_1

Identification of Orthologs from Complete Genome Data

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OMAi
NEQMRFG

Database of Orthologous Groups

More...
OrthoDBi
19161at2759

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
3.30.300.30, 1 hit
3.30.559.10, 1 hit
3.40.366.10, 1 hit
3.40.47.10, 1 hit
3.40.50.12780, 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
IPR045851, AMP-bd_C_sf
IPR020845, AMP-binding_CS
IPR000873, AMP-dep_Synth/Lig
IPR042099, ANL_N_sf
IPR023213, CAT-like_dom_sf
IPR001242, Condensatn
IPR013120, Far_NAD-bd
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
IPR006162, Ppantetheine_attach_site
IPR029063, SAM-dependent_MTases
IPR016039, Thiolase-like

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00698, Acyl_transf_1, 1 hit
PF00501, AMP-binding, 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
PF07993, NAD_binding_4, 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, 2 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF47336, SSF47336, 2 hits
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
PS00455, AMP_BINDING, 1 hit
PS00606, B_KETOACYL_SYNTHASE, 1 hit
PS50075, CARRIER, 2 hits
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.

A1CLY8-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGSFQNSSEP IAIIGTGCRF PGGCDSPSKL WELLRAPRDL LKEIPESRFS
60 70 80 90 100
VDSFYHPDNA HHGTSNVRHS YFLEEDLRQF DVQFFGIKPI EANAVDPQQR
110 120 130 140 150
LLLETVYEGL ESAGLSIQRL QGSDTAVYVG VMSADFTDLV GRDTETFPTY
160 170 180 190 200
FATGTARSIL SNRLSYFFDW HGPSLTIDTA CSSSLIAMHH AVQTLRSGDS
210 220 230 240 250
SLAIVAGSNL ILGPEQYIAE SKLQMLSPTG RSRMWDAAAD GYARGEGVAA
260 270 280 290 300
IVLKRLSQAI ADGDHIECVI RETGVNQDGK TPGITMPSAT AQAALIRSTY
310 320 330 340 350
AKAGLDLSNR SDRPQYFEAH GTGTPAGDPI EARAIQTAFF GPDLNFTADS
360 370 380 390 400
RKDTLFVGSI KTVVGHTEGT AGLAAVIKAS LALQSGTIPP NRLLEQLNPA
410 420 430 440 450
IKPFYNSLKI LAAAEDWPQL SRGGVRRVSV NSFGFGGANS HAILESYEPS
460 470 480 490 500
LHSHKGTRDI SFSPFTFSAA SETALVASLR AYRDLLSTRS DVRLTDLAWT
510 520 530 540 550
LNSRRSTLAS RVAIAASDKD DLVLKLDDRA ENYDGSDTFM DAGHRKPNAN
560 570 580 590 600
ELRILGVFTG QGAQWARMGA ELIEQCPGAS KVVDALEQSL RSLPPQDRPT
610 620 630 640 650
WSLREQLLAP PSSSMVSTAS ISQPLCTAIQ IMLVDMLREA GIQFSAVVGH
660 670 680 690 700
SSGEIGAAYA AGCLSAKDAI RVAYYRGVHL KSALQKGSML AVGTTFEDAQ
710 720 730 740 750
DLCNLPTFED RLCVAASNSP SSVTISGDSD AIEEIKVVFD EEKKFTRLLK
760 770 780 790 800
VDRAYHSHHM QDCVEPYVRS LRQCSVTFRP PNRNQCVWIS SVFVQDIHQL
810 820 830 840 850
SEDGSDRYWG SNLARPVMFA EALQLLLSLE GSFDLAVEVG PHPALKGPAS
860 870 880 890 900
QTIQDALGYS IPYTGVLSRG NSDVEAFAAA LGSIWTAFGD GAVDFSRLQK
910 920 930 940 950
FTSGSAAQPQ LLKGLPTYQW DHNRVFWHES RVSKAFRTRK DVPNELLGRQ
960 970 980 990 1000
VLDGAPNQLR WRNILRPREI AWLEGHQVQG QMVFPCAGYV SACAEASMRL
1010 1020 1030 1040 1050
AVGQNVESIE LEEFVVGQAI VFNDSNSEVE TLATLTEVVH RQQTISANFA
1060 1070 1080 1090 1100
FYSCPTGGES LELVRNASCR LRITVGDSAV DLLQPQAEAD FALLEVESDR
1110 1120 1130 1140 1150
FYNALGQLGF GYTGPFRSLT ALKRKLGIAR GLIENAPPSF NHSQPLLIHP
1160 1170 1180 1190 1200
ATLDAAIQSI MLAYCYPGDS MLRAIHLPTG IEKLTLNPVN CLKFAGQSVQ
1210 1220 1230 1240 1250
VPFDSSASTG SGRSLQGDVS IYSLDGSRAV QLEGLQTQPL SSPTEASDLN
1260 1270 1280 1290 1300
IFTELVWGVD RPDCEEILRT TVVEDFDAEL LFSLERVAYF YLRSLGEAVP
1310 1320 1330 1340 1350
ERERNGLEWH HKRLFAYVDH VLSRVARGVN RFARPEWAAD SKNDILKILQ
1360 1370 1380 1390 1400
KYPDNIDLRL MRAVGENLPA VVRGQLTMLE PMIQDNMLND FYVIAHGMPR
1410 1420 1430 1440 1450
YTKYLAAMAS QISHRYPHMN VLEIGAGTGG ATKSFLKELG EGFSTYTFTD
1460 1470 1480 1490 1500
ISSGFFEKAS QVFASYSAKM NFKVLDIEKD IESQGFAPES FDLIIASLVL
1510 1520 1530 1540 1550
HATRDLAQTV RNVRRLLKPG GYLLLLEITE NEQMRFGLIF GGLPGWWLGY
1560 1570 1580 1590 1600
EDGRPFSPCV DIEEWSRVLE QNGFSGIETA IPHHDTLPAP LSVIVSQAVN
1610 1620 1630 1640 1650
EKVQFLHNPL DSIRGSTVIP RLTIIGGGGR RSAQLIDAVS SLVQPQCGQL
1660 1670 1680 1690 1700
RVVDSLQKIC SEVLPVGGSV LSLTDFDEPV FKSMDADKLR GFQEIFKQSK
1710 1720 1730 1740 1750
NVLWVTQGSR SGDPYARMVV GFGRTIVLEM LHLRLQFLDV SPSSSPDASA
1760 1770 1780 1790 1800
IAEAMLRLEV SGSWEDEGAE DGAVLHSVEP ELSISDGRCW VPRFKPNKEQ
1810 1820 1830 1840 1850
NERYNSVRRS IETEQSFSDT CVELVYRDNS LSLLEVTHSS SEPLAEPSTK
1860 1870 1880 1890 1900
YLELDVNYSV SKAVEVVPGC YLFLILGRDT DTGDRFIALS PKQSSRVRIP
1910 1920 1930 1940 1950
RALVLPQHTS HGTINENSLD AFFHEIVARS ILRDVPYGSA AIALQPNSLL
1960 1970 1980 1990 2000
ADALREAAQD KGVTLHLWST QASDLESEWT YIHRKASKTE VQNAIPRNVT
2010 2020 2030 2040 2050
CFFDMGGDES IATKILACLP DHTQAKKEAS ITAHEAHLIP TVLPDIRSLL
2060 2070 2080 2090 2100
MDIGRAMRTR GKSSSPDLRI VDLTDIVKGQ ADSETSIINW LESSSRVPVA
2110 2120 2130 2140 2150
VEPIEARVQF RSDRTYWLVG LTGGLGLSLC EWMAQQGARY IVLSSRSPKV
2160 2170 2180 2190 2200
DGRWLAKMNR MGVTVEVVAN DISNRDSVQR VYNKIRTELP PISGVAQGAM
2210 2220 2230 2240 2250
VLHDTMFLDL DMERMNKVLR PKVDGSTYLE EIFHDTELEF FVFFSSMAAV
2260 2270 2280 2290 2300
TGNPGQSAYA AANMFMASLA NQRRQRGLNA SAVHIGAIFG NGYVTRELTL
2310 2320 2330 2340 2350
VQQEFLRKVG NLWLSEHDFR RLFAEAVYAG RHHRGRSPEL STGLKILESD
2360 2370 2380 2390 2400
ESESITWFNN PVFQHCIKQS GRVDLISETS TSAAPVKVRL AEASSSADIY
2410 2420 2430 2440 2450
DIISDAFVTK LKTSLQVEGD RPIVDLTADT LGIDSLVAVD IRSWFIKELQ
2460 2470 2480 2490 2500
VEIPVLKILS GATVGEMVTQ AQELLPKELT PNLDPNAEAK PSKPKNTVQP
2510 2520 2530 2540 2550
KQQTKKTIQL QNVAKAPQPA LSQQVSSGVQ NMIKTNPPKE AEAKQPRPEV
2560 2570 2580 2590 2600
KQAAPKDSQY PTALETPSKL QDPSRNIVVA KDLAAEEKHL TDQEPVPSNM
2610 2620 2630 2640 2650
SSSSWSEIDE SEGKVETSSS SSSTSASQII TKTKPVEVKK SVPMAFGQSR
2660 2670 2680 2690 2700
FWFLRHYLED PSSFNITVSI QLDGPLKIDH FARAVQVVGQ RHEALRTRFV
2710 2720 2730 2740 2750
TDEAQGTTKQ EVLALSNLTL EERTISTDEE AEGVYQELKG YAFDLEKGEN
2760 2770 2780 2790 2800
IRIILLKRSN RSFTLIIAYH HINMDGVSLE VLLRDLQMAY DSKFLSPRIL
2810 2820 2830 2840 2850
QYADFSEQQR RDYQSGKWAE DLAFWKKEFQ TMPGPLPLLS MARTSTRSPL
2860 2870 2880 2890 2900
TAYKTHSAEF HIDPATLDTI QSTCQRMKVT PFHFHLAVFY TMLIRLVDVE
2910 2920 2930 2940 2950
NLCIGISSAN RSQQDTLQSV GLYLNLLPLN FTPQLDQTFT NVLHIVREKS
2960 2970 2980 2990 3000
VQAFAHSKVP FDVIVNELGA ARSATHSPLF QVLVNYRAGV SERRSFCNCD
3010 3020 3030 3040 3050
SKVLTFEQGQ TPYDLSLDVI DNPGGDCHVI MAGQSVLYGA EHVAVLRGVY
3060 3070 3080 3090 3100
QNLLVAFSRN PALRLNVPPL YDTDEVKHAI KLGHGPAYNY QWPATIPERI
3110 3120 3130 3140 3150
DEIVERYPTH VALIDGDGRK MSYTEMARRV NTLAVVLLRQ DIGQGSKVGV
3160 3170 3180 3190 3200
FMEPGSSWIC SLLAILRLDA IYIPLDSRMG LDRLSTIVRD CKPDLLLVDN
3210 3220 3230 3240 3250
TTLSNVALLG LSCPTLNVDV VSPGSDQQHV PNTAQPSSTA VIMYTSGSTG
3260 3270 3280 3290 3300
VPKGIVMQHH TFRNNIETST EKWDFREGRE TTLQQSSYSF DMSLSQTFLT
3310 3320 3330 3340 3350
LSNGGTLRIV PKKLRGDPKA IASLITAEGI TFTETTPSEY ISWLRYGDVD
3360 3370 3380 3390 3400
DLRKSKWRIA VSGGETITTN LTGLLRQLEK SDLRLIDCYG PTEITFCSHG
3410 3420 3430 3440 3450
REVQYDGEGD ILSPAFRTWP NYSVYIVDSH MKPVPIGIPG EILIGGAGVV
3460 3470 3480 3490 3500
AGYVHSELDA RGFARNNFMN TMFLENAWTR LHRTGDFGRL DQEGNLILGG
3510 3520 3530 3540 3550
RIAGDTQVKL RGIRIDLQEI ESAILSSGDG KIVDAAVTVR ESADSGSEYL
3560 3570 3580 3590 3600
MAFVTTLDAG DLSLERIRQE LPLPQHMRPA NIITLDQLPM TASNKVDRLA
3610 3620 3630 3640 3650
LKSLPLPPGS HVADTGTDES PSMAKMRDVW ATVIPQEVLA HFELGPASNF
3660 3670 3680 3690 3700
FQVGGDSMLL VRLQTEINKV FGTSISLFQL FDASSLTGMV SLIDHSESTS
3710 3720 3730 3740 3750
QRSEVDWETE TTISPSLLQV PATKRFFAHP AVVVLTGATG FLGRAIVNRL
3760 3770 3780 3790 3800
LKDCSVQKIH CVAVRRDPSS LPDDFKSPKV VLHRGDLTLP QLGLTDRAAT
3810 3820 3830 3840 3850
EIFAEADAVI HNGADVSFMK TYQSLKQANL EATKELVRLS APHRLSFHYI
3860 3870 3880 3890 3900
SSASVTRLAG QESFDQSSVS AFPPSAEDGY VASKWASERY LEKVSDQCGL
3910 3920 3930 3940 3950
PIWIHRPSSI VGEGAPDTDM MASLLGYSRT LRAIPQTDGW TGWLDFVSAD
3960 3970 3980 3990 4000
RVAMQIADEV YEDYSWPGTV KYLYEAGDRE IPLSDLRGVL ERETGESFES
4010 4020 4030 4040
IPLEEWVLRA EGQGLHPLLG EYLRRVSGIP LVLPRLVQQG SFF
Length:4,043
Mass (Da):445,741
Last modified:January 23, 2007 - 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:iE914ABF892E54658
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
DS027057 Genomic DNA Translation: EAW09117.1

NCBI Reference Sequences

More...
RefSeqi
XP_001270543.1, XM_001270542.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
EAW09117; EAW09117; ACLA_078660

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
4702673

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
act:ACLA_078660

<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
DS027057 Genomic DNA Translation: EAW09117.1
RefSeqiXP_001270543.1, XM_001270542.1

3D structure databases

SMRiA1CLY8
ModBaseiSearch...

Protein-protein interaction databases

STRINGi5057.CADACLAP00007112

Proteomic databases

PRIDEiA1CLY8

Genome annotation databases

EnsemblFungiiEAW09117; EAW09117; ACLA_078660
GeneIDi4702673
KEGGiact:ACLA_078660

Organism-specific databases

VEuPathDBiFungiDB:ACLA_078660

Phylogenomic databases

eggNOGiKOG1178, Eukaryota
KOG1202, Eukaryota
HOGENOMiCLU_000022_37_5_1
OMAiNEQMRFG
OrthoDBi19161at2759

Family and domain databases

Gene3Di1.10.1200.10, 1 hit
3.10.129.110, 1 hit
3.30.300.30, 1 hit
3.30.559.10, 1 hit
3.40.366.10, 1 hit
3.40.47.10, 1 hit
3.40.50.12780, 1 hit
InterProiView protein in InterPro
IPR001227, Ac_transferase_dom_sf
IPR036736, ACP-like_sf
IPR014043, Acyl_transferase
IPR016035, Acyl_Trfase/lysoPLipase
IPR045851, AMP-bd_C_sf
IPR020845, AMP-binding_CS
IPR000873, AMP-dep_Synth/Lig
IPR042099, ANL_N_sf
IPR023213, CAT-like_dom_sf
IPR001242, Condensatn
IPR013120, Far_NAD-bd
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
IPR006162, Ppantetheine_attach_site
IPR029063, SAM-dependent_MTases
IPR016039, Thiolase-like
PfamiView protein in Pfam
PF00698, Acyl_transf_1, 1 hit
PF00501, AMP-binding, 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
PF07993, NAD_binding_4, 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, 2 hits
SUPFAMiSSF47336, SSF47336, 2 hits
SSF51735, SSF51735, 2 hits
SSF52151, SSF52151, 1 hit
SSF53335, SSF53335, 1 hit
SSF53901, SSF53901, 1 hit
SSF55048, SSF55048, 1 hit
PROSITEiView protein in PROSITE
PS00455, AMP_BINDING, 1 hit
PS00606, B_KETOACYL_SYNTHASE, 1 hit
PS50075, CARRIER, 2 hits
PS00012, PHOSPHOPANTETHEINE, 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 nameiCCSA_ASPCL
<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: A1CLY8
<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: January 7, 2015
Last sequence update: January 23, 2007
Last modified: February 23, 2022
This is version 94 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

Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
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