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Entry version 46 (16 Oct 2019)
Sequence version 3 (20 Dec 2017)
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Protein

Adenylate-forming reductase 03009

Gene

CC1G_03009

Organism
Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003) (Inky cap fungus) (Hormographiella aspergillata)
Status
Reviewed-Annotation score:

Annotation score:2 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 transcript 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

Adenylate-forming reductase, a natural product biosynthesis enzyme that resembles non-ribosomal peptide synthetases, yet serves to modify one substrate, rather than to condense two or more building blocks. The A-domain preferentially accepts L-serine, L-alanine and L-valine as substrates. The natural product of the enzyme is not yet known.1 Publication

<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 functionOxidoreductase, 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_and_taxonomy_section">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:
Adenylate-forming reductase 03009 (EC:2.3.1.-)
Alternative name(s):
Alanine/valine/serine reductase
Nonribosomal peptide synthase 12-like enzyme
Short name:
NRPS-like
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
ORF Names:CC1G_03009
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiCoprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003) (Inky cap fungus) (Hormographiella aspergillata)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri240176 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesAgaricomycetidaeAgaricalesPsathyrellaceaeCoprinopsis
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
  • UP000001861 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">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 Database Resources

More...
EuPathDBi
FungiDB:CC1G_03009

<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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004426401 – 1025Adenylate-forming reductase 03009Add BLAST1025

<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
5346.XP_001835921.2

<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

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>Regioni38 – 422Adenylation (A) domainSequence analysisAdd BLAST385
Regioni556 – 638Thiolation and peptide carrier (T) domainSequence analysisAdd BLAST83
Regioni682 – 900Thioester reductase (TR) domainSequence analysisAdd BLAST219

<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

Contains three distinct domains: an adenylation (A) domain that activates the substrate amino acid which is subsequently covalently linked as a thioester (aminoacyl-S-PCP) to the 4'-phosphopantetheine prosthetic group of the second domain, the peptidyl carrier protein (PCP) domain, as well as a thioester reductase (TR) domain of the ferredoxin-NADP reductase (FNR) type.1 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

Belongs to the adenylate-forming reductase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410ISPW Eukaryota
ENOG410XP5F LUCA

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
A8NS27

Database of Orthologous Groups

More...
OrthoDBi
808472at2759

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.50.12780, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR010071 AA_adenyl_domain
IPR020845 AMP-binding_CS
IPR000873 AMP-dep_Synth/Lig
IPR042099 AMP-dep_Synthh-like_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00501 AMP-binding, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01733 AA-adenyl-dom, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00455 AMP_BINDING, 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_length">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

A8NS27-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MASSDLLSHL SATDRALFWK YGVGAEVSVP FQCVHHAFEF HAKSNPQLTA
60 70 80 90 100
VDELGTTLSY GELDRRANCL ASRLRSVGVV QGSRVCMLVE RAVTLPVAVL
110 120 130 140 150
GILKAGAAYI PLDGNIVSDS TLKHALVDSG STVALTLRKF EHRLEGAPVP
160 170 180 190 200
VVFLDDAICP SYNPSHCVKP RDTTTSKDSV YIIYTSGTTG TPKGVHVTHG
210 220 230 240 250
NVTNLICIEP GQLGMKPGVR VSQMLNISFD FAAWEILGSL ANGATLCPRG
260 270 280 290 300
KTSKDWKAVM RSVDILFSTP SMLAPHNPVD YPNVKTVVVA GEACPKALAD
310 320 330 340 350
TWGARVKFWN ACGPTEVTIA NTMQLHIPGD IVTIGGPTPN NTAYVLDENM
360 370 380 390 400
RPVPIGQTGV MWGGGAGITK GYLNLPDKTS ERYVRDPFAN DGSMMFNTGD
410 420 430 440 450
LGKWVSNGTL QHLGRIDNQV KIKGFRVELD GVATAMETCA GVTGATALLI
460 470 480 490 500
DGELWGFVKP SNISPEDIKA AAHKVQPYYA VPSKILTMDH FPETANGKTD
510 520 530 540 550
KRVLQQMAIE SKEEEAKLKE EKAAIPENVA WISLPPTVVT APKTELTIPH
560 570 580 590 600
RPSDHSLGST NTKISAQVKE ADSSASSTSE LEKQEYIWSG YQDDDHPEKT
610 620 630 640 650
QGRLVRNLRH QIFSLYRRLF SVVFIVNAAI LIWICVKKEY DANRIGGIVI
660 670 680 690 700
ANVFIGVLMR QELVINTFFL IFTSIPSSWP LFIRRTAARV YHIGGIHSGA
710 720 730 740 750
GVSSLLWLCL FTAQATKEMI NGGKTSVRTV AITYVILAEL LGIVIFAYPA
760 770 780 790 800
LRKRLHDTFE NTHRFLGWSA LALVWVQFMF LTIDYLPEGQ MLGQTLVKTP
810 820 830 840 850
QFWLVIILTC SVIWPWFRLR KVDVKPEVLS NHAVRLWFDY VTPPAGTFMR
860 870 880 890 900
VSDAPLKEWH GFAAIPIPGR TGYSLVVSRA GDWTSKHIAN PPTKLWVKGV
910 920 930 940 950
PTYGVLKLVP MFRRMVIVAT GSGIGPCAPA IFEKRIPMRV LWTAPNVRET
960 970 980 990 1000
FGDKLVDSIL EANPEAVIYD TRKHGKPDMV KLTLRLVKEF NAEAVAIISN
1010 1020
QPLTEKVVYG MMSRGIPAFG AIWDS
Length:1,025
Mass (Da):112,552
Last modified:December 20, 2017 - v3
<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:i32E18D88FEC564EC
GO

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence EAU85986 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated

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
KX118593 mRNA Translation: ANX99777.1
AACS02000008 Genomic DNA Translation: EAU85986.2 Different initiation.

NCBI Reference Sequences

More...
RefSeqi
XP_001835921.2, XM_001835869.2

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
EAU85986; EAU85986; CC1G_03009

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
6012458

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
cci:CC1G_03009

<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
KX118593 mRNA Translation: ANX99777.1
AACS02000008 Genomic DNA Translation: EAU85986.2 Different initiation.
RefSeqiXP_001835921.2, XM_001835869.2

3D structure databases

Database of comparative protein structure models

More...
ModBasei
Search...

SWISS-MODEL Interactive Workspace

More...
SWISS-MODEL-Workspacei
Submit a new modelling project...

Protein-protein interaction databases

STRINGi5346.XP_001835921.2

Genome annotation databases

EnsemblFungiiEAU85986; EAU85986; CC1G_03009
GeneIDi6012458
KEGGicci:CC1G_03009

Organism-specific databases

EuPathDBiFungiDB:CC1G_03009

Phylogenomic databases

eggNOGiENOG410ISPW Eukaryota
ENOG410XP5F LUCA
InParanoidiA8NS27
OrthoDBi808472at2759

Family and domain databases

Gene3Di3.40.50.12780, 1 hit
InterProiView protein in InterPro
IPR010071 AA_adenyl_domain
IPR020845 AMP-binding_CS
IPR000873 AMP-dep_Synth/Lig
IPR042099 AMP-dep_Synthh-like_sf
PfamiView protein in Pfam
PF00501 AMP-binding, 1 hit
TIGRFAMsiTIGR01733 AA-adenyl-dom, 1 hit
PROSITEiView protein in PROSITE
PS00455 AMP_BINDING, 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 nameiN3009_COPC7
<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: A8NS27
Secondary accession number(s): A0A1B1ZGC6
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 20, 2017
Last sequence update: December 20, 2017
Last modified: October 16, 2019
This is version 46 of the entry and version 3 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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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