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Entry version 41 (18 Sep 2019)
Sequence version 1 (06 Feb 2013)
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Protein

Nonribosomal peptide synthase sidN

Gene

sidN

Organism
Epichloe festucae var. lolii (Neotyphodium lolii) (Acremonium lolii)
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

Nonribosomal peptide synthase required for the biosynthetis of epichloenin A, an extracellular siderophore that plays a crucial role in endophyte-grass symbioses (PubMed:23658520, PubMed:19923209). SidN assembles epichloenin A by activating and incorporating three trans-anhydromevalonylhydroxyornithine (trans-AMHO), 1 glutamine and 4 glycine moieties (PubMed:23658520). Trans-AMHO is produced from L-ornithine via 2 steps involving a L-ornithine N5-monooxygenase and an AHMO-N5-transacylase that have still to be identified (PubMed:19923209). The third adenylation domain (A3) of sidN incorporates the hydroxamate groups of the siderophore which forms an octahedral iron complex (PubMed:19923209). The other component amino acids are assembled by sidN adenylation domains A1 and A2 (PubMed:23658520, PubMed:19923209).2 Publications

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=40 µM for adenylation of cis-AMHO (by adenylation A3 domain)1 Publication

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

    This protein is involved in Siderophore biosynthesis.2 Publications
    View all proteins of this organism that are known to be involved in Siderophore biosynthesis.

    <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 functionLigase, Multifunctional enzyme

    <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:
    Nonribosomal peptide synthase sidN1 Publication (EC:6.3.2.-1 Publication)
    Short name:
    NPRS sidN1 Publication
    Alternative name(s):
    Epichloenin A synthetase1 Publication
    Extracellular siderophore synthetase N1 Publication
    <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
    Name:sidN1 Publication
    <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>OrganismiEpichloe festucae var. lolii (Neotyphodium lolii) (Acremonium lolii)
    <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 identifieri73839 [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 lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesClavicipitaceaeEpichloe

    <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

    Leads to the accumulation of the intermediate N-5-trans-anhydromevalonyl-N-5-hydroxyornithine (trans-AMHO), displays sensitivity to oxidative stress and shows deficiencies in both polarized hyphal growth and sporulation (PubMed:23658520). Changes its interaction with the plant Lolium perenne from mutually beneficial to antagonistic (PubMed:23658520).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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000444382‹1 – ›1928Nonribosomal peptide synthase sidNAdd BLAST›1928

    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 residuei102O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1
    Modified residuei1216O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1
    Modified residuei1774O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1

    Keywords - PTMi

    Phosphopantetheine, Phosphoprotein

    <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 repressed by iron (PubMed:23658520).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

    11928
    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
    K7NCP5

    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_and_domains_section">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>Domaini65 – 141Carrier 1PROSITE-ProRule annotation1 PublicationAdd BLAST77
    Domaini1178 – 1255Carrier 2PROSITE-ProRule annotation1 PublicationAdd BLAST78
    Domaini1740 – 1813Carrier 3PROSITE-ProRule annotation1 PublicationAdd BLAST74

    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>Regioni177 – 460Condensation 1Sequence analysis1 PublicationAdd BLAST284
    Regioni640 – 1045AdenylationSequence analysis1 PublicationAdd BLAST406
    Regioni1297 – 1706Condensation 2Sequence analysis1 PublicationAdd BLAST410
    Regioni1855 – 1920Condensation 3Sequence analysis1 PublicationAdd BLAST66

    <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 (By similarity). Each module is responsible for the recognition (via the A domain) and incorporation of a single amino acid into the growing peptide product (By similarity). 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 (By similarity). Occasionally, methyltransferase domains (responsible for amino acid methylation) are present within the NRP synthetase (By similarity). SidN has the following architecture: A-T-C-A-T-C-A-T-C-T-C-T-C (PubMed:23658520).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

    Belongs to the NRP synthase family.Curated

    Keywords - Domaini

    Repeat

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    1.10.1200.10, 3 hits
    3.30.559.10, 3 hits
    3.40.50.12780, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR036736 ACP-like_sf
    IPR020845 AMP-binding_CS
    IPR000873 AMP-dep_Synth/Lig
    IPR042099 AMP-dep_Synthh-like_sf
    IPR023213 CAT-like_dom_sf
    IPR001242 Condensatn
    IPR020806 PKS_PP-bd
    IPR009081 PP-bd_ACP
    IPR006162 Ppantetheine_attach_site

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00501 AMP-binding, 1 hit
    PF00668 Condensation, 2 hits
    PF00550 PP-binding, 3 hits

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM00823 PKS_PP, 3 hits

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF47336 SSF47336, 3 hits

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00455 AMP_BINDING, 1 hit
    PS50075 CARRIER, 3 hits
    PS00012 PHOSPHOPANTETHEINE, 2 hits

    <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: Fragment.

    K7NCP5-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    LVAQAVKRHA TAELPRHMVP DVFMPLNCLP RNQSSKVNRK RLLEVVGREW
    60 70 80 90 100
    SMQPMSPVAD EQVDPAWCIK HRPLLEKIQG VIKIMPKTLS RSTTLSELGV
    110 120 130 140 150
    DSIGAIRLSS RFKNDGHDIS AIQVLDSVTI EDLNNHLSVK RQGTSNWKTL
    160 170 180 190 200
    LSRYLDHWKP LVSRHLARDP AHFSLVPTTV FQDGMLVETL RDPMLYWASY
    210 220 230 240 250
    SWRLPSTVDI ARVRQAWQHV SKNHDILKVS FVPTAYFEQE ETQSSGPSSM
    260 270 280 290 300
    FIQLIDYNAS MDWQEIVSDS GDWQQSIQAV CANLQRTQHE NNFSSPPWRV
    310 320 330 340 350
    TILAQQDQRI MNLTIHHSLC DGEMLRSLMH DVAWAYSTAE LPVKRCQVQE
    360 370 380 390 400
    AVSRLAVRYS EPEGHKFWGD MLSPLVSQTS LGDATSNSPK AVVRKIRHRT
    410 420 430 440 450
    TELQATRSTS KLTGLARRLG ASSLSPLFRV TFGIMLTEYY EQQSVLFGEV
    460 470 480 490 500
    RSERLLESQL VGAMAPLSAT YPVPFRSSGN IKDMVHSQQI LVMDSIRYGP
    510 520 530 540 550
    PQPSDVRKIL KKSRDEALYS AVYVLRQRPE DDGGSLAPWE EFKDIFEIFV
    560 570 580 590 600
    DHEFALNVLE GADDTVTISL SVDETLMSSS AQAIFLQQLD ALLIAFDKSA
    610 620 630 640 650
    PEISLSGLNA HFPLDLLSIA SSKVSAQYTS TVPPSHYIET WAKTHPEWKA
    660 670 680 690 700
    VEVATGFLGS QKIVTEDWTY KKLNETANQV ANLIIHASLH GRAIAVSLDR
    710 720 730 740 750
    SLIAFAIIVG IMKSGNTYVP IEAGLPNDRK SFLLRDSRAA MAFVCDNNFD
    760 770 780 790 800
    GVELPPETKV LDTKNQSFIE NLSTQDTSDI LNNYPENLDA YLLYTSGSTG
    810 820 830 840 850
    TPKGVRVSRH NLSSFSDAWG KLIGNVAPKS LELGGVGKFL CLASRAFDVH
    860 870 880 890 900
    IGEMFLAWRF GLCAVTGERL SMLDDLPRTF RELGVTHAGI VPSLLDQTGL
    910 920 930 940 950
    VPEDAPHLVY LGVGGEKMTP RTQQIWSSSD RVALVNVYGP TEVTIGCSAG
    960 970 980 990 1000
    RILPDSDTRC IGHPLGDSVA HVLAPGSNEH VKKGMAGELV IEGSLVANGY
    1010 1020 1030 1040 1050
    LNRPDAKGFC DINGRKMYRT GDIVRMDADS SILFLGRKDE QVKVRGQRLE
    1060 1070 1080 1090 1100
    LGEVSEVIRS LSPTDIDVVT LLLNHPGTSK QFLVSFVASS GAAVRGELRW
    1110 1120 1130 1140 1150
    INENYKEINN SLRQACEQTL PAYMVPDFII PISFIPLRDT SAKTDAKALE
    1160 1170 1180 1190 1200
    HMFHTLSLGE LFGESSSLVN KPTTAPSRDL TSIEKQILTV VKSVVGQDDK
    1210 1220 1230 1240 1250
    RDTRPRSTLF QLGLDSIASV KLSFKLKKLG FSTTVARLLQ NPTIEELGRM
    1260 1270 1280 1290 1300
    KNALKESHDA EPSNSESITT RFEELEKKTM NSLKDRETTH IESIRPCMPL
    1310 1320 1330 1340 1350
    QEVLVAHTMS HGSEADNAYV SHMIFELDPA VVVEHVKAAW AAVVKNTELL
    1360 1370 1380 1390 1400
    RTCFIDREND IVQLVIKENH ATPVWKHLSN GTNMLKEELL SCKKEIADDI
    1410 1420 1430 1440 1450
    VTNIDKSPPV RFTLASCDGA DETNEMSLFM LSIHHALYDM VSIEMIFQDF
    1460 1470 1480 1490 1500
    EVAYTDSSLP RRPSTLPLLE HIAAQQQNES KAKSYWTTLF DGYDHRIEKI
    1510 1520 1530 1540 1550
    SPRTAQTTAR TLNASLTTLE SLCSQTNMTL SALIQGVFAY VLARTLKRPD
    1560 1570 1580 1590 1600
    LIFGVVLSGR SIDVEGIDAM AAPCISTIPQ RLNIGTDGET IAELITTVQD
    1610 1620 1630 1640 1650
    RLFKSMEYQY TSLRSLSRWL EISGPLFSSL FSFTKLSPPE DSGSSKSRIL
    1660 1670 1680 1690 1700
    KPTEGEMFLD FELALECEAD PGTDTVTLRT RSTMFDKMEE LDALLEQMES
    1710 1720 1730 1740 1750
    LVTSFTRGEN KAVDGDFGSM LHTRLLPPHG SLQEESDDWS VLEQQIRDVV
    1760 1770 1780 1790 1800
    VAFSGALPNE VKRTTPFIKY GIDSITTIRF STLLRKNGFW VSGADVLRNP
    1810 1820 1830 1840 1850
    SVAKLATHIQ TTSSFNGTAK DSDNEASEPA GIGNWSKALL AGAVSTKVLD
    1860 1870 1880 1890 1900
    DVVAVYPLTP LQAGMISATV MMDPTLYAHH HPFRLPQGTS IDQVRSAWSR
    1910 1920
    LVAKHDILRT SFHEINQPRP QLVGAVHQ
    Length:1,928
    Mass (Da):214,117
    Last modified:February 6, 2013 - 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:i969E7AB22C01B7F8
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section is used for sequence fragments to indicate that the residue at the extremity of the sequence is not the actual terminal residue in the complete protein sequence.<p><a href='/help/non_ter' target='_top'>More...</a></p>Non-terminal residuei1Imported1
    Non-terminal residuei1928Imported1

    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
    JN132404 Genomic DNA Translation: AET13876.1

    <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
    JN132404 Genomic DNA Translation: AET13876.1

    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
    3ITEX-ray2.00A/B617-1174[»]
    SMRiK7NCP5
    ModBaseiSearch...
    PDBe-KBiSearch...

    Family and domain databases

    Gene3Di1.10.1200.10, 3 hits
    3.30.559.10, 3 hits
    3.40.50.12780, 1 hit
    InterProiView protein in InterPro
    IPR036736 ACP-like_sf
    IPR020845 AMP-binding_CS
    IPR000873 AMP-dep_Synth/Lig
    IPR042099 AMP-dep_Synthh-like_sf
    IPR023213 CAT-like_dom_sf
    IPR001242 Condensatn
    IPR020806 PKS_PP-bd
    IPR009081 PP-bd_ACP
    IPR006162 Ppantetheine_attach_site
    PfamiView protein in Pfam
    PF00501 AMP-binding, 1 hit
    PF00668 Condensation, 2 hits
    PF00550 PP-binding, 3 hits
    SMARTiView protein in SMART
    SM00823 PKS_PP, 3 hits
    SUPFAMiSSF47336 SSF47336, 3 hits
    PROSITEiView protein in PROSITE
    PS00455 AMP_BINDING, 1 hit
    PS50075 CARRIER, 3 hits
    PS00012 PHOSPHOPANTETHEINE, 2 hits

    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 nameiSIDN_EPIFI
    <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: K7NCP5
    <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: June 20, 2018
    Last sequence update: February 6, 2013
    Last modified: September 18, 2019
    This is version 41 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. SIMILARITY comments
      Index of protein domains and families
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
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