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Entry version 76 (12 Aug 2020)
Sequence version 1 (05 Jul 2004)
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Protein

Nonribosomal peptide synthetase sirP

Gene

sirP

Organism
Leptosphaeria maculans (Blackleg fungus) (Phoma lingam)
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>
-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

Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of sirodesmin PL, an epipolythiodioxopiperazine (ETP) characterized by a disulfide bridged cyclic dipeptide and that acts as a phytotoxin which is involved in the blackleg didease of canola (PubMed:15387811, PubMed:18272357, PubMed:19762440). SirD catalyzes the O-prenylation of L-tyrosine (L-Tyr) in the presence of dimethylallyl diphosphate (DMAPP) to yield 4-O-dimethylallyl-L-Tyr, and therefore represents probably the first pathway-specific enzyme in the biosynthesis of sirodesmin PL (PubMed:19762440, PubMed:21038099, PubMed:24083562). 4-O-dimethylallyl-L-Tyr, then undergoes condensation with L-Ser in a reaction catalyzed by the non-ribosomal peptide synthase sirP to form the diketopiperazine (DKP) backbone (PubMed:18272357). Further bishydroxylation of the DKP performed by the cytochrome P450 monooxygenase sirC leads to the production of the intermediate phomamide (PubMed:27390873). This step is essential to form the reactive thiol group required for toxicity of sirodesmin PL (PubMed:27390873). The next steps of sirodesmin biosynthesis are not well understood yet, but some predictions could be made from intermediate compounds identification (PubMed:18272357). Phomamide is converted into phomalizarine via oxidation, probably by sirT (PubMed:18272357). Further oxidation, methylation (by sirM or sirN) and reduction steps convert phomalizarine to deacetyl sirodesmin (PubMed:18272357). Finally, acetyltransferase sirH probably acetylates deacetyl sirodesmin to produce sirodesmin PL (PubMed:18272357).2 Publications4 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.

<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 functionIsomerase, Ligase
Biological processVirulence

<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:
Nonribosomal peptide synthetase sirP1 Publication (EC:6.3.2.-1 Publication)
Short name:
NRPS sirPCurated
Alternative name(s):
Sirodesmin biosynthesis protein P1 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:sirP1 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>OrganismiLeptosphaeria maculans (Blackleg fungus) (Phoma lingam)
<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 identifieri5022 [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 lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaDothideomycetesPleosporomycetidaePleosporalesPleosporineaeLeptosphaeriaceaeLeptosphaeriaLeptosphaeria maculans species complex

<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

Impairs the production of sirodesmin PL (PubMed:15387811, PubMed:20507539). Decreases the number of lesions and the efficiency in colonizing stems during infection of canola (PubMed:20507539).2 Publications

<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_00004377001 – 2176Nonribosomal peptide synthetase sirPAdd BLAST2176

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 residuei571O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1
Modified residuei1606O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1
Modified residuei2140O-(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

Expressed during canola infection (PubMed:20507539). Expression is co-regulated with the other genes from the sirodesmin cluster and corresponds with sirodesmin production (PubMed:15387811).2 Publications

<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
Q6Q883

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>Domaini534 – 610Carrier 1PROSITE-ProRule annotationAdd BLAST77
Domaini1570 – 1646Carrier 2PROSITE-ProRule annotationAdd BLAST77
Domaini2106 – 2176Carrier 3PROSITE-ProRule annotationAdd BLAST71

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>Regioni51 – 434Adenylation 1Sequence analysisAdd BLAST384
Regioni643 – 1073Condensation 1Sequence analysisAdd BLAST431
Regioni1094 – 1474Adenylation 2Sequence analysisAdd BLAST381
Regioni1661 – 2070Condensation 2Sequence analysisAdd BLAST410

<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, epimerase (E) domains (responsible for L- to D-amino acid conversion) are present within the NRP synthetase (By similarity). NRPS10 has the foolowing architecture: A-T-C-A-T-C (PubMed:15387811).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, 2 hits
3.40.50.12780, 2 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR010071, AA_adenyl_domain
IPR036736, ACP-like_sf
IPR025110, AMP-bd_C
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, 2 hits
PF13193, AMP-binding_C, 1 hit
PF00668, Condensation, 2 hits
PF00550, PP-binding, 2 hits

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00823, PKS_PP, 2 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF47336, SSF47336, 3 hits

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
PS50075, CARRIER, 3 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.

Q6Q883-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MHITKDIDTI FHRSLEGLTG DDHSPESRRD FPMSQSSGCR NGTDATVCHI
60 70 80 90 100
FERIASQFPE SVAAEDGGRN ITYGELHYAS NHLANHLSQI GIQSGQKIVI
110 120 130 140 150
ISNRSLEMIV ALLGIMKSGA CVVPIDFETW SQDRIQTTLE TTQCRYAIST
160 170 180 190 200
KCIEIPNQEL ILFQEGDLQH VLDNRRDQPA SFSTRGFQLP SADDLAYTIF
210 220 230 240 250
TSGTTSKPKG VMVPHSAIAH YVQQVSDEAP FNLNVQASSR VLLVFSVAFD
260 270 280 290 300
ACLGVVLSTI CNGGTLILAT SMNFATVATT CTILPLTPTI LSTLRPGAEY
310 320 330 340 350
DSIKSIFLGG ESPSPNLLRP WLNGERRIFN CYGPTETTCT SLIKEVLPDE
360 370 380 390 400
PNHLRYTVAG SSVVLLDGNL REVSEGEIAI SGPGLAVGYF NNQALTAEKF
410 420 430 440 450
IVYKGVRHYL TGDYGRKTSF GIDFLGRKDR VVKNRGFLIN LEAEVEAVIT
460 470 480 490 500
NMKLANSAAA LMHEGRLIMF VTPETIDVSS LRSRLLEIRD SFLVPDRIYA
510 520 530 540 550
ICSFPITSNG KVDLASLRQL LQEEKFTGVA THQSSPSSNL YVVLEGFSKV
560 570 580 590 600
LGLPPSALCG SSSFLDNGGN SLSAVSLASH LRERGLSITV REIFESDTAQ
610 620 630 640 650
RICDTLSATI LSTSDSEEAD LESLRENVVR AGYPLTPRME VAYMTAIQVN
660 670 680 690 700
MIQSTIKMPS MNYIQLSITF DLSSGLFKPE VFRRAWEIIV QRHSILRATF
710 720 730 740 750
IPALEATVIA ADPTMDWREQ LVDSSEWDSA VADAREKILC SMAPLDAEYL
760 770 780 790 800
KPRSIFRLIT EPKSRTEFIW TIHHSLVDGW SIAVIMRDLQ CILSQEELPK
810 820 830 840 850
VAQFTSVATV QKALAQRSLS RGKQQSWEEK MQNYIPAPRL RLPKPQGWAR
860 870 880 890 900
AARAERRQLL GVHRSQVQRF VQEYRVSDAS IFLASWALVL SKYLSTDRVL
910 920 930 940 950
FGVVLSGRNL PMAAVDQVVG PLLDTVPFPV NTTSTQSTAE FLRTIHGTLH
960 970 980 990 1000
EMNESPWEMK LQKSSMGPES LETLVALQYD LPDSTWNVDP KTWPSPQSMK
1010 1020 1030 1040 1050
HNETTELPLH ILIDMQNGGD LEARYLYDCS HFEAAMIDQM LSHFSNMLKA
1060 1070 1080 1090 1100
ILMHPTVELV KSSMMNQLEI NDLLYSSPHM HDAYDGPQSL KQAFEEVVDT
1110 1120 1130 1140 1150
WPDAIAVESV SDSISYKELD HRSSAISNAL LPLVGPGQIV GILSDGSVSW
1160 1170 1180 1190 1200
ITAILAVLKA GAAYCPIDIA LPEERIKVML RESRCSLLLC TTEDLCELWA
1210 1220 1230 1240 1250
NHSDLTCFSI GRLLSETLQT PERLPERCSP HDPAAVIFTS GSTGVPKGIL
1260 1270 1280 1290 1300
LEHIGILSLL DFPNARLRSG PGRRNAQFLS LGFDCCVNEV FATLCYGATL
1310 1320 1330 1340 1350
VLRDPLDPVQ HIKRVHATMC TPSFLATLDV NDFPNLELIA LAGEPVPQKL
1360 1370 1380 1390 1400
VDTWGHNRVL LNVYSPSECT ISTVYPQLYP GVQVTLGSPV PRQAIYILDK
1410 1420 1430 1440 1450
DLNPVPVGVP GEICISGIQV TRGYLNRPEE TLVKFLPNPF QKGWRLYRSG
1460 1470 1480 1490 1500
DLGRLTNSHE IEYIGRIDNQ VKVRGFRIEL EEIESTIAAL NPEVRQAAVI
1510 1520 1530 1540 1550
VVNDVLIGFV TPSSLDTLAI QAIISRHLPS YCRPSYFVAL DNMPMSSNQK
1560 1570 1580 1590 1600
IDRKKLVSMK AERNHFTKVP IEGTTERIIQ EIWKDLIPEL GEVSALDNFL
1610 1620 1630 1640 1650
QIGGHSLLQA RLTRQLGMAL GNRIPLRIVI QNPVLRDLAL AIDKHILDGG
1660 1670 1680 1690 1700
SEDISRGQPE QNTVLSHLEE EMYTVHMLSS EPSAWNIPYI ARLTGPLNLA
1710 1720 1730 1740 1750
AFEASWNNII RSNSILRARY QIKDGILTRS ISTSISPVTR RYCKVTDDAL
1760 1770 1780 1790 1800
LDIVNRAFDL ANDQPIRLDL CLDRPTMSYV VLNMSHMIGD RSTMGEILRL
1810 1820 1830 1840 1850
LEEEYAQMIL NDNFNLHEPL SESLPYSVWT AMRRKREVDA GLTHVLQKSL
1860 1870 1880 1890 1900
NPSLINPPLF GTFKQELACS AHRDKRIEGD LFSSLKNLRG RFKASGHQLA
1910 1920 1930 1940 1950
IAAIGLTLHR LSHREDFIIA APIEDRTEAG TENMFGLFLD RLLIPLRFNL
1960 1970 1980 1990 2000
HSPHSADDLI HMVKSASEQA MANYIPFADL KNVLGMVGKS HSLCEIMVTY
2010 2020 2030 2040 2050
HASDLQGPNL TGVDALGIPV QPKGVKFPLM LEFSEFPESI GIDLAYDSHA
2060 2070 2080 2090 2100
IDNATMDEFE VQLMAAFRYL ADETCSSTCT TYPPRLFPLI WSQKDTNTVA
2110 2120 2130 2140 2150
PISEDQEMID LVREAMAECV GLNRCDISCS RSFFELGGSS VDCLRLQDRL
2160 2170
IKSGVSVSLS SIIHLQTAEL IAGAVE
Length:2,176
Mass (Da):241,505
Last modified:July 5, 2004 - 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:iE86AA7AD4D5136D8
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AY553235 Genomic DNA Translation: AAS92545.1

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY553235 Genomic DNA Translation: AAS92545.1

3D structure databases

SMRiQ6Q883
ModBaseiSearch...

Family and domain databases

Gene3Di1.10.1200.10, 3 hits
3.30.559.10, 2 hits
3.40.50.12780, 2 hits
InterProiView protein in InterPro
IPR010071, AA_adenyl_domain
IPR036736, ACP-like_sf
IPR025110, AMP-bd_C
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, 2 hits
PF13193, AMP-binding_C, 1 hit
PF00668, Condensation, 2 hits
PF00550, PP-binding, 2 hits
SMARTiView protein in SMART
SM00823, PKS_PP, 2 hits
SUPFAMiSSF47336, SSF47336, 3 hits
TIGRFAMsiTIGR01733, AA-adenyl-dom, 1 hit
PROSITEiView protein in PROSITE
PS00455, AMP_BINDING, 1 hit
PS50075, CARRIER, 3 hits
PS00012, PHOSPHOPANTETHEINE, 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 nameiSIRP_LEPMC
<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: Q6Q883
<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: November 2, 2016
Last sequence update: July 5, 2004
Last modified: August 12, 2020
This is version 76 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
  2. SIMILARITY comments
    Index of protein domains and families
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