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UniProtKB - Q4WMJ7 (GLIP_ASPFU)

Entry version 115 (23 Feb 2022)
Sequence version 1 (05 Jul 2005)
Previous versions | rss
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Protein

Nonribosomal peptide synthetase gliP

Gene

gliP

Organism
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Status
Reviewed-Annotation score:

Annotation score:5 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 synthetase; part of the gene cluster that mediates the biosynthesis of gliotoxin, a member of the epipolythiodioxopiperazine (ETP) class of toxins characterized by a disulfide-bridged cyclic dipeptide (PubMed:15979823, PubMed:16757745, PubMed:16956378, PubMed:21612254).

The first step in gliotoxin biosynthesis is the condensation of serine and phenylalanine to form the cyclo-L-phenylalanyl-L-serine diketopiperazine (DKP) by the NRPS gliP (PubMed:17154540, PubMed:21612254).

GliP is also able to produce the DKP cyclo-L-tryptophanyl-L-serine, suggesting that the substrate specificity of the first adenylation (A) domain in gliP is sufficiently relaxed to accommodate both L-Phe and L-Trp (PubMed:23434416).

The cytochrome P450 monooxygenase gliC has been shown to catalyze the subsequent hydroxylation of the alpha-carbon of L-Phe in cyclo-L-phenylalanyl-L-serine whereas the second cytochrome P450 enzyme, gliF, is presumably involved in the modification of the DKP side chain (PubMed:24039048, PubMed:23434416).

The glutathione S-transferase (GST) gliG then forms a bis-glutathionylated biosynthetic intermediate which is responsible for the sulfurization of gliotoxin (PubMed:21513890, PubMed:21749092).

This bis-glutathionylated intermediate is subsequently processed by the gamma-glutamyl cyclotransferase gliK to remove both gamma-glutamyl moieties (PubMed:22903976, PubMed:24039048).

Subsequent processing via gliI yields a biosynthetic intermediate, which is N-methylated via the N-methyltransferase gliN, before the gliotoxin oxidoreductase gliT-mediated disulfide bridge closure (PubMed:20548963, PubMed:22936680, PubMed:24039048, PubMed:25062268).

GliN-mediated amide methylation confers stability to ETP, damping the spontaneous formation of tri- and tetrasulfides (PubMed:25062268).

Intracellular dithiol gliotoxin oxidized by gliT is subsequently effluxed by gliA (PubMed:26150413).

Gliotoxin contributes to pathogenesis during invasive aspergillosis (PubMed:17601876, PubMed:18199036).

In macrophages and neutrophils, gliotoxin showed inhibition of various different cell functions including cytokine production, antigen presentation, phagocytosis, and production of reactive oxygen species (PubMed:17601876).

14 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=51 µM for L-phenylalanine1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: 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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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
Biological processVirulence

Enzyme and pathway databases

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		Q4WMJ7

<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 gliP1 Publication (EC:6.3.2.-1 Publication)
Short name:
NRPS gliP1 Publication
Alternative name(s):
Gliotoxin 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:gliP1 Publication
Synonyms:NRPS101 Publication, pesK1 Publication
ORF Names:AFUA_6G09660
<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>OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
<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 identifieri330879 [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 lineageiEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Aspergillaceae › Aspergillus › Aspergillus 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
  • UP000002530 <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: Chromosome 6

Organism-specific databases

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		FungiDB:Afu6g09660

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

<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 gliotoxin production (PubMed:16757745, PubMed:16956378, PubMed:17601876). In vitro, the culture supernatant of the gliP-deficient strains show a reduced cytotoxic effect on both macrophage-like cells and T-cell lines. Shows attenuated virulence in nonneutropenic mice immunosuppressed with corticosteroids, but normal virulence in neutropenic mice (PubMed:18199036). It also has reduced virulence in a Drosophila melanogaster model (PubMed:18199036).4 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi204D → A: Impairs activation of L-phenylalanine. 1 Publication1
Mutagenesisi555S → A: Impairs loading of L-phenylalanine and formation of the dipeptide. 1 Publication1
Mutagenesisi1245D → A: Impairs activation of L-serine. 1 Publication1
Mutagenesisi1582S → A: Impairs loading of L-serine and formation of the dipeptide. 1 Publication1

<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_00004165511 – 2135Nonribosomal peptide synthetase gliPAdd BLAST2135

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 residuei555O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1
Modified residuei1582O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1
Modified residuei2095O-(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 positively regulated by the brlA and abaA transcription factors (PubMed:26032501).1 Publication

<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		746128.CADAFUBP00007375

<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		Q4WMJ7

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>Domaini519 – 594Carrier 1PROSITE-ProRule annotationAdd BLAST76
Domaini1544 – 1622Carrier 2PROSITE-ProRule annotationAdd BLAST79
Domaini2061 – 2134Carrier 3PROSITE-ProRule annotationAdd 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>Regioni34 – 424Adenylation 1Sequence analysisAdd BLAST391
Regioni663 – 913Condensation 1Sequence analysisAdd BLAST251
Regioni1078 – 1458Adenylation 2Sequence analysisAdd BLAST381
Regioni1642 – 1905Condensation 2Sequence analysisAdd BLAST264

<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 (PubMed:17464044). Each module is responsible for the recognition (via the A domain) and incorporation of a single amino acid into the growing peptide product (PubMed:17464044). 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 (PubMed:17464044). Occasionally, epimerase (E) domains (responsible for L- to D-amino acid conversion) are present within the NRP synthetase (PubMed:17464044). GliP has the following architecture: A-T-C-A-T-C-T (PubMed:17154540, PubMed:17464044).2 Publications

<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 synthetase family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1178, Eukaryota

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_000022_0_5_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q4WMJ7

Identification of Orthologs from Complete Genome Data

More...OMAi		WTTPDNG

Database of Orthologous Groups

More...OrthoDBi		4243at2759

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.1200.10, 3 hits
3.30.300.30, 2 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
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
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
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, 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, 2 hits
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.

Q4WMJ7-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPSVVALDLC QLFDRSVART PHQLAVDHES GSLTYTELDV ASSNLARKLK 
        60         70         80         90        100
QEGVVPGEAV LLLTEHGTRN VVALLAILKA HACYVPLDRS SWSSERIQAV 
       110        120        130        140        150
LDGTDSRILI NTTVEPFESP RHKVIHLTSA DVTTLSTDRS TTKVIPDIAP 
       160        170        180        190        200
EDLACLIFTS GSTGVPKGVM IPHRAVANYA QTSPFNMDVQ PGDRVLHILS 
       210        220        230        240        250
VSFDASTGML FSILGNSGIV VPATMDTLFD KAQSCSILAS TPSILATLPL 
       260        270        280        290        300
PTALPDSYPY VHTILLGGES PPAPLLSSWL QFGVRILNAY GPTETTCASL 
       310        320        330        340        350
MQEVEVCQET GMINRSIIGR PMPNGPVYLL QPDTLLPVEE EGEEGEIAIA 
       360        370        380        390        400
GVGLAHGYYR NAALTAEKFI EWHGKRVYRT GDQGRWTRRN DGQRVVEFRG 
       410        420        430        440        450
RSDRTVKNRG FLVNLPADVE EPLRQMGFGV TDVYASLING LLVALVTPAT 
       460        470        480        490        500
ADLDGLQSEA DRRLSSFHRP GRYLAVDQFP LSANGKIDTK AIENMLKEYQ 
       510        520        530        540        550
ARLCEGTDDE ETTGGERPTE REQVIAECMY TALGLDLPSA SASKDFNFFA 
       560        570        580        590        600
MGGNSLAALR FTSLCRERGI LLTTRDLYLH PTVRGILPYA RDLAHSGLPL 
       610        620        630        640        650
PDKEEQIDHR LSLKAEVAAA LHLLGDIDVA PLTPLQLQLS APIFQSDGTN 
       660        670        680        690        700
TNQLRQSYPL ASAEHICNAW RQVVLSEPVF RTQIALDIGP GVQIVHAQPR 
       710        720        730        740        750
CQPQEITFHR REDYNAALSD PSRLPVGLGM RLEFMKFMPN DDDDDEGEVT 
       760        770        780        790        800
VVWTAHHSLI DGYSLGLILA RVQQASQGVA SSRVSSFVDA AWNLLSVQKQ 
       810        820        830        840        850
RDTEARRFWE QYLQPVRSLT KAEATTTPVA RPYLAQEVLF KHVGGVDELH 
       860        870        880        890        900
RLASSCSVTL AAVYYTAWAM TIARTTKSTL VTLGVVFSGR EILPDDAQAV 
       910        920        930        940        950
GPLMATLPLV CRIDGEASIE RQLQTTFEGL ATISTYAWSA PDQIGYRVDS 
       960        970        980        990       1000
LLATQYDFPT YDQPIPPQKE QFFENTTFAL SLLVEADARF RLVYNPSVHG 
      1010       1020       1030       1040       1050
EQTVQQYADT FQQALQALVG DSTMEAWLTG PTKAPLAVDQ ASDIQHVNVP 
      1060       1070       1080       1090       1100
NVASAFYASV DLHKDLIAVD GPGGTLPYRE LDQKSNAVAS HIAKHFSRAQ 
      1110       1120       1130       1140       1150
VIAIHADGTL NWVVGILGIL KAGCAYCPLD PAYPIARRVA VYEQSGASAL 
      1160       1170       1180       1190       1200
LIPNACSSSA ALLPITDLRV FTIQETETSD TSRQPSLLAN ANEDALIVFT 
      1210       1220       1230       1240       1250
SGTTGRPKGV PISHRGLLAL QSNPEATMFS RPGRRIAQFM SPAFDYCANE 
      1260       1270       1280       1290       1300
IFSALLHGGT LVLRDPSDPL AHLAKVDVST ITPSVLSVLN PDDYPNLDMV 
      1310       1320       1330       1340       1350
YATGEPVTPG LLARWGEGRA FYNAYGPAEC SICTSFTRLE PGQQVTIGNA 
      1360       1370       1380       1390       1400
VRTARMYILD PDLQPVSDGQ TGEIFLAGQQ VMRGYVGDDA KTAYSVLPDP 
      1410       1420       1430       1440       1450
WHPGERMYRT GDYGYWNADR QIVYIGRLDR QVKIRGFRVE LAAVEQKMYQ 
      1460       1470       1480       1490       1500
EEPRLTQAAA LVVNDTLVAF VMPLDVDVSR LEQRLRESLQ PSWVPQVITA 
      1510       1520       1530       1540       1550
LEEFPWTANR KVDYRKLAER ATLTRPEDSL PQQKTPAGMT AKDASIADGI 
      1560       1570       1580       1590       1600
ATLWKNVLRL QAGGGSRKLC EDDDFRALGG HSVLQMMLAA RLGSTFGISV 
      1610       1620       1630       1640       1650
SMRDVIEHST LAEQVELVRR KRQASTAKPR TICDAFPDHC LSPLERQTWF 
      1660       1670       1680       1690       1700
QYLIAADVRT FNIPVLLHLG GTFDRDRLVQ SFNAVLASRK IFRTNFVETS 
      1710       1720       1730       1740       1750
LGPCRIFRDT PPRVLVCDGA LDTTKEIDRS FDLARDELIR VFLDRRTLLV 
      1760       1770       1780       1790       1800
VTSHAVADLN SVQNLLQDVS GVYAGRTTPT PDRWHYPRAP AWSRQATEQE 
      1810       1820       1830       1840       1850
RKFWSKYLEG APQRLDIPRY PGQMAFEGRS RVSEFKGDLV RRAVTLGQEH 
      1860       1870       1880       1890       1900
GLSQHQLVCA AVAQTLQWLA GSNDVVLGSP WANRGHTVEQ ESMGLFLDRL 
      1910       1920       1930       1940       1950
PLRFKTPVNA DCATILQSTR AASQAAVCNS IPFEQVLNLL HLPRTIRQHP 
      1960       1970       1980       1990       2000
LFEAMVTFHL KGAVEDCLAI EGLEVKREMC FASGAKFLLM FEWTEIEADH 
      2010       2020       2030       2040       2050
WTLRIEYDDH QLDDATVTTI EDSIRCVLEG LADRLSRAAI HERLNAMHKT 
      2060       2070       2080       2090       2100
ARTKVDWNFY RRLVGILQRE MATCLGVSLD EFPCSVSFFE AGGDSIQAWR 
      2110       2120       2130 
LSRQLKRVGL EVPICNIFDH PTAQDLAQRL YRQVL
Length:2,135
Mass (Da):235,835
Last modified:July 5, 2005 - 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:i435B5A722BE353A9
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 AAW03307 differs from that shown. Reason: Erroneous gene model prediction.Curated

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
AY838877 Genomic DNA Translation: AAW03307.1 Sequence problems.
DQ457015 mRNA Translation: ABE60889.1
AAHF01000006 Genomic DNA Translation: EAL88817.1

NCBI Reference Sequences

More...RefSeqi		XP_750855.1, XM_745762.1

Genome annotation databases

Ensembl fungal genome annotation project

More...EnsemblFungii		EAL88817; EAL88817; AFUA_6G09660

Database of genes from NCBI RefSeq genomes

More...GeneIDi		3508160

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		afm:AFUA_6G09660

<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
AY838877 Genomic DNA Translation: AAW03307.1 Sequence problems.
DQ457015 mRNA Translation: ABE60889.1
AAHF01000006 Genomic DNA Translation: EAL88817.1
RefSeqiXP_750855.1, XM_745762.1

3D structure databases

SMRiQ4WMJ7
ModBaseiSearch...

Protein-protein interaction databases

STRINGi746128.CADAFUBP00007375

Genome annotation databases

EnsemblFungiiEAL88817; EAL88817; AFUA_6G09660
GeneIDi3508160
KEGGiafm:AFUA_6G09660

Organism-specific databases

VEuPathDBiFungiDB:Afu6g09660

Phylogenomic databases

eggNOGiKOG1178, Eukaryota
HOGENOMiCLU_000022_0_5_1
InParanoidiQ4WMJ7
OMAiWTTPDNG
OrthoDBi4243at2759

Enzyme and pathway databases

SABIO-RKiQ4WMJ7

Family and domain databases

Gene3Di1.10.1200.10, 3 hits
3.30.300.30, 2 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
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
IPR020806, PKS_PP-bd
IPR009081, PP-bd_ACP
IPR006162, Ppantetheine_attach_site
PfamiView protein in Pfam
PF00501, AMP-binding, 2 hits
PF00668, Condensation, 2 hits
PF00550, PP-binding, 3 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, 2 hits
PS50075, CARRIER, 3 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 nameiGLIP_ASPFU
<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: Q4WMJ7
Secondary accession number(s): Q1PBG5, Q5MBT9
<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: April 18, 2012
Last sequence update: July 5, 2005
Last modified: February 23, 2022
This is version 115 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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