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Database: UniProt
Entry: B6QUN9_TALMQ
LinkDB: B6QUN9_TALMQ
Original site: B6QUN9_TALMQ 
ID   B6QUN9_TALMQ            Unreviewed;       556 AA.
AC   B6QUN9;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=Exo-beta-1,3-glucanase, putative {ECO:0000313|EMBL:EEA18713.1};
GN   ORFNames=PMAA_009960 {ECO:0000313|EMBL:EEA18713.1};
OS   Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS   (Penicillium marneffei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=441960 {ECO:0000313|EMBL:EEA18713.1, ECO:0000313|Proteomes:UP000001294};
RN   [1] {ECO:0000313|Proteomes:UP000001294}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18224 / CBS 334.59 / QM 7333
RC   {ECO:0000313|Proteomes:UP000001294};
RX   PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA   Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT   "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT   (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT   (ATCC10500).";
RL   Genome Announc. 3:E0155914-E0155914(2015).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR   EMBL; DS995906; EEA18713.1; -; Genomic_DNA.
DR   RefSeq; XP_002153098.1; XM_002153062.1.
DR   AlphaFoldDB; B6QUN9; -.
DR   STRING; 441960.B6QUN9; -.
DR   VEuPathDB; FungiDB:PMAA_009960; -.
DR   HOGENOM; CLU_002540_1_1_1; -.
DR   OrthoDB; 3714838at2759; -.
DR   PhylomeDB; B6QUN9; -.
DR   Proteomes; UP000001294; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004650; F:polygalacturonase activity; IEA:InterPro.
DR   Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 2.
DR   InterPro; IPR024535; Pectate_lyase_SF_prot.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   InterPro; IPR039279; QRT3-like.
DR   PANTHER; PTHR33928:SF2; PECTATE LYASE SUPERFAMILY PROTEIN DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR33928; POLYGALACTURONASE QRT3; 1.
DR   Pfam; PF12708; Pectate_lyase_3; 2.
DR   SUPFAM; SSF51126; Pectin lyase-like; 2.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001294};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..556
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002848484"
FT   DOMAIN          123..346
FT                   /note="Pectate lyase superfamily protein"
FT                   /evidence="ECO:0000259|Pfam:PF12708"
FT   DOMAIN          472..532
FT                   /note="Pectate lyase superfamily protein"
FT                   /evidence="ECO:0000259|Pfam:PF12708"
SQ   SEQUENCE   556 AA;  58092 MW;  0126A319F794BCED CRC64;
     MAKLLGLLLA LPFLARALPA DTLAARADHS SNDPTFNVSQ FVSNDSYKPH KTGIPFTLLD
     TSIQPWAKLN QPLKTEAVAN IDAATTCTPL AASNPSTWWY ESIAHNGLSS FMSSNYRSNY
     AVFRNVVTDY GADNTGATDA SKAIQNAINA GPSNGGPVRG SGNYGTTGQP AVVYLPAGTY
     LMSKNIQLLV GTVLVGDPIN PPTLKATSSF PNDHIVYAKD PNYGGTINFY IGIKNIIIDS
     TAVNGATNIA LLDWTVSQAT QLSNVVFNMP DYSTGHVGVT SQYDSNSNII LNDLTFNGGA
     YGLKLSGQQW ILKNIKTSGT TTGISAGGFS VVCQACSFEY AATGIDATGV SGTTTVIDSS
     GLNLGVFLKG TNSGGAVNSV VLENVSYDGT TVSMSGSTVL SGSVTDTWVY GHLYSSGSSS
     SSPVTGRTVT TPRSSSLLSN GRYFITEKPL TFQEYSINQV LNIKSVAGLP VYGDGSTDDT
     ANINSILSKY AGCKVIYFPA GTYIVTNTIF IPAGSRIYGD AYGTAISAIG SNYYNPNAPG
     TMVRVGNSGD VGVANC
//
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