ID A0A135LU19_PENPA Unreviewed; 791 AA.
AC A0A135LU19;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Concanavalin A-like lectin/glucanase, subgroup {ECO:0000313|EMBL:KXG52477.1};
GN ORFNames=PGRI_087610 {ECO:0000313|EMBL:KXG52477.1};
OS Penicillium patulum (Penicillium griseofulvum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=5078 {ECO:0000313|EMBL:KXG52477.1, ECO:0000313|Proteomes:UP000070168};
RN [1] {ECO:0000313|EMBL:KXG52477.1, ECO:0000313|Proteomes:UP000070168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PG3 {ECO:0000313|EMBL:KXG52477.1,
RC ECO:0000313|Proteomes:UP000070168};
RX PubMed=26729047; DOI=10.1186/s12864-015-2347-x;
RA Banani H., Marcet-Houben M., Ballester A.R., Abbruscato P.,
RA Gonzalez-Candelas L., Gabaldon T., Spadaro D.;
RT "Genome sequencing and secondary metabolism of the postharvest pathogen
RT Penicillium griseofulvum.";
RL BMC Genomics 17:19-19(2016).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KXG52477.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LHQR01000026; KXG52477.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135LU19; -.
DR STRING; 5078.A0A135LU19; -.
DR OMA; FAIHICT; -.
DR OrthoDB; 1891044at2759; -.
DR Proteomes; UP000070168; Unassembled WGS sequence.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd18617; GH43_XynB-like; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR021833; DUF3425.
DR InterPro; IPR041542; GH43_C2.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR42812; BETA-XYLOSIDASE; 1.
DR PANTHER; PTHR42812:SF12; BETA-XYLOSIDASE-RELATED; 1.
DR Pfam; PF11905; DUF3425; 1.
DR Pfam; PF17851; GH43_C2; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lectin {ECO:0000313|EMBL:KXG52477.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000070168}.
FT DOMAIN 329..516
FT /note="Beta-xylosidase C-terminal Concanavalin A-like"
FT /evidence="ECO:0000259|Pfam:PF17851"
FT REGION 531..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..563
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..592
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 14
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 193
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 132
FT /note="Important for catalytic activity, responsible for
FT pKa modulation of the active site Glu and correct
FT orientation of both the proton donor and substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-2"
SQ SEQUENCE 791 AA; 90885 MW; 7946449BA74FB19F CRC64;
MSYVNPIIPG FNPDPSIIRV GKDFFLVTST FEYFPGVPIY HSQDLIQWRL IGHALTRTSQ
LQIHTPEPGG GVWATTIRYH AGVYYIMAAS FQRYRPQQDD RVWPQGFYVK TTDIWNDKTW
SDPIYFDQVG FDQDLFWDDD GTVYLSSTYR KTQPTAGAKL KDFAIHICTV DLATGHSTSA
PKLIRESSSG VSEGSHIFKR GRYWYLFTAE GGTESGHSEW VNRSEVGPLG PWELGPNNPL
WRNGVEDEVQ NTGHADLVED TKGQWWAVVL GVRPVRKGDT WEESVLGRET FLVPLEWKDD
WPVINGGQKI SLNSYGPGLY EFNIAVSWRD EFSETQMQVG WYRKNTPFVN DYSLTEHPNH
LRLYGGPYNL SVPASPTMFL RKQTHRHCRW QTMLSFQPTV EETEAGTVVW LNYFTYSSIG
IRKDSKGRFI RFRPSEGDMV EHRLDTNTAV TLTIDCGTEY RFGYHEDTES DIHWIGSVSN
SAATAAPPVG ANFTGMMLGL YAFGERQRCL APADFADHII SVSDDAEQVT DDWSGLTDPI
ERRRRQNRIN QRAYRKRKRL ASTKDVHPKS LVPSPHSTPT TQLQNRPSQD NPPVRLYRNH
ETLQDLLEKF AKSAYESYIR GIPTADHLIT LTRVNVFRAF THNLRLIGSS ENWMDDDAIS
PFNTALPHNP STPDNTSLIP ANLQPTRIQK TIKHHPWLDF FPFPKMRDNL IEAEDNWDDA
QLCHDIMGFW GESTMDTGLL VWGEPWNMQN WEVTESFLKK YQWVVRGCPE LMNATNSWRA
RRGEKLIFRY I
//