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Database: UniProt
Entry: A0A0A2L365_PENIT
LinkDB: A0A0A2L365_PENIT
Original site: A0A0A2L365_PENIT 
ID   A0A0A2L365_PENIT        Unreviewed;       590 AA.
AC   A0A0A2L365;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Glycoside hydrolase, superfamily {ECO:0000313|EMBL:KGO74459.1};
GN   ORFNames=PITC_021530 {ECO:0000313|EMBL:KGO74459.1};
OS   Penicillium italicum (Blue mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO74459.1, ECO:0000313|Proteomes:UP000030104};
RN   [1] {ECO:0000313|EMBL:KGO74459.1, ECO:0000313|Proteomes:UP000030104}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PHI-1 {ECO:0000313|EMBL:KGO74459.1,
RC   ECO:0000313|Proteomes:UP000030104};
RX   PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA   Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA   Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT   "Genome, transcriptome, and functional analyses of Penicillium expansum
RT   provide new insights into secondary metabolism and pathogenicity.";
RL   Mol. Plant Microbe Interact. 28:232-248(2015).
CC   -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004964}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC       {ECO:0000256|ARBA:ARBA00005641, ECO:0000256|RuleBase:RU361153}.
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:KGO74459.1}.
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DR   EMBL; JQGA01000614; KGO74459.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A2L365; -.
DR   STRING; 40296.A0A0A2L365; -.
DR   HOGENOM; CLU_018668_0_0_1; -.
DR   OMA; TVFTFEF; -.
DR   OrthoDB; 1329388at2759; -.
DR   PhylomeDB; A0A0A2L365; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000030104; Unassembled WGS sequence.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0005978; P:glycogen biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProt.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR005102; Carbo-bd_X2.
DR   InterPro; IPR001547; Glyco_hydro_5.
DR   InterPro; IPR016282; Glyco_hydro_5_endoGlcnase_B.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   PANTHER; PTHR31297:SF41; ENDOGLUCANASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_5G01830)-RELATED; 1.
DR   PANTHER; PTHR31297; GLUCAN ENDO-1,6-BETA-GLUCOSIDASE B; 1.
DR   Pfam; PF03442; CBM_X2; 1.
DR   Pfam; PF00150; Cellulase; 1.
DR   PIRSF; PIRSF001043; Endoglucanase_B; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
PE   3: Inferred from homology;
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361153};
KW   Hydrolase {ECO:0000256|RuleBase:RU361153, ECO:0000313|EMBL:KGO74459.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030104};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..590
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002002014"
FT   DOMAIN          76..341
FT                   /note="Glycoside hydrolase family 5"
FT                   /evidence="ECO:0000259|Pfam:PF00150"
FT   DOMAIN          384..468
FT                   /note="Carbohydrate binding X2"
FT                   /evidence="ECO:0000259|Pfam:PF03442"
SQ   SEQUENCE   590 AA;  63051 MW;  AF7F0CAC23B635EB CRC64;
     MQILLSGALV ALAGIAQAAT TTLTTTTKST VQAAAASTGA VCTGTFNAIS AADFVSNLHP
     GWNLGNTLDA VPNEGSWNNI PVVGSTFDTV KAAGFKSVRL PVTWAYHFTG SSPDWTVDPT
     WLQRVSDVVD MIVARGLYAI VDVHHDSWVW ADFSQSGANL TMIEEKFYSL WYQIGTKLAC
     KSNLVAFEPI NEPPCNTAAD GAELNKLNKI FLQAINDAGG FNSKRVVTLV GGSEDSIKTA
     DWFVAPSGFS NPYAIQFHYY SPYDFIFSAW GKTIWGSDSD KTAVQSDFQR LRNAFPNVPL
     VLGEYDASPT NTEPAARWKY VDFLIKTAAS LDISCVLWDN GLDHLDRTTG VWRDPNSLSI
     ITKSTESTAN SLPDSTEDGY APTQSSSAYI FHQYGTAVTA QTLPFLFNGN TLSSISDSTG
     STLSGTDYSV SGANIVFTAS YLSTHLSATT APGVIATLTL KFSGGDSSPV IQIVQWKAPT
     LSSTSAVASS VSGSDLSIPI TWGGLRTVAA VKALTKSGTY LVDDWTVSLG PLQKARATYS
     SQYNWDDSHV ILTSSAISSV ISAGQSTVFT FEFFPRDNGA VNAVNFTLTL
//
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