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Database: UniProt
Entry: A0A1V6TMG8_9EURO
LinkDB: A0A1V6TMG8_9EURO
Original site: A0A1V6TMG8_9EURO 
ID   A0A1V6TMG8_9EURO        Unreviewed;       574 AA.
AC   A0A1V6TMG8;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Glycoside hydrolase family 5 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PENFLA_c006G07603 {ECO:0000313|EMBL:OQE27029.1};
OS   Penicillium flavigenum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=254877 {ECO:0000313|EMBL:OQE27029.1, ECO:0000313|Proteomes:UP000191342};
RN   [1] {ECO:0000313|Proteomes:UP000191342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 14082 {ECO:0000313|Proteomes:UP000191342};
RX   PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA   Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA   Frisvad J.C., Workman M., Nielsen J.;
RT   "Global analysis of biosynthetic gene clusters reveals vast potential of
RT   secondary metabolite production in Penicillium species.";
RL   Nat. Microbiol. 2:17044-17044(2017).
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:OQE27029.1}.
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DR   EMBL; MLQL01000006; OQE27029.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V6TMG8; -.
DR   STRING; 254877.A0A1V6TMG8; -.
DR   OrthoDB; 1329388at2759; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000191342; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000191342};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..574
FT                   /note="Glycoside hydrolase family 5 domain-containing
FT                   protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012663982"
FT   DOMAIN          60..325
FT                   /note="Glycoside hydrolase family 5"
FT                   /evidence="ECO:0000259|Pfam:PF00150"
FT   DOMAIN          368..452
FT                   /note="Carbohydrate binding X2"
FT                   /evidence="ECO:0000259|Pfam:PF03442"
SQ   SEQUENCE   574 AA;  61826 MW;  7B3CF7732FC5B1A5 CRC64;
     MQILLSVIVT LGIARRATAL PTGAVCTGTF SAISAADFVS NLHPGWNLGN TLDAIPDEGS
     WNNVPVVAST FDTVKDAGFK SVRLPVTWAD HFTGSSPDWT VDATWLERVS DVVDMIVSRG
     LYAIVDVHHD SWVWADVTQS GANLTMIEEK FYSLWYQIGT KLACKSNLVA FEPINEPPCN
     TAADGTEINK LNKIFLQAIN DAGGFNSQRV VTLVGGGQDS IKTADWFVAP SGFSNPYAIQ
     FHYYSPYDFI FSAWGKTIWG SDSDKSAVQS DFQRLRNTFP DVPLLLGEYD ASPTNTEPAA
     RWKYVDFLIK TAASLDISCV LWDNGLDHLD RTTGVWRDTN SLSIITKSTE STANSLPDST
     EDASATTQSS SAYIFHQYGT DVTEQTLPFI FNGNKLSSIS DSTGSTLSGT DYSVSGANII
     FTASYLSKHL SSTTAPGVIA TLTLKFSGGD SSPVIQIVQW KAPTLSSTSA VASSVSGSDL
     SIPITWGGLP TVAAVKALTK SGKYLVDDWT VSLGPIQQAR ATYSSQYNWD DSHVILTSSA
     ISSVISAGQS TVFTFEFFPR DNGVVNAVNF TLTV
//
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