ID A0A177CHR4_9PLEO Unreviewed; 662 AA.
AC A0A177CHR4;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Endoglucanase Cel5C {ECO:0000313|EMBL:OAG06846.1};
GN ORFNames=CC84DRAFT_628004 {ECO:0000313|EMBL:OAG06846.1};
OS Paraphaeosphaeria sporulosa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Didymosphaeriaceae;
OC Paraphaeosphaeria.
OX NCBI_TaxID=1460663 {ECO:0000313|EMBL:OAG06846.1, ECO:0000313|Proteomes:UP000077069};
RN [1] {ECO:0000313|EMBL:OAG06846.1, ECO:0000313|Proteomes:UP000077069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP3s5-JAC2a {ECO:0000313|EMBL:OAG06846.1,
RC ECO:0000313|Proteomes:UP000077069};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; KV441551; OAG06846.1; -; Genomic_DNA.
DR RefSeq; XP_018037211.1; XM_018186934.1.
DR AlphaFoldDB; A0A177CHR4; -.
DR STRING; 1460663.A0A177CHR4; -.
DR GeneID; 28770420; -.
DR InParanoid; A0A177CHR4; -.
DR OrthoDB; 1329388at2759; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000077069; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0030248; F:cellulose binding; IEA:InterPro.
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; IPR035971; CBD_sf.
DR InterPro; IPR000254; Cellulose-bd_dom_fun.
DR InterPro; IPR001547; Glyco_hydro_5.
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; PF00734; CBM_1; 1.
DR Pfam; PF03442; CBM_X2; 1.
DR Pfam; PF00150; Cellulase; 1.
DR SMART; SM00236; fCBD; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF57180; Cellulose-binding domain; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR PROSITE; PS00562; CBM1_1; 1.
DR PROSITE; PS51164; CBM1_2; 1.
PE 3: Inferred from homology;
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023295};
KW Reference proteome {ECO:0000313|Proteomes:UP000077069};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..662
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008058188"
FT DOMAIN 19..55
FT /note="CBM1"
FT /evidence="ECO:0000259|PROSITE:PS51164"
SQ SEQUENCE 662 AA; 70887 MW; CFE058EE3964F5C3 CRC64;
MVARLGLLLF GALVQGAVAA NGPYAQCGGT GYTGETTCPS GYTCKVQNEW YYQCVPGTAA
SSAVSSARTS SSSAVSTKPS TTLVTSSTKS ASTSASASAS ASASASATSG AGVKCTGTFT
PVSASAFVKN INPGWNLGNT LDAVEDEGDW NNPKVTADTF DDIKAAGFKG VRLPVTWAYH
FTTGSPSWDV DPAWLQRVSD VTDMITTRGF YTIVNVHHDS WVWADVTAAG ANLTMIEEKF
YRLWYQIGTK LACKGSQVAF EPINEPPGTT AAHADEINKL NTIFLQAISD AGGFNAQRVV
TLVGAGEDSI KTSQWFKRPD AKFKNPWAIQ YHYYSPYDFI FSAWGKTIWG SDADKAALDA
DFAAIRNNFT DVPLIIGEWD ASYTNTETAA RWKYFDFLIR TANKYNTATV LWDNGLDQFD
RINHVWRDPT VLSILTNTTA GTTNSLPDST TDGSVTTQFS SAYAYHKAGD AVTDVVLPYL
FNGNTVSSIK NAKTGAVLTK GADYSTNSSA IILTSAFVKT VITSSTATGS LANLTVTFSS
GAPNTIEVVQ YATPVLGSTT AKLPATSADL PIPITWKGQS RPAAVKAIKS DGGILIDDWT
QYLGPLQQGR MTYSGQWDWD ANNVILKATV LDAVRSAGKT TTFTFEFYPR EPTNVANFTL
TV
//
