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Database: UniProt
Entry: A0A177E4Z2_ALTAL
LinkDB: A0A177E4Z2_ALTAL
Original site: A0A177E4Z2_ALTAL 
ID   A0A177E4Z2_ALTAL        Unreviewed;       576 AA.
AC   A0A177E4Z2;
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 B {ECO:0000313|EMBL:OAG26292.1};
GN   ORFNames=CC77DRAFT_1027366 {ECO:0000313|EMBL:OAG26292.1};
OS   Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC   Alternaria sect. Alternaria; Alternaria alternata complex.
OX   NCBI_TaxID=5599 {ECO:0000313|EMBL:OAG26292.1, ECO:0000313|Proteomes:UP000077248};
RN   [1] {ECO:0000313|EMBL:OAG26292.1, ECO:0000313|Proteomes:UP000077248}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRC1lrK2f {ECO:0000313|EMBL:OAG26292.1,
RC   ECO:0000313|Proteomes:UP000077248};
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, ECO:0000256|RuleBase:RU361153}.
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DR   EMBL; KV441469; OAG26292.1; -; Genomic_DNA.
DR   RefSeq; XP_018391713.1; XM_018526363.1.
DR   AlphaFoldDB; A0A177E4Z2; -.
DR   STRING; 5599.A0A177E4Z2; -.
DR   GeneID; 29111957; -.
DR   KEGG; aalt:CC77DRAFT_1027366; -.
DR   VEuPathDB; FungiDB:CC77DRAFT_1027366; -.
DR   OMA; TVFTFEF; -.
DR   OrthoDB; 1329388at2759; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000077248; 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:UP000077248};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..576
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008060155"
FT   DOMAIN          60..332
FT                   /note="Glycoside hydrolase family 5"
FT                   /evidence="ECO:0000259|Pfam:PF00150"
FT   DOMAIN          374..462
FT                   /note="Carbohydrate binding X2"
FT                   /evidence="ECO:0000259|Pfam:PF03442"
SQ   SEQUENCE   576 AA;  62936 MW;  9F2A4C34C99BE7E5 CRC64;
     MKISYASAAV LLNSTFAVAQ STNGTGVKCP STSKFSAISA GAFFEKLNPG WNVGNTLDAV
     ETEGSWNNPP VVGSTFDDAK RAGFKSIRLP VTWAYHFTSQ SPDWTVDPVW LQRVSDVVDM
     ITDRGLYAIV NVHHDSWTWA DLTQSSTNVT AVEERLGKLW KQIGTKLACK SEKVAFETIN
     EIPGTTAEHG AVINRLNDIF LQAINDAGGH NPKRVVTLVG AGEDGLKTIQ WFKKPDPKFK
     NPWGIQYHYY SPYDFVFQAW GKTTWGSDAD KAALEADIAA VRGNFSGIPL VIGEWAVSPV
     ATETAARWRY FDFFLRTAAK YNTTTVLWDN GADFLDRATH LWRDEVALDI YRNAVKGIAN
     ALPESTTDGS ATTQSSSAYI YHRKNETVGD VTLGFAFNGN TLSKISRGSK QLAKGKDYSV
     SGEKITFAAS YLKTILTPTS PTGTLANLTL TFNRGAALQV NVLQYTTPTL SNTSGPLPAA
     GQDLLIPITW SGQNRPAAVK AVKADGTYLV DDWTQYLGPL QQGRMTYDGQ WNWDAGHVVI
     KVAALDAVRA ASIDTTFTIE FYPREPGNAV EYTVTV
//
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