ID A0A0N0AHH1_9ACTN Unreviewed; 494 AA.
AC A0A0N0AHH1;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Glycosyl hydrolase family 5 {ECO:0000313|EMBL:KOX07994.1};
GN ORFNames=ADK66_17340 {ECO:0000313|EMBL:KOX07994.1};
OS Micromonospora sp. NRRL B-16802.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=1415541 {ECO:0000313|EMBL:KOX07994.1, ECO:0000313|Proteomes:UP000037709};
RN [1] {ECO:0000313|EMBL:KOX07994.1, ECO:0000313|Proteomes:UP000037709}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-16802 {ECO:0000313|EMBL:KOX07994.1,
RC ECO:0000313|Proteomes:UP000037709};
RA Noorani M.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {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:KOX07994.1}.
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DR EMBL; LGEB01000064; KOX07994.1; -; Genomic_DNA.
DR RefSeq; WP_053656530.1; NZ_LGEB01000064.1.
DR AlphaFoldDB; A0A0N0AHH1; -.
DR STRING; 1415541.ADK66_17340; -.
DR PATRIC; fig|1415541.3.peg.3629; -.
DR OrthoDB; 273314at2; -.
DR Proteomes; UP000037709; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:InterPro.
DR CDD; cd00161; RICIN; 1.
DR Gene3D; 2.80.10.50; -; 3.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
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; PF00150; Cellulase; 1.
DR Pfam; PF14200; RicinB_lectin_2; 2.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361153};
KW Hydrolase {ECO:0000256|RuleBase:RU361153, ECO:0000313|EMBL:KOX07994.1};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..34
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 35..494
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005843683"
FT DOMAIN 356..492
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
SQ SEQUENCE 494 AA; 53398 MW; 5828695E5D98F8D5 CRC64;
MTRIRSVRRL LITLVAALTA LAGVIVVTSS PATAATNQFR GMNWAVLGDN FSTGPLVVQG
LSASDSNATV RVKANALYDD MASTMGVNTV RLPINTHTVG TAWWEAYRGA IDAATARGFK
VILAYWEDGA ASGGRITNLA AWNAMWSTVT NTYGANTSVY FEPMNEPHGY SSAEWRNVAA
NWLSYHYSAV PGRVLIGGTG FSQDLRDICN DSRFASTLLS FHHYAFFYGA MTYDAFRSHI
QTRLGNCASR AVATEFGAPM NDGRNYADAG SSDNFVRHIR AMAQVMRDNQ MGGTYWPALG
GKPGTIGYDW YSMFSLSGTG TDLNLTVRNT SGADQIRYAW GDTIGGGPTT PPPSTGTYYR
ITVRHSGKAM DVQQPNTDNG ARVGQYTYGG SAWQQWQFQD AGSGYWRIIS RHSGKCLDVV
SASTADGAEL VQYTCGAGAN QQFQMVTSGG YFQLRARHSG KCVDVPAAST ADGVILKQYT
CNTGANQQWS RTVV
//
