ID A0A176L7F0_9ACTN Unreviewed; 410 AA.
AC A0A176L7F0;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=1,3-beta-glucanase {ECO:0000313|EMBL:OAB00429.1};
GN ORFNames=A6P39_12785 {ECO:0000313|EMBL:OAB00429.1};
OS Streptomyces sp. FXJ1.172.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=710705 {ECO:0000313|EMBL:OAB00429.1};
RN [1] {ECO:0000313|EMBL:OAB00429.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FXJ1.172 {ECO:0000313|EMBL:OAB00429.1};
RA Liu M., Liu N., Shang F., Huang Y.;
RT "Activation and identification of NC-1, a novel cryptic cyclodepsipeptide
RT from red soil-derived Streptomyces sp. FXJ1.172.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family.
CC {ECO:0000256|ARBA:ARBA00006865}.
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:OAB00429.1}.
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DR EMBL; LWRP01000062; OAB00429.1; -; Genomic_DNA.
DR RefSeq; WP_067044233.1; NZ_CP119133.1.
DR AlphaFoldDB; A0A176L7F0; -.
DR STRING; 710705.A6P39_12785; -.
DR OrthoDB; 9809583at2; -.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd08023; GH16_laminarinase_like; 1.
DR CDD; cd00161; RICIN; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.80.10.50; -; 2.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000757; GH16.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR NCBIfam; NF035930; lectin_2; 1.
DR PANTHER; PTHR10963:SF55; GH16 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR10963; GLYCOSYL HYDROLASE-RELATED; 1.
DR Pfam; PF00722; Glyco_hydro_16; 1.
DR Pfam; PF00652; Ricin_B_lectin; 1.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR PROSITE; PS51762; GH16_2; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 3: Inferred from homology;
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..410
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008047808"
FT DOMAIN 27..284
FT /note="GH16"
FT /evidence="ECO:0000259|PROSITE:PS51762"
SQ SEQUENCE 410 AA; 43042 MW; 78A2133B07CB4851 CRC64;
MASPRLLRRC LFAALSAVLV GSAAVGPARA QTAAPAAATT TFSDTFDGPA GSPVDSSKWT
TETGDNVNNH EREYYTSGTD NAALDGQGHL VITARKENPA GYQCWYGTCQ YTSARLNTAG
KFNARYGHVE ARMKIPRGQG MWPAFWMLGT PVNWPDSGEI DVMENVGFEP STVHGTIHGP
GYSGSGGIGA AYTLPGGQAF ADAFHTFAVD WAPDSITWSV DGTVYERRTP ADLGGKTWVF
NNKPFFLILN LAVGGYWPGD PDGTTQFPQQ LVVDSVSVTT SDSAAGLPIR GLAGKCVDVA
GANSANGTPV QLYDCNGTAA QNWTVGSDGT IRALGKCLDV TGNGTADGST VQLWDCTGGP
NQKWTVTGAH DIVNPQADKC LDVTGNNAAD GTRLQIWTCT GGANQKWTVG
//
