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Database: UniProt
Entry: A0A1C5GRD0_9ACTN
LinkDB: A0A1C5GRD0_9ACTN
Original site: A0A1C5GRD0_9ACTN 
ID   A0A1C5GRD0_9ACTN        Unreviewed;       590 AA.
AC   A0A1C5GRD0;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=F5/8 type C domain-containing protein {ECO:0000313|EMBL:SCG36342.1};
GN   ORFNames=GA0074704_0356 {ECO:0000313|EMBL:SCG36342.1};
OS   Micromonospora siamensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=299152 {ECO:0000313|EMBL:SCG36342.1, ECO:0000313|Proteomes:UP000198210};
RN   [1] {ECO:0000313|EMBL:SCG36342.1, ECO:0000313|Proteomes:UP000198210}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45097 {ECO:0000313|EMBL:SCG36342.1,
RC   ECO:0000313|Proteomes:UP000198210};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 26 family.
CC       {ECO:0000256|ARBA:ARBA00007754, ECO:0000256|PROSITE-ProRule:PRU01100}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01100}.
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DR   EMBL; LT607751; SCG36342.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C5GRD0; -.
DR   Proteomes; UP000198210; Chromosome i.
DR   GO; GO:0016985; F:mannan endo-1,4-beta-mannosidase activity; IEA:InterPro.
DR   GO; GO:0030247; F:polysaccharide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006080; P:substituted mannan metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.40.290; -; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR001919; CBD2.
DR   InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR   InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR   InterPro; IPR000421; FA58C.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR022790; GH26_dom.
DR   InterPro; IPR000805; Glyco_hydro_26.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR40079:SF4; GH26 DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR40079; MANNAN ENDO-1,4-BETA-MANNOSIDASE E-RELATED; 1.
DR   Pfam; PF00553; CBM_2; 1.
DR   Pfam; PF00754; F5_F8_type_C; 1.
DR   Pfam; PF02156; Glyco_hydro_26; 1.
DR   SMART; SM00637; CBD_II; 1.
DR   SMART; SM00231; FA58C; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   PROSITE; PS51173; CBM2; 1.
DR   PROSITE; PS50022; FA58C_3; 1.
DR   PROSITE; PS51764; GH26; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198210};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           34..590
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008717017"
FT   DOMAIN          31..141
FT                   /note="CBM2"
FT                   /evidence="ECO:0000259|PROSITE:PS51173"
FT   DOMAIN          162..298
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|PROSITE:PS50022"
FT   DOMAIN          306..590
FT                   /note="GH26"
FT                   /evidence="ECO:0000259|PROSITE:PS51764"
FT   REGION          136..191
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        150..166
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        167..191
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   590 AA;  62960 MW;  3019E9F83C937CBF CRC64;
     MIQRTRARAC LAGAAAAVTV LGTALVTIPA AQAAASTCQV QYQVTNSWGG GASTNVIVTN
     TTATAVNGWT VGWAFPGNQV IGDMWNATKT QSGANATATN VSYNASIPAG GSVNFGFNVT
     FSGANPAPTA FTLNGAACGD TGTNPSPTPT TSPTGTPSPS PTVDPNPTTT PTGNLALNRP
     VTASSTESPN AVGFAVDGNG GTRWSSLYSD PQWIQVDLGA TYPVAQVNLR WEAAYGKAYQ
     IQTSTDGTSW TSVYSTTTGD GGLDAVPVTG SGRYVRMSGT TRGTAWGYSL YEFEVYAVKP
     PTPPGPSCGQ EPADPQANSK VRNLICYLKT HQFVSGQTDL PDADKVQQLT GRYPAMVAFD
     FMEYTKGSIQ TQQVIDWAKS RKGIVAFQWH WYCPRGGNYS APCDFQPDLT NPSSQLYKDI
     DLVVSELKKM GDAGVPVLFR PLHEANNNYM WWTKKGQDAY KQLWRLIYDR AQRAGAHNIV
     WVFNGMASGQ GSSLASWYPG DGYVDLVTSD YFQSWGDFDT TKAVSGSKTT GVAETFSPLN
     PASDAPWPYF VVWASRDWAG SGKDVAGLWK TAMANPKTIS IDQLPDMSAW
//
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