ID A0A248YNU6_9ACTN Unreviewed; 546 AA.
AC A0A248YNU6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Cellulose-binding protein {ECO:0000313|EMBL:ASW55368.1};
GN ORFNames=CIK06_16140 {ECO:0000313|EMBL:ASW55368.1};
OS Plantactinospora sp. KBS50.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Plantactinospora.
OX NCBI_TaxID=2024580 {ECO:0000313|EMBL:ASW55368.1, ECO:0000313|Proteomes:UP000216795};
RN [1] {ECO:0000313|EMBL:ASW55368.1, ECO:0000313|Proteomes:UP000216795}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KBS50 {ECO:0000313|EMBL:ASW55368.1,
RC ECO:0000313|Proteomes:UP000216795};
RA Juboi H., Hwang S.S., Yeo T.C., Nissom P.M.;
RT "Genome sequencing and analysis of secondary metabolite biosynthetic
RT capabilities of Plantactinospora sp. KBS50.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR EMBL; CP022961; ASW55368.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A248YNU6; -.
DR KEGG; plk:CIK06_16140; -.
DR OrthoDB; 8660908at2; -.
DR Proteomes; UP000216795; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0030247; F:polysaccharide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.60.40.290; -; 1.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR InterPro; IPR001919; CBD2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR40088; PECTATE LYASE (EUROFUNG); 1.
DR PANTHER; PTHR40088:SF1; PECTATE LYASE PEL9; 1.
DR Pfam; PF00553; CBM_2; 1.
DR SMART; SM00637; CBD_II; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
DR PROSITE; PS51173; CBM2; 1.
DR PROSITE; PS51318; TAT; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000216795};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..546
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039399427"
FT DOMAIN 31..141
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT REGION 147..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 546 AA; 56119 MW; 81EEDF3B47FB7CF5 CRC64;
MIYRQRRRSL RILSVAAVAL AAAGVVVTAN AAQAAAGCRV DYTVASQWPG GFTANIDLTN
LGDPLTAWTL TWSFGAGQTV AQGWNATFSQ SGSAVQASNV SWNGGLGTNA TTTFGFNGTW
NNSSNPVPAS FAVNGVACTG GVTPTTAAPT TAAPTTAAPT TAAPTTAAPT TAAPTTAAPT
TAAPSDTIYA APTGTASAAG TMSNPTTVAA AITRVAAGGT IYLRGGTYSL SQTVTIAPGN
DGTASARKNL SAYPGETPVL NFSAMAEDSA NRGLALNGSY WHLYGLVVER AGDNGIFVGG
SNNIIERTVT RFNHDSGLQI SRISSDTPTS QWPANNLVLS SESHDNADSD GEDADGFAAK
LTAGPGNVFR YTVSHNNIDD GWDLYTKTDT GAIGPVTIED SLSYNNGTLT DGTVNANGDR
NGFKLGGEDI AVSHTIRRNI AYHNGHHGFT YNRNPGTMSI SNNLSIDNSE RNFSFDAGTS
VFRSNTSCRF SSGGSNDKTV GDADSSNQFW TGSNGSRCSA YSGTLAWSFA SDGHLVVTLG
GRVVSL
//
