ID   A0A1L7FAQ8_9PSEU        Unreviewed;       881 AA.
AC   A0A1L7FAQ8;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Putative cellulose binding protein {ECO:0000313|EMBL:APU21871.1};
DE            EC=3.2.1.- {ECO:0000313|EMBL:APU21871.1};
GN   ORFNames=UA75_19405 {ECO:0000313|EMBL:APU21871.1};
OS   Actinoalloteichus sp. GBA129-24.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Actinoalloteichus.
OX   NCBI_TaxID=1612551 {ECO:0000313|EMBL:APU21871.1, ECO:0000313|Proteomes:UP000185506};
RN   [1] {ECO:0000313|EMBL:APU21871.1, ECO:0000313|Proteomes:UP000185506}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GBA129-24 {ECO:0000313|EMBL:APU21871.1,
RC   ECO:0000313|Proteomes:UP000185506};
RA   Ruckert C., Nouioui I., Willmese J., van Wezel G., Klenk H.-P.,
RA   Kalinowski J., Zotchev S.B.;
RT   "Complete genome sequence of Actinoalloteichus fjordicus DSM 46856
RT   (=GBA129-24).";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000256|ARBA:ARBA00001935};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 74 family.
CC       {ECO:0000256|ARBA:ARBA00037986}.
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DR   EMBL; CP016077; APU21871.1; -; Genomic_DNA.
DR   RefSeq; WP_075741470.1; NZ_CP016077.1.
DR   AlphaFoldDB; A0A1L7FAQ8; -.
DR   STRING; 1612551.UA75_19405; -.
DR   KEGG; acti:UA75_19405; -.
DR   OrthoDB; 9764804at2; -.
DR   Proteomes; UP000185506; Chromosome.
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:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd15482; Sialidase_non-viral; 2.
DR   Gene3D; 2.60.40.290; -; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR   InterPro; IPR001919; CBD2.
DR   InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR   InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR   InterPro; IPR006311; TAT_signal.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   PANTHER; PTHR43739; XYLOGLUCANASE (EUROFUNG); 1.
DR   PANTHER; PTHR43739:SF2; XYLOGLUCANASE (EUROFUNG); 1.
DR   Pfam; PF00553; CBM_2; 1.
DR   SMART; SM00637; CBD_II; 1.
DR   SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR   SUPFAM; SSF110296; Oligoxyloglucan reducing end-specific cellobiohydrolase; 2.
DR   PROSITE; PS51173; CBM2; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023326};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000313|EMBL:APU21871.1};
KW   Hydrolase {ECO:0000313|EMBL:APU21871.1};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..881
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5039320255"
FT   DOMAIN          776..881
FT                   /note="CBM2"
FT                   /evidence="ECO:0000259|PROSITE:PS51173"
FT   REGION          754..781
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   881 AA;  92231 MW;  65F3161F91DE6F30 CRC64;
     MTKRRFLSAA LAAALAAGAL ALTQLPSGQS EAAAQTVNQS YSWRNAEIAG GGFVPGIIFN
     QSEPNLIYAR TDIGGAYRWE QDSGRWTPLL DWVGWDEWGY NGVVSLATDP VDTDRVYVAA
     GMYTNDWDPN NGAILRSADR GETWEVTELP FKLGGNMPGR GMGERLTVDP NDNSIVYLGA
     PSGNGLWRST DFGVTWSEVS NFPNPGNYAQ DPDDPNGYLD DNQGVTWVTF DESTGSAGEP
     TQDLYIGVAD KENTVYRSTD AGASWERVAG QPTGFLAHKG VVDHVNGFLY IATSDTGGPY
     DGAEGDVWKY ATDTGEWTQI SPVPSGAEGS DFGYSGLTID RQNPGTLMVA SQLLWWPDIV
     IFRSTDAGET WTRAWDWANY PERSFRYEID ISEVPWLDFA TNPTPPEITP KLGWMTEALE
     IDPFDSDRMM YGTGATIYGT ENLSAWDAGG RITIEPMVGG LEETAVLDLA SPPSGAPLLS
     ALGDIGGFRH DDLDSVPERM FSAPNFTSTT SIDFAETNPN FVVRAGNADG VSRAAFSQDG
     GANWYPASSE PSGVTGGGTI ASAADGDSVL WSPAGTGVHH AGSSGSSWTA STGIPAGAVV
     EADRVNPAVF YGASGGRFYV STDGGASFTA SPATGLPTGN VKFTALPDRE GEIWLAGDGG
     LVRSTDGGTT FTAVSGVDSA RNVAHGAAAP GANHPALYLV GTVGGVQGVF RSDDAGAAWV
     RINDDQHQWG NMGEALSGDP RVYGRVYLGT NGRGIQIGES GDTTPPTTTP PPTTTPPPTG
     DGCSATYAVA NSWPGGFQGA VTVRNTGSTA FDGWSASWTF PGTQTVSQAW NGEATQAGRE
     VTVRNAGYNG VIAPGGAVTV GFNGSGSGPD SIPTRIACTG G
//