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Database: UniProt
Entry: A0A0M9YB00_9ACTN
LinkDB: A0A0M9YB00_9ACTN
Original site: A0A0M9YB00_9ACTN 
ID   A0A0M9YB00_9ACTN        Unreviewed;       693 AA.
AC   A0A0M9YB00;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   SubName: Full=Oxidoreductase {ECO:0000313|EMBL:KOU38202.1};
GN   ORFNames=ADK54_28950 {ECO:0000313|EMBL:KOU38202.1};
OS   Streptomyces sp. WM6378.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1415557 {ECO:0000313|EMBL:KOU38202.1, ECO:0000313|Proteomes:UP000037774};
RN   [1] {ECO:0000313|Proteomes:UP000037774}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WM6378 {ECO:0000313|Proteomes:UP000037774};
RA   Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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:KOU38202.1}.
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DR   EMBL; LGDD01000307; KOU38202.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M9YB00; -.
DR   PATRIC; fig|1415557.3.peg.6362; -.
DR   OrthoDB; 9770043at2; -.
DR   Proteomes; UP000037774; Unassembled WGS sequence.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd04082; CBM35_pectate_lyase-like; 1.
DR   CDD; cd00063; FN3; 2.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR006584; Cellulose-bd_IV.
DR   InterPro; IPR005084; CMB_fam6.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR012938; Glc/Sorbosone_DH.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR011041; Quinoprot_gluc/sorb_DH.
DR   PANTHER; PTHR19328; HEDGEHOG-INTERACTING PROTEIN; 1.
DR   PANTHER; PTHR19328:SF13; HIPL1 PROTEIN; 1.
DR   Pfam; PF03422; CBM_6; 1.
DR   Pfam; PF00041; fn3; 2.
DR   Pfam; PF07995; GSDH; 1.
DR   SMART; SM00606; CBD_IV; 1.
DR   SMART; SM00060; FN3; 2.
DR   SUPFAM; SSF49265; Fibronectin type III; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF50952; Soluble quinoprotein glucose dehydrogenase; 1.
DR   PROSITE; PS51175; CBM6; 1.
DR   PROSITE; PS50853; FN3; 2.
PE   4: Predicted;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00023295};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           33..693
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038704745"
FT   DOMAIN          42..167
FT                   /note="CBM6"
FT                   /evidence="ECO:0000259|PROSITE:PS51175"
FT   DOMAIN          179..266
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          274..365
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   REGION          37..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          255..278
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   693 AA;  72383 MW;  1B2238D57A0F82F1 CRC64;
     MRLATPPRPA RGRARKAAAA AVLLLCAGLV QAAPQPASAA STRYEAESGT RSTGSTVDTN
     HKNYSGTGFV NSNNAVGAYV EVTVNVAAAG NATIDIRYAN GTGANRPADV SVNGAVVSVA
     RAFDATANWD TWADSTLTVA VKAGSNKIRL ASTTADGLAN IDYVDFSGAS GGDTQAPTRP
     GTPTCSAVTE SALTLSWGAS TDNVGVAKYD VYEHGNKINE VDGTLTSDHL TGLTPNTTYN
     LTVLARDAAG NVSQASPAID CTTPPSTDTN PPTKPGTLTS SHVTANSVDL NWGASTDDKG
     VTSYEVRSGD NVYKAVTGNP PGTSTTLTGL ACDSPYSLTV VAKDAGGNVS PASNAVSFTT
     ATCQTDGGVP SSITTLSIDW TIPWGTYWMP DNSSALVTER DSFKVYKVTP NGTKTQVGSV
     PNAVTTDGEG GLLGVAVDPK WATNHYVYFM HTAAEGNRVV RMTYNGSALS NYTVLLQGIK
     KNRYHNGGRL AFGPDGYLYA STGEAQTPDL AQDKNSLNGK ILRMTTDGKP APGNPFNNYV
     YSYGHRNPQG LAFDRNGRLW EAEFGDSKKD ELNLIKPGAN YGWPTCEGPC STAGMTNPKA
     SWPTGQASPS GIAIVRNVVY MAALKGERLW RIPITGDTEN VGTPTAYYVG SYGRLRTVTK
     VPGEDAFWLS TTNGDNNGTG GAGSDKIFKV LVK
//
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