ID A0A0M9ZX89_9NOCA Unreviewed; 957 AA.
AC A0A0M9ZX89;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Carbohydrate-binding protein {ECO:0000313|EMBL:KOV78576.1};
GN ORFNames=ADL03_39620 {ECO:0000313|EMBL:KOV78576.1};
OS Nocardia sp. NRRL S-836.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=1519492 {ECO:0000313|EMBL:KOV78576.1, ECO:0000313|Proteomes:UP000037746};
RN [1] {ECO:0000313|Proteomes:UP000037746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL S-836 {ECO:0000313|Proteomes:UP000037746};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the UPF0098 family.
CC {ECO:0000256|ARBA:ARBA00007120}.
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:KOV78576.1}.
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DR EMBL; LGDY01000143; KOV78576.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M9ZX89; -.
DR STRING; 1519492.ADL03_39620; -.
DR PATRIC; fig|1519492.3.peg.8448; -.
DR OrthoDB; 9770043at2; -.
DR Proteomes; UP000037746; 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; 2.
DR CDD; cd00063; FN3; 2.
DR CDD; cd00865; PEBP_bact_arch; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 3.90.280.10; PEBP-like; 1.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
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; IPR008914; PEBP.
DR InterPro; IPR036610; PEBP-like_sf.
DR InterPro; IPR011041; Quinoprot_gluc/sorb_DH.
DR InterPro; IPR005247; YbhB_YbcL/LppC-like.
DR PANTHER; PTHR19328; HEDGEHOG-INTERACTING PROTEIN; 1.
DR PANTHER; PTHR19328:SF13; HIPL1 PROTEIN; 1.
DR Pfam; PF03422; CBM_6; 2.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF07995; GSDH; 1.
DR Pfam; PF01161; PBP; 1.
DR SMART; SM00060; FN3; 2.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR SUPFAM; SSF49777; PEBP-like; 1.
DR SUPFAM; SSF50952; Soluble quinoprotein glucose dehydrogenase; 1.
DR PROSITE; PS51175; CBM6; 2.
DR PROSITE; PS50853; FN3; 2.
PE 3: Inferred from homology;
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 Reference proteome {ECO:0000313|Proteomes:UP000037746}.
FT DOMAIN 12..136
FT /note="CBM6"
FT /evidence="ECO:0000259|PROSITE:PS51175"
FT DOMAIN 144..267
FT /note="CBM6"
FT /evidence="ECO:0000259|PROSITE:PS51175"
FT DOMAIN 279..365
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 374..461
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 250..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 354..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 957 AA; 100044 MW; E617DFF9B3C15AC8 CRC64;
MVVPDSALAA PARYEAESAK ITQGVVESNH AGFSGTGFVN FDNVAGSSVE FGVMASKAGQ
AKLVFRYANG TADNRPVDVS VNGGLAVDER AFTGTGAWTT WTTVENTVNL TPGVNTIRLT
ATTAAGGPNL DHVEVEEIGS APALEQEAEN ATISQGVVES NHTGFSGTGF VNYDNVVGSY
VEYTVTAAAG GEHDLTFRYA NGTTTDRPVS VTVDGANAQT LSFPGTGAWT TWQTRTARVT
LKAGPNKVRA TATTANGGPN ADRLTAVPQG PPDTEAPTPP RDLRFVSSTH DSVSLRWEAA
TDNVGVVGYD IYQHGQLVTS VGNVLQGTAT GLRADTEYDW TVFAKDAAGN VSQASNNVAG
RTQPAPPDGQ APTTPGNLRS TGATTTSVTV AWTAATDNVG VTSYEVHVDG TLEQTADGTA
TSSTIAGLTA GQDYRVKVRA KDAAGNLSPF SNEISVRPGQ GGGTGVPNPG TVKQVVGGVD
VPWGTAFLPD GSALVTERET FNVLRVTEAG VKTVLGKVPG AVGTGGEGGA LGIEVSPTWS
TDRLIYVYHT YSGGNRLVRA QFDGTQLSNW TTLLDGVPKN RYHNGGRLRF SPDGRYLFIS
TGDAQNGTNA QNLNTNAGKI LRIHPDGSIP ADNPFAGKAI WSYGHRNVQG LDFDSQGRLW
ASEFGNSQQD EVNLITKGGN YGWDACEGTT GSCAGTIPPK KTWSTSQASP SGLTIINDYV
FVATTVGQRI YRMRIDANGN LVDQQIYFQG SYGRLRTVEV DREGDIWLTT STDKDGTTGN
DRVLHIDIVY EGGTPQFALT SPAFADDAMI PAKHTCAGDG VAGQDPSPPL AWGESTGAKA
YAIVFADRAN NGNKLHWAIW DIPASTRSLP ENLGAGFTVP GQGGAKQKAM GSGANSQKYF
GPCPGGSTNP YTFTLYALNT TSVPGITSSS TMAQIETAIK NASTANTVLR GRSNART
//
