ID A0A429B9N3_9ACTN Unreviewed; 1232 AA.
AC A0A429B9N3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=CBM6 domain-containing protein {ECO:0000259|PROSITE:PS51175};
GN ORFNames=DMB42_18260 {ECO:0000313|EMBL:RSN09257.1};
OS Nonomuraea sp. WAC 01424.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Nonomuraea.
OX NCBI_TaxID=2203200 {ECO:0000313|EMBL:RSN09257.1, ECO:0000313|Proteomes:UP000286861};
RN [1] {ECO:0000313|EMBL:RSN09257.1, ECO:0000313|Proteomes:UP000286861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WAC 01424 {ECO:0000313|EMBL:RSN09257.1,
RC ECO:0000313|Proteomes:UP000286861};
RA Waglechner N., Wright G.D.;
RT "Evolution of GPA BGCs.";
RL Submitted (MAY-2018) 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:RSN09257.1}.
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DR EMBL; QHHZ01000006; RSN09257.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A429B9N3; -.
DR OrthoDB; 9760654at2; -.
DR Proteomes; UP000286861; Unassembled WGS sequence.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProt.
DR CDD; cd04080; CBM6_cellulase-like; 1.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.40.1080; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 4.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR003343; Big_2.
DR InterPro; IPR006584; Cellulose-bd_IV.
DR InterPro; IPR005084; CMB_fam6.
DR InterPro; IPR032267; DUF4832.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR Pfam; PF02368; Big_2; 1.
DR Pfam; PF03422; CBM_6; 3.
DR Pfam; PF16116; DUF4832; 1.
DR SMART; SM00635; BID_2; 1.
DR SMART; SM00606; CBD_IV; 3.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 3.
DR SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 1.
DR PROSITE; PS51175; CBM6; 3.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000286861};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..1232
FT /note="CBM6 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019020910"
FT DOMAIN 535..656
FT /note="CBM6"
FT /evidence="ECO:0000259|PROSITE:PS51175"
FT DOMAIN 663..791
FT /note="CBM6"
FT /evidence="ECO:0000259|PROSITE:PS51175"
FT DOMAIN 796..928
FT /note="CBM6"
FT /evidence="ECO:0000259|PROSITE:PS51175"
SQ SEQUENCE 1232 AA; 134114 MW; C39894EE40DE63FC CRC64;
MSSRLLGAAL SVAVAAALAV LPGHATAAAT AAETATPRTT VTFTDTYEVL HGNPYTGTAF
DINSPKPAGE RGWVFADDPA ITAFIEGKEK IPDEADIVRL QIAWADFEPE DDAFTWDRLD
AFMKRVVEQG KTVEFQLLMS EAPDIKNDPS VFAYEYPPAW LFDQLGAGFR LAPYNTVYKS
RQPIYHDPIY LAELKEAVGA FAARYDANPG MAWVDLRAFA LFGEWSGWND AMNFPWPDNA
TRSKTLRAIM DIYAEAFTRT MVMMPNPGAD VVTTDPDADT QAKRYVAFGY EQAARNENWG
LRSDTVNSAF PWMQYGTGSE NVWVNRKLRR DLIQVSEGAG WDSGIMLNNP RLVVKNALEG
YHSNLQGINN TSFAQWQAMK DAYGEWFTTL GRYSGYRFLM PRATYDSQVA PGGAFTLAHT
WTNNGVGFSP RKYPLEVRFT DRATGEVVWR GTDASLDQTK WFKGDARELR SAFTLPAGVP
AGTYDVGIAM LGADGKPRIE LAMPDGVGKV YPIGTIKVVP EVAPAAPTAA PLTQFKIENE
DYTEAKGAYG VEAPPEGGFG SLYLDEAGEW AEYDNVVVPA SGTYRAEFRL SSEQGNRFRV
EIDGRDALGP ITVPDSGGYN VYRTIERELT LPAGRHTIRI VREDGRWFFM NWMRFTHERP
ESITIQAERP TAQEGVWLAA EDAVSEDGTP GVSVVDTGDW LRYDEVEIPA SGDYLLQFQY
STVNADSLRF RVEVDGSDVS GELSLRDTGG VNRIRTEDFV VPLTAGSHSV KVVWIEAHSN
IVWNRMRLDL QGAAEQTIEA EQYTMQWNLG QEWGWKGADT GVVVGTYQGA GGPVRAVGRV
DEGDYLRYEN VFAPHTGLYR VGFTAASGKA TSFRFEVDGD RYPVHVPDTG GDGHFTTVGT
WVKLTAGTHT FRIVAEGTGL LLDAFTVTAG TAATKALVAT GAASLRAGDT ATITTEAVSA
DGSRTPVSDG VTYVSSDPSV ATVDAHGVVK AVAWGSTTIT AIYDGLSDGY PLTVTDPTLL
LTYVNDDDRR VTYTGAFGVD RGRGLGDYGD DVHYSTEKGD HAELTFTGTG ISFLTERYTD
MGVVDLYVDG ELRASADCYG PVRQGQQRVF RLSGLELGEH TIRVVNKQSA ADTGRIAIVD
AFVVEVPRPW ADGAELTVGK KPASVKLTWP RSPIATGYAV FDGDTEVARV KANKTKATVG
SLVPGSTHTF TVRPVLPGGT TLSFGLTAEV TL
//
