GenomeNet

Database: UniProt
Entry: I0GZN1_ACTM4
LinkDB: I0GZN1_ACTM4
Original site: I0GZN1_ACTM4 
ID   I0GZN1_ACTM4            Unreviewed;       977 AA.
AC   I0GZN1;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   SubName: Full=Putative glycosyl hydrolase {ECO:0000313|EMBL:BAL86218.1};
GN   OrderedLocusNames=AMIS_9980 {ECO:0000313|EMBL:BAL86218.1};
OS   Actinoplanes missouriensis (strain ATCC 14538 / DSM 43046 / CBS 188.64 /
OS   JCM 3121 / NBRC 102363 / NCIMB 12654 / NRRL B-3342 / UNCC 431).
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Actinoplanes.
OX   NCBI_TaxID=512565 {ECO:0000313|EMBL:BAL86218.1, ECO:0000313|Proteomes:UP000007882};
RN   [1] {ECO:0000313|EMBL:BAL86218.1, ECO:0000313|Proteomes:UP000007882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14538 / DSM 43046 / CBS 188.64 / JCM 3121 / NBRC 102363 /
RC   NCIMB 12654 / NRRL B-3342 / UNCC 431
RC   {ECO:0000313|Proteomes:UP000007882};
RA   Ohnishi Y., Ishikawa J., Sekine M., Hosoyama A., Harada T., Narita H.,
RA   Hata T., Konno Y., Tutikane K., Fujita N., Horinouchi S., Hayakawa M.;
RT   "Complete genome sequence of Actinoplanes missouriensis 431 (= NBRC
RT   102363).";
RL   Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AP012319; BAL86218.1; -; Genomic_DNA.
DR   AlphaFoldDB; I0GZN1; -.
DR   STRING; 512565.AMIS_9980; -.
DR   KEGG; ams:AMIS_9980; -.
DR   PATRIC; fig|512565.3.peg.1004; -.
DR   eggNOG; COG1472; Bacteria.
DR   HOGENOM; CLU_004542_5_3_11; -.
DR   OrthoDB; 3304319at2; -.
DR   Proteomes; UP000007882; Chromosome.
DR   GO; GO:0008422; F:beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009044; F:xylan 1,4-beta-xylosidase activity; IEA:InterPro.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:InterPro.
DR   CDD; cd04084; CBM6_xylanase-like; 1.
DR   Gene3D; 2.60.120.380; -; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR   Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR044993; BXL.
DR   InterPro; IPR006584; Cellulose-bd_IV.
DR   InterPro; IPR005084; CMB_fam6.
DR   InterPro; IPR026891; Fn3-like.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR002772; Glyco_hydro_3_C.
DR   InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR   InterPro; IPR001764; Glyco_hydro_3_N.
DR   InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   PANTHER; PTHR42721:SF3; BETA-D-XYLOSIDASE 5-RELATED; 1.
DR   PANTHER; PTHR42721; SUGAR HYDROLASE-RELATED; 1.
DR   Pfam; PF03422; CBM_6; 1.
DR   Pfam; PF14310; Fn3-like; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   Pfam; PF01915; Glyco_hydro_3_C; 1.
DR   PRINTS; PR00133; GLHYDRLASE3.
DR   SMART; SM00606; CBD_IV; 1.
DR   SMART; SM01217; Fn3_like; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   PROSITE; PS51175; CBM6; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:BAL86218.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007882};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          848..977
FT                   /note="CBM6"
FT                   /evidence="ECO:0000259|PROSITE:PS51175"
FT   REGION          1..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..22
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   977 AA;  105407 MW;  58E67FA44684A733 CRC64;
     MSPKERVVTE SPTDHEPAAF REAATGKSEP TPAFREPGPG KSEPTPAFRD PQHKVAVRVA
     DLLDRLTLDE KIALLNQYQP AVPRLGVAAF RTGTEALHGV AWLGTATAFP QAVGLASSWN
     PDLMRRVGEA VGTEVRAMHH RDPENVGLNV WAPVVNLLRD PRWGRNEEGY AEDPWLTGVL
     STAYSRGLRG DHPLWLRTAP TLKHFLGYNN ETDRCLTSSN LPPRVLHEYE LPAFRPALAD
     GAAVAVMASY NLVNGRPTHL SPLIDETLRS WAEDDVLVVG DAWAVHNLAG DQHWFDDHVA
     GFAAALRAGI DCVTEDVTAT RERFTAAYDR GLITESHVDA AVRHILSIRV RLGEFDAASD
     PYRHIGPEVI DCGEHRELAH EAARASAVLL SNDGILPLDP QTVGRVAVIG PLADQVFEDW
     YSGTPPYRTT LRAGVTRRIG ADAVLFAEGV DRVALRCASG LLWASASHHL GVRGTEAPDI
     PEEALFDVLD WGEETISLRA VSTGGFVGSD ADLLVTDRPG PNGWEVRESL RFLPVPQGMV
     VHHLQSNRFL VAGDDGLIRT AATSVADATV FTVDLLVDGV AAAAEVAAEA DVVLLALGNH
     PLVAGRETAD RRDLDLPGTQ DDLMRAVRAA NPRTVLALTS SYPYAVGWAS QHLPALLWSA
     HGGQEHGAAL ADILFGAAEP SGRLTQTWYA HDGDLPDLLD YDIIASDATY LYYRGEPLFP
     FGHGLGYTSF RYENLRLDTP AIDSAGAVTV SVDVVNTGDR PGDEVVQLYT RQQRSRVKQP
     LRRLRGFQRI HLSPGGRSTV HFALTAADLA FWDVTRSRWV IEDATHTVAA GRSSTDWRQT
     TTLRVHGERI PARSPSLTMT DNDGYALAST VPIPGTAAGE ALRSSAPGAW AVFDDVDFGQ
     GLTRARATVA APAGSTIMIR LDDPLSGPVL AVLPVPVAAG ADPLIEVSSQ IPRCTGRHDV
     FVQFTEGGTT VAGLHFS
//
DBGET integrated database retrieval system