ID A0A099D9C8_9ACTN Unreviewed; 905 AA.
AC A0A099D9C8;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Family 3 glycosyl hydrolase {ECO:0000313|EMBL:ASU78334.1};
DE SubName: Full=Glycoside hydrolase family 3 {ECO:0000313|EMBL:KGI81975.1};
GN ORFNames=CDG81_08555 {ECO:0000313|EMBL:ASU78334.1}, IL38_08130
GN {ECO:0000313|EMBL:KGI81975.1};
OS Actinopolyspora erythraea.
OC Bacteria; Actinomycetota; Actinomycetes; Actinopolysporales;
OC Actinopolysporaceae; Actinopolyspora.
OX NCBI_TaxID=414996 {ECO:0000313|EMBL:ASU78334.1, ECO:0000313|Proteomes:UP000215043};
RN [1] {ECO:0000313|EMBL:KGI81975.1, ECO:0000313|Proteomes:UP000029737}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIM90600 {ECO:0000313|EMBL:KGI81975.1,
RC ECO:0000313|Proteomes:UP000029737};
RX PubMed=25250723;
RA Chen D., Feng J., Huang L., Zhang Q., Wu J., Zhu X., Duan Y., Xu Z.;
RT "Identification and Characterization of a New Erythromycin Biosynthetic
RT Gene Cluster in Actinopolyspora erythraea YIM90600, a Novel Erythronolide-
RT Producing Halophilic Actinomycete Isolated from Salt Field.";
RL PLoS ONE 9:E108129-E108129(2014).
RN [2] {ECO:0000313|EMBL:ASU78334.1, ECO:0000313|Proteomes:UP000215043}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIM 90600 {ECO:0000313|EMBL:ASU78334.1,
RC ECO:0000313|Proteomes:UP000215043};
RA Yin M., Tang S.;
RT "The complete genome sequence of moderately halophilic actinomycete
RT Actinopolyspora erythraea YIM 90600, the producer of novel erythromycin,
RT novel actinopolysporins A-C and tubercidin.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP022752; ASU78334.1; -; Genomic_DNA.
DR EMBL; JPMV01000014; KGI81975.1; -; Genomic_DNA.
DR RefSeq; WP_043571853.1; NZ_KN214175.1.
DR AlphaFoldDB; A0A099D9C8; -.
DR KEGG; aey:CDG81_08555; -.
DR eggNOG; COG1472; Bacteria.
DR eggNOG; COG5492; Bacteria.
DR HOGENOM; CLU_004542_5_3_11; -.
DR OrthoDB; 9803863at2; -.
DR Proteomes; UP000029737; Unassembled WGS sequence.
DR Proteomes; UP000215043; Chromosome.
DR GO; GO:0009044; F:xylan 1,4-beta-xylosidase activity; IEA:InterPro.
DR GO; GO:0045493; P:xylan catabolic process; IEA:InterPro.
DR Gene3D; 2.60.40.1080; -; 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; IPR026891; Fn3-like.
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 InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR PANTHER; PTHR42721:SF3; BETA-D-XYLOSIDASE 5-RELATED; 1.
DR PANTHER; PTHR42721; SUGAR HYDROLASE-RELATED; 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; SM01217; Fn3_like; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ASU78334.1};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..905
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001944604"
FT DOMAIN 707..778
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
FT REGION 781..809
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 905 AA; 100175 MW; CCAB60002A109ADA CRC64;
MRRRPTRLLM TLGLCMTCAL STAPALAQER SEETPVYLDQ NYSARERAAD LVSRMTPSEK
ASQLISSQAP AIPRLEVRAY GWWNEAAHGV AREQYNDDGN PEILTNTTSY PVSLSMGSTW
NPDLMYRVGQ ATSSEAREVV RDNSLDLNFY SPTINLSRDP RWGRNDETFS EDPGLTAAMA
SQYVNGMEGK DKQGNLLPSS EGYLKTSTTI KHFAANNSEF NRLTGTSNMD ERTLREYYTA
PFREVIRESS PGSIMSAYNR VNGVPASASV GLLDTLARKT FGFDGFFTSD CDSVYEIQHG
HNWKPEGEEE PLDHVERNAY ANAAGVDLNC NKGYHDEHHF GNTLPEAASE KIQTHNGVYT
ENFMDASLIR MFTVRIKLGE FDDAEQVPWV RRARERVPEG SWENSESNDA VTQTPQRLDL
AREAASESIV LLRNQPSEDG GELLPLRIPE SGAYRLAVVG DHANPEQMYL GGYSSDQGPS
GRANSVNGYE GLKKAVEEIN PQAVVDYLPG TKPGTENQLN RNSVRVSADY DAVVVYGGTD
ETTAKEDEDR ESLRLPQPQT KLINEVAANN PNTVVYLETI GAVDVSSFAS DVSAMLWSSY
NGQRKGEALA DVLLGESNPS GHLPFTWYRD ESQLPSIGDY SIRPADSRPG RTYMYFDGPA
AYPFGHGLGY TDFEYGDLRI ERDHVNANGT VRASARVTNT GGAAGSDVVQ LYAASSKADR
ADRPDERLVG FEKVSLRPNE TKRVEFTVPV RDLALFDQRR DRYEIGEGDY EFRLGHSSSD
VADSERVTVH GKPRPAPENV STTPRAAGDE ERGITIRRVF DRDTVVRPRT TVSLNDGTLV
GHVADERDKP LPPGMRVHYR SNRPGVVSVD PHGVIRTRDS GVATVTATVR YRGHTESTEF
VVKVR
//