ID A0A191US65_9ACTN Unreviewed; 1095 AA.
AC A0A191US65;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Hydrolase {ECO:0000313|EMBL:ANJ05549.1};
GN ORFNames=Spa2297_00255 {ECO:0000313|EMBL:ANJ05549.1};
OS Streptomyces parvulus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=146923 {ECO:0000313|EMBL:ANJ05549.1, ECO:0000313|Proteomes:UP000078468};
RN [1] {ECO:0000313|EMBL:ANJ05549.1, ECO:0000313|Proteomes:UP000078468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2297 {ECO:0000313|EMBL:ANJ05549.1,
RC ECO:0000313|Proteomes:UP000078468};
RA Nishizawa T., Miura T., Harada C., Guo Y., Narisawa K., Ohta H.,
RA Takahashi H., Shirai M.;
RT "Non-Contiguous Finished Genome Sequence of Streptomyces parvulus 2297
RT Integrated Site-Specifically with Actinophage R4.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401}.
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; CP015866; ANJ05549.1; -; Genomic_DNA.
DR RefSeq; WP_064725920.1; NZ_CP015866.1.
DR AlphaFoldDB; A0A191US65; -.
DR KEGG; spav:Spa2297_00255; -.
DR Proteomes; UP000078468; Chromosome.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 3.90.182.10; Toxin - Anthrax Protective Antigen;domain 1; 1.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR006103; Glyco_hydro_2_cat.
DR InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR InterPro; IPR006104; Glyco_hydro_2_N.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR006558; LamG-like.
DR InterPro; IPR037524; PA14/GLEYA.
DR InterPro; IPR011658; PA14_dom.
DR PANTHER; PTHR42732; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR42732:SF2; BETA-MANNOSIDASE; 1.
DR Pfam; PF00703; Glyco_hydro_2; 1.
DR Pfam; PF02836; Glyco_hydro_2_C; 1.
DR Pfam; PF02837; Glyco_hydro_2_N; 1.
DR Pfam; PF13385; Laminin_G_3; 1.
DR Pfam; PF07691; PA14; 1.
DR SMART; SM00560; LamGL; 1.
DR SMART; SM00758; PA14; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF56988; Anthrax protective antigen; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS51820; PA14; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ANJ05549.1};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..34
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 35..1095
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008248257"
FT DOMAIN 54..198
FT /note="PA14"
FT /evidence="ECO:0000259|PROSITE:PS51820"
FT REGION 310..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 888..920
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1095 AA; 118767 MW; C8AB5EF30273C2F7 CRC64;
MTRPHNRPRA RAWALLTAAA LVLPTTGFTV SATAAETASG TSTLAAEKDG ASAVQVQGLK
GEYFSMSAPG ARDFAELGGT VLDPQVNFNG LTSTFQELTG RTEHTTARWT GQIAAPATGD
YTFHAIGDNG FRLFIDGEPV IDHWQPDWDN EQTSAAVRLN ADEKHDFRLE MFQDTGGANM
FLRWSTPTMA KQIVPMSAFT PPDDFEVYPL ELNVGGDGRQ VRARFEGRVG GVDGLAEHVE
VEADTTPMPV KSVRVAPGDR NSLLITLSEP IQKDQQVKFT YDGEAGLTDG GEAVPEVVRY
AQNASTHRLT TPWGDKVDER NPLPEYPRPQ QVRSQWKNLN GPWQFSAAEA GEQPVFGRNL
DEKIIVPFPV ESQLSGLERH EDHMFYRRLV EVPKSWKVGK SDKAGNRLKL NFGAVDYQAR
VFVNGKKVAE HTGGYNAFSA DITDALKGKG PQEVVVAVTD TGGANQPMGK QSRTPGGIFY
TQSSGIWQTV WMEPVAPASV DNVVTTPDID TGSLAVTVES GDASARARVE AVARDKRGKV
VGRVSGPANQ KLRLPVAEQH LWSPDDPYLY DLDVKLVDGR STDRVGGYFG MRKISVEKVG
GFPKLVLNGK PVFSLATLDQ GFWPDGLYTA PSDDALAFDL EAHKKLGFNA VRKHIKVESP
RWFYHADRLG LLVWQDFVSG NFPDESGQQA FVDQGTEMMR QHHNSPSIIG WIVFNEGWGE
WNREATGRLA ESVKAADPSR IVNAHSGVNC CNSKGDSGKG DIIDHHDYNN EDPPFPDATR
AAMDGEHGGF TLRTPGHMWP GAPTVIYSGV ADKEALTRKY VENTEKFYLA QAGAELSGSV
YTQITDLENE LNGLYTYDRR EIKVDPVRVR EINRKVIAAG AAAGDRAPLT GGGSWSLDEG
AGATAGDSGP NGRDLTLAEG TGWTPGVSGS ALKFDGQGQS AETDGPVLDT TGSYSVSAWV
RLDALPGNYA TAVSQDTRRQ ASPFYLQYGQ GAFAFSTPGE NRARVAVTPE TGRWYHLVGV
RDGADDRLSL YVDGEPAATA AAGPAYPSTG PLTVGRAQWD GNPTDFWNGA VDQVHAYDKA
LTAEEVRALF TEERP
//
