ID   D9X8X7_STRVT            Unreviewed;       872 AA.
AC   D9X8X7;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   SubName: Full=Hydrolase {ECO:0000313|EMBL:EFL36380.1};
GN   ORFNames=SSQG_06898 {ECO:0000313|EMBL:EFL36380.1};
OS   Streptomyces viridochromogenes (strain DSM 40736 / JCM 4977 / BCRC 1201 /
OS   Tue 494).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=591159 {ECO:0000313|EMBL:EFL36380.1, ECO:0000313|Proteomes:UP000004184};
RN   [1] {ECO:0000313|Proteomes:UP000004184}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494
RC   {ECO:0000313|Proteomes:UP000004184};
RG   The Broad Institute Genome Sequencing Platform;
RG   Broad Institute Microbial Sequencing Center;
RA   Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA   Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA   Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA   Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA   Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA   Haas B., Nusbaum C., Birren B.;
RT   "Annotation of Streptomyces viridochromogenes strain DSM 40736.";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC       {ECO:0000256|ARBA:ARBA00007401}.
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DR   EMBL; GG657757; EFL36380.1; -; Genomic_DNA.
DR   RefSeq; WP_003994522.1; NZ_GG657757.1.
DR   AlphaFoldDB; D9X8X7; -.
DR   STRING; 591159.SSQG_06898; -.
DR   eggNOG; COG3250; Bacteria.
DR   HOGENOM; CLU_009935_0_0_11; -.
DR   OrthoDB; 9762066at2; -.
DR   Proteomes; UP000004184; Unassembled WGS sequence.
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; 2.60.120.260; 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; 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; 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; PF07691; PA14; 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; 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:EFL36380.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004184};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           31..872
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003131955"
FT   DOMAIN          34..178
FT                   /note="PA14"
FT                   /evidence="ECO:0000259|PROSITE:PS51820"
SQ   SEQUENCE   872 AA;  95658 MW;  892E6AB04ACB3AC6 CRC64;
     MRTGRLRNRT ALLLAALLAL TGLTVAPALA DDPEEIHGLK GEYYTQSAPG AFDFHTLKAT
     TFDQYLDFDN LEPRLNFTTG RSDDVSVRWT GRIVPEKTGA HTFSIIGDNG FRLWIDGELA
     IDHWVDDWDR EQSARPVELT AGQAYDIKVE YFEHYGGSNL HLRWTQPGGG KEPVPQSAFR
     LPAGFDYDGA LAATVQSTGR TLKLDFAQAL AAPPAGFTDH LKAVIGGAEW PLGEARPDPS
     DPTSLLVALD EPVVGNKTGT ARGTADIRYD GRGGLSDTDG NVVKEFLSSG SNHSTYQLRT
     RWADEVGPGN AHPEYPRPQL TRDAWQSLNG RWQFAAAQPG EQPPVGRTLK ERILVPYPVE
     SQLSGVERHE DRMWYRRTFT VPADWHIGSG KRLKLNFGAV DWRSEVYVNG TKVATHEGGY
     DKFAADVTDA LKPGRTQELI VGVYDPTDAA SGENPPLGKQ RLDPSGIWYT PSSGIWQTVW
     MEPVARDHVD SLKLTPDVAG EKLTVEARGV RDGVPVTATA YDGRRKVATA SGRTGRPLTL
     TVHDPHLWSP DDPFLYRLEV KAGADRVGSY FGMRSIAVEK VDGVPRTVLN GKPVFMMATL
     DQGFWPDGLH TAPTDEALAY DLKAHKRLGF NAVRKHIKVE PDRWFYWADR LGLLVWQDMP
     AMTAGVNPST ASRARYEREM KEMIDEHISS PSVVMWVTFN EGWGQYDVGR VAEQAKAWDP
     TRLVNGQSGL NLGADGGTGD IMDEHGYPSP ALPPRPDGER ALVSGEYGGL GLAVPGHAWS
     VQQSYVDVDP ATYTEDYLTK LDEVRALACE GGNGAVYTQI ADVEGELNGF LTYDRAVLKP
     DTARLKSAHE ALIRDASRVT PTGCPAPQPV LD
//