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Database: UniProt
Entry: G2GFL8_9ACTN
LinkDB: G2GFL8_9ACTN
Original site: G2GFL8_9ACTN 
ID   G2GFL8_9ACTN            Unreviewed;      1352 AA.
AC   G2GFL8;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 53.
DE   SubName: Full=Glycosyl hydrolase {ECO:0000313|EMBL:EGX57713.1};
GN   ORFNames=SZN_21511 {ECO:0000313|EMBL:EGX57713.1};
OS   Streptomyces zinciresistens K42.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=700597 {ECO:0000313|EMBL:EGX57713.1, ECO:0000313|Proteomes:UP000004217};
RN   [1] {ECO:0000313|EMBL:EGX57713.1, ECO:0000313|Proteomes:UP000004217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K42 {ECO:0000313|EMBL:EGX57713.1,
RC   ECO:0000313|Proteomes:UP000004217};
RA   Lin Y., Hao X., Johnstone L., Miller S.J., Wei G., Rensing C.;
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC       {ECO:0000256|ARBA:ARBA00007401}.
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:EGX57713.1}.
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DR   EMBL; AGBF01000081; EGX57713.1; -; Genomic_DNA.
DR   PATRIC; fig|700597.3.peg.4224; -.
DR   Proteomes; UP000004217; 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; 4.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR   InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR   InterPro; IPR043534; EBDG/EBM.
DR   InterPro; IPR000421; FA58C.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
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; IPR041351; Ig_GlcNase.
DR   InterPro; IPR006311; TAT_signal.
DR   PANTHER; PTHR43536; MANNOSYLGLYCOPROTEIN ENDO-BETA-MANNOSIDASE; 1.
DR   PANTHER; PTHR43536:SF1; MANNOSYLGLYCOPROTEIN ENDO-BETA-MANNOSIDASE; 1.
DR   Pfam; PF00754; F5_F8_type_C; 3.
DR   Pfam; PF00703; Glyco_hydro_2; 1.
DR   Pfam; PF02837; Glyco_hydro_2_N; 1.
DR   Pfam; PF18368; Ig_GlcNase; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 3.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 4.
DR   PROSITE; PS50022; FA58C_3; 3.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EGX57713.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004217};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           31..1352
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003429439"
FT   DOMAIN          28..200
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|PROSITE:PS50022"
FT   DOMAIN          599..751
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|PROSITE:PS50022"
FT   DOMAIN          779..837
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|PROSITE:PS50022"
FT   REGION          619..644
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          765..785
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1352 AA;  147428 MW;  2638ABC991198634 CRC64;
     MPSRRTVLSA GSTLLAGFGI GMSLPSVATA AGTGRPGGTA RELAAYRPVT VSSTDYAPTP
     AEFAVDGLDT VGVRGTGWRA AGGDPQWISV DLQAQCEVRS LRLTFEATAD DPPYVDAPGG
     NPRDNTTGQE ILSSCAVSFV VETSRDGTAW TAVYRTDSGR GGVAEIELER PVTARWVRMT
     VTKRSNANPL GLNGLQVYGT CDARRPGATG WTDWGVNRRT PPALKVAADG TVALESGWDL
     TMDDWAGAEG PALSRTSVDT SRWLPAAVPG TVLTSLVDEG HLPDPVAGFN NLHVPEALSR
     HSWWYRRQFK LPEGLRTGSG RRVWLEFDGV NHEAEVWLNG KRVGTVTYPF ARAALDVTEL
     LADRGENALA VRITPMPYPG SPADKGPAGL AFVDAGANMM NRNSPTYLAA SGWDWMPAVR
     DRAAGIWNHV RLRSTGAAVL GDPRVDTRLP GLPDTSTAEL TVVVPVRNAD SASRSVTVAA
     ELLGTRLTRT VTVAAGESTD VTFTPQSHSR LRLRKPKLWW PNGYGQPDLH GLALTASVAG
     QVSDRRTTRF GIRQYGYEYD VPLTFQSGSD SYAQTVEPGR QSARHVRIRC LTRATSWGSS
     LWSLSVVDSA SPGTDLALGR PATASSVDDG GNAAGNATDG DPKTRWSSAF EDDQWIRVDL
     GSQVSFDRVV LTWEQAYAKT YVVQVSDDGE TWRDTASVDN GAAPLPFRTS GSAALQNVEF
     AARTARHVRV LCGKRATTWG TSLWSLSVVD SASPGTDLAL RKEATASSAQ EGAASNAVDG
     DPNTRWSSAY EDGQWIRVDL GERVRFDRVV ILWEQAYAKT YTVQVSDDGE QWTDVKSVDN
     STVPLAISVN GVRVFCRGGN WGWDELLRRM PAERIDAAVR MHRDMNFTMI RNWLGSSNRE
     EFYASCDEQG LLVWNDFPNA WGMNPPDHKA FLSLAQDTVR RYRSHPSIVV WCGANEGNPP
     AALDEGMRAA VRAEAPDLLY QNNSASGIVT GGGPYGWVEP GRYFSPDTYG SGDFGFHTEI
     GMPVLPTAQT MRNLVGDEPE WPVKDAWYYH DWSTRGNQAP QNYRAAVESR LGEVKDLDDF
     CAKAQFVNYE NFRAMFEAWN SRLWDNATAL LLWMSHPAWY STVWQTYDYD FDVNGAYYGC
     RKASEAVHVQ ADPVSGEVIA VNHTPRRISG ATVTARRYDL SGRALGPELR EKVDVGASAT
     APAFTAGWTD GLPDFHLLRL RLVDARGEVL AENTYWRYRE PAHMRALNQA ARTRVSLEIT
     GTDRSGGRHG LTARVRNRGT TVAAMVRLSL LDAEKGGRVL PTLYSDNYLW LLPGESRTLT
     LSWPADALPS GRPAVRLEGH NVPETTVGRG RG
//
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