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Database: UniProt
Entry: A0A1E7JIZ9_9ACTN
LinkDB: A0A1E7JIZ9_9ACTN
Original site: A0A1E7JIZ9_9ACTN 
ID   A0A1E7JIZ9_9ACTN        Unreviewed;       871 AA.
AC   A0A1E7JIZ9;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Glycosyl hydrolase family 2 {ECO:0000313|EMBL:OEU86436.1};
GN   ORFNames=AN215_27405 {ECO:0000313|EMBL:OEU86436.1};
OS   Streptomyces abyssalis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=933944 {ECO:0000313|EMBL:OEU86436.1, ECO:0000313|Proteomes:UP000176087};
RN   [1] {ECO:0000313|EMBL:OEU86436.1, ECO:0000313|Proteomes:UP000176087}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCSIO 10390 {ECO:0000313|EMBL:OEU86436.1,
RC   ECO:0000313|Proteomes:UP000176087};
RX   PubMed=27446038; DOI=10.3389/fmicb.2016.00998;
RA   Tian X., Zhang Z., Yang T., Chen M., Li J., Chen F., Yang J., Li W.,
RA   Zhang B., Zhang Z., Wu J., Zhang C., Long L., Xiao J.;
RT   "Comparative Genomics Analysis of Streptomyces Species Reveals Their
RT   Adaptation to the Marine Environment and Their Diversity at the Genomic
RT   Level.";
RL   Front. Microbiol. 7:998-998(2016).
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:OEU86436.1}.
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DR   EMBL; LJGT01000041; OEU86436.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E7JIZ9; -.
DR   STRING; 933944.AN215_27405; -.
DR   PATRIC; fig|933944.5.peg.3803; -.
DR   Proteomes; UP000176087; 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:OEU86436.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000176087}.
FT   DOMAIN          21..165
FT                   /note="PA14"
FT                   /evidence="ECO:0000259|PROSITE:PS51820"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          427..447
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          504..540
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   871 AA;  95327 MW;  BC6E747E3045EC22 CRC64;
     MAVSLGSVRP AAAAPPGQAP PVVHGLKGEY WTQSAPGAYD FGTLEATAFD PSLDFADLEP
     RLKERSGRAD HASVRWTGSV TPTRTGEHTF HITGDNGFRM WVDDELVIDH WVPDWDNEQN
     SAPVRLREGA RHSVKIEYFE EEGGSGLHVR WTPPGGEKTA IPQSAYTPPE DFDYDGPAEV
     RVGTSGRTLE MAFAQRLAEP PAAFPEHLKA VIGGVEWPLD GARLDPDDDH RLVVTLPEPV
     VGQGGAADVR YDGDGGLAGA DGEQVGAFWT AGENGSEYQL RTDWAEEVGP DNALPEYPRP
     QLKRDQWRNL NGIWQFAGAE KGERPPTGEK RRLGEKVLVP YPVESQLSGV ERHEERMWYK
     RSFTVPEGWD IGSGKRLYLN FDAVDWHAAV YVNGERVGAH KGGYDRFTVD VTDALRPGRY
     QELVVGVHDP TDSPEGENPP VGKQRLEPEG IWYTPSSGIW QTVWMEPVAA EHTTDVKTTP
     DVSGEQVTVT ARGVPDGVPV TAVAYDTRGG KTGGREGPGS ERGRGVGRAT GTGDEPFDVP
     VPDPKLWSPD DPHLYTLKVT VGEGGSADAV ESYFGMREIA VKTVDGKRRM VLNGEPVFSM
     ATLDQGFWPD GLYTAPTDEA LAYDLRAHKE LGFNSVRKHI KVEPDRWFYH ADRLGLLVWQ
     DMPSMRSDRT PDQAARGQYE HEMKRMIEQH DSHPSVIMWV TFNEGWGQYD QARIADYAKG
     LDPTRLVNNM SGHNCCGAVD GGNGDISDAH GYPGAQLPEP DGERALVSGE YGGLGLAVPG
     HSWPVRHTYV GVEKEKYTDE YLTKLKDIEQ FAACEGSSGA VYTQITDLEG ELNGLMTYDR
     KVGKADTGRL AAAHAALLKG AAEGTLTCER G
//
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