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Database: UniProt
Entry: A0A1A9C2D0_9ACTN
LinkDB: A0A1A9C2D0_9ACTN
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ID   A0A1A9C2D0_9ACTN        Unreviewed;      1091 AA.
AC   A0A1A9C2D0;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Glycosyl hydrolases family 2, TIM barrel domain {ECO:0000313|EMBL:SBT93874.1};
GN   ORFNames=GA0115233_107328 {ECO:0000313|EMBL:SBT93874.1};
OS   Streptomyces sp. DI166.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1839783 {ECO:0000313|EMBL:SBT93874.1, ECO:0000313|Proteomes:UP000198690};
RN   [1] {ECO:0000313|Proteomes:UP000198690}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DI166 {ECO:0000313|Proteomes:UP000198690};
RA   Varghese N., Submissions Spin;
RL   Submitted (JUN-2016) 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; FLSP01000073; SBT93874.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1A9C2D0; -.
DR   STRING; 1839783.GA0115233_107328; -.
DR   OrthoDB; 9762066at2; -.
DR   Proteomes; UP000198690; 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; 2.60.120.200; -; 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:SBT93874.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198690};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..34
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           35..1091
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008384944"
FT   DOMAIN          51..195
FT                   /note="PA14"
FT                   /evidence="ECO:0000259|PROSITE:PS51820"
FT   REGION          306..327
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          879..920
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1091 AA;  119440 MW;  4A7532E8D25378F6 CRC64;
     MTEHRTRPRA RMWALLAAAA LILPPMGLMP SAVAAEQSAD ASATAASQDA VQTHGLKGEY
     FRMSAPGARD FAELGGTLLD PQINFSGLTS TFEELTGRTE HTTARWTGKL TAPTTGDYTF
     HAIGDNGFRL FIDGEPVIDH WVGDWDREQT SSPVRLTAGE PHEFRLEMFQ DTGGANMFLR
     WSTPTLPKQL VPMSAFTPPD DFEIYPVEPS VKEDGKRVRL RFDGRVGGLG TVKEHLKIEA
     DTTAMPIRSV TSYPGDRNSA LVTLSEPVQK NQQVRVSYDG QGGLSAGGES VPKLIRYAEN
     DSAHRLTTPW GDKVDTKNPL PEYPRPQQVR SQWKNLNGPW QFSGAEEGEE PVFGKNLDEK
     IIVPFPVESQ LSGLERHEDH MFYRKLVDVP SSWKVGKGDR NNRLKLNFGA VDYKARVYVN
     GTKVADHTGG YNAFSVDVTD ALKGTGKQEI VVAVTDTGGA NQPMGKQTTN PGGIFYTQTS
     GIWQTVWMEP VAAASIDDIV ATPDIDTSSL AMKVRSDAAS STARVEAVAR DARGKVVGRV
     SGPANKDLRL PVAKQHLWTP DDPYLYDLDV RLTDGRSTDR VSSYFGMREV GIKKVGGFNK
     LVLNGKPIFS LATLDQGFWP DGLYTAPSDE ALAFDLKAHK KLGFNAVRKH IKVEPDRWFY
     HADKLGLLIW QDFVSGNITN ETGQKAFVDQ GREMMRQHHN SPSVIGWIVF NEGWGEWNRE
     ETGRITDAVK EADPSRVVNA HSGVNCCNSK GDSGRGDIID HHDYNNTDPA FPDERRAAMD
     GEHGGFTLRT PGHMWPGAPT VIYSGVTTKA ELTRKYVENT EQFYLDQAGA ELSGSVYTQI
     TDLENELNGL YTYDRREIKV DPAPVRDINR RIIAAGAAAG SQKPLTGGGH WKLDENSGTT
     ADDEGPNDRP LTLREGASWT PGVSGSALKF DGQKQYAETA GPVLDTAGSY SVAAWVRLDQ
     VPGNYATAVS QDSRATANSF YLQYGHGNFA FSTPDERRAT APVSVERGRW YHLVGVRDAT
     TNQIRLYVDG ELAATATGGA ALPSTGPLTV GRAHWDGSKV DFWNGAVDEV HAFDKALTAK
     EVGDLYGDEK P
//
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