ID   A0A0C2JCS0_9ACTN        Unreviewed;       532 AA.
AC   A0A0C2JCS0;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   SubName: Full=FenI {ECO:0000313|EMBL:KIH96745.1};
GN   ORFNames=LP52_23075 {ECO:0000313|EMBL:KIH96745.1};
OS   Streptomonospora alba.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Nocardiopsaceae; Streptomonospora.
OX   NCBI_TaxID=183763 {ECO:0000313|EMBL:KIH96745.1, ECO:0000313|Proteomes:UP000031675};
RN   [1] {ECO:0000313|Proteomes:UP000031675}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YIM 90003 {ECO:0000313|Proteomes:UP000031675};
RX   PubMed=25601074; DOI=10.1016/j.chembiol.2014.11.017;
RA   Metelev M., Tietz J.I., Melby J.O., Blair P.M., Zhu L., Livnat I.,
RA   Severinov K., Mitchell D.A.;
RT   "Structure, bioactivity, and resistance mechanism of streptomonomicin, an
RT   unusual lasso Peptide from an understudied halophilic actinomycete.";
RL   Chem. Biol. 22:241-250(2015).
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:KIH96745.1}.
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DR   EMBL; JROO01000049; KIH96745.1; -; Genomic_DNA.
DR   RefSeq; WP_040276497.1; NZ_JROO01000049.1.
DR   AlphaFoldDB; A0A0C2JCS0; -.
DR   STRING; 183763.LP52_23075; -.
DR   OrthoDB; 9773203at2; -.
DR   Proteomes; UP000031675; Unassembled WGS sequence.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProt.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR003790; GHL10.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   PANTHER; PTHR43405; GLYCOSYL HYDROLASE DIGH; 1.
DR   PANTHER; PTHR43405:SF1; GLYCOSYL HYDROLASE DIGH; 1.
DR   Pfam; PF02638; GHL10; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000031675};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..532
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5039120572"
FT   DOMAIN          58..369
FT                   /note="Glycosyl hydrolase-like 10"
FT                   /evidence="ECO:0000259|Pfam:PF02638"
FT   REGION          28..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   532 AA;  58337 MW;  F27A476A5BC0F298 CRC64;
     MRRLLLSAAA MAATVPLLGA CVPWSSSGAD DGAGGSEAHG AMPAPGECDT DAADPKRQMR
     GTWITSVRNI DWPSESGLGK QEQQQELRDM LDRAAGLGLN TVFLHVRPTA DALYGSDKEP
     WARYLTGEQG GDPGYDPLSY AVKQAHQRGI ELHAWFNPYR VGWKDPDLEN LAPGHPARQH
     PDWLVEYGEE GYLDPGNPDV RDWVTDVVLD VVKRYDVDGV HFDDYFYPYP GEGEEFDDDE
     SFRRHGDGFD SRADWRRNNV DTLVADVHEG IQKTKPWVRF GISPFGIWRN ADSDPAGSDT
     SGLESYSAQY ADTLTWIQEG TVDYILPQLY WPRGFDTADY AELVPWWSEQ VAGTDVDLYI
     GQAAYRVGEE GFRGADALSR QLDLNAEHSE VGGDVYFSIS DLTGRAEEAM ATVGDEHYTR
     PALPPVSDSA GDPPEAVSEL DAERVSPGKV RLNWNTVEDA RFYAVYRVPG EGGDPCDLAD
     ASHLIGVTGA GGDKRAFTDT DPAEGKVRYH VTALDDHRVE SGPGPAARLS PG
//