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Database: UniProt
Entry: A0A136M0M5_9BACT
LinkDB: A0A136M0M5_9BACT
Original site: A0A136M0M5_9BACT 
ID   A0A136M0M5_9BACT        Unreviewed;       374 AA.
AC   A0A136M0M5;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   22-FEB-2023, entry version 16.
DE   SubName: Full=Putative sporulation-specific glycosylase YdhD {ECO:0000313|EMBL:KXK27426.1};
DE            EC=3.2.-.- {ECO:0000313|EMBL:KXK27426.1};
GN   Name=ydhD {ECO:0000313|EMBL:KXK27426.1};
GN   ORFNames=TR69_WS6001000302 {ECO:0000313|EMBL:KXK27426.1};
OS   candidate division WS6 bacterium OLB20.
OC   Bacteria; Candidatus Dojkabacteria.
OX   NCBI_TaxID=1617426 {ECO:0000313|EMBL:KXK27426.1, ECO:0000313|Proteomes:UP000070457};
RN   [1] {ECO:0000313|EMBL:KXK27426.1, ECO:0000313|Proteomes:UP000070457}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OLB20 {ECO:0000313|EMBL:KXK27426.1};
RA   Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT   "Improved understanding of the partial-nitritation anammox process through
RT   23 genomes representing the majority of the microbial community.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family.
CC       {ECO:0000256|RuleBase:RU004453}.
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:KXK27426.1}.
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DR   EMBL; JYNZ01000002; KXK27426.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A136M0M5; -.
DR   STRING; 1617426.TR69_WS6001000302; -.
DR   Proteomes; UP000070457; Unassembled WGS sequence.
DR   GO; GO:0008061; F:chitin binding; IEA:InterPro.
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; 3.10.50.10; -; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR011583; Chitinase_II.
DR   InterPro; IPR029070; Chitinase_insertion_sf.
DR   InterPro; IPR001223; Glyco_hydro18_cat.
DR   InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR46066:SF2; CHITINASE DOMAIN-CONTAINING PROTEIN 1; 1.
DR   PANTHER; PTHR46066; CHITINASE DOMAIN-CONTAINING PROTEIN 1 FAMILY MEMBER; 1.
DR   Pfam; PF00704; Glyco_hydro_18; 1.
DR   SMART; SM00636; Glyco_18; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS01095; GH18_1; 1.
DR   PROSITE; PS51910; GH18_2; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000489};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000489};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..374
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007475365"
FT   DOMAIN          42..374
FT                   /note="GH18"
FT                   /evidence="ECO:0000259|PROSITE:PS51910"
SQ   SEQUENCE   374 AA;  41802 MW;  70C00E56FAF6DCDA CRC64;
     MQSLRTICAV LLIIVSGTAC VQPLPEDQDT PPEAVPVATG KPLIHGWIPH WEINAGIDTM
     ESYPLFASVS PVWYEVGAGG TLLPVGGDRD PLIRYSAQTE TQLIPSIASF DHNTFSSLAA
     TDEQLYAHAD AILAEVDRYG YDGIDLDYES VKLEDGPAYM TLIRTLAEEL HAREKLLSVT
     VLAKWGDQVA YGYRPETRAV QDWTEIAVHA DQLRIMTYDF TYQGATYPGP IAPESWVRAV
     TEYAIEKAPR EKLILGVPTY AYEWFQPQGS SETLLQFEPN GLTNPQSESG NARSYPFSTV
     ERILAEYPGE SVFFQGEHIY RYKRSGEDRV VVFTDPQGIL DRYRLAEEYG LAGISFWRLG
     EEGDLYSDLS SYLD
//
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