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Database: UniProt
Entry: A0A238WIB4_9ACTN
LinkDB: A0A238WIB4_9ACTN
Original site: A0A238WIB4_9ACTN 
ID   A0A238WIB4_9ACTN        Unreviewed;       491 AA.
AC   A0A238WIB4;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Chitinase family 18 {ECO:0000313|EMBL:SNR46305.1};
GN   ORFNames=SAMN06264365_102573 {ECO:0000313|EMBL:SNR46305.1};
OS   Actinoplanes regularis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Actinoplanes.
OX   NCBI_TaxID=52697 {ECO:0000313|EMBL:SNR46305.1, ECO:0000313|Proteomes:UP000198415};
RN   [1] {ECO:0000313|EMBL:SNR46305.1, ECO:0000313|Proteomes:UP000198415}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43151 {ECO:0000313|EMBL:SNR46305.1,
RC   ECO:0000313|Proteomes:UP000198415};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family.
CC       {ECO:0000256|RuleBase:RU004453}.
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DR   EMBL; FZNR01000002; SNR46305.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A238WIB4; -.
DR   OrthoDB; 9775889at2; -.
DR   Proteomes; UP000198415; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
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   CDD; cd12215; ChiC_BD; 1.
DR   CDD; cd06548; GH18_chitinase; 1.
DR   Gene3D; 3.10.50.10; -; 1.
DR   Gene3D; 2.10.10.20; Carbohydrate-binding module superfamily 5/12; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR003610; CBM_fam5/12.
DR   InterPro; IPR036573; CBM_sf_5/12.
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   InterPro; IPR006311; TAT_signal.
DR   PANTHER; PTHR11177; CHITINASE; 1.
DR   PANTHER; PTHR11177:SF317; CHITINASE 11; 1.
DR   Pfam; PF00704; Glyco_hydro_18; 1.
DR   SMART; SM00495; ChtBD3; 1.
DR   SMART; SM00636; Glyco_18; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51055; Carbohydrate binding domain; 1.
DR   SUPFAM; SSF54556; Chitinase insertion domain; 1.
DR   PROSITE; PS01095; GH18_1; 1.
DR   PROSITE; PS51910; GH18_2; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR   PROSITE; PS51318; TAT; 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   Reference proteome {ECO:0000313|Proteomes:UP000198415};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..491
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038686931"
FT   DOMAIN          123..491
FT                   /note="GH18"
FT                   /evidence="ECO:0000259|PROSITE:PS51910"
FT   REGION          85..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        99..113
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   491 AA;  51277 MW;  331B865A25A72C72 CRC64;
     MGKSLRRALL AGAVVIGASA SVPLVQANAA TACATAWSAT SVYVKDNSAS QNGHNYTAKW
     WTQNESPDTH SGQWDVWIDN GVCGGTTTPT TAPTTAPTTA PTTTPPTTTP TTAPTTTPPT
     GGKNVVGYFA EWGVYGRNYH VKNLVTSGSA AKLTHILYAF GNTTGGQCSI GDSYADYDRA
     YSAAESVDGV ADTWDTGALR GSFNQLRKLK KQYPNLKVIW SFGGWTWSGG FTQAAANPTA
     FANSCYNLVK DSRWSDVFDG IDIDWEYPNA CGLSCDASGP AAYNNVITAL RNKFGSSFLV
     TSAISADGSN GGKLDVADYA SGIAKLNLVF PMTYDYFGAF AAQGPTAPHS PLTSYTGIPT
     AGFYSDAAIQ KLKSKGVPAN KILLGIGFYG RGWTGVTQAA PGGSATGAAP GTYEAGIEDY
     KVLKNSCPAT GTVGGTAYAY CGSNWWSYDT PSTIAGKMTY AKNQGLGGAF FWEFSGDTSN
     GELISAIKGN L
//
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