ID M0MPD1_9EURY Unreviewed; 610 AA.
AC M0MPD1;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Glycoside hydrolase family protein {ECO:0000313|EMBL:EMA46579.1};
GN ORFNames=C446_01001 {ECO:0000313|EMBL:EMA46579.1};
OS Halobiforma nitratireducens JCM 10879.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Halobiforma.
OX NCBI_TaxID=1227454 {ECO:0000313|EMBL:EMA46579.1, ECO:0000313|Proteomes:UP000011607};
RN [1] {ECO:0000313|EMBL:EMA46579.1, ECO:0000313|Proteomes:UP000011607}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10879 {ECO:0000313|EMBL:EMA46579.1,
RC ECO:0000313|Proteomes:UP000011607};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class II subfamily. {ECO:0000256|ARBA:ARBA00009121}.
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:EMA46579.1}.
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DR EMBL; AOMA01000007; EMA46579.1; -; Genomic_DNA.
DR RefSeq; WP_006671173.1; NZ_AOMA01000007.1.
DR AlphaFoldDB; M0MPD1; -.
DR STRING; 1227454.C446_01001; -.
DR PATRIC; fig|1227454.3.peg.196; -.
DR eggNOG; arCOG07581; Archaea.
DR OrthoDB; 8638at2157; -.
DR Proteomes; UP000011607; 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; cd00146; PKD; 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 Gene3D; 2.60.40.10; Immunoglobulins; 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; IPR013783; Ig-like_fold.
DR InterPro; IPR022409; PKD/Chitinase_dom.
DR InterPro; IPR000601; PKD_dom.
DR InterPro; IPR035986; PKD_dom_sf.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR11177; CHITINASE; 1.
DR PANTHER; PTHR11177:SF317; CHITINASE 11; 1.
DR Pfam; PF02839; CBM_5_12; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR Pfam; PF18911; PKD_4; 1.
DR SMART; SM00495; ChtBD3; 1.
DR SMART; SM00636; Glyco_18; 1.
DR SMART; SM00089; PKD; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51055; Carbohydrate binding domain; 1.
DR SUPFAM; SSF54556; Chitinase insertion domain; 1.
DR SUPFAM; SSF49299; PKD domain; 1.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
DR PROSITE; PS50093; PKD; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EMA46579.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000011607}.
FT DOMAIN 112..175
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 183..610
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT REGION 64..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..97
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 610 AA; 68112 MW; 18314086D57C9004 CRC64;
MKRTRRNVLS NATKLSALLA GIGASGAVAA EGNEYPEWDP ETVYTSGDRV IYEGYVWEAQ
WWTRGNEPGE GGEWGPWEEI EEHDDDDDED EDEDEDELTA RFTVSDQFPA PGEEIEFDAS
DSEGEIDSYE WEFEDGTTAS GDVVTRSFDE GQYDVTLTVE GADGETDTDS IRITAGRPSS
DEKRVVAYYR QWAQYDRDYV PADIPYDQVT HVQYAFARPE SDGSVTLVGD SHGQQAFWGE
EDWQGVEGGT FAEFAEERDD TKFVLSIGGW GDSRYFSDAA LTQESREQFA EDCIEWIERG
NLDGIDIDWE FPGGGGCTSE DADEPASVCP SDGNIVREGD QERFTLLCET VRERLDEHAQ
EVGRDEPYEL TAAVSANPEV VEGIEDGNDG LEHERLSEVL DFVLVMTFDY AGVWSETTRH
HAPLKANPDD PFDDADSWNA EYALQYWEQQ GWDPDQINMA VPFYGRSWDG VQPPEDAVGT
GEDDGLFQAF EGDGSDASMD GSYPSPPGQP GSQLGGVFEW FDLEGDGRGG SNSVDLESDD
WEVYFDEDAV AAWAWNSDSR EMISYESQES MEAKMQWLRD SPYGGTMLWA IGGDTYEEEL
IDTLWTNLNG
//
