ID A0A1I6KJU0_9EURY Unreviewed; 765 AA.
AC A0A1I6KJU0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Endo-1,4-beta-xylanase, GH35 family {ECO:0000313|EMBL:SFR91512.1};
GN ORFNames=SAMN05216559_0931 {ECO:0000313|EMBL:SFR91512.1};
OS Halomicrobium zhouii.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Halomicrobium.
OX NCBI_TaxID=767519 {ECO:0000313|EMBL:SFR91512.1, ECO:0000313|Proteomes:UP000199062};
RN [1] {ECO:0000313|EMBL:SFR91512.1, ECO:0000313|Proteomes:UP000199062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10457 {ECO:0000313|EMBL:SFR91512.1,
RC ECO:0000313|Proteomes:UP000199062};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FOZK01000001; SFR91512.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6KJU0; -.
DR STRING; 767519.SAMN05216559_0931; -.
DR OrthoDB; 8638at2157; -.
DR Proteomes; UP000199062; Unassembled WGS sequence.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR CDD; cd04080; CBM6_cellulase-like; 1.
DR CDD; cd00146; PKD; 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 InterPro; IPR006584; Cellulose-bd_IV.
DR InterPro; IPR005084; CMB_fam6.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR044846; GH10.
DR InterPro; IPR001000; GH10_dom.
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; PTHR31490:SF88; BETA-XYLANASE; 1.
DR PANTHER; PTHR31490; GLYCOSYL HYDROLASE; 1.
DR Pfam; PF03422; CBM_6; 1.
DR Pfam; PF00331; Glyco_hydro_10; 1.
DR Pfam; PF18911; PKD_4; 1.
DR SMART; SM00606; CBD_IV; 1.
DR SMART; SM00633; Glyco_10; 1.
DR SMART; SM00089; PKD; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF49299; PKD domain; 1.
DR PROSITE; PS51175; CBM6; 1.
DR PROSITE; PS51760; GH10_2; 1.
DR PROSITE; PS50093; PKD; 1.
DR PROSITE; PS51318; TAT; 1.
PE 4: Predicted;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycosidase {ECO:0000313|EMBL:SFR91512.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:SFR91512.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000199062};
KW Xylan degradation {ECO:0000313|EMBL:SFR91512.1}.
FT DOMAIN 121..412
FT /note="GH10"
FT /evidence="ECO:0000259|PROSITE:PS51760"
FT DOMAIN 508..649
FT /note="CBM6"
FT /evidence="ECO:0000259|PROSITE:PS51175"
FT DOMAIN 683..765
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 59..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 651..684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..471
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..491
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..675
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 765 AA; 82274 MW; 19185A6DC286313E CRC64;
MEDDDRRPVR DESNGSEDEP RDVEVVPEDE TKSRRNDFAA MDRRDYMKAV GAAAAATGLG
AAASSPAAGA TADTSKTPEE RIQEHRTGDL EVVVENSDGS TVSGAEVSVT QQSHDFRWGT
AVHADTLINQ NSAGDNYREY IPELFNTAVM ENQHKWALWE QNTQLADDAT NWILDQGMDM
RGHVCVYGVD YAVPSDVQTA IDNGDTETVR ELSMQHIDEI MNHYGSDIHE WEVLNEVQHS
TTIIDPFTSN PETAQIVADW YQRAEEVRPS GTTLAVNDYN AIAGDYGSDQ QGYQTHIQHL
LDNGIDLETT GLQCHFAQNE TLSDSQIISI LNEYGQLTDT LKITEYDQSG SNWDESAKAD
WFERFLRLTF SHPGVGSFLV WGFWDGRHWE DDAPFFYEDW SEKPSLDVWR NLVYGEWWND
ETGTTDSGGT YSTNAFLGEH EITVSTDSDS TTQTVSVTST GGTSVTVTVD GSGTGDGDDG
DDGDDGSDGD DGSGEQQPYN GSPHAVPGTI QAEEYDQGGS GVAYSDNTSE NEGGAMRTDE
AVDISSNSAG SGYSIGYIES GEWVEYTVDV EQAGEYTLEA LVASDSGGGS FHLEVDGQDV
SGTVSFGATG GWDSWETVST SGVSLDAGQQ VVRVAMDESW WDLNNVSLSL DGSTGGDDDG
SGDTGGDDDD GGTGGDGDTG GDLIAEISPS TTAASVGDLV QFNINDTSGS GNWITSLEWD
LGNGTTATGW YTDERYQSAG SYTVTLTATD NEGTSTTDEV TVDIS
//
