ID   Q7WTN6_RHOMR            Unreviewed;       997 AA.
AC   Q7WTN6;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   27-MAR-2024, entry version 105.
DE   SubName: Full=Xylanase {ECO:0000313|EMBL:CAA72323.2};
OS   Rhodothermus marinus (Rhodothermus obamensis).
OC   Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Rhodothermaceae;
OC   Rhodothermus.
OX   NCBI_TaxID=29549 {ECO:0000313|EMBL:CAA72323.2};
RN   [1] {ECO:0000313|EMBL:CAA72323.2}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 4252 {ECO:0000313|EMBL:CAA72323.2};
RX   PubMed=9294005; DOI=10.1016/S0167-4781(97)00093-6;
RA   Nordberg Karlsson E.M., Bartonek Roxaa E., Holst O.;
RT   "Cloning and sequence of a thermostable multidomain xylanase from the
RT   bacterium Rhodothermus marinus.";
RL   Biochim. Biophys. Acta 1353:118-124(1997).
RN   [2] {ECO:0000313|EMBL:CAA72323.2}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 4252 {ECO:0000313|EMBL:CAA72323.2};
RA   Bu Q., Yang S., Wan J.;
RL   Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0007829|PDB:3JXS}
RP   X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 212-376 IN COMPLEX WITH CALCIUM.
RX   PubMed=19950365; DOI=10.1002/prot.22642;
RA   Gullfot F., Tan T.C., von Schantz L., Karlsson E.N., Ohlin M., Brumer H.,
RA   Divne C.;
RT   "The crystal structure of XG-34, an evolved xyloglucan-specific
RT   carbohydrate-binding module.";
RL   Proteins 78:785-789(2010).
RN   [4] {ECO:0007829|PDB:2Y64, ECO:0007829|PDB:2Y6G}
RP   X-RAY CRYSTALLOGRAPHY (1.08 ANGSTROMS) OF 212-376 IN COMPLEX WITH CALCIUM.
RX   PubMed=22434778; DOI=10.1093/glycob/cws063;
RA   von Schantz L., Hakansson M., Logan D.T., Walse B., Osterlin J.,
RA   Nordberg-Karlsson E., Ohlin M.;
RT   "Structural basis for carbohydrate-binding specificity--a comparative
RT   assessment of two engineered carbohydrate-binding modules.";
RL   Glycobiology 22:948-961(2012).
RN   [5] {ECO:0007829|PDB:5DPN}
RP   STRUCTURE (1.60 ANGSTROMS) OF 212-376 IN COMPLEX WITH CALCIUM.
RX   PubMed=26451738; DOI=10.1021/acs.biochem.5b01058;
RA   Fisher S.Z., von Schantz L., Hakansson M., Logan D.T., Ohlin M.;
RT   "Neutron crystallographic studies reveal hydrogen bond and water-mediated
RT   interactions between a carbohydrate-binding module and its bound
RT   carbohydrate ligand.";
RL   Biochemistry 54:6435-6438(2015).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC       {ECO:0000256|ARBA:ARBA00007495}.
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DR   EMBL; Y11564; CAA72323.2; -; Genomic_DNA.
DR   PDB; 2Y64; X-ray; 1.40 A; A=212-376.
DR   PDB; 2Y6G; X-ray; 1.30 A; A=212-376.
DR   PDB; 2Y6H; X-ray; 1.08 A; A=212-376.
DR   PDB; 2Y6J; X-ray; 1.70 A; A=212-376.
DR   PDB; 2Y6K; X-ray; 1.36 A; A=212-376.
DR   PDB; 2Y6L; X-ray; 1.28 A; A=212-376.
DR   PDB; 3JXS; X-ray; 1.60 A; A/B/C=212-376.
DR   PDB; 5DPN; Other; 1.60 A; A=212-376.
DR   PDBsum; 2Y64; -.
DR   PDBsum; 2Y6G; -.
DR   PDBsum; 2Y6H; -.
DR   PDBsum; 2Y6J; -.
DR   PDBsum; 2Y6K; -.
DR   PDBsum; 2Y6L; -.
DR   PDBsum; 3JXS; -.
DR   PDBsum; 5DPN; -.
DR   AlphaFoldDB; Q7WTN6; -.
DR   SMR; Q7WTN6; -.
DR   CAZy; CBM4; Carbohydrate-Binding Module Family 4.
DR   CAZy; GH10; Glycoside Hydrolase Family 10.
DR   EvolutionaryTrace; Q7WTN6; -.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.4070; -; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR003305; CenC_carb-bd.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR044846; GH10.
DR   InterPro; IPR001000; GH10_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR026444; Secre_tail.
DR   NCBIfam; TIGR04183; Por_Secre_tail; 1.
DR   PANTHER; PTHR31490:SF88; BETA-XYLANASE; 1.
DR   PANTHER; PTHR31490; GLYCOSYL HYDROLASE; 1.
DR   Pfam; PF02018; CBM_4_9; 2.
DR   Pfam; PF00331; Glyco_hydro_10; 1.
DR   SMART; SM00633; Glyco_10; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR   PROSITE; PS51760; GH10_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:2Y64, ECO:0007829|PDB:2Y6G};
KW   Calcium {ECO:0007829|PDB:2Y64, ECO:0007829|PDB:2Y6G};
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Glycosidase {ECO:0000313|EMBL:CAA72323.2};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CAA72323.2};
KW   Metal-binding {ECO:0007829|PDB:2Y64, ECO:0007829|PDB:2Y6G};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW   Xylan degradation {ECO:0000313|EMBL:CAA72323.2}.
FT   DOMAIN          572..892
FT                   /note="GH10"
FT                   /evidence="ECO:0000259|PROSITE:PS51760"
FT   BINDING         219
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:2Y64, ECO:0007829|PDB:2Y6G"
FT   BINDING         221
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:2Y64, ECO:0007829|PDB:2Y6G"
FT   BINDING         232
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0007829|PDB:2Y6L"
FT   BINDING         232
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0007829|PDB:2Y64, ECO:0007829|PDB:2Y6G"
FT   BINDING         233
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0007829|PDB:2Y6L"
FT   BINDING         238
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0007829|PDB:2Y6L"
FT   BINDING         238
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0007829|PDB:2Y64, ECO:0007829|PDB:2Y6G"
FT   BINDING         239
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0007829|PDB:2Y6L"
FT   BINDING         262
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:2Y64, ECO:0007829|PDB:2Y6G"
FT   BINDING         265
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:2Y64, ECO:0007829|PDB:2Y6G"
FT   BINDING         370
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:2Y64, ECO:0007829|PDB:2Y6G"
SQ   SEQUENCE   997 AA;  110343 MW;  CE6ABF99CC4AC1A9 CRC64;
     MRTATDLRFL RNAVGNASRS AIFLFLVFSL VGQAWGQTPA NVNGSFESTP AGVVTDLAGG
     VEGWVLNVGS LVTNPPVFEV VEATDAPHGS KVLAVTVNGA GNNPWDIEAT AFPVNVEPGV
     TYTYTIWARA EQDGAVVSFT VGNQSYQEYG RLHEQQITTE WQPYTFEFTV SDQETVIRAP
     IHFGYAANAG NTIYIDALVI MGPEPEPAGP ELVANINGGF ESTPAGVVTD LAEGVEGWDL
     NVGSSVTNPP VFEVLETSDA PEGNKVLAVT VNGVGNNPWD IEATAFPVNV RPGVTYTYTI
     WARAEQDGAV VSFTVGNQSF QEYGRLHEQQ ITTEWQPFTF EFTVSDQETV IRAPIHFGYA
     ANVGNTIYID GLAIVDSVGA WRPVIVEAED GELGSEWAVE TEGNVTYITI TTDYNETTGD
     ADHPGENRTA TYQVTFPAPG WYDLYARVYV GPETFNDDSF FYADSFGVKD PESPDDWIIA
     NQLRAAGYTE PDEYVTGLGA AGSEVWKWIN LSENSFNDVP SDSFYVSPES LTVTFMIGAR
     ENGLRIDKLA FGRSDLLYTV ADLDTGGPGS PEPEEPPVVL PERPLAADVD KFLGNIYSPS
     QVENFEYYWN CVTPENAGKW GSVEGTRDQM NWSSLDAAYA LARDNGFCFN FHVLLWGAQQ
     PAWISELSPE EQLEEIQEWF QAVAERYSFT ASPFDVVQVV NEPLHQPPDG QEGRANYIEA
     LGGAGETGWD WVITAFELAR QIFPEGTRLM INDYGILSSL ETAQQYLELI QLLKERNLID
     VIGVQGHAFS TRSGAPIQEV LDLLATTGLP IQVTEMDIDG NPNQSPFVTR EQSEQNQLRD
     MQRIFPTVWY HPAVEGVTFW GWRPGLWRND YEAYLVYSNG AERPAMVWLR EFMEAYRESY
     LSANEPEGTL PEELSVVSWP NPSRGQVRFR YALPFEAEVR LQVFDVLGRE VMTLASGRHR
     AGVYEVAFDG RHLPSGLYLY RLEANGRVRS GRLVLMR
//