UniProt: B2AFS1

Database: UniProt
Entry: B2AFS1_PODAN

LinkDB:  B2AFS1_PODAN 
Original site:  B2AFS1_PODAN

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Ontology (6)   
   GO (4)   
   CAZY (2)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (2)   
   EMBL (2)   
Protein domain (12)   
   InterPro (5)   
   Pfam (2)   
   PROSITE (3)   
   SMART (2)   
Literature (2)   
   PubMed (2)   
All databases (26)   

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ID   B2AFS1_PODAN            Unreviewed;       418 AA.
AC   B2AFS1;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   27-MAR-2024, entry version 88.
DE   RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE            EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN   ORFNames=PODANS_5_12430 {ECO:0000313|EMBL:CAP62292.1};
OS   Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
OS   (Pleurage anserina).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Podosporaceae; Podospora;
OC   Podospora anserina.
OX   NCBI_TaxID=515849 {ECO:0000313|EMBL:CAP62292.1};
RN   [1] {ECO:0000313|EMBL:CAP62292.1, ECO:0000313|Proteomes:UP000001197}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC   {ECO:0000313|Proteomes:UP000001197}, and S mat+
RC   {ECO:0000313|EMBL:CAP62292.1};
RX   PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77;
RA   Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O., Porcel B.M.,
RA   Couloux A., Aury J.-M., Segurens B., Poulain J., Anthouard V.,
RA   Grossetete S., Khalili H., Coppin E., Dequard-Chablat M., Picard M.,
RA   Contamine V., Arnaise S., Bourdais A., Berteaux-Lecellier V., Gautheret D.,
RA   de Vries R.P., Battaglia E., Coutinho P.M., Danchin E.G.J., Henrissat B.,
RA   El Khoury R., Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H.,
RA   Debuchy R., Wincker P., Weissenbach J., Silar P.;
RT   "The genome sequence of the model ascomycete fungus Podospora anserina.";
RL   Genome Biol. 9:R77.1-R77.22(2008).
RN   [2] {ECO:0000313|EMBL:CAP62292.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=S mat+ {ECO:0000313|EMBL:CAP62292.1};
RA   Genoscope - CEA;
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000001197}
RP   GENOME REANNOTATION.
RC   STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC   {ECO:0000313|Proteomes:UP000001197};
RX   PubMed=24558260; DOI=10.1534/genetics.113.159988;
RA   Grognet P., Bidard F., Kuchly C., Tong L.C.H., Coppin E., Benkhali J.A.,
RA   Couloux A., Wincker P., Debuchy R., Silar P.;
RT   "Maintaining two mating types: Structure of the mating type locus and its
RT   role in heterokaryosis in Podospora anserina.";
RL   Genetics 197:421-432(2014).
RN   [4] {ECO:0000313|EMBL:CDP29703.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Grognet P., Bidard F., Kuchly C., Chan Ho Tong L., Coppin E.,
RA   Ait Benkhali J., Couloux A., Wincker P., Debuchy R., Silar P.;
RT   "Maintaining two mating types: Structure of the mating type locus and its
RT   role in heterokaryosis in Podospora anserina.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC         EC=3.2.1.8; Evidence={ECO:0000256|RuleBase:RU361174};
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC       {ECO:0000256|ARBA:ARBA00004851}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC       {ECO:0000256|ARBA:ARBA00007495, ECO:0000256|RuleBase:RU361174}.
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DR   EMBL; CU633461; CAP62292.1; -; Genomic_DNA.
DR   EMBL; FO904940; CDP29703.1; -; Genomic_DNA.
DR   RefSeq; XP_001904510.1; XM_001904475.1.
DR   AlphaFoldDB; B2AFS1; -.
DR   CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR   CAZy; GH10; Glycoside Hydrolase Family 10.
DR   GeneID; 6188644; -.
DR   KEGG; pan:PODANSg1532; -.
DR   VEuPathDB; FungiDB:PODANS_5_12430; -.
DR   eggNOG; ENOG502QR4K; Eukaryota.
DR   HOGENOM; CLU_020161_12_1_1; -.
DR   OrthoDB; 548101at2759; -.
DR   Proteomes; UP000001197; Chromosome 5.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR   GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR035971; CBD_sf.
DR   InterPro; IPR000254; Cellulose-bd_dom_fun.
DR   InterPro; IPR044846; GH10.
DR   InterPro; IPR001000; GH10_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR31490:SF35; ENDO-1,4-BETA-XYLANASE; 1.
DR   PANTHER; PTHR31490; GLYCOSYL HYDROLASE; 1.
DR   Pfam; PF00734; CBM_1; 1.
DR   Pfam; PF00331; Glyco_hydro_10; 1.
DR   PRINTS; PR00134; GLHYDRLASE10.
DR   SMART; SM00236; fCBD; 1.
DR   SMART; SM00633; Glyco_10; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF57180; Cellulose-binding domain; 1.
DR   PROSITE; PS00562; CBM1_1; 1.
DR   PROSITE; PS51164; CBM1_2; 1.
DR   PROSITE; PS51760; GH10_2; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW   ECO:0000256|RuleBase:RU361174};
KW   Glycosidase {ECO:0000256|RuleBase:RU361174};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361174};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW   ECO:0000256|RuleBase:RU361174};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001197};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..418
FT                   /note="Beta-xylanase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007638572"
FT   DOMAIN          44..335
FT                   /note="GH10"
FT                   /evidence="ECO:0000259|PROSITE:PS51760"
FT   DOMAIN          382..418
FT                   /note="CBM1"
FT                   /evidence="ECO:0000259|PROSITE:PS51164"
FT   REGION          342..391
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   418 AA;  45456 MW;  F13C4A32C2D151BA CRC64;
     MHTKALLAAL LAPAAVSAQL HELAVRAGLQ YFGTALREGA LNSDAQFAAI LRDTREFGQI
     VPENGQKWES TQPSRGQFTY SQGDITANEA KRNSQFLRCH TLVWHSQLPS WVASGSWTRA
     TLTSVIDTHM ANVMGHYKGV CGHWDVVNEA INDDGTWRDS VFYRVFGTDY LPLSFELAKK
     HDPETKLYYN DYNLEYNQAK TDRAVEIVRI IQAAGAPIDG VGFQGHLIVG STPSRANLAT
     TLRRFTALGV DVAYTELDIR HSSLPASSQA QVTQGNDFAN VVGSCLDVPR CVGVTVWSFT
     DKYSWVPSTF NGAGDALIYD SQFRKKAAWT SISSVLAAKA TGAPPVSSST STPAQPTTTL
     VTRTTSASST TQPTPTSAPT QPEQVRWGQC GGNGWTGPTT CQSPYTCQVL NPWYSQCL
//

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