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Database: UniProt
Entry: A0A094D4P1_9PEZI
LinkDB: A0A094D4P1_9PEZI
Original site: A0A094D4P1_9PEZI 
ID   A0A094D4P1_9PEZI        Unreviewed;      1691 AA.
AC   A0A094D4P1;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   08-NOV-2023, entry version 33.
DE   RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE            EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN   ORFNames=V496_05748 {ECO:0000313|EMBL:KFY59193.1};
OS   Pseudogymnoascus sp. VKM F-4515 (FW-2607).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420909 {ECO:0000313|EMBL:KFY59193.1, ECO:0000313|Proteomes:UP000029302};
RN   [1] {ECO:0000313|EMBL:KFY59193.1, ECO:0000313|Proteomes:UP000029302}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4515 (FW-2607) {ECO:0000313|Proteomes:UP000029302};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) 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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC       {ECO:0000256|ARBA:ARBA00007495, ECO:0000256|RuleBase:RU361174}.
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:KFY59193.1}.
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DR   EMBL; JPJY01001058; KFY59193.1; -; Genomic_DNA.
DR   STRING; 1420909.A0A094D4P1; -.
DR   HOGENOM; CLU_002994_0_0_1; -.
DR   OrthoDB; 204198at2759; -.
DR   Proteomes; UP000029302; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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   CDD; cd00038; CAP_ED; 1.
DR   CDD; cd07042; STAS_SulP_like_sulfate_transporter; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR   Gene3D; 3.30.750.24; STAS domain; 1.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR018490; cNMP-bd_dom_sf.
DR   InterPro; IPR001000; GH10_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011547; SLC26A/SulP_dom.
DR   InterPro; IPR002645; STAS_dom.
DR   InterPro; IPR036513; STAS_dom_sf.
DR   PANTHER; PTHR43310:SF4; SULFATE TRANSPORTER; 1.
DR   PANTHER; PTHR43310; SULFATE TRANSPORTER YBAR-RELATED; 1.
DR   Pfam; PF00027; cNMP_binding; 1.
DR   Pfam; PF00331; Glyco_hydro_10; 1.
DR   Pfam; PF01740; STAS; 1.
DR   Pfam; PF00916; Sulfate_transp; 1.
DR   PRINTS; PR00134; GLHYDRLASE10.
DR   SMART; SM00100; cNMP; 1.
DR   SMART; SM00633; Glyco_10; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR   SUPFAM; SSF52091; SpoIIaa-like; 1.
DR   PROSITE; PS50042; CNMP_BINDING_3; 1.
DR   PROSITE; PS51760; GH10_2; 1.
DR   PROSITE; PS50801; STAS; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU361174};
KW   Glycosidase {ECO:0000256|RuleBase:RU361174};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361174};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Polysaccharide degradation {ECO:0000256|RuleBase:RU361174};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029302};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        314..335
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        347..366
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        412..432
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        444..462
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        482..502
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        514..535
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        555..573
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        580..602
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        614..635
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        647..666
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        672..695
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        707..738
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          778..886
FT                   /note="STAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50801"
FT   DOMAIN          996..1095
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   DOMAIN          1363..1675
FT                   /note="GH10"
FT                   /evidence="ECO:0000259|PROSITE:PS51760"
FT   REGION          1..258
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1169..1202
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..41
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        59..82
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        90..104
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        108..138
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        176..190
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        231..252
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1691 AA;  187407 MW;  1D0C5924D528C0E8 CRC64;
     MSLPASERLA PSRRQRASSA VTSAQNLLWP GQLSGSHGDS SARPSPGLFP RSGEPSEPIG
     MPSSPSNAYS QREPTRSFFH SSFRGQPAPH DSEQHARDVR EDTAELASYA LSEQSRSMMG
     SSPRQSSPTF SNTGSNLEVW GDGEDDSATP HVSYGPAKPT VIEELSEPGT PQHEGQPYRS
     PGTSVLTNML RKAASPPDDG IDSGEGDTGE STGDEEALIP DQRKKTTPSG ADATEHTPLL
     GQQSQGHNQR PNYLSGGHDL EAQPVRRIKS WPKVNKILSK QLRKGRRAAR LVSDPKKWDK
     KVIWQRTVAE PAGYIPAVVL GALLNVLDAL SYGMILFPLG EPLFEKLGPA GISMFYVSCI
     VSQLVFSSGG SIFKGGVGSE MIEVVPFFHK MAFTILATVG EDNPKAVIST TITSYAISSI
     ITGLVFFLMG VCRFGYIVGF IPRHILIGCI GGVGWFLIAT GLEVTARLDG NLEYNWKTLH
     KLIQFNTVFQ WVTPLVLGLF LYRSSKIFTG KYYLPTFILL IPAIFYIFVF ALPQLDIPQL
     REDGWIFDAP DADEPWWYFY TLYDFKLVHW GAVAENIPAM FALTFFGVLH VPINIPALAF
     NIGEDHLDLD RELVAHGISN ALSGFAGSIQ NYLVYTNSVL FIKSGGNSRV AGFILALATF
     GILMAGPGVI GFIPVMMVGV LIFVLGFELV FEAVWDPRKK LKPLEYLTVI AIVLVMGMYD
     FVVGIFVGIA LAFVSLVVQT SRVPAVRASY SGEIAGSTVR RNPVQHDYLR QVGRQIHVTK
     LAGYLFFGTI VDVEARIRSL IKEEAFNHRP IRYLIFDLWH VTGIDYSAAE AFNRLNRIFS
     QKGVTIVMSG VSSESPIGLS LRNVGLGEGG NEVTLLPDLN SALESCENGL LKALYHNKDE
     RIAQHARSAS ILSRDVNARR LSTTSVHHPM PPLLGSPRGN HLVVAATKSL ETEHENSTHK
     WQNFKEPLRL ILQTFQGLTD KNEDFWFRAV PYFTRKEYMA GTTLFRRDQP ADGFYLLEDG
     ILRADYDLPQ GRYFESIVAG TTCGELPFFS ETERTATVIA ERDCAVWLMD RQQWEELQEK
     DKDVAQELLR ITLKLTTERM SAITSYFNES ECFLPGPGAP ARVKSIEPLE LRAGDGHFLI
     DEMQFLSSLN EAKLTVSVLV SSAPVLRNSD RGSTPVQADN YPRGLPDQQK TPPLTSPRSS
     PVYPPALKGK VGAKNAATAG YEIFTAKISI SNHKPPRLAP RLLASIQLVC MPTRALIWLE
     YSRKLPGIYP IRRYCIEDAF SSLAPLRYIT NLHKAARHHN CVHIIPAPLD GKFSLTVNMK
     FQASTLAALV AIPAVSATLG WPWIKPPHGI GHGGKHKDND LLHTLAVKAG KKYFGTATDN
     GELNNKEYTD ILNNRKQFGQ LTPSNGQKWM YIEPEQNVFN FTNGEVVGNL AKKNGQILRC
     HTLVWHSQLP EWVEFGNWTK ETLSAVVVNH ITKVLTQWKG KCYAWDVINE AFNEDGTFRE
     SVFYNVIGED YFDLAFKTAA KIDPHTKLYY NDYNLEARSD KTRAVQKLVR RLKAKNIKID
     GVGAQAHLIV GSTPTREEQI QNLQDFVATG VEVAQTELDI RLELPVNATN LAQQSIDYEN
     TVAACVAVKG CVGTTIWDFY DPYSWVPSVF EGEGAATLYF EDFSKHPAYW GVVKALASGP
     THPHWPWPFN N
//
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