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
//