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Database: UniProt
Entry: A0A094I9J2_9PEZI
LinkDB: A0A094I9J2_9PEZI
Original site: A0A094I9J2_9PEZI 
ID   A0A094I9J2_9PEZI        Unreviewed;      1362 AA.
AC   A0A094I9J2;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KFZ24330.1};
GN   ORFNames=V502_01192 {ECO:0000313|EMBL:KFZ24330.1};
OS   Pseudogymnoascus sp. VKM F-4520 (FW-2644).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420915 {ECO:0000313|EMBL:KFZ24330.1, ECO:0000313|Proteomes:UP000029308};
RN   [1] {ECO:0000313|EMBL:KFZ24330.1, ECO:0000313|Proteomes:UP000029308}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4520 (FW-2644) {ECO:0000313|Proteomes:UP000029308};
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family.
CC       {ECO:0000256|ARBA:ARBA00009902}.
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:KFZ24330.1}.
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DR   EMBL; JPKE01000451; KFZ24330.1; -; Genomic_DNA.
DR   STRING; 1420915.A0A094I9J2; -.
DR   HOGENOM; CLU_256908_0_0_1; -.
DR   OrthoDB; 2298551at2759; -.
DR   Proteomes; UP000029308; Unassembled WGS sequence.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd18621; GH32_XdINV-like; 1.
DR   CDD; cd03443; PaaI_thioesterase; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 3.10.129.10; Hotdog Thioesterase; 1.
DR   Gene3D; 3.90.700.10; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR003953; FAD-binding_2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR001362; Glyco_hydro_32.
DR   InterPro; IPR013189; Glyco_hydro_32_C.
DR   InterPro; IPR013148; Glyco_hydro_32_N.
DR   InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR   InterPro; IPR029069; HotDog_dom_sf.
DR   InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR   InterPro; IPR006683; Thioestr_dom.
DR   PANTHER; PTHR43400:SF12; FAD-DEPENDENT OXIDOREDUCTASE 2 FAD BINDING DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43400; FUMARATE REDUCTASE; 1.
DR   Pfam; PF03061; 4HBT; 1.
DR   Pfam; PF00890; FAD_binding_2; 1.
DR   Pfam; PF08244; Glyco_hydro_32C; 1.
DR   Pfam; PF00251; Glyco_hydro_32N; 1.
DR   SMART; SM00640; Glyco_32; 1.
DR   SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF56425; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR   SUPFAM; SSF54637; Thioesterase/thiol ester dehydrase-isomerase; 1.
PE   3: Inferred from homology;
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029308}.
FT   DOMAIN          12..498
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
FT   DOMAIN          641..721
FT                   /note="Thioesterase"
FT                   /evidence="ECO:0000259|Pfam:PF03061"
FT   DOMAIN          827..1140
FT                   /note="Glycosyl hydrolase family 32 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00251"
FT   DOMAIN          1201..1350
FT                   /note="Glycosyl hydrolase family 32 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08244"
SQ   SEQUENCE   1362 AA;  147616 MW;  25C40FFE5F43472B CRC64;
     MPSLSSVASA ADVLVIGGGN AGFTAAIQAA EAGVGRVVII DKCPEEWAGG NSFFTAGAFR
     TVHNGTADLL PIVNNVTAEM AKLVDLEPYT PAEFRKDIDR MTSGRTDPEL SQALIEESNA
     AVKWLAKQGV RFQLSFNRQA YKVNGRFKFW GGMSLKTDEG GKGLIQDHQN AARRHGVEVY
     YSTAAKRITM DRATGAVSGV VVEVQGIDKI IKTKAVILAA GGFEANPRMR SQYLGPGWDL
     ARVRGTPYNT GDALEFAIRD VNAKQAGNWS GCHSTCWDAN APANSGDRAI SNEFTKSGYP
     LGLMLNNGGE RFVDEGVDMR NFTYARFGRA IHGQPDGVAF QVWDQRMIPW LRDEEYRDAV
     VEKIWGSTVE ELAANCAQRG LNDPATFIST IKEYNSAVYA SQKEKPGLIW DPAVKDGLST
     QSSAVKLALP KSNWALPVDQ GPFMAVKVCC GITFTFGGLS VNPASTAVIS QSGREVEGLF
     CVGEMLGGLF YGNYPGGSGL TSGAVFGRRA GVAAARIAGA KGVAATESTA SGNNTEILRF
     IGRDCGVDME KVATCNQYYL THFLAIPWCA SLLPSTTILS SPVPSRIPNA STEGALFAQT
     LQTPDTISAL LSFSRNSPNT PTKEIHTLVT LGYLLNGYPN TAHGDIIVTI IDEAMSFFLK
     RNKEIGMLPG LGDIVTADLR VKFIRPVKTP QTVVVEARLR EVNGRKYVVE ADLKDSEGVV
     LAQGEALWIA PVSMKLSLVV AVVAVAADAA AGSVVSQRTK GQHHSIDYNH APPNLSTLAN
     ASLFETWRPR AHVLPPSGQI GDPCMHYTDP NTGLFHVGWL HSGASGATTD DLVTYRDLNP
     DGRPFIVAGG INDPIAVFDG SVIPMGIDGK PTLLYTSVSY LPIQWTIPYT RGSETQSLAV
     SYDGGRNFTK LHQGPVIPSP PFAVNVTAFR DPFVFQNAKL DSLLESSPQT WYTVISGGVH
     GDGPSQFLYR QHDPDFQYWE YLGQWWHEAA NSTWGNGDWA GQWGFNFEVG NIFSLDNNGY
     NAEGEVFTTI GAEWSFQPIV PEVSDSRQML WTAGNVTLQD GAVKFTPTMA GFLDWGASAY
     AAAGKELPAN SQASMKSNSP DRFITYVWLT GDFYSTHNFP TLQQNWTGAL LLPRELSVGT
     ISNVVDNELS RETGSWRVSS NNLGVLELTT LKQEIARETM AQLTSSASFV EPGQTLSSPG
     PVAFQHCPKS KFYVITASLS FPASARGSDL KAGFEVLSSE FETTRIYYQF SNESIIIDRT
     NSSAASRTTN GIDARNEGGK LRLFDIIENG EEQIETLELT IVVDNSIVEV HANGRFAVST
     WARSWYTASK EIRFIHDGEG EVEFGNITIH EGLFDAWPGR SR
//
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