ID A0A0D2HFV3_9EURO Unreviewed; 660 AA.
AC A0A0D2HFV3;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Nudix hydrolase domain-containing protein {ECO:0000259|PROSITE:PS51462};
GN ORFNames=Z520_03457 {ECO:0000313|EMBL:KIY00791.1};
OS Fonsecaea multimorphosa CBS 102226.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX NCBI_TaxID=1442371 {ECO:0000313|EMBL:KIY00791.1, ECO:0000313|Proteomes:UP000053411};
RN [1] {ECO:0000313|EMBL:KIY00791.1, ECO:0000313|Proteomes:UP000053411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 102226 {ECO:0000313|EMBL:KIY00791.1,
RC ECO:0000313|Proteomes:UP000053411};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Fonsecaea multimorphosa CBS 102226.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KN848066; KIY00791.1; -; Genomic_DNA.
DR RefSeq; XP_016634913.1; XM_016773967.1.
DR AlphaFoldDB; A0A0D2HFV3; -.
DR STRING; 1442371.A0A0D2HFV3; -.
DR GeneID; 27709203; -.
DR VEuPathDB; FungiDB:Z520_03457; -.
DR OrthoDB; 5399932at2759; -.
DR Proteomes; UP000053411; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016628; F:oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0000271; P:polysaccharide biosynthetic process; IEA:InterPro.
DR CDD; cd03424; ADPRase_NUDT5; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020476; Nudix_hydrolase.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR020084; NUDIX_hydrolase_CS.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR InterPro; IPR017476; UDP-Glc/GDP-Man.
DR InterPro; IPR014027; UDP-Glc/GDP-Man_DH_C.
DR InterPro; IPR036220; UDP-Glc/GDP-Man_DH_C_sf.
DR InterPro; IPR014026; UDP-Glc/GDP-Man_DH_dimer.
DR InterPro; IPR001732; UDP-Glc/GDP-Man_DH_N.
DR InterPro; IPR028359; UDP_ManNAc/GlcNAc_DH.
DR PANTHER; PTHR43491; UDP-N-ACETYL-D-MANNOSAMINE DEHYDROGENASE; 1.
DR PANTHER; PTHR43491:SF1; UDP-N-ACETYL-D-MANNOSAMINE DEHYDROGENASE; 1.
DR Pfam; PF00293; NUDIX; 1.
DR Pfam; PF00984; UDPG_MGDP_dh; 1.
DR Pfam; PF03720; UDPG_MGDP_dh_C; 1.
DR Pfam; PF03721; UDPG_MGDP_dh_N; 1.
DR PIRSF; PIRSF500136; UDP_ManNAc_DH; 1.
DR PIRSF; PIRSF000124; UDPglc_GDPman_dh; 1.
DR PRINTS; PR00502; NUDIXFAMILY.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF55811; Nudix; 1.
DR SUPFAM; SSF52413; UDP-glucose/GDP-mannose dehydrogenase C-terminal domain; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000053411}.
FT DOMAIN 491..640
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
FT REGION 436..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..454
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 660 AA; 72792 MW; 2F5E3C62FA283193 CRC64;
MSDFTVPEII CIWGGGLIGM STAVHFARQG LRSIVYDINP THVSQLNRGI FPANFESWVG
FPIKSFISSG QVRATTDPTE LSRASVKVHF VAVPTERNGE PYMVAIETVL AQIAHMSPDI
CIIESTVIPG ETEALGKRYG LPLGVATRRD WFTTTENNLE NCVRVYAGIT PEISERMEVI
LSVVCRKLAR ATSCTVVELT KCVDNGIFHT VAMYACQMAS AYPDTNTTEA LRLAATHWRL
GNHIYFPSLG TGGPCVPLAN KYLISGSPHP DKLTIASAAI EIDTAASLEV AAQVKQQLNI
EDRVAVLGIC YRGDIRVHVQ SPHLKFAREL ARLGVSVSIH DPYYSADELS EIAPDCSSLQ
FPNDLKAFDL IYVGSNHALY SKRIYSVLAF MRRGQRILDN QGIWEALADD ARSLGVSYHR
VGDARWLTSV ADDGMQKKIK TPPPLPPPPP VPQRDDSETN NVVFKTPWFQ IRSTPDFRPA
SSSCGPYYIL DRPDSVITIP FSPTSNRVLL QHQFRPPLDK SAWEFPMGCI DPGESPQHAA
RRELAEETGL IVSDSDDRDS KMELLGTYHP LPGMSAQKCH VFLARVTDEQ LLHHPRIIPK
PDADATAEYE GVSAYQTVDL AAFRELYVSG DLVDGFTLAA LAIWLSVSPE LRQVFSSPSK
//
