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Database: UniProt
Entry: G2XS20_BOTF4
LinkDB: G2XS20_BOTF4
Original site: G2XS20_BOTF4 
ID   G2XS20_BOTF4            Unreviewed;      1183 AA.
AC   G2XS20;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   SubName: Full=Similar to phosphoribosyl transferase domain protein {ECO:0000313|EMBL:CCD43457.1};
GN   ORFNames=BofuT4_P011330.1 {ECO:0000313|EMBL:CCD43457.1};
OS   Botryotinia fuckeliana (strain T4) (Noble rot fungus) (Botrytis cinerea).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Botrytis.
OX   NCBI_TaxID=999810 {ECO:0000313|EMBL:CCD43457.1, ECO:0000313|Proteomes:UP000008177};
RN   [1] {ECO:0000313|Proteomes:UP000008177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T4 {ECO:0000313|Proteomes:UP000008177};
RX   PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA   Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA   Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA   Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA   Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA   Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA   Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA   Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA   Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA   Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA   Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA   Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA   Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA   Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT   "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT   sclerotiorum and Botrytis cinerea.";
RL   PLoS Genet. 7:E1002230-E1002230(2011).
CC   -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC       family. {ECO:0000256|ARBA:ARBA00005466}.
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DR   EMBL; FQ790260; CCD43457.1; -; Genomic_DNA.
DR   AlphaFoldDB; G2XS20; -.
DR   STRING; 999810.G2XS20; -.
DR   eggNOG; KOG1712; Eukaryota.
DR   HOGENOM; CLU_003324_0_0_1; -.
DR   InParanoid; G2XS20; -.
DR   UniPathway; UPA00057; UER00099.
DR   Proteomes; UP000008177; Unplaced contigs.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0004631; F:phosphomevalonate kinase activity; IEA:InterPro.
DR   GO; GO:0006695; P:cholesterol biosynthetic process; IEA:InterPro.
DR   GO; GO:0019287; P:isopentenyl diphosphate biosynthetic process, mevalonate pathway; IEA:UniProtKB-UniPathway.
DR   CDD; cd06223; PRTases_typeI; 1.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.40.462.20; -; 1.
DR   Gene3D; 3.40.50.2020; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005919; Pmev_kin_anim.
DR   InterPro; IPR000836; PRibTrfase_dom.
DR   InterPro; IPR029057; PRTase-like.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR42973; BINDING OXIDOREDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G17690)-RELATED; 1.
DR   PANTHER; PTHR42973:SF25; PHOSPHOMEVALONATE KINASE; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   Pfam; PF04275; P-mevalo_kinase; 1.
DR   Pfam; PF00156; Pribosyltran; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   SUPFAM; SSF53271; PRTase-like; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008177};
KW   Transferase {ECO:0000313|EMBL:CCD43457.1}.
FT   DOMAIN          313..504
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   1183 AA;  130928 MW;  EC081ADA3789231C CRC64;
     MVSFNELKKA LVADITTDMS SLNEPLSDSQ YNCGFDVLLN GSEWNLYEEF IIPQLSQQVA
     SLLATRSTLS VLEIGPGSKS VLGYMPLYLR RKIRRYAAFE PNIISATSLE DWISSCPESN
     SLFPCLETTP HIYRAPFVLE DEGEKNIIET NASHDEQTFD LILFCHSMYG MKQKERFARK
     AVEMLVPNPE SGRVVIFHRD QSLELDGLAS YSTTVFPTGT VSLPDINEAL DAFAPFVVGY
     IKKDVEADMA LRIKWRETCR ALAYHDEKIT GCLFFSSPQR MVSLTRHANA LVDLVLQVPL
     AKEGRIVKSW EARLHRPTSI CRPTTVEHVR KCVQWALKHK LKLTVIGGGH SAHCLWPNVV
     SIDLEAFNRV HVITSSDNAN TRPASNSLIV AEAGCKVGDI IQEAMKFGLT VPLGSRPSVG
     AGLWLQGGFG HLSRLYGLAC DNIVGAVIVS VISGQIYHVG EVPAQNLPAG AIRPENENDL
     LWAIKGAGTN FGIVISVTFK TYSAPTYFVR NWIFPVGEGT EVRLKLGDVN SIARNLPRSC
     SIDAFLYSDK NQLHLGVTMF QASINKNFEM PSLVNDILGP VKQCKEVDGV GLFETEMYMS
     MMHGGHSGKT SSFKRCLFLD NIDDVQIVDI LREAIQNCPT PFCYLHLLQC GGATRDNTTE
     ASAFGCRDWE FACVITGVWP RNRTETEPVR TTIQWVYDIV KRLLPFCSGV YSADLGPDPR
     DNALAAKAFG ANMSRLAQLK HTMDPYNVIA YACPLFETPT KQKLIILVTG DSAAGKDFCA
     EIWVTIIIRC ASRMLTARSV SISDATKREY ATETGADINR LLSDRSYKEE HRPALTKFYE
     KQVINHPQSP MEHFQSVVRD SGSFDVLFIT GMRDEAPLTT FSHLVPDSKV LDVRVNASQA
     VLRAHQRDCY EETKVSLDGP NLSTLPYLPS LVFNNQTLGS EAAKTFAKKY FLPLLHEDFT
     RLANMVRAVP NHPRQSVTFR HVLGICQNPG GLTLCTDLLQ RHFIGEWAKV DTLVCCESGG
     FLFASPLGAQ TGIPLALVRR SGKLPPPTIS VEKSPSHISY AESGDSQQNM FEMDLGLICK
     SNSILVVDDV LATGRTLCAV LKLMMKAGVQ PKNIRVMVVA EFPTHSGREL LRQEGFGEVG
     IQSLLVFGVQ ESLGSLHEKL DKLLFNLHNN AEGTLVHTML SGI
//
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