ID M7TX67_BOTF1 Unreviewed; 446 AA.
AC M7TX67;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Putative ribose-phosphate pyrophosphokinase protein {ECO:0000313|EMBL:EMR85860.1};
GN ORFNames=BcDW1_5513 {ECO:0000313|EMBL:EMR85860.1};
OS Botryotinia fuckeliana (strain BcDW1) (Noble rot fungus) (Botrytis
OS cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=1290391 {ECO:0000313|EMBL:EMR85860.1, ECO:0000313|Proteomes:UP000012045};
RN [1] {ECO:0000313|Proteomes:UP000012045}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BcDW1 {ECO:0000313|Proteomes:UP000012045};
RX PubMed=23704180; DOI=10.1128/genomea.00252-13;
RA Blanco-Ulate B., Allen G., Powell A.L., Cantu D.;
RT "Draft genome sequence of Botrytis cinerea BcDW1, inoculum for noble rot of
RT grape berries.";
RL Genome Announc. 1:E0025213-E0025213(2013).
CC -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase family.
CC {ECO:0000256|ARBA:ARBA00006478}.
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DR EMBL; KB707880; EMR85860.1; -; Genomic_DNA.
DR AlphaFoldDB; M7TX67; -.
DR STRING; 1290391.M7TX67; -.
DR HOGENOM; CLU_033546_0_1_1; -.
DR Proteomes; UP000012045; Unassembled WGS sequence.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004749; F:ribose phosphate diphosphokinase activity; IEA:InterPro.
DR GO; GO:0009165; P:nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd06223; PRTases_typeI; 1.
DR Gene3D; 3.40.50.2020; -; 3.
DR InterPro; IPR029099; Pribosyltran_N.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR029057; PRTase-like.
DR InterPro; IPR005946; Rib-P_diPkinase.
DR NCBIfam; TIGR01251; ribP_PPkin; 1.
DR PANTHER; PTHR10210; RIBOSE-PHOSPHATE DIPHOSPHOKINASE FAMILY MEMBER; 1.
DR PANTHER; PTHR10210:SF36; RIBOSE-PHOSPHATE PYROPHOSPHOKINASE 5; 1.
DR Pfam; PF14572; Pribosyl_synth; 1.
DR Pfam; PF13793; Pribosyltran_N; 1.
DR SMART; SM01400; Pribosyltran_N; 1.
DR SUPFAM; SSF53271; PRTase-like; 2.
PE 3: Inferred from homology;
KW Kinase {ECO:0000313|EMBL:EMR85860.1};
KW Nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022727};
KW Transferase {ECO:0000313|EMBL:EMR85860.1}.
FT DOMAIN 6..99
FT /note="Ribose-phosphate pyrophosphokinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13793"
FT REGION 119..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 163..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 446 AA; 48432 MW; 060E831D5EF75BA8 CRC64;
MVRNLVVLGG NSHPQITEII CNTLGVPPCN RILKKFSVGE SRLEIQDSVR GKDVYIIQSG
GGKANDHFID LCIMISACKT GSAKRVTVVL PLFPYSRQPD LPYNKIGAPL AKGPTDVKGN
FTFESRPATP GPSSPQTPGL SNGTNGMEKL QKKLGKASLE QINTQSSNGI TPRRQDTSDS
IASLTNGRLG DGASTPVSTP HFTTHDYENP GFVNGQSKTL FQGKPGYKQW VAQAGTLVAD
LLTCSGADQV ITMDLHDPQY QGFFDIPVDN LYGKPLLKRY IQQNIPNFQD AIVVSPDAGG
AKRATAIADG LNMEFALIHK ERRPTRITDR QNATMMLVGN VRDKVAILID DLADTSNTIT
RAAKLLKKEG ATYVYALITH GVFSGDAIER INASALDKII VTNSVPQDEH QRLCPKLEVL
EVGPVFAEAI RRVHHGESIS VLFNYD
//
