ID A0A1F5LBD0_9EURO Unreviewed; 428 AA.
AC A0A1F5LBD0;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Ribose-phosphate pyrophosphokinase N-terminal domain-containing protein {ECO:0000259|Pfam:PF13793};
GN ORFNames=PENARI_c016G06360 {ECO:0000313|EMBL:OGE50495.1};
OS Penicillium arizonense.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1835702 {ECO:0000313|EMBL:OGE50495.1, ECO:0000313|Proteomes:UP000177622};
RN [1] {ECO:0000313|EMBL:OGE50495.1, ECO:0000313|Proteomes:UP000177622}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 141311 {ECO:0000313|EMBL:OGE50495.1,
RC ECO:0000313|Proteomes:UP000177622};
RX PubMed=27739446; DOI=10.1038/srep35112;
RA Grijseels S., Nielsen J.C., Randelovic M., Nielsen J., Nielsen K.F.,
RA Workman M., Frisvad J.C.;
RT "Penicillium arizonense, a new, genome sequenced fungal species, reveals a
RT high chemical diversity in secreted metabolites.";
RL Sci. Rep. 6:35112-35112(2016).
CC -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase family.
CC {ECO:0000256|ARBA:ARBA00006478}.
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:OGE50495.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LXJU01000016; OGE50495.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5LBD0; -.
DR STRING; 1835702.A0A1F5LBD0; -.
DR OrthoDB; 276387at2759; -.
DR Proteomes; UP000177622; Unassembled WGS sequence.
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 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 Nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022727};
KW Reference proteome {ECO:0000313|Proteomes:UP000177622}.
FT DOMAIN 6..99
FT /note="Ribose-phosphate pyrophosphokinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13793"
FT REGION 119..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 428 AA; 46198 MW; 57181997D157938C CRC64;
MVRNLVVIGG NSHPQLTQNI CGVLGIPPAE VLLSKFAVGE TRVEVQESVR EKDVYIIQSG
GGKVNDHLLE LLITISACKT ASARRVTAVL PLFPYSRQSD IPYDKAGAPL IKAGAPGRPA
NGGYTFESTP PTPGPGKPEG LGLMNGMDNL QKGLARAQIE ESTGSPVKRR NGLPRNDTTD
SLKSAANGAD DAASNASSKI NSFQPRPGYK QWVAQAGTLV ADLLTCAGAD HIITMDLHDP
QYQGYFDIPV DNLYGRPLLK SYIQRNIPNY KQAVIVSPDA GGAKRATAIA DQMGMEFALI
HKERRPTKIT DRQNATMMLV GDVRDRIAIL IDDLADTSNT ITRAAKLLKK EGASQVYALV
THGILSGDAI ERINASALDK VVVTNSVEQQ EHLRLCPKLE VLEVGHVFAE AIRRVHHGES
ISVLFQYD
//
