ID A0A061H130_9BASI Unreviewed; 1579 AA.
AC A0A061H130;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=phosphoribosylglycinamide formyltransferase 1 {ECO:0000256|ARBA:ARBA00012254};
DE EC=2.1.2.2 {ECO:0000256|ARBA:ARBA00012254};
GN ORFNames=PFL1_06133 {ECO:0000313|EMBL:EPQ26197.1};
OS Pseudozyma flocculosa PF-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Pseudozyma.
OX NCBI_TaxID=1277687 {ECO:0000313|EMBL:EPQ26197.1, ECO:0000313|Proteomes:UP000053664};
RN [1] {ECO:0000313|EMBL:EPQ26197.1, ECO:0000313|Proteomes:UP000053664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PF-1 {ECO:0000313|EMBL:EPQ26197.1,
RC ECO:0000313|Proteomes:UP000053664};
RX PubMed=23800965; DOI=10.1105/tpc.113.113969;
RA Lefebvre F., Joly D.L., Labbe C., Teichmann B., Linning R., Belzile F.,
RA Bakkeren G., Belanger R.R.;
RT "The transition from a phytopathogenic smut ancestor to an anamorphic
RT biocontrol agent deciphered by comparative whole-genome analysis.";
RL Plant Cell 25:1946-1959(2013).
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; N(2)-
CC formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-phospho-D-
CC ribosyl)glycinamide (10-formyl THF route): step 1/1.
CC {ECO:0000256|ARBA:ARBA00005054}.
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DR EMBL; KE361646; EPQ26197.1; -; Genomic_DNA.
DR RefSeq; XP_007881864.1; XM_007883673.1.
DR GeneID; 19320213; -.
DR KEGG; pfp:PFL1_06133; -.
DR eggNOG; KOG3076; Eukaryota.
DR HOGENOM; CLU_245177_0_0_1; -.
DR OrthoDB; 5621at2759; -.
DR Proteomes; UP000053664; Unassembled WGS sequence.
DR GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.170; Formyl transferase, N-terminal domain; 1.
DR Gene3D; 3.40.20.10; Severin; 1.
DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR InterPro; IPR002376; Formyl_transf_N.
DR InterPro; IPR036477; Formyl_transf_N_sf.
DR InterPro; IPR007122; Villin/Gelsolin.
DR PANTHER; PTHR43369; PHOSPHORIBOSYLGLYCINAMIDE FORMYLTRANSFERASE; 1.
DR PANTHER; PTHR43369:SF2; PHOSPHORIBOSYLGLYCINAMIDE FORMYLTRANSFERASE; 1.
DR Pfam; PF00551; Formyl_trans_N; 2.
DR SMART; SM00262; GEL; 1.
DR SUPFAM; SSF55753; Actin depolymerizing proteins; 1.
DR SUPFAM; SSF53328; Formyltransferase; 1.
PE 4: Predicted;
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755};
KW Reference proteome {ECO:0000313|Proteomes:UP000053664};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 810..935
FT /note="Formyl transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00551"
FT DOMAIN 953..1034
FT /note="Formyl transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00551"
FT REGION 1..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 209..809
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1050..1098
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..423
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..494
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 712..776
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1050..1074
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1579 AA; 164179 MW; 6836DA2ADD2A9A38 CRC64;
MNPLSRHTTD TDPNTNTHTG TAKTTTSSAN RPFPSDPASP PTSELASWVN QVRQRNQSFT
SSHHHNTTSS ASPIRAAGGA ASATSAAAAA SPISSASELE QDFHRQRQER QSRRNRLSTS
GVRGITDSPL SSPVSEFPPA SPARSLAGAH GTMIGAPPAH QQGMASAAAE RDKPPSSSSS
IGSPNLGSPH VRRANSLLSR YGGQYGPTGV AAGPKSASDS PVSLANFMGG KASGPRLGKL
AGDGKSAPPE ASEIHESRWV ALPGLASGGG GDHRDDVAAP PSPSIGLSTS PRKAYMDLIE
RQNADSAASA IQRPPSPSKP WERPTTTAAS PDEVMRPRSP FKPASAMAPP SPAKATSSAV
QIPAASSRLS AAGDGSHTSP RKDAATSPLK PEDVPFAKTV TASPALGSGR TAGLTNRAST
YPAAATSGAF PPSPPLPQES QRSSTFSATP PLSPSPSGGV VDRNPTASLT RLSAKKMVGQ
RIREAQERDV LAQRETEAAS PAASPAVGVG AGLSKYGGSA HGSSGVRDRW PAGASGAGSN
ASTPSILDER KKQLGGSGSG GGWSPSKFGN ALPGLAGRSP PKSSAAAATS GLGSSPSKRY
AEDEADSRAA PVRLPGLGGE TSPFKRFSAA ASSPTKEERI DSAASEGSVL EPLTKGRVRG
PQRRPAAAAA ATGSASSTAS SARAAIKVVP PASGSGAGAS AFAVPSSPRK VTSGFDAPSS
PSKTQALASK FGGSTTSAAA VPSSPIKTSF APASGGPRSP TKTTIFGSSV AAASTDRKAT
ESAAPAPAPA AAAAATAAAP TKPPRSTRGK RVHVLISGSG SNLQSLIDAT LLNPPPGIPV
IPDAQISFVL SNRKAAYGLT RASESNPPIP TKVLALKTWQ NRNPGGTREE YDRVLARAVL
DGPADEGKGT PPDLIVLAGF MHIVSEGFLH ALGHKTSLPS STPTIGVRPS KAVPIINLHP
ALPGAFDGAN AIPRAFEAYQ QGLTDRTGCM VHEVVADVDR GRPLIVREIV IQKGWDLAKL
EDEIHKVEHV IIVEGARQVL EGRLEELDRE QEAREQEQQR HQQRQRESDE RLTRQRSAAQ
GPTQRVPSPQ KAAPRAPVNL DEVVHVKTAE DAANVAFRAE QALKTSSFEP GAILEYGAPT
PSTAASQQKP KTVSIDVISI GADGSTKAVE PAAGASSSDQ RVSPLETLYD DETLAVVHRF
KASSGLMENR VWVRLGLRSP LHPAQQAAAA SDSGDEVLHR AEELAKRYGT KPTFVPAGFE
GVDLVDGIGG RWAVARQGSR ARFDSNGTAL YRVRAAAAAP AGADQTTVTQ VDLATSNLCS
GDSFVAAILG NSLVWHGRGS ERKTREAARR FAEALEVEAT GKCGGRIAEN KEGREDGFFW
DLFDRSQAYA SAWYHGLARS VSARGWRGAV QLFDLGLERG TLTLHPAIEP DCLGQMDLLS
AQRQDEVSLL NLSNRELFVV VGRRARDQRV KILAGCMLAD RLAEHLESQP GNEAGRPAAH
VVVLPSRVPR EIRAAARYWC QTGDELDGDG DGDGDIKMNV KTTREAVRDL TTDRWPRERL
LDPSYLPVGI GEEDVGADV
//
