ID A0A2C6A7N6_9HYPO Unreviewed; 669 AA.
AC A0A2C6A7N6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=6-phosphofructo-2-kinase domain-containing protein {ECO:0000259|Pfam:PF01591};
GN ORFNames=CDD83_7767 {ECO:0000313|EMBL:PHH88266.1};
OS Cordyceps sp. RAO-2017.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Cordyceps.
OX NCBI_TaxID=2004951 {ECO:0000313|EMBL:PHH88266.1, ECO:0000313|Proteomes:UP000221130};
RN [1] {ECO:0000313|Proteomes:UP000221130}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1346 {ECO:0000313|Proteomes:UP000221130};
RA de Bekker C., Evans H.C., Brachmann A., Hughes D.P.;
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PHH88266.1, ECO:0000313|Proteomes:UP000221130}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1346 {ECO:0000313|EMBL:PHH88266.1,
RC ECO:0000313|Proteomes:UP000221130};
RA De Bekker C., Evans H.C., Brachmann A., Hughes D.P.;
RT "Ant-infecting Ophiocordyceps genomes reveal a high diversity of potential
RT behavioral manipulation genes and a possible major role for enterotoxins.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
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:PHH88266.1}.
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DR EMBL; NJEV01000472; PHH88266.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C6A7N6; -.
DR STRING; 2004951.A0A2C6A7N6; -.
DR OrthoDB; 2013830at2759; -.
DR Proteomes; UP000221130; Unassembled WGS sequence.
DR GO; GO:0003873; F:6-phosphofructo-2-kinase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006003; P:fructose 2,6-bisphosphate metabolic process; IEA:InterPro.
DR GO; GO:0006000; P:fructose metabolic process; IEA:InterPro.
DR CDD; cd07067; HP_PGM_like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR InterPro; IPR003094; 6Pfruct_kin.
DR InterPro; IPR013079; 6Phosfructo_kin.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001345; PG/BPGM_mutase_AS.
DR PANTHER; PTHR10606:SF32; 6-PHOSPHOFRUCTO-2-KINASE 1; 1.
DR PANTHER; PTHR10606; 6-PHOSPHOFRUCTO-2-KINASE/FRUCTOSE-2,6-BISPHOSPHATASE; 1.
DR Pfam; PF01591; 6PF2K; 2.
DR Pfam; PF00300; His_Phos_1; 1.
DR PIRSF; PIRSF000709; 6PFK_2-Ptase; 1.
DR PRINTS; PR00991; 6PFRUCTKNASE.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR PROSITE; PS00175; PG_MUTASE; 1.
PE 4: Predicted;
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000221130}.
FT DOMAIN 142..197
FT /note="6-phosphofructo-2-kinase"
FT /evidence="ECO:0000259|Pfam:PF01591"
FT DOMAIN 249..414
FT /note="6-phosphofructo-2-kinase"
FT /evidence="ECO:0000259|Pfam:PF01591"
FT REGION 28..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..53
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 669 AA; 75112 MW; 3015F97599E2474D CRC64;
MPSAVVIPRQ DLGRKQAKQS ALAKLVMHNT LASSSPPPIS PTTSEPEPQL AVLPPPSIRY
GHSPSAASPA MAHAVRIMKD LTDTPPLCQS VSSTAPSSPR IPPQRQNSGN QTPRVRPHAT
TLNIPGMTRS RVSPDGRIPQ RDVAAKLVIV MVGLPARGKS YITKKLQRYL SWQQHESRIF
NVGNRRRHAA GIKVSAKPKL APEPDCLDPP VQAATILLNG GPAPNAATSL SRDCTEPTAL
HLDAAPDADA DQSAKFFDPR NQRAAAIRDQ VAMDTLDELL DYLLNLGGAV GILDATNSTI
RRRQQIVDRI RRREPKLGIL FIESICRDQN LLEANMRLKL SGPDYRDKDP HKSLEDFKNR
VAAYASAYEP LGEYEEDNDM QYIQIVDVGR KLVQHRLKGF LSGGISTYLS SFNLAPRQIW
ITRHGQSVDN ELGKLGGDSP LTERGHCYGQ ALYNFITQRR KEWLMEQKSK MAQASFPPLP
GDNTPPYPDM NRDLDEKNFC VWTSMLQRSV ETAEYFDVDD DYDVKNWEML NELNAGQFEG
MTYSEIAKRY PEEFHKRAED KLNYIYPGVG GEGYLQVISR LRDMVREIER ITDHVLIIGH
RSVCRVLMAY FMDLTRDDIT DMDVPLGMLY SIEPKPYGIA FHAYKYDEAQ GWFEELPHYK
PQKAARGSV
//
