ID   A0A139ICT0_9PEZI        Unreviewed;       839 AA.
AC   A0A139ICT0;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=6-phosphofructo-2-kinase domain-containing protein {ECO:0000259|Pfam:PF01591};
GN   ORFNames=AC579_10282 {ECO:0000313|EMBL:KXT12412.1};
OS   Pseudocercospora musae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX   NCBI_TaxID=113226 {ECO:0000313|EMBL:KXT12412.1, ECO:0000313|Proteomes:UP000073492};
RN   [1] {ECO:0000313|EMBL:KXT12412.1, ECO:0000313|Proteomes:UP000073492}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 116634 {ECO:0000313|EMBL:KXT12412.1,
RC   ECO:0000313|Proteomes:UP000073492};
RA   Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT   "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT   link between parallel evolutionary changes in Pseudocercospora fijiensis
RT   and Pseudocercospora eumusae and increased virulence on the banana host.";
RL   Submitted (JUL-2015) 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:KXT12412.1}.
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DR   EMBL; LFZO01000152; KXT12412.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A139ICT0; -.
DR   STRING; 113226.A0A139ICT0; -.
DR   Proteomes; UP000073492; 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; 2.
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   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.
PE   4: Predicted;
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000073492}.
FT   DOMAIN          218..300
FT                   /note="6-phosphofructo-2-kinase"
FT                   /evidence="ECO:0000259|Pfam:PF01591"
FT   DOMAIN          398..569
FT                   /note="6-phosphofructo-2-kinase"
FT                   /evidence="ECO:0000259|Pfam:PF01591"
FT   REGION          41..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          116..213
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          334..405
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        43..66
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        128..199
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   839 AA;  94996 MW;  846266B21110041B CRC64;
     MPHFTAAHKH DTILNNAHSA GTCSCVAEDT SDLGRYRRRQ SQQSKLAKAT MISNGNHTSQ
     TADQRRWSNE VAPADDRQVD QLRNHLDKTL KPTTSASNAL STIHFDASQE YLQLPHKQPP
     YSHRSGSLAA AMSRSLSDTN SATMALNDTP ATTAPSSPRL MGNTSAPSSH GSDSPGNASR
     MILPPQRQNS GTSTPRIRPT TLDIPGLTKS KVSPDGRIAQ RDVGSKLVIV MVGLPARGKS
     YITKKLARYL NWLQHDTRIF NVGERRRVVA GGPNALEKTR SQQVRDERHD STRESMAAIT
     TPSVVDQHEP LARSPTNNSD GQKHSVAQII LNGETKLEAP ATPAKEKQDS IACMNGNTNH
     DREEPQRKQS LATLVMARDA PEIKEAKIQE EKEEEEEEED NMEQNSAFFD PQNKKASMIR
     EQVAKQTLDD LLDYILDQNG SVGILDATNS TLQRRKMIMD HIRDRAGPQL NVLFLESSCV
     DQDLLEANMR LKLNGPDYKE MDPVIALEDF RKRVQEYEKA YVPLGEYEEK HNMPYIQMVD
     VGRKVISHQI KGFLMAQANY YLLNFNLAPR QIWITRHGLS MDNVSGKIGG DSDLAPEGHL
     YAKSLARFMD EKRREWDLKQ MENIKKTHFP PQPGDVTPPN PYYQPQSPTF NDNDSIITEA
     SALGYELKPF CVWTSMLKRS IQTAQYFNEE DYDTKQMRML DELNAGVMEG LTYNCISTQF
     PDEYRSRRAD KLHYRYPGPG GEGYLDIINR LRPVIVELER MTDHVLLVGH RSVARVLLAY
     FRGLKREEVA DLDVPLGMLY CLEPKPYGVD FKAYKWDKTR EWFFECPDFE LKRAEDDMQ
//