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Database: UniProt
Entry: A0A0D2ALK3_9PEZI
LinkDB: A0A0D2ALK3_9PEZI
Original site: A0A0D2ALK3_9PEZI 
ID   A0A0D2ALK3_9PEZI        Unreviewed;       746 AA.
AC   A0A0D2ALK3;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=6-phosphofructo-2-kinase domain-containing protein {ECO:0000259|Pfam:PF01591};
GN   ORFNames=PV09_08476 {ECO:0000313|EMBL:KIV99963.1};
OS   Verruconis gallopava.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Venturiales; Sympoventuriaceae; Verruconis.
OX   NCBI_TaxID=253628 {ECO:0000313|EMBL:KIV99963.1, ECO:0000313|Proteomes:UP000053259};
RN   [1] {ECO:0000313|EMBL:KIV99963.1, ECO:0000313|Proteomes:UP000053259}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 43764 {ECO:0000313|EMBL:KIV99963.1,
RC   ECO:0000313|Proteomes:UP000053259};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Ochroconis gallopava CBS43764.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KN847569; KIV99963.1; -; Genomic_DNA.
DR   EMBL; KN847569; KIV99964.1; -; Genomic_DNA.
DR   RefSeq; XP_016209833.1; XM_016362385.1.
DR   RefSeq; XP_016209834.1; XM_016362386.1.
DR   STRING; 253628.A0A0D2ALK3; -.
DR   GeneID; 27316449; -.
DR   VEuPathDB; FungiDB:PV09_08476; -.
DR   OrthoDB; 2013830at2759; -.
DR   Proteomes; UP000053259; 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; 2.
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:UP000053259}.
FT   DOMAIN          178..232
FT                   /note="6-phosphofructo-2-kinase"
FT                   /evidence="ECO:0000259|Pfam:PF01591"
FT   DOMAIN          323..489
FT                   /note="6-phosphofructo-2-kinase"
FT                   /evidence="ECO:0000259|Pfam:PF01591"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          59..173
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          285..325
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          545..569
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        96..117
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        142..157
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   746 AA;  83102 MW;  C7BDA0886A8DD9DF CRC64;
     MPHNVSDNIL DHTRAPHRPL PSPTSLTSIT AATATPAPHP RKQSQLSVYA KSVLMSNIAH
     RDPDPSTAIG SDTASPAPEV RPPAAPINGL DDPDGRQDAQ QLHHQHLKPR PRFAPESLRA
     SKDGVGPALS DTPEPSLPTT PRIPAMRSSS AASTPRIRPT TLDIPGLTKS KVSPDGRIAQ
     RDVGSKLVIV MVGLPARGKS YITKKMARYL NWLQHDTMIF NVGEKRRKFA SHAEPSAAAG
     GPDHATREMS PPHVAAHILI NGQVPTPPIP TLSLTGAVEA VQANGTGSPG VAEVQPKVDK
     PAPGSSGTLD NPGTAVHHDP MSEHTADFFD PANREAALIR EQCASETLDE LLDYILYGNG
     SVGILDATNS TISRRKMVME RIRQKAGKEL NVLFLESVCE DQTLLEANMR LKLSGPDYKD
     KDPVASLADF KKRVEQYEKK YVPLGDYEER NNMPYIKMID VGRKVITHQI RGFLSSQAAY
     YLLNFNLAPR QIWITRHGES EDNRAGKIGG DSGLTENGRK YAAALARFVD HERKAWEVRQ
     QDKAANTHFP PHPGDHTPPN PHFSPLGDEQ EEQTRNFCVW TSMLKRSIQS AEFFDEEDYE
     IKQMRMLDEL NAGLMEGMTY EEIRTHYADE YKLREHDKLQ YRYPGPGGEG YLDVINRLRP
     VIVELERMTD HCLLITHRSV ARVLLAYFMG LSRDNVADLD CPLGMLYSLE PKPYGVEFKA
     YRYNPEKDWF DYLPDFKLKK ATHPHV
//
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