ID A0A0U1M0E3_TALIS Unreviewed; 758 AA.
AC A0A0U1M0E3;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=6-phosphofructo-2-kinase {ECO:0000313|EMBL:CRG89009.1};
GN ORFNames=PISL3812_06044 {ECO:0000313|EMBL:CRG89009.1};
OS Talaromyces islandicus (Penicillium islandicum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Islandici.
OX NCBI_TaxID=28573 {ECO:0000313|EMBL:CRG89009.1, ECO:0000313|Proteomes:UP000054383};
RN [1] {ECO:0000313|EMBL:CRG89009.1, ECO:0000313|Proteomes:UP000054383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WF-38-12 {ECO:0000313|EMBL:CRG89009.1};
RA Syromyatnikov M.Y., Popov V.N.;
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CVMT01000005; CRG89009.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U1M0E3; -.
DR STRING; 28573.A0A0U1M0E3; -.
DR OrthoDB; 2013830at2759; -.
DR Proteomes; UP000054383; 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:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
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 CDD; cd00590; RRM_SF; 1.
DR Gene3D; 3.30.70.330; -; 2.
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; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001345; PG/BPGM_mutase_AS.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR10606:SF44; 6-PHOSPHOFRUCTO 2-KINASE_FRUCTOSE 2,6-BISPHOSPHATASE LONG FORM; 1.
DR PANTHER; PTHR10606; 6-PHOSPHOFRUCTO-2-KINASE/FRUCTOSE-2,6-BISPHOSPHATASE; 1.
DR Pfam; PF01591; 6PF2K; 1.
DR Pfam; PF00300; His_Phos_1; 1.
DR Pfam; PF00076; RRM_1; 1.
DR PRINTS; PR00991; 6PFRUCTKNASE.
DR SMART; SM00855; PGAM; 1.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR PROSITE; PS00175; PG_MUTASE; 1.
DR PROSITE; PS50102; RRM; 2.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:CRG89009.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000054383};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176};
KW Transferase {ECO:0000313|EMBL:CRG89009.1}.
FT DOMAIN 80..159
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 210..297
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 142..193
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 COMPBIAS 164..185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..311
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 546
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT ACT_SITE 622
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT BINDING 545..552
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 598
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ SEQUENCE 758 AA; 85447 MW; 565D220514D359E4 CRC64;
MADIAEQTAG QQQEQPWSTP TKQPFQNGVR TTGRAFNSPN WRTKTEDSPQ QTSSQANNSP
RSPFNRSWQQ TVSPAITEGR RLYVGNMPYM AKKEDVEAVF AEGGYKIERV DISIDPFTGR
NPSYCFVELE TKEQADRAMQ ELDGKDLLGR PVKVKPGVAK ASQDRSSPRP SNGFSPRSSN
DKPGSSPVAF DRWQRNDASS HFKGYSENGR RLYVGGLPKL SNQQTIDTEI QTFFNGYNIE
AVSKLISPHP SKRFEAGDHY YLFVDFASAD EATAAQAALD GQDGPWGGKI RVGKARGESW
KPDERRKWTP TQTNDAPESA TAEPSSDDTK ICVIMVGLPA RGKSLIAGKA LRYFAWVGIT
ARIFNVGTYR REKSPHPEAT FFDPHNSEGE KMRRAAAEAA VSDMLKWFKE ENGVVGIFDA
TNSTKSRRAW IHKTCEEAGI ETLFVESLCD DEDIIMNNIL EVKTTSPDYK GQDPEVAAQD
FRNRIRHYET VYETISEDEK AYTYVKLINV GSTVIINQIK DYLSSRLVYY IQNLHIKPRS
IWLSRHGESE YNLSGKIGGD SDISSRGEAY ARALPGLLKQ SGVPPDTKLT IWTSTLKRTI
QTARHLAAET GYEKLEWKAL DELESGLCDG LTYEEIAEKY PEDFAARDED KYNYRYRGGE
SYRDVVIRLE PIIMELERSE NIIIVTHQAV LRCIYSYFHN MSQEQSPWME VPLHTLIKLT
PRAYGTEEKR FKANIPAVST WRGKGTSAKH QDPGQPSH
//
