ID H2B0R5_KAZAF Unreviewed; 762 AA.
AC H2B0R5;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=6-phosphofructo-2-kinase domain-containing protein {ECO:0000259|Pfam:PF01591};
GN Name=KAFR0J01490 {ECO:0000313|EMBL:CCF60215.1};
GN ORFNames=KAFR_0J01490 {ECO:0000313|EMBL:CCF60215.1};
OS Kazachstania africana (strain ATCC 22294 / BCRC 22015 / CBS 2517 / CECT
OS 1963 / NBRC 1671 / NRRL Y-8276) (Yeast) (Kluyveromyces africanus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kazachstania.
OX NCBI_TaxID=1071382 {ECO:0000313|EMBL:CCF60215.1, ECO:0000313|Proteomes:UP000005220};
RN [1] {ECO:0000313|EMBL:CCF60215.1, ECO:0000313|Proteomes:UP000005220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22294 / BCRC 22015 / CBS 2517 / CECT 1963 / NBRC 1671 /
RC NRRL Y-8276 {ECO:0000313|Proteomes:UP000005220};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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DR EMBL; HE650830; CCF60215.1; -; Genomic_DNA.
DR RefSeq; XP_003959350.1; XM_003959301.1.
DR AlphaFoldDB; H2B0R5; -.
DR STRING; 1071382.H2B0R5; -.
DR GeneID; 13883865; -.
DR KEGG; kaf:KAFR_0J01490; -.
DR eggNOG; KOG0234; Eukaryota.
DR HOGENOM; CLU_006383_3_2_1; -.
DR InParanoid; H2B0R5; -.
DR OrthoDB; 2013830at2759; -.
DR Proteomes; UP000005220; Chromosome 10.
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 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; 1.
DR Pfam; PF00300; His_Phos_1; 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:UP000005220}.
FT DOMAIN 156..377
FT /note="6-phosphofructo-2-kinase"
FT /evidence="ECO:0000259|Pfam:PF01591"
FT REGION 1..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 693..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 724..762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..75
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 695..712
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..762
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 762 AA; 87019 MW; 93ED12579922BD51 CRC64;
MFRKVKYIDD SLTPDSSESD IEPKARSIVT NPSNSTPSST SSSSGTLKDM LPKKKHVTIQ
LDDEQSKRLD SLPSFKRRPL SDTPVTSTWT SPSVSASPSP VPSTLQLPSL SRLQKGETTP
VTSGSRSPSK FSHRTRRPTT IDVPGLTKSK TSPDGLISKE DSGSKLIIIM VGLPATGKSF
ITNKLSRYLN YSMYYCKVFN VGNTRRRFAK KHNLSDQDSK FFDPSNENSS KLRDKWALDT
LDELLDYLLE GPGSVAVFDA TNTTRTRRKK VLEKIRERNS HLKVLYLESI CTNRTVVENN
IKLKLFGPDY KGKNPEESLK DFKERLANYL RAYEPIEDDE NIPYIKMIDV GKKIISYKIE
GFLASQTVYY LLNFNLTERQ IWITRNGESE DNMLGRLGGD SHLTSRGLKY AQALTRFMDE
QREIFYFEQL KKKEANEIYS KNDIIQTYKE NGTTDPISNF FVWTSMRQRS VETAQYFNED
DYPIKQMRML DELSAGDYEG MTYSEIRANF PKEFAKRQKD KLRYRYPGIA GESYMDVINR
LRPVITELER IDDSVLIVTH RVVARALLGY YMNLNVDVIS NLDVPLHCVY CLETKPYGIT
WSLWEYDEKT DCFSKVPESH LNTTKVREVG LVYKERKYSV VPTAPPTNEL GSSDFLNRRR
ASVGFEGDGL QQDSGTIDEK VLASEPITSS NIRSEFKKAD MRPIPRKSSR ERFQIDQLNE
KLSSLKTDLG TRFRDATSPD ASDNSNITSN NSIKMTRSHS QT
//
