ID A0A421DAS7_9EURO Unreviewed; 798 AA.
AC A0A421DAS7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Carbohydrate kinase PfkB domain-containing protein {ECO:0000259|Pfam:PF00294};
GN ORFNames=CFD26_103301 {ECO:0000313|EMBL:RLL99246.1};
OS Aspergillus turcosus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1245748 {ECO:0000313|EMBL:RLL99246.1, ECO:0000313|Proteomes:UP000215289};
RN [1] {ECO:0000313|EMBL:RLL99246.1, ECO:0000313|Proteomes:UP000215289}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMR AF 1038 {ECO:0000313|EMBL:RLL99246.1};
RA Parent-Michaud M., Dufresne P.J., Fournier E., Martineau C., Moreira S.,
RA Perkins V., De Repentigny L., Dufresne S.F.;
RT "Draft genome sequences of two Aspergillus turcosus clinical strains
RT isolated from bronchoalveolar lavage fluid: one azole-susceptible and the
RT other azole-resistant.";
RL Submitted (AUG-2018) 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:RLL99246.1}.
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DR EMBL; NIDN02000035; RLL99246.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A421DAS7; -.
DR STRING; 1245748.A0A421DAS7; -.
DR Proteomes; UP000215289; Unassembled WGS sequence.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004730; F:pseudouridylate synthase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd01941; YeiC_kinase_like; 1.
DR Gene3D; 3.40.1190.20; -; 1.
DR Gene3D; 3.40.1790.10; Indigoidine synthase domain; 1.
DR HAMAP; MF_01876; PsiMP_glycosidase; 1.
DR InterPro; IPR002173; Carboh/pur_kinase_PfkB_CS.
DR InterPro; IPR022830; Indigdn_synthA-like.
DR InterPro; IPR011611; PfkB_dom.
DR InterPro; IPR007342; PsuG.
DR InterPro; IPR029056; Ribokinase-like.
DR PANTHER; PTHR42909:SF1; PFKB DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR42909; ZGC:136858; 1.
DR Pfam; PF04227; Indigoidine_A; 1.
DR Pfam; PF00294; PfkB; 1.
DR SUPFAM; SSF110581; Indigoidine synthase A-like; 1.
DR SUPFAM; SSF53613; Ribokinase-like; 1.
DR PROSITE; PS00583; PFKB_KINASES_1; 1.
DR PROSITE; PS00584; PFKB_KINASES_2; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000215289};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 394..572
FT /note="Carbohydrate kinase PfkB"
FT /evidence="ECO:0000259|Pfam:PF00294"
SQ SEQUENCE 798 AA; 84030 MW; 27CCF898A542864B CRC64;
MLSQAAARLC CRARGPARRA PRTIRSYHDV AQNKFLKVSE EIRDAVATGK PVVALETTIY
THGFPYPESV ALASLLESVV RVNGGIPATI GILNGVARVG LSAEELIELA STAEKKNALK
VSRRDLGYIC GLGMAGRQLH GGTTVSGTMV LAHLAGIKVF GTGGLGGVHR GGESSMDISA
DLTELGRTPV AVVSSGCKSF LDIPRTLEFL ETEGVCVGTF ADGREGSVDF PAFFTRDSGI
KSPRVIRDEA EAAAIIYAQS KLPVNSGIHF ANPVPAEQSI PKGEMDTIIE EAIRLAEVEG
YRGSDNTPFV LAKIKELSGG KSVIANRALV EANVKRATKV AVELAKLEQA DRGSGGRHMP
VVSENARADQ ATSEAGVNHK PLTKSTVDQL DKADVLVAGS LAIDLSCDYT PFASERDKIT
PVPQTSNPAV IGQSLGGVGH NVAIASHYLG SSVLFCSVVG DDLSGRAALS TLKEEGLPTT
GVQILPASSG ARTAQYIAVN DAKRDLVVAM ADMGIMELPE HVLDFDEFWE PLIRRTQPQW
VVVDANWSPA VLARWIAVAK QHGARVAFEP VSTAKSRRLF SKSSEAEAAI GPAGAVPNNA
VSLAAPNQYE LTAMYTTARE SGLFESEGWW RIIDAMGMSA SGSRDRLVAM TTAELVDQGI
PQQSIQLLPF IPCIITKLGA QGVLVTQLLR PGDARLTSPD SAPHILSRAS PTDELIGGVY
MRLFPSAGIL ADGEIVSVNG AGDTLLGAVV AGLAKGRGKG KTVEEVIPLA QEASLRTLKS
PGGVGRDLVA LRPLMDAL
//
