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Database: UniProt
Entry: A0A178DGU8_9PLEO
LinkDB: A0A178DGU8_9PLEO
Original site: A0A178DGU8_9PLEO 
ID   A0A178DGU8_9PLEO        Unreviewed;       555 AA.
AC   A0A178DGU8;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Phosphotransferase {ECO:0000256|RuleBase:RU362007};
DE            EC=2.7.1.- {ECO:0000256|RuleBase:RU362007};
GN   ORFNames=IQ07DRAFT_301626 {ECO:0000313|EMBL:OAL43258.1};
OS   Pyrenochaeta sp. DS3sAY3a.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Cucurbitariaceae;
OC   Pyrenochaeta.
OX   NCBI_TaxID=765867 {ECO:0000313|EMBL:OAL43258.1, ECO:0000313|Proteomes:UP000077535};
RN   [1] {ECO:0000313|EMBL:OAL43258.1, ECO:0000313|Proteomes:UP000077535}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL43258.1,
RC   ECO:0000313|Proteomes:UP000077535};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA   Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete fungi.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the hexokinase family.
CC       {ECO:0000256|ARBA:ARBA00009225, ECO:0000256|RuleBase:RU362007}.
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DR   EMBL; KV441669; OAL43258.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A178DGU8; -.
DR   STRING; 765867.A0A178DGU8; -.
DR   InParanoid; A0A178DGU8; -.
DR   OrthoDB; 5481886at2759; -.
DR   UniPathway; UPA00109; UER00180.
DR   Proteomes; UP000077535; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005536; F:glucose binding; IEA:InterPro.
DR   GO; GO:0004396; F:hexokinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0001678; P:intracellular glucose homeostasis; IEA:InterPro.
DR   CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR   Gene3D; 3.30.420.40; -; 1.
DR   Gene3D; 3.40.367.20; -; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR001312; Hexokinase.
DR   InterPro; IPR022673; Hexokinase_C.
DR   InterPro; IPR022672; Hexokinase_N.
DR   PANTHER; PTHR19443; HEXOKINASE; 1.
DR   PANTHER; PTHR19443:SF24; HEXOKINASE YLR446W-RELATED; 1.
DR   Pfam; PF00349; Hexokinase_1; 1.
DR   Pfam; PF03727; Hexokinase_2; 1.
DR   PRINTS; PR00475; HEXOKINASE.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   PROSITE; PS51748; HEXOKINASE_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362007};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Glycolysis {ECO:0000256|RuleBase:RU362007};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU362007};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU362007};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077535};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362007}.
FT   DOMAIN          103..293
FT                   /note="Hexokinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00349"
FT   DOMAIN          300..550
FT                   /note="Hexokinase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03727"
FT   COILED          74..101
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   555 AA;  61808 MW;  08219DBE4FF89373 CRC64;
     MPSLLLKRFK SRRVTLIPES DGTRDSPSSP PDSLKRCWYK QPMFDFWQGL LAALERIAML
     PSLLHSVLPS LSSRKRARDA LRTYDRTMDD LLREIQRLFE APLESAKLQQ MSIELRRQFA
     PKLQDSPICM LPSYNNTLPN GLEKGTYLAL DLGGSTFRIA LVELNGRQPG AKNMRIVTMK
     SFKIDEKVRQ RRGPDFFDWM AEKIQQALAD PKLQKSTGAR SFPMGLAWSF PVEQTSSRSA
     NLLDMGKGFR ATEGLLGQDL SELIMAPCRK RNLPVHMDSI VNDSSATLLS RAYEDPSTRF
     AVILGTGFNI SVHLPVSSLA TTKFKGYPQK WLDEATHVLV NTECSMFGKN VFPTTRWDDQ
     LNDAHVRPDF QPFEHMISGR YLGEIVRLII VEAVRTAGLF SGEMPEHLAE PYSLDTGTMA
     AMEMDSSKHL TNATSLFQSK HPLKKPATYN DIQFIRQISQ LVTHRAAALL ATGIHALWVL
     RTESEGLTPA NAGPTSIGCN GSVIEKYPFF RELCQSHLDE LAVASGAEPK SISLEIAVES
     AIFGAAVAVC CLEGQ
//
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