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Database: UniProt/TrEMBL
Entry: G0SCG9_CHATD
LinkDB: G0SCG9_CHATD
Original site: G0SCG9_CHATD 
ID   G0SCG9_CHATD            Unreviewed;       494 AA.
AC   G0SCG9;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   23-MAY-2018, entry version 35.
DE   RecName: Full=Phosphotransferase {ECO:0000256|RuleBase:RU362007};
DE            EC=2.7.1.- {ECO:0000256|RuleBase:RU362007};
GN   ORFNames=CTHT_0057190 {ECO:0000313|EMBL:EGS19095.1};
OS   Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Sordariomycetidae; Sordariales; Chaetomiaceae;
OC   Chaetomium.
OX   NCBI_TaxID=759272 {ECO:0000313|Proteomes:UP000008066};
RN   [1] {ECO:0000313|EMBL:EGS19095.1, ECO:0000313|Proteomes:UP000008066}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1495 / CBS 144.50 / IMI 039719
RC   {ECO:0000313|Proteomes:UP000008066};
RX   PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA   Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R.,
RA   Devos D.P., Arumugam M., Bork P., Hurt E.;
RT   "Insight into structure and assembly of the nuclear pore complex by
RT   utilizing the genome of a eukaryotic thermophile.";
RL   Cell 146:277-289(2011).
CC   -!- SIMILARITY: Belongs to the hexokinase family.
CC       {ECO:0000256|RuleBase:RU362007, ECO:0000256|SAAS:SAAS00672880}.
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DR   EMBL; GL988045; EGS19095.1; -; Genomic_DNA.
DR   RefSeq; XP_006696040.1; XM_006695977.1.
DR   EnsemblFungi; EGS19095; EGS19095; CTHT_0057190.
DR   GeneID; 18259757; -.
DR   KEGG; cthr:CTHT_0057190; -.
DR   KO; K00844; -.
DR   OrthoDB; EOG092C2JW4; -.
DR   Proteomes; UP000008066; Unassembled WGS sequence.
DR   GO; GO:0005623; C:cell; IEA:GOC.
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:0001678; P:cellular glucose homeostasis; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR   InterPro; IPR001312; Hexokinase.
DR   InterPro; IPR019807; Hexokinase_BS.
DR   InterPro; IPR022673; Hexokinase_C.
DR   InterPro; IPR022672; Hexokinase_N.
DR   PANTHER; PTHR19443; PTHR19443; 1.
DR   Pfam; PF00349; Hexokinase_1; 1.
DR   Pfam; PF03727; Hexokinase_2; 1.
DR   PROSITE; PS00378; HEXOKINASE_1; 1.
DR   PROSITE; PS51748; HEXOKINASE_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU362007,
KW   ECO:0000256|SAAS:SAAS00672869};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008066};
KW   Glycolysis {ECO:0000256|RuleBase:RU362007,
KW   ECO:0000256|SAAS:SAAS00672870};
KW   Kinase {ECO:0000256|RuleBase:RU362007, ECO:0000256|SAAS:SAAS00672871,
KW   ECO:0000313|EMBL:EGS19095.1};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU362007,
KW   ECO:0000256|SAAS:SAAS00672883};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008066};
KW   Transferase {ECO:0000256|RuleBase:RU362007,
KW   ECO:0000256|SAAS:SAAS00672884}.
FT   DOMAIN       29    224       Hexokinase_1. {ECO:0000259|Pfam:PF00349}.
FT   DOMAIN      230    473       Hexokinase_2. {ECO:0000259|Pfam:PF03727}.
SQ   SEQUENCE   494 AA;  54524 MW;  09CF034FB509C35D CRC64;
     MAGDDPKTPP SEKGSGSDAD VPKDLAKEIK YIEELFTVDT AKLKQITDHF VKELEKGLSV
     EGGSIPMNPT WVMGFPTGHE TGTFLALDMG GTNLRVCQVT LTDQQSEFDI IQSKYRIPPP
     LKTGTAEELF EYIADCLLQF IQTHHDDLSQ IGRMPLGFTF SYPATQNYID EGILQRWTKG
     FDIEGVEGKN VVPMFEAALA RRGVPIRLAA LINDTTGTLI ASAYTDPKMK IGCIFGTGCN
     AAYMEDCGSI PKLAHLNLPP ETPMAINCEW GAFDNEHKVL PRTPYDITID EDSPRPGQQA
     FEKMIAGLYL GEIFRLTLVD LHDNHDRRVF VGQDITKLRK PYTLDTSFLS AIEEDSDENL
     SDIAGLFQNK LNITPNKAER ILIKRLAELI GTRAARLSAC GVAAICKKKG YKECHVGADG
     SVFNKYPHFK ERGAQALREI LDWGEKKDPK EEDPIEILAA EDGSGVGAAL IAALTLERVQ
     KGNLHGILHP ENYV
//
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