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Database: UniProt/TrEMBL
Entry: A1C5Z4_ASPCL
LinkDB: A1C5Z4_ASPCL
Original site: A1C5Z4_ASPCL 
ID   A1C5Z4_ASPCL            Unreviewed;       490 AA.
AC   A1C5Z4;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   27-SEP-2017, entry version 67.
DE   RecName: Full=Phosphotransferase {ECO:0000256|RuleBase:RU362007};
DE            EC=2.7.1.- {ECO:0000256|RuleBase:RU362007};
GN   ORFNames=ACLA_068420 {ECO:0000313|EMBL:EAW13815.1};
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 /
OS   NCTC 3887 / NRRL 1).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW13815.1, ECO:0000313|Proteomes:UP000006701};
RN   [1] {ECO:0000313|EMBL:EAW13815.1, ECO:0000313|Proteomes:UP000006701}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC   {ECO:0000313|Proteomes:UP000006701};
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P.,
RA   Anderson M.J., Crabtree J., Silva J.C., Badger J.H., Albarraq A.,
RA   Angiuoli S., Bussey H., Bowyer P., Cotty P.J., Dyer P.S., Egan A.,
RA   Galens K., Fraser-Liggett C.M., Haas B.J., Inman J.M., Kent R.,
RA   Lemieux S., Malavazi I., Orvis J., Roemer T., Ronning C.M.,
RA   Sundaram J.P., Sutton G., Turner G., Venter J.C., White O.R.,
RA   Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H., Wortman J.R.,
RA   Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
CC   -!- SIMILARITY: Belongs to the hexokinase family.
CC       {ECO:0000256|RuleBase:RU362007, ECO:0000256|SAAS:SAAS00672880}.
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DR   EMBL; DS027045; EAW13815.1; -; Genomic_DNA.
DR   RefSeq; XP_001275241.1; XM_001275240.1.
DR   ProteinModelPortal; A1C5Z4; -.
DR   SMR; A1C5Z4; -.
DR   STRING; 5057.CADACLAP00006446; -.
DR   PRIDE; A1C5Z4; -.
DR   EnsemblFungi; CADACLAT00006606; CADACLAP00006446; CADACLAG00006606.
DR   GeneID; 4708030; -.
DR   KEGG; act:ACLA_068420; -.
DR   EuPathDB; FungiDB:ACLA_068420; -.
DR   HOGENOM; HOG000162670; -.
DR   KO; K00844; -.
DR   OMA; ERQFFRA; -.
DR   OrthoDB; EOG092C2JW4; -.
DR   Proteomes; UP000006701; 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:UP000006701};
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:EAW13815.1};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU362007,
KW   ECO:0000256|SAAS:SAAS00672883};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006701};
KW   Transferase {ECO:0000256|RuleBase:RU362007,
KW   ECO:0000256|SAAS:SAAS00672884}.
FT   DOMAIN       27    221       Hexokinase_1. {ECO:0000259|Pfam:PF00349}.
FT   DOMAIN      227    466       Hexokinase_2. {ECO:0000259|Pfam:PF03727}.
SQ   SEQUENCE   490 AA;  54327 MW;  037BC19FD8E1152A CRC64;
     MVGIGPKRPP SRKGSMADVP QNLLQQIKEF EDMFTVDRTK LKQVVDHFVK ELEQGLTVEG
     GNIPMNVTWV MGFPDGDEQG TFLALDMGGT NLRVCEITLT EEKGAFDICQ SKYRMPEELK
     TGTAEELWEY IADCLQQFID FHHEDEELSQ LPLGFTFSYP ATQDYIDHGV LQRWTKGFDI
     DGVEGQDVVP PLEAILQKKG LPIKVAALIN DTTGTLIASA YTDPEMKIGC IFGTGVNAAY
     MDNVGSVPKL AHMNLPPDMP VAINCEYGAF DNEHIVLPLT KYDHIIDRDS PRPGQQAFEK
     MTAGLYLGEI FRLALIDLLD SRPGLIFEGQ DTSKLRKPYL LDASFLAAIE EDPYENLEET
     QELFQRELNI KPTQAELEMI RRLAELIGTR AARLSACGVA AICKKKNIER CHVGADGSVF
     TKYPNFKARG AQALREILDW APNENDKVSI LAAEDGSGVG AALIAALTLK RVKAGNLAGI
     RNKDEMQKML
//
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