(data stored in SCRATCH zone)

SWISSPROT: B6HG11_PENRW

ID   B6HG11_PENRW            Unreviewed;       518 AA.
AC   B6HG11;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   05-JUL-2017, entry version 64.
DE   RecName: Full=Aspartokinase {ECO:0000256|RuleBase:RU003448};
DE            EC=2.7.2.4 {ECO:0000256|RuleBase:RU003448};
GN   ORFNames=Pc20g00640 {ECO:0000313|EMBL:CAP85393.1}, PCH_Pc20g00640
GN   {ECO:0000313|EMBL:CAP85393.1};
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 /
OS   Wisconsin 54-1255) (Penicillium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP85393.1, ECO:0000313|Proteomes:UP000000724};
RN   [1] {ECO:0000313|EMBL:CAP85393.1, ECO:0000313|Proteomes:UP000000724}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC   {ECO:0000313|Proteomes:UP000000724};
RX   PubMed=18820685; DOI=10.1038/nbt.1498;
RA   van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA   Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA   Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA   Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A.,
RA   van der Klei I.J., van Peij N.N.M.E., Veenhuis M., von Doehren H.,
RA   Wagner C., Wortman J.R., Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(2008).
CC   -!- CATALYTIC ACTIVITY: ATP + L-aspartate = ADP + 4-phospho-L-
CC       aspartate. {ECO:0000256|RuleBase:RU003448}.
CC   -!- SIMILARITY: Belongs to the aspartokinase family.
CC       {ECO:0000256|RuleBase:RU003448}.
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DR   EMBL; AM920435; CAP85393.1; -; Genomic_DNA.
DR   RefSeq; XP_002562626.1; XM_002562580.1.
DR   ProteinModelPortal; B6HG11; -.
DR   STRING; 500485.XP_002562626.1; -.
DR   EnsemblFungi; CAP85393; CAP85393; PCH_Pc20g00640.
DR   GeneID; 8307721; -.
DR   KEGG; pcs:Pc20g00640; -.
DR   eggNOG; KOG0456; Eukaryota.
DR   eggNOG; COG0527; LUCA.
DR   HOGENOM; HOG000293094; -.
DR   KO; K00928; -.
DR   OMA; INIMMIS; -.
DR   OrthoDB; EOG092C1PG8; -.
DR   BioCyc; PCHR:PC20G00640-MONOMER; -.
DR   Proteomes; UP000000724; Contig Pc00c20.
DR   GO; GO:0004072; F:aspartate kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:InterPro.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR   InterPro; IPR001341; Asp_kinase_dom.
DR   InterPro; IPR018042; Aspartate_kinase_CS.
DR   InterPro; IPR027795; GATS-like_ACT_dom.
DR   Pfam; PF00696; AA_kinase; 1.
DR   Pfam; PF13840; ACT_7; 1.
DR   SUPFAM; SSF53633; SSF53633; 1.
DR   TIGRFAMs; TIGR00657; asp_kinases; 1.
DR   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS00324; ASPARTOKINASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; B6HG11.
DR   SWISS-2DPAGE; B6HG11.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000724};
KW   Kinase {ECO:0000256|RuleBase:RU003448};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000724};
KW   Transferase {ECO:0000256|RuleBase:RU003448}.
FT   DOMAIN      455    518       ACT. {ECO:0000259|PROSITE:PS51671}.
SQ   SEQUENCE   518 AA;  56814 MW;  913F2B969687E973 CRC64;
     MATTILDSNL PVTAQAHSSW VVQKFGGTSV GKFARNIIEQ VVEPSLVNNR VAVVCSARSS
     STKAEGTTNR LLRAARDAES PRSRQYLTLV EAVRLEHVQV AQEELKSVEI RDQVIADITG
     ECERVLKFLE AAQTLGEISA RCVDKVMSTG EKLSCRLMAA LLQDRGVDSQ YVDLAEIIDF
     PIGPHGLDQD FYNTLAAAFG SKVEACGHRV PVMTGYFGTI PGGLLDQIGR GYTDLCAALV
     AVGTRAQELQ VWKEVDGIFT ADPRKVPTAH LLPAITPAEA AELTFYGSEV IHPFTMEQVI
     RARIPIRIKN VMNPKNEGTI IFPDSVAELE RTTPGHDPRL FRTRSPSLAN TPKRPTAVTI
     KHNILVINVH SNKRSLSHGF FAGIFSVLDK WRLSIDLIST SEVHVSLALH SEMPLLNGNG
     RDEYQVIDDD LQGALNDLKR YGTVDIIPEM AILSLVGKQM KNMIGVAGRM FTTLGENSVN
     IEMISQGASE INISCVIEER DADRALNIIH TSMFTFLD
//

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