(data stored in SCRATCH zone)

SWISSPROT: B6HG07_PENRW

ID   B6HG07_PENRW            Unreviewed;       177 AA.
AC   B6HG07;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   07-JUN-2017, entry version 50.
DE   RecName: Full=Adenylate kinase isoenzyme 6 homolog {ECO:0000256|HAMAP-Rule:MF_03173};
DE            Short=AK6 {ECO:0000256|HAMAP-Rule:MF_03173};
DE            EC=2.7.4.3 {ECO:0000256|HAMAP-Rule:MF_03173};
DE   AltName: Full=Dual activity adenylate kinase/ATPase {ECO:0000256|HAMAP-Rule:MF_03173};
DE            Short=AK/ATPase {ECO:0000256|HAMAP-Rule:MF_03173};
GN   ORFNames=Pc20g00600 {ECO:0000313|EMBL:CAP85389.1}, PCH_Pc20g00600
GN   {ECO:0000313|EMBL:CAP85389.1};
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:CAP85389.1, ECO:0000313|Proteomes:UP000000724};
RN   [1] {ECO:0000313|EMBL:CAP85389.1, 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   -!- FUNCTION: Broad-specificity nucleoside monophosphate (NMP) kinase
CC       that catalyzes the reversible transfer of the terminal phosphate
CC       group between nucleoside triphosphates and monophosphates. Has
CC       also ATPase activity. May be involved in rRNA maturation and
CC       transcription regulation. {ECO:0000256|HAMAP-Rule:MF_03173}.
CC   -!- CATALYTIC ACTIVITY: ATP + AMP = 2 ADP. {ECO:0000256|HAMAP-
CC       Rule:MF_03173}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03173}.
CC       Nucleus {ECO:0000256|HAMAP-Rule:MF_03173}.
CC   -!- SIMILARITY: Belongs to the adenylate kinase family. AK6 subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_03173}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_03173}.
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DR   EMBL; AM920435; CAP85389.1; -; Genomic_DNA.
DR   RefSeq; XP_002562622.1; XM_002562576.1.
DR   ProteinModelPortal; B6HG07; -.
DR   STRING; 500485.XP_002562622.1; -.
DR   EnsemblFungi; CAP85389; CAP85389; PCH_Pc20g00600.
DR   GeneID; 8307717; -.
DR   KEGG; pcs:Pc20g00600; -.
DR   eggNOG; KOG3347; Eukaryota.
DR   eggNOG; COG1936; LUCA.
DR   HOGENOM; HOG000224472; -.
DR   KO; K18532; -.
DR   OMA; DNVQCEI; -.
DR   OrthoDB; EOG092C5GXJ; -.
DR   BioCyc; PCHR:PC20G00600-MONOMER; -.
DR   Proteomes; UP000000724; Contig Pc00c20.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004017; F:adenylate kinase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATPase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   HAMAP; MF_00039; Adenylate_kinase_AK6; 1.
DR   InterPro; IPR020618; Adenyl_kinase_AK6.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   3: Inferred from homology;
DR   PRODOM; B6HG07.
DR   SWISS-2DPAGE; B6HG07.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_03173};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000724};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03173};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_03173};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03173};
KW   Nucleus {ECO:0000256|HAMAP-Rule:MF_03173};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000724};
KW   Ribosome biogenesis {ECO:0000256|HAMAP-Rule:MF_03173};
KW   rRNA processing {ECO:0000256|HAMAP-Rule:MF_03173};
KW   Transcription {ECO:0000256|HAMAP-Rule:MF_03173};
KW   Transcription regulation {ECO:0000256|HAMAP-Rule:MF_03173};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_03173}.
FT   REGION       34     57       NMPbind. {ECO:0000256|HAMAP-Rule:
FT                                MF_03173}.
FT   REGION      110    120       LID. {ECO:0000256|HAMAP-Rule:MF_03173}.
FT   BINDING      40     40       AMP. {ECO:0000256|HAMAP-Rule:MF_03173}.
FT   BINDING      80     80       ATP. {ECO:0000256|HAMAP-Rule:MF_03173}.
FT   BINDING     107    107       ATP. {ECO:0000256|HAMAP-Rule:MF_03173}.
FT   BINDING     111    111       ATP. {ECO:0000256|HAMAP-Rule:MF_03173}.
SQ   SEQUENCE   177 AA;  20099 MW;  C84BBCBF2A691212 CRC64;
     MRTSPNVIIT GTPGVGKTVH CEQLAQEIGL KHLSINQVAK DRGCFDEYDE ELKTWVVDED
     KLLDALEDEI PNGGYLIDWH ACDLFPKSWI DLVVVLRCPT TDVLYDRLSS RGYHEKKLEE
     NVDAEIFGVL ADEAREAFDE EIVVELNSEQ DSDVDSNCQR IAQWVDSWKQ SQAENAD
//

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