ID   KAD1_CAEEL              Reviewed;         210 AA.
AC   Q20140;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 55.
DE   RecName: Full=Probable adenylate kinase isoenzyme F38B2.4;
DE            Short=AK;
DE            EC=2.7.4.3;
DE   AltName: Full=ATP-AMP transphosphorylase;
GN   ORFNames=F38B2.4;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea;
OC   Rhabditidae; Peloderinae; Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   MEDLINE=99069613; PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for
RT   investigating biology.";
RL   Science 282:2012-2018(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Bristol N2;
RA   Kohara Y., Shin-i T., Suzuki Y., Sugano S., Potdevin M.,
RA   Thierry-Mieg Y., Thierry-Mieg D., Thierry-Mieg J.;
RT   "The Caenorhabditis elegans transcriptome project, a complementary
RT   view of the genome.";
RL   Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible transfer of the terminal
CC       phosphate group between ATP and AMP. Small ubiquitous enzyme
CC       involved in energy metabolism and nucleotide synthesis that is
CC       essential for maintenance and cell growth (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + AMP = 2 ADP.
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the adenylate kinase family.
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DR   EMBL; Z50045; CAA90364.1; -; Genomic_DNA.
DR   EMBL; AF304123; AAG50236.1; -; mRNA.
DR   PIR; T21947; T21947.
DR   RefSeq; NP_509884.1; -.
DR   UniGene; Cel.7837; -.
DR   HSSP; P00571; 3ADK.
DR   Ensembl; F38B2.4; Caenorhabditis elegans.
DR   GeneID; 181317; -.
DR   KEGG; cel:F38B2.4; -.
DR   WormBase; WBGene00009531; F38B2.4.
DR   WormPep; F38B2.4; CE02218.
DR   OMA; Q20140; PRTEENR.
DR   BRENDA; 2.7.4.3; 672.
DR   NextBio; 913424; -.
DR   ArrayExpress; Q20140; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004017; F:adenylate kinase activity; IEA:EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046034; P:ATP metabolic process; IEA:InterPro.
DR   InterPro; IPR000850; Adenylate_kin.
DR   InterPro; IPR006267; Adenylate_kin1.
DR   PANTHER; PTHR23359; Adenylate_kin; 1.
DR   Pfam; PF00406; ADK; 1.
DR   PRINTS; PR00094; ADENYLTKNASE.
DR   ProDom; PD000657; Adenylate_kin; 1.
DR   TIGRFAMs; TIGR01360; aden_kin_iso1; 1.
DR   PROSITE; PS00113; ADENYLATE_KINASE; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Complete proteome; Cytoplasm; Kinase; Nucleotide-binding;
KW   Transferase.
FT   CHAIN         1    210       Probable adenylate kinase isoenzyme
FT                                F38B2.4.
FT                                /FTId=PRO_0000158932.
FT   NP_BIND      27     35       ATP.
FT   NP_BIND     107    114       AMP (By similarity).
FT   BINDING      51     51       AMP (By similarity).
SQ   SEQUENCE   210 AA;  22597 MW;  786CB879D83DDFFC CRC64;
     MAPTVERKNI NLAPLKAAGV PIFFIVGGPG SGKGTQCDKI VAKYGLTHLS SGDLLRDEVK
     SGSPRGAQLT AIMESGALVP LEVVLDLVKE AMLKAIEKGS KGFLIDGYPR EVAQGQQFES
     EIQEAKLVLF FDVAEETLVK RLLHRAQTSG RADDNADTIK KRLHTFVTST APVVDYYESK
     GKLVRINAEG SVDDIFAVVV ANLDKATSKL
//