KARG2_CAEEL
ID KARG2_CAEEL Reviewed; 360 AA.
AC Q27535;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Probable arginine kinase ZC434.8;
DE Short=AK;
DE EC=2.7.3.3;
GN ORFNames=ZC434.8;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX 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 investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-arginine = ADP + H(+) + N(omega)-phospho-L-arginine;
CC Xref=Rhea:RHEA:22940, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:32682, ChEBI:CHEBI:58477, ChEBI:CHEBI:456216; EC=2.7.3.3;
CC -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
CC {ECO:0000255|PROSITE-ProRule:PRU00842, ECO:0000255|PROSITE-
CC ProRule:PRU00843}.
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DR EMBL; Z75714; CAB00062.1; -; Genomic_DNA.
DR PIR; T27569; T27569.
DR RefSeq; NP_492714.1; NM_060313.7.
DR AlphaFoldDB; Q27535; -.
DR SMR; Q27535; -.
DR BioGRID; 38324; 7.
DR DIP; DIP-25633N; -.
DR IntAct; Q27535; 1.
DR STRING; 6239.ZC434.8.1; -.
DR iPTMnet; Q27535; -.
DR EPD; Q27535; -.
DR PaxDb; Q27535; -.
DR PeptideAtlas; Q27535; -.
DR PRIDE; Q27535; -.
DR EnsemblMetazoa; ZC434.8.1; ZC434.8.1; WBGene00013894.
DR GeneID; 172907; -.
DR KEGG; cel:CELE_ZC434.8; -.
DR UCSC; ZC434.8.1; c. elegans.
DR CTD; 172907; -.
DR WormBase; ZC434.8; CE06583; WBGene00013894; -.
DR eggNOG; KOG3581; Eukaryota.
DR GeneTree; ENSGT00950000182772; -.
DR HOGENOM; CLU_019868_0_0_1; -.
DR InParanoid; Q27535; -.
DR OMA; EMHDGIK; -.
DR OrthoDB; 825025at2759; -.
DR PhylomeDB; Q27535; -.
DR BRENDA; 2.7.3.3; 1045.
DR PRO; PR:Q27535; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00013894; Expressed in adult organism and 4 other tissues.
DR GO; GO:0004054; F:arginine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004111; F:creatine kinase activity; IEA:InterPro.
DR GO; GO:0016301; F:kinase activity; IBA:GO_Central.
DR GO; GO:0046314; P:phosphocreatine biosynthetic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.135.10; -; 1.
DR InterPro; IPR000749; ATP-guanido_PTrfase.
DR InterPro; IPR022415; ATP-guanido_PTrfase_AS.
DR InterPro; IPR022414; ATP-guanido_PTrfase_cat.
DR InterPro; IPR022413; ATP-guanido_PTrfase_N.
DR InterPro; IPR036802; ATP-guanido_PTrfase_N_sf.
DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR PANTHER; PTHR11547; PTHR11547; 1.
DR Pfam; PF00217; ATP-gua_Ptrans; 1.
DR Pfam; PF02807; ATP-gua_PtransN; 1.
DR SUPFAM; SSF48034; SSF48034; 1.
DR SUPFAM; SSF55931; SSF55931; 1.
DR PROSITE; PS00112; PHOSPHAGEN_KINASE; 1.
DR PROSITE; PS51510; PHOSPHAGEN_KINASE_C; 1.
DR PROSITE; PS51509; PHOSPHAGEN_KINASE_N; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..360
FT /note="Probable arginine kinase ZC434.8"
FT /id="PRO_0000211989"
FT DOMAIN 10..92
FT /note="Phosphagen kinase N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00842"
FT DOMAIN 122..359
FT /note="Phosphagen kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 65..69
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 125..129
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 189
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 229
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 233
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 275
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 284..288
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 312..317
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 317
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 327
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
SQ SEQUENCE 360 AA; 40382 MW; 176760B381EF26D7 CRC64;
MTATPEVQKS IEEVYTKLQG ASDCSSLLKK HLTKDVVAKN KSKKTRLGAT LLDVIQSGGE
NLDSGVGIYA PDAESYTLFA DLFNPVIEEY HNGFKATDTQ PAMDLGEKNV GELADLDPEG
KFIVSTRIRC GRSLQGYPFN PCLSETNYKM METRMKEIFN SITDPELKGT YYPLTGMDEE
TKKKLIADHF LFKEGDRFLK AANANRYWPN GRGIFHNEKK TFLVWVNEED HLRIISMQNG
GNVGEVLARL IKGLNLVAAK APFARHPRLG WLTFCPTNLG TTVRASVHIK LPKISAKDDF
KKICSDMKLQ IRGIHGEHSE SKEGIYDISN KQRLGLTEYQ AVRQMYDGLK KLIELEKAAA
