KARG1_CAEEL
ID KARG1_CAEEL Reviewed; 396 AA.
AC Q10454; Q86NG9;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Probable arginine kinase F46H5.3;
DE Short=AK;
DE EC=2.7.3.3;
GN ORFNames=F46H5.3;
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], AND ALTERNATIVE SPLICING.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=Q10454-1; Sequence=Displayed;
CC Name=b;
CC IsoId=Q10454-2; Sequence=VSP_012750;
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; FO081399; CCD71355.1; -; Genomic_DNA.
DR EMBL; FO081399; CCD71356.1; -; Genomic_DNA.
DR PIR; T34272; T34272.
DR RefSeq; NP_509217.2; NM_076816.2.
DR RefSeq; NP_872253.1; NM_182453.5.
DR AlphaFoldDB; Q10454; -.
DR SMR; Q10454; -.
DR BioGRID; 45911; 67.
DR DIP; DIP-26821N; -.
DR IntAct; Q10454; 1.
DR STRING; 6239.F46H5.3a.3; -.
DR iPTMnet; Q10454; -.
DR World-2DPAGE; 0020:Q10454; -.
DR EPD; Q10454; -.
DR PaxDb; Q10454; -.
DR PeptideAtlas; Q10454; -.
DR EnsemblMetazoa; F46H5.3a.1; F46H5.3a.1; WBGene00018519. [Q10454-1]
DR EnsemblMetazoa; F46H5.3b.1; F46H5.3b.1; WBGene00018519. [Q10454-2]
DR UCSC; F46H5.3b.2; c. elegans. [Q10454-1]
DR WormBase; F46H5.3a; CE37112; WBGene00018519; -. [Q10454-1]
DR WormBase; F46H5.3b; CE33098; WBGene00018519; -. [Q10454-2]
DR eggNOG; KOG3581; Eukaryota.
DR GeneTree; ENSGT00950000182772; -.
DR InParanoid; Q10454; -.
DR OMA; EYHNGFG; -.
DR OrthoDB; 825025at2759; -.
DR PhylomeDB; Q10454; -.
DR BRENDA; 2.7.3.3; 1045.
DR PRO; PR:Q10454; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00018519; Expressed in larva 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 Alternative splicing; ATP-binding; Kinase; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..396
FT /note="Probable arginine kinase F46H5.3"
FT /id="PRO_0000211988"
FT DOMAIN 47..129
FT /note="Phosphagen kinase N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00842"
FT DOMAIN 159..396
FT /note="Phosphagen kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 102..106
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 162..166
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 226
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 266
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 270
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 312
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 321..325
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 349..354
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 354
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 364
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT VAR_SEQ 1..37
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_012750"
SQ SEQUENCE 396 AA; 44168 MW; 0DF10283D3FEA45B CRC64;
MLHRCSRVLS QFLGRGNSKM LREAYSTSLH CVQAQEGMSV SPDVIAKIEE GYAKLQAAPE
CHSLLKKYLT KEVVDQLKDK KTKLGANLLD VIQSGVANLD SGVGVYAPDA EAYTLFKPLF
DPLIQDYHNG FAPDAKQPNT DLGEGKTSAL VDLDPEGKFI NSTRIRCGRS LQGYPFNPCL
SEANYLEMES KVKAIFDNIT DPELAGKYFP LDGMTKEIQD QLIKDHFLFK EGDRFLQAAN
ACRYWPKGRG IFHNNQKTFL IWCNEEDHLR IISMQEGGNV GQVLERLIKG VKTIEKQAPF
SRDDRLGWLT FCPSNLGTTV RASVHIRLPK ISAKPDFKSI CDGLKLQIRG IHGEHSESEG
GVYDISNKAR LGLTEFEAVK QMYDGIAHLI ALEKAA
