KARG_APIME
ID KARG_APIME Reviewed; 355 AA.
AC O61367;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Arginine kinase;
DE Short=AK;
DE EC=2.7.3.3;
GN Name=ARGK;
OS Apis mellifera (Honeybee).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea; Apidae;
OC Apis.
OX NCBI_TaxID=7460;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=9602169; DOI=10.1016/s0378-1119(98)00114-0;
RA Kucharski R., Maleszka R.;
RT "Arginine kinase is highly expressed in the compound eye of the honey bee,
RT Apis mellifera.";
RL Gene 211:343-349(1998).
CC -!- FUNCTION: May play an important role in the energy releasing mechanism
CC in the visual system. By acting as an energy shuttle and/or as an
CC energy reservoir, ARGK can provide both spatial and temporal buffering
CC in delivering energy in sensory cells.
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 -!- TISSUE SPECIFICITY: Highest level of expression in the compound eye.
CC Relatively abundant in the brain, the thorax and the antennae. Lowest
CC expression in the ovaries.
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; AF023619; AAC39040.1; -; mRNA.
DR PIR; PC6506; PC6506.
DR RefSeq; NP_001011603.1; NM_001011603.1.
DR AlphaFoldDB; O61367; -.
DR SMR; O61367; -.
DR STRING; 7460.GB54446-PA; -.
DR PaxDb; O61367; -.
DR PRIDE; O61367; -.
DR EnsemblMetazoa; NM_001011603; NP_001011603; GeneID_550932.
DR GeneID; 550932; -.
DR KEGG; ame:550932; -.
DR CTD; 39041; -.
DR eggNOG; KOG3581; Eukaryota.
DR InParanoid; O61367; -.
DR PhylomeDB; O61367; -.
DR BRENDA; 2.7.3.3; 387.
DR Proteomes; UP000005203; Unplaced.
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: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 2: Evidence at transcript level;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..355
FT /note="Arginine kinase"
FT /id="PRO_0000211991"
FT DOMAIN 6..90
FT /note="Phosphagen kinase N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00842"
FT DOMAIN 118..355
FT /note="Phosphagen kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 63..67
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 121..125
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 184
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 224
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 228
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 270
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 279..283
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 308..313
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 313
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 355 AA; 40008 MW; E3BD2CA44BBDFFFD CRC64;
MVDQAVLDKL ETGFSKLSSS DSKSLLKKYL SKDVFDQLKT KKTSFDSTLL DCIQSGIENL
DSGVGIYAPD AEAYTLFADL FDPIIEDYHG GFKKTDKHPP KDFGDVDSLG NLDPANEFIV
STRVRCGRSL EGYPFNPCLT EAQYKEMEEK VSSTLSGLEG ELKGTFYPLT GMSKETQQKL
IDDHFLFKEG DRFLQAANAC RFWPTGRGIY HNDDKTFLVW CNEEDHLRII SMQMGGDLGQ
VYRRLVHAVN EIEKRLLFSH NDRLGFLTFC PTNLGTTVRA SVHIKLPKLA ANRAKLEEIA
GKFNLQVRGT RGEHTEAEGG IYDISNKRRL GLTEYQAVKE MHDGIAELIK LEKEL
