ID K4PWX1_BOMMO Unreviewed; 385 AA.
AC K4PWX1;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 22-FEB-2023, entry version 44.
DE RecName: Full=arginine kinase {ECO:0000256|ARBA:ARBA00012230};
DE EC=2.7.3.3 {ECO:0000256|ARBA:ARBA00012230};
GN Name=AK {ECO:0000313|EMBL:BAM62792.1};
GN Synonyms=692924 {ECO:0000313|EnsemblMetazoa:XP_012543872.1};
OS Bombyx mori (Silk moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Bombycidae; Bombycinae; Bombyx.
OX NCBI_TaxID=7091 {ECO:0000313|EMBL:BAM62792.1};
RN [1] {ECO:0000313|Proteomes:UP000005204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=p50T {ECO:0000313|Proteomes:UP000005204};
RX PubMed=19121390; DOI=10.1016/j.ibmb.2008.11.004;
RG International Silkworm Genome Consortium;
RT "The genome of a lepidopteran model insect, the silkworm Bombyx mori.";
RL Insect Biochem. Mol. Biol. 38:1036-1045(2008).
RN [2] {ECO:0000313|EMBL:BAM62792.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Reproductive organ {ECO:0000313|EMBL:BAM62792.1};
RA Nagaoka S., Otuki M.;
RT "Identification of arginine kinase from Bombyx mori.";
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblMetazoa:XP_012543872.1}
RP IDENTIFICATION.
RC STRAIN=p50T (Dazao) {ECO:0000313|EnsemblMetazoa:XP_012543872.1};
RG EnsemblMetazoa;
RL Submitted (JUN-2022) to UniProtKB.
CC -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
CC {ECO:0000256|ARBA:ARBA00006798, ECO:0000256|PROSITE-ProRule:PRU00842,
CC ECO:0000256|RuleBase:RU000505}.
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DR EMBL; AB711181; BAM62792.1; -; mRNA.
DR RefSeq; XP_012543872.1; XM_012688418.1.
DR AlphaFoldDB; K4PWX1; -.
DR Allergome; 5850; Bomb m 1.
DR EnsemblMetazoa; XM_012688418.2; XP_012543872.1; GeneID_692924.
DR GeneID; 692924; -.
DR CTD; 692924; -.
DR HOGENOM; CLU_019868_0_1_1; -.
DR OrthoDB; 35839at2759; -.
DR Proteomes; UP000005204; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004054; F:arginine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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 CDD; cd07932; arginine_kinase_like; 1.
DR Gene3D; 1.10.135.10; ATP:guanido phosphotransferase, N-terminal domain; 1.
DR Gene3D; 3.30.590.10; Glutamine synthetase/guanido kinase, catalytic domain; 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:SF38; ARGININE KINASE; 1.
DR PANTHER; PTHR11547; ARGININE OR CREATINE KINASE; 1.
DR Pfam; PF00217; ATP-gua_Ptrans; 1.
DR Pfam; PF02807; ATP-gua_PtransN; 1.
DR SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1.
DR SUPFAM; SSF48034; Guanido kinase N-terminal domain; 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00843};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PROSITE-
KW ProRule:PRU00843}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00843}; Reference proteome {ECO:0000313|Proteomes:UP000005204};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU00843}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 36..120
FT /note="Phosphagen kinase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51509"
FT DOMAIN 148..385
FT /note="Phosphagen kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51510"
FT BINDING 151..155
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT BINDING 214
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT BINDING 258
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT BINDING 309..313
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT BINDING 338..343
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
SQ SEQUENCE 385 AA; 43303 MW; F5938703B80C5A45 CRC64;
MNYKLKVTIP VVVCGGAVLA YYIMRRKAAT MVDAATLEKL EAGFSKLQGS DSKSLLKKYL
TREVFDSLKN KKTSFGSTLL DCIQSGVENL DSGVGIYAPD AESYSVFAEL FDPIIEDYHN
GFKKTDKHPP KNWGDVDTLG NLDPAGEFVV STRVRCGRSL EGYPFNPCLT ESQYKEMEDK
VSGTLSSLEG ELKGTFYPLT GMSKETQQQL IDDHFLFKEG DRFLQAANAC RFWPTGRGIY
HNENKTFLVW CNEEDHLRII SMQMGGDLQQ VYKRLVSAVN EIEKKIPFSH HDRLGFLTFC
PTNLGTTVRA SVHIKLPKLA ADKKKLEEVA SKYHLQVRGT RGEHTEAEGG VYDISNKRRM
GLTEYDAVKE MYDGIAELIK IEKSL
//
