ID A0A0M3JSD5_ANISI Unreviewed; 410 AA.
AC A0A0M3JSD5;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 22-FEB-2023, entry version 31.
DE RecName: Full=arginine kinase {ECO:0000256|ARBA:ARBA00012230};
DE EC=2.7.3.3 {ECO:0000256|ARBA:ARBA00012230};
GN ORFNames=ASIM_LOCUS10439 {ECO:0000313|EMBL:VDK42987.1};
OS Anisakis simplex (Herring worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Anisakidae; Anisakis;
OC Anisakis simplex complex.
OX NCBI_TaxID=6269 {ECO:0000313|Proteomes:UP000036680, ECO:0000313|WBParaSite:ASIM_0001088101-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:ASIM_0001088101-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDK42987.1, ECO:0000313|Proteomes:UP000267096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
CC {ECO:0000256|ARBA:ARBA00006798, ECO:0000256|PROSITE-ProRule:PRU00842}.
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DR EMBL; UYRR01030999; VDK42987.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M3JSD5; -.
DR WBParaSite; ASIM_0001088101-mRNA-1; ASIM_0001088101-mRNA-1; ASIM_0001088101.
DR Proteomes; UP000036680; Unplaced.
DR Proteomes; UP000267096; Unassembled WGS sequence.
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; 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:SF20; 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; PS51510; PHOSPHAGEN_KINASE_C; 1.
DR PROSITE; PS51509; PHOSPHAGEN_KINASE_N; 1.
PE 3: Inferred from homology;
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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00843}; Reference proteome {ECO:0000313|Proteomes:UP000267096};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU00843}.
FT DOMAIN 51..133
FT /note="Phosphagen kinase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51509"
FT DOMAIN 162..409
FT /note="Phosphagen kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51510"
FT BINDING 165..169
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT BINDING 239
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT BINDING 283
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT BINDING 334..338
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT BINDING 362..367
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
SQ SEQUENCE 410 AA; 46612 MW; 4C7E93DFCCC5D041 CRC64;
MAFLKNQKAV FSSLLAIAGG ATAFAYFYPY NRDVALVNLQ INEADASTVK KLEEAFQRLQ
KAEDCHSLLK KHLSRDVLDQ LKYKKTKLGA TLYDIIRSGV FNLDANVGVY ASDSESYKTF
AALFDPIIED YHGFSPNQKH PKVDLGVGRT ADFPPLDPDN KYILSTRIRC ARTVAGYPFN
PLLTQDDYLI LEQKGSDLFS FVLFKVKNSL SLLDGELNGN YHPLEGMSKE VQSRLIQEHF
LFKEGDRHLK EAKACNYWPK GRGIFHNKNK TFLVWVNEED HLRLISMQKG SDVGEVLDRL
NRGIQLLQSK LSFAHDDRLG WLTFCPTNLG STIRASVHIK LPKLSKRDDF KEICEKLNLQ
ARGVHGEHSK SEGGVYDISN KNRLGITEYE AVKQMYDGVK ELIRLEEQEK
//