ID A0A074ZN93_9TREM Unreviewed; 655 AA.
AC A0A074ZN93;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 13-SEP-2023, entry version 38.
DE RecName: Full=Arginine kinase {ECO:0008006|Google:ProtNLM};
GN ORFNames=T265_07596 {ECO:0000313|EMBL:KER24810.1};
OS Opisthorchis viverrini.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Opisthorchiida; Opisthorchiata; Opisthorchiidae; Opisthorchis.
OX NCBI_TaxID=6198 {ECO:0000313|EMBL:KER24810.1, ECO:0000313|Proteomes:UP000054324};
RN [1] {ECO:0000313|EMBL:KER24810.1, ECO:0000313|Proteomes:UP000054324}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Young N.D., Nagarajan N., Lin S.J., Korhonen P.K., Jex A.R., Hall R.S.,
RA Safavi-Hemami H., Kaewkong W., Bertrand D., Gao S., Seet Q., Wongkham S.,
RA Teh B.T., Wongkham C., Intapan P.M., Maleewong W., Yang X., Hu M., Wang Z.,
RA Hofmann A., Sternberg P.W., Tan P., Wang J., Gasser R.B.;
RT "Opisthorchis viverrini - life in the bile duct.";
RL Submitted (NOV-2013) 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,
CC ECO:0000256|RuleBase:RU000505}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00843}.
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DR EMBL; KL596796; KER24810.1; -; Genomic_DNA.
DR RefSeq; XP_009171424.1; XM_009173160.1.
DR AlphaFoldDB; A0A074ZN93; -.
DR STRING; 6198.A0A074ZN93; -.
DR GeneID; 20321775; -.
DR KEGG; ovi:T265_07596; -.
DR CTD; 20321775; -.
DR OrthoDB; 35839at2759; -.
DR Proteomes; UP000054324; Unassembled WGS sequence.
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; 2.
DR Gene3D; 3.30.590.10; Glutamine synthetase/guanido kinase, catalytic domain; 2.
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; 2.
DR Pfam; PF02807; ATP-gua_PtransN; 2.
DR SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 2.
DR SUPFAM; SSF48034; Guanido kinase N-terminal domain; 2.
DR PROSITE; PS00112; PHOSPHAGEN_KINASE; 2.
DR PROSITE; PS51510; PHOSPHAGEN_KINASE_C; 2.
DR PROSITE; PS51509; PHOSPHAGEN_KINASE_N; 2.
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:UP000054324};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU00843}.
FT DOMAIN 5..86
FT /note="Phosphagen kinase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51509"
FT DOMAIN 86..290
FT /note="Phosphagen kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51510"
FT DOMAIN 306..387
FT /note="Phosphagen kinase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51509"
FT DOMAIN 417..654
FT /note="Phosphagen kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51510"
FT BINDING 120
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT BINDING 164
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT BINDING 215..219
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT BINDING 243..248
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT BINDING 420..424
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT BINDING 483
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT BINDING 527
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT BINDING 578..582
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT BINDING 607..612
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
SQ SEQUENCE 655 AA; 73488 MW; 260411564F30F4D3 CRC64;
MQVEPLKSLQ QKIINDEANR SFTKKHLTNR IVDQYADKKT SFGGSLAQCV SHNARNPRCI
LPRACDLDAY EAFREFFDAV IIDYHKISTA LKNLTGEYKG TYYPLTGMKE EDRKKLVEKH
FLFRDDDSVL RDAGGYIDWP NGRGIFINDK ENFLVWINEE DHIRVISMQK GGDLIAVYKR
LANAISELGK TLTFATSDRF GFITFCPSNL GTTLRASVHA RVPYLSALPN FEQICEKYNI
QARGTHGEHT ASVGGVYDLS NKRRLGLTEI EAVTEMYNGV QALLDLEKQL ADYNKDAPAG
VMPVEPLPYL SRLLEAADPV KNYTRKHLTP EVIKKYDGVR TTHGATVAHM VRNGAYNPHS
ICPRTGEAEC YTKFVDYLDA VILDYHGVND PAFKHPPPTF GDLNNLPFGD VDPEGKFVVS
TRVRVGRSVD GFLFSTIMSK QDRLDLETKV STALKSLTGE HAGSYHPLAN MSEATRKQLV
EDHFLFKNDD PVLRDAGGYR DWPHGRGIFH NANKTFLVWL CEEDHMRIIS MQKGGDLAAV
YKRLIQGIQA IEKTLPFAHS DKYGYITCCP SNLGTTMRAS VLLKIPKLSA QKAKLDEVCA
KYRLQARGLH GEHTESPEGI HDISNKRRLG LTELEAAKEM ADGVAQMIAI EKSLP
//
