ID A0A0V1KXK9_9BILA Unreviewed; 401 AA.
AC A0A0V1KXK9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 13-SEP-2023, entry version 27.
DE RecName: Full=arginine kinase {ECO:0000256|ARBA:ARBA00012230};
DE EC=2.7.3.3 {ECO:0000256|ARBA:ARBA00012230};
GN Name=F46H5.3 {ECO:0000313|EMBL:KRZ51889.1};
GN ORFNames=D917_04732 {ECO:0000313|EMBL:OUC39588.1}, T02_6925
GN {ECO:0000313|EMBL:KRZ51889.1};
OS Trichinella nativa.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ51889.1, ECO:0000313|Proteomes:UP000054721};
RN [1] {ECO:0000313|EMBL:OUC39588.1, ECO:0000313|Proteomes:UP000243006}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS45 {ECO:0000313|EMBL:OUC39588.1,
RC ECO:0000313|Proteomes:UP000243006};
RA Mitreva M.;
RT "Draft genome of the roundworm Trichinella nativa.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRZ51889.1, ECO:0000313|Proteomes:UP000054721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS10 {ECO:0000313|EMBL:KRZ51889.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (MAY-2015) 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: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRZ51889.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JYDW01000210; KRZ51889.1; -; Genomic_DNA.
DR EMBL; LVZM01023982; OUC39588.1; -; Genomic_DNA.
DR STRING; 6335.A0A0V1KXK9; -.
DR Proteomes; UP000054721; Unassembled WGS sequence.
DR Proteomes; UP000243006; 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 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}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00843}; Reference proteome {ECO:0000313|Proteomes:UP000054721};
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 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 53..135
FT /note="Phosphagen kinase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51509"
FT DOMAIN 164..401
FT /note="Phosphagen kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51510"
FT BINDING 167..171
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT BINDING 231
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT BINDING 275
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT BINDING 326..330
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT BINDING 354..359
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
SQ SEQUENCE 401 AA; 45657 MW; 254B0C35E66B7A4A CRC64;
MAFSRLSKAS KIVVLTTGGA LLAGIGTFYY RMGDELRKNL LNIETVPKDI QKRCDEAYET
LQNAKDCHSL LKKHLTKSVL DNLKTQKTKM GGTLIDVINS GVKNLDSGIG VYATDPEAYH
VFKKLFDPII ADYHKFNPKD KQPKENFGEN ELNKFENLDP KGKYILSTRI RCGRTLKGYP
FNPLLREDDY LLIEQKMKEA LNSFTDPELQ GKYYSLSGMS ESDKKQLIKD HFLFKEGDRF
LQAAKACQYW PVGRGIFHNN AKTFLVWVNE EDHVRIISMQ QGGDVKAVFS RLIRGVKDIE
KKVSFAKDDR LGNVTFCPTN LGTTIRASVH IKLPKLSTKS DFKEVCEKLN LQVRGIHGEH
SESEGGIYDI SNKRRMGLTE FEAVKEMYDG VKKLIYMEEK A
//
