ID N6U6N6_DENPD Unreviewed; 379 AA.
AC N6U6N6;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=arginine kinase {ECO:0000256|ARBA:ARBA00012230};
DE EC=2.7.3.3 {ECO:0000256|ARBA:ARBA00012230};
DE Flags: Fragment;
GN Name=109540881 {ECO:0000313|EnsemblMetazoa:ENN74227};
GN ORFNames=D910_03558 {ECO:0000313|EMBL:ERL86145.1}, YQE_09200
GN {ECO:0000313|EMBL:ENN74227.1};
OS Dendroctonus ponderosae (Mountain pine beetle).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Curculionidae; Scolytinae; Dendroctonus.
OX NCBI_TaxID=77166 {ECO:0000313|EMBL:ENN74227.1};
RN [1] {ECO:0000313|Proteomes:UP000019118, ECO:0000313|Proteomes:UP000030742}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23537049; DOI=10.1186/gb-2013-14-3-r27;
RA Keeling C.I., Yuen M.M., Liao N.Y., Roderick Docking T., Chan S.K.,
RA Taylor G.A., Palmquist D.L., Jackman S.D., Nguyen A., Li M., Henderson H.,
RA Janes J.K., Zhao Y., Pandoh P., Moore R., Sperling F.A., W Huber D.P.,
RA Birol I., Jones S.J., Bohlmann J.;
RT "Draft genome of the mountain pine beetle, Dendroctonus ponderosae Hopkins,
RT a major forest pest.";
RL Genome Biol. 14:R27-R27(2013).
RN [2] {ECO:0000313|EnsemblMetazoa:ENN74227}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JAN-2017) 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; APGK01047206; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; APGK01047207; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KB741077; ENN74227.1; -; Genomic_DNA.
DR EMBL; KB631792; ERL86145.1; -; Genomic_DNA.
DR RefSeq; XP_019764946.1; XM_019909387.1.
DR AlphaFoldDB; N6U6N6; -.
DR STRING; 77166.N6U6N6; -.
DR EnsemblMetazoa; ENN74227; ENN74227; YQE_09200.
DR GeneID; 109540881; -.
DR KEGG; dpa:109540881; -.
DR HOGENOM; CLU_019868_0_0_1; -.
DR OMA; EYHGFTP; -.
DR OrthoDB; 35839at2759; -.
DR Proteomes; UP000019118; Unassembled WGS sequence.
DR Proteomes; UP000030742; 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; 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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00843}; Reference proteome {ECO:0000313|Proteomes:UP000030742};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU00843}.
FT DOMAIN 30..114
FT /note="Phosphagen kinase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51509"
FT DOMAIN 142..379
FT /note="Phosphagen kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51510"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 145..149
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT BINDING 208
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT BINDING 252
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT BINDING 303..307
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT BINDING 332..337
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ENN74227.1"
SQ SEQUENCE 379 AA; 42560 MW; 4E37BE28550A8B3A CRC64;
MGGCASKENT AKEPKKEDDT GKEAMVDAAV LEKLETGFKK LESTPSNSLL KKYLNKDLFD
SLKTKKTSFG SSLLDVIQSG IENPDSGIGI YAPDAESYTV FADLFDPIIE DYHKGFGRTD
KHPPKNWGDV SVFGNLDPAG EYIVSTRVRC GRSLEGYPFN PCLTEEQYKE MEQKVSTTLS
GLEGELKGTF YPLTGMSKDV QQKLIDDHFL FKEGDRFLQA ANACRFWPSG RGIYHNENKT
FLVWCNEEDH LRIISMQQGG DLGEVYRRLV TAVNDIEKRI PFSHHDRLGF LTFCPTNLGT
TVRASVHIKV PKLAANKAKL EEVASKYNLQ VRGTRGEHTE AEGGIYDISN KRRMGLTEFE
AVKEMYDGIA ELIKIEREL
//
