ID H2D0J5_9ORTH Unreviewed; 391 AA.
AC H2D0J5;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 22-FEB-2023, entry version 36.
DE RecName: Full=arginine kinase {ECO:0000256|ARBA:ARBA00012230};
DE EC=2.7.3.3 {ECO:0000256|ARBA:ARBA00012230};
DE Flags: Fragment;
OS Allonemobius socius.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Polyneoptera; Orthoptera; Ensifera; Gryllidea; Grylloidea;
OC Gryllidae; Nemobiinae; Allonemobius; Allonemobius socius complex.
OX NCBI_TaxID=208665 {ECO:0000313|EMBL:AEX96983.1};
RN [1] {ECO:0000313|EMBL:AEX96983.1}
RP NUCLEOTIDE SEQUENCE.
RA Noh S., Garcia C., Howard D.J., Marshall J.L.;
RT "Gene genealogies and fixed nonsynonymous substitutions point to putative
RT speciation genes during ongoing speciation: a case study from Allonemobius
RT crickets.";
RL Submitted (JUL-2011) 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}.
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DR EMBL; JN393664; AEX96980.1; -; mRNA.
DR EMBL; JN393665; AEX96981.1; -; mRNA.
DR EMBL; JN393667; AEX96983.1; -; mRNA.
DR EMBL; JN393668; AEX96984.1; -; mRNA.
DR EMBL; JN393670; AEX96986.1; -; mRNA.
DR EMBL; JN393671; AEX96987.1; -; mRNA.
DR AlphaFoldDB; H2D0J5; -.
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 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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00843};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU00843}.
FT DOMAIN 51..136
FT /note="Phosphagen kinase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51509"
FT DOMAIN 164..391
FT /note="Phosphagen kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51510"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 167..171
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT BINDING 230
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT BINDING 274
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT BINDING 325..329
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"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AEX96983.1"
FT NON_TER 391
FT /evidence="ECO:0000313|EMBL:AEX96983.1"
SQ SEQUENCE 391 AA; 43558 MW; 309E62B10A0B6FF5 CRC64;
KEFASMSQLP QCPPRPNEPQ ICCKLQPGEQ PCCEMGPGGG SAGSGKPVPP DVKAKIEEAF
QKLEKQESKS LLKKYLTRDV FNKLKDRVTP DGSTLLDVIQ SGVENPDSGV GIYAPDADAY
SVYAELFDPV ISDYHIGFKP TDTHPNLEWG DFSTLKDLDP DGKYIKSTRV RCGRSIKGYP
FNPRMTMEYY LQMEKDAQQA FSKLDGVHAG KYESLASMTP DRQKKLIDDH FLFKEGDRFL
QAGKACQFWP KGRGIFLNPT NTFMVWVGEE DHLRIISMQM GGDLGAIYKR MVEGVQKLEK
TLTFVRHPRL GYITFCPTNL GTTVRASVMI KLPKIGGDLD SLEAIANRYD LQVRGTAGEH
SVSADGSYDI SNKRRLGLTE YQAVSKCTKV S
//
