KARG_TRYCR
ID KARG_TRYCR Reviewed; 357 AA.
AC O96507;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Arginine kinase;
DE Short=AK;
DE EC=2.7.3.3;
OS Trypanosoma cruzi.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX NCBI_TaxID=5693;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND COFACTOR.
RC STRAIN=Tulahuen 2;
RX PubMed=10625703; DOI=10.1074/jbc.275.2.1495;
RA Pereira C.A., Alonso G.D., Paveto M.C., Iribarren A., Cabanas M.L.,
RA Torres H.N., Flawia M.M.;
RT "Trypanosoma cruzi arginine kinase characterization and cloning. A novel
RT energetic pathway in protozoan parasites.";
RL J. Biol. Chem. 275:1495-1501(2000).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX PubMed=17623863; DOI=10.1002/prot.21557;
RA Fernandez P., Haouz A., Pereira C.A., Aguilar C., Alzari P.M.;
RT "The crystal structure of Trypanosoma cruzi arginine kinase.";
RL Proteins 69:209-212(2007).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-arginine = ADP + H(+) + N(omega)-phospho-L-arginine;
CC Xref=Rhea:RHEA:22940, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:32682, ChEBI:CHEBI:58477, ChEBI:CHEBI:456216; EC=2.7.3.3;
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000269|PubMed:10625703};
CC -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
CC {ECO:0000255|PROSITE-ProRule:PRU00842, ECO:0000255|PROSITE-
CC ProRule:PRU00843}.
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; AF070451; AAC82390.1; -; Genomic_DNA.
DR PDB; 2J1Q; X-ray; 1.90 A; A=1-357.
DR PDBsum; 2J1Q; -.
DR AlphaFoldDB; O96507; -.
DR SMR; O96507; -.
DR VEuPathDB; TriTrypDB:BCY84_02037; -.
DR VEuPathDB; TriTrypDB:C3747_193g73; -.
DR VEuPathDB; TriTrypDB:C4B63_26g286; -.
DR VEuPathDB; TriTrypDB:Tc_MARK_5822; -.
DR VEuPathDB; TriTrypDB:TcBrA4_0118800; -.
DR VEuPathDB; TriTrypDB:TcCL_Unassigned02657; -.
DR VEuPathDB; TriTrypDB:TcCLB.482369.29; -.
DR VEuPathDB; TriTrypDB:TcCLB.507241.30; -.
DR VEuPathDB; TriTrypDB:TCDM_03088; -.
DR VEuPathDB; TriTrypDB:TcG_05313; -.
DR VEuPathDB; TriTrypDB:TCSYLVIO_007077; -.
DR BRENDA; 2.7.3.3; 6524.
DR EvolutionaryTrace; O96507; -.
DR GO; GO:0004054; F:arginine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; -; 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; PTHR11547; 1.
DR Pfam; PF00217; ATP-gua_Ptrans; 1.
DR Pfam; PF02807; ATP-gua_PtransN; 1.
DR SUPFAM; SSF48034; SSF48034; 1.
DR SUPFAM; SSF55931; SSF55931; 1.
DR PROSITE; PS00112; PHOSPHAGEN_KINASE; 1.
DR PROSITE; PS51510; PHOSPHAGEN_KINASE_C; 1.
DR PROSITE; PS51509; PHOSPHAGEN_KINASE_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Kinase; Nucleotide-binding; Transferase.
FT CHAIN 1..357
FT /note="Arginine kinase"
FT /id="PRO_0000211990"
FT DOMAIN 9..91
FT /note="Phosphagen kinase N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00842"
FT DOMAIN 119..356
FT /note="Phosphagen kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 64..68
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 122..126
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 185
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 225
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 229
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 271
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 280..284
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 309..314
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 314
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT HELIX 4..19
FT /evidence="ECO:0007829|PDB:2J1Q"
FT HELIX 26..30
FT /evidence="ECO:0007829|PDB:2J1Q"
FT HELIX 33..39
FT /evidence="ECO:0007829|PDB:2J1Q"
FT HELIX 51..59
FT /evidence="ECO:0007829|PDB:2J1Q"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:2J1Q"
FT HELIX 74..77
FT /evidence="ECO:0007829|PDB:2J1Q"
FT HELIX 79..89
FT /evidence="ECO:0007829|PDB:2J1Q"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:2J1Q"
FT STRAND 117..129
FT /evidence="ECO:0007829|PDB:2J1Q"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:2J1Q"
FT HELIX 142..157
FT /evidence="ECO:0007829|PDB:2J1Q"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:2J1Q"
FT STRAND 165..170
FT /evidence="ECO:0007829|PDB:2J1Q"
FT HELIX 175..183
FT /evidence="ECO:0007829|PDB:2J1Q"
FT HELIX 193..197
FT /evidence="ECO:0007829|PDB:2J1Q"
FT TURN 202..207
FT /evidence="ECO:0007829|PDB:2J1Q"
FT STRAND 209..213
FT /evidence="ECO:0007829|PDB:2J1Q"
FT STRAND 216..238
FT /evidence="ECO:0007829|PDB:2J1Q"
FT HELIX 239..254
FT /evidence="ECO:0007829|PDB:2J1Q"
FT TURN 263..265
FT /evidence="ECO:0007829|PDB:2J1Q"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:2J1Q"
FT STRAND 280..286
FT /evidence="ECO:0007829|PDB:2J1Q"
FT HELIX 297..303
FT /evidence="ECO:0007829|PDB:2J1Q"
FT STRAND 306..309
FT /evidence="ECO:0007829|PDB:2J1Q"
FT STRAND 322..328
FT /evidence="ECO:0007829|PDB:2J1Q"
FT STRAND 331..333
FT /evidence="ECO:0007829|PDB:2J1Q"
FT HELIX 335..353
FT /evidence="ECO:0007829|PDB:2J1Q"
SQ SEQUENCE 357 AA; 40197 MW; CE887C66E53CFCFF CRC64;
MASAEVVSKL EAAFAKLQNA SDCHSLLKKY LTKEVFDQLK GKQTKMGATL MDVIQSGVEN
LDSGIGVYAP DAESYTLFAA LFDPIIEDYH KGFKPSDKQP PKDFGDLNTF IDVDPDKKYV
ISTRVRCGRS LEGYPFNPCL KKQQYEEMES RVKGQLESMS GELRGKYYPL TGMTKETQKQ
LIDDHFLFKE GDRFLQAAHA CKFWPTGRGI YHNDAKTFLV WVNEEDHLRI ISMQKGGNLK
EVFGRLVTAV GVIEEKVKFS RDDRLGFLTF CPTNLGTTIR ASVHIKLPKL GADRKKLEEV
AAKYNLQVRG TAGEHSDSPD GVYDISNKRR LGLSEYEAVK EMQDGILELI KAEESAR
