ID KARG_ANTJA Reviewed; 715 AA.
AC O15992;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 22-FEB-2023, entry version 78.
DE RecName: Full=Arginine kinase;
DE Short=AK;
DE EC=2.7.3.3;
OS Anthopleura japonica (Sea anemone).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Actiniidae; Anthopleura.
OX NCBI_TaxID=67755;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=9359868; DOI=10.1042/bj3280301;
RA Suzuki T., Kawasaki Y., Furukohri T.;
RT "Evolution of phosphagen kinase. Isolation, characterization and cDNA-
RT derived amino acid sequence of two-domain arginine kinase from the sea
RT anemone Anthopleura japonicus.";
RL Biochem. J. 328:301-306(1997).
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 -!- SUBUNIT: Monomer.
CC -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
CC {ECO:0000255|PROSITE-ProRule:PRU00842, ECO:0000255|PROSITE-
CC ProRule:PRU00843}.
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DR EMBL; AB008014; BAA22888.1; -; mRNA.
DR PDB; 4RF6; X-ray; 1.95 A; A/B=1-715.
DR PDB; 4RF7; X-ray; 2.10 A; A/B=1-715.
DR PDB; 4RF8; X-ray; 2.17 A; A/B=1-715.
DR PDB; 4RF9; X-ray; 2.35 A; A/B=1-715.
DR PDBsum; 4RF6; -.
DR PDBsum; 4RF7; -.
DR PDBsum; 4RF8; -.
DR PDBsum; 4RF9; -.
DR AlphaFoldDB; O15992; -.
DR SMR; O15992; -.
DR BRENDA; 2.7.3.3; 370.
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 CDD; cd07931; eukaryotic_phosphagen_kinases; 2.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Direct protein sequencing; Kinase;
KW Nucleotide-binding; Repeat; Transferase.
FT CHAIN 1..715
FT /note="Arginine kinase"
FT /id="PRO_0000212007"
FT REPEAT 1..366
FT /note="Approximate"
FT DOMAIN 11..95
FT /note="Phosphagen kinase N-terminal 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00842"
FT DOMAIN 123..362
FT /note="Phosphagen kinase C-terminal 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT DOMAIN 365..447
FT /note="Phosphagen kinase N-terminal 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00842"
FT REPEAT 367..715
FT /note="Approximate"
FT DOMAIN 475..714
FT /note="Phosphagen kinase C-terminal 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 68..72
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 126..130
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 189
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 229
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 233
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 275
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 284..288
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 312..317
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 317
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT HELIX 4..11
FT /evidence="ECO:0007829|PDB:4RF6"
FT TURN 12..14
FT /evidence="ECO:0007829|PDB:4RF6"
FT HELIX 18..21
FT /evidence="ECO:0007829|PDB:4RF6"
FT HELIX 30..34
FT /evidence="ECO:0007829|PDB:4RF6"
FT HELIX 37..43
FT /evidence="ECO:0007829|PDB:4RF6"
FT HELIX 54..63
FT /evidence="ECO:0007829|PDB:4RF6"
FT HELIX 76..81
FT /evidence="ECO:0007829|PDB:4RF6"
FT HELIX 83..93
FT /evidence="ECO:0007829|PDB:4RF6"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:4RF6"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:4RF6"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:4RF6"
FT STRAND 122..133
FT /evidence="ECO:0007829|PDB:4RF6"
FT TURN 141..143
FT /evidence="ECO:0007829|PDB:4RF6"
FT HELIX 146..160
FT /evidence="ECO:0007829|PDB:4RF6"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:4RF6"
FT STRAND 169..174
FT /evidence="ECO:0007829|PDB:4RF6"
FT HELIX 179..187
FT /evidence="ECO:0007829|PDB:4RF6"
FT HELIX 197..201
FT /evidence="ECO:0007829|PDB:4RF6"
FT TURN 202..211
FT /evidence="ECO:0007829|PDB:4RF6"
FT STRAND 213..217
FT /evidence="ECO:0007829|PDB:4RF6"
FT STRAND 222..241
FT /evidence="ECO:0007829|PDB:4RF6"
FT HELIX 243..261
FT /evidence="ECO:0007829|PDB:4RF6"
FT TURN 267..269
FT /evidence="ECO:0007829|PDB:4RF6"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:4RF6"
FT STRAND 283..290
FT /evidence="ECO:0007829|PDB:4RF6"
FT HELIX 292..295
FT /evidence="ECO:0007829|PDB:4RF6"
FT HELIX 300..307
FT /evidence="ECO:0007829|PDB:4RF6"
FT STRAND 309..313
FT /evidence="ECO:0007829|PDB:4RF6"
FT STRAND 315..318
FT /evidence="ECO:0007829|PDB:4RF6"
FT STRAND 320..323
FT /evidence="ECO:0007829|PDB:4RF6"
FT STRAND 328..333
FT /evidence="ECO:0007829|PDB:4RF6"
FT STRAND 337..339
FT /evidence="ECO:0007829|PDB:4RF6"
FT HELIX 341..367
FT /evidence="ECO:0007829|PDB:4RF6"
FT HELIX 372..375
FT /evidence="ECO:0007829|PDB:4RF6"
FT HELIX 382..386
FT /evidence="ECO:0007829|PDB:4RF6"
FT HELIX 389..395
FT /evidence="ECO:0007829|PDB:4RF6"
FT HELIX 406..415
FT /evidence="ECO:0007829|PDB:4RF6"
FT HELIX 430..433
FT /evidence="ECO:0007829|PDB:4RF6"
FT HELIX 435..445
FT /evidence="ECO:0007829|PDB:4RF6"
FT TURN 446..448
FT /evidence="ECO:0007829|PDB:4RF6"
FT HELIX 451..453
FT /evidence="ECO:0007829|PDB:4RF6"
FT HELIX 461..463
FT /evidence="ECO:0007829|PDB:4RF6"
FT STRAND 474..485
FT /evidence="ECO:0007829|PDB:4RF6"
FT HELIX 493..495
FT /evidence="ECO:0007829|PDB:4RF6"
FT HELIX 498..513
FT /evidence="ECO:0007829|PDB:4RF6"
FT HELIX 517..519
FT /evidence="ECO:0007829|PDB:4RF6"
FT STRAND 521..526
FT /evidence="ECO:0007829|PDB:4RF6"
FT HELIX 531..539
FT /evidence="ECO:0007829|PDB:4RF6"
FT HELIX 549..554
FT /evidence="ECO:0007829|PDB:4RF6"
FT TURN 555..563
FT /evidence="ECO:0007829|PDB:4RF6"
FT STRAND 565..569
FT /evidence="ECO:0007829|PDB:4RF6"
FT STRAND 574..593
FT /evidence="ECO:0007829|PDB:4RF6"
FT HELIX 595..613
FT /evidence="ECO:0007829|PDB:4RF6"
FT TURN 619..621
FT /evidence="ECO:0007829|PDB:4RF6"
FT HELIX 628..630
FT /evidence="ECO:0007829|PDB:4RF6"
FT STRAND 635..642
FT /evidence="ECO:0007829|PDB:4RF6"
FT HELIX 644..648
FT /evidence="ECO:0007829|PDB:4RF6"
FT HELIX 652..658
FT /evidence="ECO:0007829|PDB:4RF6"
FT STRAND 661..665
FT /evidence="ECO:0007829|PDB:4RF6"
FT STRAND 679..685
FT /evidence="ECO:0007829|PDB:4RF6"
FT STRAND 689..691
FT /evidence="ECO:0007829|PDB:4RF6"
FT HELIX 693..711
FT /evidence="ECO:0007829|PDB:4RF6"
SQ SEQUENCE 715 AA; 80024 MW; C8E756E726CEDA48 CRC64;
MADPETAAKF KSKNAFPDPL NDPKCNPKSL VKKYLTPKVF ESLKNKKTKL GITLWDCINS
GVVNLDSGVG VYAGDEESYT LFGPLFDAII EDYHSPYKLA TGHNSDMNPA HVKAPDLDPA
NRYIRSTRIR VARSLKGYGL APGVTKAHRL EIEKKVVGVL TSLTGDLAGK YYPLSGMDEK
TRQQLVDDHF LFKKGDRFLE AAGINKEWPE GRGIYHNNDK TFLVWLNEED HLRIISMEKG
SDIGSVFSRL CRAVNEIDKK LGFQHTKKHG YLTSCPSNLG TGMRASVHVK IPHAKEHPDF
ENILTKYHIQ ARGIHGEHSE STGEDAGVYD ISNRRRLGLS EVQCVQDMYD GVKALMELEK
EAIAKKRSVF PEVLKNPEVK SLLRKYLTPE LFDSLKDKKT AKGISLYDCI NSGVENLDSS
CGVYAGDEEC YTLFAPLFDK IVEDYHSPYK LANKHTSDMN PEKVDAPNLD PEGTYIRSTR
IRVARNVKGY ALTPGLTRNE RLDIERKVVG VLSSLTGDLA GQYYPLTGMD EATRQKLVND
HFLFKKGDRF LEAAGVNKLW PEGRGIFHNN DKTFLVWINE EDQLRIISME KGSDIGSVFG
RLCRAVNEID KQLGFQHTDA HGYLSGCPTN LGTGMRASVH VKIPKASAHP DFQKICDEFH
IQARGIHGEH SVSTGEDAGV FDISNRRRLG LSEVQCVQDM YNGVKKLLEI EKSTK
//
