ID E4X1N9_OIKDI Unreviewed; 349 AA.
AC E4X1N9;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=creatine kinase {ECO:0000256|ARBA:ARBA00012231};
DE EC=2.7.3.2 {ECO:0000256|ARBA:ARBA00012231};
GN ORFNames=GSOID_T00015788001 {ECO:0000313|EMBL:CBY23356.1};
OS Oikopleura dioica (Tunicate).
OC Eukaryota; Metazoa; Chordata; Tunicata; Appendicularia; Copelata;
OC Oikopleuridae; Oikopleura.
OX NCBI_TaxID=34765 {ECO:0000313|EMBL:CBY23356.1};
RN [1] {ECO:0000313|EMBL:CBY23356.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21097902; DOI=10.1126/science.1194167;
RA Denoeud F., Henriet S., Mungpakdee S., Aury J.M., Da Silva C.,
RA Brinkmann H., Mikhaleva J., Olsen L.C., Jubin C., Canestro C.,
RA Bouquet J.M., Danks G., Poulain J., Campsteijn C., Adamski M., Cross I.,
RA Yadetie F., Muffato M., Louis A., Butcher S., Tsagkogeorga G., Konrad A.,
RA Singh S., Jensen M.F., Cong E.H., Eikeseth-Otteraa H., Noel B.,
RA Anthouard V., Porcel B.M., Kachouri-Lafond R., Nishino A., Ugolini M.,
RA Chourrout P., Nishida H., Aasland R., Huzurbazar S., Westhof E., Delsuc F.,
RA Lehrach H., Reinhardt R., Weissenbach J., Roy S.W., Artiguenave F.,
RA Postlethwait J.H., Manak J.R., Thompson E.M., Jaillon O., Du Pasquier L.,
RA Boudinot P., Liberles D.A., Volff J.N., Philippe H., Lenhard B.,
RA Roest Crollius H., Wincker P., Chourrout D.;
RT "Plasticity of animal genome architecture unmasked by rapid evolution of a
RT pelagic tunicate.";
RL Science 330:1381-1385(2010).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + creatine = ADP + H(+) + N-phosphocreatine;
CC Xref=Rhea:RHEA:17157, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57947, ChEBI:CHEBI:58092, ChEBI:CHEBI:456216; EC=2.7.3.2;
CC Evidence={ECO:0000256|ARBA:ARBA00036020};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17158;
CC Evidence={ECO:0000256|ARBA:ARBA00036020};
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; FN653021; CBY23356.1; -; Genomic_DNA.
DR AlphaFoldDB; E4X1N9; -.
DR InParanoid; E4X1N9; -.
DR Proteomes; UP000001307; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004111; F:creatine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046314; P:phosphocreatine biosynthetic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00716; creatine_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; ARGININE OR CREATINE KINASE; 1.
DR PANTHER; PTHR11547:SF23; CREATINE KINASE B-TYPE; 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:UP000001307};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU00843}.
FT DOMAIN 1..65
FT /note="Phosphagen kinase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51509"
FT DOMAIN 91..333
FT /note="Phosphagen kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51510"
FT BINDING 94..98
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT BINDING 157
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT BINDING 202
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT BINDING 258..262
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT BINDING 286..291
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
SQ SEQUENCE 349 AA; 39067 MW; 7D0EA1566FB57999 CRC64;
MTPELYKRMR ARQTKSGFTI DDAIQTGVDN PGHPFIMTVG CVAGDEDSYE AFAEFFDQII
ESRHGGYKAT DTHKTDLSDG LVMEEPFDPD YVFSVRVRTG RSIRGYALPP WCSRAERRKV
ESISLGALDR FDGDLKGKYF PLYEMTDAAQ EQLIADHFLF DKPVSPLLTS AGMARDWPDA
RGIWHNDQKN FLVWINEEDH LRVISMQKDG DMQACWKRWI DGLNKFEAYV KEAGADFMHS
EHLGYILTCP SNLGTGVRAG VHMKLEKLSE HAKFDDLLGK LRLQKRGTGG VDTASEGGMF
DISNADRLGF SELELVQMLV DGVNALIAIE KKLQAGENAD SDISAVAQK
//
