ID Q9YI15_CYPCA Unreviewed; 381 AA.
AC Q9YI15;
DT 01-MAY-1999, integrated into UniProtKB/TrEMBL.
DT 01-MAY-1999, sequence version 1.
DT 22-FEB-2023, entry version 84.
DE RecName: Full=creatine kinase {ECO:0000256|ARBA:ARBA00012231};
DE EC=2.7.3.2 {ECO:0000256|ARBA:ARBA00012231};
OS Cyprinus carpio (Common carp).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Cyprininae; Cyprinus.
OX NCBI_TaxID=7962 {ECO:0000313|EMBL:AAC96093.1};
RN [1] {ECO:0000313|EMBL:AAC96093.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Striated muscle {ECO:0000313|EMBL:AAC96093.1};
RX PubMed=9837966; DOI=10.1074/jbc.273.50.33774;
RA Sun H.W., Hui C.F., Wu J.L.;
RT "Cloning, characterization, and expression in Escherichia coli of three
RT creatine kinase muscle isoenzyme cDNAs from carp (Cyprinus carpio) striated
RT muscle.";
RL J. Biol. Chem. 273:33774-33780(1998).
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; AF055289; AAC96093.1; -; mRNA.
DR AlphaFoldDB; Q9YI15; -.
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:SF62; 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 11..98
FT /note="Phosphagen kinase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51509"
FT DOMAIN 125..367
FT /note="Phosphagen kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51510"
FT BINDING 128..132
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT BINDING 191
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT BINDING 236
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT BINDING 292..296
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT BINDING 320..325
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
SQ SEQUENCE 381 AA; 42928 MW; DFC14F9FB7CD7E5A CRC64;
MPFGNTHNNF KLNYSVDEEY PDLTKHNNHM AKVLTKEMYG KLRDKQTPTG FTVDDVIQTG
VDNPGHPFIM TVGCVAGDEE SYEVFKDLLD PVISDRHNGY KATDKHKTDL NFENLKGGDD
LDPNYVLSSR VRTGRSIKGY ALPPHNSRGE RRAVEKLSVE ALNSLDGEFK GKYYPLKSMT
DAEQEQLIAD HFLFDKPVSP LLLAAGMARD WPDARGIWHN ENKTFLVWVN EEDHLRVISM
QQGGNMKEVF KRFCVGLQRI EEIFKKHNHG FMWNEHLGFI LTCPSNLGTG LRGGVHVKLP
KLSTHPKFEE ILTRLRLLKR GTGGVDTASV GGVFDISNAD RIGSSEVEQV QCVVDGVKLM
IEMEKKLEKG ESIDSMIPAQ K
//
