ID   KCRM_TORCA              Reviewed;         381 AA.
AC   P04414;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   04-NOV-2008, entry version 60.
DE   RecName: Full=Creatine kinase M-type;
DE            EC=2.7.3.2;
DE   AltName: Full=Creatine kinase M chain;
DE   AltName: Full=M-CK;
OS   Torpedo californica (Pacific electric ray).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Elasmobranchii; Squalea; Hypnosqualea; Pristiorajea; Batoidea;
OC   Torpediniformes; Torpedinoidei; Torpedinidae; Torpedo.
OX   NCBI_TaxID=7787;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Electric organ;
RX   MEDLINE=85063721; PubMed=6594677;
RA   West B.L., Babbitt P.C., Mendez B., Baxter J.D.;
RT   "Creatine kinase protein sequence encoded by a cDNA made from Torpedo
RT   californica electric organ mRNA.";
RL   Proc. Natl. Acad. Sci. U.S.A. 81:7007-7011(1984).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH ATP ANALOG, AND
RP   SUBUNIT.
RX   PubMed=12437342; DOI=10.1021/bi026655p;
RA   Lahiri S.D., Wang P.-F., Babbitt P.C., McLeish M.J., Kenyon G.L.,
RA   Allen K.N.;
RT   "The 2.1 A structure of Torpedo californica creatine kinase complexed
RT   with the ADP-Mg(2+)-NO(3)(-)-creatine transition-state analogue
RT   complex.";
RL   Biochemistry 41:13861-13867(2002).
CC   -!- FUNCTION: Reversibly catalyzes the transfer of phosphate between
CC       ATP and various phosphogens (e.g. creatine phosphate). Creatine
CC       kinase isoenzymes play a central role in energy transduction in
CC       tissues with large, fluctuating energy demands, such as skeletal
CC       muscle, heart, brain and spermatozoa.
CC   -!- CATALYTIC ACTIVITY: ATP + creatine = ADP + phosphocreatine.
CC   -!- SUBUNIT: Dimer of identical or non-identical chains. With MM being
CC       the major form in skeletal muscle and myocardium, MB existing in
CC       myocardium, and BB existing in many tissues, especially brain.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- MISCELLANEOUS: This electric ray muscle-specific creatine kinase
CC       (MM isozyme) is isolated from the electric organ, which derives
CC       embryologically from skeletal muscle. It may be involved in the
CC       electrical discharge process.
CC   -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
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DR   EMBL; M36427; AAA49278.1; -; mRNA.
DR   PIR; A00677; KIRYCT.
DR   PDB; 1VRP; X-ray; 2.10 A; A/B=1-381.
DR   PDBsum; 1VRP; -.
DR   HOVERGEN; P04414; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004111; F:creatine kinase activity; IEA:EC.
DR   InterPro; IPR000749; ATP-gua_Ptrans.
DR   InterPro; IPR014746; Gln_synth/guanido_kin_cat.
DR   Gene3D; G3DSA:1.10.135.10; ATP-gua_Ptrans; 1.
DR   Gene3D; G3DSA:3.30.590.10; ATP-gua_Ptrans; 1.
DR   PANTHER; PTHR11547; ATP-gua_Ptrans; 1.
DR   Pfam; PF00217; ATP-gua_Ptrans; 1.
DR   Pfam; PF02807; ATP-gua_PtransN; 1.
DR   PROSITE; PS00112; GUANIDO_KINASE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding;
KW   Transferase.
FT   CHAIN         1    381       Creatine kinase M-type.
FT                                /FTId=PRO_0000211981.
FT   NP_BIND     128    132       ATP.
FT   NP_BIND     320    325       ATP.
FT   BINDING     191    191       ATP (By similarity).
FT   BINDING     236    236       ATP (By similarity).
FT   BINDING     292    292       ATP.
FT   BINDING     335    335       ATP.
FT   HELIX        16     19
FT   HELIX        29     33
FT   HELIX        36     42
FT   HELIX        53     62
FT   STRAND       67     69
FT   HELIX        81     84
FT   HELIX        86     96
FT   HELIX       112    114
FT   TURN        123    125
FT   STRAND      126    135
FT   TURN        143    145
FT   HELIX       148    162
FT   HELIX       167    169
FT   STRAND      171    175
FT   HELIX       176    178
FT   HELIX       181    189
FT   HELIX       200    203
FT   TURN        204    214
FT   STRAND      216    220
FT   STRAND      223    244
FT   HELIX       246    266
FT   TURN        275    277
FT   HELIX       284    286
FT   STRAND      292    298
FT   HELIX       302    304
FT   HELIX       308    315
FT   STRAND      317    321
FT   STRAND      324    329
FT   STRAND      333    338
FT   STRAND      342    344
FT   HELIX       346    368
FT   HELIX       374    376
SQ   SEQUENCE   381 AA;  42934 MW;  DF4A54FDDF3BD570 CRC64;
     MPFGNTHNKW KLNYSAAEEF PDLSKHNNHM AKALTLDIYK KLRDKETPSG FTLDDIIQTG
     VDNPGHPFIM TVGCVAGDEE CYEVFKDLFD PVIEDRHGGY KPTDKHKTDL NQENLKGGDD
     LDPNYVLSSR VRTGRSIKGI ALPPHCSRGE RRLVEKLCID GLATLTGEFQ GKYYPLSSMS
     DAEQQQLIDD HFLFDKPISP LLLASGMARD WPDGRGIWHN NDKTFLVWVN EEDHLRVISM
     QKGGNMKEVF RRFCVGLKKI EDIFVKAGRG FMWNEHLGYV LTCPSNLGTG LRGGVHVKIP
     HLCKHEKFSE VLKRTRLQKR GTGGVDTAAV GSIYDISNAD RLGFSEVEQV QMVVDGVKLM
     VEMEKRLENG KSIDDLMPAQ K
//