ID H9ZVS9_PROAN Unreviewed; 381 AA.
AC H9ZVS9;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Creatine kinase M-type {ECO:0000256|ARBA:ARBA00040658};
DE EC=2.7.3.2 {ECO:0000256|ARBA:ARBA00012231};
DE AltName: Full=Creatine kinase M chain {ECO:0000256|ARBA:ARBA00042004};
DE AltName: Full=Creatine phosphokinase M-type {ECO:0000256|ARBA:ARBA00042833};
DE AltName: Full=M-CK {ECO:0000256|ARBA:ARBA00041807};
DE Flags: Fragment;
GN Name=ckm {ECO:0000313|EMBL:AFH40439.1};
OS Protopterus annectens (African lungfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Dipnomorpha; Ceratodontiformes; Lepidosirenoidei; Protopteridae;
OC Protopterus.
OX NCBI_TaxID=7888 {ECO:0000313|EMBL:AFH40439.1};
RN [1] {ECO:0000313|EMBL:AFH40439.1}
RP NUCLEOTIDE SEQUENCE.
RA Loong A.M., Ip Y.K.;
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Dimer of identical or non-identical chains, which can be
CC either B (brain type) or M (muscle type). With MM being the major form
CC in skeletal muscle and myocardium, MB existing in myocardium, and BB
CC existing in many tissues, especially brain.
CC {ECO:0000256|ARBA:ARBA00038548}.
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; JN674454; AFH40439.1; -; mRNA.
DR AlphaFoldDB; H9ZVS9; -.
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:SF63; CREATINE KINASE M-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 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"
FT NON_TER 381
FT /evidence="ECO:0000313|EMBL:AFH40439.1"
SQ SEQUENCE 381 AA; 42677 MW; 95A8547FF485EBE9 CRC64;
MPFGNTHNKF KMNYSAEEEF PDLSQHNNHM AKALTLDIYK RLRDKETPSG FTLDDIIQTG
VDNPGHPFIM TVGCVAGDEE SYEVFKDLLD PVIEDRHGGY KATDKHRTDL NPANLKGGDD
LDPNYVISSR VRTGRSIKGY TLPPHCSRGE RRAIEKLSIQ ALDSLSGDLK GKYYPLKGMS
DAEQQQLIDD HFLLDKPVSP LLLASGMARD WPDARGIWHN DNKTFLVWVN EEDHLRVISM
QKGGNMKEVF TRFCVGLQQI EEIFKKAGHG FMWNEHLGYI LTCPSNLGTG LRGGVHVKIP
HLCKHEKFAE IVKRLRLQTR GTGGVDTGAV GGVYDISNAD RLGSSEVEQV QLVVDGVKLI
IEMEKRLEQG KSIDDLIPAQ K
//