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Database: UniProt
Entry: H9ZVS9_PROAN
LinkDB: H9ZVS9_PROAN
Original site: H9ZVS9_PROAN 
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
//
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