ID B5MGP6_MOLTE Unreviewed; 406 AA.
AC B5MGP6;
DT 04-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 04-NOV-2008, sequence version 1.
DT 22-FEB-2023, entry version 51.
DE RecName: Full=creatine kinase {ECO:0000256|ARBA:ARBA00012231};
DE EC=2.7.3.2 {ECO:0000256|ARBA:ARBA00012231};
GN Name=CK {ECO:0000313|EMBL:BAG71435.1};
OS Molgula tectiformis (Ascidian).
OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Stolidobranchia;
OC Molgulidae; Molgula.
OX NCBI_TaxID=30286 {ECO:0000313|EMBL:BAG71435.1};
RN [1] {ECO:0000313|EMBL:BAG71435.1}
RP NUCLEOTIDE SEQUENCE.
RA Gyoja F.;
RT "Expression of minor muscle structural genes in urodele ascidian Ciona
RT intestinalis and anural ascidian Molgula tectiformis.";
RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
CC {ECO:0000256|ARBA:ARBA00006798, ECO:0000256|PROSITE-ProRule:PRU00842}.
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DR EMBL; AB458826; BAG71435.1; -; mRNA.
DR AlphaFoldDB; B5MGP6; -.
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; 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:SF57; MITOCHONDRIAL 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; 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}; Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU00843}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..406
FT /note="creatine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002836807"
FT DOMAIN 38..125
FT /note="Phosphagen kinase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51509"
FT DOMAIN 152..394
FT /note="Phosphagen kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51510"
FT BINDING 155..159
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT BINDING 218
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT BINDING 263
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT BINDING 319..323
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT BINDING 347..352
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
SQ SEQUENCE 406 AA; 45399 MW; 4CA3064CB082B9BC CRC64;
MSSILAYSGA LAAAGAVGAF ATLCQKKNVN ARLMPTRKLM YPPSADYPDL SKHHNIMKNH
LTPGVYAKLR DRVTKNGCTL ETCIQTGVDN PGHPYIKIVG MVAGDEECYE EFKEIFNPVI
KERHNGYDPE TMIHPINLDA SQINGGKFDE KYVLSSRVRT GRAIRGIPHP PMCSRAERRE
VEKVTCDALK GLPADLAGTY YSLKSMTDEE QEQLINDHFL FDKPVSPLLT SSGMARDWPD
ARGIFHNDKK NFLVWVNEED HTRIISMDKG GDMKTVFARF CRGINEVERL IGQQGWEFQR
SDNLGYILTC PSNLGNGLRC GVHVKLPKLA TDKRFSEILE KLRLQKRGTG GVDTAAVGGT
FDISNLDRLG KSEVQLVQEV IDGVNLLIDM EKKLEKRQSI NHLIPK
//
