ID A7RQU9_NEMVE Unreviewed; 376 AA. AC A7RQU9; DT 02-OCT-2007, integrated into UniProtKB/TrEMBL. DT 02-OCT-2007, sequence version 1. DT 24-JAN-2024, entry version 95. DE SubName: Full=Cytoplasmic creatine kinase protein {ECO:0000313|EMBL:BAL73226.1}; GN Name=cytoplasmic creatine kinase {ECO:0000313|EMBL:BAL73226.1}; GN ORFNames=NEMVEDRAFT_v1g234345 {ECO:0000313|EMBL:EDO46231.1}; OS Nematostella vectensis (Starlet sea anemone). OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria; OC Edwardsiidae; Nematostella. OX NCBI_TaxID=45351 {ECO:0000313|EMBL:EDO46231.1, ECO:0000313|Proteomes:UP000001593}; RN [1] {ECO:0000313|EMBL:EDO46231.1, ECO:0000313|Proteomes:UP000001593} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CH2 X CH6 {ECO:0000313|Proteomes:UP000001593}, and CH2 x CH6 RC {ECO:0000313|EMBL:EDO46231.1}; RX PubMed=17615350; DOI=10.1126/science.1139158; RA Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., Salamov A., RA Terry A., Shapiro H., Lindquist E., Kapitonov V.V., Jurka J., RA Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., Finnerty J.R., RA Technau U., Martindale M.Q., Rokhsar D.S.; RT "Sea anemone genome reveals ancestral eumetazoan gene repertoire and RT genomic organization."; RL Science 317:86-94(2007). RN [2] {ECO:0000313|EMBL:BAL73226.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=22305986; DOI=10.1016/j.gene.2012.01.036; RA Uda K., Ellington W.R., Suzuki T.; RT "A diverse array of creatine kinase and arginine kinase isoform genes is RT present in the starlet sea anemone Nematostella vectensis, a cnidarian RT model system for studying developmental evolution."; RL Gene 497:214-227(2012). CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + creatine = ADP + H(+) + N-phosphocreatine; CC Xref=Rhea:RHEA:17157, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:57947, ChEBI:CHEBI:58092, ChEBI:CHEBI:456216; EC=2.7.3.2; CC Evidence={ECO:0000256|ARBA:ARBA00036020}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17158; CC Evidence={ECO:0000256|ARBA:ARBA00036020}; CC -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family. CC {ECO:0000256|ARBA:ARBA00006798, ECO:0000256|PROSITE-ProRule:PRU00842, CC ECO:0000256|RuleBase:RU000505}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB665525; BAL73226.1; -; mRNA. DR EMBL; DS469529; EDO46231.1; -; Genomic_DNA. DR RefSeq; XP_001638294.1; XM_001638244.1. DR AlphaFoldDB; A7RQU9; -. DR STRING; 45351.A7RQU9; -. DR EnsemblMetazoa; EDO46231; EDO46231; NEMVEDRAFT_v1g234345. DR GeneID; 5518278; -. DR KEGG; nve:5518278; -. DR eggNOG; KOG3581; Eukaryota. DR HOGENOM; CLU_019868_4_2_1; -. DR InParanoid; A7RQU9; -. DR OMA; PAIYEQL; -. DR OrthoDB; 35839at2759; -. DR Proteomes; UP000001593; Unassembled WGS sequence. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004111; F:creatine kinase activity; IBA:GO_Central. DR GO; GO:0046314; P:phosphocreatine biosynthetic process; IBA:GO_Central. 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:SF23; CREATINE KINASE B-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}; Reference proteome {ECO:0000313|Proteomes:UP000001593}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE- KW ProRule:PRU00843}. FT DOMAIN 9..95 FT /note="Phosphagen kinase N-terminal" FT /evidence="ECO:0000259|PROSITE:PS51509" FT DOMAIN 121..364 FT /note="Phosphagen kinase C-terminal" FT /evidence="ECO:0000259|PROSITE:PS51510" FT BINDING 124..128 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843" FT BINDING 187 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843" FT BINDING 232 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843" FT BINDING 288..292 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843" FT BINDING 317..322 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843" SQ SEQUENCE 376 AA; 42117 MW; D5933E6281037882 CRC64; MTSVKSAYKQ FSADDDFPDL SQHNNYMAKV LTKEIYRSLR DKSTKNGFTL DDIIQTGVDN PGHPFIMTVG CVAGDEESYD VFAELLDPVI ELRHGGYKKT DKHKTDLNPD NLKGGALDPK YVLSSRVRTG RSIRGFCLPP HCSRAERRSV EKISVDALAK LDGEFKGKYY PLNKMTDEEQ EQLINDHFLF DKPVSPLLTC AGMARDWPDA RGIWHNENKN FLVWVNEEDH TRVISMEKGG DMRAVFTRFC NGLNKVESLI KEAGYEFMWN EHLGYVLTCP SNLGTGLRAG VHLKIPLLSQ DEKRLDAILA KLKLQKRGTG GVDTASVGGV YDISNADRIG FSEVELVQGM VDGVGLLIEM EKRLEEGKAI DDLIPK //