ID Q4AEC6_9ANNE Unreviewed; 365 AA.
AC Q4AEC6;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 13-SEP-2023, entry version 66.
DE SubName: Full=Taurocyamine kinase {ECO:0000313|EMBL:BAE16473.1};
OS Arenicola brasiliensis.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Polychaeta;
OC Sedentaria; Scolecida; Arenicolidae; Arenicola.
OX NCBI_TaxID=289432 {ECO:0000313|EMBL:BAE16473.1};
RN [1] {ECO:0000313|EMBL:BAE16473.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16008553; DOI=10.1111/j.1742-4658.2005.04767.x;
RA Uda K., Saishoji N., Ichinari S., Ellington W.R., Suzuki T.;
RT "Origin and properties of cytoplasmic and mitochondrial isoforms of
RT taurocyamine kinase.";
RL FEBS J. 272:3521-3530(2005).
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; AB186411; BAE16473.1; -; mRNA.
DR AlphaFoldDB; Q4AEC6; -.
DR BioCyc; MetaCyc:MONOMER-18470; -.
DR BRENDA; 2.7.3.4; 8000.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004111; F:creatine kinase activity; IEA:InterPro.
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: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; 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 2..84
FT /note="Phosphagen kinase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51509"
FT DOMAIN 111..353
FT /note="Phosphagen kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51510"
FT BINDING 114..118
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT BINDING 177
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT BINDING 222
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT BINDING 278..282
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT BINDING 306..311
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
SQ SEQUENCE 365 AA; 41351 MW; 191C63768F4CCA67 CRC64;
MSTFTAQQNF PIYTTHQNKV RTHLTPEMYE KMYKRVTPNG VTVDKCIQPS VDYTGKIVGL
VAGDEESYTT FNEIFDAVLD DHHLGFSTTD KHPPPELDAS KLVNAKMDEK YVKSCRIRTG
RSIRGLCLPP AISRAERREV ERTLVDALAG LKGDLSGKYY PLLKMTPEEE KQLIEDHFLF
QKPTGHLMVN SNAVRDWPDG RGIWHNNNKT FLIWVNEEDH CRVISMQQGG DMQGVFARFC
TGLKEIEGLM KAKGRQFMWS ERLGYLCTCP TNIGTGLRCS VHVQLHKLSK DARFDDIVVK
LKMQKRGTAG EHTAAVDDVY DLSNAARLKS TEREFVQLLI DGVGKLIEME KRLEAGKSID
DLVPK
//
