KCRF_STRPU
ID KCRF_STRPU Reviewed; 1174 AA.
AC P18294;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Creatine kinase, flagellar;
DE EC=2.7.3.2;
OS Strongylocentrotus purpuratus (Purple sea urchin).
OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC Euechinoidea; Echinacea; Camarodonta; Echinidea; Strongylocentrotidae;
OC Strongylocentrotus.
OX NCBI_TaxID=7668;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Testis;
RX PubMed=2367531; DOI=10.1073/pnas.87.13.5203;
RA Wothe D.D., Charbonneau H., Shapiro B.M.;
RT "The phosphocreatine shuttle of sea urchin sperm: flagellar creatine kinase
RT resulted from a gene triplication.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:5203-5207(1990).
CC -!- FUNCTION: This axonemal protein participates in an energy shuttle that
CC utilizes phosphocreatine to transfer the energy from ATP generated by
CC the mitochondrion in the sperm head to dynein in the distal portions of
CC the flagellum.
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:0000255|PROSITE-ProRule:PRU10029};
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, flagellum axoneme.
CC Note=Associates specifically with the axoneme and may bind directly to
CC polymerized microtubules.
CC -!- DOMAIN: Contains three complete but non-identical creatine kinase
CC segments flanked by unique regions.
CC -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
CC {ECO:0000255|PROSITE-ProRule:PRU00842, ECO:0000255|PROSITE-
CC ProRule:PRU00843}.
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DR EMBL; M33763; AAA30049.1; -; mRNA.
DR PIR; A43736; A43736.
DR RefSeq; NP_999687.1; NM_214522.1.
DR AlphaFoldDB; P18294; -.
DR SMR; P18294; -.
DR STRING; 7668.SPU_014785-tr; -.
DR EnsemblMetazoa; NM_214522; NP_999687; GeneID_373287.
DR GeneID; 373287; -.
DR KEGG; spu:373287; -.
DR CTD; 373287; -.
DR eggNOG; KOG3581; Eukaryota.
DR HOGENOM; CLU_273780_0_0_1; -.
DR OMA; FTRFCEG; -.
DR PhylomeDB; P18294; -.
DR Proteomes; UP000007110; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004111; F:creatine kinase activity; IBA:GO_Central.
DR GO; GO:0016301; F:kinase activity; IBA:GO_Central.
DR GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
DR GO; GO:0046314; P:phosphocreatine biosynthetic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.135.10; -; 3.
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; PTHR11547; 6.
DR Pfam; PF00217; ATP-gua_Ptrans; 3.
DR Pfam; PF02807; ATP-gua_PtransN; 3.
DR SUPFAM; SSF48034; SSF48034; 3.
DR SUPFAM; SSF55931; SSF55931; 3.
DR PROSITE; PS00112; PHOSPHAGEN_KINASE; 3.
DR PROSITE; PS51510; PHOSPHAGEN_KINASE_C; 3.
DR PROSITE; PS51509; PHOSPHAGEN_KINASE_N; 3.
PE 1: Evidence at protein level;
KW ATP-binding; Cell projection; Cilium; Cilium biogenesis/degradation;
KW Cytoplasm; Cytoskeleton; Direct protein sequencing; Flagellum; Kinase;
KW Nucleotide-binding; Reference proteome; Repeat; Transferase.
FT CHAIN 1..1174
FT /note="Creatine kinase, flagellar"
FT /id="PRO_0000212010"
FT DOMAIN 53..139
FT /note="Phosphagen kinase N-terminal 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00842"
FT REPEAT 61..414
FT /note="1; approximate"
FT DOMAIN 166..408
FT /note="Phosphagen kinase C-terminal 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT DOMAIN 426..512
FT /note="Phosphagen kinase N-terminal 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00842"
FT REPEAT 434..787
FT /note="2; approximate"
FT DOMAIN 539..781
FT /note="Phosphagen kinase C-terminal 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT DOMAIN 800..886
FT /note="Phosphagen kinase N-terminal 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00842"
FT REPEAT 808..1161
FT /note="3; approximate"
FT DOMAIN 913..1155
FT /note="Phosphagen kinase C-terminal 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 169..173
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 232
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 277
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 333..337
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 542..546
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 605
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 706
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 734..739
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 749
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
SQ SEQUENCE 1174 AA; 130869 MW; B8F4FBA5AC48EE93 CRC64;
MGCAASSQQT TATGGQPAAG EKANPAPANN NPNAANKAET TGAAEELTKE SEPFVEPDPN
YPDLSKHNNY LAESLTPSIY NKICNLRTLS GYSVDGCMQT GVDNPGHPFI KTVGLVAGDE
ECYDLFADLF DPTIDKRHNG YPRNAKHTTD LNPDHLKGGD DFDPKYVLSC RVRTGRCIRG
YGLPPHCTRA ERRDVEKVCK DALATLDGPL KGTYYPLTGM TEEMQDKLIA DHFLFDKPVS
PLLMSARMAR DWPDGRGIWH NADKNFLVWI NEEDHTRVIS METSGNMKNV FKRFCNGLNK
VENALKAKGY EFSWNEHLGY VLTCPSNLGT GVRAGVHIKI PLFSKHAGFE SILKHYRLQK
RGTGGVDTAS TDGTFDISNL DRLGTSEVQQ VQSVVDGVKK LIELEKALEK GSDISGQIPR
DPAIVRAEQV KEGYPDLSKH NNHLAHCLTY DIWKSLKDKK TPSGFTLDGC IQTGVMNPGH
PHIMTVGMVA GDEESYDVFA DIFDPVIDAR HGGYPKDAVH VTNINHADLK GGDNLDPKYV
LSCRVRTGRS IIGYSLPPHC TVEERAAVET ITIGALDKFD GDLQGKYYPL EGMSDETQTQ
LIDDHFLFDK PVSPLLTAAR MHRDWPQGRG IWHNENKNFL VWVNEEDHIR VISMEKDGNM
RAVFKRFCEG LQKFEQMIKK DGKEFMWNKH LGYVLTCPSN LGTGLRAGVH VKLPLLSKYP
RFDQILRALR LQKRGTGGVD TASTDGTFDI SNLDRLGSSE VQQVQFVVDG VELLVQMEKK
LEKGEDIFDI LPQQCRPKPP IKPFSYDYPD FSLHNNWMSK CMTEEIYNKL CNLKTKGGVT
LNDCIQTGID NPGHPYIMTV GLVAGDEECY EVFAPLFDPV ISARHGGYAL DAKHPTNLNA
AELKGGDDLD PEFVLSCRVR TGRCIRGLAL PPCCTRAERA EVEKITTEAL STLSGPLKGK
YYPLTGMTDE EQEKLIEDHF LFDKPVSPLL LCANMARDWP QGRGIWHNDE KNFLVWVNEE
DHTRVISMEK SGNMKRVFER FCDGLKKVED SIKSKGYQFM WNEHLGYVLT CPSNLGTGLR
AGVHVKVPLL SQQKIFDSIL DHMRLQKRGT GGVDTASTDG TFDISNSDRI GFSEVHLVQQ
LVDGVKLLVN LEKALMKGED INSLLPEKLR EDSS
