Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-7668-00644
Entry Name
UniProt Accession
Theoretical PI
5.9
Molecular Weight
130869.43
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Creatine kinase, flagellar
Protein Synonyms/Alias
2.7.3.2;
Gene Name
Gene Synonyms/Alias
Created Date
01-NOV-1990
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
2
Canonical
******MGCAASSQQ
[1]
N-Myristoylation
Organism
Strongylocentrotus purpuratus (Purple sea urchin)
NCBI Taxa ID
7668
Reference
[1] Quest AF, Chadwick JK, Wothe DD, McIlhinney RA, Shapiro BM. Myristoylation of flagellar creatine kinase in the sperm phosphocreatine shuttle is linked to itsmembrane association properties. J Biol Chem. 1992 Jul 25;267(21):15080-5. PubMedPMID: 1634544.[PMID:1634544]
Functional Description
This axonemal protein participates in an energy shuttle that utilizes phosphocreatine to transfer the energy from ATP generated by the mitochondrion in the sperm head to dynein in the distal portions of the flagellum.
Sequence Annotation
Domain: 53 139 Phosphagen kinase N-terminal 1.
Domain: 166 408 Phosphagen kinase C-terminal 1.
Domain: 426 512 Phosphagen kinase N-terminal 2.
Domain: 539 781 Phosphagen kinase C-terminal 2.
Domain: 800 886 Phosphagen kinase N-terminal 3.
Domain: 913 1155 Phosphagen kinase C-terminal 3.
Nucleotide-binding: 169 173 ATP.
Nucleotide-binding: 333 337 ATP.
Nucleotide-binding: 542 546 ATP.
Nucleotide-binding: 734 739 ATP.
Binding site: 232 232 ATP.
Binding site: 277 277 ATP.
Binding site: 605 605 ATP.
Binding site: 706 706 ATP.
Binding site: 749 749 ATP.
Protein Length
1174 AA.
Protein Sequence
(Canonical)
MGCAASSQQT TATGGQPAAG EKANPAPANN NPNAANKAET TGAAEELTKE SEPFVEPDPN  60
YPDLSKHNNY LAESLTPSIY NKICNLRTLS GYSVDGCMQT GVDNPGHPFI KTVGLVAGDE  120
ECYDLFADLF DPTIDKRHNG YPRNAKHTTD LNPDHLKGGD DFDPKYVLSC RVRTGRCIRG  180
YGLPPHCTRA ERRDVEKVCK DALATLDGPL KGTYYPLTGM TEEMQDKLIA DHFLFDKPVS  240
PLLMSARMAR DWPDGRGIWH NADKNFLVWI NEEDHTRVIS METSGNMKNV FKRFCNGLNK  300
VENALKAKGY EFSWNEHLGY VLTCPSNLGT GVRAGVHIKI PLFSKHAGFE SILKHYRLQK  360
RGTGGVDTAS TDGTFDISNL DRLGTSEVQQ VQSVVDGVKK LIELEKALEK GSDISGQIPR  420
DPAIVRAEQV KEGYPDLSKH NNHLAHCLTY DIWKSLKDKK TPSGFTLDGC IQTGVMNPGH  480
PHIMTVGMVA GDEESYDVFA DIFDPVIDAR HGGYPKDAVH VTNINHADLK GGDNLDPKYV  540
LSCRVRTGRS IIGYSLPPHC TVEERAAVET ITIGALDKFD GDLQGKYYPL EGMSDETQTQ  600
LIDDHFLFDK PVSPLLTAAR MHRDWPQGRG IWHNENKNFL VWVNEEDHIR VISMEKDGNM  660
RAVFKRFCEG LQKFEQMIKK DGKEFMWNKH LGYVLTCPSN LGTGLRAGVH VKLPLLSKYP  720
RFDQILRALR LQKRGTGGVD TASTDGTFDI SNLDRLGSSE VQQVQFVVDG VELLVQMEKK  780
LEKGEDIFDI LPQQCRPKPP IKPFSYDYPD FSLHNNWMSK CMTEEIYNKL CNLKTKGGVT  840
LNDCIQTGID NPGHPYIMTV GLVAGDEECY EVFAPLFDPV ISARHGGYAL DAKHPTNLNA  900
AELKGGDDLD PEFVLSCRVR TGRCIRGLAL PPCCTRAERA EVEKITTEAL STLSGPLKGK  960
YYPLTGMTDE EQEKLIEDHF LFDKPVSPLL LCANMARDWP QGRGIWHNDE KNFLVWVNEE  1020
DHTRVISMEK SGNMKRVFER FCDGLKKVED SIKSKGYQFM WNEHLGYVLT CPSNLGTGLR  1080
AGVHVKVPLL SQQKIFDSIL DHMRLQKRGT GGVDTASTDG TFDISNSDRI GFSEVHLVQQ  1140
LVDGVKLLVN LEKALMKGED INSLLPEKLR EDSS                              1174
FASTA
(Canonical)
>LipidDB-7668-00644|P18294
MGCAASSQQTTATGGQPAAGEKANPAPANNNPNAANKAETTGAAEELTKESEPFVEPDPN
YPDLSKHNNYLAESLTPSIYNKICNLRTLSGYSVDGCMQTGVDNPGHPFIKTVGLVAGDE
ECYDLFADLFDPTIDKRHNGYPRNAKHTTDLNPDHLKGGDDFDPKYVLSCRVRTGRCIRG
YGLPPHCTRAERRDVEKVCKDALATLDGPLKGTYYPLTGMTEEMQDKLIADHFLFDKPVS
PLLMSARMARDWPDGRGIWHNADKNFLVWINEEDHTRVISMETSGNMKNVFKRFCNGLNK
VENALKAKGYEFSWNEHLGYVLTCPSNLGTGVRAGVHIKIPLFSKHAGFESILKHYRLQK
RGTGGVDTASTDGTFDISNLDRLGTSEVQQVQSVVDGVKKLIELEKALEKGSDISGQIPR
DPAIVRAEQVKEGYPDLSKHNNHLAHCLTYDIWKSLKDKKTPSGFTLDGCIQTGVMNPGH
PHIMTVGMVAGDEESYDVFADIFDPVIDARHGGYPKDAVHVTNINHADLKGGDNLDPKYV
LSCRVRTGRSIIGYSLPPHCTVEERAAVETITIGALDKFDGDLQGKYYPLEGMSDETQTQ
LIDDHFLFDKPVSPLLTAARMHRDWPQGRGIWHNENKNFLVWVNEEDHIRVISMEKDGNM
RAVFKRFCEGLQKFEQMIKKDGKEFMWNKHLGYVLTCPSNLGTGLRAGVHVKLPLLSKYP
RFDQILRALRLQKRGTGGVDTASTDGTFDISNLDRLGSSEVQQVQFVVDGVELLVQMEKK
LEKGEDIFDILPQQCRPKPPIKPFSYDYPDFSLHNNWMSKCMTEEIYNKLCNLKTKGGVT
LNDCIQTGIDNPGHPYIMTVGLVAGDEECYEVFAPLFDPVISARHGGYALDAKHPTNLNA
AELKGGDDLDPEFVLSCRVRTGRCIRGLALPPCCTRAERAEVEKITTEALSTLSGPLKGK
YYPLTGMTDEEQEKLIEDHFLFDKPVSPLLLCANMARDWPQGRGIWHNDEKNFLVWVNEE
DHTRVISMEKSGNMKRVFERFCDGLKKVEDSIKSKGYQFMWNEHLGYVLTCPSNLGTGLR
AGVHVKVPLLSQQKIFDSILDHMRLQKRGTGGVDTASTDGTFDISNSDRIGFSEVHLVQQ
LVDGVKLLVNLEKALMKGEDINSLLPEKLREDSS
Gene Ontology
GO:0005737; C:cytoplasm; IEA:UniProtKB-KW
GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW
GO:0031514; C:motile cilium; IEA:UniProtKB-KW
GO:0005524; F:ATP binding; IEA:UniProtKB-KW
GO:0004111; F:creatine kinase activity; IEA:UniProtKB-EC
GO:0030030; P:cell projection organization; IEA:UniProtKB-KW
Interpro
InterPro; IPR022415; ATP-guanido_PTrfase_AS
InterPro; IPR022414; ATP-guanido_PTrfase_cat
InterPro; IPR022413; ATP-guanido_PTrfase_N
InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom
Pfam
Pfam; PF00217; ATP-gua_Ptrans;
Pfam; PF02807; ATP-gua_PtransN;
SMART
PROSITE
PROSITE; PS00112; PHOSPHAGEN_KINASE;
PROSITE; PS51510; PHOSPHAGEN_KINASE_C;
PROSITE; PS51509; PHOSPHAGEN_KINASE_N;
PRINTS