TTBK6_CAEEL
ID TTBK6_CAEEL Reviewed; 290 AA.
AC Q09503;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2002, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Inactive tau-tubulin kinase ttbk-6 {ECO:0000305};
GN Name=ttbk-6 {ECO:0000312|WormBase:C45G9.1};
GN ORFNames=C45G9.1 {ECO:0000312|WormBase:C45G9.1};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CK1 Ser/Thr
CC protein kinase family. {ECO:0000305}.
CC -!- CAUTION: Although it belongs to the protein kinase family, lacks the
CC active site Asp residue which has been changed to Asn so is unlikely to
CC be catalytically active. {ECO:0000305}.
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DR EMBL; BX284603; CCD67390.1; -; Genomic_DNA.
DR PIR; C88449; C88449.
DR RefSeq; NP_498080.1; NM_065679.1.
DR AlphaFoldDB; Q09503; -.
DR SMR; Q09503; -.
DR STRING; 6239.C45G9.1; -.
DR PaxDb; Q09503; -.
DR EnsemblMetazoa; C45G9.1.1; C45G9.1.1; WBGene00016673.
DR GeneID; 183478; -.
DR KEGG; cel:CELE_C45G9.1; -.
DR UCSC; C45G9.1; c. elegans.
DR CTD; 183478; -.
DR WormBase; C45G9.1; CE24851; WBGene00016673; ttbk-6.
DR eggNOG; KOG1164; Eukaryota.
DR GeneTree; ENSGT00970000196711; -.
DR HOGENOM; CLU_019279_2_5_1; -.
DR InParanoid; Q09503; -.
DR OMA; RYHAREN; -.
DR OrthoDB; 919785at2759; -.
DR PhylomeDB; Q09503; -.
DR PRO; PR:Q09503; -.
DR Proteomes; UP000001940; Chromosome III.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 3: Inferred from homology;
KW Reference proteome.
FT CHAIN 1..290
FT /note="Inactive tau-tubulin kinase ttbk-6"
FT /id="PRO_0000086838"
FT DOMAIN 1..240
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 244..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 268..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 290 AA; 33803 MW; 6595F28BAABD6180 CRC64;
MEDHVLKKLN ANGPAPHIPN LNLYGKKMNF SYMVMTLLGR NLQDLESTNF VVNKGFSRGT
WSRVGIQWVY ALKYVHYNGF IHRNVNTQNL FLGNEKDSER AKIIHILDFG LGRPFARYHA
RENKWIVRIA RHSAEFRGSF RYASPNVHLR KEQGRVDDVW SLPYVIIELN GGKALPWQTD
YRRGRVEQMK LNLTPKDVMS DMPACMDKLM PHLASLNYYQ RPDDHMIFKC FWQVMENEKI
TPSSKFDWEN EEPDMSVPPA AWENPDGRYF QSNPLEINGP PTPAEVDFVL