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Database: UniProt
Entry: A0AAF3E844_9BILA
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ID   A0AAF3E844_9BILA        Unreviewed;      1024 AA.
AC   A0AAF3E844;
DT   29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2024, sequence version 1.
DT   28-JAN-2026, entry version 8.
DE   RecName: Full=Cyclin-dependent kinase 12 {ECO:0000256|ARBA:ARBA00040213};
DE            EC=2.7.11.22 {ECO:0000256|ARBA:ARBA00012425};
DE            EC=2.7.11.23 {ECO:0000256|ARBA:ARBA00012409};
DE   AltName: Full=Cell division protein kinase 12 {ECO:0000256|ARBA:ARBA00041920};
OS   Mesorhabditis belari.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Mesorhabditinae;
OC   Mesorhabditis.
OX   NCBI_TaxID=2138241 {ECO:0000313|Proteomes:UP000887575, ECO:0000313|WBParaSite:MBELARI_LOCUS10087.2};
RN   [1] {ECO:0000313|WBParaSite:MBELARI_LOCUS10087.2}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2024) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +
CC         H(+); Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.22;
CC         Evidence={ECO:0000256|ARBA:ARBA00048367};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +
CC         ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.22;
CC         Evidence={ECO:0000256|ARBA:ARBA00047811};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[DNA-directed RNA polymerase] + ATP = phospho-[DNA-directed
CC         RNA polymerase] + ADP + H(+); Xref=Rhea:RHEA:10216, Rhea:RHEA-
CC         COMP:11321, Rhea:RHEA-COMP:11322, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43176, ChEBI:CHEBI:68546,
CC         ChEBI:CHEBI:456216; EC=2.7.11.23;
CC         Evidence={ECO:0000256|ARBA:ARBA00049280};
CC   -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC       {ECO:0000256|ARBA:ARBA00004138}. Cytoplasm, cytoskeleton
CC       {ECO:0000256|ARBA:ARBA00004245}. Nucleus
CC       {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the BBS5 family.
CC       {ECO:0000256|ARBA:ARBA00005822}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC       protein kinase family. CDC2/CDKX subfamily.
CC       {ECO:0000256|ARBA:ARBA00006485}.
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DR   AlphaFoldDB; A0AAF3E844; -.
DR   WBParaSite; MBELARI_LOCUS10087.2; MBELARI_LOCUS10087.2; MBELARI_LOCUS10087.
DR   Proteomes; UP000887575; Unassembled WGS sequence.
DR   GO; GO:0034464; C:BBSome; IEA:InterPro.
DR   GO; GO:0036064; C:ciliary basal body; IEA:TreeGrafter.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IEA:TreeGrafter.
DR   GO; GO:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0060271; P:cilium assembly; IEA:TreeGrafter.
DR   FunFam; 1.10.510.10:FF:000415; CMGC/CDK/CRK7 protein kinase, variant; 1.
DR   FunFam; 3.30.200.20:FF:000074; cyclin-dependent kinase 12 isoform X2; 1.
DR   Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR006606; BBL5.
DR   InterPro; IPR014003; BBS5_PH.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR21351:SF0; BARDET-BIEDL SYNDROME 5 PROTEIN; 1.
DR   PANTHER; PTHR21351; BARDET-BIEDL SYNDROME PROTEIN 5; 1.
DR   Pfam; PF07289; BBL5; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00683; DM16; 2.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW   Cilium {ECO:0000256|ARBA:ARBA00023069};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000887575};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          686..979
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          348..532
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        362..388
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        438..452
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        462..471
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         715
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1024 AA;  115951 MW;  3A287DE49B1A273E CRC64;
     MNKGDKINGE DVWQDREIRF DVDARMLRLI PGEVLVDKID NVEDTKGNNG DRGVMRVTNL
     RLIWHASAMP RINLSIGYST VNGISAKKAN SKIRGEVESL YIMAKAPSTR FEFIFTALNP
     GNVRLFTTVM SIHRAYETTK MYRELKMRGA VVDENEQLRI LPLEQQADRM GGVWNLSSDQ
     GNLGVFIITN VRVVWYASMN PQYNVSIPYL QLFSCRVRDS KFGLALVLET TSTSGEYVLG
     FRIDPEEKLQ QVCKAIQSLH KSFMMKPVFG VQVTRERPAT PRLGATEAMD TVEDDVEVLE
     KMGRPDAFAA YFSDGIVSEE PRLPVFSEEL GLAVEQLKHE RLKLLNVGKM SRMTGKSGQN
     GRSDRHKSES SSDTDRELYR AAKREHSPPR KRKDHSRNSP PPMSRSRRSR SPSPSNSRRG
     DFREKRRSRD RSRSKSRGDR RRKDEKRRRG RSKSSEKDRK KSERKSKRKR YSSGESTDDL
     VELREGSTLG SLIKKKQGDS EHKKKKKKGS KDSSSSSTSF DDETPIERSK IAGLQAPSNG
     YYLPYGASLP NTGAGPSGIV FNSGDQAPSI STFHIPMPPG PAQTYSVMNI PVPPLMAQPI
     HGAVHQSAQN LPPTIASAPI HAHFSLQQSQ QIVANIAPST LAEPVLTHLP PQAPHQPVRR
     KRPTVLNAVQ RPVHFDPWGV GFVEQYDVKD QVGEGTYGQV YKAVNKFSGE QVALKKVRLE
     NEKEGFPISA VREIKILRQL DHKNIVRLIN IVTDKTQVAD WRHTKNSFYL VFEYVDHDLM
     GLLESHMVTF TDEQIAGLFK QLLEGLEYCH AKNFLHRDIK CSNILVNNKG ELKLADFGLA
     RLFLHDVDRP YTNRVITLWY RPPELLLGEE KYGPSVDVWS VGCILGELYN KKPLFQGQTE
     QSQLDLITKI CGSPTPQNWP DVANLPLYPT FIAKRVHPRN LKTALAFIPR ATLELLDKLL
     ALDPKKRPTC SEALRHPFVA NIDPNKVKPL SLPIEQDCHE LWSKRLRKER CVQALQQELK
     KKQE
//
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