VRK1_CAEBR
ID VRK1_CAEBR Reviewed; 559 AA.
AC A8WU31;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Serine/threonine-protein kinase VRK1 {ECO:0000250|UniProtKB:Q19848};
DE EC=2.7.11.1;
DE AltName: Full=Vaccinia-related kinase 1 {ECO:0000250|UniProtKB:Q19848};
GN Name=vrk-1 {ECO:0000312|WormBase:CBG02540}; ORFNames=CBG02540;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- FUNCTION: Serine/threonine kinase that phosphorylates baf-1, thus
CC regulating the association of baf-1 with chromatin and nuclear membrane
CC proteins during nuclear envelope formation. May act through the egl-17
CC signaling pathway. Essential in hermaphrodites for formation of the
CC vulva, uterus, and uterine seam cells and for development and
CC maintenance of the somatic gonad and thus the germ line. Acts to
CC prevent cep-1 from triggering an inappropriate cell cycle arrest,
CC thereby promoting germ cell proliferation. Regulates anchor cell
CC polarity and the timing of anchor cell invasion through the basement
CC membranes separating vulval and somatic gonadal cells during the L3
CC larval stage (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; 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=2.7.11.1;
CC Evidence={ECO:0000250|UniProtKB:Q19848};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q19848};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q19848}.
CC Note=Nuclear during interphase, accumulates at the nuclear rim in
CC prophase and localizes to chromatin throughout metaphase, anaphase and
CC telophase. {ECO:0000250|UniProtKB:Q19848}.
CC -!- PTM: Autophosphorylates in vitro. {ECO:0000250|UniProtKB:Q19848}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CK1 Ser/Thr
CC protein kinase family. VRK subfamily. {ECO:0000255}.
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DR EMBL; HE601438; CAP23993.1; -; Genomic_DNA.
DR RefSeq; XP_002630833.1; XM_002630787.1.
DR AlphaFoldDB; A8WU31; -.
DR SMR; A8WU31; -.
DR STRING; 6238.CBG02540; -.
DR EnsemblMetazoa; CBG02540.1; CBG02540.1; WBGene00025576.
DR GeneID; 8572349; -.
DR KEGG; cbr:CBG_02540; -.
DR CTD; 8572349; -.
DR WormBase; CBG02540; CBP06284; WBGene00025576; Cbr-vrk-1.
DR eggNOG; KOG1164; Eukaryota.
DR HOGENOM; CLU_019279_4_0_1; -.
DR InParanoid; A8WU31; -.
DR OMA; PDYDKCR; -.
DR OrthoDB; 834667at2759; -.
DR Proteomes; UP000008549; Chromosome II.
DR GO; GO:0000785; C:chromatin; IEA:EnsemblMetazoa.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005635; C:nuclear envelope; IEA:EnsemblMetazoa.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0001708; P:cell fate specification; IEA:EnsemblMetazoa.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IEA:EnsemblMetazoa.
DR GO; GO:0008406; P:gonad development; IEA:EnsemblMetazoa.
DR GO; GO:0016572; P:histone phosphorylation; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0040036; P:regulation of fibroblast growth factor receptor signaling pathway; IEA:EnsemblMetazoa.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding; Developmental protein; Kinase; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..559
FT /note="Serine/threonine-protein kinase VRK1"
FT /id="PRO_0000405307"
FT DOMAIN 32..388
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 315..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 448..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..354
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..380
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..403
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..419
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..479
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..547
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 167
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 38..46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 61
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 559 AA; 62090 MW; B7AF2EA44CF57D88 CRC64;
MPPKKAAPKK LHELAPEVRV GLKIDDISKK TYIVGKQFAT GGFGRIHTCT EDGKSQQMVM
KIEPSTNGPL LTEVVVFNRI LKKDMIENYK KAKKIQWIGL PHLIANGYFT YNNEKMRYMI
IPKYATSLEA VREANGGSLS AKDSLTVADC VLGALEYLHD SDYAHADVKA ANILLEKPND
FSSAVLVDFG LAHRTTNNVD KPDKKRAHNG TCIFTSTDAH RGNNPSFRGD VEILAYNLIM
WISGSLPWLS LEASPDKVFE AKQKFVGGLP GTLQSILTNQ PAPVAGCITT MFDVSRKTDY
THKVDMAKLR KKVTEAAQSA STGAQKKPKM TPSRDTTATP KRKSQRAPRV ESEDEEEEEK
KEVEIKPKKK VQRSRKVVED DDEEEEVIIP KSTRSRKTKE EGTPRSFNLG MTSSTATSDR
VAKKIEMKYK RLATNKPSLV PVTVADASSC ESQYESNEPG PSSRVVKKRT SEERDANGEV
QLKTPALVSP DVKKTKYKSG ISSATKASPT ELRRVPGVRN FPKGRRSMII KETSARYQEK
RATRNTKPTF DDSSCSSEV
