ID A0A0D8XCG8_DICVI Unreviewed; 1022 AA.
AC A0A0D8XCG8;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=DICVIV_12685 {ECO:0000313|EMBL:KJH41344.1};
OS Dictyocaulus viviparus (Bovine lungworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Metastrongylidae; Dictyocaulus.
OX NCBI_TaxID=29172 {ECO:0000313|EMBL:KJH41344.1, ECO:0000313|Proteomes:UP000053766};
RN [1] {ECO:0000313|EMBL:KJH41344.1, ECO:0000313|Proteomes:UP000053766}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HannoverDv2000 {ECO:0000313|EMBL:KJH41344.1,
RC ECO:0000313|Proteomes:UP000053766};
RA Mitreva M.;
RT "Draft genome of the bovine lungworm Dictyocaulus viviparus.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000053766}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HannoverDv2000 {ECO:0000313|Proteomes:UP000053766};
RX PubMed=26856411; DOI=10.1038/srep20316;
RA McNulty S.N., Strube C., Rosa B.A., Martin J.C., Tyagi R., Choi Y.J.,
RA Wang Q., Hallsworth Pepin K., Zhang X., Ozersky P., Wilson R.K.,
RA Sternberg P.W., Gasser R.B., Mitreva M.;
RT "Dictyocaulus viviparus genome, variome and transcriptome elucidate
RT lungworm biology and support future intervention.";
RL Sci. Rep. 6:20316-20316(2016).
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:0000256|ARBA:ARBA00001433};
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:0000256|ARBA:ARBA00000775};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. RIO-type Ser/Thr
CC kinase family. {ECO:0000256|ARBA:ARBA00009196}.
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DR EMBL; KN716847; KJH41344.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D8XCG8; -.
DR STRING; 29172.A0A0D8XCG8; -.
DR Proteomes; UP000053766; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05144; RIO2_C; 1.
DR Gene3D; 3.40.50.2020; -; 1.
DR Gene3D; 6.10.250.3030; -; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002083; MATH/TRAF_dom.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR029057; PRTase-like.
DR InterPro; IPR030484; Rio2.
DR InterPro; IPR015285; RIO2_wHTH_N.
DR InterPro; IPR000687; RIO_kinase.
DR InterPro; IPR018935; RIO_kinase_CS.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR008974; TRAF-like.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR45852; SER/THR-PROTEIN KINASE RIO2; 1.
DR PANTHER; PTHR45852:SF1; SERINE_THREONINE-PROTEIN KINASE RIO2; 1.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF00156; Pribosyltran; 1.
DR Pfam; PF01163; RIO1; 1.
DR Pfam; PF09202; Rio2_N; 1.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00090; RIO; 1.
DR SUPFAM; SSF54695; POZ domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF53271; PRTase-like; 1.
DR SUPFAM; SSF49599; TRAF domain-like; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS50144; MATH; 1.
DR PROSITE; PS01245; RIO1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000053766};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 52..186
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 234..305
FT /note="BTB"
FT /evidence="ECO:0000259|PROSITE:PS50097"
SQ SEQUENCE 1022 AA; 116486 MW; 9F160FAB7DD14A68 CRC64;
MSEGPNQRVR SRPRGRDESC SITRIDSFTP RFVRKIGSSL TNECVTNVEP VLLTQRWTVN
NFSSLLKLSQ PGLCLRSSVF KYPTMPDACW QLCLYPGGKR PENANNVSLF LKMSATSPLK
EVVVKAEYRF FFLDDDDEIK FSNVNIGDFH AKPPKGGHSW GLRNIPRQKV QNSIRADHSL
VISCTIELLP DAGRIPCRRV EPSAMAITEM AEVSRAHVEN ELAMFTSSEN STYSDINVTA
GTGEDRMVFA VHKFKLITHS DVFRAMLDHN MEESKTNMIM IEDFSAASVK IMLTFIYTGS
ISPQELELED ASDVMQLADK YNIPALKTMC EQDLISRVSS TNVIECMELA DFHQASYLYE
HCLDFMNANR CDTLNTESCM GRMDIEKFRY LQKDDFRVLT AIEMGMKNHE IVPLPLVAVI
AGIHRGAVVR ILADLCKYAL VAFERSKKFD GYRLTVLGYD FLALKALCTR NVVGSVGNQI
GVGKESDVFV GGDPDRNDLC LKFHRLGRTS FRKIKEKRDY HKKRRSASWL YLSRIAATKE
FTFLQALSAH GFPVPKPVDI CRHLVVMELI EGKTLCHVND VKDVAALYDR LMSIIVKFAR
HGLIHGDFNE FNVMLLEGEK VVVFDFPQMV SIVHQNAQFY FERDVECVRT FFRRKFNYDS
DDYPKFMDIE RKYNLDIELE ASGFTKQMGV DLDKAYDSEN FRAVHEAGVE EQNHSVVIES
ESECSSVSKL DKDEEELSKE EKFREHKAKI LSQSERFTNW LGEATSQLQH LVVEENEVSL
DNPVVDHTKD EDHRIERDKE RQVLSGMCVG VQREQQSIED YSHLSRSTNQ KVKLLQHKKF
GGASSLVSNS STISPEEIKK RLALEKMRSK EKLDMAQGEA CIPDDFELPV NAFDIPRCYE
GDLSAVVISE GLIRDRVRRL AKDIHETIGA SQLSLLCVLK GSYKFFNTLV DELGNARWLC
KEPMTVDFIR CKSYEDDSSS GTVQIIGLTN LEELRGKNIL DQSCFKWIHL RQRFHALLVN
VD
//
