ID A0A1V9XDV1_9ACAR Unreviewed; 1323 AA.
AC A0A1V9XDV1;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=BIW11_10830 {ECO:0000313|EMBL:OQR71714.1};
OS Tropilaelaps mercedesae.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Parasitiformes; Mesostigmata; Gamasina; Dermanyssoidea; Laelapidae;
OC Tropilaelaps.
OX NCBI_TaxID=418985 {ECO:0000313|EMBL:OQR71714.1, ECO:0000313|Proteomes:UP000192247};
RN [1] {ECO:0000313|EMBL:OQR71714.1, ECO:0000313|Proteomes:UP000192247}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wuxi-XJTLU {ECO:0000313|EMBL:OQR71714.1};
RX PubMed=28327890; DOI=10.1093/gigascience/gix008;
RA Dong X., Armstrong S.D., Xia D., Makepeace B.L., Darby A.C., Kadowaki T.;
RT "Draft genome of the honey bee ectoparasitic mite, Tropilaelaps mercedesae,
RT is shaped by the parasitic life history.";
RL Gigascience 6:1-17(2017).
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
CC Target cell membrane {ECO:0000256|ARBA:ARBA00004175}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OQR71714.1}.
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DR EMBL; MNPL01013772; OQR71714.1; -; Genomic_DNA.
DR STRING; 418985.A0A1V9XDV1; -.
DR InParanoid; A0A1V9XDV1; -.
DR OrthoDB; 148126at2759; -.
DR Proteomes; UP000192247; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0044231; C:host cell presynaptic membrane; IEA:UniProtKB-KW.
DR GO; GO:0044218; C:other organism cell membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009966; P:regulation of signal transduction; IEA:UniProt.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 3.
DR Gene3D; 3.30.70.1390; ROC domain from the Parkinson's disease-associated leucine-rich repeat kinase 2; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR032171; COR.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020859; ROC_dom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR48051; -; 1.
DR PANTHER; PTHR48051:SF26; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 1.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF16095; COR; 1.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF08477; Roc; 1.
DR PRINTS; PR00449; RASTRNSFRMNG.
DR SMART; SM00248; ANK; 4.
DR SMART; SM00364; LRR_BAC; 5.
DR SMART; SM00369; LRR_TYP; 7.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
DR PROSITE; PS51450; LRR; 2.
DR PROSITE; PS51424; ROC; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Exocytosis {ECO:0000256|ARBA:ARBA00022483};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:OQR71714.1};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Membrane {ECO:0000256|ARBA:ARBA00022537};
KW Neurotoxin {ECO:0000256|ARBA:ARBA00022699};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Presynaptic neurotoxin {ECO:0000256|ARBA:ARBA00023028};
KW Reference proteome {ECO:0000313|Proteomes:UP000192247};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Target cell membrane {ECO:0000256|ARBA:ARBA00022537};
KW Target membrane {ECO:0000256|ARBA:ARBA00023298};
KW Toxin {ECO:0000256|ARBA:ARBA00022656};
KW Transferase {ECO:0000256|ARBA:ARBA00022527}.
FT REPEAT 163..195
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 711..922
FT /note="Roc"
FT /evidence="ECO:0000259|PROSITE:PS51424"
FT REGION 439..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1108..1151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1114..1147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1323 AA; 149233 MW; C6FBDCBD950BD0E7 CRC64;
MDILQQFPDL ARQTTVERWL ALHAAALNGH HRIVERLFNH QYPPSMKTTF RDASGRWEFT
MPFDVNAKDV ADQSALYAAC RQGDQRTVEA LLKFKVWAHR VVSDLSDTSV LEVSPVRGGT
GGGKLRSIMT RLTMENSGEE IPSDLQQLCP LRLNDLNRSD CGREETALHV AVRRKHQQIS
SALLRAGADP NIVSKGDEER SPIEDACRLR DNQVMELLLR HGATDSDSGA LRAAAAVNDD
RAVTKLLSLK AHKDNENKVN KKALEALSES AYTAALLIPN TPVMINWHRL GCHFSRIDQQ
WLVDAGIVLN MKLKLSPQSR VPALGAITRL DVSANELIDL PECVFSTMPS LKVLTASQNK
IAALPAGFST THCNIEEIHL QDNRIEDVPA VFFRLPQLQL MDVSNNKIQQ VPSDVWHAPR
LKDLNLSMNL LRDLPGAAGY QQEPVMTPEE QGLQTRNRRR KNPREPQRLK HHTRWRESLQ
LVESHPEENE SNRALQSLNL SHNAFEWVPA VLACNAPQLA RLSLAYNKLI YVGPLNCYPA
QIRHLDLSCN QIGEWLIAPG RPHVEPCSAA NKEVSGGGGS KHRCIHRAHS RLESLRTLLL
GNNRLTQVVI SSTAKDDEKL LFPNLSMLDM ANNSLTSIPP LIAELQSTLS VLNLSGNTGI
VHLPPELGLL NKLWNLNLRG CSLQEPLRTM IESRKYKTID IVGYLKSILE DARPYARIKL
MVVGTHGIGK TSLLEVLRGE GCGRTKAPDH WAKRMGNKNI NLKNAKGVSL STVGVDVGDW
VFEKKPGRGP ALFRTWDFGG QREYYATHQY FLSKRSLYLV VWSMLEGERG VRSLHQWLVN
IQARAPNSPV IIVATHHDLV QERYPSTYSE DLQQMVRDRF LQTVDADKRG LPRVIDSIEV
SCKTKHNIRR LAELVYETAY DLRCTGSKER LLEQRIPASY LALEDIVHHL AVERRTKGKD
PVLKSEEYVK IVGEEMKKRF NMTFRDKSEL NQATMFLHES GVLLHYEDAT LRDLYFIDPQ
WLCDMLAHVV TIREVNPFAR QGIMRVEDLK IVFKASICAP ADPESYILSL LNKFEVALTW
DGRNLLIPSL LPTEDQIRAG TDVKVPARSR TWVPRGPKNS SSNDLSRTSS VSSVQSESGQ
GTPLHRASQP DMIQDVDREI RRVIVLSYLP SGFWPRLITR ILADDLIMEA LRAYYVVPPN
CPPLPPEIKK SAEWICWQTG VELHYAGVTI LRISEVLPHV STYPDYFDSK IVAKCEQHWE
TIDVSTYTIL DVKLPRYSIK LDIAPSVEAT EQHKHEESKL HETHILRCGV DMSFLAVYMN
QSG
//
