ID A0A132A2Y4_SARSC Unreviewed; 2491 AA.
AC A0A132A2Y4;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=QR98_0037450 {ECO:0000313|EMBL:KPM05284.1};
OS Sarcoptes scabiei (Itch mite) (Acarus scabiei).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Sarcoptiformes; Astigmata; Psoroptidia; Sarcoptoidea;
OC Sarcoptidae; Sarcoptinae; Sarcoptes.
OX NCBI_TaxID=52283 {ECO:0000313|EMBL:KPM05284.1, ECO:0000313|Proteomes:UP000616769};
RN [1] {ECO:0000313|EMBL:KPM05284.1, ECO:0000313|Proteomes:UP000616769}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Arlian Lab {ECO:0000313|EMBL:KPM05284.1};
RX PubMed=26555130; DOI=10.1186/s13071-015-1198-2;
RA Rider S.D.Jr., Morgan M.S., Arlian L.G.;
RT "Draft genome of the scabies mite.";
RL Parasit. Vectors 8:585-585(2015).
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:KPM05284.1}.
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DR EMBL; JXLN01010180; KPM05284.1; -; Genomic_DNA.
DR VEuPathDB; VectorBase:SSCA009127; -.
DR OMA; YLVVWRI; -.
DR OrthoDB; 148126at2759; -.
DR Proteomes; UP000616769; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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:InterPro.
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:0048583; P:regulation of response to stimulus; 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; 1.
DR Gene3D; 3.30.70.1390; ROC domain from the Parkinson's disease-associated leucine-rich repeat kinase 2; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR020859; ROC_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR24198; ANKYRIN REPEAT AND PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24198:SF165; IPT_TIG DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF08477; Roc; 1.
DR SMART; SM00248; ANK; 6.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 2.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS51424; ROC; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043};
KW Exocytosis {ECO:0000256|ARBA:ARBA00022483};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KPM05284.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023298};
KW Neurotoxin {ECO:0000256|ARBA:ARBA00022699};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Presynaptic neurotoxin {ECO:0000256|ARBA:ARBA00023028};
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:ARBA00022777, ECO:0000313|EMBL:KPM05284.1}.
SQ SEQUENCE 2491 AA; 285424 MW; D6C98E302125D8DD CRC64;
MSKSERDTKS FTTNRLQDDQ NDPRHGLNNE DCNGNRFSNE GDDNFKGKLL HLSCIWNNPE
LLGDLLLGYE AQNINSQDDK GRTALHEAVI ANSLECVQLL LENGANPNLK QNYSDDLNQS
GKTPLHLAVQ NGRLDLVKVL LKNNANIFIR DGNHLTASKL ARSLKYYEIC QMLRSSLDSY
RSNLYESLAV LVHKGDMISF EDLLSKTIQE IRDDLNGSIE IDEASNLKLL RSIVNFVPYG
SNTLLFKACQ EGHQEIVEKL IDIGADSRQH PQTKYSPLYI ASYHNRIQIC RLLLNRFPES
VSVYSVERWL PIHAAVINGH QEIVKLLIEF EYPQEILLPF WIEKSNRSIE LIDDHNRFNS
IQSSKSQTKN SNIENCSKKF IYLMPFDVNA QDVAGQTILY LATLIGNQFL VNYLLDLRVK
SILIDSIRDD DGLIHSWIAN NEFVGLKFKS SFQDNDFDFR DRQTEIFEDC RSDFSDKSDD
DFSNSSGDTS PDVTVIQNFK ENGQQRSSNN RQQKLSTRKS SCDNHFDNLT EKLQEISHIL
NKSDSKFGLD IKADSHQIYL INPIKIDLYC DGNHETALHC AAKPLLEELI DWIEMEFESP
GRSQSKDMSS KFNFFSVISK TKSPENLKQS SYAAHISSNP ILSKLLPIFA ANLDEKIESN
STPTSSILNL EDLHPNSKAS KISKLFFPNV SMLDFSENEI RTIPKSISLL TQLSVLNMSG
NVELTSLPPE MGLLTKLWNL NTRNCDAIEE PLKTMINSKS YKTCDIISYL HSILEHSKPY
NRLKLMLVGF HSIGKTTLLE QLRHEGCTRR SHRSVPDHWG KRIGNKSLNM KTPRGVTLST
VGVDLCEWTY EMRPLKVSNL RDRSLSRTRL SNFQPISNQN LTEQYNIGPI TFRTWDFGGQ
KEYYATHQYF LSKQSIYLVV WKITEGEKGV QGLRSWLVNI QSRAPNSPVI IVGTHYDLVK
EFYPPFYSNE LQNMIRERYM SDSMDSDKRG LPKVVATIEV STKTRHNIRL LANLIYQTAC
EIRTSDGKNR LLEQKVPETY IALEEIVTAI AFARRTKNLE PVLSGKEFRQ EVSLLMKERF
DLSFRDYSEL QRAVRFLHEN GVLLHYDDAH LKDLYFLDPQ WLCDISYLIN LLNKFELAIT
WDNRTLLIPS LLPTEEQIYT GHSGWDIVIP LKSKLKLRNS AESSLINNCQ ISYKFINDLK
FNEISVPSIS DNRNPNKQNN VPSCTIRALA RHDHSILRIL LLSYVPCGFW SRLITRILAD
ESITELVRPF YVLPSSSTKP ENDPILTDFI DNSKFNWHCW QTGFGLRFHD TFLLRVKEYK
LDNNQLEPSR LVSINRLKNF SYPYDYNRIK FFLHQPKNQK DSIASLPVQL DQNDDANGND
QKDSNVWSKI NISSQTSSLI EIYVPNQSLH LESHFNYSDV KNGDNWVCNN YRLEPNVESL
TKLLVIIVEH IDTLLEDWYP SLGTRFIHTS DGKFLITRIV PCFSCMKMTI VDDQKTTVIP
SEQKKFDSEH GSFDICKTKE ILSPDTTDID SNLVDFYKFE VKKAQLEAAS VDGIAPLKPN
QKDSINQNKS FRVNAWMVEE CILSVYEDAK LRCPQHDRIR ISTISPDIVF KDLPSNYRIE
NERLQFGKLL GRGSFGFVFR AFYQNKLTST KNNRDFTMKY STTNSTFYST TSTENLNSTE
VALKLLQPIS LELRSLSGIR KGDVEAYQAL KSKWERDPLQ YSCKAYCTAR NELNILLTLK
HSNIASIIGV CPKPLALVLT LAPQGSLDLH VKSYRRSGVR ILPSILQKTF LQISKALEYL
HQHHIIYRDL KSENILVWSF PQPITCHSSS FQKSIDLVDA EEIHLKIADY GISRSSLPTG
TKGFGGTEGF MAPEIMLFNG EEEYTEKVDC FSFAMLMYEL STLHYPFEGQ EFAIRESILD
GIRPSISQRD VDNLPETFID LMTRSWAHEP NERPTMSQIV SILSAPEFGS LQNICSFSDD
VICAIGFRIK IQSESSLRNR YGMFLSKTGN QLDFLKIDEN KWNPIGYQII TENLQNRKIT
SCCIVDENQL WLGDSAAHLN IYNFDMAKQN DHFLFVCSIE LEFDNLSPSK SIKSIHWMSN
VRIVTIVSND GNVWLVNFET FLRTLSTTSN LNVDLKSRSV GFKRIENFPP FLCVANVAFC
GGKNSRDRSK ALDNEENDHF TIWCGQIDGK IAILNVAISN LSIIDQLTLD HYKDIEFNQA
NVTISTLMDV FLLCGSTSTI QPYIYSVLFS GNIIYQWNTR DKSIAHKLDC SKLAPCSESL
MSISIEEHLK PTNCRISEIS INEIQEELYV GTNFGCIIVA ELHSLQPITV FRPYHREVKF
ILSLGIYDIS PNREDNEDDY EPEDCMDSKN DFIKSKNSNK DSRLSVIKSI WPFGKSLGST
DPYSMKVSDK NPINTVVGST KRSNRKRVKR LPFVTIGRGY RNLMDRFINQ KCEDLQNEKP
STLRLNDSVK QSENDTETSR FHAIIWESGF W
//
