ID A0A084W2H4_ANOSI Unreviewed; 694 AA.
AC A0A084W2H4;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=ZHAS_00012200 {ECO:0000313|EMBL:KFB44418.1};
OS Anopheles sinensis (Mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=74873 {ECO:0000313|EMBL:KFB44418.1};
RN [1] {ECO:0000313|EMBL:KFB44418.1, ECO:0000313|Proteomes:UP000030765}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24438588; DOI=10.1186/1471-2164-15-42;
RA Zhou D., Zhang D., Ding G., Shi L., Hou Q., Ye Y., Xu Y., Zhou H.,
RA Xiong C., Li S., Yu J., Hong S., Yu X., Zou P., Chen C., Chang X., Wang W.,
RA Lv Y., Sun Y., Ma L., Shen B., Zhu C.;
RT "Genome sequence of Anopheles sinensis provides insight into genetics basis
RT of mosquito competence for malaria parasites.";
RL BMC Genomics 15:42-42(2014).
RN [2] {ECO:0000313|EnsemblMetazoa:ASIC012200-PA}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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};
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DR EMBL; ATLV01019619; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KE525275; KFB44418.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A084W2H4; -.
DR STRING; 74873.A0A084W2H4; -.
DR EnsemblMetazoa; ASIC012200-RA; ASIC012200-PA; ASIC012200.
DR VEuPathDB; VectorBase:ASIC012200; -.
DR VEuPathDB; VectorBase:ASIS018101; -.
DR OMA; KSEMDER; -.
DR Proteomes; UP000030765; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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; PTHR47634; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR47634:SF9; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR Pfam; PF00069; Pkinase; 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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000030765};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 120..692
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 15..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..96
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..407
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..458
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 149
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 694 AA; 75793 MW; 0CA18DD490354E09 CRC64;
MMLGASALDG VGGVVMQQQQ QQQQQHRASD VRKGAVGAAK PIQSVDRTTS SSNETIEQDR
DRGDRDRDRD RDRDRDDEDA GDDRDADGYT SEEEEQECRD DYCRGGYHPV KLGDLFLQRY
HVIRKLGWGH FSTVWLSWDL EEKRYVALKI VKSAQHFSDT AKDEIHILKS ILNADPTDPK
RSKVVQLLND FRITGVNGTH ICMVFEVLGH NLLKLIMKSN YRGIPLANVK SIIRQVLEGL
DYLHTKCKII HTDIKPENVL VCVNESYVRK LACEATEMHA MGCKLPISLI SAAPPQFQEQ
PASTNMSKAK KKKMKKKAKL QTELIRQQME HIQQLEFGAL ENGTTDATGP EQLTIGGGSG
DGHTREDKGR TESVTTEKSS TVDLTTTATA TTTGNQLSET TRLLLNGTGG GGSEGLGAGG
GGSSSSGEED RPTLTPNAST LSSPSVSEAT SSNNNDDHGG GGGGGGQTGD KKCRGDGAGS
PGDCKSPEKP SSSCANSVTS ASKLDISESV RKILSSVKEC KDPAFEVCGI DVKIADLGNA
CWVDKHFTED IQTRQYRSLE VIIGAGYDTS ADIWSTACMA FELATGDYLF EPYSGNDYCR
DDDHIAHIIE LLGPIPKRIA LSGKNSSHAF NSKGLLKNIT GLKPWGLVDV LIEKYEWPVA
DAYEFSDFLK PMLDYDPRTR ATAADCLQHS WLRH
//
