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Database: UniProt
Entry: A0A084W8H3_ANOSI
LinkDB: A0A084W8H3_ANOSI
Original site: A0A084W8H3_ANOSI 
ID   A0A084W8H3_ANOSI        Unreviewed;      1427 AA.
AC   A0A084W8H3;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 50.
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_00014509 {ECO:0000313|EMBL:KFB46517.1};
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:KFB46517.1};
RN   [1] {ECO:0000313|EMBL:KFB46517.1, 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:ASIC014509-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};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC       protein kinase family. {ECO:0000256|ARBA:ARBA00005843}.
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DR   EMBL; ATLV01021433; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ATLV01021434; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KE525318; KFB46517.1; -; Genomic_DNA.
DR   STRING; 74873.A0A084W8H3; -.
DR   EnsemblMetazoa; ASIC014509-RA; ASIC014509-PA; ASIC014509.
DR   VEuPathDB; VectorBase:ASIC014509; -.
DR   VEuPathDB; VectorBase:ASIS016024; -.
DR   OMA; RKCRPFG; -.
DR   Proteomes; UP000030765; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   CDD; cd09365; LIM2_LIMK; 1.
DR   CDD; cd00992; PDZ_signaling; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   Gene3D; 2.10.110.10; Cysteine Rich Protein; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001781; Znf_LIM.
DR   PANTHER; PTHR46485; LIM DOMAIN KINASE 1; 1.
DR   PANTHER; PTHR46485:SF4; LIM DOMAIN KINASE 1; 1.
DR   Pfam; PF00412; LIM; 2.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00132; LIM; 2.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 2.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00478; LIM_DOMAIN_1; 2.
DR   PROSITE; PS50023; LIM_DOMAIN_2; 2.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   LIM domain {ECO:0000256|ARBA:ARBA00023038, ECO:0000256|PROSITE-
KW   ProRule:PRU00125};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00125};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030765};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00125}.
FT   DOMAIN          20..79
FT                   /note="LIM zinc-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50023"
FT   DOMAIN          81..140
FT                   /note="LIM zinc-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50023"
FT   DOMAIN          184..263
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          375..654
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1033..1162
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1241..1260
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1266..1331
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1054..1078
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1103..1162
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         404
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1427 AA;  153932 MW;  E64C746D4F37EE2F CRC64;
     MPKGDGGAGQ RSGGGKKDST ACASCYNAIE PEQHVAAVGQ LWHAECFRCS VCDARLSSWY
     FEKDGLLFCK EDHWSKFGDC CQQCSQIISG PVMFAGDHKF HSECFRCESC KVFIAEGETY
     TLLERSKLYC GQCYKRHQSA FVEVSRNGTT TTSSLVRGEK AKQQPLPHTI RLVEIPWTNA
     RTDRIRLATD DKLFGASGKG AGAGCKSVRI SEVTLNSDLM SLRVGDKVLE VNGTPVRDVP
     LENLQNLIEN SAGKVLQLTV EHDPELVDQQ QQQRSVNGVL SASYCGTQCP DTCNNNEDED
     NQSSRSLSPS KLERIFRKND EGYMSGSSRK LQKRLKDVNC NTGSIAAGGE FYDLSRTKSF
     RVEPKAARIF RASDLVQGEL LGKGFFGQVF KVTHRVTQEV MVLKELYRVD EEAQKNFLKE
     VAVLRSLSHH NVLRFIGVLY KDKKLHLVTE FIPGGSLKEL IHDSGQPLSW EQRISFARDI
     SCGMSYLHSM NIIHRDLNSL NCLVREDGTV IVADFGLARI IKQPLLSTAY EKCSASAATP
     GNGNGTIGRR GRPRRQRYTV VGNPYWMAPE MMRGNKYDEK VDIFSFGIML CEIIGRVQAD
     PDYLPRLPDF GLNQTVFREK FCGQCPEPFF KIAFLCCDLN PDKRPPFHVL QDWLETMVTM
     TALNKPLPAK IVYDIEHFKG QRSTDSSLCT TPDGLATPPP SAGYSLKPSL SRKRICEGPE
     DTVEPQPKLS DLQTTSSLDV VDGVIGVGVR PPTVENNATP CCPDATNGFI VADCIEIPKS
     PHLGKDFSAN GDRIRDSIRA KRRHRMMLSR ENQRKSLDSS VLAARLGSDR LFADVNDVAD
     NGSASEPISL IMTSEMIAND AAKIAEATAG GRRERPSTDE LLASVKDSLE LNKSLIGAGG
     DGIRPNNGAW GPVPAKVKHY GEKGFVIHVQ NGHLTLNNVR DLENCSDFDS SCDTSLNYIE
     VNGNRMESES CETPEVEVKC DTVVSSGVGG VAVTSCPPPP LEPVHLSRGT CEKENISTES
     PPLTVLGKAK ITPTQSKPNF SPFAPIPPER NGSIGNGTLP TKVEEKKQPS SAQKAVQYTR
     KLFRSAMEPS GNTSKPVHDL PGTHLPSSTT KGTPSSRGHT RTSSSERSAL FSTKQKISPT
     SDPEPQPSFG VTGAGSSARP KSNTVLNSVF SYKSKPNEPS VDGARVAQGG NVFAASGSTI
     RRVGAKGSVG GKASPGGVMN AACVESIPPA TGKPPIGTYT PAALAGSGSP GSSILRFGKS
     TRTYRPVEKM TTVSGESRTA TGVRVEKYTT FSPPSGSSGS NSRTDSPSPP VPNGTRSSIG
     GTAGSRTIGI LSPSSIRRLN ARLLEARKGN GTFGSEQPTP TPVVPRTKVA TIVSISGGTK
     LPGVARKVPP VTTSSSGASR GTILSAVAGC SRERRSTRCP GGPHMGV
//
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