ID A0A084VDM6_ANOSI Unreviewed; 1719 AA.
AC A0A084VDM6;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=AGAP006094-PA-like protein {ECO:0000313|EMBL:KFB36070.1};
DE SubName: Full=Non-specific serine/threonine protein kinase {ECO:0000313|EnsemblMetazoa:ASIC003100-PA};
GN ORFNames=ZHAS_00003100 {ECO:0000313|EMBL:KFB36070.1};
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:KFB36070.1};
RN [1] {ECO:0000313|EMBL:KFB36070.1, 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:ASIC003100-PA}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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DR EMBL; ATLV01011630; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KE524705; KFB36070.1; -; Genomic_DNA.
DR STRING; 74873.A0A084VDM6; -.
DR EnsemblMetazoa; ASIC003100-RA; ASIC003100-PA; ASIC003100.
DR VEuPathDB; VectorBase:ASIC003100; -.
DR VEuPathDB; VectorBase:ASIS003047; -.
DR VEuPathDB; VectorBase:ASIS009650; -.
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; 2.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24351:SF175; CHROMOSOMAL SERINE_THREONINE-PROTEIN KINASE JIL-1; 1.
DR PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR Pfam; PF00069; Pkinase; 2.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 2.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 2.
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}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000030765};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 421..687
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 688..756
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 792..1075
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 87..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1133..1240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1289..1410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1485..1504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..176
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..197
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..216
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..292
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1133..1237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1291..1310
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1311..1328
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1329..1347
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1348..1373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1375..1399
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 453
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 824
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1719 AA; 192616 MW; E42A375840824878 CRC64;
MRPKSRTRAG AIAATKPPAP SGRIAAQEKS LCQDFRALDV LMRQDGGGAR GGGGGKVRAA
AAKRKGLSES ILPAQLVAQV VADRMQQLRG QPQQPALVGR GGGAGGSQGT KHRPMAMVRP
TQLVVDTDGS SDEEEQQSGQ EDEELGADVD CVDEEQDDEE QDDEEEEEEE PDEEEEPVNP
SSKRRTARRT ADTTSSLHAD EDEDEEEDDQ DVNMDSVEAG QDDAGDSWPV EDEEDGEDGG
EEEEVLEDCE EAEEEEYEQG QGEEYATVEG EEDDDYYYAN GMEQEGEEQE EGIIEVDDEE
DANEFAEHEE EDEDDDVQEV IDVEEHEDAQ LLKIKYMNQH AAGGRQHQWN GGAASGSGMG
ATNNNTINGK HGQQQDQDVI YTGTRTNPQG DRDREQEMIR ITTINTKVKL CEEDKVSLDD
FQLLKVLGTG AYGTVFLVRK LTGIDRNKIY AMKVLRKCVV ILKEKTAEHT RTERQILEAV
IDAPFLATMH YAFQTESKLY VVLDFVIGGE LFTHLFKRES FTEDEVKIYI AEIVVAIEQL
HKLGILYRDI KLENILIDAD GHIVLTDFGL SRELLHVKER AHSFCGTIEY MAPEIVKSRH
NDGHDTSVDW WSVGVLTYEL LTGVSPFHND DGQTEISRRI MEDEANIPSR LSDAATDFIR
KLLTKDPRRR LGSGKQDANE LKMHPFLRDT KWDLLVAKQV AAPFKPVVTS ETDTTYFSEE
FTQQESVDKP CSPPKNGHRL FRGYSFVSPK LLSCKVYDRN KFVPIHNTRP QENLIRKSAS
KLYSEFFKKY ELTGDQAIGV GTYSVCLKCR PVRPDQQGTI YAVKVLFNHA ETAGYAQREA
AALRHCQGHP NVVRFVELIE DRNYVYIVLE LVDGGELLQY INDCPERLTE AQVRPLFHQL
VDAVAFIHRC GFAHRDLKPE NILLERGGKR GSVRLRVIDF GFAQALNGDD ASDRISSWEP
AGTLGYVAPE VVSQSSVLPY ALEAADLWSL GVILYTMLSG QPPFIPQNFV GHDNLASTAK
QTELITSNIR RGLFDLSNST WQSVSDSAQD LVRSLLTVNP ERRITMQELQ DHCWLLQQKD
ASDIMPVSSS SQRHGTRKPF EQLRQAVRNT FDAFKKAEEK GFRLQGEVSS RLRLANTTTT
APENNSYKPM TTTTVPNNSN SSSSSSRKNG ADRTATKSTT AVSGKRTTTV PEVSSTKSIE
SQYSSSMEES TSSGIGRSKS SKSSLSLSGS PMRDRNLSNG SCVVILDDDD EDEEQRPVHV
EIKTPTTDVV VSPVCDLVVE TPLLKVSADA EQEQQHSHDQ KTLEELSEEV TKLSEEQEET
DEIAVDVEDD EANVRTTSEE KQQPDEELVT ESSSTEALTT TEESNNNEVA VVMEEQEDTT
AKEHNHRHRI PEEEMASSKE ATDNQPNLTE EVSDQLPTVV SNDDVAFIIE GETLSTAELS
EENGIIIPLD IQGEAEIVVG QYVISLQVPE EKVINRRSQM RVRFEDSRTS VSRRRSRNAS
PPSYGAVADG VRDWKRIVDL SPEGMVKKEA EFRSCRGYEM FAFVCYDPDR RLPRPTDGPS
DDPSDDDDAA AGVLLGFDEW EADGPFAGFS EEECYRFFGY YEWELAVKHG KRRKREPQLP
ERITKRRREI SSYEEIDVRP KRRCTDYAYY GTSKRLMRTL ARMKQEEEKF PPVEILSAPP
PPPQSHLDGA GLGFMIKPEH DWLKKNRMES VWTVGGGSE
//
