ID A0A182P5D9_9DIPT Unreviewed; 1882 AA.
AC A0A182P5D9;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
OS Anopheles epiroticus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=199890 {ECO:0000313|EnsemblMetazoa:AEPI002129-PA, ECO:0000313|Proteomes:UP000075885};
RN [1] {ECO:0000313|Proteomes:UP000075885}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Epiroticus2 {ECO:0000313|Proteomes:UP000075885};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Howell P., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles epiroticus epiroticus2.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AEPI002129-PA}
RP IDENTIFICATION.
RC STRAIN=Epiroticus2 {ECO:0000313|EnsemblMetazoa:AEPI002129-PA};
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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|PROSITE-ProRule:PRU00782}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the TRAFAC class
CC myosin-kinesin ATPase superfamily. Myosin family.
CC {ECO:0000256|ARBA:ARBA00006998}.
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DR STRING; 199890.A0A182P5D9; -.
DR EnsemblMetazoa; AEPI002129-RA; AEPI002129-PA; AEPI002129.
DR VEuPathDB; VectorBase:AEPI002129; -.
DR OrthoDB; 1094820at2759; -.
DR Proteomes; UP000075885; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003774; F:cytoskeletal motor activity; 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 GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR CDD; cd01379; MYSc_Myo3; 1.
DR CDD; cd06608; STKc_myosinIII_N_like; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.190; -; 1.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 6.20.240.20; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR036083; MYSc_Myo3.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR46256; AGAP011099-PA; 1.
DR PANTHER; PTHR46256:SF3; MYOSIN III; 1.
DR Pfam; PF00612; IQ; 2.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00015; IQ; 4.
DR SMART; SM00242; MYSc; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50096; IQ; 2.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Myosin {ECO:0000256|ARBA:ARBA00023123, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; Sensory transduction {ECO:0000256|ARBA:ARBA00022606};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Vision {ECO:0000256|ARBA:ARBA00023305}.
FT DOMAIN 22..289
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 340..1045
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 308..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 926..948
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1427..1454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1471..1602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1697..1721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1787..1818
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1850..1882
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1089..1138
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1435..1454
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1526..1556
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1557..1580
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1582..1601
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1787..1803
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1804..1818
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 433..440
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1882 AA; 215003 MW; E61FEDB628959525 CRC64;
MAYNGLSQHV DFSRLPNPSE RFELLDLIGE GTYGEVYSAK DKHTGRKYAV KILESIADNI
EEIEEEYLVL RDLSKHPNIP DFAGLFLKRG TTVEDDQLWF VLELCTGGSV TDLVQGLRSR
GARLSNNQIA YILRETVQAL VFLHENHCMH RDIKGHNILL TETGHVKLVD FGVSSHLAAT
MARRNTSVGT PYWMAPEVIA CEQQLDQSYD SRCDVWSVGI TAIELAEGDP PLCELHPMRA
LFQIPRNPPP KLSHPEQYSS MLSDFISECL VKDLEQRPFS KELVTHPFLK SVGPYVDQIR
QELRSEIARQ REDGRAPSQA IATTKYGKLK SDRKSKPQKM YMDDLAALDV LTEDAIVEQL
QKRYETNQIY TYIGDILIAV NPFSHVGLYT TQHQRKYTGQ ARSDNPPHIF AIADAAHQAL
VHQRQNQAIV ISGESGSGKT ESANLLLKQL VYLGKAVTKN LEERILQVNP IMEAFGNART
GINANSSRFG KYLELTMARS GKVNGARIFV YLLEQSRVVK QAEGEGNFHV FYYMYDGLQA
EGRLEEYYLH PSYRKTHRYL QETATLPKTN VDRWKQLLAS FRVLGFKDDE VDMVNRVLAA
ILNLGDIEFG EMDSNDNTDS RARVIDVAPM HRVSKLLGVD SADLLEALSS NSVVTRGETI
TRHNNVAEAC TARDAMAKGL YGRLFDWMVN QINLLLVHNR NSNSPEQLAI GLLDIFGFEN
FSKNSFEQLC INIANEQIQY YFNQHIFTWE QQEYMAEGIP VDLVEFADNR PVLDMLLSRP
LGLLALLDEE SRFPRSTDRS LIEKFHNNVK SKFYQRPKSD AVCFAIHHFA GRVVYQADGF
LEKNRNFLPA EIIQLIRQSQ YDMIRFLFQC PITKTGNLYS AIQDTGSRQN VPSFIKVDTK
EKFNSRGLAS QSRAQQTVAT YFRYSLMDLL QKMVTGTPQF IRCIKPNEQK AAKSFDAAKV
LKQLRYTGVL ETIRIRQHGF SHRFTFADFL RKYCFLAYSF EERVVSNRES CRLLLVRLKM
DGWALGKSKV FLKYYHVEYL SKLYEEHVRK IILVQACVRR WLAKAFYKRE KQRVALSAVT
LQKHVRGWLT RRRMRILKEK QERERLEQER LEKERLAKEK KNNEQNKAKQ ALAKAKLIHQ
LSNHQLEAKH DKRGADMNNK ENERAAIVIQ SYYRGYTIRK MRMTPEIEAK TKYILGIAKN
RVEAQRMMQK EGFTKEDAAR IIQRYYRTQK SKHNNNRDAM AAAVGAAVNR KGPAPQPQPK
PLTTKDQQMD LIAFSQNVHM LNQEVHKNLR VNKAGVPLEA IEKLPNDYRR PPGFVLVPGL
LGTVPGGNDC AKYSSLRSVD CDHEMTKEVI QRTPPPAADF DDISPWDMPF YEVERNLRSQ
RQRNMQQPPQ RIDINRNDIL GDRKMELGDR KQQLSSNWHQ AFQATEGTPQ DKFKGLARSP
QNQNEPGHIR SIPAFSYLNP NNQQILRYSP NQHRDASGEP TAHPQPPHPS PVRQSPVEQP
TREASTPPTR LGLLGLGGGG AGKKAAKAEL KAREKENKER KKREKKAKKE KEKAAANGHT
PSSTSSSGGS ALSSGASSGE KQRKEPAGRK KRSEQKDAQQ EQKIVSRFAG VDDQSLHEYH
QQYHQQQQQQ QVPQKRLIEH HEYQNISEET KIDSKSPVMR MFGDTNFLVN HRRKAAEQKQ
QQLVQLQQVH QYQKQQQQQK ARQQQQQQQH HLQQSNGNGG WRQQELNCGQ GVCELLNGVY
RFSPHITSFA QMDSKSASSL SDDRSTLDKD YQNFNVSKYL NIDVKGPIHH QRDRARDSGV
HERDVSSNSS SLSTGSSGMN SLNSFDSVEQ AIIFQKDRNA DSYLGPFNFR QLLRPTQGPT
ESLRKRKGIN PPSPPPPQRG KS
//
