ID A0A1S3PN40_SALSA Unreviewed; 1373 AA. AC A0A1S3PN40; DT 12-APR-2017, integrated into UniProtKB/TrEMBL. DT 12-APR-2017, sequence version 1. DT 29-MAY-2024, entry version 34. DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513}; DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513}; GN Name=myo3b {ECO:0000313|RefSeq:XP_014028714.1}; OS Salmo salar (Atlantic salmon). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes; OC Salmonidae; Salmoninae; Salmo. OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014028714.1}; RN [1] {ECO:0000313|RefSeq:XP_014028714.1} RP IDENTIFICATION. RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014028714.1}; RG RefSeq; RL Submitted (FEB-2024) 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR RefSeq; XP_014028714.1; XM_014173239.1. DR KEGG; sasa:106586216; -. DR OrthoDB; 1094820at2759; -. DR Proteomes; UP000087266; Chromosome ssa25. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0032433; C:filopodium tip; IEA:TreeGrafter. DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW. DR GO; GO:0001917; C:photoreceptor inner segment; IEA:TreeGrafter. DR GO; GO:0032426; C:stereocilium tip; IEA:TreeGrafter. DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0000146; F:microfilament motor activity; IEA:TreeGrafter. 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:0051491; P:positive regulation of filopodium assembly; IEA:TreeGrafter. DR GO; GO:0030832; P:regulation of actin filament length; IEA:TreeGrafter. DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW. DR GO; GO:0007605; P:sensory perception of sound; IEA:TreeGrafter. DR GO; GO:0048731; P:system development; IEA:UniProt. DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW. DR CDD; cd01379; MYSc_Myo3; 1. DR Gene3D; 1.10.10.820; -; 1. DR Gene3D; 1.20.5.190; -; 2. 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:SF1; MYOSIN-IIIB; 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; 3. 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 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}; Reference proteome {ECO:0000313|Proteomes:UP000087266}; KW 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 95..361 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT DOMAIN 407..1129 FT /note="Myosin motor" FT /evidence="ECO:0000259|PROSITE:PS51456" FT REGION 1010..1032 FT /note="Actin-binding" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782" FT REGION 1199..1264 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1287..1306 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1350..1373 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1199..1216 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1217..1264 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 124 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" FT BINDING 500..507 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782" SQ SEQUENCE 1373 AA; 157394 MW; AF17AB09D8C67D6D CRC64; MELFSHALIT RALKYPPQAS LHLRNLLVPC FGFGFTNGNT DAATTGIHGN TEENHLKAKE FFHLHGRIWR SLYGLYPYKA SMIGLESLAD PSGDWDIAET IGKGTYGKVY RVNNRKDGSQ AAVKVLDPIN DVDEEIEAEY NILRTLSNHP NVVKFYGMFY KSDDLSGGQL WLVLELCNGG SVTDLIKGLL MRGQRLLEPV IAYILYGALL GLQHLHNNRI IHRDVKGNNI LLTTEGGVKL VDFGVSAQLT SARLRRNTSV GTPFWMAPEV IACEQQYDST YDARCDVWSL GITAIELADG DPPLSEMHPV KALFKIPRNP SPTLRNPEEW CRSFSHFIAQ CLIKDFETRP SVTHLLEHPF IKQAHGKEMA LGQQLSTLIC EQQDLGCKLK TKHERINTRK TLIIETSPDD DLVNLEFLDE ETIIKHLSKR YDELQIYTYV GDILIALNPF QTLSIYSPQF SKLYHGVKRA DNPPHIFATA DAAYQGMVTF CKDQCIIISG ESGAGKTESA HLIVQHLTFL GKANNRTLRE KILQVNPLVE AFGNACTAIN DNSSRFGKYL EMKFTPTGAV MGAKISEYLL EKSRVIKQAT GEKNFHIFYY IYAGLYHQEK LKKYRLPDKK PPRYIENQHG KVMQDIVSSK LYKEQFDAIQ DCFRIIGFTD EEVNSVYRIL CAILNTGNIE FTAITSQHQT DKSEVPNVEA LENAAALLCI GPEELTEALT SHCVVTRGET IIRTNTVDKA TDVRDAMSKA LYGRLFSWIV NRINALLQPD MNICVAESGM NVGILDIFGF ENFKKNSFEQ LCINIANEQI QFYFNQHIFA LEQMEYQSEG VDASLVEYED NRPILDMFLQ KPMGLLSLLD EESRFPQATD QTLVDKFEDN LRYKYFWRPK RFELCFGIQH YAGKVLYNVN GFLEKNRDTL PADIVVVLRT SENKLLQQLF SSPLTKTGNL ATSRARVTAA SRSLPPQLSS GRNKSPKYLL KVDTMEMMRH PEETTNMRRQ TVASYFRYSL MDLLSKMVVG QPHFVRCIKP NDDRQALRFF KERVMVQLRY TGILETVNIR RQGYSHRILF EEFVNRYYYL AFRAHQMPDT SKENAVAILE RAKLENWVLG KTKVFLKYYH VEQLNLLLRE LIARVMVMQA YTKGWLGARR YRREKEKRNR GAVVIQSAWR GHTTRQNFKR TRKEREDAAV CIQSAYRGHR VRKNHGIQRH RSHPGARGHT DRNEYFGYDG RHTSNDHREK VAPDRHDKQL RNDSRDKVRE DTVVKPCRET GSLRDTQCKQ GPVLKLQQRT PRRRGQQPKL LNSPEDSLYY NQLNRTLDYQ GSKRKPRKLG QIKVLDGEDE YYKLLSTVES IPEEDYLTGP PPTLSRGPLV SQS //