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Database: UniProt
Entry: H2MS45_ORYLA
LinkDB: H2MS45_ORYLA
Original site: H2MS45_ORYLA 
ID   H2MS45_ORYLA            Unreviewed;      1247 AA.
AC   H2MS45;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 2.
DT   27-MAR-2024, entry version 80.
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|Ensembl:ENSORLP00000021580.2};
OS   Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC   Oryzias.
OX   NCBI_TaxID=8090 {ECO:0000313|Ensembl:ENSORLP00000021580.2, ECO:0000313|Proteomes:UP000001038};
RN   [1] {ECO:0000313|Ensembl:ENSORLP00000021580.2, ECO:0000313|Proteomes:UP000001038}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000021580.2,
RC   ECO:0000313|Proteomes:UP000001038};
RX   PubMed=17554307; DOI=10.1038/nature05846;
RA   Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., Yamada T.,
RA   Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., Shimada A.,
RA   Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., Asakawa S.,
RA   Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., Sugano S.,
RA   Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., Nomoto H., Nogata K.,
RA   Morishita T., Endo T., Shin-I T., Takeda H., Morishita S., Kohara Y.;
RT   "The medaka draft genome and insights into vertebrate genome evolution.";
RL   Nature 447:714-719(2007).
RN   [2] {ECO:0000313|Ensembl:ENSORLP00000021580.2}
RP   IDENTIFICATION.
RC   STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000021580.2};
RG   Ensembl;
RL   Submitted (NOV-2023) 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   AlphaFoldDB; H2MS45; -.
DR   STRING; 8090.ENSORLP00000021580; -.
DR   Ensembl; ENSORLT00000021581.2; ENSORLP00000021580.2; ENSORLG00000017248.2.
DR   eggNOG; KOG0587; Eukaryota.
DR   eggNOG; KOG4229; Eukaryota.
DR   GeneTree; ENSGT00940000159309; -.
DR   HOGENOM; CLU_000192_10_2_1; -.
DR   InParanoid; H2MS45; -.
DR   TreeFam; TF326512; -.
DR   Proteomes; UP000001038; Chromosome 21.
DR   Bgee; ENSORLG00000017248; Expressed in intestine and 3 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0032433; C:filopodium tip; IBA:GO_Central.
DR   GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR   GO; GO:0001917; C:photoreceptor inner segment; IBA:GO_Central.
DR   GO; GO:0032426; C:stereocilium tip; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0051491; P:positive regulation of filopodium assembly; IBA:GO_Central.
DR   GO; GO:0030832; P:regulation of actin filament length; IBA:GO_Central.
DR   GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR   GO; GO:0007605; P:sensory perception of sound; IBA:GO_Central.
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; -; 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:SF1; MYOSIN-IIIB; 1.
DR   Pfam; PF00612; IQ; 1.
DR   Pfam; PF00063; Myosin_head; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00015; IQ; 2.
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:UP000001038};
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          14..270
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          316..1031
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   REGION          912..934
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          1222..1247
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         43
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT   BINDING         409..416
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1247 AA;  142260 MW;  C02FFB2F49E9BCC8 CRC64;
     MIGFENLGDP SSNWEIVETI GKGTYGKVYR VTSKKDGSQA AVKVLDPIND VDEEIEAEYN
     ILRSLSNHPN VVKFYGMFYK TDKLSGGQLW LVLELCNGGS VTELIKSLLM RGQRLQEPLI
     SYILYSALLG LQHLHNNRII HRDVKGNNIL LTTNGGVKLV DFGVSAQLTS ARLRRNTSVG
     TPFWMAPEVR VSMFISTSAA LTDVFMLYKE RKEGAPQLLQ SLLCVIINPS PTLRSPDQWC
     RSFSHFISQC LIKDFEARPS VIHLLEHPFI KQTHGKDEAL RQQLAALIRE QQEVSYKNKT
     KHERINSRKT LIVESCPGDD LVNLDFLDEE TIISHLLKRY DELQVYTYVG DILIALNPFQ
     NLSIYSPQFS KLYHGVKRAD NPPHIFATAD AAYQGMVTFC KDQCIIISGE SGAGKTESAH
     LIVQHLTFLG KANNRSLREK ILQVNPLVEA FGNACTAIND NSSRFGKYLE MKFSPSGAVV
     GAKISEYLLE KSRVIKQASG EKNFHIFYYM YAGLHHQDKL KTYRLPDRTP PRYIDSRQYK
     VMHDIISRKL YKEQFDAIQE CFRNIGFTEE EVISVYRILS AILNTGNIEF AAITSQHQTD
     KSEVPNSEAL ENAASLLSIG AEELQEALTS QCVVTRGETI IRTNSVDKAT DVRDAMSKAL
     YGRLFSWIVN RINSLLQPDV NICAAESCMN VGILDIFGFE NFKKNSFEQL CINIANEQIQ
     FYFNQHIFAL EQMEYQSEGV DASLVEYEDN RPILDMFLQK PMGLLSLLDE ESRFPQATDQ
     TLVDKFEDNL RCKYFWIPKR VELCFGIQHY AGKVMYSVNG FLEKNRDTLP ADIVVVLRTS
     ENKLLQQLFS SPLTKTGNLA TSRARVTAAS RSLPPQLSSG RSKVDTMEMM RHPDETTNMR
     RQTVASYFRY SLMDLLSKMV VGQPHFVRCI KPNDDRQALR FCRERVMVQL RYTGILEMVN
     IRRQGYSHRI LFEEFVPRYY YLAFRAHQVP ENSKENVVLI LQRTKLEHWV LGNTKVFLKY
     YHVEQLNLLL RDVMARVVVM QAYTKGWLGA RRYQKEKRRR NRGAIIIQSA WRGYVARQNV
     KQIKIEREEA AVRRPPGKRT CRADILDVSH NLTPGNSTAD GLPSWSCSSV LLFCLLGSLP
     WISSVAGPVM KLQQRAARRR GQQPKLLNSP EDSLYYNQLN RTLDYQGSKR KPRKLGQIKV
     LDGEDEYYKL LSTVESIPEE ELVTAPSPAP LVGPSSVRPE PHIRVSR
//
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