ID A0A3B4VBK7_SERDU Unreviewed; 1230 AA.
AC A0A3B4VBK7;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
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:ENSSDUP00000028206.1};
OS Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000028206.1, ECO:0000313|Proteomes:UP000261420};
RN [1] {ECO:0000313|Ensembl:ENSSDUP00000028206.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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; A0A3B4VBK7; -.
DR Ensembl; ENSSDUT00000028697.1; ENSSDUP00000028206.1; ENSSDUG00000020313.1.
DR GeneTree; ENSGT00940000159309; -.
DR OMA; QPDKNIW; -.
DR Proteomes; UP000261420; Unplaced.
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: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; 1.20.5.4820; -; 1.
DR Gene3D; 1.20.58.530; -; 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; 3.
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}; 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..280
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 326..1048
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 929..951
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1117..1189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1127..1189
FT /note="Basic and acidic residues"
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 419..426
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1230 AA; 140677 MW; C6077C84851C9F08 CRC64;
MIGLESLGDP SGNWDIVETI GKGTYGKVYR VTNKKDGSQA AVKVLDPIND VDEEIEAEYN
ILRSLSNHPN VVKFYGMFYK SDNLSGGQLW LVLELCNGGS VTELIKGLLM RGQRLQEPVI
SYILYSALLG LQHLHNNRII HRDVKGNNIL LTTEGGVKLV DFGVSAQLTS ARLRRNTSVG
TPFWMAPEVI ACEQQYDYSY DARCDVWSLG ITAIELADGD PPLAEMHPVK ALFKIPRNPS
PTLRNPEQWC RSFSHFIGQC LIKDFEARPS VTHLLEHPFI KQAHGKDVAL PQQLAALIQE
QQEMGCKTKT KHERINTRKN LIIESCPDDD LVNLEFLDEE TIISHLQKRY DELQVYTYVG
DILIALNPFQ NLSIYSPQFS KLYHGVKRAD NPPHIFASAD AAYQGMVTFC KDQCIVISGE
SGAGKTESAH LIVQHLTFLG KANNRTLREK ILQVNPLVEA FGNACTAIND NSSRFGKYLE
MKFTPTGAVI GAKISEYLLE KSRVIKQATG EKNFHIFYYI YAGLYHQDKL KTYRLPDRTP
PRYIDSQHCK VMQDIVSSKL YQEQFDAIQE CFRNIGFTEE EVNSVYRILS AILNTGNIEF
AAITSQHQTD KSEVPNSEAL ENAASLLSIG PEELQEALTS QCVVTRGETI IRTNTVDKAV
DVRDAMSKAL YGRLFSWIVN RINSLLQPDM NICAAESSMN VGILDIFGFE NFKKNSFEQL
CINIANEQIQ FYFNQHIFAL EQMEYQSEGV DASLVEYEDN RPILDMFLQK PMGLLSLLDE
ESRFPQATEQ TLVDKFEDNL RCKYFWIPKR VELCFGIQHY AGKVMYNVNG FLEKNRDTLP
ADIVVVLRTS ENKLLQQLFS SPLTKTGNLA TSRARITAAS RSLPPQLGSG RTKSPKYLLK
VDTMEMMRHP DETTNMRRQT VASYFRYSLM DLLSKMVVGQ PHFVRCIKPN DDRQALRFCK
ERVMVQLRYT GILETVNIRR QGYSHRILFE EFVKRYYYLA FRAHQMPETS KENAVAILER
AKLEGWVLGK TKVFLRYYHV EQLNLLLREV IARVVVMQAY TKGWLGARRY RKEREKRNRG
AIIIQSAWRG FVARQNLKQI KKEREEAAVR IQSAYRGHRV RRDHGPQRHR CHPEAGGKTT
KEEHMRSNSP ESKGAHTDHI HRGHVGPDSR DRQVKDFKRD KGRAEDSVAK PCRETARLRD
MQCKQANPLL PFFVDSRRRE ALWVIISAVF
//
