ID A0A3Q3GPN3_KRYMA Unreviewed; 1827 AA.
AC A0A3Q3GPN3;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000025332.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000025332.1}
RP IDENTIFICATION.
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 RefSeq; XP_017262316.1; XM_017406827.1.
DR STRING; 37003.ENSKMAP00000025332; -.
DR Ensembl; ENSKMAT00000025652.1; ENSKMAP00000025332.1; ENSKMAG00000018687.1.
DR GeneID; 108230522; -.
DR KEGG; kmr:108230522; -.
DR CTD; 53904; -.
DR GeneTree; ENSGT00940000155939; -.
DR OMA; DRQARKY; -.
DR OrthoDB; 1094820at2759; -.
DR Proteomes; UP000264800; 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; -; 5.
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 PANTHER; PTHR46256; AGAP011099-PA; 1.
DR PANTHER; PTHR46256:SF4; MYOSIN-IIIA; 1.
DR Pfam; PF00612; IQ; 8.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00015; IQ; 9.
DR SMART; SM00242; MYSc; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50096; IQ; 9.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 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:UP000264800};
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 27..293
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 357..1088
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 322..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 969..991
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1180..1550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1658..1827
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..355
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1196..1239
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1250..1301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1302..1319
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1320..1350
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1378..1414
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1449..1478
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1479..1493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1513..1540
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1673..1693
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1694..1713
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1717..1747
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1774..1795
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 56
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 450..457
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1827 AA; 207349 MW; FA59ECB0B1171693 CRC64;
MRSLLKMFPQ SGKSIVFDNF PDPTDTWEII ETIGKGTYGK VYKVLHKPDG SKAAVKILDP
IHDIDEEIEA EYNILKALSD HSNVVKFYGM YYKKDLKCGD QLWLVLELCN GGSVTDLAKG
MLKRGDRMDE AIIAYILHEA LMGLQHLHIN KTIHRDVKGN NILLTTQGGI KLVDFGVSAQ
LTNTRLRRNT SVGTPFWMAP EVIACEQQLD STYDARCDVW SLGITAIELG DGDPPLSDLH
PMRALFKIPR NPPPTLHQPE LWSDDFNDFI SKCLIKDFEL RPNVLDLLQH VFIKQTVGRE
KILQKQLIEL IDLNQQMGVI EKTSHHGKTD RSTESNDRHE RIHTKKGSHM KSQNDSDEVD
DLAILEILDE NTVTDQLQSR YGTGQIYTYV GDILIAVNPF HQMEIYTPEY TKIYIGAKRT
ANPPHIFAVA DIAYQSMVSY NTDQCVVISG ESGAGKTESA HLLVQQLTVL GKANNRTLQE
KILLVNSLVE AFGNAGTAIN DNSSRFGKYL EMKFTHGGTV VGAQISEYLL EKSRVIHQAI
GEKNFHIFYY IYAGLADRKK LAHYKLSDSK TPKYLYNESI KLGPDIVSNA SYKEQFDAVE
QCFKVIGFTL EELGAVYSIL AAILNSGDIE FSAVASEHQT DKSNITNISV LENVASLLRI
RSDELQEALT SHCVVARGET IVRPNTVEKA VEVRDAMGKA LYARLFSWIV NRINTLLRPD
SQLGEEDKGL NIGILDIFGF ENFKKNSFEQ LCINIANEQM QFYFNQHIFA WEQDEYLNEE
VDARMIEYED NRPLLDLFLQ KPMGLLSLLD EESRFPQATD QTLVAKFEDN LKTKTFWRPK
RVDLGFGIHH YAGKVIYNAA GFLAKNRETL PADIILLLRS SENELIRKLV THPLTKTGNL
AHTKGKGANT MRTPRTPTRT MTLAKMGVLT LYSSFSFSEP VESGDTPYHP RETTNMKTQT
VASYFRYSLM DLLSKMVAGQ PHFVRCIKPS NDRQANKFDR EKVLVQLRYT GVLETAKIRR
QGYSHRVLFA NFIKRYYILA FSAHEEPAVT PETCAAILEK ANLENWAMGK TKVFLKYYHV
EHLNLMVQQA THRIVLLQAC VRGWLGAKRY QRMLKEREQS ALVLQSAYRG HKVRKKVADD
KSKAKFDAFM VQFQAVCRGY LARKKYKEMV DEKNKAAAKI QARYRGHKER KSFQRKREAK
QKEKEEKALQ DKEEAASEPT KSASDESASK EENNEEEETK AAVVLQSNYR GYKERKKFKE
RKTTMAGAET ELSNERIKEK EEEEPNNTGE DLRKAANEQG DEEDESTYEA EENDDSDHTQ
VPEDDEHTEV GEEPVIRDAD AGKEGQNAEE SGQEKTPGNE AVNVAEEAKA ATVIQSNFRG
HKERKRLQEE GKIPAKKQKG SSPAGDKEEI CNEETESSGA QAAADVSSND VKLDDPDETK
AAVVIQSNFR GHKERKRLEE EGKIPKKKTK ERTQEENVVQ TEEPVPDSQE DISSDNPDGL
DEEKAATVLQ SNFRGHRDRK KLKAEKEAQQ KAKEENVAVS ESEQELEDED KVLDVTDVVI
ERKKETDVEK ERQEEEEAAV KLQSNFRGYK DRKNLKANKE AAKNEAEQLE NFSEEIAKTS
QDFAALQQKL NEIIQAHQSN PENNGMFVRG KAINGYAPQI QSAEKRLSRA PRRTQQPKTL
NSPEDSTYYT LIHRSLQDDK RKPRKEDPGK QLDVDDQYYP TLSTSRSEPS IATEDASQDT
SQDALQDAPD RGRSVDRGES TEQTPAGSGR PQRERAVSEP ELPKPAKDNR RSVPRMSSTE
SRATDNPYDY RHLLRKTSQR RKLIKQY
//
