ID W5MLY3_LEPOC Unreviewed; 1752 AA.
AC W5MLY3;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000009392.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000009392.1}
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 EMBL; AHAT01027043; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 7918.ENSLOCP00000009392; -.
DR Ensembl; ENSLOCT00000009403.1; ENSLOCP00000009392.1; ENSLOCG00000007720.1.
DR eggNOG; KOG0587; Eukaryota.
DR eggNOG; KOG4229; Eukaryota.
DR GeneTree; ENSGT00940000155939; -.
DR HOGENOM; CLU_000192_10_0_1; -.
DR InParanoid; W5MLY3; -.
DR OMA; DRQARKY; -.
DR Proteomes; UP000018468; Linkage group LG9.
DR Bgee; ENSLOCG00000007720; Expressed in camera-type eye and 4 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; cd21956; MBD_Myo3a; 1.
DR CDD; cd01379; MYSc_Myo3; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.190; -; 4.
DR Gene3D; 1.20.58.530; -; 2.
DR Gene3D; 6.20.240.20; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 2.
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:SF3; MYOSIN III; 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; 3.
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:UP000018468};
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 46..312
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 378..1126
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 342..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1007..1029
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1219..1565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1607..1752
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1234..1260
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1295..1317
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1324..1344
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1355..1412
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1423..1461
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1484..1503
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1544..1565
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1615..1648
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1649..1666
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1673..1697
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1727..1741
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 75
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 471..478
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1752 AA; 200172 MW; F40A221BB1A0E736 CRC64;
MLKDLGGTDH LIKVLFGKTM RSLLKMFPVS GKSIVFDNFP DPSDTWEIIE TIGKGTYGKV
FKVLNKTSGS KAAVKVLDPI HDIDEEIEAE YNILKALSDH PNVVKFYGMF YKKDVKNGDQ
LWLVLELCNG GSVTDLVKGL LKRGDRMDEP IIAYILHEAL MGLQHLHRNK TIHRDVKGNN
ILLTTEGGIK LVDFGVSAQL TNTRLRRNTS VGTPFWMAPE VIACEQQLDS TYDARCDVWS
LGITAIELGD GDPPLADLHP MRALFKIPRN PPPTLHQPEL WSADFNDFIY KCLIKDFEQR
PHVPDLLQHA FIKQIGGKEK ILQMQLMELI DLHQQMGVIE KTREQGKHSE RFTDSNERHE
RIHTKKGSYM KSQSSNLDNV DDLATLEVLD ENTVAEQLQK RYSKSQIYTY VGDILIAVNP
FQKMDIYTPQ CSKIYIGAKR TANPPHIFAV ADIAYQSMVS YSADQCIVIS GESGAGKTES
AHLLVQQLTV LGKANNRTLQ EKILLVNNLV EAFGNACTVI NDNSSRFGKY LEMKFTCSGT
VVGAQISEYL LEKSRVIHQA LGEKNFHIFY YLYAGLAERK KLAHYKLSDS KTPKYLESEH
IKLVPDILNN AFYKEQFDSV EQCFKVIGFT LEELGSVYSI LAAILNAGDI EFTSVASEHQ
TDKSNISNTA MLESAASLLY IRADELQEAL TSHCVVTRGE TIVRPNTVEK AAEVRDAMGK
ALFGRLFSWI VNRINTLLKP YTQLSEEDNG LNIGILDIFG FENFKRNSFE QLCINIANEQ
IQFYFNQHIF AWEQNEYLNE DVDARLIEYE DNRPLLDMFL QKPMGLLSLL DEESRFPQAT
DQTLIEKFED NLQSKNFWRP KRVDLSFGIH HYAGKVLYNA SGFLAKNRDT LPADIVLLLR
SSENDLIRKL VTHPLTKTVR PSEKRCQSNY MNGWSVPRNL AHTKGKGVGN IRNCTPQHSI
NVSKMEMLVL FSSLSVCEGD SGESVHHPRE TTNMRTQTVA SYFRYSLMDL LSKMVAGQPH
FVRCIKPNND RQASKFDREK VLVQLRYTGV LETAKIRRQG YSHRILFANF IKRYLILAFR
SNEDPPVSPD TCAVILEKAK LENWVLGKTK VFLKYYHVEQ LNLMIKETVD RIILVQACVR
GWLGAKRYRK MQEKREQSAV VLQSAYRGYK VRKEYTGDKN KSKNETFIAK FQAACRGYLA
RKKYKELVDE KNKAAVKIQA HYRGHKERRS FKRKKEAMKK EEQPAETVQE TPEEGAMQEK
RQPETAGVNT EKGSQPQSGE DDEAKAAVVL QSNYRGYRDR KRLKQERELK NYDFDDLPPP
VEEDDFEQAS HTLPGNEEAN TEEEAKAATV IQSNFRGHRE RKRLEEEGKI PPRGKKGTAG
EESRQPGKES GKSELELNDK RTADETANEE EETRAAVVIQ SNFRGHKDRK RLQEEGKIPK
KSQREMKRES AKAKPETVVE EPEPPSDGQG LDEEKAATVI QSNFRGHRER KKLKEEREMA
GTDEMARQGN SASEPPGADP VREAQSLEEE LDEEQAAVRI QSNFRGYKDR KNLKEVSARE
REEFETFSKQ INRFSEDYLS LQKKLNEIIL ARQLNPFNRG VFVKEKPLNG FPTNDLPPDQ
KQVRTPRRTQ QPKTLNTPED STYYNLIHRS LQDDKRKPRK QSPGKLLDIE DSYYQELSSN
TSMNSSPERN TSPDQKSPTR PAPEPKVLPP SHTGRQPLAK LTSTESQEED NPYDYRKLLR
KTSQRQRLIK QC
//
