ID A0A093HPQ1_STRCA Unreviewed; 1639 AA.
AC A0A093HPQ1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=N308_01672 {ECO:0000313|EMBL:KFV83736.1};
OS Struthio camelus australis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Struthioniformes; Struthionidae;
OC Struthio.
OX NCBI_TaxID=441894 {ECO:0000313|EMBL:KFV83736.1, ECO:0000313|Proteomes:UP000053584};
RN [1] {ECO:0000313|EMBL:KFV83736.1, ECO:0000313|Proteomes:UP000053584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N308 {ECO:0000313|EMBL:KFV83736.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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; KL206564; KFV83736.1; -; Genomic_DNA.
DR STRING; 441894.ENSSCUP00000019903; -.
DR Proteomes; UP000053584; Unassembled WGS sequence.
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: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; -; 3.
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; 5.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00015; IQ; 5.
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; 5.
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:UP000053584};
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 21..287
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 338..1053
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 934..956
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1107..1162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1228..1317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1398..1447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1492..1555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1574..1625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1134..1162
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1228..1242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1249..1265
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1266..1296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1297..1311
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1398..1425
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1432..1447
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1581..1625
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 50
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 431..438
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1639 AA; 187648 MW; F45D09CF0BCD474A CRC64;
MLPVTGKTII FDSFPDPSDT WEIIETIGKG TYGKVFKVLN KKNGSKAAVK ILDPVHDIDE
EIEAEYNILQ ALSDHPNVVK FYGMYYKKDV KNGDQLWLVL ELCNGGSVTD LVKGFLKRGE
RMNELIIAYI LHEALTGLQH LHENKTIHRD IKGNNILLTT EGGVKLVDFG VSAQLTSTRL
RRNTSVGTPF WMAPEVIACE QQLDSSYDAR CDAWSLGITA IELGDGDPPL ADLHPMRALF
KIPRNPPPTL QQPELWSSEF NDFINKCLTK DYEKRPTVSI LLQHDFIKQI EGKENMLQRQ
LMEFIDVHQQ MGVTEKARFE RIHTKKGNYS KSLVSNQEEV DDLATLEVLD ENTVTEQLQK
GYVKDQIYTY VGDILVAVNP FRNIDIYSSQ HSKLYIGAKR TANPPHIFAV ADIGYQSMVT
YNSDQCIVIS GESGAGKTQS AHLLVQQLTV LGKANNRTLQ EKILQVNNLV EAFGNAGTII
NDNSSRFGKY LEMKFTCGGT VVGAQISEYL LEKSRVVHQA VGEKNFHIFY YIYAGLAEKK
KLAHYKLPEY RPPRYLQNDH FRIVQDFMNN SFYKSQFELI EQCFKVIGFT LEELGSVYSV
LAAILNVGNI EFSAVVSEHM IDKSNISNPV ALENCASLLC IQADELQEAL TSHCVVTRGE
TIIRPNTVEK ATDVRDAMAK ALYGRLFSWI VNRINTLLKP DKHLSENDGG LNIGILDIFG
FENFKKNSFE QLCINIANEQ IQFYFNQHVF AWEQNEYLYE GVDARVIEYE DNRPLLDMFL
QKPMGLLSLL DEESRFPQAT DQTLVEKFED NLKSKYFWRP KRVDLTFGIY HYAGKVLYNA
SGFLAKNRDT LPADIVLLLR SSENNLIRQL VTHPLTKTGN LAHTKSKTTI SYQMWTPQKS
ISRTKNETGD TGHHPRETTS MKTQTVASYF RYSLMDLLSK MVVGQPHFVR CIKPNNDRQA
NKFDKEKVLV QLRYTGILET ARIRRQGYSH RILFANFIKR YYLICYKTND DPPVSPETCA
AILEKAHLDN WVLGKTKVFL KYYHVEQLNL MRKETVDMII LIQAYVRGWL GSKRYKKLKE
QREQSAIKIQ SVARGYLLRK KRKELTESRN KAATTIQSHY RGYKERKNFK RRRESLQKKE
QTENTTSINE KEKGARLQDD EENLAGAKST LPQTEEEAAV IVQSSYRGYR ARKKIKEQHK
KLAEEELPAM EYLEAEVKAA ENITLEKAAN KESQNGTDTV TDSKCAGFRD RGNTQEQKKG
STKGEGDSLK QNSTKQQVSE DEEQVAVEQL SDKSSVKITA EPDHQQEQTN EDTVKADQQN
KVYAVVLPKT DRHLERNHLK QEAMISTGYK GITRKESIRG SRKQVVVEKQ DSEDREKAAV
VIQSNYRGYK RRGQLRKEGK LPGKNQEKTI KESREVAHIQ NSDPKTTKNK ENTGTQAEDH
KTLKEGSEKE ACDLAAFSRQ ISKLSEDYLA LQQKLNEMIL SHQLRPVMLS KDKQTDGRLS
SHVCQSVASK VEDSHPKQRP PRRPRKPKTL NNPEDSTYYT LIHKSIQDEK RKPRKDSLGK
VLDLDVYYQE ISSIDSTSKD SSSTTKKKRQ PAERRTLRAT ERSRVAESPL EESKTEDNPY
DYRRLLRKTS QRRRLIQQF
//
