ID E3VQ36_BOMMO Unreviewed; 1360 AA.
AC E3VQ36;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 83.
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=100529202 {ECO:0000313|EnsemblMetazoa:NP_001188507.1};
OS Bombyx mori (Silk moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Bombycidae; Bombycinae; Bombyx.
OX NCBI_TaxID=7091 {ECO:0000313|EMBL:ADP21243.1};
RN [1] {ECO:0000313|Proteomes:UP000005204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=p50T {ECO:0000313|Proteomes:UP000005204};
RX PubMed=19121390; DOI=10.1016/j.ibmb.2008.11.004;
RG International Silkworm Genome Consortium;
RT "The genome of a lepidopteran model insect, the silkworm Bombyx mori.";
RL Insect Biochem. Mol. Biol. 38:1036-1045(2008).
RN [2] {ECO:0000313|EMBL:ADP21243.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21040523; DOI=10.1186/1471-2164-11-611;
RA Zhang J.Y., Pan M.H., Sun Z.Y., Huang S.J., Yu Z.S., Liu D., Zhao D.H.,
RA Lu C.;
RT "The genomic underpinnings of apoptosis in the silkworm, Bombyx mori.";
RL BMC Genomics 11:611-611(2010).
RN [3] {ECO:0000313|EMBL:ADP21243.1}
RP NUCLEOTIDE SEQUENCE.
RA Zhang J.-Y., Pan M.-H., Lu C.;
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EnsemblMetazoa:NP_001188507.1}
RP IDENTIFICATION.
RC STRAIN=p50T (Dazao) {ECO:0000313|EnsemblMetazoa:NP_001188507.1};
RG EnsemblMetazoa;
RL Submitted (JUN-2022) to UniProtKB.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000256|ARBA:ARBA00009903}.
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DR EMBL; HQ179969; ADP21243.1; -; mRNA.
DR RefSeq; NP_001188507.1; NM_001201578.1.
DR SMR; E3VQ36; -.
DR STRING; 7091.E3VQ36; -.
DR PaxDb; 7091-BGIBMGA003038-TA; -.
DR EnsemblMetazoa; NM_001201578.1; NP_001188507.1; GeneID_100529202.
DR GeneID; 100529202; -.
DR KEGG; bmor:100529202; -.
DR CTD; 6093; -.
DR eggNOG; KOG0612; Eukaryota.
DR HOGENOM; CLU_000288_140_0_1; -.
DR InParanoid; E3VQ36; -.
DR OMA; ERDKYNQ; -.
DR OrthoDB; 4221785at2759; -.
DR Proteomes; UP000005204; Unassembled WGS sequence.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0007266; P:Rho protein signal transduction; IEA:UniProtKB-UniRule.
DR CDD; cd20813; C1_ROCK; 1.
DR CDD; cd01242; PH_ROCK; 1.
DR CDD; cd22250; ROCK_SBD; 1.
DR CDD; cd05596; STKc_ROCK; 1.
DR Gene3D; 1.20.5.340; -; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.20.5.730; Single helix bin; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR015008; ROCK_Rho-bd_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR22988; MYOTONIC DYSTROPHY S/T KINASE-RELATED; 1.
DR PANTHER; PTHR22988:SF73; RHO-ASSOCIATED PROTEIN KINASE; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF08912; Rho_Binding; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF103652; G protein-binding domain; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS51859; RHO_BD; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|PROSITE-
KW ProRule:PRU01206}; Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|ARBA:ARBA00022475};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000005204};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 77..339
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 340..410
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 940..1004
FT /note="RhoBD"
FT /evidence="ECO:0000259|PROSITE:PS51859"
FT DOMAIN 1104..1303
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1217..1271
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT REGION 1192..1215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1306..1336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 436..467
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 496..674
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 729..756
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 848..882
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 960..987
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1023..1096
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 106
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1360 AA; 156076 MW; 0FD1DCE47262C259 CRC64;
MEVKDEDRMR RLHALEERLC DPRSTGNVDC LLDTVTALVS DCDHPAIRRM KNVEAYTSRY
EEFSSEIINL RMKAADFHLI KVIGRGAFGE VQLVRQKSTN HVYAMKLLSK VEMIKRSDST
FFWEERHIMA HANSDWILKL HFAFQDHKYL YMVMDYMPGG DLVSLMSNYD IPEKWAKFYT
MEIVLALDVI HGMGFVHRDV KPDNMLIDKH GHLKLADFGT CMRMGLDGLV RASNAVGTPD
YISPEVLQSQ NGEGVYGREC DWWAVGIFLY EMLIGDPPFY ADSLVGTYGK IMDHRNSLQF
PDDVEISKEA KSLIRGLLTD RTKRLGRNSV DEIKQHPFFI NDQWSFENLR DSVPPVVPEL
SSDDDTRNFD DIEKSDALDE SFPVPKAFVG NHLPFVGFTY NGDYQLCTRQ KKANDVVDTI
SNNHINNDGS EAIYQLEKLL ERERDGKRKL EDTQAALCAQ LEELSQRELR NKKIISESDK
EVALLRHDLK EIQRIAELEV ESRRKAEANL NEAKRRLEEE QTKRTKEMSN LHIYNEKINA
LEKQLEELRE KLKQESEAAA KSRKQAAELS AAQAAAAAVN DGTVTSLRAQ RDALERERSI
LSEELSEVKA ARQRSEAAVT EATCRLNAAH AELERTSTRL SQMIADNRQL TERVSSLEKE
CTSLSHELRS AQHLYQQELR AHQDTQRSQL LSKQEANLEL VKTLQTKLNE EKTARQRSES
ACQEKDRQMS MLSVDYRQMQ QRLQKLEGEH RQESEKVCGL VASLEQERAA RLAASGEVSA
AEAAARTALA ERDARARDLH AVRAALHDAS EKLAAASAER DMYYARSEEL RSQLENEQHY
CHVYRSQVNE IRTQVEESSR AARDLEQERS SLLHQLQLAI ARADSEAIAR SIAEETVGEL
EKEKTMKELE MREAVSQHRA ELAARDNMLQ GLRDRDHENR ATIDLQRKEV DELRRSGTAL
AERVASLQRL QDELDRLNKK LNSEIMLKQQ AVNKLAEIMN RKDMNPTAGK NKSKMSVRKD
KDYRKLQQEL TREKEKFDQH ISKLQRDLQD CQQQLLDEQS TRLRLAMEVD SKDAEIEQLK
EKLAALTSET ASQSSADAED GENEQILEGW LSVPFKQNIR RHGWKKQYVV VSSKKIIFYN
SENDKQNTTD PVMILDLSKV FHVRSVTQGD VIRADAKDIP RIFQLLYAGE GEARRPDQQD
QPQDSTDHQG NTVQHKGHDL VSITYHIPTA CEVCTRPLWH MFRPPQAYEC RRCRMKIHAE
HLTEGEGVAA CKLHADRARE LLLLAPAAPE QRRWVARLAR RVQRHGYRAA HHNHDHRLSP
RYARTPPTHT RTTYAHTKGP CPFSLGVWAP KKSRVMMVLT
//
