ID A0A3P8RM62_AMPPE Unreviewed; 1364 AA. AC A0A3P8RM62; DT 13-FEB-2019, integrated into UniProtKB/TrEMBL. DT 13-FEB-2019, sequence version 1. DT 08-MAY-2019, entry version 3. DE RecName: Full=Rho-associated protein kinase {ECO:0000256|PIRNR:PIRNR037568}; DE EC=2.7.11.1 {ECO:0000256|PIRNR:PIRNR037568}; OS Amphiprion percula (Orange clownfish) (Lutjanus percula). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Pomacentridae; Amphiprion. OX NCBI_TaxID=161767 {ECO:0000313|Ensembl:ENSAPEP00000001286, ECO:0000313|Proteomes:UP000265080}; RN [1] {ECO:0000313|Ensembl:ENSAPEP00000001286, ECO:0000313|Proteomes:UP000265080} RP NUCLEOTIDE SEQUENCE. RA Lehmann R.; RT "Finding Nemo's genes: A chromosome-scale reference assembly of the RT genome of the orange clownfish Amphiprion percula."; RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSAPEP00000001286} RP IDENTIFICATION. RG Ensembl; RL Submitted (DEC-2018) to UniProtKB. CC -!- FUNCTION: Protein kinase which is a key regulator of actin CC cytoskeleton and cell polarity. {ECO:0000256|PIRNR:PIRNR037568}. 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|PIRNR:PIRNR037568}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|PIRNR:PIRNR037568}; CC -!- ACTIVITY REGULATION: Activated by RHOA binding. Inhibited by Y- CC 27632. {ECO:0000256|PIRNR:PIRNR037568}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|PIRNR:PIRNR037568}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr CC protein kinase family. {ECO:0000256|PIRNR:PIRNR037568, CC ECO:0000256|SAAS:SAAS00784564}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR Ensembl; ENSAPET00000001319; ENSAPEP00000001286; ENSAPEG00000000855. DR GeneTree; ENSGT00950000182698; -. DR Proteomes; UP000265080; Chromosome 10. DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. 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 CDD; cd00029; C1; 1. DR CDD; cd11639; HR1_ROCK1; 1. DR Gene3D; 2.30.29.30; -; 1. DR InterPro; IPR000961; AGC-kinase_C. 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; Rho-bd_dom. DR InterPro; IPR020684; ROCK1/ROCK2. DR InterPro; IPR037310; ROCK1_HR1. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR Pfam; PF00069; Pkinase; 1. DR Pfam; PF08912; Rho_Binding; 1. DR PIRSF; PIRSF037568; Rho_kinase; 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; SSF56112; SSF56112; 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; PS50081; ZF_DAG_PE_2; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|PIRNR:PIRNR037568, KW ECO:0000256|SAAS:SAAS00593399}; Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000265080}; KW Cytoplasm {ECO:0000256|PIRNR:PIRNR037568}; KW Cytoskeleton {ECO:0000256|PIRNR:PIRNR037568}; KW Kinase {ECO:0000256|PIRNR:PIRNR037568, ECO:0000256|SAAS:SAAS00593820}; KW Magnesium {ECO:0000256|PIRNR:PIRNR037568}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR037568, KW ECO:0000256|SAAS:SAAS00253054}; KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR037568, KW ECO:0000256|SAAS:SAAS00593601}; KW Serine/threonine-protein kinase {ECO:0000256|PIRNR:PIRNR037568, KW ECO:0000256|SAAS:SAAS00593706}; KW Transferase {ECO:0000256|PIRNR:PIRNR037568, KW ECO:0000256|SAAS:SAAS00592725}; Zinc {ECO:0000256|SAAS:SAAS00253075}; KW Zinc-finger {ECO:0000256|SAAS:SAAS00795753}. FT DOMAIN 76 338 Protein kinase. {ECO:0000259|PROSITE: FT PS50011}. FT DOMAIN 341 409 AGC-kinase C-terminal. FT {ECO:0000259|PROSITE:PS51285}. FT DOMAIN 1128 1327 PH. {ECO:0000259|PROSITE:PS50003}. FT DOMAIN 1238 1293 Phorbol-ester/DAG-type. FT {ECO:0000259|PROSITE:PS50081}. FT COILED 422 484 {ECO:0000256|SAM:Coils}. FT COILED 499 571 {ECO:0000256|SAM:Coils}. FT COILED 579 676 {ECO:0000256|SAM:Coils}. FT COILED 752 786 {ECO:0000256|SAM:Coils}. FT COILED 801 849 {ECO:0000256|SAM:Coils}. FT COILED 857 898 {ECO:0000256|SAM:Coils}. FT COILED 931 993 {ECO:0000256|SAM:Coils}. FT COILED 1028 1073 {ECO:0000256|SAM:Coils}. FT COILED 1081 1115 {ECO:0000256|SAM:Coils}. FT ACT_SITE 198 198 Proton acceptor. {ECO:0000256|PIRSR: FT PIRSR037568-1}. FT BINDING 105 105 ATP. {ECO:0000256|PIRSR:PIRSR037568-2}. SQ SEQUENCE 1364 AA; 158462 MW; 663C897E2637FB85 CRC64; MSAGESMEAR FEKIDAMLKD PKSEINTDCL LDGLDALVYD LDFPALRKNK SIDNFLNRYK ETISKIRDLR MKAEDYEVVK VIGRGAFGEV QLVRHKATSK VYAMKLLSKF EMIKRSDSAF FWEERDIMAF ANSSWVVQLF FAFQDDRYLY MVMEYMPGGD LVNLMSNYDV PEKWARFYTA EVVLALDGIH SMGFIHRDVK PDNMLLDKAG HLKLADFGTC MKMNKDGMVR CDTAVGTPDY ISPEVLKSQG GDGYYGRECD WWSVGVFLYE MLVGDTPFYA DSLVGTYSKI MNHKNALTFP DDSDISNDAK NLICAFLTDR EVRLGRNGVD EIKRHPFFKN DQWTWENIRE TAAPVVPELS SDIDTSNFDD IEEDRGEEET FPIPKAFVGN QLPFVGFTYY SNQHPLRSST ATKTSDKRSS STKEDKSHLE NLQKRIYQLE EQLHSEMQLK DELEQKCRTS NTKIEKIMKE LDEEANLRKS AEASVSLLEK DKIMLQHRFT EYQRKADQEA EKRRNLENEV STLKEQLEDM KKISQNSQAS NDKIAQLQSQ LEEANDLLRA ESDTAARLRK SHTEVAKSMS QLESLNRDLQ ERSRAADGEK AQLEKELLLL QSTLDSERRN YSQGSEEIRE LQARMAGLQE DNKNLKLSLS KVETERKQAQ ERSNNLEKEK NNLEIDLNYK LKTLQQRLEQ EHTEHRVTRA QLTDKYESIE EAKSAAMTAV QQKMSEENGA RMRAESRVVE VEKQCSMLEF DLKQSVQKME QLMKQKERLE DEVKILRIQV EQESSKRGLT QNELKSRMQE VDRLRCSEKQ LKQEINTALE SKRSLEFQLA QLTKQYRGNE GQMRELQDQL EAEQYFSTLY KTQVKELKEE IEERNRQVQE AHKRMQDLNS ERDSLSAQLD LTVTKAESEQ LARALQEEQY FELSQENKKA VTRHKQEIGE KESTITRLEE SNKTLTKDVE NLSKEKTELN EKLRTQEEEY AAQKEEIANT IKANYEKVLN TERTLKTQAV NKLAEIMNRK DMKLDQKKKG STADLRKKEK ENRKLQLELN QEKEKFNHMA IKYQKELSEM QAQLSEECTY RNELQMQLDS KESDIEQLRE KLNDLQQRMD NSSVTSLQTD ETDSNIAESR LEGWLSIPNR ANIKRYGWKK QYVVVSSKKI LFYNDEQDKE QSNPSMVLDI DKLFHVRPVT QGDVYRAETE EIPRIFQILY ANEGECRKEA EMETVPQGDK TNCLPHKGHE FIPTLYHFPS NCEACAKPLW HVFKPPPALE CRRCHVKCHK DHLDKKEDVI PPCKVNYDVT SARDMLLLAL TQDEQKKWIG HLGKKIPKTP PSTFSRASPR SMSTRSGPNQ SFRKNPKSNT GKLS //