ID   O73732_XENLA            Unreviewed;      1370 AA.
AC   O73732;
DT   01-AUG-1998, integrated into UniProtKB/TrEMBL.
DT   01-AUG-1998, sequence version 1.
DT   13-JUL-2010, entry version 71.
DE   SubName: Full=Rho-associated kinase alpha;
GN   Name=rock2;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Amphibia; Batrachia; Anura; Mesobatrachia; Pipoidea; Pipidae;
OC   Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=98136181; PubMed=9468537; DOI=10.1074/jbc.273.8.4740;
RA   Farah S., Agazie Y., Ohan N., Ngsee J.K., Liu X.J.;
RT   "A rho-associated protein kinase, ROKalpha, binds insulin receptor
RT   substrate-1 and modulates insulin signaling.";
RL   J. Biol. Chem. 273:4740-4746(1998).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily.
CC   -!- SIMILARITY: Contains 1 AGC-kinase C-terminal domain.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
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DR   EMBL; AF037073; AAC06351.1; -; mRNA.
DR   RefSeq; NP_001080945.1; -.
DR   UniGene; Xl.265; -.
DR   HSSP; Q28021; 1UIX.
DR   SMR; O73732; 14-403, 964-1033, 1239-1302.
DR   GeneID; 394289; -.
DR   KEGG; xla:394289; -.
DR   CTD; 394289; -.
DR   Xenbase; XB-GENE-959454; rock2.
DR   HOVERGEN; HBG053111; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000910; P:cytokinesis; IEA:InterPro.
DR   GO; GO:0006468; P:protein amino acid phosphorylation; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR000861; HR1-like_rho-bd.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR017892; Pkinase_C.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR002219; Prot_Kinase_C-like_PE/DAG-bd.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR020684; Rho-assoc_coiled-coil_kin-like.
DR   InterPro; IPR015751; Rho-assoc_coiled-coil_kinase.
DR   InterPro; IPR015008; Rho-bd.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Gene3D; G3DSA:1.20.5.730; Rho_bd; 1.
DR   PANTHER; PTHR22988:SF3; Rho_kinase; 1.
DR   Pfam; PF02185; HR1; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00433; Pkinase_C; 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; Kinase_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; PS50081; ZF_DAG_PE_2; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Metal-binding; Nucleotide-binding;
KW   Serine/threonine-protein kinase; Transferase; Zinc.
SQ   SEQUENCE   1370 AA;  159285 MW;  882639150AB6452D CRC64;
     MSPRQDEYMG TRWQTLEAIL RDPRSPINVE GLLDGLNSIV LDLDFPALRK NKNIDNFLNR
     YEKIVREVRK LQMKAEDYDV VKVIGRGAFG EVQLVRHKSS QKVYAMKLLS KFEMIKRSDS
     AFFWEERDIM AFANSPWVVQ LFCAFQDEKH LYMVMEYMPG GDLVNLMSNY DVPEKWAKFY
     TAEVVLALNA IHSMGLIHRD VKPDNMLLDK YGHLKLADFG TCMKMDQTGM VRCDTAVGTP
     DYISPEVLKS QGGDGYYGRE CDWWSVGVFL FEMLVGDTPF YADSLVGTYS KIMDHKNSLN
     FPEDVEISAH AKNLICAFLT DREVRLGRNG IEDIKQHPFF KNDQWNWDNI RETVAPVVPE
     LASDIDTSNF DDIEDDKGDA ETFQIPKAFA GNQLPFVGFT YYRENLLLSE SSQNCKEKKI
     LCPTNERAVS TSCKKSINKL EEQLHNEMQT KDELEQKFRA VNLRLEKIVK ELDEEASSRK
     NIESTTRQLE REKALLQHKN TEYQRKAEND ADKKRSLENE VNSLKDQLED MKRRNQNSQI
     SNEKMNQLQR QLDEANAQLR TESDAAARLR KTQTEMSKQI QQLETNNREF QDKTCMLENA
     KLKLEKDFIN LQSALESERR DRTQGSEVIS DLQGRISVLE EDLKKGKELL ARADAEKQQL
     HERLAILEKE KSNMEIDMTY KLKALQQSVE KEESEHKATK ARLADKNKIY QSIEETKSEA
     MKDMEKKLQE ERVAKQRLEN NLLETEKQYS MLDCDLKQAK QKINELEALK DKLSEDIKNL
     TLKAEQETQK RSLSQNDLKM QLQQVNCLKM SEKQLKQEVN HLTEIKLNLE KQNNELRKER
     VDADGQMKEL QDQLEAEQYF STLYKTQVRE LKEECEVKGK MYKEVQQKVQ ELQDERDSLA
     AQLEITLTKA DSEQLARSIA EEQYSDLEKE KIMKELEIKE MMARHKQELA EKYATITSLE
     ETNKTLTIDV GNLANEKEDL NNRLKEAHEQ IQRLKEEENS VVTIKTQFEK QLLTERTLKT
     QAVNKLAEIM NRKLPTKRGP DTDVRRKEKE NRKLQLDLKS EREKFTQLVI KYQREMNDMQ
     AQIADENQVR IELQMALDSK DSDIEQLRSQ MLGLDSTSIG SGHGDTDAED GFPESRLEGW
     LSLPLRNAKK FGWNKKYVVV SSRKILFYDS EQDKELSNPS MVLDIDKLFH VRPVTQTDVY
     RADAKEIPRI FQILYANEGE SKKEQEFQVD PLEKSNYICH KGHEFIPTLY HFPTSCDACM
     KPLWHMFKPP AALECRRCHI KCHKDHMDKK EEIIAPCKVN YDISTAKNLL LLANSTEEQQ
     KWVSRLVKKI PKKPPASEHQ ARSSPRPPAK ASLNQSMRRP SRQLPPNKPS
//