ID G9KLM5_MUSPF Unreviewed; 1343 AA. AC G9KLM5; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 16-SEP-2015, entry version 23. DE SubName: Full=Rho-associated, coiled-coil containing protein kinase 2 {ECO:0000313|EMBL:AES05804.1}; DE Flags: Fragment; OS Mustela putorius furo (European domestic ferret) (Mustela furo). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Mustelidae; OC Mustelinae; Mustela. OX NCBI_TaxID=9669 {ECO:0000313|EMBL:AES05804.1}; RN [1] {ECO:0000313|EMBL:AES05804.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Lungs {ECO:0000313|EMBL:AES05804.1}; RX PubMed=23236062; DOI=10.1128/JVI.02476-12; RA Leon A.J., Banner D., Xu L., Ran L., Peng Z., Yi K., Chen C., Xu F., RA Huang J., Zhao Z., Lin Z., Huang S.H., Fang Y., Kelvin A.A., RA Ross T.M., Farooqui A., Kelvin D.J.; RT "Sequencing, annotation, and characterization of the influenza ferret RT infectome."; RL J. Virol. 87:1957-1966(2013). CC -!- SIMILARITY: Contains 1 PH domain. {ECO:0000256|RuleBase:RU003350}. CC -!- SIMILARITY: Contains AGC-kinase C-terminal domain. CC {ECO:0000256|SAAS:SAAS00128355}. CC -!- SIMILARITY: Contains PH domain. {ECO:0000256|SAAS:SAAS00128084}. CC -!- SIMILARITY: Contains protein kinase domain. CC {ECO:0000256|SAAS:SAAS00105938}. 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 EMBL; JP017206; AES05804.1; -; mRNA. DR STRING; 9669.ENSMPUP00000013446; -. DR GO; GO:0005622; C:intracellular; IEA:GOC. 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 GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro. DR GO; GO:0010825; P:positive regulation of centrosome duplication; IEA:InterPro. DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IEA:InterPro. DR GO; GO:0007266; P:Rho protein signal transduction; IEA:InterPro. DR GO; GO:0006939; P:smooth muscle contraction; IEA:InterPro. DR Gene3D; 2.30.29.30; -; 2. DR InterPro; IPR000961; AGC-kinase_C. DR InterPro; IPR011009; Kinase-like_dom. DR InterPro; IPR002219; PE/DAG-bd. DR InterPro; IPR011993; PH/PTB_dom. 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; IPR029878; ROCK2. DR InterPro; IPR002290; Ser/Thr_dual-sp_kinase. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR22988:SF24; PTHR22988:SF24; 1. 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 2: Evidence at transcript level; KW ATP-binding {ECO:0000256|RuleBase:RU000304, KW ECO:0000256|SAAS:SAAS00128419}; KW Kinase {ECO:0000256|SAAS:SAAS00128365, ECO:0000313|EMBL:AES05804.1}; KW Metal-binding {ECO:0000256|SAAS:SAAS00128042}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU000304, KW ECO:0000256|SAAS:SAAS00128193}; KW Serine/threonine-protein kinase {ECO:0000256|SAAS:SAAS00128360}; KW Transferase {ECO:0000256|SAAS:SAAS00128072}; KW Zinc {ECO:0000256|SAAS:SAAS00128354}; KW Zinc-finger {ECO:0000256|SAAS:SAAS00128318}. FT NON_TER 1 1 {ECO:0000313|EMBL:AES05804.1}. FT NON_TER 1343 1343 {ECO:0000313|EMBL:AES05804.1}. SQ SEQUENCE 1343 AA; 156053 MW; A9B0684385E5043D CRC64; DGLNSLVLDL DFPALRKNKN IDNFLNRYEK IVKKIRGLQM KAEDYDVVKV IGRGAFGEVQ EVQLVRHKAS QKVYAMKLLS KFEMIKRSDS AFFWEERDIM AFANSPWVVQ LFCAFQDDKY LYMVMEYMPG GDLVNLMSNY DVPEKWAKFY TAEVVLALDA IHSMGLIHRD VKPDNMLLDK HGHLKLADFG TCMKMDETGM VHCDTAVGTP DYISPEVLKS QGGDGYYGRE CDWWSVGVFL FEMLVGDTPF YADSLVGTYS KIMDHKNSLC FPEDAEISKH AKNLICAFLT DREVRLGRNG VEEIKQHPFF KNDQWNWDNI RETAAPVVPE LSSDIDSSNF DDIEDDKGDV ETFPIPKAFV GNQLPFIGFT YYRENLLLSD SSPCRENDSV QSRKNEESQE IQKKLYTLEE HLSTEMQAKE ELEQKCKSVN TRLEKVAKEL EEEITLRKSV ESALRQLERE KALLQHKNAE YQRKADHEAD KKRNLENDVN SLKDQLEDLK KRNQNSQIST EKVNQLQRQL DETNALLRTE SDTAARLRKT QAESSKQIQQ LESNNRDLQD KNCLLETAKL KLEKEFMNLQ SVLESERRDR THGSEIINDL QGRISGLEED LKNGKTLLAK AEMEKRQLQE KLTDLEKEKN NMEIDMTYQL KVIQQSLEQE EAEHKATKAR LADKNKIYES IEEAKSEAMK EMEKKLSEER TLKQKVENLL LEAEKRCSIF DCDLKQSQQK INELLKQKDV LNEDVRNLTL KIEQETQKRC LTQNDLKMQT QQVNTLKMSE KQLKQENNHL MEMKMSLEKQ NAELRKERQD ADGQMKELQD QLEAEQYFST LYKTQVRELK EECEEKTKLC KELQQKKQDL QEERDSLAAQ LEITLTKADS EQLARSIAEE QYSDLEKEKI MKELEIKEMM ARHKQELTEK DATIASLEET NRTLTSDVAN LANEKEELNN KLKDAQEQLS RLKDEEISAA AIKAQFEKQL LTERTLKTQA VNKLAEIMNR KEPVKRGSDT DVRRKEKENR KLHMELKSER EKLTQQMIKY QKELNEMQAQ IAEESQIRIE LQMTLDSKDS DIEQLRSQLQ ALHIGLDSSS IGSGPGDAEA DDGFPESRLE GWLSLPVRNN TKKFGWVKKY VIVSSKKILF YDSEQDKEQS NPYMVLDIDK LFHVRPVTQT DVYRADAKEI PRIFQILYAN EGESKKEQEF PVEPVGEKSN YICHKGHEFI PTLYHFPTNC EACMKPLWHM FKPPPALECR RCHIKCHKDH MDKKEEIIAP CKVYYDISTA KNLLLLANST EEQQKWVSRL VKKIPKKPPA PDPFARSSPR TSMKIQQNQS IRRPSRQLAP NKP //