ID KAPR_TRIAT STANDARD; PRT; 462 AA. AC Q86ZN7; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 07-FEB-2006, entry version 17. DE cAMP-dependent protein kinase regulatory subunit (PKA regulatory DE subunit). GN Name=pkar1; OS Trichoderma atroviride. OC Eukaryota; Fungi; Ascomycota; Pezizomycotina; Sordariomycetes; OC Hypocreomycetidae; Hypocreales; mitosporic Hypocreales; Trichoderma. OX NCBI_TaxID=63577; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Zeilinger S., Kubicek C.; RT "Trichoderma atroviride cAMP-dependent protein kinase regulatory RT subunit."; RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases. CC -!- SUBUNIT: Tetramer, composed of 2 regulatory (R) and 2 catalytic CC (C) subunits. In the presence of cAMP it dissociates into 2 active CC monomeric C subunits and an R dimer (By similarity). CC -!- SIMILARITY: Belongs to the cAMP-dependent kinase regulatory chain CC family. CC -!- SIMILARITY: Contains 2 cyclic nucleotide-binding domains. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF473578; AAO33461.1; -; Genomic_DNA. DR HSSP; P12369; 1CX4. DR InterPro; IPR002373; cAMP_kin. DR InterPro; IPR000595; cNMP_bd. DR InterPro; IPR012198; PK_regulatory. DR InterPro; IPR003117; RIIa. DR Pfam; PF00027; cNMP_binding; 2. DR Pfam; PF02197; RIIa; 1. DR PIRSF; PIRSF000548; PK_regulatory; 1. DR PRINTS; PR00103; CAMPKINASE. DR SMART; SM00100; cNMP; 2. DR PROSITE; PS00888; CNMP_BINDING_1; 2. DR PROSITE; PS00889; CNMP_BINDING_2; 2. DR PROSITE; PS50042; CNMP_BINDING_3; 2. KW cAMP; cAMP-binding; Nucleotide-binding; Phosphorylation; Repeat. FT CHAIN 1 462 cAMP-dependent protein kinase regulatory FT subunit. FT /FTId=PRO_0000205415. FT NP_BIND 204 333 cAMP 1. FT NP_BIND 336 453 cAMP 2. FT REGION 54 203 Dimerization and phosphorylation FT (Potential). FT BINDING 282 282 cAMP 1 (By similarity). FT BINDING 291 291 cAMP 1 (By similarity). FT BINDING 401 401 cAMP 2 (By similarity). FT BINDING 410 410 cAMP 2 (By similarity). FT MOD_RES 164 164 Phosphoserine (By similarity). SQ SEQUENCE 462 AA; 50151 MW; 8281DDE474ABA145 CRC64; MSLPEAYQLE IQALNKQVLQ TCPSDILQFC ADFFNSRLAT ERAASISLFR DRGTPSPRFP PSPTNPHFGM MSSQFSSPFG ANANPFGGSS SNPNPFGGSA SPMSSSVMHR VVEEDESDNH LAPGGSLFSG AFGGDASTEA PPTLRAPPTT DSYPAQYNFS RRTSVSAESL KPSADGFDNW TPPYTDKTPE QVERLKYAIE GNFLFSHLDD EQSAQILGAL VEKPIPARGI KVISQGDAGD YFYVVERGSF DVYVNDCGFI EPGPDGLGNK VGTIQAGGSF GELALMYNAP RAATIISAEG SCTLWALDRV TFRRILMEST FARRRMYENF LEEVPILSSL TPYERSKISD ALETQKFAPG DVIIHEGDPG HSFYLLESGE AAAFKGEEQV LSYKKGDFFG ELALLNDAPR AASVIATSDV KVATLGKNAF QRLLGPVEGL LRRTRYLGVK TGVEEMDPLH TQ //