#=GF ID AvrPtoB-E3_ubiq
#=GF AC PF09046.14
#=GF DE AvrPtoB E3 ubiquitin ligase
#=GF AU Mistry J;0000-0003-2479-5322
#=GF AU Sammut SJ;0000-0003-4472-904X
#=GF SE pdb_2fd4
#=GF GA 25.00 25.00;
#=GF TC 27.60 100.00;
#=GF NC 21.00 18.10;
#=GF BM hmmbuild HMM.ann SEED.ann
#=GF SM hmmsearch --cpu 4 -Z 75585367 -E 1000 HMM pfamseq
#=GF TP Domain
#=GF RN [1]
#=GF RM 16373536
#=GF RT A bacterial inhibitor of host programmed cell death defenses is
#=GF RT an E3 ubiquitin ligase.
#=GF RA Janjusevic R, Abramovitch RB, Martin GB, Stebbins CE;
#=GF RL Science. 2006;311:222-226.
#=GF DR INTERPRO; IPR015133;
#=GF DR SO; 0000417; polypeptide_domain;
#=GF CC The E3 ubiquitin ligase domain found in the bacterial protein
#=GF CC AvrPtoB inhibits immunity-associated programmed cell death (PCD)
#=GF CC when translocated into plant cells, probably by recruiting E2
#=GF CC enzymes and transferring ubiquitin molecules to cellular
#=GF CC proteins involved in regulation of PCD and targeting them for
#=GF CC degradation. The structure of this domain reveals a globular
#=GF CC fold centred on a four-stranded beta-sheet that packs against
#=GF CC two helices on one face and has three very extended loops
#=GF CC connecting the elements of secondary structure, with remarkable
#=GF CC homology to the RING-finger and U-box families of proteins
#=GF CC involved in ubiquitin ligase complexes in eukaryotes [1].
#=GF SQ 2
#=GS A0A3D8JU15_9BURK/428-562 AC A0A3D8JU15.1
#=GS HPAB2_PSESM/428-553 AC Q8RSY1.1
A0A3D8JU15_9BURK/428-562 gd--VMTDLRTQLDayeAVNAKFSGLRPISRAYAE-EHMQFKDAAIYNQDDegpfskdlATACMFGEDLSLSNPNQRVIGLATVRSSREQAFDPDVNKEIVFMDMNKLAEFLVNNPKHPHNNQPLNVNNIADYAFKI--s
HPAB2_PSESM/428-553 ..PAVVANIRAALD...PIASQFSQLRTISKADAESEELGFKDAADHHTDD........VTHCLFGGELSLSNPDQQVIGLAGNPTDTSQPYSQEGNKDLAFMDMKKLAQFLAGKPEHPMTRETLNAENIAKYAFRIVP.
#=GC seq_cons ....VhsslRstLD...slsupFStLRsIS+A.AE.EchtFKDAA.appDD........sTtChFGt-LSLSNPsQpVIGLAss.osppQsas.-sNK-lsFMDMpKLApFLsspPcHPhsppsLNspNIAcYAF+I...
//