#=GF ID   PIMT_C
#=GF AC   PF20799.1
#=GF DE   Protein-L-isoaspartyl O-methyltransferase, C-terminal domain
#=GF AU   Bateman A;0000-0002-6982-4660
#=GF AU   Lazaro Pinto Beatriz;0000-0001-6837-2941
#=GF AU   Chuguransky S;0000-0002-0520-0736
#=GF SE   ECOD:331.8.1
#=GF GA   22.90 22.90;
#=GF TC   22.90 236.70;
#=GF NC   22.50 21.50;
#=GF BM   hmmbuild HMM.ann SEED.ann
#=GF SM   hmmsearch -Z 75585367 -E 1000 --cpu 4 HMM pfamseq
#=GF TP   Domain
#=GF RC   Paper describing PDB structure 1dl5
#=GF RN   [1]
#=GF RM   11080641
#=GF RT   Crystal structure of protein isoaspartyl methyltransferase: a
#=GF RT   catalyst for protein repair.
#=GF RA   Skinner MM, Puvathingal JM, Walter RL, Friedman AM;
#=GF RL   Structure. 2000;8:1189-1201.
#=GF DR   SO; 0000417; polypeptide_domain;
#=GF CC   Protein-L-isoaspartyl O-methyltransferase (PIMT) from Thermotoga
#=GF CC   maritima is a conserved and nearly ubiquitous enzyme involved in
#=GF CC   the repair of proteins damaged by age-related isoaspartyl
#=GF CC   formation. PIMT consists of three domains. This entry represents
#=GF CC   its C-terminal domain, which shows a five-stranded beta meander
#=GF CC   flanked on both sides by alpha helices. Its function is unknown
#=GF CC   [1].
#=GF SQ   1
#=GS PIMT_THEMA/214-317  AC Q56308.1
PIMT_THEMA/214-317             NLLERNRKLLREFPFNREILLVRSHIFVELVDLLTRRLTEIDGTFYYAGPNGVVEFLDDRMRIYGDAPEIENLLTQWESCGYRSFEYLMLHVGYNAFSHISCSI
#=GC seq_cons                  NLLERNRKLLREFPFNREILLVRSHIFVELVDLLTRRLTEIDGTFYYAGPNGVVEFLDDRMRIYGDAPEIENLLTQWESCGYRSFEYLMLHVGYNAFSHISCSI
//