#=GF ID   PMT_C3
#=GF AC   PF20900.1
#=GF DE   Pasteurella multocida toxin, C3 domain
#=GF AU   Lazaro Pinto Beatriz;0000-0001-6837-2941
#=GF AU   Chuguransky S;0000-0002-0520-0736
#=GF AU   Bateman A;0000-0002-6982-4660
#=GF SE   ECOD:4311.1.1
#=GF GA   27.00 27.00;
#=GF TC   27.60 65.50;
#=GF NC   26.80 17.70;
#=GF BM   hmmbuild HMM.ann SEED.ann
#=GF SM   hmmsearch -E 1000 --cpu 4 -Z 75585367 HMM pfamseq
#=GF TP   Domain
#=GF CL   CL0125
#=GF RC   Paper describing PDB structure 2ebf
#=GF RN   [1]
#=GF RM   17360394
#=GF RT   Crystal structures reveal a thiol protease-like catalytic triad
#=GF RT   in the C-terminal region of Pasteurella multocida toxin. 
#=GF RA   Kitadokoro K, Kamitani S, Miyazawa M, Hanajima-Ozawa M, Fukui A,
#=GF RA   Miyake M, Horiguchi Y; 
#=GF RL   Proc Natl Acad Sci U S A. 2007;104:5139-5144.
#=GF RC   Paper describing PDB structure 5w6l
#=GF RN   [2]
#=GF RM   30279169
#=GF RT   The bacterial Ras/Rap1 site-specific endopeptidase RRSP cleaves
#=GF RT   Ras through an atypical mechanism to disrupt Ras-ERK signaling.
#=GF RA   Biancucci M, Minasov G, Banerjee A, Herrera A, Woida PJ, Kieffer
#=GF RA   MB, Bindu L, Abreu-Blanco M, Anderson WF, Gaponenko V, Stephen
#=GF RA   AG, Holderfield M, Satchell KJF;
#=GF RL   Sci Signal. 2018; [Epub ahead of print]
#=GF DR   SO; 0000417; polypeptide_domain;
#=GF CC   Pasteurella multocida toxin (PMT) inhibits osteoblastic
#=GF CC   differentiation in mammals and birds. Its N-terminal region
#=GF CC   binds to target cells, while its C-terminal region, with a
#=GF CC   Trojan horse-like shape, carries the intracellularly active
#=GF CC   moiety. The latter consists of three distinct domains: C1
#=GF CC   (Pfam:PF11647), C2 and C3. This entry represents the C-terminal
#=GF CC   catalytic domain C3, which has a Cys-His-Asp triad known to
#=GF CC   perform acyl-hydrolysis such as peptidase activity or an
#=GF CC   acyl-transfer reaction. This domain adopts a typical alpha-beta
#=GF CC   protein fold with seven beta-strands and eight helices. It is
#=GF CC   organised into two subdomains that form the the biologically
#=GF CC   active cleft space [1,2].
#=GF SQ   2
#=GS A0A383TWB5_9FLAO/1092-1270  AC A0A383TWB5.1
#=GS G8X771_FLACA/6-179          AC G8X771.1
A0A383TWB5_9FLAO/1092-1270             .............GKVLGWKTYGGKDYLkPNQSTRRDLFI.KGRDAHQATELLNEIDVLKGHI--ADLATASSGSCASVSAKVLQNLRTLGYNTGRGYSLAYWKKRGNDYFPF-NHTATSVWLQNEEFVVDATHLQFP.HAPEDAEqIIVQRPEDWAEEIASRAEAIRPWLEHGLKGVSVIGYFEPPIYTKPRIL---kq.
G8X771_FLACA/6-179                     lflffikgfsqdp---------------.---CSRFAIVSsNLQTEQQKEELRQYLDRAKDAIK--EFISTNGGACVDVI-RVKMLLSSKGFSVGEGATFAYWKWRYP-QYESFNHTAVTIIFKGKELVLDPTHKQFRgVDPLDED.IICLPAKDWMNELVTRTKGQNPVLDHQLRSGESLYTFVCPECTKPKLS---eqq
#=GC seq_cons                          ................................soRhslh..phpstpQtpELhp.lDhhKstI...-hhossuGuCssV..+Vh..LpohGassGcGhohAYWKhRhs..a...NHTAsolhhpscEhVlDsTHhQF..hsP.Dt-.IIs..scDWhpElsoRscu.pPhL-HtL+uspslhhF.sP.hTKP+l....cQ.
//