#=GF ID CTD3
#=GF AC PF20395.3
#=GF DE C-terminal domain 3 of the ABC-three component (ABC-3C) systems
#=GF AU Aravind L;0000-0003-0771-253X
#=GF AU Iyer LM;0000-0002-4844-2022
#=GF AU Chuguransky S;0000-0002-0520-0736
#=GF SE Aravind L
#=GF GA 28.00 28.00;
#=GF TC 28.30 204.50;
#=GF NC 27.60 19.70;
#=GF BM hmmbuild HMM.ann SEED.ann
#=GF SM hmmsearch -E 1000 --cpu 4 -Z 81514348 HMM pfamseq
#=GF TP Domain
#=GF RN [1]
#=GF RM 32894288
#=GF RT Comprehensive classification of ABC ATPases and their functional
#=GF RT radiation in nucleoprotein dynamics and biological conflict
#=GF RT systems.
#=GF RA Krishnan A, Burroughs AM, Iyer LM, Aravind L;
#=GF RL Nucleic Acids Res. 2020;48:10045-10075.
#=GF DR INTERPRO; IPR046870;
#=GF DR SO; 0000417; polypeptide_domain;
#=GF CC C-terminal domains (CTDs) of ABC-3C systems, contain distinct
#=GF CC patterns of charged and polar residues and are not yet unifiable
#=GF CC with known domains. These domains are found at the C-terminus of
#=GF CC the effector component of the systems, which are upstream of the
#=GF CC Middle Component and ABC ATPase components on the genome. Due to
#=GF CC the typically large size of these CTDs relative to the actual
#=GF CC effector and MC domains, the CTDs are predicted to serves as the
#=GF CC platform on which the remaining two components assemble.
#=GF CC Therewith, conformational changes transmitted by the ABC
#=GF CC ATPase-mediated detection of invasive elements like DNA viruses
#=GF CC would result in an unfurling and activation of the
#=GF CC CTD-associated effector [1].
#=GF SQ 1
#=GS A0A5C6UP12_9SPHN/266-427 AC A0A5C6UP12.1
A0A5C6UP12_9SPHN/266-427 ELHRFTLRYPQQADFSSSLGSGLQKIRAHLETGNYPSGSLIAGSIISGVDRDPDMNGDDFFTVANALSEGLNTLAFVADLDGSTWQQDPAEAGQMRRGETNVLVWRDPRLSGRAIMRTLQDWALKGAAHPPLQVIARGNPDDVALGPVIPDRKSDISQPPT-e
#=GC seq_cons ELHRFTLRYPQQADFSSSLGSGLQKIRAHLETGNYPSGSLIAGSIISGVDRDPDMNGDDFFTVANALSEGLNTLAFVADLDGSTWQQDPAEAGQMRRGETNVLVWRDPRLSGRAIMRTLQDWALKGAAHPPLQVIARGNPDDVALGPVIPDRKSDISQPPT.E
//