#=GF ID Atg11_middle
#=GF AC PF19697.3
#=GF DE Atg11 middle domain
#=GF AU Chuguransky S;0000-0002-0520-0736
#=GF AU Wood V;0000-0001-6330-7526
#=GF SE UniProt accession O14261
#=GF GA 26.00 26.00;
#=GF TC 26.40 26.40;
#=GF NC 25.50 22.60;
#=GF BM hmmbuild HMM.ann SEED.ann
#=GF SM hmmsearch -Z 75585367 --cpu 4 -E 1000 HMM pfamseq
#=GF TP Domain
#=GF RN [1]
#=GF RM 32909946
#=GF RT Atg1 kinase in fission yeast is activated by Atg11-mediated
#=GF RT dimerization and cis-autophosphorylation.
#=GF RA Pan ZQ, Shao GC, Liu XM, Chen Q, Dong MQ, Du LL;
#=GF RL Elife. 2020; [Epub ahead of print]
#=GF DR INTERPRO; IPR045593;
#=GF DR SO; 0000417; polypeptide_domain;
#=GF CC This domain represents the region comprised between residues 522
#=GF CC and 583 from fission yeast protein Atg11, which is necessary and
#=GF CC sufficient for Atg11 autophagy function and for supporting Atg1
#=GF CC kinase activity as it harbours an Atg1-binding domain at the
#=GF CC N-terminal and a homodimerisation domain at the C-terminal. The
#=GF CC N-terminal part contains the conserved aromatic residues Phe and
#=GF CC Tyr necessary for the direct and specific interaction with the
#=GF CC tMIT domain of Atg1. This interaction is required for the
#=GF CC autophagy function of Atg11. The C-terminal part of this domain,
#=GF CC residues 546-583, is predicted to adopt a coiled-coil
#=GF CC conformation which mediates Atg11 homodimerisation [1]. It seems
#=GF CC to be conserved among Schizosaccharomyces.
#=GF SQ 3
#=GS ATG11_SCHPO/511-589 AC O14261.2
#=GS S9VXW3_SCHCR/519-597 AC S9VXW3.1
#=GS B6K701_SCHJY/519-594 AC B6K701.1
ATG11_SCHPO/511-589 ....APHPPINEQSNSSQPFYRVSPSIVPLNVIRKLTNRKTSFTDS.HILRLQDEVNQLRNELDLVNKRNEDLLIELQGKEEKI...
S9VXW3_SCHCR/519-597 ....PNTPRADVMDDGSQPFYRTSPSIVPLNIIRKFSQRKTSFSEG.LASKYQVEVEQLRHELGEVVKRNSNLSIELNSKKERV...
B6K701_SCHJY/519-594 leks--------KSQGTAPFFEESPSLIPISVIQQLSRGGSNPQESaQIQQLKSEISNLQTQLAQANLRIEEQNGELKSKN---ili
#=GC seq_cons ....sspP.hs.pSsGSQPFYRsSPSIVPLNVIRKLSpRKTSFoES.pIp+LQsEVsQLRsELupVNKRNE-LsIELpSKcE+l...
//