#=GF ID AF2331-like
#=GF AC PF14556.10
#=GF DE AF2331-like protein
#=GF AU Coggill P;0000-0001-5731-1588
#=GF SE CATH:2fdoA00
#=GF GA 27.00 27.00;
#=GF TC 27.40 152.50;
#=GF NC 22.80 19.40;
#=GF BM hmmbuild HMM.ann SEED.ann
#=GF SM hmmsearch -Z 75585367 -E 1000 --cpu 4 HMM pfamseq
#=GF TP Domain
#=GF RN [1]
#=GF RM 19768810
#=GF RT The crystal structure of the AF2331 protein from Archaeoglobus
#=GF RT fulgidus DSM 4304 forms an unusual interdigitated dimer with a
#=GF RT new type of alpha + beta fold.
#=GF RA Wang S, Kirillova O, Chruszcz M, Gront D, Zimmerman MD,
#=GF RA Cymborowski MT, Shumilin IA, Skarina T, Gorodichtchenskaia E,
#=GF RA Savchenko A, Edwards AM, Minor W;
#=GF RL Protein Sci. 2009;18:2410-2419.
#=GF DR INTERPRO; IPR028986;
#=GF DR SO; 0000417; polypeptide_domain;
#=GF CC AF2331-like is a 11-kDa orphan protein of unknown function from
#=GF CC Archaeoglobus fulgidus. The structure consists of an alpha +
#=GF CC beta fold formed by an unusual homodimer, where the two core
#=GF CC beta-sheets are interdigitated, containing strands alternating
#=GF CC from both subunits. AF2331 contains multiple negatively charged
#=GF CC surface clusters and is located on the same operon as the basic
#=GF CC protein AF2330. It is suggested that AF2331 and AF2330 may form
#=GF CC a charge-stabilized complex in vivo, though the role of the
#=GF CC negatively charged surface clusters is not clear.
#=GF SQ 3
#=GS D2RIC1_ARCPA/1-90 AC D2RIC1.1
#=GS F2KSY2_ARCVS/1-93 AC F2KSY2.1
#=GS Y2331_ARCFU/1-90 AC O27953.1
D2RIC1_ARCPA/1-90 MPTYVFNENSFLDFIKKNV-EGKVAVVSSDVLDVDIEEMETH.LGVKKHFVVKFAISADVFKEVDLDKFDEILKYCVVFVESDEL.SEIGKKA
F2KSY2_ARCVS/1-93 MPTYVFDKEGFMKFLEKNLGEDTMVIVSSDVTDIDEASGNSYgLGKRDFYMVTIGVVADVFKEKDVDEFDEKPKYLVVFTSSDELtSEAIEKA
Y2331_ARCFU/1-90 MPAYVFSKESFLKFLEGHLEDDVVVVVSSDVTDFCKKLSESM.VGEKEYCFAEFAFPADIF-DADEDEIDEMMKYAIVFVEKEKL.SEAGRNA
#=GC seq_cons MPTYVFsKESFLKFLEKNLtEDsVVVVSSDVTDlDccpuESa.LGcK-aahVcFAlsADVFKEsDlDEFDEhhKYsVVFVESDEL.SEAG+KA
//
