#=GF ID   SH3_18
#=GF AC   PF18354.5
#=GF DE   CarS bacterial SH3 domain
#=GF AU   El-Gebali S;0000-0003-1378-5495
#=GF SE   ECOD:EUF05339
#=GF GA   25.00 25.00;
#=GF TC   32.90 32.70;
#=GF NC   24.60 22.20;
#=GF BM   hmmbuild HMM.ann SEED.ann
#=GF SM   hmmsearch -E 1000 -Z 75585367 --cpu 4 HMM pfamseq
#=GF TP   Domain
#=GF CL   CL0010
#=GF RN   [1]
#=GF RM   20410074
#=GF RT   A bacterial antirepressor with SH3 domain topology mimics
#=GF RT   operator DNA in sequestering the repressor DNA recognition
#=GF RT   helix.
#=GF RA   Leon E, Navarro-Aviles G, Santiveri CM, Flores-Flores C, Rico M,
#=GF RA   Gonzalez C, Murillo FJ, Elias-Arnanz M, Jimenez MA, Padmanabhan
#=GF RA   S;
#=GF RL   Nucleic Acids Res. 2010;38:5226-5241.
#=GF DR   INTERPRO; IPR041199;
#=GF DR   SO; 0000417; polypeptide_domain;
#=GF CC   This is an SH3 domain found in antirepressor proteins such as
#=GF CC   CarS from Myxococcus xanthus.  CarS antirepressor recognizes and
#=GF CC   neutralizes its cognate repressors to turn on a photo-inducible
#=GF CC   promoter. CarS physically interacts with the MerR-type
#=GF CC   winged-helix DNA-binding domain of these repressors leading to
#=GF CC   activation of carB operon. Structural studies of CarS from M.
#=GF CC   Xanthus reveals a beta-barrel fold akin to that in SH3 domains.
#=GF CC   However, it diverges from the typical SH3 domain fold in the
#=GF CC   lengths and conformations of the connecting loops. Functional
#=GF CC   analysis reveal that SH3 domain-like fold in the antirepressor
#=GF CC   CasS, mimics operator DNA in sequestering the repressor DNA
#=GF CC   recognition helix to activate transcription [1].
#=GF SQ   10
#=GS A0A2T4VU17_VITXG/1-86    AC A0A2T4VU17.1
#=GS S9QRX5_9DELT/1-85        AC S9QRX5.1
#=GS A0A085W929_9DELT/16-100  AC A0A085W929.1
#=GS E3FPY6_STIAD/1-85        AC E3FPY6.1
#=GS Q1D505_MYXXD/1-85        AC Q1D505.1
#=GS A0A250IND0_9DELT/1-85    AC A0A250IND0.1
#=GS H8MSI7_CORCM/1-85        AC H8MSI7.1
#=GS A0A1E3XBC3_9BACT/16-96   AC A0A1E3XBC3.1
#=GS A0A848L820_9DELT/1-85    AC A0A848L820.1
#=GS A0A0G2ZSG2_9DELT/1-85    AC A0A0G2ZSG2.1
A0A2T4VU17_VITXG/1-86               ....MIQDPSLIVVEDVDGAPVRMGESVKVVSV.SADDsSMDRHFLGRTGVVVALVFDEPRLQ.FPHDPLIQVRV..DGLGEDLFFPEELELAP.........
S9QRX5_9DELT/1-85                   ....MSQQTALIFSHDVEGAPVRIGEPMRIALT.ASEE.SLDKRFLGRWGIVVALVYDDPHRQ.YPHEPLVKVRV..EDLGEDLFFPWELER--ss.......
A0A085W929_9DELT/16-100             ....MIQDPSLIVFEDVNGAPVKMGEAVKIVET.SEDG.SIGRRFLGRTGTVVGLVYDDPEVQ.YPRDPLVRVRV..EGLGEDLFFVGELEPAP.........
E3FPY6_STIAD/1-85                   ....MTRDPSLIVTVDVEGAPVRIGEQVRIVSA.SRED.SIDPRFLGCSGIVVALVFDDPWLQ.YPADPLIRVRV..HGLGEDLFFVRELDGLP.........
Q1D505_MYXXD/1-85                   ....MIQDPSLIICHDVDGAPVRIGAKVKVVPH.SEDG.TISQRFLGQTGIVVGLVFDDPATQ.YPDDPLIQVLV..EGLGEDLFFPEELELAP.........
A0A250IND0_9DELT/1-85               ....MNHDTGLVFLEDVKGAPVRMGEPVRISGS.PLDG.SLDPRFVGHRGVVVGLVYDEPSTQ.YPGDPLIQVRV..EDLGEDLFFARELERSP.........
H8MSI7_CORCM/1-85                   ....MKHDPSLILTEDVDGAPVRMGAAVMIVRT.EADD.SVSERFLGRVGVVVALVFDDPPMQ.YPRDPLIQVRV..AGLGEDLFFAREIVEVP.........
A0A1E3XBC3_9BACT/16-96              pnyt---------FKNIKGAPFKISDKVLVLDNpNNDN.SFNNEFVGKKGHVFYFEYDCGCGQtFPSDPLIGVKFinKKVGE------------ywkeeiqll
A0A848L820_9DELT/1-85               ....MTQDPSLIVCSDVDGAPVRIGEAVRIVSR.SDDG.TISQRFLGHTGVVVALVYDDPTTQ.YPADPLIQVQV..EGLGEDLFFAEELEL--as.......
A0A0G2ZSG2_9DELT/1-85               ....MIQDVTLIVDEDVEGAPVRIGERVKVVSH.SADD.SMNRGFLGQAGVVVALVFDDPDLQ.YPHDPLIQVRV..DDVGEDLFFPEELELGP.........
#=GC seq_cons                       ....MhQDPSLIlscDV-GAPVRIGEsV+IVss.SsDs.SlspRFLG+sGlVVALVaDDPshQ.YPcDPLIQVRV..-GLGEDLFFscELEhsP.........
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