#=GF ID   pAdhesive_8
#=GF AC   PF20602.2
#=GF DE   Putative adhesive domain (group 8)
#=GF AU   Monzon V;0000-0001-7125-6212
#=GF AU   Bateman A;0000-0002-6982-4660
#=GF SE   Monzon V
#=GF GA   27.00 27.00;
#=GF TC   28.20 107.10;
#=GF NC   26.00 22.90;
#=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   25331888
#=GF RT   An intramolecular lock facilitates folding and stabilizes the
#=GF RT   tertiary structure  of Streptococcus mutans adhesin P1.
#=GF RA   Heim KP, Crowley PJ, Long JR, Kailasan S, McKenna R, Brady LJ;
#=GF RL   Proc Natl Acad Sci U S A. 2014;111:15746-15751.
#=GF DR   INTERPRO; IPR046767;
#=GF DR   SO; 0000417; polypeptide_domain;
#=GF CC   The structure model of this domain resembles the  C-terminal
#=GF CC   domains of the Streptococcus intermedius  antigen I/II (AgI/II).
#=GF CC   The N-terminal domain of AgI/II  (also called adhesin P1,
#=GF CC   antigen B or PAc) folds towards  the stalk, where it gets locked
#=GF CC   in place [1]. Given that this domain  is found N-terminal to
#=GF CC   repeating stalk domains in bacterial  surface proteins, the
#=GF CC   domain is suggested to have a potential  protein binding
#=GF CC   function.
#=GF SQ   8
#=GS A0A0R2BDG6_SECCO/26-165  AC A0A0R2BDG6.1
#=GS A0A0R2F8T2_9LACO/3-144   AC A0A0R2F8T2.1
#=GS A0A0R1HLQ6_9LACO/27-169  AC A0A0R1HLQ6.1
#=GS A0A1Z5I8V8_9LACO/25-166  AC A0A1Z5I8V8.1
#=GS A0A1S6QI99_9LACO/31-165  AC A0A1S6QI99.1
#=GS J9W466_LENBU/30-163      AC J9W466.1
#=GS C0XGW7_LENH9/31-164      AC C0XGW7.1
#=GS A0A081BHT6_9LACO/28-169  AC A0A081BHT6.1
A0A0R2BDG6_SECCO/26-165             .ALADNVGQFEIHSSKVMDKEGNAVER.VKAGSKQNLVFEMTINNKDGDKAAGSTNVFIPENQMKVLKDKVSAESSIPDAKASLYLSK-.KRNLRLKWSGVNNSAT.FKLEVPVKIGNPMTLTDLPVAVDDATSYTQQMIVLAED.
A0A0R2F8T2_9LACO/3-144              .ALASNTKRIEIQSARLIDKDNTAPAT.VKAGSEHELVVNLTINNKDGDHESGTTQLWVPEQQLTLLEKKATFEPETAADNARLVYEKLsNNQLQLSWQNVTNTAT.FKVELPVRVNHAMTEMQLPIAVGSATDYLQPLTVLNED.
A0A0R1HLQ6_9LACO/27-169             l-ATTSVEPVAINSARLVTSDDQVIGDrVKSGTDANLQLQVTLSPQSGDTDRGRVQIWLPEEQLKIVTDKLPLEVDATTGGGTVEIRRNrQQKLSLNWFNVENTAT.FSVTLPVQLGTPMTRYALPVMIGDATTRLSPLEILAGD.
A0A1Z5I8V8_9LACO/25-166             .ALADDRSRTELSGVQLSDSEGNKLHQ.VKVNETSELEMTVTVNNKDGENAKGGAAMWLPEDQLEVLKDEVKAESAVADTNATLIYERRkKEQPQLKWKNVETTAT.FKLKLPVQFKETMTKMILPVALGTQRAYLQPLTVVKEN.
A0A1S6QI99_9LACO/31-165             .ADTSQTREVSAGNAAIVDDERRMVGG.ARVGDKKKLFFNVLAN---GNEKSGTVNFAYNHDFLEIKKKKYHYAAGDAELTVKID----.GDESTISWQNVDNRQHiFNVELPVEFKKTIESGNLAIQVDGKNTKLPFIQVVPK-a
J9W466_LENBU/30-163                 .ADVISTKEVVVDNAKLIDDKRALVTK.SKVGDSANLAFDMTVG---GLSQAGTVHFDYNADYFKVKKKQFKFSNGDTKVVVDID----.GEESTISWTNAIDKTD.LEVILPVKFNRTVNDRELDFVVDDKKIKLPTLTVLDED.
C0XGW7_LENH9/31-164                 .ADAVSTDEIAVKNAKFVNQHQQFVSN.SKVGDRAQLSFDLTVG---AISKSGAVTFGYDEESLTIKKKRYRYTNGQTVVVVDVD----.GKDSTIHWRNAVGRTN.MEVKLPVKFRRAMNQHRLTVAVDHKLVKLPFLTIVSK-e
A0A081BHT6_9LACO/28-169             l-ANGHRSQVEIESAMLVDKDDRMINQtVREGDDAKLIFNLAITNQSGAEPDGKAELSVPESQLLLKRKKQRFTVSNSEAVLTFEYIRR.TKKYELSWTNVESTTN.FQVELSLTMGTPMEVSQLGIAVGDQEANLQALSIAGKD.
#=GC seq_cons                       .AssssscclplpuA+LlDc-sphlsp.VKsG-cupLhFslTlsspsGsppuGssphhlPE-QLclhKKKh+apsusscssssl-h.+..scc.pLsWpNVpsoss.FcVcLPVchscsMsptpLslAVscppspLpsLoVlscD.
//