#=GF ID OST_P1
#=GF AC PF21618.2
#=GF DE Oligosaccharyl transferase, Peripheral 1 domain
#=GF AU Bateman A;0000-0002-6982-4660
#=GF AU Lazaro Pinto Beatriz;0000-0001-6837-2941
#=GF SE ECOD:EF19587
#=GF GA 27.00 27.00;
#=GF TC 30.10 130.30;
#=GF NC 26.70 19.90;
#=GF BM hmmbuild HMM.ann SEED.ann
#=GF SM hmmsearch -Z 81514348 --cpu 4 -E 1000 HMM pfamseq
#=GF TP Domain
#=GF RC Paper describing PDB structure 2zag
#=GF RN [1]
#=GF RM 18046457
#=GF RT Structure-guided identification of a new catalytic motif of
#=GF RT oligosaccharyltransferase.
#=GF RA Igura M, Maita N, Kamishikiryo J, Yamada M, Obita T, Maenaka K,
#=GF RA Kohda D;
#=GF RL EMBO J. 2008;27:234-243.
#=GF RC Paper describing PDB structure 3vu1
#=GF RN [2]
#=GF RM 23177926
#=GF RT Crystallographic and NMR evidence for flexibility in
#=GF RT oligosaccharyltransferases and its catalytic significance.
#=GF RA Nyirenda J, Matsumoto S, Saitoh T, Maita N, Noda NN, Inagaki F,
#=GF RA Kohda D;
#=GF RL Structure. 2013;21:32-41.
#=GF RC Paper describing PDB structure 5aza
#=GF RN [3]
#=GF RM 26694222
#=GF RT Rational design of crystal contact-free space in protein
#=GF RT crystals for analyzing spatial distribution of motions within
#=GF RT protein molecules.
#=GF RA Matsuoka R, Shimada A, Komuro Y, Sugita Y, Kohda D;
#=GF RL Protein Sci. 2016;25:754-768.
#=GF DR INTERPRO; IPR048858;
#=GF DR SO; 0000417; polypeptide_domain;
#=GF CC This domain is found in Oligosaccharyl transferase from
#=GF CC Pyrococcus furiosus (OST, also known as AglB-L) and similar
#=GF CC archaeal sequences. OST catalyses the co-translational transfer
#=GF CC of an oligosaccharide from a lipid donor to an asparagine
#=GF CC residue in nascent polypeptide chains. This protein is organised
#=GF CC into four regions: a N-terminal half (Pfam:PF02516), the central
#=GF CC core (CC) domain that includes the IS (insert) domain
#=GF CC (Pfam:PF18246) and two peripheral domains, P1 (this entry) and
#=GF CC P2 (Pfam:PF18235). This domain, which consists mainly of
#=GF CC beta-strands, encircles the central core domain [1].
#=GF SQ 4
#=GS AGLB1_PYRFU/726-818 AC Q8U4D2.1
#=GS AGLB1_PYRFU/726-818 DR PDB; 2ZAG C; 726-818;
#=GS AGLB1_PYRFU/726-818 DR PDB; 2ZAI B; 726-818;
#=GS AGLB1_PYRFU/726-818 DR PDB; 2ZAG B; 726-818;
#=GS AGLB1_PYRFU/726-818 DR PDB; 2ZAI D; 726-818;
#=GS AGLB1_PYRFU/726-818 DR PDB; 2ZAG A; 726-818;
#=GS AGLB1_PYRFU/726-818 DR PDB; 2ZAI C; 726-818;
#=GS AGLB1_PYRFU/726-818 DR PDB; 2ZAG D; 726-818;
#=GS AGLB1_PYRFU/726-818 DR PDB; 2ZAI A; 726-818;
#=GS Q5JH70_THEKO/748-856 AC Q5JH70.1
#=GS C6A1I9_THESM/717-809 AC C6A1I9.1
#=GS F0LKR3_THEBM/712-804 AC F0LKR3.1
AGLB1_PYRFU/726-818 PFGIYKIEENINGTWKQVYN...............L.TPGKHELKLYISAFGRDIENATLYIYAINNEKIIEKIKIAEISHMDYLNEYPIAVNVTLPNATSYRFVLVQK
#=GR AGLB1_PYRFU/726-818 SS SEEEEEEEEESSSEEEEESS...............B.-SEEEEEEEEEEE-SS-EEEEEEEEEEESSSCEEEEEEEEEEEEEBTTS--EEEEEEEE-S-SEEEEEEEEE
Q5JH70_THEKO/748-856 PFAIHRIEAMMNGNWTRVYDsinggglevksgnttLpLTGEQKLRLYISAFGRDVKNGTLIFEAYNGTELVDRQVLVKNLNIDHLNETPVEVTVKIPQAEKYRFILLQE
C6A1I9_THESM/717-809 PFGLYRIEIYENNTWKSVSK...............L.IPGNYKARLYISAFGRDVKDAVIKLRAYDGDRIVSEQVIAQNVNINHLNEIPIEVSLEVPNATRYQLVLIQE
F0LKR3_THEBM/712-804 PFVVYKIEVYKNGTWSPIKK...............L.EPGEYKARLYISAFGRDVKDATIKLRAYKNGKLIADETIATNVNIDHLNEKPVEVMLNVPNATKYEIVLIQK
#=GC SS_cons SEEEEEEEEESSSEEEEESS...............B.-SEEEEEEEEEEE-SS-EEEEEEEEEEESSSCEEEEEEEEEEEEEBTTS--EEEEEEEE-S-SEEEEEEEEE
#=GC seq_cons PFulY+IEhhhNGTWppVhc...............L.hPGcaKhRLYISAFGRDVKsATlhlcAYsss+llscpsIApNlNIDHLNEhPlEVslplPNAT+YchVLlQc
//
