Annexin; This family of annexins also includes giardin that has been shown to function as an annexin.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568986509  202 RDAEVLRKAMKGFGTDEQAIIDCLGSRSNKQRQQILLSFKTAYGKDLIKDLKSELSGNFEKTILAL 267
Cdd:pfam00191   1 YDAELLRKAMKGLGTDESTLIEILATRSNAQLQAIREAYKKLYGKDLEKDIKSETSGDFEKLLLAL 66

Annexin; This family of annexins also includes giardin that has been shown to function as an annexin.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568986509  274 FDVYEIKEAIKGAGTDEACLIEIFASRSNEHIRELSRAYKTEFQKTLEEAIRSDTSGHFQRLLISL 339
Cdd:pfam00191   1 YDAELLRKAMKGLGTDESTLIEILATRSNAQLQAIREAYKKLYGKDLEKDIKSETSGDFEKLLLAL 66

Cornifin (SPRR) family; SPRR genes (formerly SPR) encode a novel class of polypeptides (small proline rich proteins) that are strongly induced during differentiation of human epidermal keratinocytes in vitro and in vivo. The most characteriztic feature of the SPRR gene family resides in the structure of the central segments of the encoded polypeptides that are built up from tandemly repeated units of either eight (SPRR1 and SPRR3) or nine (SPRR2) amino acids with the general consensus XKXPEPXX where X is any amino acid. In order to avoid bacterial contamination due to the high polar-nature of the HMM the threshold has been set very high.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568986509  120 PAYPGAPVPGQPMPPTGQQPPGAYPGQPPMTYPGQSPMPPPGQQPVPSypgySGSSTITPAvpPAQ 185
Cdd:pfam02389  72 PCYPKVPEPCSPKVPEPCHPKAPEPCHPKVPEPCYPKAPEPCQPKVPE----PCPSTVTPG--PAQ 131

Annexin; This family of annexins also includes giardin that has been shown to function as an annexin.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568986509  202 RDAEVLRKAMKGFGTDEQAIIDCLGSRSNKQRQQILLSFKTAYGKDLIKDLKSELSGNFEKTILAL 267
Cdd:pfam00191   1 YDAELLRKAMKGLGTDESTLIEILATRSNAQLQAIREAYKKLYGKDLEKDIKSETSGDFEKLLLAL 66

Annexin; This family of annexins also includes giardin that has been shown to function as an annexin.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568986509  274 FDVYEIKEAIKGAGTDEACLIEIFASRSNEHIRELSRAYKTEFQKTLEEAIRSDTSGHFQRLLISL 339
Cdd:pfam00191   1 YDAELLRKAMKGLGTDESTLIEILATRSNAQLQAIREAYKKLYGKDLEKDIKSETSGDFEKLLLAL 66

Annexin repeats;

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 568986509   446 GTKDRTLIRIMVSRSELDLLDIRAEYKRMYGKSLYHDITGDTSGDYRKILL 496
Cdd:smart00335   1 GTDEKTLIEILASRSNAQLQAIKQAYKKRYGKDLEDDIKSETSGDFEKLLL 51

Annexin repeats;

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 568986509   287 GTDEACLIEIFASRSNEHIRELSRAYKTEFQKTLEEAIRSDTSGHFQRLLISL 339
Cdd:smart00335   1 GTDEKTLIEILASRSNAQLQAIKQAYKKRYGKDLEDDIKSETSGDFEKLLLAL 53

Cornifin (SPRR) family; SPRR genes (formerly SPR) encode a novel class of polypeptides (small proline rich proteins) that are strongly induced during differentiation of human epidermal keratinocytes in vitro and in vivo. The most characteriztic feature of the SPRR gene family resides in the structure of the central segments of the encoded polypeptides that are built up from tandemly repeated units of either eight (SPRR1 and SPRR3) or nine (SPRR2) amino acids with the general consensus XKXPEPXX where X is any amino acid. In order to avoid bacterial contamination due to the high polar-nature of the HMM the threshold has been set very high.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568986509  120 PAYPGAPVPGQPMPPTGQQPPGAYPGQPPMTYPGQSPMPPPGQQPVPSypgySGSSTITPAvpPAQ 185
Cdd:pfam02389  72 PCYPKVPEPCSPKVPEPCHPKAPEPCHPKVPEPCYPKAPEPCQPKVPE----PCPSTVTPG--PAQ 131

Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem to regulate formation of crystallites during the secretory stage of tooth enamel development and are thought to play a major role in the structural organisation and mineralisation of developing enamel. The extracellular matrix of the developing enamel comprises two major classes of protein: the hydrophobic amelogenins and the acidic enamelins. Circular dichroism studies of porcine amelogenin have shown that the protein consists of 3 discrete folding units: the N-terminal region appears to contain beta-strand structures, while the C-terminal region displays characteristics of a random coil conformation. Subsequent studies on the bovine protein have indicated the amelogenin structure to contain a repetitive beta-turn segment and a "beta-spiral" between Gln112 and Leu138, which sequester a (Pro, Leu, Gln) rich region. The beta-spiral offers a probable site for interactions with Ca2+ ions. Muatations in the human amelogenin gene (AMGX) cause X-linked hypoplastic amelogenesis imperfecta, a disease characterised by defective enamel. A 9bp deletion in exon 2 of AMGX results in the loss of codons for Ile5, Leu6, Phe7 and Ala8, and replacement by a new threonine codon, disrupting the 16-residue (Met1-Ala16) amelogenin signal peptide.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 568986509   120 PAYPGAPVPGQ-PMPPTGQQPPGAYPGQPPMTYPgQSPMPPPGQQPVPSYP 169
Cdd:smart00818  69 PQQPLMPVPGQhSMTPTQHHQPNLPQPAQQPFQP-QPLQPPQPQQPMQPQP 118

Annexin; This family of annexins also includes giardin that has been shown to function as an annexin.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568986509  202 RDAEVLRKAMKGFGTDEQAIIDCLGSRSNKQRQQILLSFKTAYGKDLIKDLKSELSGNFEKTILAL 267
Cdd:pfam00191   1 YDAELLRKAMKGLGTDESTLIEILATRSNAQLQAIREAYKKLYGKDLEKDIKSETSGDFEKLLLAL 66

Annexin; This family of annexins also includes giardin that has been shown to function as an annexin.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568986509  274 FDVYEIKEAIKGAGTDEACLIEIFASRSNEHIRELSRAYKTEFQKTLEEAIRSDTSGHFQRLLISL 339
Cdd:pfam00191   1 YDAELLRKAMKGLGTDESTLIEILATRSNAQLQAIREAYKKLYGKDLEKDIKSETSGDFEKLLLAL 66

Annexin repeats;

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 568986509   446 GTKDRTLIRIMVSRSELDLLDIRAEYKRMYGKSLYHDITGDTSGDYRKILL 496
Cdd:smart00335   1 GTDEKTLIEILASRSNAQLQAIKQAYKKRYGKDLEDDIKSETSGDFEKLLL 51

Annexin repeats;

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 568986509   287 GTDEACLIEIFASRSNEHIRELSRAYKTEFQKTLEEAIRSDTSGHFQRLLISL 339
Cdd:smart00335   1 GTDEKTLIEILASRSNAQLQAIKQAYKKRYGKDLEDDIKSETSGDFEKLLLAL 53

Cornifin (SPRR) family; SPRR genes (formerly SPR) encode a novel class of polypeptides (small proline rich proteins) that are strongly induced during differentiation of human epidermal keratinocytes in vitro and in vivo. The most characteriztic feature of the SPRR gene family resides in the structure of the central segments of the encoded polypeptides that are built up from tandemly repeated units of either eight (SPRR1 and SPRR3) or nine (SPRR2) amino acids with the general consensus XKXPEPXX where X is any amino acid. In order to avoid bacterial contamination due to the high polar-nature of the HMM the threshold has been set very high.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568986509  120 PAYPGAPVPGQPMPPTGQQPPGAYPGQPPMTYPGQSPMPPPGQQPVPSypgySGSSTITPAvpPAQ 185
Cdd:pfam02389  72 PCYPKVPEPCSPKVPEPCHPKAPEPCHPKVPEPCYPKAPEPCQPKVPE----PCPSTVTPG--PAQ 131

ORF080 virion core protein; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568986509 120 PAYPGAPVPGQPMPPTGQQPPGAYPGQPPMTY--PGQSPMPPPgqQPVPSypgySGSSTITPAVPPAQF--GNRGTITAA 195
Cdd:PHA02682 114 PACPPATAPTCPPPAVCPAPARPAPACPPSTRqcPPAPPLPTP--KPAPA----AKPIFLHNQLPPPDYpaASCPTIETA 187

                         90       100
                 ....*....|....*....|....*.
gi 568986509 196 SGFDPLRDAEVLRKAMKGFGTDEQAI 221
Cdd:PHA02682 188 PAASPVLEPRIPDKIIDADNDDKDLI 213

Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment proteins (FAP). Family members are rich in alanine and proline, are approximately 300 long, and seem to be restricted to mycobacteria. These proteins contain a fibronectin-binding motif that allows mycobacteria to bind to fibronectin in the extracellular matrix.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568986509  120 PAYPGA-PVPGQPMPPTGQQPPGAYPGQPPMTYPGQSPMPPPGQQPVPSYPGYSGSSTITPAV------PPAQFGN---R 189
Cdd:pfam07174  34 PAVAHAdPEPAPPPPSTATAPPAPPPPPPAPAAPAPPPPPAAPNAPNAPPPPADPNAPPPPPAdpnappPPAVDPNapeP 113

                          90
                  ....*....|
gi 568986509  190 GTIT-AASGF 198
Cdd:pfam07174 114 GRIDnAVGGF 123

Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem to regulate formation of crystallites during the secretory stage of tooth enamel development and are thought to play a major role in the structural organisation and mineralisation of developing enamel. The extracellular matrix of the developing enamel comprises two major classes of protein: the hydrophobic amelogenins and the acidic enamelins. Circular dichroism studies of porcine amelogenin have shown that the protein consists of 3 discrete folding units: the N-terminal region appears to contain beta-strand structures, while the C-terminal region displays characteristics of a random coil conformation. Subsequent studies on the bovine protein have indicated the amelogenin structure to contain a repetitive beta-turn segment and a "beta-spiral" between Gln112 and Leu138, which sequester a (Pro, Leu, Gln) rich region. The beta-spiral offers a probable site for interactions with Ca2+ ions. Muatations in the human amelogenin gene (AMGX) cause X-linked hypoplastic amelogenesis imperfecta, a disease characterised by defective enamel. A 9bp deletion in exon 2 of AMGX results in the loss of codons for Ile5, Leu6, Phe7 and Ala8, and replacement by a new threonine codon, disrupting the 16-residue (Met1-Ala16) amelogenin signal peptide.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 568986509   120 PAYPGAPVPGQPMPPTGQQPPGAyPGQPPMTYPGQSPMPPpgQQPVP 166
Cdd:smart00818  99 PFQPQPLQPPQPQQPMQPQPPVH-PIPPLPPQPPLPPMFP--MQPLP 142

High molecular weight glutenin subunit; Members of this family include high molecular weight subunits of glutenin. This group of gluten proteins is thought to be largely responsible for the elastic properties of gluten, and hence, doughs. Indeed, glutenin high molecular weight subunits are classified as elastomeric proteins, because the glutenin network can withstand significant deformations without breaking, and return to the original conformation when the stress is removed. Elastomeric proteins differ considerably in amino acid sequence, but they are all polymers whose subunits consist of elastomeric domains, composed of repeated motifs, and non-elastic domains that mediate cross-linking between the subunits. The elastomeric domain motifs are all rich in glycine residues in addition to other hydrophobic residues. High molecular weight glutenin subunits have an extensive central elastomeric domain, flanked by two terminal non-elastic domains that form disulphide cross-links. The central elastomeric domain is characterized by the following three repeated motifs: PGQGQQ, GYYPTS[P/L]QQ, GQQ. It possesses overlapping beta-turns within and between the repeated motifs, and assumes a regular helical secondary structure with a diameter of approx. 1.9 nm and a pitch of approx. 1.5 nm.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568986509  120 PAYPGAPVPGQpMPPTGQQP----PGAYPGQPPMtyPGQSPMPPPGQQPVPSYPGYSGSSTITP 179
Cdd:pfam03157 571 GQQPGQGQQGQ-QPGQGQQPgqgqPGYYPTSPQQ--SGQGQQPGQWQQPGQGQPGYYPTSSLQL 631

EBNA-3C; Provisional

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568986509  120 PAYPGAPVPGQPMPPTGQQPPGAYPGQPPMTYPGQSPMPPPGQQ-PVPSYPGYSGSSTITPAVP 182
Cdd:PHA03377  741 PPSHQAPYSGHEEPQAQQAPYPGYWEPRPPQAPYLGYQEPQAQGvQVSSYPGYAGPWGLRAQHP 804

conjugal transfer pilus assembly protein TraB; Provisional

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568986509 124 GAPVPGQPMPPTGQQPpGAYPGQPPMTYPGQSPMPPPGqqPVPSYPGysgSSTITPAVPPAQ 185
Cdd:PRK13729 132 GEPVPQMPASPPGPEG-EPQPGNTPVSFPPQGSVAVPP--PTAFYPG---NGVTPPPQVTYQ 187

DAZ associated protein 2 (DAZAP2); DAZ associated protein 2 has a highly conserved sequence throughout evolution including a conserved polyproline region and several SH2/SH3 binding sites. It occurs as a single copy gene with a four-exon organization and is located on chromosome 12. It encodes a ubiquitously expressed protein and binds to DAZ and DAZL1 through DAZ repeats.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568986509  119 YPAYP------GAPVPGQPMPPTGQQPP--GAYPGQ---PPMTYPGQSP----MPPPGQQPVPSYPGYSGS--------S 175
Cdd:pfam11029   1 YPDAPpaysqlYQPRYAHPPYAASVAPSmsAAYPPAqayPPMAQMASPPpmayQPPGPAQPPGQTVVVPGGfdagarfgA 80

                  ....*...
gi 568986509  176 TITPAVPP 183
Cdd:pfam11029  81 GSQPSIPP 88

large tegument protein UL36; Provisional

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568986509  123 PGAPVPGQPMPPTGQQPPGAYPGQP-PMTYPGQSPMPPPgqqPVPSYPGYSGSSTITPAVPPAQFG 187
Cdd:PHA03247 2903 DQPERPPQPQAPPPPQPQPQPPPPPqPQPPPPPPPRPQP---PLAPTTDPAGAGEPSGAVPQPWLG 2965

EBNA-3B; Provisional

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568986509 120 PAYPGAPVPGQPMPPTGQQPPGAYPG--QPPMTYPGQspMPPPGQQPVPSYPGYSGSSTITPAVPP 183
Cdd:PHA03378 717 PAAATGRARPPAAAPGRARPPAAAPGraRPPAAAPGR--ARPPAAAPGRARPPAAAPGAPTPQPPP 780