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Conserved domains on  [gi|568986509|ref|XP_006518514|]
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annexin A11 isoform X1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Annexin pfam00191
Annexin; This family of annexins also includes giardin that has been shown to function as an ...
202-267 6.72e-30

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


:

Pssm-ID: 395139  Cd Length: 66  Bit Score: 111.41  E-value: 6.72e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568986509  202 RDAEVLRKAMKGFGTDEQAIIDCLGSRSNKQRQQILLSFKTAYGKDLIKDLKSELSGNFEKTILAL 267
Cdd:pfam00191   1 YDAELLRKAMKGLGTDESTLIEILATRSNAQLQAIREAYKKLYGKDLEKDIKSETSGDFEKLLLAL 66
Annexin pfam00191
Annexin; This family of annexins also includes giardin that has been shown to function as an ...
433-498 1.17e-29

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


:

Pssm-ID: 395139  Cd Length: 66  Bit Score: 110.64  E-value: 1.17e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568986509  433 FFAERLNKAMRGAGTKDRTLIRIMVSRSELDLLDIRAEYKRMYGKSLYHDITGDTSGDYRKILLKI 498
Cdd:pfam00191   1 YDAELLRKAMKGLGTDESTLIEILATRSNAQLQAIREAYKKLYGKDLEKDIKSETSGDFEKLLLAL 66
Annexin pfam00191
Annexin; This family of annexins also includes giardin that has been shown to function as an ...
274-339 1.51e-26

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


:

Pssm-ID: 395139  Cd Length: 66  Bit Score: 102.17  E-value: 1.51e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568986509  274 FDVYEIKEAIKGAGTDEACLIEIFASRSNEHIRELSRAYKTEFQKTLEEAIRSDTSGHFQRLLISL 339
Cdd:pfam00191   1 YDAELLRKAMKGLGTDESTLIEILATRSNAQLQAIREAYKKLYGKDLEKDIKSETSGDFEKLLLAL 66
Annexin pfam00191
Annexin; This family of annexins also includes giardin that has been shown to function as an ...
357-423 3.17e-24

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


:

Pssm-ID: 395139  Cd Length: 66  Bit Score: 95.62  E-value: 3.17e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568986509  357 RDVQELYAAgENRLGTDESKFNAILCSRSRAHLVAVFNEYQRMTGRDIEKSICREMSGDLEQGMLAV 423
Cdd:pfam00191   1 YDAELLRKA-MKGLGTDESTLIEILATRSNAQLQAIREAYKKLYGKDLEKDIKSETSGDFEKLLLAL 66
Cornifin super family cl25524
Cornifin (SPRR) family; SPRR genes (formerly SPR) encode a novel class of polypeptides (small ...
120-185 1.17e-06

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.


The actual alignment was detected with superfamily member pfam02389:

Pssm-ID: 280537 [Multi-domain]  Cd Length: 135  Bit Score: 47.74  E-value: 1.17e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568986509  120 PAYPGAPVPGQPMPPTGQQPPGAYPGQPPMTYPGQSPMPPPGQQPVPSypgySGSSTITPAvpPAQ 185
Cdd:pfam02389  72 PCYPKVPEPCSPKVPEPCHPKAPEPCHPKVPEPCYPKAPEPCQPKVPE----PCPSTVTPG--PAQ 131
 
Name Accession Description Interval E-value
Annexin pfam00191
Annexin; This family of annexins also includes giardin that has been shown to function as an ...
202-267 6.72e-30

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


Pssm-ID: 395139  Cd Length: 66  Bit Score: 111.41  E-value: 6.72e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568986509  202 RDAEVLRKAMKGFGTDEQAIIDCLGSRSNKQRQQILLSFKTAYGKDLIKDLKSELSGNFEKTILAL 267
Cdd:pfam00191   1 YDAELLRKAMKGLGTDESTLIEILATRSNAQLQAIREAYKKLYGKDLEKDIKSETSGDFEKLLLAL 66
Annexin pfam00191
Annexin; This family of annexins also includes giardin that has been shown to function as an ...
433-498 1.17e-29

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


Pssm-ID: 395139  Cd Length: 66  Bit Score: 110.64  E-value: 1.17e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568986509  433 FFAERLNKAMRGAGTKDRTLIRIMVSRSELDLLDIRAEYKRMYGKSLYHDITGDTSGDYRKILLKI 498
Cdd:pfam00191   1 YDAELLRKAMKGLGTDESTLIEILATRSNAQLQAIREAYKKLYGKDLEKDIKSETSGDFEKLLLAL 66
Annexin pfam00191
Annexin; This family of annexins also includes giardin that has been shown to function as an ...
274-339 1.51e-26

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


Pssm-ID: 395139  Cd Length: 66  Bit Score: 102.17  E-value: 1.51e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568986509  274 FDVYEIKEAIKGAGTDEACLIEIFASRSNEHIRELSRAYKTEFQKTLEEAIRSDTSGHFQRLLISL 339
Cdd:pfam00191   1 YDAELLRKAMKGLGTDESTLIEILATRSNAQLQAIREAYKKLYGKDLEKDIKSETSGDFEKLLLAL 66
Annexin pfam00191
Annexin; This family of annexins also includes giardin that has been shown to function as an ...
357-423 3.17e-24

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


Pssm-ID: 395139  Cd Length: 66  Bit Score: 95.62  E-value: 3.17e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568986509  357 RDVQELYAAgENRLGTDESKFNAILCSRSRAHLVAVFNEYQRMTGRDIEKSICREMSGDLEQGMLAV 423
Cdd:pfam00191   1 YDAELLRKA-MKGLGTDESTLIEILATRSNAQLQAIREAYKKLYGKDLEKDIKSETSGDFEKLLLAL 66
ANX smart00335
Annexin repeats;
446-496 5.66e-23

Annexin repeats;


Pssm-ID: 197661  Cd Length: 53  Bit Score: 91.70  E-value: 5.66e-23
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 568986509   446 GTKDRTLIRIMVSRSELDLLDIRAEYKRMYGKSLYHDITGDTSGDYRKILL 496
Cdd:smart00335   1 GTDEKTLIEILASRSNAQLQAIKQAYKKRYGKDLEDDIKSETSGDFEKLLL 51
ANX smart00335
Annexin repeats;
215-267 1.87e-22

Annexin repeats;


Pssm-ID: 197661  Cd Length: 53  Bit Score: 90.16  E-value: 1.87e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 568986509   215 GTDEQAIIDCLGSRSNKQRQQILLSFKTAYGKDLIKDLKSELSGNFEKTILAL 267
Cdd:smart00335   1 GTDEKTLIEILASRSNAQLQAIKQAYKKRYGKDLEDDIKSETSGDFEKLLLAL 53
ANX smart00335
Annexin repeats;
287-339 1.84e-21

Annexin repeats;


Pssm-ID: 197661  Cd Length: 53  Bit Score: 87.46  E-value: 1.84e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 568986509   287 GTDEACLIEIFASRSNEHIRELSRAYKTEFQKTLEEAIRSDTSGHFQRLLISL 339
Cdd:smart00335   1 GTDEKTLIEILASRSNAQLQAIKQAYKKRYGKDLEDDIKSETSGDFEKLLLAL 53
ANX smart00335
Annexin repeats;
371-423 1.74e-18

Annexin repeats;


Pssm-ID: 197661  Cd Length: 53  Bit Score: 78.99  E-value: 1.74e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 568986509   371 GTDESKFNAILCSRSRAHLVAVFNEYQRMTGRDIEKSICREMSGDLEQGMLAV 423
Cdd:smart00335   1 GTDEKTLIEILASRSNAQLQAIKQAYKKRYGKDLEDDIKSETSGDFEKLLLAL 53
Cornifin pfam02389
Cornifin (SPRR) family; SPRR genes (formerly SPR) encode a novel class of polypeptides (small ...
120-185 1.17e-06

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.


Pssm-ID: 280537 [Multi-domain]  Cd Length: 135  Bit Score: 47.74  E-value: 1.17e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568986509  120 PAYPGAPVPGQPMPPTGQQPPGAYPGQPPMTYPGQSPMPPPGQQPVPSypgySGSSTITPAvpPAQ 185
Cdd:pfam02389  72 PCYPKVPEPCSPKVPEPCHPKAPEPCHPKVPEPCYPKAPEPCQPKVPE----PCPSTVTPG--PAQ 131
PHA02682 PHA02682
ORF080 virion core protein; Provisional
120-221 1.65e-04

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 43.70  E-value: 1.65e-04
                         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
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
120-169 2.04e-04

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.


Pssm-ID: 197891 [Multi-domain]  Cd Length: 165  Bit Score: 42.08  E-value: 2.04e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 568986509   120 PAYPGAPVPGQ-PMPPTGQQPPGAYPGQPPMTYPgQSPMPPPGQQPVPSYP 169
Cdd:smart00818  69 PQQPLMPVPGQhSMTPTQHHQPNLPQPAQQPFQP-QPLQPPQPQQPMQPQP 118
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
118-190 3.06e-03

PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];


Pssm-ID: 444064 [Multi-domain]  Cd Length: 548  Bit Score: 40.05  E-value: 3.06e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568986509 118 SYPAYPGAPVPGQPMPPTGQQPPGAYPGQPPMTypgqspmpPPGQQPVPSYPGYSGSSTITPAVPPAQFGNRG 190
Cdd:COG5180  353 SAYPPAEEAVPGKPLEQGAPRPGSSGGDGAPFQ--------PPNGAPQPGLGRRGAPGPPMGAGDLVQAALDG 417
 
Name Accession Description Interval E-value
Annexin pfam00191
Annexin; This family of annexins also includes giardin that has been shown to function as an ...
202-267 6.72e-30

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


Pssm-ID: 395139  Cd Length: 66  Bit Score: 111.41  E-value: 6.72e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568986509  202 RDAEVLRKAMKGFGTDEQAIIDCLGSRSNKQRQQILLSFKTAYGKDLIKDLKSELSGNFEKTILAL 267
Cdd:pfam00191   1 YDAELLRKAMKGLGTDESTLIEILATRSNAQLQAIREAYKKLYGKDLEKDIKSETSGDFEKLLLAL 66
Annexin pfam00191
Annexin; This family of annexins also includes giardin that has been shown to function as an ...
433-498 1.17e-29

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


Pssm-ID: 395139  Cd Length: 66  Bit Score: 110.64  E-value: 1.17e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568986509  433 FFAERLNKAMRGAGTKDRTLIRIMVSRSELDLLDIRAEYKRMYGKSLYHDITGDTSGDYRKILLKI 498
Cdd:pfam00191   1 YDAELLRKAMKGLGTDESTLIEILATRSNAQLQAIREAYKKLYGKDLEKDIKSETSGDFEKLLLAL 66
Annexin pfam00191
Annexin; This family of annexins also includes giardin that has been shown to function as an ...
274-339 1.51e-26

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


Pssm-ID: 395139  Cd Length: 66  Bit Score: 102.17  E-value: 1.51e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568986509  274 FDVYEIKEAIKGAGTDEACLIEIFASRSNEHIRELSRAYKTEFQKTLEEAIRSDTSGHFQRLLISL 339
Cdd:pfam00191   1 YDAELLRKAMKGLGTDESTLIEILATRSNAQLQAIREAYKKLYGKDLEKDIKSETSGDFEKLLLAL 66
Annexin pfam00191
Annexin; This family of annexins also includes giardin that has been shown to function as an ...
357-423 3.17e-24

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


Pssm-ID: 395139  Cd Length: 66  Bit Score: 95.62  E-value: 3.17e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568986509  357 RDVQELYAAgENRLGTDESKFNAILCSRSRAHLVAVFNEYQRMTGRDIEKSICREMSGDLEQGMLAV 423
Cdd:pfam00191   1 YDAELLRKA-MKGLGTDESTLIEILATRSNAQLQAIREAYKKLYGKDLEKDIKSETSGDFEKLLLAL 66
ANX smart00335
Annexin repeats;
446-496 5.66e-23

Annexin repeats;


Pssm-ID: 197661  Cd Length: 53  Bit Score: 91.70  E-value: 5.66e-23
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 568986509   446 GTKDRTLIRIMVSRSELDLLDIRAEYKRMYGKSLYHDITGDTSGDYRKILL 496
Cdd:smart00335   1 GTDEKTLIEILASRSNAQLQAIKQAYKKRYGKDLEDDIKSETSGDFEKLLL 51
ANX smart00335
Annexin repeats;
215-267 1.87e-22

Annexin repeats;


Pssm-ID: 197661  Cd Length: 53  Bit Score: 90.16  E-value: 1.87e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 568986509   215 GTDEQAIIDCLGSRSNKQRQQILLSFKTAYGKDLIKDLKSELSGNFEKTILAL 267
Cdd:smart00335   1 GTDEKTLIEILASRSNAQLQAIKQAYKKRYGKDLEDDIKSETSGDFEKLLLAL 53
ANX smart00335
Annexin repeats;
287-339 1.84e-21

Annexin repeats;


Pssm-ID: 197661  Cd Length: 53  Bit Score: 87.46  E-value: 1.84e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 568986509   287 GTDEACLIEIFASRSNEHIRELSRAYKTEFQKTLEEAIRSDTSGHFQRLLISL 339
Cdd:smart00335   1 GTDEKTLIEILASRSNAQLQAIKQAYKKRYGKDLEDDIKSETSGDFEKLLLAL 53
ANX smart00335
Annexin repeats;
371-423 1.74e-18

Annexin repeats;


Pssm-ID: 197661  Cd Length: 53  Bit Score: 78.99  E-value: 1.74e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 568986509   371 GTDESKFNAILCSRSRAHLVAVFNEYQRMTGRDIEKSICREMSGDLEQGMLAV 423
Cdd:smart00335   1 GTDEKTLIEILASRSNAQLQAIKQAYKKRYGKDLEDDIKSETSGDFEKLLLAL 53
Cornifin pfam02389
Cornifin (SPRR) family; SPRR genes (formerly SPR) encode a novel class of polypeptides (small ...
120-185 1.17e-06

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.


Pssm-ID: 280537 [Multi-domain]  Cd Length: 135  Bit Score: 47.74  E-value: 1.17e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568986509  120 PAYPGAPVPGQPMPPTGQQPPGAYPGQPPMTYPGQSPMPPPGQQPVPSypgySGSSTITPAvpPAQ 185
Cdd:pfam02389  72 PCYPKVPEPCSPKVPEPCHPKAPEPCHPKVPEPCYPKAPEPCQPKVPE----PCPSTVTPG--PAQ 131
Cornifin pfam02389
Cornifin (SPRR) family; SPRR genes (formerly SPR) encode a novel class of polypeptides (small ...
120-171 1.31e-05

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.


Pssm-ID: 280537 [Multi-domain]  Cd Length: 135  Bit Score: 45.04  E-value: 1.31e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568986509  120 PAYPGAPVPGQPMPPTGQQPPGAYPGQPPMTYPGQSPMPPPGQQPVPSyPGY 171
Cdd:pfam02389  40 PCCPKVPEPCCPKVPEPCCPKVPEPCCPKVPEPCYPKVPEPCSPKVPE-PCH 90
PHA02682 PHA02682
ORF080 virion core protein; Provisional
120-221 1.65e-04

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 43.70  E-value: 1.65e-04
                         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
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
120-169 2.04e-04

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.


Pssm-ID: 197891 [Multi-domain]  Cd Length: 165  Bit Score: 42.08  E-value: 2.04e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 568986509   120 PAYPGAPVPGQ-PMPPTGQQPPGAYPGQPPMTYPgQSPMPPPGQQPVPSYP 169
Cdd:smart00818  69 PQQPLMPVPGQhSMTPTQHHQPNLPQPAQQPFQP-QPLQPPQPQQPMQPQP 118
FAP pfam07174
Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment ...
120-198 5.01e-04

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.


Pssm-ID: 429334  Cd Length: 301  Bit Score: 42.22  E-value: 5.01e-04
                          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
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
123-185 5.35e-04

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 42.83  E-value: 5.35e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568986509  123 PGAP-VPGQPMPPTGQQPPGAYPGQPPMTYPGQSPMPPPGQQPVPSYPgysgSSTITPAVPPAQ 185
Cdd:pfam03154 201 PSAPsVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQRLPSPHPP----LQPMTQPPPPSQ 260
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
120-166 7.36e-04

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.


Pssm-ID: 197891 [Multi-domain]  Cd Length: 165  Bit Score: 40.16  E-value: 7.36e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 568986509   120 PAYPGAPVPGQPMPPTGQQPPGAyPGQPPMTYPGQSPMPPpgQQPVP 166
Cdd:smart00818  99 PFQPQPLQPPQPQQPMQPQPPVH-PIPPLPPQPPLPPMFP--MQPLP 142
PRK10263 PRK10263
DNA translocase FtsK; Provisional
120-200 1.74e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 41.22  E-value: 1.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568986509  120 PAYPGAPVPGQPMPPtgQQP-------PGAYPGQP-----PMTYPGQS-------PMPPPGQQPVPSYPGYSGSSTITPA 180
Cdd:PRK10263  339 PVTQTPPVASVDVPP--AQPtvawqpvPGPQTGEPviapaPEGYPQQSqyaqpavQYNEPLQQPVQPQQPYYAPAAEQPA 416
                          90       100
                  ....*....|....*....|
gi 568986509  181 VPPAQFGNRGTITAASGFDP 200
Cdd:PRK10263  417 QQPYYAPAPEQPAQQPYYAP 436
Glutenin_hmw pfam03157
High molecular weight glutenin subunit; Members of this family include high molecular weight ...
120-179 1.78e-03

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.


Pssm-ID: 367362 [Multi-domain]  Cd Length: 786  Bit Score: 41.09  E-value: 1.78e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568986509  120 PAYPGAPVPGQpMPPTGQQP----PGAYPGQPPMtyPGQSPMPPPGQQPVPSYPGYSGSSTITP 179
Cdd:pfam03157 571 GQQPGQGQQGQ-QPGQGQQPgqgqPGYYPTSPQQ--SGQGQQPGQWQQPGQGQPGYYPTSSLQL 631
PHA03369 PHA03369
capsid maturational protease; Provisional
121-185 1.99e-03

capsid maturational protease; Provisional


Pssm-ID: 223061 [Multi-domain]  Cd Length: 663  Bit Score: 40.75  E-value: 1.99e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568986509 121 AYPGAPVPGQPMPPTG---QQPPGAYPGQPpmtYPGQSPMPPPGQQPVPSYPGYSGSSTITPAVPPAQ 185
Cdd:PHA03369 362 AAAKVAVIAAPQTHTGpadRQRPQRPDGIP---YSVPARSPMTAYPPVPQFCGDPGLVSPYNPQSPGT 426
PHA03377 PHA03377
EBNA-3C; Provisional
120-182 2.25e-03

EBNA-3C; Provisional


Pssm-ID: 177614 [Multi-domain]  Cd Length: 1000  Bit Score: 40.81  E-value: 2.25e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568986509  120 PAYPGAPVPGQPMPPTGQQPPGAYPGQPPMTYPGQSPMPPPGQQ-PVPSYPGYSGSSTITPAVP 182
Cdd:PHA03377  741 PPSHQAPYSGHEEPQAQQAPYPGYWEPRPPQAPYLGYQEPQAQGvQVSSYPGYAGPWGLRAQHP 804
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
118-190 3.06e-03

PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];


Pssm-ID: 444064 [Multi-domain]  Cd Length: 548  Bit Score: 40.05  E-value: 3.06e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568986509 118 SYPAYPGAPVPGQPMPPTGQQPPGAYPGQPPMTypgqspmpPPGQQPVPSYPGYSGSSTITPAVPPAQFGNRG 190
Cdd:COG5180  353 SAYPPAEEAVPGKPLEQGAPRPGSSGGDGAPFQ--------PPNGAPQPGLGRRGAPGPPMGAGDLVQAALDG 417
PRK13729 PRK13729
conjugal transfer pilus assembly protein TraB; Provisional
124-185 4.36e-03

conjugal transfer pilus assembly protein TraB; Provisional


Pssm-ID: 184281 [Multi-domain]  Cd Length: 475  Bit Score: 39.42  E-value: 4.36e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568986509 124 GAPVPGQPMPPTGQQPpGAYPGQPPMTYPGQSPMPPPGqqPVPSYPGysgSSTITPAVPPAQ 185
Cdd:PRK13729 132 GEPVPQMPASPPGPEG-EPQPGNTPVSFPPQGSVAVPP--PTAFYPG---NGVTPPPQVTYQ 187
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
120-193 5.16e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 39.37  E-value: 5.16e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568986509 120 PAYPGAPVPGQPMPPTGQQPPGAYPGQPPMTYPGQSPMPPPGQQPVPSypgysgSSTITPAVPPAQFGNRGTIT 193
Cdd:PRK14971 392 PSAAAAASPSPSQSSAAAQPSAPQSATQPAGTPPTVSVDPPAAVPVNP------PSTAPQAVRPAQFKEEKKIP 459
DAZAP2 pfam11029
DAZ associated protein 2 (DAZAP2); DAZ associated protein 2 has a highly conserved sequence ...
119-183 5.46e-03

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.


Pssm-ID: 402565 [Multi-domain]  Cd Length: 129  Bit Score: 37.02  E-value: 5.46e-03
                          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
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
124-209 6.59e-03

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 39.22  E-value: 6.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568986509  124 GAPVPGQPMPPtGQQPPGAYPGQPPmtyPGQsPMPPPGQQPVPS---YPGYSGSSTITPAVPPAQFGNRGTITAASGFDP 200
Cdd:pfam09606 392 FMRQSPQPSVP-SPQGPGSQPPQSH---PGG-MIPSPALIPSPSpqmSQQPAQQRTIGQDSPGGSLNTPGQSAVNSPLNP 466

                  ....*....
gi 568986509  201 LRDAEVLRK 209
Cdd:pfam09606 467 QEEQLYREK 475
PHA03247 PHA03247
large tegument protein UL36; Provisional
123-187 7.11e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.15  E-value: 7.11e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568986509  123 PGAPVPGQPMPPTGQQPPGAYPGQP-PMTYPGQSPMPPPgqqPVPSYPGYSGSSTITPAVPPAQFG 187
Cdd:PHA03247 2903 DQPERPPQPQAPPPPQPQPQPPPPPqPQPPPPPPPRPQP---PLAPTTDPAGAGEPSGAVPQPWLG 2965
DUF3824 pfam12868
Domain of unknwon function (DUF3824); This is a repeating domain found in fungal proteins. It ...
118-169 7.54e-03

Domain of unknwon function (DUF3824); This is a repeating domain found in fungal proteins. It is proline-rich, and the function is not known.


Pssm-ID: 372351 [Multi-domain]  Cd Length: 145  Bit Score: 37.03  E-value: 7.54e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568986509  118 SYPAYPGAPVPGQPMPPTGqqpPGAYPGQPPMTYPGQSPMPPPGQQPVPSYP 169
Cdd:pfam12868  88 STPQPPVDPQPNAPPPPYN---PADYPPPPGAAPPPQPYQYPPPPGPDPYAP 136
PHA03378 PHA03378
EBNA-3B; Provisional
120-183 7.77e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 38.89  E-value: 7.77e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568986509 120 PAYPGAPVPGQPMPPTGQQPPGAYPG--QPPMTYPGQspMPPPGQQPVPSYPGYSGSSTITPAVPP 183
Cdd:PHA03378 717 PAAATGRARPPAAAPGRARPPAAAPGraRPPAAAPGR--ARPPAAAPGRARPPAAAPGAPTPQPPP 780
YppG pfam14179
YppG-like protein; The YppG-like protein family includes the B. subtilis YppG protein, which ...
118-167 9.52e-03

YppG-like protein; The YppG-like protein family includes the B. subtilis YppG protein, which is functionally uncharacterized. This family of proteins is found in bacteria. Proteins in this family are typically between 115 and 181 amino acids in length. There are two completely conserved residues (F and G) that may be functionally important.


Pssm-ID: 372950 [Multi-domain]  Cd Length: 101  Bit Score: 35.94  E-value: 9.52e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568986509  118 SYPAYPGAPV--PGQP-MPPtgQQPPGAYPgQPPMTYPGQSPMPPPGQQPvPS 167
Cdd:pfam14179   7 PYPYFSQQVYqqPVQPqYPP--FAPQQYMP-QPPMPYMNPYPKQQPQQQQ-PS 55
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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