|
Name |
Accession |
Description |
Interval |
E-value |
| Auts2 |
pfam15336 |
Autism susceptibility gene 2 protein; Auts2, or FBRSL2, Fibrosin-1-like protein 2, is a family ... |
644-848 |
2.71e-80 |
|
Autism susceptibility gene 2 protein; Auts2, or FBRSL2, Fibrosin-1-like protein 2, is a family of eukaryotic proteins associated both with a susceptibility to autism and with influencing the number of corpora lutea produced by breeding sows.
Pssm-ID: 464656 Cd Length: 217 Bit Score: 262.47 E-value: 2.71e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249172 644 KPGKWCAMHVHIAWQIYHHQQKVKkQMQSDPHKLDFGLKPEFLSRPPGPSLFGAIHHPHDLARPSTLFSAAGAAHPTGTP 723
Cdd:pfam15336 1 KPGKWCAMHVRIAWQIYHHQQKVK-QMQLDPHKLDVGLKLELLSRPPGPGVFGGFPYPHDLARPATLFSATGAAHPSATP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249172 724 FGPPPHHSNFLNPAAHLEPFNRPSTFTGLAAVGGNAFGGLGNPSVTPNSVFGHKDSPSVQNFSNPHEPWNRLHRTPPSFP 803
Cdd:pfam15336 80 FGPSPPHGSFLSPASHLDPFSRPSTFGGLGALSSGAFGGLGSPSLTANSVFGHKEGPPLQGFSSPHDPWNRLHRTPPSFP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1390249172 804 TPPPWLKPGELERSASAAAHDRDRDVDKRD----SSVSKDDKERESVEK 848
Cdd:pfam15336 160 TPPPWPKPGDAERSSSLESHERERDRERERekrdSSVIKDEKDRDSLDK 208
|
|
| PAT1 |
pfam09770 |
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ... |
297-490 |
2.07e-07 |
|
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.
Pssm-ID: 401645 [Multi-domain] Cd Length: 846 Bit Score: 55.43 E-value: 2.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249172 297 PHPQLPQLPSQAQAEPQ--------LQIPSPGPDLVP----------RTEAPPQFPPPSTQPAQGPP-----------EA 347
Cdd:pfam09770 122 SLPQYQYASQQSQQPSKpvrtgyekYKEPEPIPDLQVdaslwgvapkKAAAPAPAPQPAAQPASLPApsrkmmsleevEA 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249172 348 QLQP-APLPQVQQRPPRPQSPSHLLQQTLPPVQSHPssqslsqplsaYNSSSLSLNSLSSRSSTPAKTQPAPPHISHHPS 426
Cdd:pfam09770 202 AMRAqAKKPAQQPAPAPAQPPAAPPAQQAQQQQQFP-----------PQIQQQQQPQQQPQQPQQHPGQGHPVTILQRPQ 270
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249172 427 ASPFPLSLPNHSPLHSFTPTLQPPAHSH------HPNMFAPPTALPPPPPLTsGSLQVPGHPAGSTYSEQ 490
Cdd:pfam09770 271 SPQPDPAQPSIQPQAQQFHQQPPPVPVQptqilqNPNRLSAARVGYPQNPQP-GVQPAPAHQAHRQQGSF 339
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
308-456 |
3.21e-06 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 51.62 E-value: 3.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249172 308 AQAEPQLQIPSpgpdlVPRTEAPPQFPPPSTQPAQGP--PEAQLQPAP--LPQVQQRPPRPQSPSHLLQQTLPPVQSHPS 383
Cdd:PRK10263 335 APVEPVTQTPP-----VASVDVPPAQPTVAWQPVPGPqtGEPVIAPAPegYPQQSQYAQPAVQYNEPLQQPVQPQQPYYA 409
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1390249172 384 SQSLSQPLSAYNSSSLSLNSLSSRSsTPAKTQPAPPHISHHPSASPFPLSLPNHSPLHSFT-PTLQPPAHSHHP 456
Cdd:PRK10263 410 PAAEQPAQQPYYAPAPEQPAQQPYY-APAPEQPVAGNAWQAEEQQSTFAPQSTYQTEQTYQqPAAQEPLYQQPQ 482
|
|
| Amelogenin |
smart00818 |
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ... |
297-378 |
9.43e-03 |
|
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: 38.23 E-value: 9.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249172 297 PHPQLPQLPSQAQAEPQL-QIPSPGPD-LVPRTEAPPQFPPPSTQPAQGPPEAQLQPAPL--PQVQQRPPRPQSPSHLLQ 372
Cdd:smart00818 54 PHHHIPVLPAQQPVVPQQpLMPVPGQHsMTPTQHHQPNLPQPAQQPFQPQPLQPPQPQQPmqPQPPVHPIPPLPPQPPLP 133
|
90
....*....|.
gi 1390249172 373 -----QTLPPV 378
Cdd:smart00818 134 pmfpmQPLPPL 144
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| Auts2 |
pfam15336 |
Autism susceptibility gene 2 protein; Auts2, or FBRSL2, Fibrosin-1-like protein 2, is a family ... |
644-848 |
2.71e-80 |
|
Autism susceptibility gene 2 protein; Auts2, or FBRSL2, Fibrosin-1-like protein 2, is a family of eukaryotic proteins associated both with a susceptibility to autism and with influencing the number of corpora lutea produced by breeding sows.
Pssm-ID: 464656 Cd Length: 217 Bit Score: 262.47 E-value: 2.71e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249172 644 KPGKWCAMHVHIAWQIYHHQQKVKkQMQSDPHKLDFGLKPEFLSRPPGPSLFGAIHHPHDLARPSTLFSAAGAAHPTGTP 723
Cdd:pfam15336 1 KPGKWCAMHVRIAWQIYHHQQKVK-QMQLDPHKLDVGLKLELLSRPPGPGVFGGFPYPHDLARPATLFSATGAAHPSATP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249172 724 FGPPPHHSNFLNPAAHLEPFNRPSTFTGLAAVGGNAFGGLGNPSVTPNSVFGHKDSPSVQNFSNPHEPWNRLHRTPPSFP 803
Cdd:pfam15336 80 FGPSPPHGSFLSPASHLDPFSRPSTFGGLGALSSGAFGGLGSPSLTANSVFGHKEGPPLQGFSSPHDPWNRLHRTPPSFP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1390249172 804 TPPPWLKPGELERSASAAAHDRDRDVDKRD----SSVSKDDKERESVEK 848
Cdd:pfam15336 160 TPPPWPKPGDAERSSSLESHERERDRERERekrdSSVIKDEKDRDSLDK 208
|
|
| PAT1 |
pfam09770 |
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ... |
297-490 |
2.07e-07 |
|
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.
Pssm-ID: 401645 [Multi-domain] Cd Length: 846 Bit Score: 55.43 E-value: 2.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249172 297 PHPQLPQLPSQAQAEPQ--------LQIPSPGPDLVP----------RTEAPPQFPPPSTQPAQGPP-----------EA 347
Cdd:pfam09770 122 SLPQYQYASQQSQQPSKpvrtgyekYKEPEPIPDLQVdaslwgvapkKAAAPAPAPQPAAQPASLPApsrkmmsleevEA 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249172 348 QLQP-APLPQVQQRPPRPQSPSHLLQQTLPPVQSHPssqslsqplsaYNSSSLSLNSLSSRSSTPAKTQPAPPHISHHPS 426
Cdd:pfam09770 202 AMRAqAKKPAQQPAPAPAQPPAAPPAQQAQQQQQFP-----------PQIQQQQQPQQQPQQPQQHPGQGHPVTILQRPQ 270
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249172 427 ASPFPLSLPNHSPLHSFTPTLQPPAHSH------HPNMFAPPTALPPPPPLTsGSLQVPGHPAGSTYSEQ 490
Cdd:pfam09770 271 SPQPDPAQPSIQPQAQQFHQQPPPVPVQptqilqNPNRLSAARVGYPQNPQP-GVQPAPAHQAHRQQGSF 339
|
|
| PAT1 |
pfam09770 |
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ... |
287-426 |
3.68e-07 |
|
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.
Pssm-ID: 401645 [Multi-domain] Cd Length: 846 Bit Score: 54.66 E-value: 3.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249172 287 PVFEPVVLKDPHPQLPQLPSQAQAEPQLQIPSPGPdlvPRTEAPPQFPPPSTQPAQGPPEAQLQPAPLPQVQQRPPRPQS 366
Cdd:pfam09770 222 PAAPPAQQAQQQQQFPPQIQQQQQPQQQPQQPQQH---PGQGHPVTILQRPQSPQPDPAQPSIQPQAQQFHQQPPPVPVQ 298
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249172 367 PSHLLQQtlPPVQSHPSSQSLSQPLSAYNSSSLSLNSLSSRSstpaktQPAPPHISHHPS 426
Cdd:pfam09770 299 PTQILQN--PNRLSAARVGYPQNPQPGVQPAPAHQAHRQQGS------FGRQAPIITHPQ 350
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
308-456 |
3.21e-06 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 51.62 E-value: 3.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249172 308 AQAEPQLQIPSpgpdlVPRTEAPPQFPPPSTQPAQGP--PEAQLQPAP--LPQVQQRPPRPQSPSHLLQQTLPPVQSHPS 383
Cdd:PRK10263 335 APVEPVTQTPP-----VASVDVPPAQPTVAWQPVPGPqtGEPVIAPAPegYPQQSQYAQPAVQYNEPLQQPVQPQQPYYA 409
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1390249172 384 SQSLSQPLSAYNSSSLSLNSLSSRSsTPAKTQPAPPHISHHPSASPFPLSLPNHSPLHSFT-PTLQPPAHSHHP 456
Cdd:PRK10263 410 PAAEQPAQQPYYAPAPEQPAQQPYY-APAPEQPVAGNAWQAEEQQSTFAPQSTYQTEQTYQqPAAQEPLYQQPQ 482
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
286-378 |
4.65e-06 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 51.24 E-value: 4.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249172 286 EPVFEPVVLKDPHPQLPQLPSQAQAEPQLQIPSPGPDLVPRTEAPPQFPPPSTQPAQGPPEAQLQP----APLPQVQQrP 361
Cdd:PRK10263 742 EPLFTPIVEPVQQPQQPVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPqqpvAPQPQYQQ-P 820
|
90
....*....|....*..
gi 1390249172 362 PRPQSPSHLLQQTLPPV 378
Cdd:PRK10263 821 QQPVAPQPQYQQPQQPV 837
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
233-377 |
8.23e-05 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 47.00 E-value: 8.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249172 233 DASSEKLFN-TVLVNKDPELGVGALPEHNQDAGPIVPKiSGLERSQEKSQDCCKEPVFEPVVLKDPHPQLPQLPSQaqae 311
Cdd:PRK10263 738 DGPHEPLFTpIVEPVQQPQQPVAPQQQYQQPQQPVAPQ-PQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVA---- 812
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1390249172 312 PQLQIPSPGPDLVPrteaPPQFPPPSTQPAQGPPEAQLQPAPLPQVQQRP-PRPQSPSHLLQQTLPP 377
Cdd:PRK10263 813 PQPQYQQPQQPVAP----QPQYQQPQQPVAPQPQDTLLHPLLMRNGDSRPlHKPTTPLPSLDLLTPP 875
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
318-431 |
2.29e-04 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 45.85 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249172 318 SPGPDLVPRTEAPPQFPPpSTQPAQGPPEaQLQPAPLPQVQQRPPRPQSPSHLLQQTLPPVQSHPSSQSLSQPLSAYNSS 397
Cdd:PRK10263 730 SPMKALLDDGPHEPLFTP-IVEPVQQPQQ-PVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQP 807
|
90 100 110
....*....|....*....|....*....|....
gi 1390249172 398 SLSLNSLSSRSSTPAKTQPAPPHISHHPSASPFP 431
Cdd:PRK10263 808 QQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQP 841
|
|
| PHA02682 |
PHA02682 |
ORF080 virion core protein; Provisional |
294-379 |
4.84e-04 |
|
ORF080 virion core protein; Provisional
Pssm-ID: 177464 [Multi-domain] Cd Length: 280 Bit Score: 43.70 E-value: 4.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249172 294 LKDPHPQLPQLPSQAQAEPQLQIPSPGPDLV--------PRTEAPPQFPPPSTQPAQGPPEAQLQPAPLPQVQQRPPRPQ 365
Cdd:PHA02682 73 MQRPSGQSPLAPSPACAAPAPACPACAPAAPapavtcpaPAPACPPATAPTCPPPAVCPAPARPAPACPPSTRQCPPAPP 152
|
90 100
....*....|....*....|...
gi 1390249172 366 SPSH---------LLQQTLPPVQ 379
Cdd:PHA02682 153 LPTPkpapaakpiFLHNQLPPPD 175
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
287-627 |
5.90e-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: 44.37 E-value: 5.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249172 287 PVFEPVVLKDPHPQLPQLPSQAQAE-PQLQIPSPGPDLVPRTEAPPQfpPPSTQPAQGPPEAQLQPAPLPQVQ---QRPP 362
Cdd:pfam03154 200 TPSAPSVPPQGSPATSQPPNQTQSTaAPHTLIQQTPTLHPQRLPSPH--PPLQPMTQPPPPSQVSPQPLPQPSlhgQMPP 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249172 363 RPQS----PSHLlQQTLPPVQSHPSSQSLSQPLSAYNSSSLSLNSLSSRSSTPAKTQPAPPHISHHPSASPFPLSLPNHS 438
Cdd:pfam03154 278 MPHSlqtgPSHM-QHPVPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSMPHIK 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249172 439 PLHSfTPTLQPPAHSHHPNmfapptalpppppltsgslqvPGHPAG-STYSEQDILRQELNTRFLASQSADRGASLGPPP 517
Cdd:pfam03154 357 PPPT-TPIPQLPNPQSHKH---------------------PPHLSGpSPFQMNSNLPPPPALKPLSSLSTHHPPSAHPPP 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249172 518 YLRTEFHQHQHQHQHTHQHTHQHTFTPFPHAIPPTAIMPTPAPPMfdkyptkvDPFYRHSLFHSYPPAVsgIPPMIPPTG 597
Cdd:pfam03154 415 LQLMPQSQQLPPPPAQPPVLTQSQSLPPPAASHPPTSGLHQVPSQ--------SPFPQHPFVPGGPPPI--TPPSGPPTS 484
|
330 340 350
....*....|....*....|....*....|
gi 1390249172 598 PFGSLQGAFQPKTSNPIDVAARPGTVPHTL 627
Cdd:pfam03154 485 TSSAMPGIQPPSSASVSSSGPVPAAVSCPL 514
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
299-434 |
6.72e-04 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 43.93 E-value: 6.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249172 299 PQLPQLPSQAQAEPQLQIPSPGPDLVPRTEAPPQFPPPSTQPAQGPPEAQLQPAP---LPQVQQRPPRPQSPSHLLQQTL 375
Cdd:PRK14951 371 EAAAPAEKKTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPvaaPAAAAPAAAPAAAPAAVALAPA 450
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1390249172 376 PPVQShpssqslsqplsaynsSSLSLNSLSSRSSTPAKTQPAPPHISHHPSASPFPLSL 434
Cdd:PRK14951 451 PPAQA----------------APETVAIPVRVAPEPAVASAAPAPAAAPAAARLTPTEE 493
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
296-638 |
1.13e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 43.39 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249172 296 DPHPQLPQLPSQAQAEPQLQIPSPGP--------DLVPRTEAPPQFPPPSTQPA-QGPPEAQLQPAPLPQvQQRPPRPQS 366
Cdd:PHA03247 2550 DPPPPLPPAAPPAAPDRSVPPPRPAPrpsepavtSRARRPDAPPQSARPRAPVDdRGDPRGPAPPSPLPP-DTHAPDPPP 2628
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249172 367 PSHLLQQTLPPVQSHPSSQSLSQPLSAYNSSSLSLNSLSSRSSTPAKTQpAPPHISHHPSASPFPLSLPNHSPLHSFTPT 446
Cdd:PHA03247 2629 PSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQAS-SPPQRPRRRAARPTVGSLTSLADPPPPPPT 2707
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249172 447 LQPPAHSHHPNMFAPPTALPPPPPLTSGSLQvPGHPAGSTYSEQDILRQELNTRFL----ASQSADRGASLGPPPYLRTE 522
Cdd:PHA03247 2708 PEPAPHALVSATPLPPGPAAARQASPALPAA-PAPPAVPAGPATPGGPARPARPPTtagpPAPAPPAAPAAGPPRRLTRP 2786
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249172 523 FHQHQHQHQHTHQHTHQHTFTPFPHAIPPTAIMPTPAPPMFDKYPTKVDPfyrhslfhSYPPAVSGIPPMIPPTGPFGSL 602
Cdd:PHA03247 2787 AVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQP--------TAPPPPPGPPPPSLPLGGSVAP 2858
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1390249172 603 QGAF--QPKTSNPIDVAARPGTVPHTLLQKD--PRLTDPF 638
Cdd:PHA03247 2859 GGDVrrRPPSRSPAAKPAAPARPPVRRLARPavSRSTESF 2898
|
|
| PRK12757 |
PRK12757 |
cell division protein FtsN; Provisional |
300-368 |
2.36e-03 |
|
cell division protein FtsN; Provisional
Pssm-ID: 237191 [Multi-domain] Cd Length: 256 Bit Score: 41.18 E-value: 2.36e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1390249172 300 QLPQLP----SQAQAEPQLQIPSPGPDLVPRTE----APPQFPPPSTQPAQGPPEAQLQPAPLPQVQQRPPRPQSPS 368
Cdd:PRK12757 101 QLSEVPyneqTPQVPRSTVQIQQQAQQQQPPATtaqpQPVTPPRQTTAPVQPQTPAPVRTQPAAPVTQAVEAPKVEA 177
|
|
| Amelogenin |
smart00818 |
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ... |
297-378 |
9.43e-03 |
|
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: 38.23 E-value: 9.43e-03
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....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249172 297 PHPQLPQLPSQAQAEPQL-QIPSPGPD-LVPRTEAPPQFPPPSTQPAQGPPEAQLQPAPL--PQVQQRPPRPQSPSHLLQ 372
Cdd:smart00818 54 PHHHIPVLPAQQPVVPQQpLMPVPGQHsMTPTQHHQPNLPQPAQQPFQPQPLQPPQPQQPmqPQPPVHPIPPLPPQPPLP 133
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90
....*....|.
gi 1390249172 373 -----QTLPPV 378
Cdd:smart00818 134 pmfpmQPLPPL 144
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