|
Name |
Accession |
Description |
Interval |
E-value |
| CHRD |
smart00754 |
A domain in the BMP inhibitor chordin and in microbial proteins; |
559-673 |
3.68e-28 |
|
A domain in the BMP inhibitor chordin and in microbial proteins; :
Pssm-ID: 214804 Cd Length: 118 Bit Score: 109.36 E-value: 3.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593363 559 DTLPVPLAGALVLPPVKSQAAGHAWLSLDTHCHLHYEVLLAGLGGSEQgtvTAHL-LGPPGTPGP--RRLLKGF--YGSE 633
Cdd:smart00754 1 ETFSALLTGSQEVPPVNTGAVGGAWFTLDDDGSLHYQVTLSGLSGPET---AAHIhEGEIGTNGPvvRIPLPNPtsREGP 77
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2462593363 634 AQGVVKDLEPELLRHLAKGMASLMITTKGSPRGELRGQVH 673
Cdd:smart00754 78 FAGSVKTLTDEELRQLLAGNLYVNVHTKANPGGEIRGQVA 117
|
|
| CHRD |
smart00754 |
A domain in the BMP inhibitor chordin and in microbial proteins; |
431-548 |
6.43e-26 |
|
A domain in the BMP inhibitor chordin and in microbial proteins; :
Pssm-ID: 214804 Cd Length: 118 Bit Score: 103.19 E-value: 6.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593363 431 DVLQSVLCGADALIPVQTGAAGSASLTLLGNGSLIYQVQVVGTSSEVVAMTLETKPQRRD---QRTVLCHMaglQPGGHT 507
Cdd:smart00754 1 ETFSALLTGSQEVPPVNTGAVGGAWFTLDDDGSLHYQVTLSGLSGPETAAHIHEGEIGTNgpvVRIPLPNP---TSREGP 77
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2462593363 508 AVGICPGLGARGAHMLLQNELFLNVGTKDFPDGELRGHVAA 548
Cdd:smart00754 78 FAGSVKTLTDEELRQLLAGNLYVNVHTKANPGGEIRGQVAK 118
|
|
| CHRD |
smart00754 |
A domain in the BMP inhibitor chordin and in microbial proteins; |
170-274 |
4.01e-18 |
|
A domain in the BMP inhibitor chordin and in microbial proteins; :
Pssm-ID: 214804 Cd Length: 118 Bit Score: 80.85 E-value: 4.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593363 170 TDFVALLTG------PRSQAVARARVSLL-RSSLRFSISYRRLDRPTR-----IRFSDSNGSVLFEHPAAPT-QDGLVCG 236
Cdd:smart00754 1 ETFSALLTGsqevppVNTGAVGGAWFTLDdDGSLHYQVTLSGLSGPETaahihEGEIGTNGPVVRIPLPNPTsREGPFAG 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 2462593363 237 VWRAVPRLSLRLLRAEQLHVALVTLTHPSGEVWGPLIR 274
Cdd:smart00754 81 SVKTLTDEELRQLLAGNLYVNVHTKANPGGEIRGQVAK 118
|
|
| CHRD |
smart00754 |
A domain in the BMP inhibitor chordin and in microbial proteins; |
281-426 |
1.61e-16 |
|
A domain in the BMP inhibitor chordin and in microbial proteins; :
Pssm-ID: 214804 Cd Length: 118 Bit Score: 76.23 E-value: 1.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593363 281 ETFSAILTLE---GPPQQGVGGITLLTLsDTEDSLHFLLLFRGLLEPrsggkwdggktrekvrestclrkahmcglagLT 357
Cdd:smart00754 1 ETFSALLTGSqevPPVNTGAVGGAWFTL-DDDGSLHYQVTLSGLSGP-------------------------------ET 48
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593363 358 QVPLRL-QILHQGQLLRELQANVSAQEPGFAEVLPNLTVQEMDWLVLGELQMALEWAGRPGLRISGHIAA 426
Cdd:smart00754 49 AAHIHEgEIGTNGPVVRIPLPNPTSREGPFAGSVKTLTDEELRQLLAGNLYVNVHTKANPGGEIRGQVAK 118
|
|
| VWC |
pfam00093 |
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ... |
51-125 |
9.85e-08 |
|
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with pfam00094. :
Pssm-ID: 278520 Cd Length: 57 Bit Score: 49.35 E-value: 9.85e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462593363 51 CTFGGKVYALDETWHPDLgepfgvmrCVLCACEapqwgrrtrgPGRVSCKNIKpeCPTPACGQPR--QLPGHCCQTC 125
Cdd:pfam00093 1 CVQNGVVYENGETWKPDL--------CTICTCD----------DGKVLCDKII--CPPLDCPNPRleIPPGECCPVC 57
|
|
| VWC super family |
cl17735 |
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ... |
732-789 |
2.25e-06 |
|
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with pfam00094. The actual alignment was detected with superfamily member pfam00093:
Pssm-ID: 450195 Cd Length: 57 Bit Score: 45.49 E-value: 2.25e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593363 732 CFFEGQQRPHGARWAPNydpLCSLCTCQRRTVICDPVVCPPPSCPHP--VQAPDQCCPVC 789
Cdd:pfam00093 1 CVQNGVVYENGETWKPD---LCTICTCDDGKVLCDKIICPPLDCPNPrlEIPPGECCPVC 57
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| CHRD |
smart00754 |
A domain in the BMP inhibitor chordin and in microbial proteins; |
559-673 |
3.68e-28 |
|
A domain in the BMP inhibitor chordin and in microbial proteins;
Pssm-ID: 214804 Cd Length: 118 Bit Score: 109.36 E-value: 3.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593363 559 DTLPVPLAGALVLPPVKSQAAGHAWLSLDTHCHLHYEVLLAGLGGSEQgtvTAHL-LGPPGTPGP--RRLLKGF--YGSE 633
Cdd:smart00754 1 ETFSALLTGSQEVPPVNTGAVGGAWFTLDDDGSLHYQVTLSGLSGPET---AAHIhEGEIGTNGPvvRIPLPNPtsREGP 77
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2462593363 634 AQGVVKDLEPELLRHLAKGMASLMITTKGSPRGELRGQVH 673
Cdd:smart00754 78 FAGSVKTLTDEELRQLLAGNLYVNVHTKANPGGEIRGQVA 117
|
|
| CHRD |
smart00754 |
A domain in the BMP inhibitor chordin and in microbial proteins; |
431-548 |
6.43e-26 |
|
A domain in the BMP inhibitor chordin and in microbial proteins;
Pssm-ID: 214804 Cd Length: 118 Bit Score: 103.19 E-value: 6.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593363 431 DVLQSVLCGADALIPVQTGAAGSASLTLLGNGSLIYQVQVVGTSSEVVAMTLETKPQRRD---QRTVLCHMaglQPGGHT 507
Cdd:smart00754 1 ETFSALLTGSQEVPPVNTGAVGGAWFTLDDDGSLHYQVTLSGLSGPETAAHIHEGEIGTNgpvVRIPLPNP---TSREGP 77
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2462593363 508 AVGICPGLGARGAHMLLQNELFLNVGTKDFPDGELRGHVAA 548
Cdd:smart00754 78 FAGSVKTLTDEELRQLLAGNLYVNVHTKANPGGEIRGQVAK 118
|
|
| CHRD |
smart00754 |
A domain in the BMP inhibitor chordin and in microbial proteins; |
170-274 |
4.01e-18 |
|
A domain in the BMP inhibitor chordin and in microbial proteins;
Pssm-ID: 214804 Cd Length: 118 Bit Score: 80.85 E-value: 4.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593363 170 TDFVALLTG------PRSQAVARARVSLL-RSSLRFSISYRRLDRPTR-----IRFSDSNGSVLFEHPAAPT-QDGLVCG 236
Cdd:smart00754 1 ETFSALLTGsqevppVNTGAVGGAWFTLDdDGSLHYQVTLSGLSGPETaahihEGEIGTNGPVVRIPLPNPTsREGPFAG 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 2462593363 237 VWRAVPRLSLRLLRAEQLHVALVTLTHPSGEVWGPLIR 274
Cdd:smart00754 81 SVKTLTDEELRQLLAGNLYVNVHTKANPGGEIRGQVAK 118
|
|
| CHRD |
smart00754 |
A domain in the BMP inhibitor chordin and in microbial proteins; |
281-426 |
1.61e-16 |
|
A domain in the BMP inhibitor chordin and in microbial proteins;
Pssm-ID: 214804 Cd Length: 118 Bit Score: 76.23 E-value: 1.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593363 281 ETFSAILTLE---GPPQQGVGGITLLTLsDTEDSLHFLLLFRGLLEPrsggkwdggktrekvrestclrkahmcglagLT 357
Cdd:smart00754 1 ETFSALLTGSqevPPVNTGAVGGAWFTL-DDDGSLHYQVTLSGLSGP-------------------------------ET 48
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593363 358 QVPLRL-QILHQGQLLRELQANVSAQEPGFAEVLPNLTVQEMDWLVLGELQMALEWAGRPGLRISGHIAA 426
Cdd:smart00754 49 AAHIHEgEIGTNGPVVRIPLPNPTSREGPFAGSVKTLTDEELRQLLAGNLYVNVHTKANPGGEIRGQVAK 118
|
|
| CHRD |
pfam07452 |
CHRD domain; CHRD (after SWISS-PROT abbreviation for chordin) is a novel domain identified in ... |
561-672 |
1.23e-14 |
|
CHRD domain; CHRD (after SWISS-PROT abbreviation for chordin) is a novel domain identified in chordin, an inhibitor of bone morphogenetic proteins. This family includes bacterial homologs. It is anticipated to have an immunoglobulin-like beta-barrel structure based on limited similarity to superoxide dismutases but, as yet, no clear functional prediction can be made. Its most conserved feature is a GE[I/L]RCG[V/I/L] motif towards its C-terminal end Most bacterial proteins in this family have only one CHRD domain, whereas it is found repeated in many eukaryotic proteins such as human chordin and Drosophila SOG..
Pssm-ID: 462167 Cd Length: 118 Bit Score: 70.97 E-value: 1.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593363 561 LPVPLAGALVLPP-VKSQAAGHAWLSLDTHCH-LHYEVLLAGLggseQGTVTAHL-LGPPGTPGPrrLLKGFYG------ 631
Cdd:pfam07452 1 FSALLTGAQEVPPpVTTGAGGTAVLTLDDTENtLHYTLTFSGL----SVPTAAHIhAGAAGFNGP--VVVPLEGgprktt 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2462593363 632 -SEAQGVVKDLEPELLRHL--AKGMASLMITTKGSPRGELRGQV 672
Cdd:pfam07452 75 lLAVPEGLATLTAAQLAALlaQQGELYVNVHTEGNPGGEIRGQI 118
|
|
| CHRD |
pfam07452 |
CHRD domain; CHRD (after SWISS-PROT abbreviation for chordin) is a novel domain identified in ... |
433-546 |
2.23e-12 |
|
CHRD domain; CHRD (after SWISS-PROT abbreviation for chordin) is a novel domain identified in chordin, an inhibitor of bone morphogenetic proteins. This family includes bacterial homologs. It is anticipated to have an immunoglobulin-like beta-barrel structure based on limited similarity to superoxide dismutases but, as yet, no clear functional prediction can be made. Its most conserved feature is a GE[I/L]RCG[V/I/L] motif towards its C-terminal end Most bacterial proteins in this family have only one CHRD domain, whereas it is found repeated in many eukaryotic proteins such as human chordin and Drosophila SOG..
Pssm-ID: 462167 Cd Length: 118 Bit Score: 64.42 E-value: 2.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593363 433 LQSVLCGADALIP-VQTGAAGSASLTL-LGNGSLIYQVQVVGTS--------------SEVVAMTLETKPQRRDqrtvlc 496
Cdd:pfam07452 1 FSALLTGAQEVPPpVTTGAGGTAVLTLdDTENTLHYTLTFSGLSvptaahihagaagfNGPVVVPLEGGPRKTT------ 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2462593363 497 hmaglqpgGHTAVGICPGLGARGAHMLLQN--ELFLNVGTKDFPDGELRGHV 546
Cdd:pfam07452 75 --------LLAVPEGLATLTAAQLAALLAQqgELYVNVHTEGNPGGEIRGQI 118
|
|
| VWC |
pfam00093 |
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ... |
51-125 |
9.85e-08 |
|
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with pfam00094.
Pssm-ID: 278520 Cd Length: 57 Bit Score: 49.35 E-value: 9.85e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462593363 51 CTFGGKVYALDETWHPDLgepfgvmrCVLCACEapqwgrrtrgPGRVSCKNIKpeCPTPACGQPR--QLPGHCCQTC 125
Cdd:pfam00093 1 CVQNGVVYENGETWKPDL--------CTICTCD----------DGKVLCDKII--CPPLDCPNPRleIPPGECCPVC 57
|
|
| CHRD |
pfam07452 |
CHRD domain; CHRD (after SWISS-PROT abbreviation for chordin) is a novel domain identified in ... |
283-424 |
2.51e-07 |
|
CHRD domain; CHRD (after SWISS-PROT abbreviation for chordin) is a novel domain identified in chordin, an inhibitor of bone morphogenetic proteins. This family includes bacterial homologs. It is anticipated to have an immunoglobulin-like beta-barrel structure based on limited similarity to superoxide dismutases but, as yet, no clear functional prediction can be made. Its most conserved feature is a GE[I/L]RCG[V/I/L] motif towards its C-terminal end Most bacterial proteins in this family have only one CHRD domain, whereas it is found repeated in many eukaryotic proteins such as human chordin and Drosophila SOG..
Pssm-ID: 462167 Cd Length: 118 Bit Score: 50.17 E-value: 2.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593363 283 FSAILT--LEGPP--QQGVGGITLLTLSDTEDSLHFLLLFRGLLEPRSggkwdggktrekvrestclrkAH-MCGLAGLT 357
Cdd:pfam07452 1 FSALLTgaQEVPPpvTTGAGGTAVLTLDDTENTLHYTLTFSGLSVPTA---------------------AHiHAGAAGFN 59
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462593363 358 QVPLRlqILHQGQLLRELQANVSAQEPGFAEVLPNLTVQEmdwlvlGELQMALEWAGRPGLRISGHI 424
Cdd:pfam07452 60 GPVVV--PLEGGPRKTTLLAVPEGLATLTAAQLAALLAQQ------GELYVNVHTEGNPGGEIRGQI 118
|
|
| VWC |
pfam00093 |
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ... |
732-789 |
2.25e-06 |
|
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with pfam00094.
Pssm-ID: 278520 Cd Length: 57 Bit Score: 45.49 E-value: 2.25e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593363 732 CFFEGQQRPHGARWAPNydpLCSLCTCQRRTVICDPVVCPPPSCPHP--VQAPDQCCPVC 789
Cdd:pfam00093 1 CVQNGVVYENGETWKPD---LCTICTCDDGKVLCDKIICPPLDCPNPrlEIPPGECCPVC 57
|
|
| VWC |
smart00214 |
von Willebrand factor (vWF) type C domain; |
732-789 |
6.13e-04 |
|
von Willebrand factor (vWF) type C domain;
Pssm-ID: 214564 Cd Length: 59 Bit Score: 38.65 E-value: 6.13e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462593363 732 CFFEGQQRPHGARWAPNYdplCSLCTCQRRTVI-CDPVVCPPPSC-PHP--VQAPDQCCPVC 789
Cdd:smart00214 1 CVHNGRVYNDGETWKPDP---CQICTCLDGTTVlCDPVECPPPPDcPNPerVKPPGECCPRC 59
|
|
| CHRD |
pfam07452 |
CHRD domain; CHRD (after SWISS-PROT abbreviation for chordin) is a novel domain identified in ... |
172-272 |
3.17e-03 |
|
CHRD domain; CHRD (after SWISS-PROT abbreviation for chordin) is a novel domain identified in chordin, an inhibitor of bone morphogenetic proteins. This family includes bacterial homologs. It is anticipated to have an immunoglobulin-like beta-barrel structure based on limited similarity to superoxide dismutases but, as yet, no clear functional prediction can be made. Its most conserved feature is a GE[I/L]RCG[V/I/L] motif towards its C-terminal end Most bacterial proteins in this family have only one CHRD domain, whereas it is found repeated in many eukaryotic proteins such as human chordin and Drosophila SOG..
Pssm-ID: 462167 Cd Length: 118 Bit Score: 38.23 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593363 172 FVALLTGP-------RSQAVARARVSLLRS--SLRFSISYRRLDRPTRIRF----SDSNGSVL--FEHPAAPTQDGLVCG 236
Cdd:pfam07452 1 FSALLTGAqevpppvTTGAGGTAVLTLDDTenTLHYTLTFSGLSVPTAAHIhagaAGFNGPVVvpLEGGPRKTTLLAVPE 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 2462593363 237 VWRAVPRLSLRLLRAEQ--LHVALVTLTHPSGEVWGPL 272
Cdd:pfam07452 81 GLATLTAAQLAALLAQQgeLYVNVHTEGNPGGEIRGQI 118
|
|
| VWC |
smart00214 |
von Willebrand factor (vWF) type C domain; |
51-125 |
3.50e-03 |
|
von Willebrand factor (vWF) type C domain;
Pssm-ID: 214564 Cd Length: 59 Bit Score: 36.34 E-value: 3.50e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462593363 51 CTFGGKVYALDETWHPDlgepfgvmRCVLCACeapqwgrrTRGpGRVSCKNIkpECPT-PAC--GQPRQLPGHCCQTC 125
Cdd:smart00214 1 CVHNGRVYNDGETWKPD--------PCQICTC--------LDG-TTVLCDPV--ECPPpPDCpnPERVKPPGECCPRC 59
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| CHRD |
smart00754 |
A domain in the BMP inhibitor chordin and in microbial proteins; |
559-673 |
3.68e-28 |
|
A domain in the BMP inhibitor chordin and in microbial proteins;
Pssm-ID: 214804 Cd Length: 118 Bit Score: 109.36 E-value: 3.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593363 559 DTLPVPLAGALVLPPVKSQAAGHAWLSLDTHCHLHYEVLLAGLGGSEQgtvTAHL-LGPPGTPGP--RRLLKGF--YGSE 633
Cdd:smart00754 1 ETFSALLTGSQEVPPVNTGAVGGAWFTLDDDGSLHYQVTLSGLSGPET---AAHIhEGEIGTNGPvvRIPLPNPtsREGP 77
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2462593363 634 AQGVVKDLEPELLRHLAKGMASLMITTKGSPRGELRGQVH 673
Cdd:smart00754 78 FAGSVKTLTDEELRQLLAGNLYVNVHTKANPGGEIRGQVA 117
|
|
| CHRD |
smart00754 |
A domain in the BMP inhibitor chordin and in microbial proteins; |
431-548 |
6.43e-26 |
|
A domain in the BMP inhibitor chordin and in microbial proteins;
Pssm-ID: 214804 Cd Length: 118 Bit Score: 103.19 E-value: 6.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593363 431 DVLQSVLCGADALIPVQTGAAGSASLTLLGNGSLIYQVQVVGTSSEVVAMTLETKPQRRD---QRTVLCHMaglQPGGHT 507
Cdd:smart00754 1 ETFSALLTGSQEVPPVNTGAVGGAWFTLDDDGSLHYQVTLSGLSGPETAAHIHEGEIGTNgpvVRIPLPNP---TSREGP 77
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2462593363 508 AVGICPGLGARGAHMLLQNELFLNVGTKDFPDGELRGHVAA 548
Cdd:smart00754 78 FAGSVKTLTDEELRQLLAGNLYVNVHTKANPGGEIRGQVAK 118
|
|
| CHRD |
smart00754 |
A domain in the BMP inhibitor chordin and in microbial proteins; |
170-274 |
4.01e-18 |
|
A domain in the BMP inhibitor chordin and in microbial proteins;
Pssm-ID: 214804 Cd Length: 118 Bit Score: 80.85 E-value: 4.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593363 170 TDFVALLTG------PRSQAVARARVSLL-RSSLRFSISYRRLDRPTR-----IRFSDSNGSVLFEHPAAPT-QDGLVCG 236
Cdd:smart00754 1 ETFSALLTGsqevppVNTGAVGGAWFTLDdDGSLHYQVTLSGLSGPETaahihEGEIGTNGPVVRIPLPNPTsREGPFAG 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 2462593363 237 VWRAVPRLSLRLLRAEQLHVALVTLTHPSGEVWGPLIR 274
Cdd:smart00754 81 SVKTLTDEELRQLLAGNLYVNVHTKANPGGEIRGQVAK 118
|
|
| CHRD |
smart00754 |
A domain in the BMP inhibitor chordin and in microbial proteins; |
281-426 |
1.61e-16 |
|
A domain in the BMP inhibitor chordin and in microbial proteins;
Pssm-ID: 214804 Cd Length: 118 Bit Score: 76.23 E-value: 1.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593363 281 ETFSAILTLE---GPPQQGVGGITLLTLsDTEDSLHFLLLFRGLLEPrsggkwdggktrekvrestclrkahmcglagLT 357
Cdd:smart00754 1 ETFSALLTGSqevPPVNTGAVGGAWFTL-DDDGSLHYQVTLSGLSGP-------------------------------ET 48
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593363 358 QVPLRL-QILHQGQLLRELQANVSAQEPGFAEVLPNLTVQEMDWLVLGELQMALEWAGRPGLRISGHIAA 426
Cdd:smart00754 49 AAHIHEgEIGTNGPVVRIPLPNPTSREGPFAGSVKTLTDEELRQLLAGNLYVNVHTKANPGGEIRGQVAK 118
|
|
| CHRD |
pfam07452 |
CHRD domain; CHRD (after SWISS-PROT abbreviation for chordin) is a novel domain identified in ... |
561-672 |
1.23e-14 |
|
CHRD domain; CHRD (after SWISS-PROT abbreviation for chordin) is a novel domain identified in chordin, an inhibitor of bone morphogenetic proteins. This family includes bacterial homologs. It is anticipated to have an immunoglobulin-like beta-barrel structure based on limited similarity to superoxide dismutases but, as yet, no clear functional prediction can be made. Its most conserved feature is a GE[I/L]RCG[V/I/L] motif towards its C-terminal end Most bacterial proteins in this family have only one CHRD domain, whereas it is found repeated in many eukaryotic proteins such as human chordin and Drosophila SOG..
Pssm-ID: 462167 Cd Length: 118 Bit Score: 70.97 E-value: 1.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593363 561 LPVPLAGALVLPP-VKSQAAGHAWLSLDTHCH-LHYEVLLAGLggseQGTVTAHL-LGPPGTPGPrrLLKGFYG------ 631
Cdd:pfam07452 1 FSALLTGAQEVPPpVTTGAGGTAVLTLDDTENtLHYTLTFSGL----SVPTAAHIhAGAAGFNGP--VVVPLEGgprktt 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2462593363 632 -SEAQGVVKDLEPELLRHL--AKGMASLMITTKGSPRGELRGQV 672
Cdd:pfam07452 75 lLAVPEGLATLTAAQLAALlaQQGELYVNVHTEGNPGGEIRGQI 118
|
|
| CHRD |
pfam07452 |
CHRD domain; CHRD (after SWISS-PROT abbreviation for chordin) is a novel domain identified in ... |
433-546 |
2.23e-12 |
|
CHRD domain; CHRD (after SWISS-PROT abbreviation for chordin) is a novel domain identified in chordin, an inhibitor of bone morphogenetic proteins. This family includes bacterial homologs. It is anticipated to have an immunoglobulin-like beta-barrel structure based on limited similarity to superoxide dismutases but, as yet, no clear functional prediction can be made. Its most conserved feature is a GE[I/L]RCG[V/I/L] motif towards its C-terminal end Most bacterial proteins in this family have only one CHRD domain, whereas it is found repeated in many eukaryotic proteins such as human chordin and Drosophila SOG..
Pssm-ID: 462167 Cd Length: 118 Bit Score: 64.42 E-value: 2.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593363 433 LQSVLCGADALIP-VQTGAAGSASLTL-LGNGSLIYQVQVVGTS--------------SEVVAMTLETKPQRRDqrtvlc 496
Cdd:pfam07452 1 FSALLTGAQEVPPpVTTGAGGTAVLTLdDTENTLHYTLTFSGLSvptaahihagaagfNGPVVVPLEGGPRKTT------ 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2462593363 497 hmaglqpgGHTAVGICPGLGARGAHMLLQN--ELFLNVGTKDFPDGELRGHV 546
Cdd:pfam07452 75 --------LLAVPEGLATLTAAQLAALLAQqgELYVNVHTEGNPGGEIRGQI 118
|
|
| VWC |
pfam00093 |
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ... |
51-125 |
9.85e-08 |
|
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with pfam00094.
Pssm-ID: 278520 Cd Length: 57 Bit Score: 49.35 E-value: 9.85e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462593363 51 CTFGGKVYALDETWHPDLgepfgvmrCVLCACEapqwgrrtrgPGRVSCKNIKpeCPTPACGQPR--QLPGHCCQTC 125
Cdd:pfam00093 1 CVQNGVVYENGETWKPDL--------CTICTCD----------DGKVLCDKII--CPPLDCPNPRleIPPGECCPVC 57
|
|
| CHRD |
pfam07452 |
CHRD domain; CHRD (after SWISS-PROT abbreviation for chordin) is a novel domain identified in ... |
283-424 |
2.51e-07 |
|
CHRD domain; CHRD (after SWISS-PROT abbreviation for chordin) is a novel domain identified in chordin, an inhibitor of bone morphogenetic proteins. This family includes bacterial homologs. It is anticipated to have an immunoglobulin-like beta-barrel structure based on limited similarity to superoxide dismutases but, as yet, no clear functional prediction can be made. Its most conserved feature is a GE[I/L]RCG[V/I/L] motif towards its C-terminal end Most bacterial proteins in this family have only one CHRD domain, whereas it is found repeated in many eukaryotic proteins such as human chordin and Drosophila SOG..
Pssm-ID: 462167 Cd Length: 118 Bit Score: 50.17 E-value: 2.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593363 283 FSAILT--LEGPP--QQGVGGITLLTLSDTEDSLHFLLLFRGLLEPRSggkwdggktrekvrestclrkAH-MCGLAGLT 357
Cdd:pfam07452 1 FSALLTgaQEVPPpvTTGAGGTAVLTLDDTENTLHYTLTFSGLSVPTA---------------------AHiHAGAAGFN 59
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462593363 358 QVPLRlqILHQGQLLRELQANVSAQEPGFAEVLPNLTVQEmdwlvlGELQMALEWAGRPGLRISGHI 424
Cdd:pfam07452 60 GPVVV--PLEGGPRKTTLLAVPEGLATLTAAQLAALLAQQ------GELYVNVHTEGNPGGEIRGQI 118
|
|
| VWC |
pfam00093 |
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ... |
732-789 |
2.25e-06 |
|
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with pfam00094.
Pssm-ID: 278520 Cd Length: 57 Bit Score: 45.49 E-value: 2.25e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593363 732 CFFEGQQRPHGARWAPNydpLCSLCTCQRRTVICDPVVCPPPSCPHP--VQAPDQCCPVC 789
Cdd:pfam00093 1 CVQNGVVYENGETWKPD---LCTICTCDDGKVLCDKIICPPLDCPNPrlEIPPGECCPVC 57
|
|
| VWC |
smart00214 |
von Willebrand factor (vWF) type C domain; |
732-789 |
6.13e-04 |
|
von Willebrand factor (vWF) type C domain;
Pssm-ID: 214564 Cd Length: 59 Bit Score: 38.65 E-value: 6.13e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462593363 732 CFFEGQQRPHGARWAPNYdplCSLCTCQRRTVI-CDPVVCPPPSC-PHP--VQAPDQCCPVC 789
Cdd:smart00214 1 CVHNGRVYNDGETWKPDP---CQICTCLDGTTVlCDPVECPPPPDcPNPerVKPPGECCPRC 59
|
|
| CHRD |
pfam07452 |
CHRD domain; CHRD (after SWISS-PROT abbreviation for chordin) is a novel domain identified in ... |
172-272 |
3.17e-03 |
|
CHRD domain; CHRD (after SWISS-PROT abbreviation for chordin) is a novel domain identified in chordin, an inhibitor of bone morphogenetic proteins. This family includes bacterial homologs. It is anticipated to have an immunoglobulin-like beta-barrel structure based on limited similarity to superoxide dismutases but, as yet, no clear functional prediction can be made. Its most conserved feature is a GE[I/L]RCG[V/I/L] motif towards its C-terminal end Most bacterial proteins in this family have only one CHRD domain, whereas it is found repeated in many eukaryotic proteins such as human chordin and Drosophila SOG..
Pssm-ID: 462167 Cd Length: 118 Bit Score: 38.23 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593363 172 FVALLTGP-------RSQAVARARVSLLRS--SLRFSISYRRLDRPTRIRF----SDSNGSVL--FEHPAAPTQDGLVCG 236
Cdd:pfam07452 1 FSALLTGAqevpppvTTGAGGTAVLTLDDTenTLHYTLTFSGLSVPTAAHIhagaAGFNGPVVvpLEGGPRKTTLLAVPE 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 2462593363 237 VWRAVPRLSLRLLRAEQ--LHVALVTLTHPSGEVWGPL 272
Cdd:pfam07452 81 GLATLTAAQLAALLAQQgeLYVNVHTEGNPGGEIRGQI 118
|
|
| VWC |
smart00214 |
von Willebrand factor (vWF) type C domain; |
51-125 |
3.50e-03 |
|
von Willebrand factor (vWF) type C domain;
Pssm-ID: 214564 Cd Length: 59 Bit Score: 36.34 E-value: 3.50e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462593363 51 CTFGGKVYALDETWHPDlgepfgvmRCVLCACeapqwgrrTRGpGRVSCKNIkpECPT-PAC--GQPRQLPGHCCQTC 125
Cdd:smart00214 1 CVHNGRVYNDGETWKPD--------PCQICTC--------LDG-TTVLCDPV--ECPPpPDCpnPERVKPPGECCPRC 59
|
|
|