|
Name |
Accession |
Description |
Interval |
E-value |
| CHRD |
smart00754 |
A domain in the BMP inhibitor chordin and in microbial proteins; |
544-656 |
6.72e-25 |
|
A domain in the BMP inhibitor chordin and in microbial proteins; :
Pssm-ID: 214804 Cd Length: 118 Bit Score: 100.11 E-value: 6.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852260 544 LPVPLAGALVLPPVRSQAAGHAWLSLDTHCHLHYEVLLAGLGGSEQgtvTAHL-LGPPGMPGPQR--LLKGF--YGSEAQ 618
Cdd:smart00754 3 FSALLTGSQEVPPVNTGAVGGAWFTLDDDGSLHYQVTLSGLSGPET---AAHIhEGEIGTNGPVVriPLPNPtsREGPFA 79
|
90 100 110
....*....|....*....|....*....|....*...
gi 1046852260 619 GVVKDLEPVLLRHLTQGTASLLITTKSNPRGELRGQVH 656
Cdd:smart00754 80 GSVKTLTDEELRQLLAGNLYVNVHTKANPGGEIRGQVA 117
|
|
| CHRD |
smart00754 |
A domain in the BMP inhibitor chordin and in microbial proteins; |
414-531 |
8.30e-24 |
|
A domain in the BMP inhibitor chordin and in microbial proteins; :
Pssm-ID: 214804 Cd Length: 118 Bit Score: 97.03 E-value: 8.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852260 414 DVLQSVLCGADALIPVQTGAAGSASFILLGNGSLIYQVQVIGTGSEVVAMTLETKPQRKN---QRTVLCHMaglQLGGHM 490
Cdd:smart00754 1 ETFSALLTGSQEVPPVNTGAVGGAWFTLDDDGSLHYQVTLSGLSGPETAAHIHEGEIGTNgpvVRIPLPNP---TSREGP 77
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1046852260 491 AVGVCSGLGARGAHMLLQNELFLNIGTKDFPDGELRGHVTA 531
Cdd:smart00754 78 FAGSVKTLTDEELRQLLAGNLYVNVHTKANPGGEIRGQVAK 118
|
|
| CHRD |
smart00754 |
A domain in the BMP inhibitor chordin and in microbial proteins; |
184-287 |
2.76e-11 |
|
A domain in the BMP inhibitor chordin and in microbial proteins; :
Pssm-ID: 214804 Cd Length: 118 Bit Score: 61.21 E-value: 2.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852260 184 TDFVALLTG------PRTQAVARARVSLL-RSSLRFSISYQRLDRPSRV-----RFTDPTG---NILFEHPAAptQDGLV 248
Cdd:smart00754 1 ETFSALLTGsqevppVNTGAVGGAWFTLDdDGSLHYQVTLSGLSGPETAahiheGEIGTNGpvvRIPLPNPTS--REGPF 78
|
90 100 110
....*....|....*....|....*....|....*....
gi 1046852260 249 CGVWRAVPRLSVRLLRAEQLRVALVTPTHPSEEVWGPLI 287
Cdd:smart00754 79 AGSVKTLTDEELRQLLAGNLYVNVHTKANPGGEIRGQVA 117
|
|
| CHRD |
smart00754 |
A domain in the BMP inhibitor chordin and in microbial proteins; |
295-408 |
3.85e-09 |
|
A domain in the BMP inhibitor chordin and in microbial proteins; :
Pssm-ID: 214804 Cd Length: 118 Bit Score: 55.04 E-value: 3.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852260 295 ETFSAILTLE---DPLQRGVGGIALLTLSDTEDAL-HFLLLFRGLLGGLAHVPLKlQILHQGQLLRELQANASAQEPGFA 370
Cdd:smart00754 1 ETFSALLTGSqevPPVNTGAVGGAWFTLDDDGSLHyQVTLSGLSGPETAAHIHEG-EIGTNGPVVRIPLPNPTSREGPFA 79
|
90 100 110
....*....|....*....|....*....|....*...
gi 1046852260 371 EVLPSLTDQEMDWLVLGELQMVLEKMGGPELRISGYIT 408
Cdd:smart00754 80 GSVKTLTDEELRQLLAGNLYVNVHTKANPGGEIRGQVA 117
|
|
| VWC |
pfam00093 |
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ... |
65-139 |
4.54e-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: 50.12 E-value: 4.54e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1046852260 65 CSFGGKVYALDETWHPDLgepfgvmrCVLCACEapqwarrgrgPGRVSCKNIKpqCPTLACRQPR--QLPGHCCQTC 139
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 ... |
715-772 |
2.54e-05 |
|
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: 42.41 E-value: 2.54e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852260 715 CFFEGQQRPHGARWAPNydpLCSLCTCQRRTVICDPVVCPPPSCPHP--VQALDQCCPVC 772
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; |
544-656 |
6.72e-25 |
|
A domain in the BMP inhibitor chordin and in microbial proteins;
Pssm-ID: 214804 Cd Length: 118 Bit Score: 100.11 E-value: 6.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852260 544 LPVPLAGALVLPPVRSQAAGHAWLSLDTHCHLHYEVLLAGLGGSEQgtvTAHL-LGPPGMPGPQR--LLKGF--YGSEAQ 618
Cdd:smart00754 3 FSALLTGSQEVPPVNTGAVGGAWFTLDDDGSLHYQVTLSGLSGPET---AAHIhEGEIGTNGPVVriPLPNPtsREGPFA 79
|
90 100 110
....*....|....*....|....*....|....*...
gi 1046852260 619 GVVKDLEPVLLRHLTQGTASLLITTKSNPRGELRGQVH 656
Cdd:smart00754 80 GSVKTLTDEELRQLLAGNLYVNVHTKANPGGEIRGQVA 117
|
|
| CHRD |
smart00754 |
A domain in the BMP inhibitor chordin and in microbial proteins; |
414-531 |
8.30e-24 |
|
A domain in the BMP inhibitor chordin and in microbial proteins;
Pssm-ID: 214804 Cd Length: 118 Bit Score: 97.03 E-value: 8.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852260 414 DVLQSVLCGADALIPVQTGAAGSASFILLGNGSLIYQVQVIGTGSEVVAMTLETKPQRKN---QRTVLCHMaglQLGGHM 490
Cdd:smart00754 1 ETFSALLTGSQEVPPVNTGAVGGAWFTLDDDGSLHYQVTLSGLSGPETAAHIHEGEIGTNgpvVRIPLPNP---TSREGP 77
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1046852260 491 AVGVCSGLGARGAHMLLQNELFLNIGTKDFPDGELRGHVTA 531
Cdd:smart00754 78 FAGSVKTLTDEELRQLLAGNLYVNVHTKANPGGEIRGQVAK 118
|
|
| CHRD |
pfam07452 |
CHRD domain; CHRD (after SWISS-PROT abbreviation for chordin) is a novel domain identified in ... |
544-655 |
2.10e-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: 70.20 E-value: 2.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852260 544 LPVPLAGALVLPP-VRSQAAGHAWLSLDTHCH-LHYEVLLAGLggseQGTVTAHL-LGPPGMPGPQRL-----LKGFYGS 615
Cdd:pfam07452 1 FSALLTGAQEVPPpVTTGAGGTAVLTLDDTENtLHYTLTFSGL----SVPTAAHIhAGAAGFNGPVVVpleggPRKTTLL 76
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1046852260 616 EAQGVVKDLEPVLLRHLTQGTASLLIT--TKSNPRGELRGQV 655
Cdd:pfam07452 77 AVPEGLATLTAAQLAALLAQQGELYVNvhTEGNPGGEIRGQI 118
|
|
| CHRD |
smart00754 |
A domain in the BMP inhibitor chordin and in microbial proteins; |
184-287 |
2.76e-11 |
|
A domain in the BMP inhibitor chordin and in microbial proteins;
Pssm-ID: 214804 Cd Length: 118 Bit Score: 61.21 E-value: 2.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852260 184 TDFVALLTG------PRTQAVARARVSLL-RSSLRFSISYQRLDRPSRV-----RFTDPTG---NILFEHPAAptQDGLV 248
Cdd:smart00754 1 ETFSALLTGsqevppVNTGAVGGAWFTLDdDGSLHYQVTLSGLSGPETAahiheGEIGTNGpvvRIPLPNPTS--REGPF 78
|
90 100 110
....*....|....*....|....*....|....*....
gi 1046852260 249 CGVWRAVPRLSVRLLRAEQLRVALVTPTHPSEEVWGPLI 287
Cdd:smart00754 79 AGSVKTLTDEELRQLLAGNLYVNVHTKANPGGEIRGQVA 117
|
|
| CHRD |
pfam07452 |
CHRD domain; CHRD (after SWISS-PROT abbreviation for chordin) is a novel domain identified in ... |
416-529 |
1.03e-10 |
|
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: 59.80 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852260 416 LQSVLCGADALIP-VQTGAAGSASFIL-LGNGSLIYQVQVIGTG--------------SEVVAMTLETKPQRKNQRTVlc 479
Cdd:pfam07452 1 FSALLTGAQEVPPpVTTGAGGTAVLTLdDTENTLHYTLTFSGLSvptaahihagaagfNGPVVVPLEGGPRKTTLLAV-- 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1046852260 480 hmaglqlgghmaVGVCSGLGARGAHMLLQN--ELFLNIGTKDFPDGELRGHV 529
Cdd:pfam07452 79 ------------PEGLATLTAAQLAALLAQqgELYVNVHTEGNPGGEIRGQI 118
|
|
| CHRD |
smart00754 |
A domain in the BMP inhibitor chordin and in microbial proteins; |
295-408 |
3.85e-09 |
|
A domain in the BMP inhibitor chordin and in microbial proteins;
Pssm-ID: 214804 Cd Length: 118 Bit Score: 55.04 E-value: 3.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852260 295 ETFSAILTLE---DPLQRGVGGIALLTLSDTEDAL-HFLLLFRGLLGGLAHVPLKlQILHQGQLLRELQANASAQEPGFA 370
Cdd:smart00754 1 ETFSALLTGSqevPPVNTGAVGGAWFTLDDDGSLHyQVTLSGLSGPETAAHIHEG-EIGTNGPVVRIPLPNPTSREGPFA 79
|
90 100 110
....*....|....*....|....*....|....*...
gi 1046852260 371 EVLPSLTDQEMDWLVLGELQMVLEKMGGPELRISGYIT 408
Cdd:smart00754 80 GSVKTLTDEELRQLLAGNLYVNVHTKANPGGEIRGQVA 117
|
|
| VWC |
pfam00093 |
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ... |
65-139 |
4.54e-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: 50.12 E-value: 4.54e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1046852260 65 CSFGGKVYALDETWHPDLgepfgvmrCVLCACEapqwarrgrgPGRVSCKNIKpqCPTLACRQPR--QLPGHCCQTC 139
Cdd:pfam00093 1 CVQNGVVYENGETWKPDL--------CTICTCD----------DGKVLCDKII--CPPLDCPNPRleIPPGECCPVC 57
|
|
| VWC |
pfam00093 |
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ... |
715-772 |
2.54e-05 |
|
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with pfam00094.
Pssm-ID: 278520 Cd Length: 57 Bit Score: 42.41 E-value: 2.54e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852260 715 CFFEGQQRPHGARWAPNydpLCSLCTCQRRTVICDPVVCPPPSCPHP--VQALDQCCPVC 772
Cdd:pfam00093 1 CVQNGVVYENGETWKPD---LCTICTCDDGKVLCDKIICPPLDCPNPrlEIPPGECCPVC 57
|
|
| VWC |
smart00214 |
von Willebrand factor (vWF) type C domain; |
715-772 |
7.78e-03 |
|
von Willebrand factor (vWF) type C domain;
Pssm-ID: 214564 Cd Length: 59 Bit Score: 35.57 E-value: 7.78e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1046852260 715 CFFEGQQRPHGARWAPNYdplCSLCTCQRRTVI-CDPVV-CPPPSCPHPVQAL--DQCCPVC 772
Cdd:smart00214 1 CVHNGRVYNDGETWKPDP---CQICTCLDGTTVlCDPVEcPPPPDCPNPERVKppGECCPRC 59
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| CHRD |
smart00754 |
A domain in the BMP inhibitor chordin and in microbial proteins; |
544-656 |
6.72e-25 |
|
A domain in the BMP inhibitor chordin and in microbial proteins;
Pssm-ID: 214804 Cd Length: 118 Bit Score: 100.11 E-value: 6.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852260 544 LPVPLAGALVLPPVRSQAAGHAWLSLDTHCHLHYEVLLAGLGGSEQgtvTAHL-LGPPGMPGPQR--LLKGF--YGSEAQ 618
Cdd:smart00754 3 FSALLTGSQEVPPVNTGAVGGAWFTLDDDGSLHYQVTLSGLSGPET---AAHIhEGEIGTNGPVVriPLPNPtsREGPFA 79
|
90 100 110
....*....|....*....|....*....|....*...
gi 1046852260 619 GVVKDLEPVLLRHLTQGTASLLITTKSNPRGELRGQVH 656
Cdd:smart00754 80 GSVKTLTDEELRQLLAGNLYVNVHTKANPGGEIRGQVA 117
|
|
| CHRD |
smart00754 |
A domain in the BMP inhibitor chordin and in microbial proteins; |
414-531 |
8.30e-24 |
|
A domain in the BMP inhibitor chordin and in microbial proteins;
Pssm-ID: 214804 Cd Length: 118 Bit Score: 97.03 E-value: 8.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852260 414 DVLQSVLCGADALIPVQTGAAGSASFILLGNGSLIYQVQVIGTGSEVVAMTLETKPQRKN---QRTVLCHMaglQLGGHM 490
Cdd:smart00754 1 ETFSALLTGSQEVPPVNTGAVGGAWFTLDDDGSLHYQVTLSGLSGPETAAHIHEGEIGTNgpvVRIPLPNP---TSREGP 77
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1046852260 491 AVGVCSGLGARGAHMLLQNELFLNIGTKDFPDGELRGHVTA 531
Cdd:smart00754 78 FAGSVKTLTDEELRQLLAGNLYVNVHTKANPGGEIRGQVAK 118
|
|
| CHRD |
pfam07452 |
CHRD domain; CHRD (after SWISS-PROT abbreviation for chordin) is a novel domain identified in ... |
544-655 |
2.10e-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: 70.20 E-value: 2.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852260 544 LPVPLAGALVLPP-VRSQAAGHAWLSLDTHCH-LHYEVLLAGLggseQGTVTAHL-LGPPGMPGPQRL-----LKGFYGS 615
Cdd:pfam07452 1 FSALLTGAQEVPPpVTTGAGGTAVLTLDDTENtLHYTLTFSGL----SVPTAAHIhAGAAGFNGPVVVpleggPRKTTLL 76
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1046852260 616 EAQGVVKDLEPVLLRHLTQGTASLLIT--TKSNPRGELRGQV 655
Cdd:pfam07452 77 AVPEGLATLTAAQLAALLAQQGELYVNvhTEGNPGGEIRGQI 118
|
|
| CHRD |
smart00754 |
A domain in the BMP inhibitor chordin and in microbial proteins; |
184-287 |
2.76e-11 |
|
A domain in the BMP inhibitor chordin and in microbial proteins;
Pssm-ID: 214804 Cd Length: 118 Bit Score: 61.21 E-value: 2.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852260 184 TDFVALLTG------PRTQAVARARVSLL-RSSLRFSISYQRLDRPSRV-----RFTDPTG---NILFEHPAAptQDGLV 248
Cdd:smart00754 1 ETFSALLTGsqevppVNTGAVGGAWFTLDdDGSLHYQVTLSGLSGPETAahiheGEIGTNGpvvRIPLPNPTS--REGPF 78
|
90 100 110
....*....|....*....|....*....|....*....
gi 1046852260 249 CGVWRAVPRLSVRLLRAEQLRVALVTPTHPSEEVWGPLI 287
Cdd:smart00754 79 AGSVKTLTDEELRQLLAGNLYVNVHTKANPGGEIRGQVA 117
|
|
| CHRD |
pfam07452 |
CHRD domain; CHRD (after SWISS-PROT abbreviation for chordin) is a novel domain identified in ... |
416-529 |
1.03e-10 |
|
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: 59.80 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852260 416 LQSVLCGADALIP-VQTGAAGSASFIL-LGNGSLIYQVQVIGTG--------------SEVVAMTLETKPQRKNQRTVlc 479
Cdd:pfam07452 1 FSALLTGAQEVPPpVTTGAGGTAVLTLdDTENTLHYTLTFSGLSvptaahihagaagfNGPVVVPLEGGPRKTTLLAV-- 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1046852260 480 hmaglqlgghmaVGVCSGLGARGAHMLLQN--ELFLNIGTKDFPDGELRGHV 529
Cdd:pfam07452 79 ------------PEGLATLTAAQLAALLAQqgELYVNVHTEGNPGGEIRGQI 118
|
|
| CHRD |
smart00754 |
A domain in the BMP inhibitor chordin and in microbial proteins; |
295-408 |
3.85e-09 |
|
A domain in the BMP inhibitor chordin and in microbial proteins;
Pssm-ID: 214804 Cd Length: 118 Bit Score: 55.04 E-value: 3.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852260 295 ETFSAILTLE---DPLQRGVGGIALLTLSDTEDAL-HFLLLFRGLLGGLAHVPLKlQILHQGQLLRELQANASAQEPGFA 370
Cdd:smart00754 1 ETFSALLTGSqevPPVNTGAVGGAWFTLDDDGSLHyQVTLSGLSGPETAAHIHEG-EIGTNGPVVRIPLPNPTSREGPFA 79
|
90 100 110
....*....|....*....|....*....|....*...
gi 1046852260 371 EVLPSLTDQEMDWLVLGELQMVLEKMGGPELRISGYIT 408
Cdd:smart00754 80 GSVKTLTDEELRQLLAGNLYVNVHTKANPGGEIRGQVA 117
|
|
| VWC |
pfam00093 |
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ... |
65-139 |
4.54e-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: 50.12 E-value: 4.54e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1046852260 65 CSFGGKVYALDETWHPDLgepfgvmrCVLCACEapqwarrgrgPGRVSCKNIKpqCPTLACRQPR--QLPGHCCQTC 139
Cdd:pfam00093 1 CVQNGVVYENGETWKPDL--------CTICTCD----------DGKVLCDKII--CPPLDCPNPRleIPPGECCPVC 57
|
|
| VWC |
pfam00093 |
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ... |
715-772 |
2.54e-05 |
|
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with pfam00094.
Pssm-ID: 278520 Cd Length: 57 Bit Score: 42.41 E-value: 2.54e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852260 715 CFFEGQQRPHGARWAPNydpLCSLCTCQRRTVICDPVVCPPPSCPHP--VQALDQCCPVC 772
Cdd:pfam00093 1 CVQNGVVYENGETWKPD---LCTICTCDDGKVLCDKIICPPLDCPNPrlEIPPGECCPVC 57
|
|
| Amnionless |
pfam14828 |
Amnionless; The amnionless protein forms a complex with cubilin. This complex is necessary for ... |
66-139 |
5.50e-04 |
|
Amnionless; The amnionless protein forms a complex with cubilin. This complex is necessary for vitamin B12 uptake.
Pssm-ID: 464340 Cd Length: 449 Bit Score: 43.15 E-value: 5.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852260 66 SFGGKVYALDETWHPDLGEPFGVM----------------RCVLCAC---EAPQWArrgrgpgrvsCKNIKPQCPTLACR 126
Cdd:pfam14828 153 SLLGQTFTSDEDFAEFLSSRLGQLqfhgagalrvgpeacsDPSGCGCgndENLERI----------CANVLQRCPPPHCL 222
|
90
....*....|...
gi 1046852260 127 QPRQLPGHCCQTC 139
Cdd:pfam14828 223 SPLRPEGHCCDVC 235
|
|
| VWC |
smart00214 |
von Willebrand factor (vWF) type C domain; |
715-772 |
7.78e-03 |
|
von Willebrand factor (vWF) type C domain;
Pssm-ID: 214564 Cd Length: 59 Bit Score: 35.57 E-value: 7.78e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1046852260 715 CFFEGQQRPHGARWAPNYdplCSLCTCQRRTVI-CDPVV-CPPPSCPHPVQAL--DQCCPVC 772
Cdd:smart00214 1 CVHNGRVYNDGETWKPDP---CQICTCLDGTTVlCDPVEcPPPPDCPNPERVKppGECCPRC 59
|
|
|