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Conserved domains on  [gi|1034636152|ref|XP_016862877|]
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chordin isoform X1 [Homo sapiens]

Protein Classification

follistatin-related protein 1( domain architecture ID 10356082)

follistatin-related protein 1 is an extracellular calcium-binding protein belonging to the BM-40/SPARC/osteonectin family and containing Kazal-type serine protease inhibitor/follistatin-like and EF-hand domains, that is involved in various physiological processes, such as angiogenesis, regulation of the immune response, cell proliferation and differentiation

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CHRD smart00754
A domain in the BMP inhibitor chordin and in microbial proteins;
559-673 3.96e-29

A domain in the BMP inhibitor chordin and in microbial proteins;


:

Pssm-ID: 214804  Cd Length: 118  Bit Score: 112.44  E-value: 3.96e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636152  559 DTLPVPLAGALVLPPVKSQAAGHAWLSLDTHCHLHYEVLLAGLGGSEQgtvTAHL-LGPPGTPGP--RRLLKGF--YGSE 633
Cdd:smart00754   1 ETFSALLTGSQEVPPVNTGAVGGAWFTLDDDGSLHYQVTLSGLSGPET---AAHIhEGEIGTNGPvvRIPLPNPtsREGP 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1034636152  634 AQGVVKDLEPELLRHLAKGMASLMITTKGSPRGELRGQVH 673
Cdd:smart00754  78 FAGSVKTLTDEELRQLLAGNLYVNVHTKANPGGEIRGQVA 117
CHRD smart00754
A domain in the BMP inhibitor chordin and in microbial proteins;
431-548 1.01e-26

A domain in the BMP inhibitor chordin and in microbial proteins;


:

Pssm-ID: 214804  Cd Length: 118  Bit Score: 105.51  E-value: 1.01e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636152  431 DVLQSVLCGADALIPVQTGAAGSASLTLLGNGSLIYQVQVVGTSSEVVAMTLETKPQRRD---QRTVLCHMaglQPGGHT 507
Cdd:smart00754   1 ETFSALLTGSQEVPPVNTGAVGGAWFTLDDDGSLHYQVTLSGLSGPETAAHIHEGEIGTNgpvVRIPLPNP---TSREGP 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1034636152  508 AVGICPGLGARGAHMLLQNELFLNVGTKDFPDGELRGHVAA 548
Cdd:smart00754  78 FAGSVKTLTDEELRQLLAGNLYVNVHTKANPGGEIRGQVAK 118
CHRD smart00754
A domain in the BMP inhibitor chordin and in microbial proteins;
170-274 7.58e-19

A domain in the BMP inhibitor chordin and in microbial proteins;


:

Pssm-ID: 214804  Cd Length: 118  Bit Score: 83.16  E-value: 7.58e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636152  170 TDFVALLTG------PRSQAVARARVSLL-RSSLRFSISYRRLDRPTR-----IRFSDSNGSVLFEHPAAPT-QDGLVCG 236
Cdd:smart00754   1 ETFSALLTGsqevppVNTGAVGGAWFTLDdDGSLHYQVTLSGLSGPETaahihEGEIGTNGPVVRIPLPNPTsREGPFAG 80
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1034636152  237 VWRAVPRLSLRLLRAEQLHVALVTLTHPSGEVWGPLIR 274
Cdd:smart00754  81 SVKTLTDEELRQLLAGNLYVNVHTKANPGGEIRGQVAK 118
CHRD smart00754
A domain in the BMP inhibitor chordin and in microbial proteins;
281-426 2.75e-17

A domain in the BMP inhibitor chordin and in microbial proteins;


:

Pssm-ID: 214804  Cd Length: 118  Bit Score: 78.54  E-value: 2.75e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636152  281 ETFSAILTLE---GPPQQGVGGITLLTLsDTEDSLHFLLLFRGLLEPrsggkwdggktrekvrestclrkahmcglagLT 357
Cdd:smart00754   1 ETFSALLTGSqevPPVNTGAVGGAWFTL-DDDGSLHYQVTLSGLSGP-------------------------------ET 48
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636152  358 QVPLRL-QILHQGQLLRELQANVSAQEPGFAEVLPNLTVQEMDWLVLGELQMALEWAGRPGLRISGHIAA 426
Cdd:smart00754  49 AAHIHEgEIGTNGPVVRIPLPNPTSREGPFAGSVKTLTDEELRQLLAGNLYVNVHTKANPGGEIRGQVAK 118
VWC smart00214
von Willebrand factor (vWF) type C domain;
811-877 1.80e-07

von Willebrand factor (vWF) type C domain;


:

Pssm-ID: 214564  Cd Length: 59  Bit Score: 48.67  E-value: 1.80e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034636152  811 CYFDGDrsWRAAGTRWHPVVppfglikCAVCTCKGGTgEVHCEKVQCPR-LACAQPVRVNPTD-CCKQC 877
Cdd:smart00214   1 CVHNGR--VYNDGETWKPDP-------CQICTCLDGT-TVLCDPVECPPpPDCPNPERVKPPGeCCPRC 59
VWC super family cl17735
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
51-125 7.82e-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: 43.95  E-value: 7.82e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034636152  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 5.52e-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: 41.64  E-value: 5.52e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636152 732 CFFEGQQRPHGARWAPNydpLCSLCTCQRRTVICDPVVCPPPSCPHP--VQAPDQCCPVC 789
Cdd:pfam00093   1 CVQNGVVYENGETWKPD---LCTICTCDDGKVLCDKIICPPLDCPNPrlEIPPGECCPVC 57
VWC super family cl17735
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
899-959 1.69e-04

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: 40.49  E-value: 1.69e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034636152 899 CRFAGQWFPESQSWHPSvppfgemSCITCRCGAGVPHCERDDCSlPLSCGSGKES----RCCSRC 959
Cdd:pfam00093   1 CVQNGVVYENGETWKPD-------LCTICTCDDGKVLCDKIICP-PLDCPNPRLEippgECCPVC 57
 
Name Accession Description Interval E-value
CHRD smart00754
A domain in the BMP inhibitor chordin and in microbial proteins;
559-673 3.96e-29

A domain in the BMP inhibitor chordin and in microbial proteins;


Pssm-ID: 214804  Cd Length: 118  Bit Score: 112.44  E-value: 3.96e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636152  559 DTLPVPLAGALVLPPVKSQAAGHAWLSLDTHCHLHYEVLLAGLGGSEQgtvTAHL-LGPPGTPGP--RRLLKGF--YGSE 633
Cdd:smart00754   1 ETFSALLTGSQEVPPVNTGAVGGAWFTLDDDGSLHYQVTLSGLSGPET---AAHIhEGEIGTNGPvvRIPLPNPtsREGP 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1034636152  634 AQGVVKDLEPELLRHLAKGMASLMITTKGSPRGELRGQVH 673
Cdd:smart00754  78 FAGSVKTLTDEELRQLLAGNLYVNVHTKANPGGEIRGQVA 117
CHRD smart00754
A domain in the BMP inhibitor chordin and in microbial proteins;
431-548 1.01e-26

A domain in the BMP inhibitor chordin and in microbial proteins;


Pssm-ID: 214804  Cd Length: 118  Bit Score: 105.51  E-value: 1.01e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636152  431 DVLQSVLCGADALIPVQTGAAGSASLTLLGNGSLIYQVQVVGTSSEVVAMTLETKPQRRD---QRTVLCHMaglQPGGHT 507
Cdd:smart00754   1 ETFSALLTGSQEVPPVNTGAVGGAWFTLDDDGSLHYQVTLSGLSGPETAAHIHEGEIGTNgpvVRIPLPNP---TSREGP 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1034636152  508 AVGICPGLGARGAHMLLQNELFLNVGTKDFPDGELRGHVAA 548
Cdd:smart00754  78 FAGSVKTLTDEELRQLLAGNLYVNVHTKANPGGEIRGQVAK 118
CHRD smart00754
A domain in the BMP inhibitor chordin and in microbial proteins;
170-274 7.58e-19

A domain in the BMP inhibitor chordin and in microbial proteins;


Pssm-ID: 214804  Cd Length: 118  Bit Score: 83.16  E-value: 7.58e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636152  170 TDFVALLTG------PRSQAVARARVSLL-RSSLRFSISYRRLDRPTR-----IRFSDSNGSVLFEHPAAPT-QDGLVCG 236
Cdd:smart00754   1 ETFSALLTGsqevppVNTGAVGGAWFTLDdDGSLHYQVTLSGLSGPETaahihEGEIGTNGPVVRIPLPNPTsREGPFAG 80
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1034636152  237 VWRAVPRLSLRLLRAEQLHVALVTLTHPSGEVWGPLIR 274
Cdd:smart00754  81 SVKTLTDEELRQLLAGNLYVNVHTKANPGGEIRGQVAK 118
CHRD smart00754
A domain in the BMP inhibitor chordin and in microbial proteins;
281-426 2.75e-17

A domain in the BMP inhibitor chordin and in microbial proteins;


Pssm-ID: 214804  Cd Length: 118  Bit Score: 78.54  E-value: 2.75e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636152  281 ETFSAILTLE---GPPQQGVGGITLLTLsDTEDSLHFLLLFRGLLEPrsggkwdggktrekvrestclrkahmcglagLT 357
Cdd:smart00754   1 ETFSALLTGSqevPPVNTGAVGGAWFTL-DDDGSLHYQVTLSGLSGP-------------------------------ET 48
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636152  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 1.85e-15

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: 73.28  E-value: 1.85e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636152 561 LPVPLAGALVLPP-VKSQAAGHAWLSLDTHCH-LHYEVLLAGLggseQGTVTAHL-LGPPGTPGPrrLLKGFYG------ 631
Cdd:pfam07452   1 FSALLTGAQEVPPpVTTGAGGTAVLTLDDTENtLHYTLTFSGL----SVPTAAHIhAGAAGFNGP--VVVPLEGgprktt 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1034636152 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 4.38e-13

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: 66.73  E-value: 4.38e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636152 433 LQSVLCGADALIP-VQTGAAGSASLTL-LGNGSLIYQVQVVGTS--------------SEVVAMTLETKPQRRDqrtvlc 496
Cdd:pfam07452   1 FSALLTGAQEVPPpVTTGAGGTAVLTLdDTENTLHYTLTFSGLSvptaahihagaagfNGPVVVPLEGGPRKTT------ 74
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1034636152 497 hmaglqpgGHTAVGICPGLGARGAHMLLQN--ELFLNVGTKDFPDGELRGHV 546
Cdd:pfam07452  75 --------LLAVPEGLATLTAAQLAALLAQqgELYVNVHTEGNPGGEIRGQI 118
CHRD pfam07452
CHRD domain; CHRD (after SWISS-PROT abbreviation for chordin) is a novel domain identified in ...
283-424 5.89e-08

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: 52.10  E-value: 5.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636152 283 FSAILT--LEGPP--QQGVGGITLLTLSDTEDSLHFLLLFRGLLEPRSggkwdggktrekvrestclrkAH-MCGLAGLT 357
Cdd:pfam07452   1 FSALLTgaQEVPPpvTTGAGGTAVLTLDDTENTLHYTLTFSGLSVPTA---------------------AHiHAGAAGFN 59
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034636152 358 QVPLRlqILHQGQLLRELQANVSAQEPGFAEVLPNLTVQEmdwlvlGELQMALEWAGRPGLRISGHI 424
Cdd:pfam07452  60 GPVVV--PLEGGPRKTTLLAVPEGLATLTAAQLAALLAQQ------GELYVNVHTEGNPGGEIRGQI 118
VWC smart00214
von Willebrand factor (vWF) type C domain;
811-877 1.80e-07

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214564  Cd Length: 59  Bit Score: 48.67  E-value: 1.80e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034636152  811 CYFDGDrsWRAAGTRWHPVVppfglikCAVCTCKGGTgEVHCEKVQCPR-LACAQPVRVNPTD-CCKQC 877
Cdd:smart00214   1 CVHNGR--VYNDGETWKPDP-------CQICTCLDGT-TVLCDPVECPPpPDCPNPERVKPPGeCCPRC 59
VWC pfam00093
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
51-125 7.82e-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: 43.95  E-value: 7.82e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034636152  51 CTFGGKVYALDETWHPDLgepfgvmrCVLCACEapqwgrrtrgPGRVSCKNIKpeCPTPACGQPR--QLPGHCCQTC 125
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 ...
732-789 5.52e-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: 41.64  E-value: 5.52e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636152 732 CFFEGQQRPHGARWAPNydpLCSLCTCQRRTVICDPVVCPPPSCPHP--VQAPDQCCPVC 789
Cdd:pfam00093   1 CVQNGVVYENGETWKPD---LCTICTCDDGKVLCDKIICPPLDCPNPrlEIPPGECCPVC 57
VWC pfam00093
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
899-959 1.69e-04

von Willebrand factor type C domain; The high cutoff was used to prevent overlap with pfam00094.


Pssm-ID: 278520  Cd Length: 57  Bit Score: 40.49  E-value: 1.69e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034636152 899 CRFAGQWFPESQSWHPSvppfgemSCITCRCGAGVPHCERDDCSlPLSCGSGKES----RCCSRC 959
Cdd:pfam00093   1 CVQNGVVYENGETWKPD-------LCTICTCDDGKVLCDKIICP-PLDCPNPRLEippgECCPVC 57
CHRD pfam07452
CHRD domain; CHRD (after SWISS-PROT abbreviation for chordin) is a novel domain identified in ...
172-272 1.13e-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: 39.77  E-value: 1.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636152 172 FVALLTGP-------RSQAVARARVSLLRS--SLRFSISYRRLDRPTRIRF----SDSNGSVL--FEHPAAPTQDGLVCG 236
Cdd:pfam07452   1 FSALLTGAqevpppvTTGAGGTAVLTLDDTenTLHYTLTFSGLSVPTAAHIhagaAGFNGPVVvpLEGGPRKTTLLAVPE 80
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1034636152 237 VWRAVPRLSLRLLRAEQ--LHVALVTLTHPSGEVWGPL 272
Cdd:pfam07452  81 GLATLTAAQLAALLAQQgeLYVNVHTEGNPGGEIRGQI 118
 
Name Accession Description Interval E-value
CHRD smart00754
A domain in the BMP inhibitor chordin and in microbial proteins;
559-673 3.96e-29

A domain in the BMP inhibitor chordin and in microbial proteins;


Pssm-ID: 214804  Cd Length: 118  Bit Score: 112.44  E-value: 3.96e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636152  559 DTLPVPLAGALVLPPVKSQAAGHAWLSLDTHCHLHYEVLLAGLGGSEQgtvTAHL-LGPPGTPGP--RRLLKGF--YGSE 633
Cdd:smart00754   1 ETFSALLTGSQEVPPVNTGAVGGAWFTLDDDGSLHYQVTLSGLSGPET---AAHIhEGEIGTNGPvvRIPLPNPtsREGP 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1034636152  634 AQGVVKDLEPELLRHLAKGMASLMITTKGSPRGELRGQVH 673
Cdd:smart00754  78 FAGSVKTLTDEELRQLLAGNLYVNVHTKANPGGEIRGQVA 117
CHRD smart00754
A domain in the BMP inhibitor chordin and in microbial proteins;
431-548 1.01e-26

A domain in the BMP inhibitor chordin and in microbial proteins;


Pssm-ID: 214804  Cd Length: 118  Bit Score: 105.51  E-value: 1.01e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636152  431 DVLQSVLCGADALIPVQTGAAGSASLTLLGNGSLIYQVQVVGTSSEVVAMTLETKPQRRD---QRTVLCHMaglQPGGHT 507
Cdd:smart00754   1 ETFSALLTGSQEVPPVNTGAVGGAWFTLDDDGSLHYQVTLSGLSGPETAAHIHEGEIGTNgpvVRIPLPNP---TSREGP 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1034636152  508 AVGICPGLGARGAHMLLQNELFLNVGTKDFPDGELRGHVAA 548
Cdd:smart00754  78 FAGSVKTLTDEELRQLLAGNLYVNVHTKANPGGEIRGQVAK 118
CHRD smart00754
A domain in the BMP inhibitor chordin and in microbial proteins;
170-274 7.58e-19

A domain in the BMP inhibitor chordin and in microbial proteins;


Pssm-ID: 214804  Cd Length: 118  Bit Score: 83.16  E-value: 7.58e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636152  170 TDFVALLTG------PRSQAVARARVSLL-RSSLRFSISYRRLDRPTR-----IRFSDSNGSVLFEHPAAPT-QDGLVCG 236
Cdd:smart00754   1 ETFSALLTGsqevppVNTGAVGGAWFTLDdDGSLHYQVTLSGLSGPETaahihEGEIGTNGPVVRIPLPNPTsREGPFAG 80
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1034636152  237 VWRAVPRLSLRLLRAEQLHVALVTLTHPSGEVWGPLIR 274
Cdd:smart00754  81 SVKTLTDEELRQLLAGNLYVNVHTKANPGGEIRGQVAK 118
CHRD smart00754
A domain in the BMP inhibitor chordin and in microbial proteins;
281-426 2.75e-17

A domain in the BMP inhibitor chordin and in microbial proteins;


Pssm-ID: 214804  Cd Length: 118  Bit Score: 78.54  E-value: 2.75e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636152  281 ETFSAILTLE---GPPQQGVGGITLLTLsDTEDSLHFLLLFRGLLEPrsggkwdggktrekvrestclrkahmcglagLT 357
Cdd:smart00754   1 ETFSALLTGSqevPPVNTGAVGGAWFTL-DDDGSLHYQVTLSGLSGP-------------------------------ET 48
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636152  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 1.85e-15

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: 73.28  E-value: 1.85e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636152 561 LPVPLAGALVLPP-VKSQAAGHAWLSLDTHCH-LHYEVLLAGLggseQGTVTAHL-LGPPGTPGPrrLLKGFYG------ 631
Cdd:pfam07452   1 FSALLTGAQEVPPpVTTGAGGTAVLTLDDTENtLHYTLTFSGL----SVPTAAHIhAGAAGFNGP--VVVPLEGgprktt 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1034636152 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 4.38e-13

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: 66.73  E-value: 4.38e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636152 433 LQSVLCGADALIP-VQTGAAGSASLTL-LGNGSLIYQVQVVGTS--------------SEVVAMTLETKPQRRDqrtvlc 496
Cdd:pfam07452   1 FSALLTGAQEVPPpVTTGAGGTAVLTLdDTENTLHYTLTFSGLSvptaahihagaagfNGPVVVPLEGGPRKTT------ 74
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1034636152 497 hmaglqpgGHTAVGICPGLGARGAHMLLQN--ELFLNVGTKDFPDGELRGHV 546
Cdd:pfam07452  75 --------LLAVPEGLATLTAAQLAALLAQqgELYVNVHTEGNPGGEIRGQI 118
CHRD pfam07452
CHRD domain; CHRD (after SWISS-PROT abbreviation for chordin) is a novel domain identified in ...
283-424 5.89e-08

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: 52.10  E-value: 5.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636152 283 FSAILT--LEGPP--QQGVGGITLLTLSDTEDSLHFLLLFRGLLEPRSggkwdggktrekvrestclrkAH-MCGLAGLT 357
Cdd:pfam07452   1 FSALLTgaQEVPPpvTTGAGGTAVLTLDDTENTLHYTLTFSGLSVPTA---------------------AHiHAGAAGFN 59
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034636152 358 QVPLRlqILHQGQLLRELQANVSAQEPGFAEVLPNLTVQEmdwlvlGELQMALEWAGRPGLRISGHI 424
Cdd:pfam07452  60 GPVVV--PLEGGPRKTTLLAVPEGLATLTAAQLAALLAQQ------GELYVNVHTEGNPGGEIRGQI 118
VWC smart00214
von Willebrand factor (vWF) type C domain;
811-877 1.80e-07

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214564  Cd Length: 59  Bit Score: 48.67  E-value: 1.80e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034636152  811 CYFDGDrsWRAAGTRWHPVVppfglikCAVCTCKGGTgEVHCEKVQCPR-LACAQPVRVNPTD-CCKQC 877
Cdd:smart00214   1 CVHNGR--VYNDGETWKPDP-------CQICTCLDGT-TVLCDPVECPPpPDCPNPERVKPPGeCCPRC 59
VWC pfam00093
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
51-125 7.82e-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: 43.95  E-value: 7.82e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034636152  51 CTFGGKVYALDETWHPDLgepfgvmrCVLCACEapqwgrrtrgPGRVSCKNIKpeCPTPACGQPR--QLPGHCCQTC 125
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 ...
732-789 5.52e-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: 41.64  E-value: 5.52e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636152 732 CFFEGQQRPHGARWAPNydpLCSLCTCQRRTVICDPVVCPPPSCPHP--VQAPDQCCPVC 789
Cdd:pfam00093   1 CVQNGVVYENGETWKPD---LCTICTCDDGKVLCDKIICPPLDCPNPrlEIPPGECCPVC 57
VWC pfam00093
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
899-959 1.69e-04

von Willebrand factor type C domain; The high cutoff was used to prevent overlap with pfam00094.


Pssm-ID: 278520  Cd Length: 57  Bit Score: 40.49  E-value: 1.69e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034636152 899 CRFAGQWFPESQSWHPSvppfgemSCITCRCGAGVPHCERDDCSlPLSCGSGKES----RCCSRC 959
Cdd:pfam00093   1 CVQNGVVYENGETWKPD-------LCTICTCDDGKVLCDKIICP-PLDCPNPRLEippgECCPVC 57
CHRD pfam07452
CHRD domain; CHRD (after SWISS-PROT abbreviation for chordin) is a novel domain identified in ...
172-272 1.13e-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: 39.77  E-value: 1.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636152 172 FVALLTGP-------RSQAVARARVSLLRS--SLRFSISYRRLDRPTRIRF----SDSNGSVL--FEHPAAPTQDGLVCG 236
Cdd:pfam07452   1 FSALLTGAqevpppvTTGAGGTAVLTLDDTenTLHYTLTFSGLSVPTAAHIhagaAGFNGPVVvpLEGGPRKTTLLAVPE 80
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1034636152 237 VWRAVPRLSLRLLRAEQ--LHVALVTLTHPSGEVWGPL 272
Cdd:pfam07452  81 GLATLTAAQLAALLAQQgeLYVNVHTEGNPGGEIRGQI 118
 
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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