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Conserved domains on  [gi|755534056|ref|XP_011241649|]
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collagen alpha-1(XVIII) chain isoform X5 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CRD_Collagen_XVIII cd07455
Cysteine-rich domain of the variant 3 of collagen XVIII (V3C18 ); The cysteine-rich domain ...
 366-488 3.87e-58

Cysteine-rich domain of the variant 3 of collagen XVIII (V3C18 ); The cysteine-rich domain (CRD) is an essential part of the variant 3 of collagen XVIII (V3C18), which regulates major cellular functions such as the differential epithelial morphogenesis of early lung and kidney development. V3C18 is a 170 kD protein, which is proteolotically processed into the CRD-containing 50 kD glucoprotein precursor that binds Wnt3a through its CRD domain and suppresses the Wnt3a-induced stabilization of beta catenin. Full-length V3C18 is unable to inhibit Wnt signaling.


:

Pssm-ID: 143564  Cd Length: 123  Bit Score: 195.42  E-value: 3.87e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534056 366 STSRCLPLPPTLTLCSRLGIGHFWLPNHLHHTDSVEVEATVQAWGRFLHTNCHPFLAWFFCLLLAPSCGPGPPPPLPPCR 445
Cdd:cd07455    1 PRPRCLPVPSSLPFCSRLGIRSFWLPNFLNHTSVEEVRAVLAEWAWLLESGCHPSLEWFFCLLLVPSCGGGPPPPPPPCR 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 755534056 446 QFCEALEDECWNYLAGDRLPVVCASLPSQEDGYCVFIGPAAEN 488
Cdd:cd07455   81 QFCEVLQDSCWNLLEGGRLPVACASLPEQEDGYCVLIGPPAEN 123
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 492-680 8.48e-51

Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of thrombospondin


:

Pssm-ID: 214560  Cd Length: 184  Bit Score: 176.78  E-value: 8.48e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534056   492 EVGLLQLLGDP-LPEKISQIDDPHVG-PAYIFGPDSNSGQVAQYHFPKLFFRDFSLLFHVRPATEAAGVLFAITDaAQVV 569
Cdd:smart00210   1 GQDLLQVFDLPsLSFAIRQVVGPEPGsPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPKSRGVLFAIYD-AQNV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534056   570 VSLGVKLsevrDGQQNISLLYTEpGASQTQTGASFR-LPAFVGQWTHFALSVDGGSVALYVDCEEFQRVPFARASQglEL 648
Cdd:smart00210  80 RQFGLEV----DGRANTLLLRYQ-GVDGKQHTVSFRnLPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGQ--PP 152

                          170       180       190
                   ....*....|....*....|....*....|..
gi 755534056   649 ERGAGLFVGQAGTADPDKFQGMISELKVRKTP 680
Cdd:smart00210 153 IDTDGIEVRGAQAADRKPFQGDLQQLKIVCDP 184
DUF959 super family cl25749
Domain of Unknown Function (DUF959); This N-terminal domain is not expressed in the 'Short' ...
 37-218 5.14e-47

Domain of Unknown Function (DUF959); This N-terminal domain is not expressed in the 'Short' isoform of Collagen A.


The actual alignment was detected with superfamily member pfam06121:

Pssm-ID: 399255 [Multi-domain]  Cd Length: 192  Bit Score: 166.54  E-value: 5.14e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534056   37 LVWLWPPKTSDSLEGPVSKPQNSSPVQSTENPTTHVVPQDGLTEQQTTPASselppEEEEEEDQKAGQGGSPATPAVPIP 116
Cdd:pfam06121  16 LDLLWFLDIADPEDTLASEPQGGLAVQPAAAPATHVAPQDDPAEQATAAAS-----PELPLEELEAAPGRAPGAPISAAA 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534056  117 LVAPAASPDMKEENVAGVGAKILNVAQGIRSFVQLWDEDSTIGHSAGTEVPDSSIPTVLPSPAELSSAPQGSKTTLWLSS 196
Cdd:pfam06121  91 PAALAARPDMREENVAGVGAKILNIAQGIQSFIQLWNDAAPTESPAGAGTLAASAPTDPLALAEPSGPAAESGTALGPHR 170

                         170       180
                  ....*....|....*....|..
gi 755534056  197 AIPSSPDAQTTEAGTLAVPTQL 218
Cdd:pfam06121 171 GALSSLDTPRAESGTLAVPTQL 192
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 840-875 3.05e-05

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


:

Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.48  E-value: 3.05e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 755534056  840 PGRDGEPGDPGEDGRPGDTGPQGFPGTPGDVGPKGE 875
Cdd:pfam01391  21 PGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
 
Name Accession Description Interval E-value
CRD_Collagen_XVIII cd07455
Cysteine-rich domain of the variant 3 of collagen XVIII (V3C18 ); The cysteine-rich domain ...
 366-488 3.87e-58

Cysteine-rich domain of the variant 3 of collagen XVIII (V3C18 ); The cysteine-rich domain (CRD) is an essential part of the variant 3 of collagen XVIII (V3C18), which regulates major cellular functions such as the differential epithelial morphogenesis of early lung and kidney development. V3C18 is a 170 kD protein, which is proteolotically processed into the CRD-containing 50 kD glucoprotein precursor that binds Wnt3a through its CRD domain and suppresses the Wnt3a-induced stabilization of beta catenin. Full-length V3C18 is unable to inhibit Wnt signaling.


Pssm-ID: 143564  Cd Length: 123  Bit Score: 195.42  E-value: 3.87e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534056 366 STSRCLPLPPTLTLCSRLGIGHFWLPNHLHHTDSVEVEATVQAWGRFLHTNCHPFLAWFFCLLLAPSCGPGPPPPLPPCR 445
Cdd:cd07455    1 PRPRCLPVPSSLPFCSRLGIRSFWLPNFLNHTSVEEVRAVLAEWAWLLESGCHPSLEWFFCLLLVPSCGGGPPPPPPPCR 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 755534056 446 QFCEALEDECWNYLAGDRLPVVCASLPSQEDGYCVFIGPAAEN 488
Cdd:cd07455   81 QFCEVLQDSCWNLLEGGRLPVACASLPEQEDGYCVLIGPPAEN 123
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 492-680 8.48e-51

Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of thrombospondin


Pssm-ID: 214560  Cd Length: 184  Bit Score: 176.78  E-value: 8.48e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534056   492 EVGLLQLLGDP-LPEKISQIDDPHVG-PAYIFGPDSNSGQVAQYHFPKLFFRDFSLLFHVRPATEAAGVLFAITDaAQVV 569
Cdd:smart00210   1 GQDLLQVFDLPsLSFAIRQVVGPEPGsPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPKSRGVLFAIYD-AQNV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534056   570 VSLGVKLsevrDGQQNISLLYTEpGASQTQTGASFR-LPAFVGQWTHFALSVDGGSVALYVDCEEFQRVPFARASQglEL 648
Cdd:smart00210  80 RQFGLEV----DGRANTLLLRYQ-GVDGKQHTVSFRnLPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGQ--PP 152

                          170       180       190
                   ....*....|....*....|....*....|..
gi 755534056   649 ERGAGLFVGQAGTADPDKFQGMISELKVRKTP 680
Cdd:smart00210 153 IDTDGIEVRGAQAADRKPFQGDLQQLKIVCDP 184
DUF959 pfam06121
Domain of Unknown Function (DUF959); This N-terminal domain is not expressed in the 'Short' ...
 37-218 5.14e-47

Domain of Unknown Function (DUF959); This N-terminal domain is not expressed in the 'Short' isoform of Collagen A.


Pssm-ID: 399255 [Multi-domain]  Cd Length: 192  Bit Score: 166.54  E-value: 5.14e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534056   37 LVWLWPPKTSDSLEGPVSKPQNSSPVQSTENPTTHVVPQDGLTEQQTTPASselppEEEEEEDQKAGQGGSPATPAVPIP 116
Cdd:pfam06121  16 LDLLWFLDIADPEDTLASEPQGGLAVQPAAAPATHVAPQDDPAEQATAAAS-----PELPLEELEAAPGRAPGAPISAAA 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534056  117 LVAPAASPDMKEENVAGVGAKILNVAQGIRSFVQLWDEDSTIGHSAGTEVPDSSIPTVLPSPAELSSAPQGSKTTLWLSS 196
Cdd:pfam06121  91 PAALAARPDMREENVAGVGAKILNIAQGIQSFIQLWNDAAPTESPAGAGTLAASAPTDPLALAEPSGPAAESGTALGPHR 170

                         170       180
                  ....*....|....*....|..
gi 755534056  197 AIPSSPDAQTTEAGTLAVPTQL 218
Cdd:pfam06121 171 GALSSLDTPRAESGTLAVPTQL 192
FRI smart00063
Frizzled; Drosophila melanogaster frizzled mediates signalling that polarises a precursor cell ...
 370-482 2.14e-29

Frizzled; Drosophila melanogaster frizzled mediates signalling that polarises a precursor cell along the anteroposterior axis. Homologues of the N-terminal region of frizzled exist either as transmembrane or secreted molecules. Frizzled homologues are reported to be receptors for the Wnt growth factors. (Not yet in MEDLINE: the FRI domain occurs in several receptor tyrosine kinases [Xu, Y.K. and Nusse, Curr. Biol. 8 R405-R406 (1998); Masiakowski, P. and Yanopoulos, G.D., Curr. Biol. 8, R407 (1998)].


Pssm-ID: 214498  Cd Length: 113  Bit Score: 113.17  E-value: 2.14e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534056   370 CLPLppTLTLCSRLGIGHFWLPNHLHHTDSVEVEATVQAWGRFLHTNCHPFLAWFFCLLLApSCGPGPPPPLPPCRQFCE 449
Cdd:smart00063   1 CEPI--TIPLCKDLGYNLTSMPNLLGHTTQEEAGLELEQFHPLLNVQCSPDLRFFLCSVYA-PICTEDLRPILPCRSLCE 77

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 755534056   450 ALEDECWNYLAGDRLP----VVCASLPSQEDgYCVFI 482
Cdd:smart00063  78 AAREGCEPLMEKFGFPwpefLRCDRFPVQEE-LCMDP 113
Fz pfam01392
Fz domain; Also known as the CRD (cysteine rich domain), the C6 box in MuSK receptor. This ...
 370-474 1.91e-13

Fz domain; Also known as the CRD (cysteine rich domain), the C6 box in MuSK receptor. This domain of unknown function has been independently identified by several groups. The domain contains 10 conserved cysteines.


Pssm-ID: 460190  Cd Length: 116  Bit Score: 67.59  E-value: 1.91e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534056  370 CLPLppTLTLCSRLGIGHFWLPNHLHHTDSVEVE-----ATVQAWGRFLHTNCHPFLAWFFCLLLAPSCGPGPPPPLPPC 444
Cdd:pfam01392   1 CEPI--TLPMCLGLGYNATVFPNLLGHQTQEEAElslayLVLSEFEPLVDLSCSPSLRLFLCSLYFPPCTLGPSPKPVCP 78

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 755534056  445 --RQFCEALEDECWNYLAGDR----LP--VVCASLPSQ 474
Cdd:pfam01392  79 pcRSLCEEVRYGCEPLLEEAKfgfsWPefLDCDSLPAD 116
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 528-676 2.07e-06

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.


Pssm-ID: 238058 [Multi-domain]  Cd Length: 151  Bit Score: 48.57  E-value: 2.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534056 528 GQVAQYHFPKLFFRDFSLLFHVRPaTEAAGVLFAITDAAQV-VVSLgvklsEVRDGQqnISLLYTEPGASqtqtgASFRL 606
Cdd:cd00110    7 SSYVRLPTLPAPRTRLSISFSFRT-TSPNGLLLYAGSQNGGdFLAL-----ELEDGR--LVLRYDLGSGS-----LVLSS 73

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755534056 607 PAFV--GQWTHFALSVDGGSVALYVDCEEFQRVPFARASQGLELErgAGLFVG-------QAGTADPDKFQGMISELKV 676
Cdd:cd00110   74 KTPLndGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLD--GPLYLGglpedlkSPGLPVSPGFVGCIRDLKV 150
Laminin_G_3 pfam13385
Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin ...
 542-676 1.80e-05

Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin A-like lectin/glucanases superfamily.


Pssm-ID: 463865 [Multi-domain]  Cd Length: 151  Bit Score: 45.84  E-value: 1.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534056  542 DFSLLFHVRP--ATEAAGVLFAITDAAQVVVSLGvklsevRDGQQNISLLYTEPGASQTQTGASFRLpafvGQWTHFALS 619
Cdd:pfam13385  18 DFTVSAWVKPdsLPGWARAIISSSGGGGYSLGLD------GDGRLRFAVNGGNGGWDTVTSGASVPL----GQWTHVAVT 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 755534056  620 VDGGSVALYVDCEEFQRVPfarASQGLELERGAGLFVGQAGTADPDkFQGMISELKV 676
Cdd:pfam13385  88 YDGGTLRLYVNGVLVGSST---LTGGPPPGTGGPLYIGRSPGGDDY-FNGLIDEVRI 140
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 840-875 3.05e-05

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.48  E-value: 3.05e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 755534056  840 PGRDGEPGDPGEDGRPGDTGPQGFPGTPGDVGPKGE 875
Cdd:pfam01391  21 PGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 836-874 6.14e-04

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 43.36  E-value: 6.14e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 755534056 836 KDGTPGRDGEPGDPGEDGRPGDTGPQGFPGTPGDVGPKG 874
Cdd:NF038329 294 KDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDG 332
MJ1470 COG5306
Uncharacterized conserved protein MJ1470, contains DUF2341 domain, predicted component of type ...
 553-630 3.27e-03

Uncharacterized conserved protein MJ1470, contains DUF2341 domain, predicted component of type IV pili-like system [General function prediction only];


Pssm-ID: 444105 [Multi-domain]  Cd Length: 529  Bit Score: 41.04  E-value: 3.27e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755534056 553 TEAAGVLFAITDAAQVVVSLGVKLSEVRDGQQNISLlytePGASQTQTGASFRLPAfvGQWTHFALSVDGGSVALYVD 630
Cdd:COG5306  200 TFSAWIKPAQLDGNAVLYSRRDGANGLDNGAPFVEV----GGAGGTRSAAGAPLAA--GTWHHLAVVADAGKVTLYVN 271
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
 42-282 5.06e-03

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 40.68  E-value: 5.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534056  42 PPKTSDSLEGPvskpqnsSPVqstenPTTHVVPQDGLTEQQTTPASSElppeeeeeedQKAGQGGSPAT-------PAVP 114
Cdd:PLN03209 329 PPKESDAADGP-------KPV-----PTKPVTPEAPSPPIEEEPPQPK----------AVVPRPLSPYTayedlkpPTSP 386

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534056 115 IPLVAPAASPDMKEENVAGVGAKI-LNVAQGIRSFVqlwDEDSTIGHSAGTEVPDSSI-------PTVLPSPaelsSAPQ 186
Cdd:PLN03209 387 IPTPPSSSPASSKSVDAVAKPAEPdVVPSPGSASNV---PEVEPAQVEAKKTRPLSPYaryedlkPPTSPSP----TAPT 459

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534056 187 GSKTTLWLSSAIPSSPDaqtTEAGTLAVPTQLPPfqsnlqAPLGRPSAPpdFPGRAFLSSPRIRAP--PWGNQEPPRQPQ 264
Cdd:PLN03209 460 GVSPSVSSTSSVPAVPD---TAPATAATDAAAPP------PANMRPLSP--YAVYDDLKPPTSPSPaaPVGKVAPSSTNE 528

                        250
                 ....*....|....*...
gi 755534056 265 HLEGKGFLPMTARSSQQH 282
Cdd:PLN03209 529 VVKVGNSAPPTALADEQH 546
 
Name Accession Description Interval E-value
CRD_Collagen_XVIII cd07455
Cysteine-rich domain of the variant 3 of collagen XVIII (V3C18 ); The cysteine-rich domain ...
 366-488 3.87e-58

Cysteine-rich domain of the variant 3 of collagen XVIII (V3C18 ); The cysteine-rich domain (CRD) is an essential part of the variant 3 of collagen XVIII (V3C18), which regulates major cellular functions such as the differential epithelial morphogenesis of early lung and kidney development. V3C18 is a 170 kD protein, which is proteolotically processed into the CRD-containing 50 kD glucoprotein precursor that binds Wnt3a through its CRD domain and suppresses the Wnt3a-induced stabilization of beta catenin. Full-length V3C18 is unable to inhibit Wnt signaling.


Pssm-ID: 143564  Cd Length: 123  Bit Score: 195.42  E-value: 3.87e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534056 366 STSRCLPLPPTLTLCSRLGIGHFWLPNHLHHTDSVEVEATVQAWGRFLHTNCHPFLAWFFCLLLAPSCGPGPPPPLPPCR 445
Cdd:cd07455    1 PRPRCLPVPSSLPFCSRLGIRSFWLPNFLNHTSVEEVRAVLAEWAWLLESGCHPSLEWFFCLLLVPSCGGGPPPPPPPCR 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 755534056 446 QFCEALEDECWNYLAGDRLPVVCASLPSQEDGYCVFIGPAAEN 488
Cdd:cd07455   81 QFCEVLQDSCWNLLEGGRLPVACASLPEQEDGYCVLIGPPAEN 123
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 492-680 8.48e-51

Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of thrombospondin


Pssm-ID: 214560  Cd Length: 184  Bit Score: 176.78  E-value: 8.48e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534056   492 EVGLLQLLGDP-LPEKISQIDDPHVG-PAYIFGPDSNSGQVAQYHFPKLFFRDFSLLFHVRPATEAAGVLFAITDaAQVV 569
Cdd:smart00210   1 GQDLLQVFDLPsLSFAIRQVVGPEPGsPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPKSRGVLFAIYD-AQNV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534056   570 VSLGVKLsevrDGQQNISLLYTEpGASQTQTGASFR-LPAFVGQWTHFALSVDGGSVALYVDCEEFQRVPFARASQglEL 648
Cdd:smart00210  80 RQFGLEV----DGRANTLLLRYQ-GVDGKQHTVSFRnLPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGQ--PP 152

                          170       180       190
                   ....*....|....*....|....*....|..
gi 755534056   649 ERGAGLFVGQAGTADPDKFQGMISELKVRKTP 680
Cdd:smart00210 153 IDTDGIEVRGAQAADRKPFQGDLQQLKIVCDP 184
DUF959 pfam06121
Domain of Unknown Function (DUF959); This N-terminal domain is not expressed in the 'Short' ...
 37-218 5.14e-47

Domain of Unknown Function (DUF959); This N-terminal domain is not expressed in the 'Short' isoform of Collagen A.


Pssm-ID: 399255 [Multi-domain]  Cd Length: 192  Bit Score: 166.54  E-value: 5.14e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534056   37 LVWLWPPKTSDSLEGPVSKPQNSSPVQSTENPTTHVVPQDGLTEQQTTPASselppEEEEEEDQKAGQGGSPATPAVPIP 116
Cdd:pfam06121  16 LDLLWFLDIADPEDTLASEPQGGLAVQPAAAPATHVAPQDDPAEQATAAAS-----PELPLEELEAAPGRAPGAPISAAA 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534056  117 LVAPAASPDMKEENVAGVGAKILNVAQGIRSFVQLWDEDSTIGHSAGTEVPDSSIPTVLPSPAELSSAPQGSKTTLWLSS 196
Cdd:pfam06121  91 PAALAARPDMREENVAGVGAKILNIAQGIQSFIQLWNDAAPTESPAGAGTLAASAPTDPLALAEPSGPAAESGTALGPHR 170

                         170       180
                  ....*....|....*....|..
gi 755534056  197 AIPSSPDAQTTEAGTLAVPTQL 218
Cdd:pfam06121 171 GALSSLDTPRAESGTLAVPTQL 192
FRI smart00063
Frizzled; Drosophila melanogaster frizzled mediates signalling that polarises a precursor cell ...
 370-482 2.14e-29

Frizzled; Drosophila melanogaster frizzled mediates signalling that polarises a precursor cell along the anteroposterior axis. Homologues of the N-terminal region of frizzled exist either as transmembrane or secreted molecules. Frizzled homologues are reported to be receptors for the Wnt growth factors. (Not yet in MEDLINE: the FRI domain occurs in several receptor tyrosine kinases [Xu, Y.K. and Nusse, Curr. Biol. 8 R405-R406 (1998); Masiakowski, P. and Yanopoulos, G.D., Curr. Biol. 8, R407 (1998)].


Pssm-ID: 214498  Cd Length: 113  Bit Score: 113.17  E-value: 2.14e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534056   370 CLPLppTLTLCSRLGIGHFWLPNHLHHTDSVEVEATVQAWGRFLHTNCHPFLAWFFCLLLApSCGPGPPPPLPPCRQFCE 449
Cdd:smart00063   1 CEPI--TIPLCKDLGYNLTSMPNLLGHTTQEEAGLELEQFHPLLNVQCSPDLRFFLCSVYA-PICTEDLRPILPCRSLCE 77

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 755534056   450 ALEDECWNYLAGDRLP----VVCASLPSQEDgYCVFI 482
Cdd:smart00063  78 AAREGCEPLMEKFGFPwpefLRCDRFPVQEE-LCMDP 113
CRD_FZ cd07066
CRD_domain cysteine-rich domain, also known as Fz (frizzled) domain; CRD_FZ is an essential ...
 369-480 4.92e-17

CRD_domain cysteine-rich domain, also known as Fz (frizzled) domain; CRD_FZ is an essential component of a number of cell surface receptors, which are involved in multiple signal transduction pathways, particularly in modulating the activity of the Wnt proteins, which play a fundamental role in the early development of metazoans. CRD is also found in secreted frizzled related proteins (SFRPs), which lack the transmembrane segment found in the frizzled protein. The CRD domain is also present in the alpha-1 chain of mouse type XVIII collagen, in carboxypeptidase Z, several receptor tyrosine kinases, and the mosaic transmembrane serine protease corin. The CRD domain is well conserved in metazoans - 10 frizzled proteins have been identified in mammals, 4 in Drosophila and 3 in Caenorhabditis elegans. CRD domains have also been identified in multiple tandem copies in a Dictyostelium discoideum protein. Very little is known about the mechanism by which CRD domains interact with their ligands. The domain contains 10 conserved cysteines.


Pssm-ID: 143549  Cd Length: 119  Bit Score: 77.93  E-value: 4.92e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534056 369 RCLPLPptLTLCSRLGIGHFWLPNHLHHTDSVEVEATVQAWGRFLHTNCHPFLAWFFCLLLAPSCGPGPPPPLPPCRQFC 448
Cdd:cd07066    1 KCEPIP--LPLCRGLPYNTTRFPNLLGHESQEEAEQELESFTPLVNSGCHPDLRFFLCSLYFPECTPDGDRPIPPCRSLC 78

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 755534056 449 EALEDECWNYLAG----DRLPVVCASLPSQ-EDGYCV 480
Cdd:cd07066   79 EEVRDSCEPLMLAfgfpWPEPLDCDRFPDSnEEGLCI 115
Fz pfam01392
Fz domain; Also known as the CRD (cysteine rich domain), the C6 box in MuSK receptor. This ...
 370-474 1.91e-13

Fz domain; Also known as the CRD (cysteine rich domain), the C6 box in MuSK receptor. This domain of unknown function has been independently identified by several groups. The domain contains 10 conserved cysteines.


Pssm-ID: 460190  Cd Length: 116  Bit Score: 67.59  E-value: 1.91e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534056  370 CLPLppTLTLCSRLGIGHFWLPNHLHHTDSVEVE-----ATVQAWGRFLHTNCHPFLAWFFCLLLAPSCGPGPPPPLPPC 444
Cdd:pfam01392   1 CEPI--TLPMCLGLGYNATVFPNLLGHQTQEEAElslayLVLSEFEPLVDLSCSPSLRLFLCSLYFPPCTLGPSPKPVCP 78

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 755534056  445 --RQFCEALEDECWNYLAGDR----LP--VVCASLPSQ 474
Cdd:pfam01392  79 pcRSLCEEVRYGCEPLLEEAKfgfsWPefLDCDSLPAD 116
CRD_sizzled cd07452
Cysteine-rich domain of the sizzled protein; The cysteine-rich domain (CRD) is an essential ...
 367-476 8.75e-11

Cysteine-rich domain of the sizzled protein; The cysteine-rich domain (CRD) is an essential part of the sizzled protein, which regulates bone morphogenetic protein (Bmp) signaling by stabilizing chordin, and plays a critical role in the patterning of vertebrate and invertebrate embryos. Sizzled also functions in the ventral region as a Wnt inhibitor and modulates canonical Wnt signaling. Sizzled proteins belong to the secreted frizzled-related protein family (SFRP), and have be identified in the genomes of birds, fishes and frogs, but not mammals.


Pssm-ID: 143561  Cd Length: 141  Bit Score: 60.66  E-value: 8.75e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534056 367 TSRCLPLPPTLTLCSRLGIGHFWLPNHLHHTDSVEVEATVQAWGRFLHTNCHPFLAWFFCLLLApscGPGPPPPLPPCRQ 446
Cdd:cd07452    6 STKCVPIPPEMSMCQDVGYSEMRLPNLLGHTSMAEVVPKSADWQTLLHTGCHPHARTFLCSLFA---PVCLDTFIQPCRS 82

                         90       100       110
                 ....*....|....*....|....*....|....
gi 755534056 447 FCEALEDECWNYLA--GDRLP--VVCASLPSQED 476
Cdd:cd07452   83 MCVAVRDSCAPVLAchGHSWPesLDCDRFPAGED 116
CRD_SFRP1 cd07443
Cysteine-rich domain of the secreted frizzled-related protein 1 (SFRP1), a regulator of Wnt ...
 365-455 3.41e-09

Cysteine-rich domain of the secreted frizzled-related protein 1 (SFRP1), a regulator of Wnt activity; The cysteine-rich domain (CRD) is an essential part of the secreted frizzled-related protein 1 (SFRP1), which regulates the activity of Wnt proteins, key players in a number of fundamental cellular processes such as embryogenesis and postnatal development. SFRPs antagonize the activation of Wnt signaling by binding to the CRDs domains of frizzled (Fz) proteins, thereby preventing Wnt proteins from binding to these receptors. SFRPs are also known to have functions unrelated to Wnt, as enhancers of procollagen cleavage by the TLD proteinases. SFRPs and Fz proteins both contain CRD domains, but SFRPs lack the seven-pass transmembrane domain which is an integral part of Fzs. SFRP1 is expressed in many tissues and is involved in the regulation of Wnt signaling in osteoblasts, leading to enhanced trabecular bone formation in adults; it has also been shown to control the growth of retinal ganglion cell axons and the elongation of the antero-posterior axis.


Pssm-ID: 143552  Cd Length: 124  Bit Score: 55.67  E-value: 3.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534056 365 TSTSRCLPLPPTLTLCSRLGIGHFWLPNHLHHTDSVEVEATVQAWGRFLHTNCHPFLAWFFCLLLApscGPGPPPPLPPC 444
Cdd:cd07443    2 TKPPQCVDIPADLRLCHNVGYKKMVLPNLLDHETMAEVKQQASSWVPLLNKNCHKGTQVFLCSLFA---PVCLDRPVYPC 78

                         90
                 ....*....|.
gi 755534056 445 RQFCEALEDEC 455
Cdd:cd07443   79 RWLCEAVRDSC 89
CRD_SFRP2 cd07446
Cysteine-rich domain of the secreted frizzled-related protein 2 (SFRP2), a regulator of Wnt ...
 368-455 4.38e-07

Cysteine-rich domain of the secreted frizzled-related protein 2 (SFRP2), a regulator of Wnt activity; The cysteine-rich-domain (CRD) is an essential part of the secreted frizzled related protein 2 (SFRP2), which regulates the activity of Wnt proteins, key players in a number of fundamental cellular processes such as embryogenesis and postnatal development. SFRPs antagonize the activation of Wnt signaling by binding to CRD domains of frizzled (Fz) proteins, thereby preventing Wnt proteins from binding to these receptors. SFRPs and Fz proteins both contain CRD domains, but SFRPs lack the seven-pass transmembrane domain which is an integral part of Fzs. As a Wnt antagonist, SFRP2 regulates Nkx2.2 expression in the ventral spinal cord and anteroposterior axis elongation. SFRP2 also has a Wnt-independent function as an enhancer of procollagen cleavage by the TLD proteinases. SFRP2 binds both procollagen and TLD, thus facilitating the enzymatic reaction by bringing together the proteinase and its substrate.


Pssm-ID: 143555  Cd Length: 128  Bit Score: 49.91  E-value: 4.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534056 368 SRCLPLPPTLTLCSRLGIGHFWLPNHLHHTDSVEVEATVQAWGRFLHTNCHPFLAWFFCLLLAPSCGPGPPPPLPPCRQF 447
Cdd:cd07446    3 SNCKPIPANMLLCHGIEYTNMRLPNLLGHETMKEVLQQAGSWIPLVQKQCHPDTKKFLCSLFAPVCLDDLDEAIQPCRSL 82


                 ....*...
gi 755534056 448 CEALEDEC 455
Cdd:cd07446   83 CEAVKDGC 90
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 528-676 2.07e-06

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.


Pssm-ID: 238058 [Multi-domain]  Cd Length: 151  Bit Score: 48.57  E-value: 2.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534056 528 GQVAQYHFPKLFFRDFSLLFHVRPaTEAAGVLFAITDAAQV-VVSLgvklsEVRDGQqnISLLYTEPGASqtqtgASFRL 606
Cdd:cd00110    7 SSYVRLPTLPAPRTRLSISFSFRT-TSPNGLLLYAGSQNGGdFLAL-----ELEDGR--LVLRYDLGSGS-----LVLSS 73

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755534056 607 PAFV--GQWTHFALSVDGGSVALYVDCEEFQRVPFARASQGLELErgAGLFVG-------QAGTADPDKFQGMISELKV 676
Cdd:cd00110   74 KTPLndGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLD--GPLYLGglpedlkSPGLPVSPGFVGCIRDLKV 150
CRD_crescent cd07453
Cysteine-rich domain of the crescent protein; The cysteine-rich domain (CRD) is an essential ...
 368-455 2.42e-06

Cysteine-rich domain of the crescent protein; The cysteine-rich domain (CRD) is an essential part of the crescent protein, a member of the secreted frizzled-related protein (SFRP) family, which regulates convergent extension movements (CEMs) during gastrulation and neurulation. Xenopus laevis crescent efficiently forms inhibitory complexes with Wnt5a and Wnt11, but this effect is cancelled in the presence of another member of the SFRP family, Frzb1. A potential role for Crescent in head formation is to regulate a non-canonical Wnt pathway positively in the adjacent posterior mesoderm, and negatively in the overlying anterior neuroectoderm.


Pssm-ID: 143562 [Multi-domain]  Cd Length: 135  Bit Score: 48.01  E-value: 2.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534056 368 SRCLPLPPTLTLCSRLGIGHFWLPNHLHHTDSVEVEATVQAWGRFLHTNCHPFLAWFFCLLLApscGPGPPPPLPPCRQF 447
Cdd:cd07453    1 SPCMRIPKSMALCYDIGYSEMRIPNLLEHETMAEVIQQSSSWLPLLARECHPDARIFLCSLFA---PICWDRPIYPCRSL 77


                 ....*...
gi 755534056 448 CEALEDEC 455
Cdd:cd07453   78 CEAVRSSC 85
LamG smart00282
Laminin G domain;
544-676 1.56e-05

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 45.41  E-value: 1.56e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534056   544 SLLFHVRPaTEAAGVLFAITDAAQV-VVSLgvklsEVRDGQqnISLLYTEPGASQTQTGASFRLPAfvGQWTHFALSVDG 622
Cdd:smart00282   1 SISFSFRT-TSPNGLLLYAGSKGGGdYLAL-----ELRDGR--LVLRYDLGSGPARLTSDPTPLND--GQWHRVAVERNG 70

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755534056   623 GSVALYVDCEEFQRVPFARASQGLELErgAGLFVG-------QAGTADPDKFQGMISELKV 676
Cdd:smart00282  71 RSVTLSVDGGNRVSGESPGGLTILNLD--GPLYLGglpedlkLPPLPVTPGFRGCIRNLKV 129
CRD_SFRP5 cd07444
Cysteine-rich domain of the secreted frizzled-related protein 5 (SFRP5), a regulator of Wnt ...
 365-455 1.64e-05

Cysteine-rich domain of the secreted frizzled-related protein 5 (SFRP5), a regulator of Wnt activity; The cysteine-rich domain (CRD) is an essential part of the secreted frizzled-related Protein 5 (SFRP5), which regulates the activity of Wnt proteins, key players in a number of fundamental cellular processes such as embryogenesis and postnatal development. SFRPs antagonize the activation of Wnt signaling by binding to the CRD domains of frizzled (Fz) proteins, thereby preventing Wnt proteins from binding to these receptors. SFRPs are also known to have functions unrelated to Wnt, as enhancers of procollagen cleavage by the TLD proteinases. SFRPs and Fz proteins both contain CRD domains, but SFRPs lack the seven-pass transmembrane domain which is an integral part of Fzs.


Pssm-ID: 143553  Cd Length: 127  Bit Score: 45.32  E-value: 1.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534056 365 TSTSRCLPLPPTLTLCSRLGIGHFWLPNHLHHTDSVEVEATVQAWGRFLHTNCHPFLAWFFCLLLApscGPGPPPPLPPC 444
Cdd:cd07444    2 SKQPQCVDIPADLPLCHNVGYKRMRLPNLLEHESMAEVKQQASSWVPLLAKRCHADTQVFLCSLFA---PVCLDRPIYPC 78

                         90
                 ....*....|.
gi 755534056 445 RQFCEALEDEC 455
Cdd:cd07444   79 RSLCEAVRDSC 89
Laminin_G_3 pfam13385
Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin ...
 542-676 1.80e-05

Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin A-like lectin/glucanases superfamily.


Pssm-ID: 463865 [Multi-domain]  Cd Length: 151  Bit Score: 45.84  E-value: 1.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534056  542 DFSLLFHVRP--ATEAAGVLFAITDAAQVVVSLGvklsevRDGQQNISLLYTEPGASQTQTGASFRLpafvGQWTHFALS 619
Cdd:pfam13385  18 DFTVSAWVKPdsLPGWARAIISSSGGGGYSLGLD------GDGRLRFAVNGGNGGWDTVTSGASVPL----GQWTHVAVT 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 755534056  620 VDGGSVALYVDCEEFQRVPfarASQGLELERGAGLFVGQAGTADPDkFQGMISELKV 676
Cdd:pfam13385  88 YDGGTLRLYVNGVLVGSST---LTGGPPPGTGGPLYIGRSPGGDDY-FNGLIDEVRI 140
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 840-875 3.05e-05

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.48  E-value: 3.05e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 755534056  840 PGRDGEPGDPGEDGRPGDTGPQGFPGTPGDVGPKGE 875
Cdd:pfam01391  21 PGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
CRD_SFRP4 cd07442
Cysteine-rich domain of the secreted frizzled-related protein 4 (SFRP4), a Wnt antagonist; The ...
 370-486 1.22e-04

Cysteine-rich domain of the secreted frizzled-related protein 4 (SFRP4), a Wnt antagonist; The cysteine-rich domain (CRD) is an essential part of the secreted frizzled-related Protein 4 (SFRP4), which regulates the activity of Wnt proteins, key players in a number of fundamental cellular processes such as embryogenesis and postnatal development. SFRPs antagonize the activation of Wnt signaling by binding to the CRDs domains of frizzled (Fz) proteins, thereby preventing Wnt proteins from binding to these receptors. SFRPs are also known to have functions unrelated to Wnt, as enhancers of procollagen cleavage by the TLD proteinases. SFRPs and Fz proteins both contain CRD domains, but SFRPs lack the seven-pass transmembrane domain which is an integral part of Fzs.


Pssm-ID: 143551  Cd Length: 127  Bit Score: 42.71  E-value: 1.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534056 370 CLPLPPTLTLcsrlgighfwLPNHLHHTDSVEVEATVQAWGRFLHTNCHPFLAWFFCLLLAPS-CGPGPPPPLPPCRQFC 448
Cdd:cd07442   13 CRHMPWNITR----------MPNHLHHSTQENAVLAIEQYEELVDTGCSPVLPFFLCAMYAPIcTLEFLYDPIKPCRSVC 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 755534056 449 EALEDEC------WNYLAGDRLpvVCASLPSQEDGYCvfIGPAA 486
Cdd:cd07442   83 QRARDGCepimrrYNHSWPESL--ACDDLPVYDRGVC--ISPEA 122
CRD_LIN_17 cd07454
Cysteine-rich domain (CRD) of LIN_17; A cysteine-rich domain (CRD) is an essential component ...
 366-476 2.21e-04

Cysteine-rich domain (CRD) of LIN_17; A cysteine-rich domain (CRD) is an essential component of a number of cell surface receptors, which are involved in multiple signal transduction pathways, particularly in modulating the activity of the Wnt proteins, which play a fundamental role in the early development of metazoans. CRD is also found in secreted frizzled related proteins (SFRPs), which lack the transmembrane segment found in the frizzled protein. The CRD domain is also present in the alpha-1 chain of mouse type XVIII collagen, in carboxypeptidase Z, several receptor tyrosine kinases, and the mosaic transmembrane serine protease corin. The CRD domain is well conserved in metazoans - 10 frizzled proteins have been identified in mammals, 4 in Drosophila and 3 in Caenorhabditis elegans. CRD domains have also been identified in multiple tandem copies in a Dictyostelium discoideum protein. Very little is known about the mechanism by which CRD domains interact with their ligands. The domain contains 10 conserved cysteines. The protein lin-17 is involved in cell type specification during Caenorhabditis elegans vulval development.


Pssm-ID: 143563  Cd Length: 124  Bit Score: 42.08  E-value: 2.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534056 366 STSRCLPLPPTLtlCSRLGIGHFWLPNHLHHTDSVEVEATVQAWGRFLHTNCHPFLAWFFCLLLAPSCGPGPPPPLPPCR 445
Cdd:cd07454    1 VKGKCIPIDIEL--CKDLPYNYTYFPNTILHNDQHTLQTHTEHFKPLMKTKCHPHIHFFICSVFAPMCPIGMPQAVTSCK 78

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 755534056 446 QFCEALEDECWNYLA--GDRLP--VVCASLPSQED 476
Cdd:cd07454   79 SVCEQVKADCFSILEefGIGWPepLNCAQFPDPPE 113
CRD_FZ9 cd07463
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 9 (Fz9) receptor; The cysteine-rich ...
 368-476 3.13e-04

Cysteine-rich Wnt-binding domain (CRD) of the frizzled 9 (Fz9) receptor; The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 9 (Fz9) receptor, and is required for binding Wnt proteins, which play fundamental roles in many aspects of early development, such as cell and tissue polarity, neural synapse formation, and the regulation of proliferation. Fz proteins serve as Wnt receptors for multiple signal transduction pathways, including both beta-catenin dependent and -independent cellular signaling, as well as the planar cell polarity pathway and Ca(2+) modulating signaling pathway. CRD containing Fzs have been found in diverse species from amoebas to mammals. 10 different frizzled proteins are found in vertebrata. Fz9 may play a signaling role in lymphoid development and maturation, particularly at points where B cells undergo self-renewal prior to further differentiation.


Pssm-ID: 143572  Cd Length: 127  Bit Score: 41.55  E-value: 3.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534056 368 SRCLPLppTLTLCSRLGIGHFWLPNHLHHTDSVEVEATVQAWGRFLHTNCHPFLAWFFCLLLAPSCGPGPPPPLPPCRQF 447
Cdd:cd07463    3 AKCQPV--VIPMCRGIGYNLTRMPNFLGHDSQREAAIKLNEFAPLVEYGCHVHLRFFLCSLYAPMCTDQVSTSIPACRPM 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 755534056 448 CEALEDEC------WNYLAGDRLPvvCASLPSQED 476
Cdd:cd07463   81 CEQARQKCspimeqFNFGWPESLD--CSRLPTRND 113
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 836-874 6.14e-04

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 43.36  E-value: 6.14e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 755534056 836 KDGTPGRDGEPGDPGEDGRPGDTGPQGFPGTPGDVGPKG 874
Cdd:NF038329 294 KDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDG 332
CRD_FZ9_like cd07457
Cysteine-rich Wnt-binding domain (CRD) of receptors similar to frizzled 9; The cysteine-rich ...
 368-476 7.52e-04

Cysteine-rich Wnt-binding domain (CRD) of receptors similar to frizzled 9; The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 9 (Fz9) and frizzled 10 (Fz10) receptors, and similar proteins. This domain is required for binding Wnt proteins, which play fundamental roles in many aspects of early development, such as cell and tissue polarity, neural synapse formation, and the regulation of proliferation. Fz proteins serve as Wnt receptors for multiple signal transduction pathways, including both beta-catenin dependent and -independent cellular signaling, as well as the planar cell polarity pathway and Ca(2+) modulating signaling pathway. The CRD domain is well conserved in metazoans - 10 frizzled proteins have been identified in mammals, 4 in Drosophila and 3 in Caenorhabditis elegans. Very little is known about the mechanism by which CRD domains interact with their ligands. The domain contains 10 conserved cysteines.


Pssm-ID: 143566  Cd Length: 121  Bit Score: 40.55  E-value: 7.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534056 368 SRCLPLppTLTLCSRLGIGHFWLPNHLHHTDSVEVEATVQAWGRFLHTNCHPFLAWFFCLLLAPSCGPGPPPPLPPCRQF 447
Cdd:cd07457    1 GKCERI--TIPMCQGIGYNMTRMPNLLGHESQSEAAISIHEFAPLVQYGCAEHLRFFLCSLYAPMCTEQVSIPIPACRSM 78

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 755534056 448 CEALEDEC------WNYLAGDRLPvvCASLPSQED 476
Cdd:cd07457   79 CEQARDKCspimeqFSFSWPDSLD--CDRLPRKND 111
CRD_FZ10 cd07462
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 10 (Fz10) receptor; The cysteine-rich ...
 369-476 8.23e-04

Cysteine-rich Wnt-binding domain (CRD) of the frizzled 10 (Fz10) receptor; The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 10 (Fz10) receptor, and is required for binding Wnt proteins, which play fundamental roles in many aspects of early development, such as cell and tissue polarity, neural synapse formation, and the regulation of proliferation. Fz proteins serve as Wnt receptors for multiple signal transduction pathways, including both beta-catenin dependent and -independent cellular signaling, as well as the planar cell polarity pathway and Ca(2+) modulating signaling pathway. CRD containing Fzs have been found in diverse species from amoebas to mammals. 10 different frizzled proteins are found in vertebrata. The cellular functon of Fz10 is unknown.


Pssm-ID: 143571  Cd Length: 127  Bit Score: 40.39  E-value: 8.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534056 369 RCLPLppTLTLCSRLGIGHFWLPNHLHHTDSVEVEATVQAWGRFLHTNCHPFLAWFFCLLLAPSCGPGPPPPLPPCRQFC 448
Cdd:cd07462    4 RCQPI--EIPMCKDIGYNMTRMPNLMGHENQREAAIQLHEFAPLVEYGCHSHLKFFLCSLYAPMCTEQVSTPIPACRVMC 81

                         90       100       110
                 ....*....|....*....|....*....|....
gi 755534056 449 EALEDEC------WNYLAGDRLPvvCASLPSQED 476
Cdd:cd07462   82 EQARLKCspimeqFNFKWPDSLD--CSKLPNKND 113
CRD_corin_2 cd07888
One of two cysteine-rich domains of the corin protein, a type II transmembrane serine protease ...
 374-474 9.72e-04

One of two cysteine-rich domains of the corin protein, a type II transmembrane serine protease ; The cysteine-rich domain (CRD) is an essential component of corin, a type II transmembrane serine protease which functions as the convertase of the pro-atrial natriuretic peptide (pro-ANP) in the heart. Corin contains two CRDs in its extracellular region, which play an important role in recognition of the physiological substrate, pro-ANP. This model characterizes the second (C-terminal) CRD.


Pssm-ID: 143579 [Multi-domain]  Cd Length: 122  Bit Score: 40.00  E-value: 9.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534056 374 PPTLTLCSRLGIGHFWLPNHLHHTDSVEVEATVQA--WGRFLHTNCHPFLAWFFCLLLAPSCGPGPPPPLPPCRQFCEAL 451
Cdd:cd07888    4 PITLELCMNLPYNTTRYPNYLGHRTQKEASISWESslFPALVQTNCYKYLMFFACTILVPKCDPVTQQRIPPCRSLCRNS 83

                         90       100
                 ....*....|....*....|....*..
gi 755534056 452 EDECWNYLA--GDRLP--VVCASLPSQ 474
Cdd:cd07888   84 KERCESVLGivGLQWPedTDCAQFPEE 110
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 841-873 1.04e-03

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 38.24  E-value: 1.04e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 755534056  841 GRDGEPGDPGEDGRPGDTGPQGFPGTPGDVGPK 873
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEP 33
CRD_SFRP3 cd07441
Cysteine-rich domain of the secreted frizzled-related protein 3 (SFRP3, alias FRZB), a Wnt ...
 374-430 2.73e-03

Cysteine-rich domain of the secreted frizzled-related protein 3 (SFRP3, alias FRZB), a Wnt antagonist; The cysteine-rich domain (CRD) is an essential part of the secreted frizzled-related protein 3 (SFRP3, alias FRZB), which plays important roles in embryogenesis and postnatal development as an antagonist of Wnt proteins, key players in a number of fundamental cellular processes. SFRPs antagonize the activation of Wnt signaling by binding to the CRD domains of frizzled proteins (Fz), thereby preventing Wnt proteins from binding to these receptors. SFRPs are also known to have functions unrelated to Wnt, as enhancers of procollagen cleavage by the TLD proteinases. SFRPs and Fz proteins both contain CRD domains, but SFRPs lack the seven-pass transmembrane domain which is an integral part of Fzs. SFRP3 regulates Wnt signaling activity in bone development and homeostasis. It is also involved in the control of planar cell polarity.


Pssm-ID: 143550  Cd Length: 126  Bit Score: 38.88  E-value: 2.73e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 755534056 374 PPTLTLCSRLGIGHFWLPNHLHHTDSVEVEATVQAWGRFLHTNCHPFLAWFFCLLLA 430
Cdd:cd07441    6 PVRIPMCKSMPWNMTKMPNHLHHSTQANAVLAIEQFEGLLGTQCSPDLLFFLCAMYA 62
MJ1470 COG5306
Uncharacterized conserved protein MJ1470, contains DUF2341 domain, predicted component of type ...
 553-630 3.27e-03

Uncharacterized conserved protein MJ1470, contains DUF2341 domain, predicted component of type IV pili-like system [General function prediction only];


Pssm-ID: 444105 [Multi-domain]  Cd Length: 529  Bit Score: 41.04  E-value: 3.27e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755534056 553 TEAAGVLFAITDAAQVVVSLGVKLSEVRDGQQNISLlytePGASQTQTGASFRLPAfvGQWTHFALSVDGGSVALYVD 630
Cdd:COG5306  200 TFSAWIKPAQLDGNAVLYSRRDGANGLDNGAPFVEV----GGAGGTRSAAGAPLAA--GTWHHLAVVADAGKVTLYVN 271
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
 42-282 5.06e-03

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 40.68  E-value: 5.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534056  42 PPKTSDSLEGPvskpqnsSPVqstenPTTHVVPQDGLTEQQTTPASSElppeeeeeedQKAGQGGSPAT-------PAVP 114
Cdd:PLN03209 329 PPKESDAADGP-------KPV-----PTKPVTPEAPSPPIEEEPPQPK----------AVVPRPLSPYTayedlkpPTSP 386

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534056 115 IPLVAPAASPDMKEENVAGVGAKI-LNVAQGIRSFVqlwDEDSTIGHSAGTEVPDSSI-------PTVLPSPaelsSAPQ 186
Cdd:PLN03209 387 IPTPPSSSPASSKSVDAVAKPAEPdVVPSPGSASNV---PEVEPAQVEAKKTRPLSPYaryedlkPPTSPSP----TAPT 459

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534056 187 GSKTTLWLSSAIPSSPDaqtTEAGTLAVPTQLPPfqsnlqAPLGRPSAPpdFPGRAFLSSPRIRAP--PWGNQEPPRQPQ 264
Cdd:PLN03209 460 GVSPSVSSTSSVPAVPD---TAPATAATDAAAPP------PANMRPLSP--YAVYDDLKPPTSPSPaaPVGKVAPSSTNE 528

                        250
                 ....*....|....*...
gi 755534056 265 HLEGKGFLPMTARSSQQH 282
Cdd:PLN03209 529 VVKVGNSAPPTALADEQH 546
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
 553-676 6.50e-03

Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.


Pssm-ID: 460494 [Multi-domain]  Cd Length: 126  Bit Score: 37.78  E-value: 6.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534056  553 TEAAGVLFAITDAAQVVVSLgvklsEVRDGQqnISLLYTEPGASQTQTGASFRLPAfvGQWTHFALSVDGGSVALYVDCE 632
Cdd:pfam02210   4 RQPNGLLLYAGGGGSDFLAL-----ELVNGR--LVLRYDLGSGPESLLSSGKNLND--GQWHSVRVERNGNTLTLSVDGQ 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 755534056  633 EFQRVPFARASQGLELERgaGLFVGQAGTADPDK-------FQGMISELKV 676
Cdd:pfam02210  75 TVVSSLPPGESLLLNLNG--PLYLGGLPPLLLLPalpvragFVGCIRDVRV 123
 
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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