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Conserved domains on  [gi|568966577|ref|XP_006513237|]
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collagen alpha-1(XVIII) chain isoform X2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Endostatin-like cd00247
Endostatin-like domain; the angiogenesis inhibitor endostatin is a C-terminal fragment of ...
 1596-1766 1.16e-113

Endostatin-like domain; the angiogenesis inhibitor endostatin is a C-terminal fragment of collagen XV/XVIII, a proteoglycan/collagen found in vessel walls and basement membranes; this domain has a compact globular fold similar to that of C-type lectins; endostatin XVIII is monomeric and contains a heparin-binding epitope and zinc binding sites while endostatin XV is trimeric and contains neither of these sites; the generation of endostatin or endostatin-like collagen XV/XVIII fragments is catalyzed by proteolytic enzymes within the protease-sensitive hinge region of the C-terminal domain; endostatin inhibits endothelial cell migration in vitro and appears to be highly effective in murine in vivo studies


:

Pssm-ID: 238151  Cd Length: 171  Bit Score: 356.64  E-value: 1.16e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577 1596 QPVLHLVALNTPLSGGMRGIRGADFQCFQQARAVGLSGTFRAFLSSRLQDLYSIVRRADRGSVPIVNLKDEVLSPSWDSL 1675
Cdd:cd00247     1 QPVLHLVALNTPLSGDMRGIRGADFQCFQQARAAGLKGTFRAFLSSRLQDLYSIVRRADRDSLPIVNLKGEVLFNSWESL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577 1676 FSGSQGQLQPGARIFSFDGRDVLRHPAWPQKSVWHGSDPSGRRLMESYCETWRTETTGATGQASSLLSGRLLEQKAASCH 1755
Cdd:cd00247    81 FSGSGGQFNPGARIYSFDGRDVLTDPAWPQKMVWHGSDPNGRRLTDSYCEAWRTGDSAVTGQASSLSSGKLLEQKAYSCE 160

                         170
                  ....*....|.
gi 568966577 1756 NSYIVLCIENS 1766
Cdd:cd00247   161 NKLIVLCIENS 171
CRD_Collagen_XVIII cd07455
Cysteine-rich domain of the variant 3 of collagen XVIII (V3C18 ); The cysteine-rich domain ...
 366-488 4.00e-59

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: 199.27  E-value: 4.00e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577  366 STSRCLPLPPTLTLCSRLGIGHFWLPNHLHHTDSVEVEATVQAWGRFLHTNCHPFLAWFFCLLLAPSCGPGPPPPLPPCR 445
Cdd:cd07455     1 PRPRCLPVPSSLPFCSRLGIRSFWLPNFLNHTSVEEVRAVLAEWAWLLESGCHPSLEWFFCLLLVPSCGGGPPPPPPPCR 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 568966577  446 QFCEALEDECWNYLAGDRLPVVCASLPSQEDGYCVFIGPAAEN 488
Cdd:cd07455    81 QFCEVLQDSCWNLLEGGRLPVACASLPEQEDGYCVLIGPPAEN 123
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 492-680 8.18e-51

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


:

Pssm-ID: 214560  Cd Length: 184  Bit Score: 177.93  E-value: 8.18e-51
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577    492 EVGLLQLLGDP-LPEKISQIDDPHVG-PAYIFGPDSNSGQVAQYHFPKLFFRDFSLLFHVRPATEAAGVLFAITDaAQVV 569
Cdd:smart00210    1 GQDLLQVFDLPsLSFAIRQVVGPEPGsPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPKSRGVLFAIYD-AQNV 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577    570 VSLGVKLsevrDGQQNISLLYTEpGASQTQTGASFR-LPAFVGQWTHFALSVDGGSVALYVDCEEFQRVPFARASQglEL 648
Cdd:smart00210   80 RQFGLEV----DGRANTLLLRYQ-GVDGKQHTVSFRnLPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGQ--PP 152

                           170       180       190
                    ....*....|....*....|....*....|..
gi 568966577    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 2.50e-48

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: 171.17  E-value: 2.50e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577    37 LVWLWPPKTSDSLEGPVSKPQNSSPVQSTENPTTHVVPQDGLTEQQTTPASselppEEEEEEDQKAGQGGSPATPAVPIP 116
Cdd:pfam06121   16 LDLLWFLDIADPEDTLASEPQGGLAVQPAAAPATHVAPQDDPAEQATAAAS-----PELPLEELEAAPGRAPGAPISAAA 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577   117 LVAPAASPDMKEENVAGVGAKILNVAQGIRSFVQLWDEDSTIGHSAGTEVPDSSIPTVLPSPAELSSAPQGSKTTLWLSS 196
Cdd:pfam06121   91 PAALAARPDMREENVAGVGAKILNIAQGIQSFIQLWNDAAPTESPAGAGTLAASAPTDPLALAEPSGPAAESGTALGPHR 170

                          170       180
                   ....*....|....*....|..
gi 568966577   197 AIPSSPDAQTTEAGTLAVPTQL 218
Cdd:pfam06121  171 GALSSLDTPRAESGTLAVPTQL 192
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1066-1322 3.32e-26

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.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 113.85  E-value: 3.32e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577 1066 GLQGPPGSPGLKGDPGVAGLPGAKGEVGADGAQGIPGPPGREGAAGSPGPKGEKGMPGEKGNPGKDGVGRPGLPGPPGPP 1145
Cdd:NF038329  126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGE 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577 1146 gpviyvssedKAIVSTPGPEGKPGYAGFPGPAGPKGDlGSKGEQGLPGPKGEKGEPGtifsPDGRALGHPQKGAKGEPGf 1225
Cdd:NF038329  206 ----------QGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQG----PDGPAGKDGPRGDRGEAG- 269

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577 1226 rgppgpygRPGHKGEIGFPGRPGRPGTNGLKGEKGEPGDASlgfsMRGlpgppgppgppgppgmpiydsnafvESGRPGL 1305
Cdd:NF038329  270 --------PDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDG----KDG-------------------------QNGKDGL 312

                         250
                  ....*....|....*..
gi 568966577 1306 PGQQGVQGPSGPKGDKG 1322
Cdd:NF038329  313 PGKDGKDGQPGKDGLPG 329
Collagen_trimer pfam20010
Collagen trimerization domain; This small domain mediate trimerization in various collagen ...
 1462-1509 1.12e-16

Collagen trimerization domain; This small domain mediate trimerization in various collagen proteins.


:

Pssm-ID: 466257  Cd Length: 49  Bit Score: 75.33  E-value: 1.12e-16
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 568966577  1462 VRIWATYQTMLDKIREVPEGWLIFVAEREELYVRVRNGFRKVLLEART 1509
Cdd:pfam20010    1 VTVFQNYDTMLQKTHRVPEGTLVYVREREELYIRVRNGWRKIQLGELI 48
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 836-1130 7.57e-13

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.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 72.63  E-value: 7.57e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577  836 KDGTPGRDGEPGDPGEDGRPGDTGPQGFPGTPGDVGPKGEKGDPGIGPRGPPGPPGPPGpsfrqdkltfidmegsGFSGD 915
Cdd:NF038329  139 DRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPR----------------GETGP 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577  916 ieslRGPRGFPGPPGPPGVPGLPGEPGRFGINGSYAPGPAGLPGvpgkegppgfpgppgppgppgkegppgVAGQKGSVG 995
Cdd:NF038329  203 ----AGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPG---------------------------PTGEDGPQG 251

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577  996 DVGIPGPKGSKGDLGPIGMPGKSGlagspgpvgppgppgppgppgpgfaagfddmegsgiplwttarsSDGLQGPPGSPG 1075
Cdd:NF038329  252 PDGPAGKDGPRGDRGEAGPDGPDG--------------------------------------------KDGERGPVGPAG 287

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568966577 1076 LKGDPGVAGLPGAKGEvgaDGAQGIPGPPGREGAAGSPGPKGEKGMPGEKGNPGK 1130
Cdd:NF038329  288 KDGQNGKDGLPGKDGK---DGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGK 339
 
Name Accession Description Interval E-value
Endostatin-like cd00247
Endostatin-like domain; the angiogenesis inhibitor endostatin is a C-terminal fragment of ...
 1596-1766 1.16e-113

Endostatin-like domain; the angiogenesis inhibitor endostatin is a C-terminal fragment of collagen XV/XVIII, a proteoglycan/collagen found in vessel walls and basement membranes; this domain has a compact globular fold similar to that of C-type lectins; endostatin XVIII is monomeric and contains a heparin-binding epitope and zinc binding sites while endostatin XV is trimeric and contains neither of these sites; the generation of endostatin or endostatin-like collagen XV/XVIII fragments is catalyzed by proteolytic enzymes within the protease-sensitive hinge region of the C-terminal domain; endostatin inhibits endothelial cell migration in vitro and appears to be highly effective in murine in vivo studies


Pssm-ID: 238151  Cd Length: 171  Bit Score: 356.64  E-value: 1.16e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577 1596 QPVLHLVALNTPLSGGMRGIRGADFQCFQQARAVGLSGTFRAFLSSRLQDLYSIVRRADRGSVPIVNLKDEVLSPSWDSL 1675
Cdd:cd00247     1 QPVLHLVALNTPLSGDMRGIRGADFQCFQQARAAGLKGTFRAFLSSRLQDLYSIVRRADRDSLPIVNLKGEVLFNSWESL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577 1676 FSGSQGQLQPGARIFSFDGRDVLRHPAWPQKSVWHGSDPSGRRLMESYCETWRTETTGATGQASSLLSGRLLEQKAASCH 1755
Cdd:cd00247    81 FSGSGGQFNPGARIYSFDGRDVLTDPAWPQKMVWHGSDPNGRRLTDSYCEAWRTGDSAVTGQASSLSSGKLLEQKAYSCE 160

                         170
                  ....*....|.
gi 568966577 1756 NSYIVLCIENS 1766
Cdd:cd00247   161 NKLIVLCIENS 171
Endostatin pfam06482
Collagenase NC10 and Endostatin; NC10 stands for Non-helical region 10 and is taken from Swiss: ...
 1599-1767 1.71e-111

Collagenase NC10 and Endostatin; NC10 stands for Non-helical region 10 and is taken from Swiss:P39059. A mutation in this region in Swiss:P39060 is associated with an increased risk of prostrate cancer. This domain is cleaved from the precursor and forms endostatin. Endostatin is a key tumour suppressor and has been used highly successfully to treat cancer. It is a potent angiogenesis inhibitor. Endostatin also binds a zinc ion near the N-terminus; this is likely to be of structural rather than functional importance according to.


Pssm-ID: 461931  Cd Length: 169  Bit Score: 350.59  E-value: 1.71e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577  1599 LHLVALNTPLSGGMRGIRGADFQCFQQARAVGLSGTFRAFLSSRLQDLYSIVRRADRGSVPIVNLKDEVLSPSWDSLFSG 1678
Cdd:pfam06482    1 LHLIALNTPQSGDMRGIRGADFLCFQQARAAGLKGTFRAFLSSRLQDLYSIVRKADRENVPIVNLKDEVLFDSWESIFSG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577  1679 SQGQLQPGARIFSFDGRDVLRHPAWPQKSVWHGSDPSGRRLMESYCETWRTETTGATGQASSLLSGRLLEQKAASCHNSY 1758
Cdd:pfam06482   81 SGGQMKPNVPIYSFDGRDVLRDPAWPQKMVWHGSTSKGHRLTDNYCEAWRTGDQAVTGQASSLQSGKLLQQSPSSCSNSY 160


                   ....*....
gi 568966577  1759 IVLCIENSF 1767
Cdd:pfam06482  161 IVLCIENSY 169
CRD_Collagen_XVIII cd07455
Cysteine-rich domain of the variant 3 of collagen XVIII (V3C18 ); The cysteine-rich domain ...
 366-488 4.00e-59

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: 199.27  E-value: 4.00e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577  366 STSRCLPLPPTLTLCSRLGIGHFWLPNHLHHTDSVEVEATVQAWGRFLHTNCHPFLAWFFCLLLAPSCGPGPPPPLPPCR 445
Cdd:cd07455     1 PRPRCLPVPSSLPFCSRLGIRSFWLPNFLNHTSVEEVRAVLAEWAWLLESGCHPSLEWFFCLLLVPSCGGGPPPPPPPCR 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 568966577  446 QFCEALEDECWNYLAGDRLPVVCASLPSQEDGYCVFIGPAAEN 488
Cdd:cd07455    81 QFCEVLQDSCWNLLEGGRLPVACASLPEQEDGYCVLIGPPAEN 123
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 492-680 8.18e-51

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


Pssm-ID: 214560  Cd Length: 184  Bit Score: 177.93  E-value: 8.18e-51
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577    492 EVGLLQLLGDP-LPEKISQIDDPHVG-PAYIFGPDSNSGQVAQYHFPKLFFRDFSLLFHVRPATEAAGVLFAITDaAQVV 569
Cdd:smart00210    1 GQDLLQVFDLPsLSFAIRQVVGPEPGsPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPKSRGVLFAIYD-AQNV 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577    570 VSLGVKLsevrDGQQNISLLYTEpGASQTQTGASFR-LPAFVGQWTHFALSVDGGSVALYVDCEEFQRVPFARASQglEL 648
Cdd:smart00210   80 RQFGLEV----DGRANTLLLRYQ-GVDGKQHTVSFRnLPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGQ--PP 152

                           170       180       190
                    ....*....|....*....|....*....|..
gi 568966577    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 2.50e-48

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: 171.17  E-value: 2.50e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577    37 LVWLWPPKTSDSLEGPVSKPQNSSPVQSTENPTTHVVPQDGLTEQQTTPASselppEEEEEEDQKAGQGGSPATPAVPIP 116
Cdd:pfam06121   16 LDLLWFLDIADPEDTLASEPQGGLAVQPAAAPATHVAPQDDPAEQATAAAS-----PELPLEELEAAPGRAPGAPISAAA 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577   117 LVAPAASPDMKEENVAGVGAKILNVAQGIRSFVQLWDEDSTIGHSAGTEVPDSSIPTVLPSPAELSSAPQGSKTTLWLSS 196
Cdd:pfam06121   91 PAALAARPDMREENVAGVGAKILNIAQGIQSFIQLWNDAAPTESPAGAGTLAASAPTDPLALAEPSGPAAESGTALGPHR 170

                          170       180
                   ....*....|....*....|..
gi 568966577   197 AIPSSPDAQTTEAGTLAVPTQL 218
Cdd:pfam06121  171 GALSSLDTPRAESGTLAVPTQL 192
FRI smart00063
Frizzled; Drosophila melanogaster frizzled mediates signalling that polarises a precursor cell ...
 370-482 6.12e-30

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: 115.49  E-value: 6.12e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577    370 CLPLppTLTLCSRLGIGHFWLPNHLHHTDSVEVEATVQAWGRFLHTNCHPFLAWFFCLLLApSCGPGPPPPLPPCRQFCE 449
Cdd:smart00063    1 CEPI--TIPLCKDLGYNLTSMPNLLGHTTQEEAGLELEQFHPLLNVQCSPDLRFFLCSVYA-PICTEDLRPILPCRSLCE 77

                            90       100       110
                    ....*....|....*....|....*....|....*..
gi 568966577    450 ALEDECWNYLAGDRLP----VVCASLPSQEDgYCVFI 482
Cdd:smart00063   78 AAREGCEPLMEKFGFPwpefLRCDRFPVQEE-LCMDP 113
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1066-1322 3.32e-26

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: 113.85  E-value: 3.32e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577 1066 GLQGPPGSPGLKGDPGVAGLPGAKGEVGADGAQGIPGPPGREGAAGSPGPKGEKGMPGEKGNPGKDGVGRPGLPGPPGPP 1145
Cdd:NF038329  126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGE 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577 1146 gpviyvssedKAIVSTPGPEGKPGYAGFPGPAGPKGDlGSKGEQGLPGPKGEKGEPGtifsPDGRALGHPQKGAKGEPGf 1225
Cdd:NF038329  206 ----------QGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQG----PDGPAGKDGPRGDRGEAG- 269

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577 1226 rgppgpygRPGHKGEIGFPGRPGRPGTNGLKGEKGEPGDASlgfsMRGlpgppgppgppgppgmpiydsnafvESGRPGL 1305
Cdd:NF038329  270 --------PDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDG----KDG-------------------------QNGKDGL 312

                         250
                  ....*....|....*..
gi 568966577 1306 PGQQGVQGPSGPKGDKG 1322
Cdd:NF038329  313 PGKDGKDGQPGKDGLPG 329
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 988-1265 5.28e-25

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: 110.38  E-value: 5.28e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577  988 AGQKGSVGDVGIPGPKGSKGDLGPIGMPGKSGLAGspgpvgppgppgppgppgpgfaagfddmegsgiplwttarsSDGL 1067
Cdd:NF038329  128 AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKG-----------------------------------------PAGP 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577 1068 QGPPGSPGLKGDPGVAGLPGAKGEVGADGAQGIPGPPGREGAAGSPGPKGEKGMPGEKGNPGKDGVGRPGLPGPpgppgp 1147
Cdd:NF038329  167 QGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGD------ 240

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577 1148 viyvssedkaivstPGPEGKPGYAGFPGPAGPKGDLGSKGEQGLPGPKGEKGEPGtifsPDGRALGHPQKGAKGEPGfrg 1227
Cdd:NF038329  241 --------------PGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERG----PVGPAGKDGQNGKDGLPG--- 299

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 568966577 1228 ppgpygRPGHKGEIGFPGRPGRPGTNGLKGEKGEPGDA 1265
Cdd:NF038329  300 ------KDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKD 331
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 952-1202 1.68e-20

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: 96.51  E-value: 1.68e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577  952 PGPAGLPGVPGKEGPPGFPGPPGPPGPPGKEGPPGVAGQKGSVGDVGIPGPKGSKGDLGPIGMPGKSGLAGspgpvgppg 1031
Cdd:NF038329  128 AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRG--------- 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577 1032 PPGPPGPPGPGFAAGFDDMEGSGIPLWTTARSSDGLQGPPGSPGLKGDPGVAGLPGAKGEVGADGAQGIPGPPGREGAAG 1111
Cdd:NF038329  199 ETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDG 278

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577 1112 SPGPKGEKGMPGEKGNPGkdgvgrpglpgppgppgpviyvssedkaivsTPGPEGKPGYAGFPGPAGPKGDLGSKGEQGL 1191
Cdd:NF038329  279 ERGPVGPAGKDGQNGKDG-------------------------------LPGKDGKDGQNGKDGLPGKDGKDGQPGKDGL 327

                         250
                  ....*....|.
gi 568966577 1192 PGPKGEKGEPG 1202
Cdd:NF038329  328 PGKDGKDGQPG 338
Collagen_trimer pfam20010
Collagen trimerization domain; This small domain mediate trimerization in various collagen ...
 1462-1509 1.12e-16

Collagen trimerization domain; This small domain mediate trimerization in various collagen proteins.


Pssm-ID: 466257  Cd Length: 49  Bit Score: 75.33  E-value: 1.12e-16
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 568966577  1462 VRIWATYQTMLDKIREVPEGWLIFVAEREELYVRVRNGFRKVLLEART 1509
Cdd:pfam20010    1 VTVFQNYDTMLQKTHRVPEGTLVYVREREELYIRVRNGWRKIQLGELI 48
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1123-1367 1.01e-14

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: 78.79  E-value: 1.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577 1123 GEKGNPGkdgvgrpglpgPPGPPGPviyvssedkaivstPGPEGKPGYAGFPGPAGPKGDLGSKGEQGLPGPKGEKGEPG 1202
Cdd:NF038329  117 GEKGEPG-----------PAGPAGP--------------AGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAG 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577 1203 tifsPDGRALGHPQKGAKGEPGFRGPPGPYGRPGHKGEIGFPGRPGRPGTNGLKGEKGEPGDASLGfsmrglpgppgppg 1282
Cdd:NF038329  172 ----PQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDG-------------- 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577 1283 ppgppgmpiydsnafvESGRPGLPGQQGVQGPSGPKGDKGEVGPpgppgqfpidlfhleaemKGDKGDRGDAGQKGERGE 1362
Cdd:NF038329  234 ----------------QQGPDGDPGPTGEDGPQGPDGPAGKDGP------------------RGDRGEAGPDGPDGKDGE 279


                  ....*
gi 568966577 1363 PGAPG 1367
Cdd:NF038329  280 RGPVG 284
Fz pfam01392
Fz domain; Also known as the CRD (cysteine rich domain), the C6 box in MuSK receptor. This ...
 370-474 3.43e-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: 3.43e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577   370 CLPLppTLTLCSRLGIGHFWLPNHLHHTDSVEVE-----ATVQAWGRFLHTNCHPFLAWFFCLLLAPSCGPGPPPPLPPC 444
Cdd:pfam01392    1 CEPI--TLPMCLGLGYNATVFPNLLGHQTQEEAElslayLVLSEFEPLVDLSCSPSLRLFLCSLYFPPCTLGPSPKPVCP 78

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 568966577   445 --RQFCEALEDECWNYLAGDR----LP--VVCASLPSQ 474
Cdd:pfam01392   79 pcRSLCEEVRYGCEPLLEEAKfgfsWPefLDCDSLPAD 116
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 836-1130 7.57e-13

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: 72.63  E-value: 7.57e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577  836 KDGTPGRDGEPGDPGEDGRPGDTGPQGFPGTPGDVGPKGEKGDPGIGPRGPPGPPGPPGpsfrqdkltfidmegsGFSGD 915
Cdd:NF038329  139 DRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPR----------------GETGP 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577  916 ieslRGPRGFPGPPGPPGVPGLPGEPGRFGINGSYAPGPAGLPGvpgkegppgfpgppgppgppgkegppgVAGQKGSVG 995
Cdd:NF038329  203 ----AGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPG---------------------------PTGEDGPQG 251

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577  996 DVGIPGPKGSKGDLGPIGMPGKSGlagspgpvgppgppgppgppgpgfaagfddmegsgiplwttarsSDGLQGPPGSPG 1075
Cdd:NF038329  252 PDGPAGKDGPRGDRGEAGPDGPDG--------------------------------------------KDGERGPVGPAG 287

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568966577 1076 LKGDPGVAGLPGAKGEvgaDGAQGIPGPPGREGAAGSPGPKGEKGMPGEKGNPGK 1130
Cdd:NF038329  288 KDGQNGKDGLPGKDGK---DGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGK 339
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1072-1128 1.75e-10

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: 57.89  E-value: 1.75e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 568966577  1072 GSPGLKGDPGVAGLPGAKGEVGADGAQGIPGPPGREGAAGSPGPKGEKGMPGEKGNP 1128
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 528-676 4.64e-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: 48.18  E-value: 4.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577  528 GQVAQYHFPKLFFRDFSLLFHVRPaTEAAGVLFAITDAAQV-VVSLgvklsEVRDGQqnISLLYTEPGASqtqtgASFRL 606
Cdd:cd00110     7 SSYVRLPTLPAPRTRLSISFSFRT-TSPNGLLLYAGSQNGGdFLAL-----ELEDGR--LVLRYDLGSGS-----LVLSS 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568966577  607 PAFV--GQWTHFALSVDGGSVALYVDCEEFQRVPFARASQGLELErgAGLFVG-------QAGTADPDKFQGMISELKV 676
Cdd:cd00110    74 KTPLndGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLD--GPLYLGglpedlkSPGLPVSPGFVGCIRDLKV 150
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
989-1207 9.47e-06

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 50.41  E-value: 9.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577  989 GQKGSVGDVGIPGPKGSKGDLGPIGMPGKSGLAGSPGPVGPPGPPGPPGPPGPGFAAGFDDMEGSGIPLWTTARS----- 1063
Cdd:COG5164    61 GGTRPAGNQGATGPAQNQGGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTppgdg 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577 1064 -----SDGLQGPPGSPGLKGDPGVAGLPGAKGEVGADGAQGIPGPPGrEGAAGSPGPKGEKGMPGEKGNPGKDGVGRpgl 1138
Cdd:COG5164   141 gstppGPGSTGPGGSTTPPGDGGSTTPPGPGGSTTPPDDGGSTTPPN-KGETGTDIPTGGTPRQGPDGPVKKDDKNG--- 216

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568966577 1139 pgppgppgpviyvssedkaivSTPGPEGKPGYAGFPGPAGPKGDLGSKGEQGLPGPKGEKGEPGTIFSP 1207
Cdd:COG5164   217 ---------------------KGNPPDDRGGKTGPKDQRPKTNPIERRGPERPEAAALPAELTALEAEN 264
Laminin_G_3 pfam13385
Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin ...
 542-676 2.34e-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: 46.22  E-value: 2.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577   542 DFSLLFHVRP--ATEAAGVLFAITDAAQVvvSLGVklseVRDGQQNISLLYTEPGASQTQTGASFRLpafvGQWTHFALS 619
Cdd:pfam13385   18 DFTVSAWVKPdsLPGWARAIISSSGGGGY--SLGL----DGDGRLRFAVNGGNGGWDTVTSGASVPL----GQWTHVAVT 87

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 568966577   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 4.76e-04

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: 39.78  E-value: 4.76e-04
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 568966577   840 PGRDGEPGDPGEDGRPGDTGPQGFPGTPGDVGPKGE 875
Cdd:pfam01391   21 PGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
 42-282 3.38e-03

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 42.22  E-value: 3.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577   42 PPKTSDSLEGPvskpqnsSPVqstenPTTHVVPQDGLTEQQTTPASSElppeeeeeedQKAGQGGSPAT-------PAVP 114
Cdd:PLN03209  329 PPKESDAADGP-------KPV-----PTKPVTPEAPSPPIEEEPPQPK----------AVVPRPLSPYTayedlkpPTSP 386

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577  115 IPLVAPAASPDMKEENVAGVGAKI-LNVAQGIRSFVqlwDEDSTIGHSAGTEVPDSSI-------PTVLPSPaelsSAPQ 186
Cdd:PLN03209  387 IPTPPSSSPASSKSVDAVAKPAEPdVVPSPGSASNV---PEVEPAQVEAKKTRPLSPYaryedlkPPTSPSP----TAPT 459

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577  187 GSKTTLWLSSAIPSSPDaqtTEAGTLAVPTQLPPfqsnlqAPLGRPSAPpdFPGRAFLSSPRIRAP--PWGNQEPPRQPQ 264
Cdd:PLN03209  460 GVSPSVSSTSSVPAVPD---TAPATAATDAAAPP------PANMRPLSP--YAVYDDLKPPTSPSPaaPVGKVAPSSTNE 528

                         250
                  ....*....|....*...
gi 568966577  265 HLEGKGFLPMTARSSQQH 282
Cdd:PLN03209  529 VVKVGNSAPPTALADEQH 546
MJ1470 COG5306
Uncharacterized conserved protein MJ1470, contains DUF2341 domain, predicted component of type ...
 553-663 4.39e-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: 41.81  E-value: 4.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577  553 TEAAGVLFAITDAAQVVVSLGVKLSEVRDGQQNISLlytePGASQTQTGASFRLPAfvGQWTHFALSVDGGSVALYVDCE 632
Cdd:COG5306   200 TFSAWIKPAQLDGNAVLYSRRDGANGLDNGAPFVEV----GGAGGTRSAAGAPLAA--GTWHHLAVVADAGKVTLYVNGV 273

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 568966577  633 EFQRVPFAR------ASQGLELERGAGLFVGQAGTAD 663
Cdd:COG5306   274 AAGSLDASLptvtggATIGAVGLAAIASLSGQAVEAG 310
 
Name Accession Description Interval E-value
Endostatin-like cd00247
Endostatin-like domain; the angiogenesis inhibitor endostatin is a C-terminal fragment of ...
 1596-1766 1.16e-113

Endostatin-like domain; the angiogenesis inhibitor endostatin is a C-terminal fragment of collagen XV/XVIII, a proteoglycan/collagen found in vessel walls and basement membranes; this domain has a compact globular fold similar to that of C-type lectins; endostatin XVIII is monomeric and contains a heparin-binding epitope and zinc binding sites while endostatin XV is trimeric and contains neither of these sites; the generation of endostatin or endostatin-like collagen XV/XVIII fragments is catalyzed by proteolytic enzymes within the protease-sensitive hinge region of the C-terminal domain; endostatin inhibits endothelial cell migration in vitro and appears to be highly effective in murine in vivo studies


Pssm-ID: 238151  Cd Length: 171  Bit Score: 356.64  E-value: 1.16e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577 1596 QPVLHLVALNTPLSGGMRGIRGADFQCFQQARAVGLSGTFRAFLSSRLQDLYSIVRRADRGSVPIVNLKDEVLSPSWDSL 1675
Cdd:cd00247     1 QPVLHLVALNTPLSGDMRGIRGADFQCFQQARAAGLKGTFRAFLSSRLQDLYSIVRRADRDSLPIVNLKGEVLFNSWESL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577 1676 FSGSQGQLQPGARIFSFDGRDVLRHPAWPQKSVWHGSDPSGRRLMESYCETWRTETTGATGQASSLLSGRLLEQKAASCH 1755
Cdd:cd00247    81 FSGSGGQFNPGARIYSFDGRDVLTDPAWPQKMVWHGSDPNGRRLTDSYCEAWRTGDSAVTGQASSLSSGKLLEQKAYSCE 160

                         170
                  ....*....|.
gi 568966577 1756 NSYIVLCIENS 1766
Cdd:cd00247   161 NKLIVLCIENS 171
Endostatin pfam06482
Collagenase NC10 and Endostatin; NC10 stands for Non-helical region 10 and is taken from Swiss: ...
 1599-1767 1.71e-111

Collagenase NC10 and Endostatin; NC10 stands for Non-helical region 10 and is taken from Swiss:P39059. A mutation in this region in Swiss:P39060 is associated with an increased risk of prostrate cancer. This domain is cleaved from the precursor and forms endostatin. Endostatin is a key tumour suppressor and has been used highly successfully to treat cancer. It is a potent angiogenesis inhibitor. Endostatin also binds a zinc ion near the N-terminus; this is likely to be of structural rather than functional importance according to.


Pssm-ID: 461931  Cd Length: 169  Bit Score: 350.59  E-value: 1.71e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577  1599 LHLVALNTPLSGGMRGIRGADFQCFQQARAVGLSGTFRAFLSSRLQDLYSIVRRADRGSVPIVNLKDEVLSPSWDSLFSG 1678
Cdd:pfam06482    1 LHLIALNTPQSGDMRGIRGADFLCFQQARAAGLKGTFRAFLSSRLQDLYSIVRKADRENVPIVNLKDEVLFDSWESIFSG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577  1679 SQGQLQPGARIFSFDGRDVLRHPAWPQKSVWHGSDPSGRRLMESYCETWRTETTGATGQASSLLSGRLLEQKAASCHNSY 1758
Cdd:pfam06482   81 SGGQMKPNVPIYSFDGRDVLRDPAWPQKMVWHGSTSKGHRLTDNYCEAWRTGDQAVTGQASSLQSGKLLQQSPSSCSNSY 160


                   ....*....
gi 568966577  1759 IVLCIENSF 1767
Cdd:pfam06482  161 IVLCIENSY 169
CRD_Collagen_XVIII cd07455
Cysteine-rich domain of the variant 3 of collagen XVIII (V3C18 ); The cysteine-rich domain ...
 366-488 4.00e-59

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: 199.27  E-value: 4.00e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577  366 STSRCLPLPPTLTLCSRLGIGHFWLPNHLHHTDSVEVEATVQAWGRFLHTNCHPFLAWFFCLLLAPSCGPGPPPPLPPCR 445
Cdd:cd07455     1 PRPRCLPVPSSLPFCSRLGIRSFWLPNFLNHTSVEEVRAVLAEWAWLLESGCHPSLEWFFCLLLVPSCGGGPPPPPPPCR 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 568966577  446 QFCEALEDECWNYLAGDRLPVVCASLPSQEDGYCVFIGPAAEN 488
Cdd:cd07455    81 QFCEVLQDSCWNLLEGGRLPVACASLPEQEDGYCVLIGPPAEN 123
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 492-680 8.18e-51

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


Pssm-ID: 214560  Cd Length: 184  Bit Score: 177.93  E-value: 8.18e-51
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577    492 EVGLLQLLGDP-LPEKISQIDDPHVG-PAYIFGPDSNSGQVAQYHFPKLFFRDFSLLFHVRPATEAAGVLFAITDaAQVV 569
Cdd:smart00210    1 GQDLLQVFDLPsLSFAIRQVVGPEPGsPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPKSRGVLFAIYD-AQNV 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577    570 VSLGVKLsevrDGQQNISLLYTEpGASQTQTGASFR-LPAFVGQWTHFALSVDGGSVALYVDCEEFQRVPFARASQglEL 648
Cdd:smart00210   80 RQFGLEV----DGRANTLLLRYQ-GVDGKQHTVSFRnLPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGQ--PP 152

                           170       180       190
                    ....*....|....*....|....*....|..
gi 568966577    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 2.50e-48

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: 171.17  E-value: 2.50e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577    37 LVWLWPPKTSDSLEGPVSKPQNSSPVQSTENPTTHVVPQDGLTEQQTTPASselppEEEEEEDQKAGQGGSPATPAVPIP 116
Cdd:pfam06121   16 LDLLWFLDIADPEDTLASEPQGGLAVQPAAAPATHVAPQDDPAEQATAAAS-----PELPLEELEAAPGRAPGAPISAAA 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577   117 LVAPAASPDMKEENVAGVGAKILNVAQGIRSFVQLWDEDSTIGHSAGTEVPDSSIPTVLPSPAELSSAPQGSKTTLWLSS 196
Cdd:pfam06121   91 PAALAARPDMREENVAGVGAKILNIAQGIQSFIQLWNDAAPTESPAGAGTLAASAPTDPLALAEPSGPAAESGTALGPHR 170

                          170       180
                   ....*....|....*....|..
gi 568966577   197 AIPSSPDAQTTEAGTLAVPTQL 218
Cdd:pfam06121  171 GALSSLDTPRAESGTLAVPTQL 192
FRI smart00063
Frizzled; Drosophila melanogaster frizzled mediates signalling that polarises a precursor cell ...
 370-482 6.12e-30

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: 115.49  E-value: 6.12e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577    370 CLPLppTLTLCSRLGIGHFWLPNHLHHTDSVEVEATVQAWGRFLHTNCHPFLAWFFCLLLApSCGPGPPPPLPPCRQFCE 449
Cdd:smart00063    1 CEPI--TIPLCKDLGYNLTSMPNLLGHTTQEEAGLELEQFHPLLNVQCSPDLRFFLCSVYA-PICTEDLRPILPCRSLCE 77

                            90       100       110
                    ....*....|....*....|....*....|....*..
gi 568966577    450 ALEDECWNYLAGDRLP----VVCASLPSQEDgYCVFI 482
Cdd:smart00063   78 AAREGCEPLMEKFGFPwpefLRCDRFPVQEE-LCMDP 113
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1066-1322 3.32e-26

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: 113.85  E-value: 3.32e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577 1066 GLQGPPGSPGLKGDPGVAGLPGAKGEVGADGAQGIPGPPGREGAAGSPGPKGEKGMPGEKGNPGKDGVGRPGLPGPPGPP 1145
Cdd:NF038329  126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGE 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577 1146 gpviyvssedKAIVSTPGPEGKPGYAGFPGPAGPKGDlGSKGEQGLPGPKGEKGEPGtifsPDGRALGHPQKGAKGEPGf 1225
Cdd:NF038329  206 ----------QGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQG----PDGPAGKDGPRGDRGEAG- 269

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577 1226 rgppgpygRPGHKGEIGFPGRPGRPGTNGLKGEKGEPGDASlgfsMRGlpgppgppgppgppgmpiydsnafvESGRPGL 1305
Cdd:NF038329  270 --------PDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDG----KDG-------------------------QNGKDGL 312

                         250
                  ....*....|....*..
gi 568966577 1306 PGQQGVQGPSGPKGDKG 1322
Cdd:NF038329  313 PGKDGKDGQPGKDGLPG 329
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 988-1265 5.28e-25

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: 110.38  E-value: 5.28e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577  988 AGQKGSVGDVGIPGPKGSKGDLGPIGMPGKSGLAGspgpvgppgppgppgppgpgfaagfddmegsgiplwttarsSDGL 1067
Cdd:NF038329  128 AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKG-----------------------------------------PAGP 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577 1068 QGPPGSPGLKGDPGVAGLPGAKGEVGADGAQGIPGPPGREGAAGSPGPKGEKGMPGEKGNPGKDGVGRPGLPGPpgppgp 1147
Cdd:NF038329  167 QGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGD------ 240

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577 1148 viyvssedkaivstPGPEGKPGYAGFPGPAGPKGDLGSKGEQGLPGPKGEKGEPGtifsPDGRALGHPQKGAKGEPGfrg 1227
Cdd:NF038329  241 --------------PGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERG----PVGPAGKDGQNGKDGLPG--- 299

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 568966577 1228 ppgpygRPGHKGEIGFPGRPGRPGTNGLKGEKGEPGDA 1265
Cdd:NF038329  300 ------KDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKD 331
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 952-1202 1.68e-20

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: 96.51  E-value: 1.68e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577  952 PGPAGLPGVPGKEGPPGFPGPPGPPGPPGKEGPPGVAGQKGSVGDVGIPGPKGSKGDLGPIGMPGKSGLAGspgpvgppg 1031
Cdd:NF038329  128 AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRG--------- 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577 1032 PPGPPGPPGPGFAAGFDDMEGSGIPLWTTARSSDGLQGPPGSPGLKGDPGVAGLPGAKGEVGADGAQGIPGPPGREGAAG 1111
Cdd:NF038329  199 ETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDG 278

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577 1112 SPGPKGEKGMPGEKGNPGkdgvgrpglpgppgppgpviyvssedkaivsTPGPEGKPGYAGFPGPAGPKGDLGSKGEQGL 1191
Cdd:NF038329  279 ERGPVGPAGKDGQNGKDG-------------------------------LPGKDGKDGQNGKDGLPGKDGKDGQPGKDGL 327

                         250
                  ....*....|.
gi 568966577 1192 PGPKGEKGEPG 1202
Cdd:NF038329  328 PGKDGKDGQPG 338
CRD_FZ cd07066
CRD_domain cysteine-rich domain, also known as Fz (frizzled) domain; CRD_FZ is an essential ...
 369-480 2.51e-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: 79.47  E-value: 2.51e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577  369 RCLPLPptLTLCSRLGIGHFWLPNHLHHTDSVEVEATVQAWGRFLHTNCHPFLAWFFCLLLAPSCGPGPPPPLPPCRQFC 448
Cdd:cd07066     1 KCEPIP--LPLCRGLPYNTTRFPNLLGHESQEEAEQELESFTPLVNSGCHPDLRFFLCSLYFPECTPDGDRPIPPCRSLC 78

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 568966577  449 EALEDECWNYLAG----DRLPVVCASLPSQ-EDGYCV 480
Cdd:cd07066    79 EEVRDSCEPLMLAfgfpWPEPLDCDRFPDSnEEGLCI 115
Collagen_trimer pfam20010
Collagen trimerization domain; This small domain mediate trimerization in various collagen ...
 1462-1509 1.12e-16

Collagen trimerization domain; This small domain mediate trimerization in various collagen proteins.


Pssm-ID: 466257  Cd Length: 49  Bit Score: 75.33  E-value: 1.12e-16
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 568966577  1462 VRIWATYQTMLDKIREVPEGWLIFVAEREELYVRVRNGFRKVLLEART 1509
Cdd:pfam20010    1 VTVFQNYDTMLQKTHRVPEGTLVYVREREELYIRVRNGWRKIQLGELI 48
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1123-1367 1.01e-14

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: 78.79  E-value: 1.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577 1123 GEKGNPGkdgvgrpglpgPPGPPGPviyvssedkaivstPGPEGKPGYAGFPGPAGPKGDLGSKGEQGLPGPKGEKGEPG 1202
Cdd:NF038329  117 GEKGEPG-----------PAGPAGP--------------AGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAG 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577 1203 tifsPDGRALGHPQKGAKGEPGFRGPPGPYGRPGHKGEIGFPGRPGRPGTNGLKGEKGEPGDASLGfsmrglpgppgppg 1282
Cdd:NF038329  172 ----PQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDG-------------- 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577 1283 ppgppgmpiydsnafvESGRPGLPGQQGVQGPSGPKGDKGEVGPpgppgqfpidlfhleaemKGDKGDRGDAGQKGERGE 1362
Cdd:NF038329  234 ----------------QQGPDGDPGPTGEDGPQGPDGPAGKDGP------------------RGDRGEAGPDGPDGKDGE 279


                  ....*
gi 568966577 1363 PGAPG 1367
Cdd:NF038329  280 RGPVG 284
Fz pfam01392
Fz domain; Also known as the CRD (cysteine rich domain), the C6 box in MuSK receptor. This ...
 370-474 3.43e-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: 3.43e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577   370 CLPLppTLTLCSRLGIGHFWLPNHLHHTDSVEVE-----ATVQAWGRFLHTNCHPFLAWFFCLLLAPSCGPGPPPPLPPC 444
Cdd:pfam01392    1 CEPI--TLPMCLGLGYNATVFPNLLGHQTQEEAElslayLVLSEFEPLVDLSCSPSLRLFLCSLYFPPCTLGPSPKPVCP 78

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 568966577   445 --RQFCEALEDECWNYLAGDR----LP--VVCASLPSQ 474
Cdd:pfam01392   79 pcRSLCEEVRYGCEPLLEEAKfgfsWPefLDCDSLPAD 116
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 836-1130 7.57e-13

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: 72.63  E-value: 7.57e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577  836 KDGTPGRDGEPGDPGEDGRPGDTGPQGFPGTPGDVGPKGEKGDPGIGPRGPPGPPGPPGpsfrqdkltfidmegsGFSGD 915
Cdd:NF038329  139 DRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPR----------------GETGP 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577  916 ieslRGPRGFPGPPGPPGVPGLPGEPGRFGINGSYAPGPAGLPGvpgkegppgfpgppgppgppgkegppgVAGQKGSVG 995
Cdd:NF038329  203 ----AGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPG---------------------------PTGEDGPQG 251

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577  996 DVGIPGPKGSKGDLGPIGMPGKSGlagspgpvgppgppgppgppgpgfaagfddmegsgiplwttarsSDGLQGPPGSPG 1075
Cdd:NF038329  252 PDGPAGKDGPRGDRGEAGPDGPDG--------------------------------------------KDGERGPVGPAG 287

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568966577 1076 LKGDPGVAGLPGAKGEvgaDGAQGIPGPPGREGAAGSPGPKGEKGMPGEKGNPGK 1130
Cdd:NF038329  288 KDGQNGKDGLPGKDGK---DGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGK 339
CRD_sizzled cd07452
Cysteine-rich domain of the sizzled protein; The cysteine-rich domain (CRD) is an essential ...
 367-476 6.05e-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: 62.21  E-value: 6.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577  367 TSRCLPLPPTLTLCSRLGIGHFWLPNHLHHTDSVEVEATVQAWGRFLHTNCHPFLAWFFCLLLApscGPGPPPPLPPCRQ 446
Cdd:cd07452     6 STKCVPIPPEMSMCQDVGYSEMRLPNLLGHTSMAEVVPKSADWQTLLHTGCHPHARTFLCSLFA---PVCLDTFIQPCRS 82

                          90       100       110
                  ....*....|....*....|....*....|....
gi 568966577  447 FCEALEDECWNYLA--GDRLP--VVCASLPSQED 476
Cdd:cd07452    83 MCVAVRDSCAPVLAchGHSWPesLDCDRFPAGED 116
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1072-1128 1.75e-10

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: 57.89  E-value: 1.75e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 568966577  1072 GSPGLKGDPGVAGLPGAKGEVGADGAQGIPGPPGREGAAGSPGPKGEKGMPGEKGNP 1128
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1064-1115 8.30e-10

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: 55.96  E-value: 8.30e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568966577  1064 SDGLQGPPGSPGLKGDPGVAGLPGAKGEVGADGAQGIPGPPGREGAAGSPGP 1115
Cdd:pfam01391    5 PPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1066-1122 8.72e-10

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: 55.96  E-value: 8.72e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 568966577  1066 GLQGPPGSPGLKGDPGVAGLPGAKGEVGADGAQGIPGPPGREGAAGSPGPKGEKGMP 1122
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1078-1129 1.07e-09

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: 55.58  E-value: 1.07e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568966577  1078 GDPGVAGLPGAKGEVGADGAQGIPGPPGREGAAGSPGPKGEKGMPGEKGNPG 1129
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPG 52
CRD_SFRP1 cd07443
Cysteine-rich domain of the secreted frizzled-related protein 1 (SFRP1), a regulator of Wnt ...
 365-455 3.25e-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: 56.45  E-value: 3.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577  365 TSTSRCLPLPPTLTLCSRLGIGHFWLPNHLHHTDSVEVEATVQAWGRFLHTNCHPFLAWFFCLLLApscGPGPPPPLPPC 444
Cdd:cd07443     2 TKPPQCVDIPADLRLCHNVGYKKMVLPNLLDHETMAEVKQQASSWVPLLNKNCHKGTQVFLCSLFA---PVCLDRPVYPC 78

                          90
                  ....*....|.
gi 568966577  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 5.02e-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: 50.29  E-value: 5.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577  368 SRCLPLPPTLTLCSRLGIGHFWLPNHLHHTDSVEVEATVQAWGRFLHTNCHPFLAWFFCLLLAPSCGPGPPPPLPPCRQF 447
Cdd:cd07446     3 SNCKPIPANMLLCHGIEYTNMRLPNLLGHETMKEVLQQAGSWIPLVQKQCHPDTKKFLCSLFAPVCLDDLDEAIQPCRSL 82


                  ....*...
gi 568966577  448 CEALEDEC 455
Cdd:cd07446    83 CEAVKDGC 90
CRD_crescent cd07453
Cysteine-rich domain of the crescent protein; The cysteine-rich domain (CRD) is an essential ...
 368-455 2.76e-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: 48.40  E-value: 2.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577  368 SRCLPLPPTLTLCSRLGIGHFWLPNHLHHTDSVEVEATVQAWGRFLHTNCHPFLAWFFCLLLApscGPGPPPPLPPCRQF 447
Cdd:cd07453     1 SPCMRIPKSMALCYDIGYSEMRIPNLLEHETMAEVIQQSSSWLPLLARECHPDARIFLCSLFA---PICWDRPIYPCRSL 77


                  ....*...
gi 568966577  448 CEALEDEC 455
Cdd:cd07453    78 CEAVRSSC 85
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 528-676 4.64e-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: 48.18  E-value: 4.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577  528 GQVAQYHFPKLFFRDFSLLFHVRPaTEAAGVLFAITDAAQV-VVSLgvklsEVRDGQqnISLLYTEPGASqtqtgASFRL 606
Cdd:cd00110     7 SSYVRLPTLPAPRTRLSISFSFRT-TSPNGLLLYAGSQNGGdFLAL-----ELEDGR--LVLRYDLGSGS-----LVLSS 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568966577  607 PAFV--GQWTHFALSVDGGSVALYVDCEEFQRVPFARASQGLELErgAGLFVG-------QAGTADPDKFQGMISELKV 676
Cdd:cd00110    74 KTPLndGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLD--GPLYLGglpedlkSPGLPVSPGFVGCIRDLKV 150
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1162-1202 7.16e-06

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: 44.79  E-value: 7.16e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 568966577  1162 PGPEGKPGYAGFPGPAGPKGDLGSKGEQGLPGPKGEKGEPG 1202
Cdd:pfam01391   12 PGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPG 52
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1111-1197 9.15e-06

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: 44.41  E-value: 9.15e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577  1111 GSPGPKGEKGMPGEKGNPGKdgvgrpglpgppgppgpviyvssedkaivstPGPEGKPGYAGFPGPAGPKGDLGSKGEQG 1190
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGP-------------------------------PGPPGPPGPPGEPGPPGPPGPPGPPGPPG 49


                   ....*..
gi 568966577  1191 LPGPKGE 1197
Cdd:pfam01391   50 APGAPGP 56
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
989-1207 9.47e-06

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 50.41  E-value: 9.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577  989 GQKGSVGDVGIPGPKGSKGDLGPIGMPGKSGLAGSPGPVGPPGPPGPPGPPGPGFAAGFDDMEGSGIPLWTTARS----- 1063
Cdd:COG5164    61 GGTRPAGNQGATGPAQNQGGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTppgdg 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577 1064 -----SDGLQGPPGSPGLKGDPGVAGLPGAKGEVGADGAQGIPGPPGrEGAAGSPGPKGEKGMPGEKGNPGKDGVGRpgl 1138
Cdd:COG5164   141 gstppGPGSTGPGGSTTPPGDGGSTTPPGPGGSTTPPDDGGSTTPPN-KGETGTDIPTGGTPRQGPDGPVKKDDKNG--- 216

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568966577 1139 pgppgppgpviyvssedkaivSTPGPEGKPGYAGFPGPAGPKGDLGSKGEQGLPGPKGEKGEPGTIFSP 1207
Cdd:COG5164   217 ---------------------KGNPPDDRGGKTGPKDQRPKTNPIERRGPERPEAAALPAELTALEAEN 264
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1184-1265 1.97e-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: 43.64  E-value: 1.97e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577  1184 GSKGEQGLPGPKGEKGEPGtifspdgralghpQKGAKGEPGfrgppgpygrpgHKGEIGFPGRPGRPGTNGLKGEKGEPG 1263
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPG-------------PPGPPGPPG------------PPGEPGPPGPPGPPGPPGPPGAPGAPG 55


                   ..
gi 568966577  1264 DA 1265
Cdd:pfam01391   56 PP 57
CRD_SFRP5 cd07444
Cysteine-rich domain of the secreted frizzled-related protein 5 (SFRP5), a regulator of Wnt ...
 365-455 2.01e-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: 45.71  E-value: 2.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577  365 TSTSRCLPLPPTLTLCSRLGIGHFWLPNHLHHTDSVEVEATVQAWGRFLHTNCHPFLAWFFCLLLApscGPGPPPPLPPC 444
Cdd:cd07444     2 SKQPQCVDIPADLPLCHNVGYKRMRLPNLLEHESMAEVKQQASSWVPLLAKRCHADTQVFLCSLFA---PVCLDRPIYPC 78

                          90
                  ....*....|.
gi 568966577  445 RQFCEALEDEC 455
Cdd:cd07444    79 RSLCEAVRDSC 89
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1162-1202 2.15e-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: 43.64  E-value: 2.15e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 568966577  1162 PGPEGKPGYAGFPGPAGPKGDLGSKGEQGLPGPKGEKGEPG 1202
Cdd:pfam01391   15 PGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Laminin_G_3 pfam13385
Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin ...
 542-676 2.34e-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: 46.22  E-value: 2.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577   542 DFSLLFHVRP--ATEAAGVLFAITDAAQVvvSLGVklseVRDGQQNISLLYTEPGASQTQTGASFRLpafvGQWTHFALS 619
Cdd:pfam13385   18 DFTVSAWVKPdsLPGWARAIISSSGGGGY--SLGL----DGDGRLRFAVNGGNGGWDTVTSGASVPL----GQWTHVAVT 87

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 568966577   620 VDGGSVALYVDCEEFQRVPfarASQGLELERGAGLFVGQAGTADPDkFQGMISELKV 676
Cdd:pfam13385   88 YDGGTLRLYVNGVLVGSST---LTGGPPPGTGGPLYIGRSPGGDDY-FNGLIDEVRI 140
LamG smart00282
Laminin G domain;
544-676 3.84e-05

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 45.02  E-value: 3.84e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577    544 SLLFHVRPaTEAAGVLFAITDAAQV-VVSLgvklsEVRDGQqnISLLYTEPGASQTQTGASFRLPAfvGQWTHFALSVDG 622
Cdd:smart00282    1 SISFSFRT-TSPNGLLLYAGSKGGGdYLAL-----ELRDGR--LVLRYDLGSGPARLTSDPTPLND--GQWHRVAVERNG 70

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568966577    623 GSVALYVDCEEFQRVPFARASQGLELErgAGLFVG-------QAGTADPDKFQGMISELKV 676
Cdd:smart00282   71 RSVTLSVDGGNRVSGESPGGLTILNLD--GPLYLGglpedlkLPPLPVTPGFRGCIRNLKV 129
CRD_SFRP4 cd07442
Cysteine-rich domain of the secreted frizzled-related protein 4 (SFRP4), a Wnt antagonist; The ...
 370-486 1.54e-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: 43.48  E-value: 1.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577  370 CLPLPPTLTLcsrlgighfwLPNHLHHTDSVEVEATVQAWGRFLHTNCHPFLAWFFCLLLAPS-CGPGPPPPLPPCRQFC 448
Cdd:cd07442    13 CRHMPWNITR----------MPNHLHHSTQENAVLAIEQYEELVDTGCSPVLPFFLCAMYAPIcTLEFLYDPIKPCRSVC 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 568966577  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 2.17e-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: 42.85  E-value: 2.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577  366 STSRCLPLPPTLtlCSRLGIGHFWLPNHLHHTDSVEVEATVQAWGRFLHTNCHPFLAWFFCLLLAPSCGPGPPPPLPPCR 445
Cdd:cd07454     1 VKGKCIPIDIEL--CKDLPYNYTYFPNTILHNDQHTLQTHTEHFKPLMKTKCHPHIHFFICSVFAPMCPIGMPQAVTSCK 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 568966577  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 4.28e-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: 41.93  E-value: 4.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577  368 SRCLPLppTLTLCSRLGIGHFWLPNHLHHTDSVEVEATVQAWGRFLHTNCHPFLAWFFCLLLAPSCGPGPPPPLPPCRQF 447
Cdd:cd07463     3 AKCQPV--VIPMCRGIGYNLTRMPNFLGHDSQREAAIKLNEFAPLVEYGCHVHLRFFLCSLYAPMCTDQVSTSIPACRPM 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 568966577  448 CEALEDEC------WNYLAGDRLPvvCASLPSQED 476
Cdd:cd07463    81 CEQARQKCspimeqFNFGWPESLD--CSRLPTRND 113
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 840-875 4.76e-04

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: 39.78  E-value: 4.76e-04
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 568966577   840 PGRDGEPGDPGEDGRPGDTGPQGFPGTPGDVGPKGE 875
Cdd:pfam01391   21 PGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
CRD_FZ9_like cd07457
Cysteine-rich Wnt-binding domain (CRD) of receptors similar to frizzled 9; The cysteine-rich ...
 368-476 1.13e-03

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: 1.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577  368 SRCLPLppTLTLCSRLGIGHFWLPNHLHHTDSVEVEATVQAWGRFLHTNCHPFLAWFFCLLLAPSCGPGPPPPLPPCRQF 447
Cdd:cd07457     1 GKCERI--TIPMCQGIGYNMTRMPNLLGHESQSEAAISIHEFAPLVQYGCAEHLRFFLCSLYAPMCTEQVSIPIPACRSM 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 568966577  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 1.35e-03

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: 40.77  E-value: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577  369 RCLPLppTLTLCSRLGIGHFWLPNHLHHTDSVEVEATVQAWGRFLHTNCHPFLAWFFCLLLAPSCGPGPPPPLPPCRQFC 448
Cdd:cd07462     4 RCQPI--EIPMCKDIGYNMTRMPNLMGHENQREAAIQLHEFAPLVEYGCHSHLKFFLCSLYAPMCTEQVSTPIPACRVMC 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 568966577  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 1.84e-03

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: 1.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577  374 PPTLTLCSRLGIGHFWLPNHLHHTDSVEVEATVQA--WGRFLHTNCHPFLAWFFCLLLAPSCGPGPPPPLPPCRQFCEAL 451
Cdd:cd07888     4 PITLELCMNLPYNTTRYPNYLGHRTQKEASISWESslFPALVQTNCYKYLMFFACTILVPKCDPVTQQRIPPCRSLCRNS 83

                          90       100
                  ....*....|....*....|....*..
gi 568966577  452 EDECWNYLA--GDRLP--VVCASLPSQ 474
Cdd:cd07888    84 KERCESVLGivGLQWPedTDCAQFPEE 110
CRD_SFRP3 cd07441
Cysteine-rich domain of the secreted frizzled-related protein 3 (SFRP3, alias FRZB), a Wnt ...
 374-430 3.13e-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: 39.65  E-value: 3.13e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568966577  374 PPTLTLCSRLGIGHFWLPNHLHHTDSVEVEATVQAWGRFLHTNCHPFLAWFFCLLLA 430
Cdd:cd07441     6 PVRIPMCKSMPWNMTKMPNHLHHSTQANAVLAIEQFEGLLGTQCSPDLLFFLCAMYA 62
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
 42-282 3.38e-03

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 42.22  E-value: 3.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577   42 PPKTSDSLEGPvskpqnsSPVqstenPTTHVVPQDGLTEQQTTPASSElppeeeeeedQKAGQGGSPAT-------PAVP 114
Cdd:PLN03209  329 PPKESDAADGP-------KPV-----PTKPVTPEAPSPPIEEEPPQPK----------AVVPRPLSPYTayedlkpPTSP 386

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577  115 IPLVAPAASPDMKEENVAGVGAKI-LNVAQGIRSFVqlwDEDSTIGHSAGTEVPDSSI-------PTVLPSPaelsSAPQ 186
Cdd:PLN03209  387 IPTPPSSSPASSKSVDAVAKPAEPdVVPSPGSASNV---PEVEPAQVEAKKTRPLSPYaryedlkPPTSPSP----TAPT 459

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577  187 GSKTTLWLSSAIPSSPDaqtTEAGTLAVPTQLPPfqsnlqAPLGRPSAPpdFPGRAFLSSPRIRAP--PWGNQEPPRQPQ 264
Cdd:PLN03209  460 GVSPSVSSTSSVPAVPD---TAPATAATDAAAPP------PANMRPLSP--YAVYDDLKPPTSPSPaaPVGKVAPSSTNE 528

                         250
                  ....*....|....*...
gi 568966577  265 HLEGKGFLPMTARSSQQH 282
Cdd:PLN03209  529 VVKVGNSAPPTALADEQH 546
MJ1470 COG5306
Uncharacterized conserved protein MJ1470, contains DUF2341 domain, predicted component of type ...
 553-663 4.39e-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: 41.81  E-value: 4.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966577  553 TEAAGVLFAITDAAQVVVSLGVKLSEVRDGQQNISLlytePGASQTQTGASFRLPAfvGQWTHFALSVDGGSVALYVDCE 632
Cdd:COG5306   200 TFSAWIKPAQLDGNAVLYSRRDGANGLDNGAPFVEV----GGAGGTRSAAGAPLAA--GTWHHLAVVADAGKVTLYVNGV 273

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 568966577  633 EFQRVPFAR------ASQGLELERGAGLFVGQAGTAD 663
Cdd:COG5306   274 AAGSLDASLptvtggATIGAVGLAAIASLSGQAVEAG 310
 
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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