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Conserved domains on  [gi|206597445|ref|NP_569711|]
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collagen alpha-1(XVIII) chain isoform 3 preproprotein [Homo sapiens]

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 ...
 1575-1745 8.18e-114

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: 357.03  E-value: 8.18e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445 1575 QPVLHLVALNSPLSGGMRGIRGADFQCFQQARAVGLAGTFRAFLSSRLQDLYSIVRRADRAAVPIVNLKDELLFPSWEAL 1654
Cdd:cd00247     1 QPVLHLVALNTPLSGDMRGIRGADFQCFQQARAAGLKGTFRAFLSSRLQDLYSIVRRADRDSLPIVNLKGEVLFNSWESL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445 1655 FSGSEGPLKPGARIFSFDGKDVLRHPTWPQKSVWHGSDPNGRRLTESYCETWRTEAPSATGQASSLLGGRLLGQSAASCH 1734
Cdd:cd00247    81 FSGSGGQFNPGARIYSFDGRDVLTDPAWPQKMVWHGSDPNGRRLTDSYCEAWRTGDSAVTGQASSLSSGKLLEQKAYSCE 160

                         170
                  ....*....|.
gi 206597445 1735 HAYIVLCIENS 1745
Cdd:cd00247   161 NKLIVLCIENS 171
CRD_Collagen_XVIII cd07455
Cysteine-rich domain of the variant 3 of collagen XVIII (V3C18 ); The cysteine-rich domain ...
 330-452 3.66e-64

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: 213.52  E-value: 3.66e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445  330 PAGRCLPLPPSLPVCGHLGISRFWLPNHLHHESGEQVRAGARAWGGLLQTHCHPFLAWFFCLLLVPPCGSVPPPAPPPCC 409
Cdd:cd07455     1 PRPRCLPVPSSLPFCSRLGIRSFWLPNFLNHTSVEEVRAVLAEWAWLLESGCHPSLEWFFCLLLVPSCGGGPPPPPPPCR 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 206597445  410 QFCEALQDACWSRLGGGRLPVACASLPTQEDGYCVLIGPAAER 452
Cdd:cd07455    81 QFCEVLQDSCWNLLEGGRLPVACASLPEQEDGYCVLIGPPAEN 123
DUF959 super family cl25749
Domain of Unknown Function (DUF959); This N-terminal domain is not expressed in the 'Short' ...
 23-194 2.48e-51

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: 179.64  E-value: 2.48e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445    23 ANLLNLNWLWFNnEDTSHAATTIPEPQGPLPVQPTADTTTHVTPRNGSTEPATAPGSPEPPSELLEDGQD-TPTS----- 96
Cdd:pfam06121   11 AHILGLDLLWFL-DIADPEDTLASEPQGGLAVQPAAAPATHVAPQDDPAEQATAAASPELPLEELEAAPGrAPGApisaa 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445    97 -----AESPDAPEENIAGVGAEILNVAKGIRSFVQLWNDTVPTESLARAETLVLETPVGPLALAGPSSTPQENGTTLWPS 171
Cdd:pfam06121   90 apaalAARPDMREENVAGVGAKILNIAQGIQSFIQLWNDAAPTESPAGAGTLAASAPTDPLALAEPSGPAAESGTALGPH 169

                          170       180
                   ....*....|....*....|...
gi 206597445   172 RGIPSSPGAHTTEAGTLPAPTPS 194
Cdd:pfam06121  170 RGALSSLDTPRAESGTLAVPTQL 192
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 456-644 3.45e-42

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


:

Pssm-ID: 214560  Cd Length: 184  Bit Score: 153.28  E-value: 3.45e-42
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445    456 EVGLLQLLGDPP-PQQVTQTDDPDVG-LAYVFGPDANSGQVARYHFPSLFFRDFSLLFHIRPATEGPGVLFAITDsAQAM 533
Cdd:smart00210    1 GQDLLQVFDLPSlSFAIRQVVGPEPGsPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPKSRGVLFAIYD-AQNV 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445    534 VLLGVKLsgvqDGHQDISLLYTEPGAGQTHTAASFRLPAFVGQWTHLALSVAGGFVALYVDCEEFQRMPLARSSRGLELe 613
Cdd:smart00210   80 RQFGLEV----DGRANTLLLRYQGVDGKQHTVSFRNLPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGQPPID- 154

                           170       180       190
                    ....*....|....*....|....*....|.
gi 206597445    614 pGAGLFVAQAGGADPDKFQGVIAELKVRRDP 644
Cdd:smart00210  155 -TDGIEVRGAQAADRKPFQGDLQQLKIVCDP 184
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1056-1246 8.63e-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.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 94.59  E-value: 8.63e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445 1056 KGDPGVPGLPGAKGEVGADGVPGFPGLPGREGIAGPQGPKGDRGSRGEKGDPGKDGVGQPGLPGPPGPPGPVVyvseqdg 1135
Cdd:NF038329  137 RGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPA------- 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445 1136 svlSVPGPEGRPGFAGFPGPAGPKGNL-----GSKGERGSPGPKGEKGEPGSIfSPDGGALGPAQKGAKGEPGFRGPPGP 1210
Cdd:NF038329  210 ---GPAGPDGEAGPAGEDGPAGPAGDGqqgpdGDPGPTGEDGPQGPDGPAGKD-GPRGDRGEAGPDGPDGKDGERGPVGP 285

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 206597445 1211 YGRPGYKGEIGFPGRPGRPGMNGLKGEKGEPGDASL 1246
Cdd:NF038329  286 AGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQ 321
Collagen_trimer pfam20010
Collagen trimerization domain; This small domain mediate trimerization in various collagen ...
 1442-1490 1.33e-18

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


:

Pssm-ID: 466257  Cd Length: 49  Bit Score: 80.73  E-value: 1.33e-18
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 206597445  1442 VRLWATRQAMLGQVHEVPEGWLIFVAEQEELYVRVQNGFRKVQLEARTP 1490
Cdd:pfam20010    1 VTVFQNYDTMLQKTHRVPEGTLVYVREREELYIRVRNGWRKIQLGELIP 49
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 156-345 7.61e-05

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.01  E-value: 7.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445  156 GPSSTPQENGTTLWPSRGIPSSPGAHTTEAGTLPAPTPSPPSlgrpwaplTGPSVPPPSSGRASLSSLLGGAPPWGSLQD 235
Cdd:PHA03247 2579 EPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPD--------THAPDPPPPSPSPAANEPDPHPPPTVPPPE 2650

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445  236 PDSQGLSPAAAAPSQQLQR---------PDVRLRTPLLHPLVmGSLGKHA-----------APSAFSSGLPGALSQVAVt 295
Cdd:PHA03247 2651 RPRDDPAPGRVSRPRRARRlgraaqassPPQRPRRRAARPTV-GSLTSLAdpppppptpepAPHALVSATPLPPGPAAA- 2728

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 206597445  296 tltrdSGAWVSHVANSVGPGLANNSALLGAD-----PEAPAGRCLPLPPSLPVCG 345
Cdd:PHA03247 2729 -----RQASPALPAAPAPPAVPAGPATPGGParparPPTTAGPPAPAPPAAPAAG 2778
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 789-995 2.13e-04

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


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 45.67  E-value: 2.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445  789 PLGPAGPA-LQTVPGPQGPPGPPGRDGTPGRDGEPGDPGEDGKPGDTGPQGFPGTPGDVGPKGDKGDPGVGERGPPGPQG 867
Cdd:NF038329  124 PAGPAGPAgEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPA 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445  868 PPGPPGPSFRHDKLTFIDMEGSGFGGDLEALRGPRGFPGPPGPPGVPGLPGEPGRFGVNSSD-VPGPAGLPGVPGREGPp 946
Cdd:NF038329  204 GEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRgEAGPDGPDGKDGERGP- 282

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 206597445  947 gfPGLPGPPGPPGREGPPGRTGQKGSLGEAGAPGHKGSKGAPGPAGARG 995
Cdd:NF038329  283 --VGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPG 329
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 713-856 3.69e-03

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: 41.81  E-value: 3.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445  713 EVEEQTTVASLGAQTLPGSDSVSTWDGSVRTPGGRVKEG-----GLKGQKGEPGVPGPPGRAGPPGSPCLPGPPGLPCPV 787
Cdd:NF038329  142 ETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGeagakGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPA 221

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 206597445  788 SPLGPAGPALQTVPGPQGPPGPPGRDGTPGRDGEPGDPGEDGKPGDTGPQGFPGTPGDVGPKGDKGDPG 856
Cdd:NF038329  222 GEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDG 290
 
Name Accession Description Interval E-value
Endostatin-like cd00247
Endostatin-like domain; the angiogenesis inhibitor endostatin is a C-terminal fragment of ...
 1575-1745 8.18e-114

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: 357.03  E-value: 8.18e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445 1575 QPVLHLVALNSPLSGGMRGIRGADFQCFQQARAVGLAGTFRAFLSSRLQDLYSIVRRADRAAVPIVNLKDELLFPSWEAL 1654
Cdd:cd00247     1 QPVLHLVALNTPLSGDMRGIRGADFQCFQQARAAGLKGTFRAFLSSRLQDLYSIVRRADRDSLPIVNLKGEVLFNSWESL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445 1655 FSGSEGPLKPGARIFSFDGKDVLRHPTWPQKSVWHGSDPNGRRLTESYCETWRTEAPSATGQASSLLGGRLLGQSAASCH 1734
Cdd:cd00247    81 FSGSGGQFNPGARIYSFDGRDVLTDPAWPQKMVWHGSDPNGRRLTDSYCEAWRTGDSAVTGQASSLSSGKLLEQKAYSCE 160

                         170
                  ....*....|.
gi 206597445 1735 HAYIVLCIENS 1745
Cdd:cd00247   161 NKLIVLCIENS 171
Endostatin pfam06482
Collagenase NC10 and Endostatin; NC10 stands for Non-helical region 10 and is taken from Swiss: ...
 1578-1746 4.81e-112

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: 352.13  E-value: 4.81e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445  1578 LHLVALNSPLSGGMRGIRGADFQCFQQARAVGLAGTFRAFLSSRLQDLYSIVRRADRAAVPIVNLKDELLFPSWEALFSG 1657
Cdd:pfam06482    1 LHLIALNTPQSGDMRGIRGADFLCFQQARAAGLKGTFRAFLSSRLQDLYSIVRKADRENVPIVNLKDEVLFDSWESIFSG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445  1658 SEGPLKPGARIFSFDGKDVLRHPTWPQKSVWHGSDPNGRRLTESYCETWRTEAPSATGQASSLLGGRLLGQSAASCHHAY 1737
Cdd:pfam06482   81 SGGQMKPNVPIYSFDGRDVLRDPAWPQKMVWHGSTSKGHRLTDNYCEAWRTGDQAVTGQASSLQSGKLLQQSPSSCSNSY 160


                   ....*....
gi 206597445  1738 IVLCIENSF 1746
Cdd:pfam06482  161 IVLCIENSY 169
CRD_Collagen_XVIII cd07455
Cysteine-rich domain of the variant 3 of collagen XVIII (V3C18 ); The cysteine-rich domain ...
 330-452 3.66e-64

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: 213.52  E-value: 3.66e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445  330 PAGRCLPLPPSLPVCGHLGISRFWLPNHLHHESGEQVRAGARAWGGLLQTHCHPFLAWFFCLLLVPPCGSVPPPAPPPCC 409
Cdd:cd07455     1 PRPRCLPVPSSLPFCSRLGIRSFWLPNFLNHTSVEEVRAVLAEWAWLLESGCHPSLEWFFCLLLVPSCGGGPPPPPPPCR 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 206597445  410 QFCEALQDACWSRLGGGRLPVACASLPTQEDGYCVLIGPAAER 452
Cdd:cd07455    81 QFCEVLQDSCWNLLEGGRLPVACASLPEQEDGYCVLIGPPAEN 123
DUF959 pfam06121
Domain of Unknown Function (DUF959); This N-terminal domain is not expressed in the 'Short' ...
 23-194 2.48e-51

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: 179.64  E-value: 2.48e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445    23 ANLLNLNWLWFNnEDTSHAATTIPEPQGPLPVQPTADTTTHVTPRNGSTEPATAPGSPEPPSELLEDGQD-TPTS----- 96
Cdd:pfam06121   11 AHILGLDLLWFL-DIADPEDTLASEPQGGLAVQPAAAPATHVAPQDDPAEQATAAASPELPLEELEAAPGrAPGApisaa 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445    97 -----AESPDAPEENIAGVGAEILNVAKGIRSFVQLWNDTVPTESLARAETLVLETPVGPLALAGPSSTPQENGTTLWPS 171
Cdd:pfam06121   90 apaalAARPDMREENVAGVGAKILNIAQGIQSFIQLWNDAAPTESPAGAGTLAASAPTDPLALAEPSGPAAESGTALGPH 169

                          170       180
                   ....*....|....*....|...
gi 206597445   172 RGIPSSPGAHTTEAGTLPAPTPS 194
Cdd:pfam06121  170 RGALSSLDTPRAESGTLAVPTQL 192
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 456-644 3.45e-42

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


Pssm-ID: 214560  Cd Length: 184  Bit Score: 153.28  E-value: 3.45e-42
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445    456 EVGLLQLLGDPP-PQQVTQTDDPDVG-LAYVFGPDANSGQVARYHFPSLFFRDFSLLFHIRPATEGPGVLFAITDsAQAM 533
Cdd:smart00210    1 GQDLLQVFDLPSlSFAIRQVVGPEPGsPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPKSRGVLFAIYD-AQNV 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445    534 VLLGVKLsgvqDGHQDISLLYTEPGAGQTHTAASFRLPAFVGQWTHLALSVAGGFVALYVDCEEFQRMPLARSSRGLELe 613
Cdd:smart00210   80 RQFGLEV----DGRANTLLLRYQGVDGKQHTVSFRNLPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGQPPID- 154

                           170       180       190
                    ....*....|....*....|....*....|.
gi 206597445    614 pGAGLFVAQAGGADPDKFQGVIAELKVRRDP 644
Cdd:smart00210  155 -TDGIEVRGAQAADRKPFQGDLQQLKIVCDP 184
FRI smart00063
Frizzled; Drosophila melanogaster frizzled mediates signalling that polarises a precursor cell ...
 334-444 3.78e-22

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: 93.14  E-value: 3.78e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445    334 CLPLppSLPVCGHLGISRFWLPNHLHHESGEQVRAGARAWGGLLQTHCHPFLAWFFCLLLVPPCGsVPPPAPPPCCQFCE 413
Cdd:smart00063    1 CEPI--TIPLCKDLGYNLTSMPNLLGHTTQEEAGLELEQFHPLLNVQCSPDLRFFLCSVYAPICT-EDLRPILPCRSLCE 77

                            90       100       110
                    ....*....|....*....|....*....|....*
gi 206597445    414 ALQDACWSRLGGGRLP----VACASLPTQEDgYCV 444
Cdd:smart00063   78 AAREGCEPLMEKFGFPwpefLRCDRFPVQEE-LCM 111
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1056-1246 8.63e-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: 94.59  E-value: 8.63e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445 1056 KGDPGVPGLPGAKGEVGADGVPGFPGLPGREGIAGPQGPKGDRGSRGEKGDPGKDGVGQPGLPGPPGPPGPVVyvseqdg 1135
Cdd:NF038329  137 RGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPA------- 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445 1136 svlSVPGPEGRPGFAGFPGPAGPKGNL-----GSKGERGSPGPKGEKGEPGSIfSPDGGALGPAQKGAKGEPGFRGPPGP 1210
Cdd:NF038329  210 ---GPAGPDGEAGPAGEDGPAGPAGDGqqgpdGDPGPTGEDGPQGPDGPAGKD-GPRGDRGEAGPDGPDGKDGERGPVGP 285

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 206597445 1211 YGRPGYKGEIGFPGRPGRPGMNGLKGEKGEPGDASL 1246
Cdd:NF038329  286 AGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQ 321
Fz pfam01392
Fz domain; Also known as the CRD (cysteine rich domain), the C6 box in MuSK receptor. This ...
 334-438 7.49e-19

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: 83.77  E-value: 7.49e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445   334 CLPLppSLPVCGHLGISRFWLPNHLHHESGEQVRAGAR-----AWGGLLQTHCHPFLAWFFCLLLVPPCGSVPPPAPPP- 407
Cdd:pfam01392    1 CEPI--TLPMCLGLGYNATVFPNLLGHQTQEEAELSLAylvlsEFEPLVDLSCSPSLRLFLCSLYFPPCTLGPSPKPVCp 78

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 206597445   408 -CCQFCEALQDACWSRL----GGGRLP--VACASLPTQ 438
Cdd:pfam01392   79 pCRSLCEEVRYGCEPLLeeakFGFSWPefLDCDSLPAD 116
Collagen_trimer pfam20010
Collagen trimerization domain; This small domain mediate trimerization in various collagen ...
 1442-1490 1.33e-18

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


Pssm-ID: 466257  Cd Length: 49  Bit Score: 80.73  E-value: 1.33e-18
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 206597445  1442 VRLWATRQAMLGQVHEVPEGWLIFVAEQEELYVRVQNGFRKVQLEARTP 1490
Cdd:pfam20010    1 VTVFQNYDTMLQKTHRVPEGTLVYVREREELYIRVRNGWRKIQLGELIP 49
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 931-1181 2.86e-17

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: 86.50  E-value: 2.86e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445  931 PGPAGLPGVPGREGPPGFPGLPGPPGPPGREGPPGRTGQKGSLGEAGAPGHKGSKGAPGPAGARGESGLAGAPGPAgppg 1010
Cdd:NF038329  134 QGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPA---- 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445 1011 ppgppgppgpglpagfddmeGSGGPFWSTARSADGPQGPPGLPGLKGDPGVPGLPGAKGEVGADGVPGFPGLPGREGIAG 1090
Cdd:NF038329  210 --------------------GPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAG 269

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445 1091 PQGPKGDRGSRGEKGDPGKDGvgqpglpgppgppgpvvyvseQDGSVlSVPGPEGRPGFAGFPGPAGPKGNLGSKGERGS 1170
Cdd:NF038329  270 PDGPDGKDGERGPVGPAGKDG---------------------QNGKD-GLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGL 327

                         250
                  ....*....|.
gi 206597445 1171 PGPKGEKGEPG 1181
Cdd:NF038329  328 PGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 959-1242 4.51e-17

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: 86.11  E-value: 4.51e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445  959 GREGPPGRTGQKGSLGEAGAPGHKGSKGAPGPAGARGESglagapgpagppgppgppgppgpglpagfddmegsgGPfws 1038
Cdd:NF038329  132 GEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEA------------------------------------GP--- 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445 1039 tarsadgpqgppglpglKGDPGVPGLPGAKGEVGADGVPGFPGLPGREGIAGPQGPKGDRGSRGEKGDPGKDGVGQPGLP 1118
Cdd:NF038329  173 -----------------QGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQ 235

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445 1119 GPPGPpgpvvyvseqdgsvlsvPGPEGRPGFAGFPGPAGPKGNLGSKGERGSPGPKGEKGEPGsifsPDGGALGPAQKGA 1198
Cdd:NF038329  236 GPDGD-----------------PGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERG----PVGPAGKDGQNGK 294

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 206597445 1199 KGEPGFRGPPGPYGRPGYKGEIGFPGRPGRPGMNGLKGEKGEPG 1242
Cdd:NF038329  295 DGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1074-1334 2.03e-11

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: 68.39  E-value: 2.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445 1074 DGVPGFPGLPGREGIAGPQGPKGDRGSRGEKGDPGKDGVGqpglpgppgppgpvvyvseqdgsvlsvpGPEGRPGFAGFP 1153
Cdd:NF038329  116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQ----------------------------GERGEKGPAGPQ 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445 1154 GPAGPKGNLGSKGERGSPGPKGEKGEPGsifspdggalgpaqkgAKGEPGfrgppgpygrpgYKGEIGFPGRPGRPGMNG 1233
Cdd:NF038329  168 GEAGPQGPAGKDGEAGAKGPAGEKGPQG----------------PRGETG------------PAGEQGPAGPAGPDGEAG 219

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445 1234 LKGEKGEPGdaslgfgmrgmpgppgppgppgppgtpvydsnvfaessrPGPPGLPGNQGPPGPKGAKGEVGPPGppgqfp 1313
Cdd:NF038329  220 PAGEDGPAG---------------------------------------PAGDGQQGPDGDPGPTGEDGPQGPDG------ 254

                         250       260
                  ....*....|....*....|.
gi 206597445 1314 fdflqlEAEMKGEKGDRGDAG 1334
Cdd:NF038329  255 ------PAGKDGPRGDRGEAG 269
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1057-1107 9.59e-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: 9.59e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 206597445  1057 GDPGVPGLPGAKGEVGADGVPGFPGLPGREGIAGPQGPKGDRGSRGEKGDP 1107
Cdd:pfam01391    7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Laminin_G_3 pfam13385
Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin ...
 488-640 4.06e-05

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


Pssm-ID: 463865 [Multi-domain]  Cd Length: 151  Bit Score: 45.45  E-value: 4.06e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445   488 DANSGQVAryhFPSLFF--RDFSLLFHIRP-ATEGPGVLFAITDSAQAMVLlgvklsGVQDGHQDISLLYTEPGAGQTHT 564
Cdd:pfam13385    1 DGGSDYVT---LPDALLptSDFTVSAWVKPdSLPGWARAIISSSGGGGYSL------GLDGDGRLRFAVNGGNGGWDTVT 71

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 206597445   565 AASfrlPAFVGQWTHLALSVAGGFVALYVDCEEFQRmplaRSSRGLELEPGAGLFV--AQAGGADPdkFQGVIAELKV 640
Cdd:pfam13385   72 SGA---SVPLGQWTHVAVTYDGGTLRLYVNGVLVGS----STLTGGPPPGTGGPLYigRSPGGDDY--FNGLIDEVRI 140
PHA03247 PHA03247
large tegument protein UL36; Provisional
 156-345 7.61e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.01  E-value: 7.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445  156 GPSSTPQENGTTLWPSRGIPSSPGAHTTEAGTLPAPTPSPPSlgrpwaplTGPSVPPPSSGRASLSSLLGGAPPWGSLQD 235
Cdd:PHA03247 2579 EPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPD--------THAPDPPPPSPSPAANEPDPHPPPTVPPPE 2650

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445  236 PDSQGLSPAAAAPSQQLQR---------PDVRLRTPLLHPLVmGSLGKHA-----------APSAFSSGLPGALSQVAVt 295
Cdd:PHA03247 2651 RPRDDPAPGRVSRPRRARRlgraaqassPPQRPRRRAARPTV-GSLTSLAdpppppptpepAPHALVSATPLPPGPAAA- 2728

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 206597445  296 tltrdSGAWVSHVANSVGPGLANNSALLGAD-----PEAPAGRCLPLPPSLPVCG 345
Cdd:PHA03247 2729 -----RQASPALPAAPAPPAVPAGPATPGGParparPPTTAGPPAPAPPAAPAAG 2778
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 789-995 2.13e-04

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 45.67  E-value: 2.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445  789 PLGPAGPA-LQTVPGPQGPPGPPGRDGTPGRDGEPGDPGEDGKPGDTGPQGFPGTPGDVGPKGDKGDPGVGERGPPGPQG 867
Cdd:NF038329  124 PAGPAGPAgEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPA 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445  868 PPGPPGPSFRHDKLTFIDMEGSGFGGDLEALRGPRGFPGPPGPPGVPGLPGEPGRFGVNSSD-VPGPAGLPGVPGREGPp 946
Cdd:NF038329  204 GEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRgEAGPDGPDGKDGERGP- 282

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 206597445  947 gfPGLPGPPGPPGREGPPGRTGQKGSLGEAGAPGHKGSKGAPGPAGARG 995
Cdd:NF038329  283 --VGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPG 329
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 492-640 2.85e-04

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: 43.18  E-value: 2.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445  492 GQVARYHFPSLFFRDFSLLFHIRPaTEGPGVLFAITDSAQAMVLLgVKLSgvqDGHqdISLLYtEPGAGQThtaaSFRLP 571
Cdd:cd00110     7 SSYVRLPTLPAPRTRLSISFSFRT-TSPNGLLLYAGSQNGGDFLA-LELE---DGR--LVLRY-DLGSGSL----VLSSK 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445  572 AFV--GQWTHLALSVAGGFVALYVDCEEFQRMPLARSSRGLELEpgAGLFVaqaGGADPDK----------FQGVIAELK 639
Cdd:cd00110    75 TPLndGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLD--GPLYL---GGLPEDLkspglpvspgFVGCIRDLK 149


                  .
gi 206597445  640 V 640
Cdd:cd00110   150 V 150
PHA03247 PHA03247
large tegument protein UL36; Provisional
 44-342 8.27e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.54  E-value: 8.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445   44 TIPEPQ-GPLPVQPTA-----------DTTTHVTPRNGSTEP-ATAPGSPEPPSElleDGQDTPTSAESPDAPEENIAGV 110
Cdd:PHA03247 2567 SVPPPRpAPRPSEPAVtsrarrpdappQSARPRAPVDDRGDPrGPAPPSPLPPDT---HAPDPPPPSPSPAANEPDPHPP 2643

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445  111 GAEILNVAKGIRSFVQLWNDTVPTESLARAetlvletpvgplalAGPSSTPQEngttlWPSRGIPSSPGAHTTEAGTlPA 190
Cdd:PHA03247 2644 PTVPPPERPRDDPAPGRVSRPRRARRLGRA--------------AQASSPPQR-----PRRRAARPTVGSLTSLADP-PP 2703

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445  191 PTPSPPSLGRPWAPLTGPSVPPPSSGRASLSSLLGGAPPwgslqdpdsqglsPAAAAPSQqlqrpDVRLRTPLLHPLVMG 270
Cdd:PHA03247 2704 PPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPP-------------AVPAGPAT-----PGGPARPARPPTTAG 2765

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 206597445  271 SlGKHAAPSAFSSGLPGALSQVAVTTLTRDSGAWVS------HVANSVGPGLANNSALLGADPEAPAGRCLPLPPSLP 342
Cdd:PHA03247 2766 P-PAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSpwdpadPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPP 2842
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 819-856 9.82e-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: 39.01  E-value: 9.82e-04
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 206597445   819 DGEPGDPGEDGKPGDTGPQGFPGTPGDVGPKGDKGDPG 856
Cdd:pfam01391   12 PGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPG 49
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 713-856 3.69e-03

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: 41.81  E-value: 3.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445  713 EVEEQTTVASLGAQTLPGSDSVSTWDGSVRTPGGRVKEG-----GLKGQKGEPGVPGPPGRAGPPGSPCLPGPPGLPCPV 787
Cdd:NF038329  142 ETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGeagakGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPA 221

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 206597445  788 SPLGPAGPALQTVPGPQGPPGPPGRDGTPGRDGEPGDPGEDGKPGDTGPQGFPGTPGDVGPKGDKGDPG 856
Cdd:NF038329  222 GEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDG 290
 
Name Accession Description Interval E-value
Endostatin-like cd00247
Endostatin-like domain; the angiogenesis inhibitor endostatin is a C-terminal fragment of ...
 1575-1745 8.18e-114

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: 357.03  E-value: 8.18e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445 1575 QPVLHLVALNSPLSGGMRGIRGADFQCFQQARAVGLAGTFRAFLSSRLQDLYSIVRRADRAAVPIVNLKDELLFPSWEAL 1654
Cdd:cd00247     1 QPVLHLVALNTPLSGDMRGIRGADFQCFQQARAAGLKGTFRAFLSSRLQDLYSIVRRADRDSLPIVNLKGEVLFNSWESL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445 1655 FSGSEGPLKPGARIFSFDGKDVLRHPTWPQKSVWHGSDPNGRRLTESYCETWRTEAPSATGQASSLLGGRLLGQSAASCH 1734
Cdd:cd00247    81 FSGSGGQFNPGARIYSFDGRDVLTDPAWPQKMVWHGSDPNGRRLTDSYCEAWRTGDSAVTGQASSLSSGKLLEQKAYSCE 160

                         170
                  ....*....|.
gi 206597445 1735 HAYIVLCIENS 1745
Cdd:cd00247   161 NKLIVLCIENS 171
Endostatin pfam06482
Collagenase NC10 and Endostatin; NC10 stands for Non-helical region 10 and is taken from Swiss: ...
 1578-1746 4.81e-112

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: 352.13  E-value: 4.81e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445  1578 LHLVALNSPLSGGMRGIRGADFQCFQQARAVGLAGTFRAFLSSRLQDLYSIVRRADRAAVPIVNLKDELLFPSWEALFSG 1657
Cdd:pfam06482    1 LHLIALNTPQSGDMRGIRGADFLCFQQARAAGLKGTFRAFLSSRLQDLYSIVRKADRENVPIVNLKDEVLFDSWESIFSG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445  1658 SEGPLKPGARIFSFDGKDVLRHPTWPQKSVWHGSDPNGRRLTESYCETWRTEAPSATGQASSLLGGRLLGQSAASCHHAY 1737
Cdd:pfam06482   81 SGGQMKPNVPIYSFDGRDVLRDPAWPQKMVWHGSTSKGHRLTDNYCEAWRTGDQAVTGQASSLQSGKLLQQSPSSCSNSY 160


                   ....*....
gi 206597445  1738 IVLCIENSF 1746
Cdd:pfam06482  161 IVLCIENSY 169
CRD_Collagen_XVIII cd07455
Cysteine-rich domain of the variant 3 of collagen XVIII (V3C18 ); The cysteine-rich domain ...
 330-452 3.66e-64

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: 213.52  E-value: 3.66e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445  330 PAGRCLPLPPSLPVCGHLGISRFWLPNHLHHESGEQVRAGARAWGGLLQTHCHPFLAWFFCLLLVPPCGSVPPPAPPPCC 409
Cdd:cd07455     1 PRPRCLPVPSSLPFCSRLGIRSFWLPNFLNHTSVEEVRAVLAEWAWLLESGCHPSLEWFFCLLLVPSCGGGPPPPPPPCR 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 206597445  410 QFCEALQDACWSRLGGGRLPVACASLPTQEDGYCVLIGPAAER 452
Cdd:cd07455    81 QFCEVLQDSCWNLLEGGRLPVACASLPEQEDGYCVLIGPPAEN 123
DUF959 pfam06121
Domain of Unknown Function (DUF959); This N-terminal domain is not expressed in the 'Short' ...
 23-194 2.48e-51

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: 179.64  E-value: 2.48e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445    23 ANLLNLNWLWFNnEDTSHAATTIPEPQGPLPVQPTADTTTHVTPRNGSTEPATAPGSPEPPSELLEDGQD-TPTS----- 96
Cdd:pfam06121   11 AHILGLDLLWFL-DIADPEDTLASEPQGGLAVQPAAAPATHVAPQDDPAEQATAAASPELPLEELEAAPGrAPGApisaa 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445    97 -----AESPDAPEENIAGVGAEILNVAKGIRSFVQLWNDTVPTESLARAETLVLETPVGPLALAGPSSTPQENGTTLWPS 171
Cdd:pfam06121   90 apaalAARPDMREENVAGVGAKILNIAQGIQSFIQLWNDAAPTESPAGAGTLAASAPTDPLALAEPSGPAAESGTALGPH 169

                          170       180
                   ....*....|....*....|...
gi 206597445   172 RGIPSSPGAHTTEAGTLPAPTPS 194
Cdd:pfam06121  170 RGALSSLDTPRAESGTLAVPTQL 192
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 456-644 3.45e-42

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


Pssm-ID: 214560  Cd Length: 184  Bit Score: 153.28  E-value: 3.45e-42
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445    456 EVGLLQLLGDPP-PQQVTQTDDPDVG-LAYVFGPDANSGQVARYHFPSLFFRDFSLLFHIRPATEGPGVLFAITDsAQAM 533
Cdd:smart00210    1 GQDLLQVFDLPSlSFAIRQVVGPEPGsPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPKSRGVLFAIYD-AQNV 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445    534 VLLGVKLsgvqDGHQDISLLYTEPGAGQTHTAASFRLPAFVGQWTHLALSVAGGFVALYVDCEEFQRMPLARSSRGLELe 613
Cdd:smart00210   80 RQFGLEV----DGRANTLLLRYQGVDGKQHTVSFRNLPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGQPPID- 154

                           170       180       190
                    ....*....|....*....|....*....|.
gi 206597445    614 pGAGLFVAQAGGADPDKFQGVIAELKVRRDP 644
Cdd:smart00210  155 -TDGIEVRGAQAADRKPFQGDLQQLKIVCDP 184
FRI smart00063
Frizzled; Drosophila melanogaster frizzled mediates signalling that polarises a precursor cell ...
 334-444 3.78e-22

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: 93.14  E-value: 3.78e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445    334 CLPLppSLPVCGHLGISRFWLPNHLHHESGEQVRAGARAWGGLLQTHCHPFLAWFFCLLLVPPCGsVPPPAPPPCCQFCE 413
Cdd:smart00063    1 CEPI--TIPLCKDLGYNLTSMPNLLGHTTQEEAGLELEQFHPLLNVQCSPDLRFFLCSVYAPICT-EDLRPILPCRSLCE 77

                            90       100       110
                    ....*....|....*....|....*....|....*
gi 206597445    414 ALQDACWSRLGGGRLP----VACASLPTQEDgYCV 444
Cdd:smart00063   78 AAREGCEPLMEKFGFPwpefLRCDRFPVQEE-LCM 111
CRD_FZ cd07066
CRD_domain cysteine-rich domain, also known as Fz (frizzled) domain; CRD_FZ is an essential ...
 333-444 6.47e-22

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: 92.57  E-value: 6.47e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445  333 RCLPLPPSLpvCGHLGISRFWLPNHLHHESGEQVRAGARAWGGLLQTHCHPFLAWFFCLLLVPPCGSVPPPAPPPCCQFC 412
Cdd:cd07066     1 KCEPIPLPL--CRGLPYNTTRFPNLLGHESQEEAEQELESFTPLVNSGCHPDLRFFLCSLYFPECTPDGDRPIPPCRSLC 78

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 206597445  413 EALQDACWSRL----GGGRLPVACASLPTQ-EDGYCV 444
Cdd:cd07066    79 EEVRDSCEPLMlafgFPWPEPLDCDRFPDSnEEGLCI 115
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1056-1246 8.63e-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: 94.59  E-value: 8.63e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445 1056 KGDPGVPGLPGAKGEVGADGVPGFPGLPGREGIAGPQGPKGDRGSRGEKGDPGKDGVGQPGLPGPPGPPGPVVyvseqdg 1135
Cdd:NF038329  137 RGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPA------- 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445 1136 svlSVPGPEGRPGFAGFPGPAGPKGNL-----GSKGERGSPGPKGEKGEPGSIfSPDGGALGPAQKGAKGEPGFRGPPGP 1210
Cdd:NF038329  210 ---GPAGPDGEAGPAGEDGPAGPAGDGqqgpdGDPGPTGEDGPQGPDGPAGKD-GPRGDRGEAGPDGPDGKDGERGPVGP 285

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 206597445 1211 YGRPGYKGEIGFPGRPGRPGMNGLKGEKGEPGDASL 1246
Cdd:NF038329  286 AGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQ 321
Fz pfam01392
Fz domain; Also known as the CRD (cysteine rich domain), the C6 box in MuSK receptor. This ...
 334-438 7.49e-19

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: 83.77  E-value: 7.49e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445   334 CLPLppSLPVCGHLGISRFWLPNHLHHESGEQVRAGAR-----AWGGLLQTHCHPFLAWFFCLLLVPPCGSVPPPAPPP- 407
Cdd:pfam01392    1 CEPI--TLPMCLGLGYNATVFPNLLGHQTQEEAELSLAylvlsEFEPLVDLSCSPSLRLFLCSLYFPPCTLGPSPKPVCp 78

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 206597445   408 -CCQFCEALQDACWSRL----GGGRLP--VACASLPTQ 438
Cdd:pfam01392   79 pCRSLCEEVRYGCEPLLeeakFGFSWPefLDCDSLPAD 116
Collagen_trimer pfam20010
Collagen trimerization domain; This small domain mediate trimerization in various collagen ...
 1442-1490 1.33e-18

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


Pssm-ID: 466257  Cd Length: 49  Bit Score: 80.73  E-value: 1.33e-18
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 206597445  1442 VRLWATRQAMLGQVHEVPEGWLIFVAEQEELYVRVQNGFRKVQLEARTP 1490
Cdd:pfam20010    1 VTVFQNYDTMLQKTHRVPEGTLVYVREREELYIRVRNGWRKIQLGELIP 49
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 931-1181 2.86e-17

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: 86.50  E-value: 2.86e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445  931 PGPAGLPGVPGREGPPGFPGLPGPPGPPGREGPPGRTGQKGSLGEAGAPGHKGSKGAPGPAGARGESGLAGAPGPAgppg 1010
Cdd:NF038329  134 QGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPA---- 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445 1011 ppgppgppgpglpagfddmeGSGGPFWSTARSADGPQGPPGLPGLKGDPGVPGLPGAKGEVGADGVPGFPGLPGREGIAG 1090
Cdd:NF038329  210 --------------------GPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAG 269

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445 1091 PQGPKGDRGSRGEKGDPGKDGvgqpglpgppgppgpvvyvseQDGSVlSVPGPEGRPGFAGFPGPAGPKGNLGSKGERGS 1170
Cdd:NF038329  270 PDGPDGKDGERGPVGPAGKDG---------------------QNGKD-GLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGL 327

                         250
                  ....*....|.
gi 206597445 1171 PGPKGEKGEPG 1181
Cdd:NF038329  328 PGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 959-1242 4.51e-17

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: 86.11  E-value: 4.51e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445  959 GREGPPGRTGQKGSLGEAGAPGHKGSKGAPGPAGARGESglagapgpagppgppgppgppgpglpagfddmegsgGPfws 1038
Cdd:NF038329  132 GEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEA------------------------------------GP--- 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445 1039 tarsadgpqgppglpglKGDPGVPGLPGAKGEVGADGVPGFPGLPGREGIAGPQGPKGDRGSRGEKGDPGKDGVGQPGLP 1118
Cdd:NF038329  173 -----------------QGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQ 235

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445 1119 GPPGPpgpvvyvseqdgsvlsvPGPEGRPGFAGFPGPAGPKGNLGSKGERGSPGPKGEKGEPGsifsPDGGALGPAQKGA 1198
Cdd:NF038329  236 GPDGD-----------------PGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERG----PVGPAGKDGQNGK 294

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 206597445 1199 KGEPGFRGPPGPYGRPGYKGEIGFPGRPGRPGMNGLKGEKGEPG 1242
Cdd:NF038329  295 DGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1074-1334 2.03e-11

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: 68.39  E-value: 2.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445 1074 DGVPGFPGLPGREGIAGPQGPKGDRGSRGEKGDPGKDGVGqpglpgppgppgpvvyvseqdgsvlsvpGPEGRPGFAGFP 1153
Cdd:NF038329  116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQ----------------------------GERGEKGPAGPQ 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445 1154 GPAGPKGNLGSKGERGSPGPKGEKGEPGsifspdggalgpaqkgAKGEPGfrgppgpygrpgYKGEIGFPGRPGRPGMNG 1233
Cdd:NF038329  168 GEAGPQGPAGKDGEAGAKGPAGEKGPQG----------------PRGETG------------PAGEQGPAGPAGPDGEAG 219

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445 1234 LKGEKGEPGdaslgfgmrgmpgppgppgppgppgtpvydsnvfaessrPGPPGLPGNQGPPGPKGAKGEVGPPGppgqfp 1313
Cdd:NF038329  220 PAGEDGPAG---------------------------------------PAGDGQQGPDGDPGPTGEDGPQGPDG------ 254

                         250       260
                  ....*....|....*....|.
gi 206597445 1314 fdflqlEAEMKGEKGDRGDAG 1334
Cdd:NF038329  255 ------PAGKDGPRGDRGEAG 269
CRD_SFRP1 cd07443
Cysteine-rich domain of the secreted frizzled-related protein 1 (SFRP1), a regulator of Wnt ...
 333-419 3.58e-11

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: 62.22  E-value: 3.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445  333 RCLPLPPSLPVCGHLGISRFWLPNHLHHESGEQVRAGARAWGGLLQTHCHPFLAWFFCLLLVPPCgsvPPPAPPPCCQFC 412
Cdd:cd07443     6 QCVDIPADLRLCHNVGYKKMVLPNLLDHETMAEVKQQASSWVPLLNKNCHKGTQVFLCSLFAPVC---LDRPVYPCRWLC 82


                  ....*..
gi 206597445  413 EALQDAC 419
Cdd:cd07443    83 EAVRDSC 89
CRD_SFRP5 cd07444
Cysteine-rich domain of the secreted frizzled-related protein 5 (SFRP5), a regulator of Wnt ...
 333-419 3.88e-11

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: 62.27  E-value: 3.88e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445  333 RCLPLPPSLPVCGHLGISRFWLPNHLHHESGEQVRAGARAWGGLLQTHCHPFLAWFFCLLLVPPCgsvPPPAPPPCCQFC 412
Cdd:cd07444     6 QCVDIPADLPLCHNVGYKRMRLPNLLEHESMAEVKQQASSWVPLLAKRCHADTQVFLCSLFAPVC---LDRPIYPCRSLC 82


                  ....*..
gi 206597445  413 EALQDAC 419
Cdd:cd07444    83 EAVRDSC 89
CRD_sizzled cd07452
Cysteine-rich domain of the sizzled protein; The cysteine-rich domain (CRD) is an essential ...
 333-440 5.69e-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: 5.69e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445  333 RCLPLPPSLPVCGHLGISRFWLPNHLHHESGEQVRAGARAWGGLLQTHCHPFLAWFFCLLLVPPCgsvPPPAPPPCCQFC 412
Cdd:cd07452     8 KCVPIPPEMSMCQDVGYSEMRLPNLLGHTSMAEVVPKSADWQTLLHTGCHPHARTFLCSLFAPVC---LDTFIQPCRSMC 84

                          90       100       110
                  ....*....|....*....|....*....|..
gi 206597445  413 EALQDACWSRLG--GGRLP--VACASLPTQED 440
Cdd:cd07452    85 VAVRDSCAPVLAchGHSWPesLDCDRFPAGED 116
CRD_SFRP2 cd07446
Cysteine-rich domain of the secreted frizzled-related protein 2 (SFRP2), a regulator of Wnt ...
 334-419 3.41e-10

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: 59.54  E-value: 3.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445  334 CLPLPPSLPVCGHLGISRFWLPNHLHHESGEQVRAGARAWGGLLQTHCHPFLAWFFCLLLVPPCGSVPPPAPPPCCQFCE 413
Cdd:cd07446     5 CKPIPANMLLCHGIEYTNMRLPNLLGHETMKEVLQQAGSWIPLVQKQCHPDTKKFLCSLFAPVCLDDLDEAIQPCRSLCE 84


                  ....*.
gi 206597445  414 ALQDAC 419
Cdd:cd07446    85 AVKDGC 90
CRD_crescent cd07453
Cysteine-rich domain of the crescent protein; The cysteine-rich domain (CRD) is an essential ...
 333-419 1.31e-09

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: 58.03  E-value: 1.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445  333 RCLPLPPSLPVCGHLGISRFWLPNHLHHESGEQVRAGARAWGGLLQTHCHPFLAWFFCLLLVPPCgsvPPPAPPPCCQFC 412
Cdd:cd07453     2 PCMRIPKSMALCYDIGYSEMRIPNLLEHETMAEVIQQSSSWLPLLARECHPDARIFLCSLFAPIC---WDRPIYPCRSLC 78


                  ....*..
gi 206597445  413 EALQDAC 419
Cdd:cd07453    79 EAVRSSC 85
CRD_corin_2 cd07888
One of two cysteine-rich domains of the corin protein, a type II transmembrane serine protease ...
 338-448 3.32e-09

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: 56.56  E-value: 3.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445  338 PPSLPVCGHLGISRFWLPNHLHHESGEQ--VRAGARAWGGLLQTHCHPFLAWFFCLLLVPPCGSVPPPAPPPCCQFCEAL 415
Cdd:cd07888     4 PITLELCMNLPYNTTRYPNYLGHRTQKEasISWESSLFPALVQTNCYKYLMFFACTILVPKCDPVTQQRIPPCRSLCRNS 83

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 206597445  416 QDACWSRLG--GGRLP--VACASLP--TQEDGYCVLIGP 448
Cdd:cd07888    84 KERCESVLGivGLQWPedTDCAQFPeeNSDNQTCLLPDE 122
CRD_SFRP3 cd07441
Cysteine-rich domain of the secreted frizzled-related protein 3 (SFRP3, alias FRZB), a Wnt ...
 338-450 1.09e-08

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: 55.06  E-value: 1.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445  338 PPSLPVCGHLGISRFWLPNHLHHESGEQVRAGARAWGGLLQTHCHPFLAWFFCLLLVPPCG-SVPPPAPPPCCQFCEALQ 416
Cdd:cd07441     6 PVRIPMCKSMPWNMTKMPNHLHHSTQANAVLAIEQFEGLLGTQCSPDLLFFLCAMYAPICTiDFQHEPIKPCKSVCERAR 85

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 206597445  417 DACWSRLGGGRL----PVACASLPTQEDGYCvlIGPAA 450
Cdd:cd07441    86 AGCEPVLIRYRHtwpeSLACEELPVYDRGVC--ISPEA 121
CRD_SFRP4 cd07442
Cysteine-rich domain of the secreted frizzled-related protein 4 (SFRP4), a Wnt antagonist; The ...
 341-450 3.07e-08

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: 53.88  E-value: 3.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445  341 LPVCGHL--GISRfwLPNHLHHESGEQVRAGARAWGGLLQTHCHPFLAWFFCLLLVPPCG-SVPPPAPPPCCQFCEALQD 417
Cdd:cd07442    10 IPMCRHMpwNITR--MPNHLHHSTQENAVLAIEQYEELVDTGCSPVLPFFLCAMYAPICTlEFLYDPIKPCRSVCQRARD 87

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 206597445  418 ACWS--RLGGGRLP--VACASLPTQEDGYCvlIGPAA 450
Cdd:cd07442    88 GCEPimRRYNHSWPesLACDDLPVYDRGVC--ISPEA 122
CRD_FZ9_like cd07457
Cysteine-rich Wnt-binding domain (CRD) of receptors similar to frizzled 9; The cysteine-rich ...
 332-419 7.31e-07

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: 49.80  E-value: 7.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445  332 GRCLPLppSLPVCGHLGISRFWLPNHLHHESGEQVRAGARAWGGLLQTHCHPFLAWFFCLLLVPPCGSVPPPAPPPCCQF 411
Cdd:cd07457     1 GKCERI--TIPMCQGIGYNMTRMPNLLGHESQSEAAISIHEFAPLVQYGCAEHLRFFLCSLYAPMCTEQVSIPIPACRSM 78


                  ....*...
gi 206597445  412 CEALQDAC 419
Cdd:cd07457    79 CEQARDKC 86
CRD_FZ9 cd07463
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 9 (Fz9) receptor; The cysteine-rich ...
 331-440 1.31e-06

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: 49.25  E-value: 1.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445  331 AGRCLPLppSLPVCGHLGISRFWLPNHLHHESGEQVRAGARAWGGLLQTHCHPFLAWFFCLLLVPPCGSVPPPAPPPCCQ 410
Cdd:cd07463     2 AAKCQPV--VIPMCRGIGYNLTRMPNFLGHDSQREAAIKLNEFAPLVEYGCHVHLRFFLCSLYAPMCTDQVSTSIPACRP 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 206597445  411 FCEALQDACWSRLG----GGRLPVACASLPTQED 440
Cdd:cd07463    80 MCEQARQKCSPIMEqfnfGWPESLDCSRLPTRND 113
CRD_FZ10 cd07462
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 10 (Fz10) receptor; The cysteine-rich ...
 332-419 7.46e-06

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: 46.94  E-value: 7.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445  332 GRCLPLppSLPVCGHLGISRFWLPNHLHHESGEQVRAGARAWGGLLQTHCHPFLAWFFCLLLVPPCGSVPPPAPPPCCQF 411
Cdd:cd07462     3 GRCQPI--EIPMCKDIGYNMTRMPNLMGHENQREAAIQLHEFAPLVEYGCHSHLKFFLCSLYAPMCTEQVSTPIPACRVM 80


                  ....*...
gi 206597445  412 CEALQDAC 419
Cdd:cd07462    81 CEQARLKC 88
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1057-1107 9.59e-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: 9.59e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 206597445  1057 GDPGVPGLPGAKGEVGADGVPGFPGLPGREGIAGPQGPKGDRGSRGEKGDP 1107
Cdd:pfam01391    7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
CRD_LIN_17 cd07454
Cysteine-rich domain (CRD) of LIN_17; A cysteine-rich domain (CRD) is an essential component ...
 332-440 9.65e-06

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: 46.70  E-value: 9.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445  332 GRCLPLPPSLpvCGHLGISRFWLPNHLHHESGEQVRAGARAWGGLLQTHCHPFLAWFFCLLLVPPCGSVPPPAPPPCCQF 411
Cdd:cd07454     3 GKCIPIDIEL--CKDLPYNYTYFPNTILHNDQHTLQTHTEHFKPLMKTKCHPHIHFFICSVFAPMCPIGMPQAVTSCKSV 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 206597445  412 CEALQDACWSRLG--GGRLP--VACASLPTQED 440
Cdd:cd07454    81 CEQVKADCFSILEefGIGWPepLNCAQFPDPPE 113
CRD_FZ8 cd07461
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 8 (Fz8) receptor; The cysteine-rich ...
 340-444 1.56e-05

Cysteine-rich Wnt-binding domain (CRD) of the frizzled 8 (Fz8) receptor; The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 8 (Fz8) 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. Xenopus Fz8 is important in Wnt/beta-catenin signaling pathways controlling the transcriptional activation of target genes Siamois and Xnr3 in the animal caps of late blastula.


Pssm-ID: 143570  Cd Length: 125  Bit Score: 46.13  E-value: 1.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445  340 SLPVCGHLGISRFWLPNHLHHESGEQVRAGARAWGGLLQTHCHPFLAWFFCLLLVPPCGSVPPPAPPPCCQFCEALQDAC 419
Cdd:cd07461     9 TVPLCKGIGYNYTYMPNQFNHDTQDEAGLEVHQFWPLVEIQCSPDLKFFLCSMYTPICLEDYKKPLPPCRSVCERAKAGC 88

                          90       100       110
                  ....*....|....*....|....*....|.
gi 206597445  420 --WSRLGGGRLP--VACASLPTQ--EDGYCV 444
Cdd:cd07461    89 apLMRQYGFPWPdrMRCDLLPEQgnPDTLCM 119
CRD_FZ5 cd07460
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 5 (Fz5) receptor.proteins; The ...
 340-430 1.91e-05

Cysteine-rich Wnt-binding domain (CRD) of the frizzled 5 (Fz5) receptor.proteins; The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 5 (Fz5) 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. Fz5 plays critical regulating roles in the yolk sac and placental angiogenesis, in the maturation of the Paneth cell phenotype, in governing the neural potential of progenitors in the developing retina, and in neuronal survival in the parafascicular nucleus.


Pssm-ID: 143569 [Multi-domain]  Cd Length: 127  Bit Score: 45.78  E-value: 1.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445  340 SLPVCGHLGISRFWLPNHLHHESGEQVRAGARAWGGLLQTHCHPFLAWFFCLLLVPPCGSVPPPAPPPCCQFCEALQDAC 419
Cdd:cd07460     9 TVPMCKGIGYNLTYMPNQFNHDTQDEAGLEVHQFWPLVEIQCSPDLRFFLCSMYTPICLPDYRKPLPPCRSVCERAKAGC 88

                          90       100
                  ....*....|....*....|..
gi 206597445  420 ----------W-SRLGGGRLPV 430
Cdd:cd07460    89 splmrqygfaWpERMNCDRLPV 110
Laminin_G_3 pfam13385
Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin ...
 488-640 4.06e-05

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


Pssm-ID: 463865 [Multi-domain]  Cd Length: 151  Bit Score: 45.45  E-value: 4.06e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445   488 DANSGQVAryhFPSLFF--RDFSLLFHIRP-ATEGPGVLFAITDSAQAMVLlgvklsGVQDGHQDISLLYTEPGAGQTHT 564
Cdd:pfam13385    1 DGGSDYVT---LPDALLptSDFTVSAWVKPdSLPGWARAIISSSGGGGYSL------GLDGDGRLRFAVNGGNGGWDTVT 71

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 206597445   565 AASfrlPAFVGQWTHLALSVAGGFVALYVDCEEFQRmplaRSSRGLELEPGAGLFV--AQAGGADPdkFQGVIAELKV 640
Cdd:pfam13385   72 SGA---SVPLGQWTHVAVTYDGGTLRLYVNGVLVGS----STLTGGPPPGTGGPLYigRSPGGDDY--FNGLIDEVRI 140
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1141-1181 5.35e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.48  E-value: 5.35e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 206597445  1141 PGPEGRPGFAGFPGPAGPKGNLGSKGERGSPGPKGEKGEPG 1181
Cdd:pfam01391    6 PGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPG 46
CRD_FZ5_like cd07456
Cysteine-rich Wnt-binding domain (CRD) of receptors similar to frizzled 5; The cysteine-rich ...
 333-440 7.21e-05

Cysteine-rich Wnt-binding domain (CRD) of receptors similar to frizzled 5; The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 5 (Fz5) and frizzled 8 (Fz8) 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: 143565  Cd Length: 120  Bit Score: 43.93  E-value: 7.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445  333 RCLPLppSLPVCGHLGISRFWLPNHLHHESGEQVRAGARAWGGLLQTHCHPFLAWFFCLLLVPPCGSVPPPAPPPCCQFC 412
Cdd:cd07456     1 KCEEI--TIPMCKGIGYNMTYMPNQFNHDTQEEAGLEVHQFWPLVEIQCSPDLKFFLCSMYTPICLEDYDKPLPPCRSVC 78

                          90       100       110
                  ....*....|....*....|....*....|..
gi 206597445  413 EALQDACWS--RLGGGRLP--VACASLPTQED 440
Cdd:cd07456    79 ERARDGCAPimRQYGFAWPerMSCDALPEGGD 110
PHA03247 PHA03247
large tegument protein UL36; Provisional
 156-345 7.61e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.01  E-value: 7.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445  156 GPSSTPQENGTTLWPSRGIPSSPGAHTTEAGTLPAPTPSPPSlgrpwaplTGPSVPPPSSGRASLSSLLGGAPPWGSLQD 235
Cdd:PHA03247 2579 EPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPD--------THAPDPPPPSPSPAANEPDPHPPPTVPPPE 2650

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445  236 PDSQGLSPAAAAPSQQLQR---------PDVRLRTPLLHPLVmGSLGKHA-----------APSAFSSGLPGALSQVAVt 295
Cdd:PHA03247 2651 RPRDDPAPGRVSRPRRARRlgraaqassPPQRPRRRAARPTV-GSLTSLAdpppppptpepAPHALVSATPLPPGPAAA- 2728

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 206597445  296 tltrdSGAWVSHVANSVGPGLANNSALLGAD-----PEAPAGRCLPLPPSLPVCG 345
Cdd:PHA03247 2729 -----RQASPALPAAPAPPAVPAGPATPGGParparPPTTAGPPAPAPPAAPAAG 2778
CRD_FZ7 cd07466
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 7 (Fz7) receptor; The cysteine-rich ...
 332-419 1.66e-04

Cysteine-rich Wnt-binding domain (CRD) of the frizzled 7 (Fz7) receptor; The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 7 (Fz7) 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. Xenopus Fz7 is important in Wnt/beta-catenin signaling pathways controlling the transcriptional activation of target genes Siamois and Xnr3 in the animal caps of late blastula.


Pssm-ID: 143575 [Multi-domain]  Cd Length: 125  Bit Score: 43.15  E-value: 1.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445  332 GRCLPLppSLPVCGHLGISRFWLPNHLHHESGEQVRAGARAWGGLLQTHCHPFLAWFFCLLLVPPCgSVPPPAPPPCCQF 411
Cdd:cd07466     3 GFCQPI--SIPLCTDIAYNQTIMPNLLGHTNQEDAGLEVHQFYPLVKVQCSPELKFFLCSMYAPVC-TVLEQAIPPCRSL 79


                  ....*...
gi 206597445  412 CEALQDAC 419
Cdd:cd07466    80 CERARQGC 87
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 789-995 2.13e-04

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 45.67  E-value: 2.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445  789 PLGPAGPA-LQTVPGPQGPPGPPGRDGTPGRDGEPGDPGEDGKPGDTGPQGFPGTPGDVGPKGDKGDPGVGERGPPGPQG 867
Cdd:NF038329  124 PAGPAGPAgEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPA 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445  868 PPGPPGPSFRHDKLTFIDMEGSGFGGDLEALRGPRGFPGPPGPPGVPGLPGEPGRFGVNSSD-VPGPAGLPGVPGREGPp 946
Cdd:NF038329  204 GEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRgEAGPDGPDGKDGERGP- 282

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 206597445  947 gfPGLPGPPGPPGREGPPGRTGQKGSLGEAGAPGHKGSKGAPGPAGARG 995
Cdd:NF038329  283 --VGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPG 329
CRD_FZ2 cd07464
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 2 (Fz2) receptor; The cysteine-rich ...
 332-419 2.57e-04

Cysteine-rich Wnt-binding domain (CRD) of the frizzled 2 (Fz2) receptor; The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 2 (Fz2) 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. Fz2 is involved in the Wnt/beta-catenin signaling pathway and in the activation of protein kinase C and calcium/calmodulin-dependent protein kinase (CaM kinase).


Pssm-ID: 143573  Cd Length: 127  Bit Score: 42.77  E-value: 2.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445  332 GRCLPLppSLPVCGHLGISRFWLPNHLHHESGEQVRAGARAWGGLLQTHCHPFLAWFFCLLLVPPCgSVPPPAPPPCCQF 411
Cdd:cd07464     3 GFCQPI--SIPLCTDIAYNQTIMPNLLGHTNQEDAGLEVHQFYPLVKVQCSLELRFFLCSMYAPVC-TVLEQAIPPCRSI 79


                  ....*...
gi 206597445  412 CEALQDAC 419
Cdd:cd07464    80 CERARQGC 87
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 38-338 2.68e-04

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 46.06  E-value: 2.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445    38 TSHAATTIPEPQGPLPVQPTADTTThvtPRNGSTEPATAPGSPEPPSelledgQDTPTSAESPDAPEENIAgVGAEILNV 117
Cdd:pfam05109  451 STHVPTNLTAPASTGPTVSTADVTS---PTPAGTTSGASPVTPSPSP------RDNGTESKAPDMTSPTSA-VTTPTPNA 520

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445   118 AKGIRSFvqlwndTVPTESlARAETLVLETPVGPLALAGPSST-PQENGTTLWPSRGIPSSPGAHTTEAGTLPAPTPSPP 196
Cdd:pfam05109  521 TSPTPAV------TTPTPN-ATSPTLGKTSPTSAVTTPTPNATsPTPAVTTPTPNATIPTLGKTSPTSAVTTPTPNATSP 593

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445   197 SLGR--PWAPLTG------PSVP----PPSSGRASLSS----LLGGAPPWGSLQDPD-SQGLSPAAAAPSQQlqrpdvrl 259
Cdd:pfam05109  594 TVGEtsPQANTTNhtlggtSSTPvvtsPPKNATSAVTTgqhnITSSSTSSMSLRPSSiSETLSPSTSDNSTS-------- 665

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445   260 RTPLL---HP--------LVMGSLGKHAAPSAFSSGLPGALSQVavttltrdSGAwvSHVANSVGPGLANNSALL----G 324
Cdd:pfam05109  666 HMPLLtsaHPtggenitqVTPASTSTHHVSTSSPAPRPGTTSQA--------SGP--GNSSTSTKPGEVNVTKGTppknA 735

                          330
                   ....*....|....
gi 206597445   325 ADPEAPAGRCLPLP 338
Cdd:pfam05109  736 TSPQAPSGQKTAVP 749
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 492-640 2.85e-04

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: 43.18  E-value: 2.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445  492 GQVARYHFPSLFFRDFSLLFHIRPaTEGPGVLFAITDSAQAMVLLgVKLSgvqDGHqdISLLYtEPGAGQThtaaSFRLP 571
Cdd:cd00110     7 SSYVRLPTLPAPRTRLSISFSFRT-TSPNGLLLYAGSQNGGDFLA-LELE---DGR--LVLRY-DLGSGSL----VLSSK 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445  572 AFV--GQWTHLALSVAGGFVALYVDCEEFQRMPLARSSRGLELEpgAGLFVaqaGGADPDK----------FQGVIAELK 639
Cdd:cd00110    75 TPLndGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLD--GPLYL---GGLPEDLkspglpvspgFVGCIRDLK 149


                  .
gi 206597445  640 V 640
Cdd:cd00110   150 V 150
LamG smart00282
Laminin G domain;
508-640 4.11e-04

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 41.94  E-value: 4.11e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445    508 SLLFHIRPaTEGPGVLFAITDSAQAMVLlGVKLSgvqDGHqdISLLYTEPGagqthTAASFRLPAFV---GQWTHLALSV 584
Cdd:smart00282    1 SISFSFRT-TSPNGLLLYAGSKGGGDYL-ALELR---DGR--LVLRYDLGS-----GPARLTSDPTPlndGQWHRVAVER 68

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 206597445    585 AGGFVALYVDCEEFQRMPLARSSRGLELEpgAGLFVaqaGGADPDK----------FQGVIAELKV 640
Cdd:smart00282   69 NGRSVTLSVDGGNRVSGESPGGLTILNLD--GPLYL---GGLPEDLklpplpvtpgFRGCIRNLKV 129
PHA03247 PHA03247
large tegument protein UL36; Provisional
 44-342 8.27e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.54  E-value: 8.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445   44 TIPEPQ-GPLPVQPTA-----------DTTTHVTPRNGSTEP-ATAPGSPEPPSElleDGQDTPTSAESPDAPEENIAGV 110
Cdd:PHA03247 2567 SVPPPRpAPRPSEPAVtsrarrpdappQSARPRAPVDDRGDPrGPAPPSPLPPDT---HAPDPPPPSPSPAANEPDPHPP 2643

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445  111 GAEILNVAKGIRSFVQLWNDTVPTESLARAetlvletpvgplalAGPSSTPQEngttlWPSRGIPSSPGAHTTEAGTlPA 190
Cdd:PHA03247 2644 PTVPPPERPRDDPAPGRVSRPRRARRLGRA--------------AQASSPPQR-----PRRRAARPTVGSLTSLADP-PP 2703

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445  191 PTPSPPSLGRPWAPLTGPSVPPPSSGRASLSSLLGGAPPwgslqdpdsqglsPAAAAPSQqlqrpDVRLRTPLLHPLVMG 270
Cdd:PHA03247 2704 PPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPP-------------AVPAGPAT-----PGGPARPARPPTTAG 2765

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 206597445  271 SlGKHAAPSAFSSGLPGALSQVAVTTLTRDSGAWVS------HVANSVGPGLANNSALLGADPEAPAGRCLPLPPSLP 342
Cdd:PHA03247 2766 P-PAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSpwdpadPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPP 2842
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 819-856 9.82e-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: 39.01  E-value: 9.82e-04
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 206597445   819 DGEPGDPGEDGKPGDTGPQGFPGTPGDVGPKGDKGDPG 856
Cdd:pfam01391   12 PGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPG 49
CRD_FZ1 cd07465
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 1 (Fz1) receptor; The cysteine-rich ...
 332-419 1.59e-03

Cysteine-rich Wnt-binding domain (CRD) of the frizzled 1 (Fz1) receptor; The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 1 (Fz1) 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.


Pssm-ID: 143574  Cd Length: 127  Bit Score: 40.42  E-value: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445  332 GRCLPLppSLPVCGHLGISRFWLPNHLHHESGEQVRAGARAWGGLLQTHCHPFLAWFFCLLLVPPCgSVPPPAPPPCCQF 411
Cdd:cd07465     3 GYCQPI--SIPLCTDIAYNQTIMPNLLGHTNQEDAGLEVHQFYPLVKVQCSAELKFFLCSMYAPVC-TVLEQALPPCRSL 79


                  ....*...
gi 206597445  412 CEALQDAC 419
Cdd:cd07465    80 CERARQGC 87
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 46-342 2.03e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.05  E-value: 2.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445   46 PEPQGPLPVQPTADTTTHVTPRNGSTEPATAPGSPEPPSELLEDGqdtPTSAESPDAPEENIAGVGA------------- 112
Cdd:PRK07764  439 PAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPA---PPAAPAPAAAPAAPAAPAApagaddaatlrer 515

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445  113 --EILNVAKGIRSFVqlWNDTVPTESLA--RAETLVLETPVGPLA--LAGPSSTP-------QENGTTLWPSRGIPSSPG 179
Cdd:PRK07764  516 wpEILAAVPKRSRKT--WAILLPEATVLgvRGDTLVLGFSTGGLArrFASPGNAEvlvtalaEELGGDWQVEAVVGPAPG 593

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445  180 AHTTEAGTLPAPTPSPPSLGRPWAPlTGPSVPPPSSGraslssllGGAPPWGSLQDPDSQGLSPAAAAPSQQLQRPDVRL 259
Cdd:PRK07764  594 AAGGEGPPAPASSGPPEEAARPAAP-AAPAAPAAPAP--------AGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASD 664

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445  260 RTPLLHPLVMGSLGKHAAPSAFSSGLPGAlsQVAVTTLTRDSGAWVSHVANSVGPGLANNSALLGADPEAPAGRCLPLPP 339
Cdd:PRK07764  665 GGDGWPAKAGGAAPAAPPPAPAPAAPAAP--AGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLP 742


                  ...
gi 206597445  340 SLP 342
Cdd:PRK07764  743 PEP 745
PHA03247 PHA03247
large tegument protein UL36; Provisional
 38-345 2.80e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 2.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445   38 TSHAATTIPEPQGPLPVQPTADTTTHVTPRNGSTEPATAPGSPEPPSELLEDGQDTPTSAESPDAPEENIAGVGAEilNV 117
Cdd:PHA03247 2583 TSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAP--GR 2660

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445  118 AKGIRSFVQLWNDTVPTESLARAETLVLETPVGPLA-LAGPsstpqengttlwPSRGIPSSPGAHTTEAGTLPAPTPSPP 196
Cdd:PHA03247 2661 VSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTsLADP------------PPPPPTPEPAPHALVSATPLPPGPAAA 2728

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445  197 SLGRPWAPLTgPSVPPPSSGRAslssLLGGAPPWGSlqdPDSQGLSPAAAAPSQQLQRPDVRLRTPLLHPLvmgSLGKHA 276
Cdd:PHA03247 2729 RQASPALPAA-PAPPAVPAGPA----TPGGPARPAR---PPTTAGPPAPAPPAAPAAGPPRRLTRPAVASL---SESRES 2797

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 206597445  277 APSAFSSGLPGALSQVAVTTLTrdsgawvshVANSVGPGLANNSALLGADPEAPAGrclPLPPSLPVCG 345
Cdd:PHA03247 2798 LPSPWDPADPPAAVLAPAAALP---------PAASPAGPLPPPTSAQPTAPPPPPG---PPPPSLPLGG 2854
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 713-856 3.69e-03

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: 41.81  E-value: 3.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445  713 EVEEQTTVASLGAQTLPGSDSVSTWDGSVRTPGGRVKEG-----GLKGQKGEPGVPGPPGRAGPPGSPCLPGPPGLPCPV 787
Cdd:NF038329  142 ETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGeagakGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPA 221

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 206597445  788 SPLGPAGPALQTVPGPQGPPGPPGRDGTPGRDGEPGDPGEDGKPGDTGPQGFPGTPGDVGPKGDKGDPG 856
Cdd:NF038329  222 GEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDG 290
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 38-306 3.94e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.08  E-value: 3.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445   38 TSHAATTIPEPQGPLPVQPTADTTTHVTPRNGSTEPATAPGSPEPPSELLEDGQDTPTSAESPDAPEENIAGVGAEILNV 117
Cdd:PHA03307   58 GAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEM 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445  118 AKGIRSFVQLWNDTVPTESLARAEtlVLETPVGPLALAGPSSTPQENGTTlwpsrgiPSSPGAHTTEAGTLPAPTPSPPS 197
Cdd:PHA03307  138 LRPVGSPGPPPAASPPAAGASPAA--VASDAASSRQAALPLSSPEETARA-------PSSPPAEPPPSTPPAAASPRPPR 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445  198 LGRPWAPltGPSVPPPSSGRASLSSLLGGAPPWGSLQDPDSQGlspaaaapsqqlqrpDVRLRTPLLHPLVMGSLGKHAA 277
Cdd:PHA03307  209 RSSPISA--SASSPAPAPGRSAADDAGASSSDSSSSESSGCGW---------------GPENECPLPRPAPITLPTRIWE 271

                         250       260
                  ....*....|....*....|....*....
gi 206597445  278 PSAFSSGLPGALSQVAVTTLTRDSGAWVS 306
Cdd:PHA03307  272 ASGWNGPSSRPGPASSSSSPRERSPSPSP 300
PHA03247 PHA03247
large tegument protein UL36; Provisional
 46-255 5.34e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.85  E-value: 5.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445   46 PEPQGPLPVQPTADTTTHVTPRNGSTEPATAPGSPEPPSELLEDGQD-------TPTSAESPDAPEENIAGVGAEIlnva 118
Cdd:PHA03247 2708 PEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGParparppTTAGPPAPAPPAAPAAGPPRRL---- 2783

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206597445  119 kgirsfvqlwndTVPTESLARAETLVLETPVGPLALAGPSSTPQEN-GTTLWPSRGIPSSPGAHTTEAGTLPAPTPSPPS 197
Cdd:PHA03247 2784 ------------TRPAVASLSESRESLPSPWDPADPPAAVLAPAAAlPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLP 2851

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 206597445  198 LGRPWAPlTGPSVPPPSSGRASLSSLLGGAPPWGSLQDPDSQGLSPAAAAPSQQLQRP 255
Cdd:PHA03247 2852 LGGSVAP-GGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERP 2908
 
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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