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Conserved domains on  [gi|116008152|ref|NP_001846|]
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collagen alpha-1(XV) chain precursor [Homo sapiens]

Protein Classification

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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 ...
 1215-1381 4.54e-112

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: 349.32  E-value: 4.54e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008152 1215 KPALHLAALNMPFSGDIR----ADFQCFKQARAAGLLSTYRAFLSSHLQDLSTIVRKAERYSLPIVNLKGQVLFNNWDSI 1290
Cdd:cd00247     1 QPVLHLVALNTPLSGDMRgirgADFQCFQQARAAGLKGTFRAFLSSRLQDLYSIVRRADRDSLPIVNLKGEVLFNSWESL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008152 1291 FSGHGGQFNMHIPIYSFDGRDIMTDPSWPQKVIWHGSSPHGVRLVDNYCEAWRTADTAVTGLASPLSTGKILDQKAYSCA 1370
Cdd:cd00247    81 FSGSGGQFNPGARIYSFDGRDVLTDPAWPQKMVWHGSDPNGRRLTDSYCEAWRTGDSAVTGQASSLSSGKLLEQKAYSCE 160

                         170
                  ....*....|.
gi 116008152 1371 NRLIVLCIENS 1381
Cdd:cd00247   161 NKLIVLCIENS 171
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 40-228 3.84e-53

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


:

Pssm-ID: 214560  Cd Length: 184  Bit Score: 184.10  E-value: 3.84e-53
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008152     40 HLDLTQLIGVP-LPSSVSFVTGY-GGFPAYSFGPGANVGRPARTLIPSTFFRDFAISVVVKPSSTRGGVLFAITDAfQKV 117
Cdd:smart00210    1 GQDLLQVFDLPsLSFAIRQVVGPePGSPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPKSRGVLFAIYDA-QNV 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008152    118 IYLGLRLsgveDGHQRIILYYTEpGSHVSQEAAAFS-VPVMTHRWNRFAMIVQGEEVTLLVNCEEHSRIPFQRSSQalAF 196
Cdd:smart00210   80 RQFGLEV----DGRANTLLLRYQ-GVDGKQHTVSFRnLPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGQ--PP 152

                           170       180       190
                    ....*....|....*....|....*....|..
gi 116008152    197 ESSAGIFMGNAGATGLERFTGSLQQLTVHPDP 228
Cdd:smart00210  153 IDTDGIEVRGAQAADRKPFQGDLQQLKIVCDP 184
Collagen_trimer pfam20010
Collagen trimerization domain; This small domain mediate trimerization in various collagen ...
 1135-1181 4.54e-21

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


:

Pssm-ID: 466257  Cd Length: 49  Bit Score: 87.66  E-value: 4.54e-21
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 116008152  1135 VTAFSNMDDMLQKAHLVIEGTFIYLRDSTEFFIRVRDGWKKLQLGEL 1181
Cdd:pfam20010    1 VTVFQNYDTMLQKTHRVPEGTLVYVREREELYIRVRNGWRKIQLGEL 47
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 838-1043 8.20e-10

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: 62.62  E-value: 8.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008152  838 GPRGPKGDTGLPGFPGLKGEQGEKGEPGAILTEDIPLERlmGKKGEPGMHGAPGPMGPKGPPGHKGEFGLPGRPGRPGLN 917
Cdd:NF038329  144 GPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEA--GAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPA 221

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008152  918 GLKGTKGDPGVIMQGPPGLPGPPGPPGPPGavinikgaifpiPVRPHCKMPVDtAHPGSPELITFHGVKGEKGSWGLPGS 997
Cdd:NF038329  222 GEDGPAGPAGDGQQGPDGDPGPTGEDGPQG------------PDGPAGKDGPR-GDRGEAGPDGPDGKDGERGPVGPAGK 288

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 116008152  998 KGEKGDQGAQGPPGPpldlaylrhflnnlKGENGDKGFKGEKGEKG 1043
Cdd:NF038329  289 DGQNGKDGLPGKDGK--------------DGQNGKDGLPGKDGKDG 320
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 624-927 1.77e-09

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: 61.84  E-value: 1.77e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008152  624 PgppglpgipgkpgtdvfmGPPGSPGEDGPAGEPGPPGPEGQPGVDGATGLPGMKGEKGARGPNGSVGEKGDPGNRGLPG 703
Cdd:NF038329  125 A------------------GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKG 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008152  704 PPGKKGQAGPPGVMGPPgppgppgppgpgctmglGFEDTEGSGSTQLLNEPKLSRPTAAIGLKGEKGDRGPKGERGMDGA 783
Cdd:NF038329  187 PAGEKGPQGPRGETGPA-----------------GEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGP 249

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008152  784 SivgppgprgppghikvlsnslinithgfmnfsdipelvgppgpdglpGLPGFPGPRGPKGDTGLPGFPGLKGEQGEKGE 863
Cdd:NF038329  250 Q-----------------------------------------------GPDGPAGKDGPRGDRGEAGPDGPDGKDGERGP 282

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 116008152  864 PGailtediplerLMGKKGEpgmhgapgpmgpkgppghKGEFGLPGRPGRPGLNGLKGTKGDPG 927
Cdd:NF038329  283 VG-----------PAGKDGQ------------------NGKDGLPGKDGKDGQNGKDGLPGKDG 317
 
Name Accession Description Interval E-value
Endostatin-like cd00247
Endostatin-like domain; the angiogenesis inhibitor endostatin is a C-terminal fragment of ...
 1215-1381 4.54e-112

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: 349.32  E-value: 4.54e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008152 1215 KPALHLAALNMPFSGDIR----ADFQCFKQARAAGLLSTYRAFLSSHLQDLSTIVRKAERYSLPIVNLKGQVLFNNWDSI 1290
Cdd:cd00247     1 QPVLHLVALNTPLSGDMRgirgADFQCFQQARAAGLKGTFRAFLSSRLQDLYSIVRRADRDSLPIVNLKGEVLFNSWESL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008152 1291 FSGHGGQFNMHIPIYSFDGRDIMTDPSWPQKVIWHGSSPHGVRLVDNYCEAWRTADTAVTGLASPLSTGKILDQKAYSCA 1370
Cdd:cd00247    81 FSGSGGQFNPGARIYSFDGRDVLTDPAWPQKMVWHGSDPNGRRLTDSYCEAWRTGDSAVTGQASSLSSGKLLEQKAYSCE 160

                         170
                  ....*....|.
gi 116008152 1371 NRLIVLCIENS 1381
Cdd:cd00247   161 NKLIVLCIENS 171
Endostatin pfam06482
Collagenase NC10 and Endostatin; NC10 stands for Non-helical region 10 and is taken from Swiss: ...
 1218-1382 1.07e-107

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: 337.49  E-value: 1.07e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008152  1218 LHLAALNMPFSGDIR----ADFQCFKQARAAGLLSTYRAFLSSHLQDLSTIVRKAERYSLPIVNLKGQVLFNNWDSIFSG 1293
Cdd:pfam06482    1 LHLIALNTPQSGDMRgirgADFLCFQQARAAGLKGTFRAFLSSRLQDLYSIVRKADRENVPIVNLKDEVLFDSWESIFSG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008152  1294 HGGQFNMHIPIYSFDGRDIMTDPSWPQKVIWHGSSPHGVRLVDNYCEAWRTADTAVTGLASPLSTGKILDQKAYSCANRL 1373
Cdd:pfam06482   81 SGGQMKPNVPIYSFDGRDVLRDPAWPQKMVWHGSTSKGHRLTDNYCEAWRTGDQAVTGQASSLQSGKLLQQSPSSCSNSY 160


                   ....*....
gi 116008152  1374 IVLCIENSF 1382
Cdd:pfam06482  161 IVLCIENSY 169
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 40-228 3.84e-53

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


Pssm-ID: 214560  Cd Length: 184  Bit Score: 184.10  E-value: 3.84e-53
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008152     40 HLDLTQLIGVP-LPSSVSFVTGY-GGFPAYSFGPGANVGRPARTLIPSTFFRDFAISVVVKPSSTRGGVLFAITDAfQKV 117
Cdd:smart00210    1 GQDLLQVFDLPsLSFAIRQVVGPePGSPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPKSRGVLFAIYDA-QNV 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008152    118 IYLGLRLsgveDGHQRIILYYTEpGSHVSQEAAAFS-VPVMTHRWNRFAMIVQGEEVTLLVNCEEHSRIPFQRSSQalAF 196
Cdd:smart00210   80 RQFGLEV----DGRANTLLLRYQ-GVDGKQHTVSFRnLPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGQ--PP 152

                           170       180       190
                    ....*....|....*....|....*....|..
gi 116008152    197 ESSAGIFMGNAGATGLERFTGSLQQLTVHPDP 228
Cdd:smart00210  153 IDTDGIEVRGAQAADRKPFQGDLQQLKIVCDP 184
Collagen_trimer pfam20010
Collagen trimerization domain; This small domain mediate trimerization in various collagen ...
 1135-1181 4.54e-21

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


Pssm-ID: 466257  Cd Length: 49  Bit Score: 87.66  E-value: 4.54e-21
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 116008152  1135 VTAFSNMDDMLQKAHLVIEGTFIYLRDSTEFFIRVRDGWKKLQLGEL 1181
Cdd:pfam20010    1 VTVFQNYDTMLQKTHRVPEGTLVYVREREELYIRVRNGWRKIQLGEL 47
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 838-1043 8.20e-10

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: 62.62  E-value: 8.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008152  838 GPRGPKGDTGLPGFPGLKGEQGEKGEPGAILTEDIPLERlmGKKGEPGMHGAPGPMGPKGPPGHKGEFGLPGRPGRPGLN 917
Cdd:NF038329  144 GPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEA--GAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPA 221

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008152  918 GLKGTKGDPGVIMQGPPGLPGPPGPPGPPGavinikgaifpiPVRPHCKMPVDtAHPGSPELITFHGVKGEKGSWGLPGS 997
Cdd:NF038329  222 GEDGPAGPAGDGQQGPDGDPGPTGEDGPQG------------PDGPAGKDGPR-GDRGEAGPDGPDGKDGERGPVGPAGK 288

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 116008152  998 KGEKGDQGAQGPPGPpldlaylrhflnnlKGENGDKGFKGEKGEKG 1043
Cdd:NF038329  289 DGQNGKDGLPGKDGK--------------DGQNGKDGLPGKDGKDG 320
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 624-927 1.77e-09

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: 61.84  E-value: 1.77e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008152  624 PgppglpgipgkpgtdvfmGPPGSPGEDGPAGEPGPPGPEGQPGVDGATGLPGMKGEKGARGPNGSVGEKGDPGNRGLPG 703
Cdd:NF038329  125 A------------------GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKG 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008152  704 PPGKKGQAGPPGVMGPPgppgppgppgpgctmglGFEDTEGSGSTQLLNEPKLSRPTAAIGLKGEKGDRGPKGERGMDGA 783
Cdd:NF038329  187 PAGEKGPQGPRGETGPA-----------------GEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGP 249

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008152  784 SivgppgprgppghikvlsnslinithgfmnfsdipelvgppgpdglpGLPGFPGPRGPKGDTGLPGFPGLKGEQGEKGE 863
Cdd:NF038329  250 Q-----------------------------------------------GPDGPAGKDGPRGDRGEAGPDGPDGKDGERGP 282

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 116008152  864 PGailtediplerLMGKKGEpgmhgapgpmgpkgppghKGEFGLPGRPGRPGLNGLKGTKGDPG 927
Cdd:NF038329  283 VG-----------PAGKDGQ------------------NGKDGLPGKDGKDGQNGKDGLPGKDG 317
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 556-710 5.24e-09

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: 60.30  E-value: 5.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008152  556 GMKGQAGPKGEKGDAGEELP-GPPEPSGPVGPTAGAEAEGSGLGWGSDVGSGSGDlvgseqllRGPPGPPGPPGLPGIPG 634
Cdd:NF038329  183 GAKGPAGEKGPQGPRGETGPaGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGP--------DGDPGPTGEDGPQGPDG 254

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008152  635 KPGTDVFMGPPGSPGEDGPAGEPGPPGPEGQPGVDGATGLPGMKGEKGARGPNGSVGEKGD------PGNRGLPGPPGKK 708
Cdd:NF038329  255 PAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKdgkdgqPGKDGLPGKDGKD 334


                  ..
gi 116008152  709 GQ 710
Cdd:NF038329  335 GQ 336
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 670-716 1.19e-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: 44.02  E-value: 1.19e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 116008152   670 GATGLPGMKGEKGARGPNGSVGEKGDPGNRGLPGPPGKKGQAGPPGV 716
Cdd:pfam01391    4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGA 50
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 838-927 1.00e-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: 41.33  E-value: 1.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008152   838 GPRGPKGDTGLPGFPGLKGEQGEKGEPgailtediplerlmgkkgepgmhgapgpmgpkgppGHKGEFGLPGRPGRPGLN 917
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPP-----------------------------------GPPGEPGPPGPPGPPGPP 45

                           90
                   ....*....|
gi 116008152   918 GLKGTKGDPG 927
Cdd:pfam01391   46 GPPGAPGAPG 55
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 66-225 1.39e-03

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: 40.86  E-value: 1.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008152   66 AYSFGPGANVgrpaRTLIPSTFFRDFAISVVVKPSSTRGgVLFAITDAFQKViYLGLRLsgvEDGHqrIILYY-TEPGSH 144
Cdd:cd00110     1 GVSFSGSSYV----RLPTLPAPRTRLSISFSFRTTSPNG-LLLYAGSQNGGD-FLALEL---EDGR--LVLRYdLGSGSL 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008152  145 VSQeaaaFSVPVMTHRWNRFAMIVQGEEVTLLVNCEEHSRIPFQRSSQALafESSAGIFMGNA-------GATGLERFTG 217
Cdd:cd00110    70 VLS----SKTPLNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALL--NLDGPLYLGGLpedlkspGLPVSPGFVG 143


                  ....*...
gi 116008152  218 SLQQLTVH 225
Cdd:cd00110   144 CIRDLKVN 151
 
Name Accession Description Interval E-value
Endostatin-like cd00247
Endostatin-like domain; the angiogenesis inhibitor endostatin is a C-terminal fragment of ...
 1215-1381 4.54e-112

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: 349.32  E-value: 4.54e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008152 1215 KPALHLAALNMPFSGDIR----ADFQCFKQARAAGLLSTYRAFLSSHLQDLSTIVRKAERYSLPIVNLKGQVLFNNWDSI 1290
Cdd:cd00247     1 QPVLHLVALNTPLSGDMRgirgADFQCFQQARAAGLKGTFRAFLSSRLQDLYSIVRRADRDSLPIVNLKGEVLFNSWESL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008152 1291 FSGHGGQFNMHIPIYSFDGRDIMTDPSWPQKVIWHGSSPHGVRLVDNYCEAWRTADTAVTGLASPLSTGKILDQKAYSCA 1370
Cdd:cd00247    81 FSGSGGQFNPGARIYSFDGRDVLTDPAWPQKMVWHGSDPNGRRLTDSYCEAWRTGDSAVTGQASSLSSGKLLEQKAYSCE 160

                         170
                  ....*....|.
gi 116008152 1371 NRLIVLCIENS 1381
Cdd:cd00247   161 NKLIVLCIENS 171
Endostatin pfam06482
Collagenase NC10 and Endostatin; NC10 stands for Non-helical region 10 and is taken from Swiss: ...
 1218-1382 1.07e-107

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: 337.49  E-value: 1.07e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008152  1218 LHLAALNMPFSGDIR----ADFQCFKQARAAGLLSTYRAFLSSHLQDLSTIVRKAERYSLPIVNLKGQVLFNNWDSIFSG 1293
Cdd:pfam06482    1 LHLIALNTPQSGDMRgirgADFLCFQQARAAGLKGTFRAFLSSRLQDLYSIVRKADRENVPIVNLKDEVLFDSWESIFSG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008152  1294 HGGQFNMHIPIYSFDGRDIMTDPSWPQKVIWHGSSPHGVRLVDNYCEAWRTADTAVTGLASPLSTGKILDQKAYSCANRL 1373
Cdd:pfam06482   81 SGGQMKPNVPIYSFDGRDVLRDPAWPQKMVWHGSTSKGHRLTDNYCEAWRTGDQAVTGQASSLQSGKLLQQSPSSCSNSY 160


                   ....*....
gi 116008152  1374 IVLCIENSF 1382
Cdd:pfam06482  161 IVLCIENSY 169
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 40-228 3.84e-53

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


Pssm-ID: 214560  Cd Length: 184  Bit Score: 184.10  E-value: 3.84e-53
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008152     40 HLDLTQLIGVP-LPSSVSFVTGY-GGFPAYSFGPGANVGRPARTLIPSTFFRDFAISVVVKPSSTRGGVLFAITDAfQKV 117
Cdd:smart00210    1 GQDLLQVFDLPsLSFAIRQVVGPePGSPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPKSRGVLFAIYDA-QNV 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008152    118 IYLGLRLsgveDGHQRIILYYTEpGSHVSQEAAAFS-VPVMTHRWNRFAMIVQGEEVTLLVNCEEHSRIPFQRSSQalAF 196
Cdd:smart00210   80 RQFGLEV----DGRANTLLLRYQ-GVDGKQHTVSFRnLPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGQ--PP 152

                           170       180       190
                    ....*....|....*....|....*....|..
gi 116008152    197 ESSAGIFMGNAGATGLERFTGSLQQLTVHPDP 228
Cdd:smart00210  153 IDTDGIEVRGAQAADRKPFQGDLQQLKIVCDP 184
Collagen_trimer pfam20010
Collagen trimerization domain; This small domain mediate trimerization in various collagen ...
 1135-1181 4.54e-21

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


Pssm-ID: 466257  Cd Length: 49  Bit Score: 87.66  E-value: 4.54e-21
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 116008152  1135 VTAFSNMDDMLQKAHLVIEGTFIYLRDSTEFFIRVRDGWKKLQLGEL 1181
Cdd:pfam20010    1 VTVFQNYDTMLQKTHRVPEGTLVYVREREELYIRVRNGWRKIQLGEL 47
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 838-1043 8.20e-10

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: 62.62  E-value: 8.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008152  838 GPRGPKGDTGLPGFPGLKGEQGEKGEPGAILTEDIPLERlmGKKGEPGMHGAPGPMGPKGPPGHKGEFGLPGRPGRPGLN 917
Cdd:NF038329  144 GPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEA--GAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPA 221

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008152  918 GLKGTKGDPGVIMQGPPGLPGPPGPPGPPGavinikgaifpiPVRPHCKMPVDtAHPGSPELITFHGVKGEKGSWGLPGS 997
Cdd:NF038329  222 GEDGPAGPAGDGQQGPDGDPGPTGEDGPQG------------PDGPAGKDGPR-GDRGEAGPDGPDGKDGERGPVGPAGK 288

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 116008152  998 KGEKGDQGAQGPPGPpldlaylrhflnnlKGENGDKGFKGEKGEKG 1043
Cdd:NF038329  289 DGQNGKDGLPGKDGK--------------DGQNGKDGLPGKDGKDG 320
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 624-927 1.77e-09

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: 61.84  E-value: 1.77e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008152  624 PgppglpgipgkpgtdvfmGPPGSPGEDGPAGEPGPPGPEGQPGVDGATGLPGMKGEKGARGPNGSVGEKGDPGNRGLPG 703
Cdd:NF038329  125 A------------------GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKG 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008152  704 PPGKKGQAGPPGVMGPPgppgppgppgpgctmglGFEDTEGSGSTQLLNEPKLSRPTAAIGLKGEKGDRGPKGERGMDGA 783
Cdd:NF038329  187 PAGEKGPQGPRGETGPA-----------------GEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGP 249

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008152  784 SivgppgprgppghikvlsnslinithgfmnfsdipelvgppgpdglpGLPGFPGPRGPKGDTGLPGFPGLKGEQGEKGE 863
Cdd:NF038329  250 Q-----------------------------------------------GPDGPAGKDGPRGDRGEAGPDGPDGKDGERGP 282

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 116008152  864 PGailtediplerLMGKKGEpgmhgapgpmgpkgppghKGEFGLPGRPGRPGLNGLKGTKGDPG 927
Cdd:NF038329  283 VG-----------PAGKDGQ------------------NGKDGLPGKDGKDGQNGKDGLPGKDG 317
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 556-710 5.24e-09

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: 60.30  E-value: 5.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008152  556 GMKGQAGPKGEKGDAGEELP-GPPEPSGPVGPTAGAEAEGSGLGWGSDVGSGSGDlvgseqllRGPPGPPGPPGLPGIPG 634
Cdd:NF038329  183 GAKGPAGEKGPQGPRGETGPaGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGP--------DGDPGPTGEDGPQGPDG 254

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008152  635 KPGTDVFMGPPGSPGEDGPAGEPGPPGPEGQPGVDGATGLPGMKGEKGARGPNGSVGEKGD------PGNRGLPGPPGKK 708
Cdd:NF038329  255 PAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKdgkdgqPGKDGLPGKDGKD 334


                  ..
gi 116008152  709 GQ 710
Cdd:NF038329  335 GQ 336
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 670-716 1.19e-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: 44.02  E-value: 1.19e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 116008152   670 GATGLPGMKGEKGARGPNGSVGEKGDPGNRGLPGPPGKKGQAGPPGV 716
Cdd:pfam01391    4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGA 50
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 838-927 1.00e-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: 41.33  E-value: 1.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008152   838 GPRGPKGDTGLPGFPGLKGEQGEKGEPgailtediplerlmgkkgepgmhgapgpmgpkgppGHKGEFGLPGRPGRPGLN 917
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPP-----------------------------------GPPGEPGPPGPPGPPGPP 45

                           90
                   ....*....|
gi 116008152   918 GLKGTKGDPG 927
Cdd:pfam01391   46 GPPGAPGAPG 55
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 66-225 1.39e-03

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: 40.86  E-value: 1.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008152   66 AYSFGPGANVgrpaRTLIPSTFFRDFAISVVVKPSSTRGgVLFAITDAFQKViYLGLRLsgvEDGHqrIILYY-TEPGSH 144
Cdd:cd00110     1 GVSFSGSSYV----RLPTLPAPRTRLSISFSFRTTSPNG-LLLYAGSQNGGD-FLALEL---EDGR--LVLRYdLGSGSL 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008152  145 VSQeaaaFSVPVMTHRWNRFAMIVQGEEVTLLVNCEEHSRIPFQRSSQALafESSAGIFMGNA-------GATGLERFTG 217
Cdd:cd00110    70 VLS----SKTPLNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALL--NLDGPLYLGGLpedlkspGLPVSPGFVG 143


                  ....*...
gi 116008152  218 SLQQLTVH 225
Cdd:cd00110   144 CIRDLKVN 151
LamG smart00282
Laminin G domain;
93-225 2.42e-03

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 39.63  E-value: 2.42e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008152     93 ISVVVKPSSTRGgVLFAITDAfQKVIYLGLRLsgvEDGHqrIILYYTEpGSHVSQEAAAfSVPVMTHRWNRFAMIVQGEE 172
Cdd:smart00282    2 ISFSFRTTSPNG-LLLYAGSK-GGGDYLALEL---RDGR--LVLRYDL-GSGPARLTSD-PTPLNDGQWHRVAVERNGRS 72

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008152    173 VTLLVNCEEHSRIPFQRSSQALafESSAGIFMGNAGATGLER-------FTGSLQQLTVH 225
Cdd:smart00282   73 VTLSVDGGNRVSGESPGGLTIL--NLDGPLYLGGLPEDLKLPplpvtpgFRGCIRNLKVN 130
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 837-866 2.85e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 37.09  E-value: 2.85e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 116008152   837 PGPRGPKGDTGLPGFPGLKGEQGEKGEPGA 866
Cdd:pfam01391   27 PGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 836-866 5.51e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 36.32  E-value: 5.51e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 116008152   836 FPGPRGPKGDTGLPGFPGLKGEQGEKGEPGA 866
Cdd:pfam01391   23 PPGPPGPPGEPGPPGPPGPPGPPGPPGAPGA 53
 
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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