NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|386770700|ref|NP_001246651|]
View 

multiplexin, isoform R [Drosophila melanogaster]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 831-999 3.00e-106

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: 328.14  E-value: 3.00e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770700  831 RMLRVAALNEPSTGDLQGIRGADFACYRQGRRAGLLGTFKAFLSSRVQNLDTIVRPADRD-LPVVNTRGDVLFNSWKGIF 909
Cdd:cd00247     2 PVLHLVALNTPLSGDMRGIRGADFQCFQQARAAGLKGTFRAFLSSRLQDLYSIVRRADRDsLPIVNLKGEVLFNSWESLF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770700  910 NGQGGFFSQAPRIYSFSGKNVMTDSTWPMKMVWHGSLPNGERSMDTYCDAWHSGDHLKGSFASNLDGHKLLEQKRQSCDS 989
Cdd:cd00247    82 SGSGGQFNPGARIYSFDGRDVLTDPAWPQKMVWHGSDPNGRRLTDSYCEAWRTGDSAVTGQASSLSSGKLLEQKAYSCEN 161

                         170
                  ....*....|
gi 386770700  990 KLIILCVEAL 999
Cdd:cd00247   162 KLIVLCIENS 171
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 379-616 1.51e-25

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


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 111.15  E-value: 1.51e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770700  379 RGAPGTPGKDGKPGTPGHTGATGVPGARGARGSEGAQGLKGEPGVDGLpgvmgppgppgppglpenydeslmVNSMGAFR 458
Cdd:NF038329  122 PGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGE------------------------AGPQGPAG 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770700  459 GTTQPGAKGVPGEKGDAGQKGERGDPGHKGAHGPSGAKGEPGEPGTPGLPGLPGQVGQ----PGGLDGLASANGtkgekg 534
Cdd:NF038329  178 KDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQgpdgDPGPTGEDGPQG------ 251

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770700  535 ekgekgmrgrrggtgatgPIGPPGKPGPMGDIGHSGRPGMTGPKGEMGPKGPKGDSG--GREGLKGDKGDRGQDGRDGLP 612
Cdd:NF038329  252 ------------------PDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGqnGKDGLPGKDGKDGQNGKDGLP 313


                  ....
gi 386770700  613 GPPG 616
Cdd:NF038329  314 GKDG 317
Collagen_trimer pfam20010
Collagen trimerization domain; This small domain mediate trimerization in various collagen ...
 744-792 6.52e-18

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


:

Pssm-ID: 466257  Cd Length: 49  Bit Score: 78.03  E-value: 6.52e-18
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 386770700   744 AVTFQNIDEMTKKSALNPPGTLAYITEEEALLVRVNKGWQYIALGTLVP 792
Cdd:pfam20010    1 VTVFQNYDTMLQKTHRVPEGTLVYVREREELYIRVRNGWRKIQLGELIP 49
LamG super family cl22861
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 58-222 2.52e-14

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.


The actual alignment was detected with superfamily member smart00210:

Pssm-ID: 473984  Cd Length: 184  Bit Score: 72.39  E-value: 2.52e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770700     58 AEDGFPAFRFLQTADVKSPYRMLLPEKL-YEFAILITFRQSSLKGGYLFSVVNPlDTVVQLGVhlspVVKNSYNVSLVYT 136
Cdd:smart00210   23 PEPGSPAYRLGDPALVPQPTRDLFPSGLpEDFSLLTTFRQTPKSRGVLFAIYDA-QNVRQFGL----EVDGRANTLLLRY 97

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770700    137 QADQniGR-KLASFGVAHVPD-KWNSIALQVLSDKVSFYYDCELRnTTLVTREPIELVFDSAS-TLYIGQAGSiiGGKFE 213
Cdd:smart00210   98 QGVD--GKqHTVSFRNLPLADgQWHKLALSVSGSSATLYVDCNEI-DSRPLDRPGQPPIDTDGiEVRGAQAAD--RKPFQ 172


                    ....*....
gi 386770700    214 GYLEKINVY 222
Cdd:smart00210  173 GDLQQLKIV 181
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 292-421 4.35e-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: 44.13  E-value: 4.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770700  292 PPGQTQYTHERPYRGIKGEKGERGPKGDSIRGPPGPPGPPGPKGETAPYPPFVETTSAGAK----YTGECTCNASDiLEA 367
Cdd:NF038329  202 PAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRgdrgEAGPDGPDGKD-GER 280

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770700  368 IKDNESLRESLRGAPGTPGKDG------KPGTPGHTGATGVPGARGARGSEGAQGLKGEP 421
Cdd:NF038329  281 GPVGPAGKDGQNGKDGLPGKDGkdgqngKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
 
Name Accession Description Interval E-value
Endostatin-like cd00247
Endostatin-like domain; the angiogenesis inhibitor endostatin is a C-terminal fragment of ...
 831-999 3.00e-106

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: 328.14  E-value: 3.00e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770700  831 RMLRVAALNEPSTGDLQGIRGADFACYRQGRRAGLLGTFKAFLSSRVQNLDTIVRPADRD-LPVVNTRGDVLFNSWKGIF 909
Cdd:cd00247     2 PVLHLVALNTPLSGDMRGIRGADFQCFQQARAAGLKGTFRAFLSSRLQDLYSIVRRADRDsLPIVNLKGEVLFNSWESLF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770700  910 NGQGGFFSQAPRIYSFSGKNVMTDSTWPMKMVWHGSLPNGERSMDTYCDAWHSGDHLKGSFASNLDGHKLLEQKRQSCDS 989
Cdd:cd00247    82 SGSGGQFNPGARIYSFDGRDVLTDPAWPQKMVWHGSDPNGRRLTDSYCEAWRTGDSAVTGQASSLSSGKLLEQKAYSCEN 161

                         170
                  ....*....|
gi 386770700  990 KLIILCVEAL 999
Cdd:cd00247   162 KLIVLCIENS 171
Endostatin pfam06482
Collagenase NC10 and Endostatin; NC10 stands for Non-helical region 10 and is taken from Swiss: ...
 833-997 8.45e-75

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: 243.50  E-value: 8.45e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770700   833 LRVAALNEPSTGDLQGIRGADFACYRQGRRAGLLGTFKAFLSSRVQNLDTIVRPADRD-LPVVNTRGDVLFNSWKGIFNG 911
Cdd:pfam06482    1 LHLIALNTPQSGDMRGIRGADFLCFQQARAAGLKGTFRAFLSSRLQDLYSIVRKADREnVPIVNLKDEVLFDSWESIFSG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770700   912 QGGFFSQAPRIYSFSGKNVMTDSTWPMKMVWHGSLPNGERSMDTYCDAWHSGDHLKGSFASNLDGHKLLEQKRQSCDSKL 991
Cdd:pfam06482   81 SGGQMKPNVPIYSFDGRDVLRDPAWPQKMVWHGSTSKGHRLTDNYCEAWRTGDQAVTGQASSLQSGKLLQQSPSSCSNSY 160


                   ....*.
gi 386770700   992 IILCVE 997
Cdd:pfam06482  161 IVLCIE 166
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 379-616 1.51e-25

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 111.15  E-value: 1.51e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770700  379 RGAPGTPGKDGKPGTPGHTGATGVPGARGARGSEGAQGLKGEPGVDGLpgvmgppgppgppglpenydeslmVNSMGAFR 458
Cdd:NF038329  122 PGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGE------------------------AGPQGPAG 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770700  459 GTTQPGAKGVPGEKGDAGQKGERGDPGHKGAHGPSGAKGEPGEPGTPGLPGLPGQVGQ----PGGLDGLASANGtkgekg 534
Cdd:NF038329  178 KDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQgpdgDPGPTGEDGPQG------ 251

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770700  535 ekgekgmrgrrggtgatgPIGPPGKPGPMGDIGHSGRPGMTGPKGEMGPKGPKGDSG--GREGLKGDKGDRGQDGRDGLP 612
Cdd:NF038329  252 ------------------PDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGqnGKDGLPGKDGKDGQNGKDGLP 313


                  ....
gi 386770700  613 GPPG 616
Cdd:NF038329  314 GKDG 317
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 309-616 6.48e-24

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: 106.14  E-value: 6.48e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770700  309 GEKGERGPKgdsirgppgppGPPGPKGETAPYPPFVETTSAGAKYTGECTCNASDILEAIKDNEslreslRGAPGTPGKD 388
Cdd:NF038329  117 GEKGEPGPA-----------GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGE------AGPQGPAGKD 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770700  389 GKPGTPGHTGATGVPGARGARGSEGAQGLKGEPGVDGlpgvmgppgppgppglpenydeslmvnsmgafrgttQPGAKGV 468
Cdd:NF038329  180 GEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDG------------------------------------EAGPAGE 223

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770700  469 PGEKGDAG--QKGERGDPGHKGAHGPSGAKGEPGEPGTPGLPGLPGqvgqPGGLDGLASANGTkgekgekgekgmrgrrg 546
Cdd:NF038329  224 DGPAGPAGdgQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAG----PDGPDGKDGERGP----------------- 282

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770700  547 gtgatgpigppgkpgpmgdIGHSGRPGMTGPKGEMGPKGPKGDSgGREGLKGDKGDRGQDGRDGLPGPPG 616
Cdd:NF038329  283 -------------------VGPAGKDGQNGKDGLPGKDGKDGQN-GKDGLPGKDGKDGQPGKDGLPGKDG 332
Collagen_trimer pfam20010
Collagen trimerization domain; This small domain mediate trimerization in various collagen ...
 744-792 6.52e-18

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


Pssm-ID: 466257  Cd Length: 49  Bit Score: 78.03  E-value: 6.52e-18
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 386770700   744 AVTFQNIDEMTKKSALNPPGTLAYITEEEALLVRVNKGWQYIALGTLVP 792
Cdd:pfam20010    1 VTVFQNYDTMLQKTHRVPEGTLVYVREREELYIRVRNGWRKIQLGELIP 49
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 58-222 2.52e-14

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


Pssm-ID: 214560  Cd Length: 184  Bit Score: 72.39  E-value: 2.52e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770700     58 AEDGFPAFRFLQTADVKSPYRMLLPEKL-YEFAILITFRQSSLKGGYLFSVVNPlDTVVQLGVhlspVVKNSYNVSLVYT 136
Cdd:smart00210   23 PEPGSPAYRLGDPALVPQPTRDLFPSGLpEDFSLLTTFRQTPKSRGVLFAIYDA-QNVRQFGL----EVDGRANTLLLRY 97

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770700    137 QADQniGR-KLASFGVAHVPD-KWNSIALQVLSDKVSFYYDCELRnTTLVTREPIELVFDSAS-TLYIGQAGSiiGGKFE 213
Cdd:smart00210   98 QGVD--GKqHTVSFRNLPLADgQWHKLALSVSGSSATLYVDCNEI-DSRPLDRPGQPPIDTDGiEVRGAQAAD--RKPFQ 172


                    ....*....
gi 386770700    214 GYLEKINVY 222
Cdd:smart00210  173 GDLQQLKIV 181
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 464-714 1.63e-13

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 74.17  E-value: 1.63e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770700  464 GAKGVPGEKGDAGQKGERGDPGHKGAHGPSGAKGEPGEPGTPGLPGLPGQVGQPGgldglasangtkgekgekgekgmrg 543
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAG------------------------- 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770700  544 rrggtgatgPIGPPgkpgpmgdiGHSGRPGMTGPKGEMGPKGPKGDSG-----GREGLKGDKGDRGQDGRDGLPGPPGLP 618
Cdd:NF038329  172 ---------PQGPA---------GKDGEAGAKGPAGEKGPQGPRGETGpageqGPAGPAGPDGEAGPAGEDGPAGPAGDG 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770700  619 STgggdgdsggvqyipmpgppgppgppglpglsisGPKGEPGVDSRSSFFGDASYYGRPGARSslDELKALRELQDLRDR 698
Cdd:NF038329  234 QQ---------------------------------GPDGDPGPTGEDGPQGPDGPAGKDGPRG--DRGEAGPDGPDGKDG 278

                         250
                  ....*....|....*.
gi 386770700  699 PDGTAEPPRQPGHSHK 714
Cdd:NF038329  279 ERGPVGPAGKDGQNGK 294
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 467-518 7.22e-13

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: 64.05  E-value: 7.22e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 386770700   467 GVPGEKGDAGQKGERGDPGHKGAHGPSGAKGEPGEPGTPGLPGLPGQVGQPG 518
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPG 52
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 292-421 4.35e-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: 44.13  E-value: 4.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770700  292 PPGQTQYTHERPYRGIKGEKGERGPKGDSIRGPPGPPGPPGPKGETAPYPPFVETTSAGAK----YTGECTCNASDiLEA 367
Cdd:NF038329  202 PAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRgdrgEAGPDGPDGKD-GER 280

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770700  368 IKDNESLRESLRGAPGTPGKDG------KPGTPGHTGATGVPGARGARGSEGAQGLKGEP 421
Cdd:NF038329  281 GPVGPAGKDGQNGKDGLPGKDGkdgqngKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
 
Name Accession Description Interval E-value
Endostatin-like cd00247
Endostatin-like domain; the angiogenesis inhibitor endostatin is a C-terminal fragment of ...
 831-999 3.00e-106

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: 328.14  E-value: 3.00e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770700  831 RMLRVAALNEPSTGDLQGIRGADFACYRQGRRAGLLGTFKAFLSSRVQNLDTIVRPADRD-LPVVNTRGDVLFNSWKGIF 909
Cdd:cd00247     2 PVLHLVALNTPLSGDMRGIRGADFQCFQQARAAGLKGTFRAFLSSRLQDLYSIVRRADRDsLPIVNLKGEVLFNSWESLF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770700  910 NGQGGFFSQAPRIYSFSGKNVMTDSTWPMKMVWHGSLPNGERSMDTYCDAWHSGDHLKGSFASNLDGHKLLEQKRQSCDS 989
Cdd:cd00247    82 SGSGGQFNPGARIYSFDGRDVLTDPAWPQKMVWHGSDPNGRRLTDSYCEAWRTGDSAVTGQASSLSSGKLLEQKAYSCEN 161

                         170
                  ....*....|
gi 386770700  990 KLIILCVEAL 999
Cdd:cd00247   162 KLIVLCIENS 171
Endostatin pfam06482
Collagenase NC10 and Endostatin; NC10 stands for Non-helical region 10 and is taken from Swiss: ...
 833-997 8.45e-75

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: 243.50  E-value: 8.45e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770700   833 LRVAALNEPSTGDLQGIRGADFACYRQGRRAGLLGTFKAFLSSRVQNLDTIVRPADRD-LPVVNTRGDVLFNSWKGIFNG 911
Cdd:pfam06482    1 LHLIALNTPQSGDMRGIRGADFLCFQQARAAGLKGTFRAFLSSRLQDLYSIVRKADREnVPIVNLKDEVLFDSWESIFSG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770700   912 QGGFFSQAPRIYSFSGKNVMTDSTWPMKMVWHGSLPNGERSMDTYCDAWHSGDHLKGSFASNLDGHKLLEQKRQSCDSKL 991
Cdd:pfam06482   81 SGGQMKPNVPIYSFDGRDVLRDPAWPQKMVWHGSTSKGHRLTDNYCEAWRTGDQAVTGQASSLQSGKLLQQSPSSCSNSY 160


                   ....*.
gi 386770700   992 IILCVE 997
Cdd:pfam06482  161 IVLCIE 166
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 379-616 1.51e-25

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 111.15  E-value: 1.51e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770700  379 RGAPGTPGKDGKPGTPGHTGATGVPGARGARGSEGAQGLKGEPGVDGLpgvmgppgppgppglpenydeslmVNSMGAFR 458
Cdd:NF038329  122 PGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGE------------------------AGPQGPAG 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770700  459 GTTQPGAKGVPGEKGDAGQKGERGDPGHKGAHGPSGAKGEPGEPGTPGLPGLPGQVGQ----PGGLDGLASANGtkgekg 534
Cdd:NF038329  178 KDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQgpdgDPGPTGEDGPQG------ 251

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770700  535 ekgekgmrgrrggtgatgPIGPPGKPGPMGDIGHSGRPGMTGPKGEMGPKGPKGDSG--GREGLKGDKGDRGQDGRDGLP 612
Cdd:NF038329  252 ------------------PDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGqnGKDGLPGKDGKDGQNGKDGLP 313


                  ....
gi 386770700  613 GPPG 616
Cdd:NF038329  314 GKDG 317
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 309-616 6.48e-24

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: 106.14  E-value: 6.48e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770700  309 GEKGERGPKgdsirgppgppGPPGPKGETAPYPPFVETTSAGAKYTGECTCNASDILEAIKDNEslreslRGAPGTPGKD 388
Cdd:NF038329  117 GEKGEPGPA-----------GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGE------AGPQGPAGKD 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770700  389 GKPGTPGHTGATGVPGARGARGSEGAQGLKGEPGVDGlpgvmgppgppgppglpenydeslmvnsmgafrgttQPGAKGV 468
Cdd:NF038329  180 GEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDG------------------------------------EAGPAGE 223

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770700  469 PGEKGDAG--QKGERGDPGHKGAHGPSGAKGEPGEPGTPGLPGLPGqvgqPGGLDGLASANGTkgekgekgekgmrgrrg 546
Cdd:NF038329  224 DGPAGPAGdgQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAG----PDGPDGKDGERGP----------------- 282

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770700  547 gtgatgpigppgkpgpmgdIGHSGRPGMTGPKGEMGPKGPKGDSgGREGLKGDKGDRGQDGRDGLPGPPG 616
Cdd:NF038329  283 -------------------VGPAGKDGQNGKDGLPGKDGKDGQN-GKDGLPGKDGKDGQPGKDGLPGKDG 332
Collagen_trimer pfam20010
Collagen trimerization domain; This small domain mediate trimerization in various collagen ...
 744-792 6.52e-18

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


Pssm-ID: 466257  Cd Length: 49  Bit Score: 78.03  E-value: 6.52e-18
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 386770700   744 AVTFQNIDEMTKKSALNPPGTLAYITEEEALLVRVNKGWQYIALGTLVP 792
Cdd:pfam20010    1 VTVFQNYDTMLQKTHRVPEGTLVYVREREELYIRVRNGWRKIQLGELIP 49
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 58-222 2.52e-14

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


Pssm-ID: 214560  Cd Length: 184  Bit Score: 72.39  E-value: 2.52e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770700     58 AEDGFPAFRFLQTADVKSPYRMLLPEKL-YEFAILITFRQSSLKGGYLFSVVNPlDTVVQLGVhlspVVKNSYNVSLVYT 136
Cdd:smart00210   23 PEPGSPAYRLGDPALVPQPTRDLFPSGLpEDFSLLTTFRQTPKSRGVLFAIYDA-QNVRQFGL----EVDGRANTLLLRY 97

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770700    137 QADQniGR-KLASFGVAHVPD-KWNSIALQVLSDKVSFYYDCELRnTTLVTREPIELVFDSAS-TLYIGQAGSiiGGKFE 213
Cdd:smart00210   98 QGVD--GKqHTVSFRNLPLADgQWHKLALSVSGSSATLYVDCNEI-DSRPLDRPGQPPIDTDGiEVRGAQAAD--RKPFQ 172


                    ....*....
gi 386770700    214 GYLEKINVY 222
Cdd:smart00210  173 GDLQQLKIV 181
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 464-714 1.63e-13

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 74.17  E-value: 1.63e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770700  464 GAKGVPGEKGDAGQKGERGDPGHKGAHGPSGAKGEPGEPGTPGLPGLPGQVGQPGgldglasangtkgekgekgekgmrg 543
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAG------------------------- 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770700  544 rrggtgatgPIGPPgkpgpmgdiGHSGRPGMTGPKGEMGPKGPKGDSG-----GREGLKGDKGDRGQDGRDGLPGPPGLP 618
Cdd:NF038329  172 ---------PQGPA---------GKDGEAGAKGPAGEKGPQGPRGETGpageqGPAGPAGPDGEAGPAGEDGPAGPAGDG 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770700  619 STgggdgdsggvqyipmpgppgppgppglpglsisGPKGEPGVDSRSSFFGDASYYGRPGARSslDELKALRELQDLRDR 698
Cdd:NF038329  234 QQ---------------------------------GPDGDPGPTGEDGPQGPDGPAGKDGPRG--DRGEAGPDGPDGKDG 278

                         250
                  ....*....|....*.
gi 386770700  699 PDGTAEPPRQPGHSHK 714
Cdd:NF038329  279 ERGPVGPAGKDGQNGK 294
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 467-518 7.22e-13

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: 64.05  E-value: 7.22e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 386770700   467 GVPGEKGDAGQKGERGDPGHKGAHGPSGAKGEPGEPGTPGLPGLPGQVGQPG 518
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPG 52
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 462-518 2.25e-11

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: 59.81  E-value: 2.25e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 386770700   462 QPGAKGVPGEKGDAGQKGERGDPGHKGahgPSGAKGEPGEPGTPGLPGLPGQVGQPG 518
Cdd:pfam01391    2 PPGPPGPPGPPGPPGPPGPPGPPGPPG---PPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 462-508 1.03e-09

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 55.19  E-value: 1.03e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 386770700   462 QPGAKGVPGEKGDAGQKGERGDPGHKGAHGPSGAKGEPGEPGTPGLP 508
Cdd:pfam01391   11 PPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 463-511 1.52e-09

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 54.81  E-value: 1.52e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 386770700   463 PGAKGVPGEKGDAGQKGERGDPGHKGAHGPSGAKGEPGEPGTPGLPGLP 511
Cdd:pfam01391    9 PGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 570-618 4.64e-07

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: 47.49  E-value: 4.64e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 386770700   570 GRPGMTGPKGEMGPKGPKGDSGGReglkGDKGDRGQDGRDGLPGPPGLP 618
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPP----GPPGPPGEPGPPGPPGPPGPP 45
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 380-423 9.13e-07

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: 46.72  E-value: 9.13e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 386770700   380 GAPGTPGKDGKPGTPGHTGATGVPGARGARGSEGAQGLKGEPGV 423
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGP 44
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 567-615 4.84e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 44.79  E-value: 4.84e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 386770700   567 GHSGRPGMTGPKGEMGPKGPKGDSG--GREGLKGDKGDRGQDGRDGLPGPP 615
Cdd:pfam01391    7 GPPGPPGPPGPPGPPGPPGPPGPPGepGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 378-436 8.52e-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: 41.33  E-value: 8.52e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 386770700   378 LRGAPGTPGKDGKPGTPGHTGATGVPGARGARGSEGAQGLKGEPGvdglpgvmgPPGPP 436
Cdd:pfam01391    2 PPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPG---------PPGAP 51
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 491-591 2.08e-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: 40.17  E-value: 2.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770700   491 GPSGAKGEPGEPGTPGLPGLPGQVGQPGgldglasangtkgekgekgekgmrgrrggtgatgpigppgkpgpmgdigHSG 570
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPG-------------------------------------------------PPG 31

                           90       100
                   ....*....|....*....|.
gi 386770700   571 RPGMTGPKGEMGPKGPKGDSG 591
Cdd:pfam01391   32 EPGPPGPPGPPGPPGPPGAPG 52
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 292-421 4.35e-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: 44.13  E-value: 4.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770700  292 PPGQTQYTHERPYRGIKGEKGERGPKGDSIRGPPGPPGPPGPKGETAPYPPFVETTSAGAK----YTGECTCNASDiLEA 367
Cdd:NF038329  202 PAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRgdrgEAGPDGPDGKD-GER 280

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770700  368 IKDNESLRESLRGAPGTPGKDG------KPGTPGHTGATGVPGARGARGSEGAQGLKGEP 421
Cdd:NF038329  281 GPVGPAGKDGQNGKDGLPGKDGkdgqngKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 379-414 2.51e-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: 37.09  E-value: 2.51e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 386770700   379 RGAPGTPGKDGKPGTPGHTGATGVPGARGARGSEGA 414
Cdd:pfam01391   21 PGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH