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Conserved domains on  [gi|28574366|ref|NP_788471|]
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multiplexin, isoform E [Drosophila melanogaster]

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 ...
 569-738 3.38e-109

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: 330.06  E-value: 3.38e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574366 569 TPTLRVAALNEPSTGDLQGIRGADFACYRQGRRAGLLGTFKAFLSSRVQNLDTIVRPADRD-LPVVNTRGDVLFNSWKGI 647
Cdd:cd00247   1 QPVLHLVALNTPLSGDMRGIRGADFQCFQQARAAGLKGTFRAFLSSRLQDLYSIVRRADRDsLPIVNLKGEVLFNSWESL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574366 648 FNGQGGFFSQAPRIYSFSGKNVMTDSTWPMKMVWHGSLPNGERSMDTYCDAWHSGDHLKGSFASNLDGHKLLEQKRQSCD 727
Cdd:cd00247  81 FSGSGGQFNPGARIYSFDGRDVLTDPAWPQKMVWHGSDPNGRRLTDSYCEAWRTGDSAVTGQASSLSSGKLLEQKAYSCE 160

                       170
                ....*....|.
gi 28574366 728 SKLIILCVEAL 738
Cdd:cd00247 161 NKLIVLCIENS 171
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 149-386 3.26e-23

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: 103.45  E-value: 3.26e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574366  149 RGAPGTPGKDGKPGTPGHTGATGVPGARGARGSEGAQGLKGEPGVDGLPGVMGPPGPPGppglpenydeslmvnsmgafr 228
Cdd:NF038329 122 PGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDG--------------------- 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574366  229 gttQPGAKGVPGEKGDAGQKGERGDPGHKGAHGPSGAKGEPGEPGTPGLPGLPGQVGQ----PGGLDGLASANGtkgekg 304
Cdd:NF038329 181 ---EAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQgpdgDPGPTGEDGPQG------ 251

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574366  305 ekgekgmrgrrggtgatgPIGPPGKPGPMGDIGHSGRPGMTGPKGEMGPKGPKGDSG--GREGLKGDKGDRGQDGRDGLP 382
Cdd:NF038329 252 ------------------PDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGqnGKDGLPGKDGKDGQNGKDGLP 313


                 ....
gi 28574366  383 GPPG 386
Cdd:NF038329 314 GKDG 317
Collagen_trimer pfam20010
Collagen trimerization domain; This small domain mediate trimerization in various collagen ...
 488-536 4.88e-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: 4.88e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 28574366   488 AVTFQNIDEMTKKSALNPPGTLAYITEEEALLVRVNKGWQYIALGTLVP 536
Cdd:pfam20010   1 VTVFQNYDTMLQKTHRVPEGTLVYVREREELYIRVRNGWRKIQLGELIP 49
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 62-191 2.55e-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: 41.04  E-value: 2.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574366   62 PPGQTQYTHERPYRGIKGEKGERGPKGDSIRGPPGPPGPPGPKGETAPYPPFVETTSAGAK----YTGECTCNASDiLEA 137
Cdd:NF038329 202 PAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRgdrgEAGPDGPDGKD-GER 280

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574366  138 IKDNESLRESLRGAPGTPGKDG------KPGTPGHTGATGVPGARGARGSEGAQGLKGEP 191
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 ...
 569-738 3.38e-109

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: 330.06  E-value: 3.38e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574366 569 TPTLRVAALNEPSTGDLQGIRGADFACYRQGRRAGLLGTFKAFLSSRVQNLDTIVRPADRD-LPVVNTRGDVLFNSWKGI 647
Cdd:cd00247   1 QPVLHLVALNTPLSGDMRGIRGADFQCFQQARAAGLKGTFRAFLSSRLQDLYSIVRRADRDsLPIVNLKGEVLFNSWESL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574366 648 FNGQGGFFSQAPRIYSFSGKNVMTDSTWPMKMVWHGSLPNGERSMDTYCDAWHSGDHLKGSFASNLDGHKLLEQKRQSCD 727
Cdd:cd00247  81 FSGSGGQFNPGARIYSFDGRDVLTDPAWPQKMVWHGSDPNGRRLTDSYCEAWRTGDSAVTGQASSLSSGKLLEQKAYSCE 160

                       170
                ....*....|.
gi 28574366 728 SKLIILCVEAL 738
Cdd:cd00247 161 NKLIVLCIENS 171
Endostatin pfam06482
Collagenase NC10 and Endostatin; NC10 stands for Non-helical region 10 and is taken from Swiss: ...
 572-736 3.19e-76

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: 3.19e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574366   572 LRVAALNEPSTGDLQGIRGADFACYRQGRRAGLLGTFKAFLSSRVQNLDTIVRPADRD-LPVVNTRGDVLFNSWKGIFNG 650
Cdd:pfam06482   1 LHLIALNTPQSGDMRGIRGADFLCFQQARAAGLKGTFRAFLSSRLQDLYSIVRKADREnVPIVNLKDEVLFDSWESIFSG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574366   651 QGGFFSQAPRIYSFSGKNVMTDSTWPMKMVWHGSLPNGERSMDTYCDAWHSGDHLKGSFASNLDGHKLLEQKRQSCDSKL 730
Cdd:pfam06482  81 SGGQMKPNVPIYSFDGRDVLRDPAWPQKMVWHGSTSKGHRLTDNYCEAWRTGDQAVTGQASSLQSGKLLQQSPSSCSNSY 160


                  ....*.
gi 28574366   731 IILCVE 736
Cdd:pfam06482 161 IVLCIE 166
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 149-386 3.26e-23

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: 103.45  E-value: 3.26e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574366  149 RGAPGTPGKDGKPGTPGHTGATGVPGARGARGSEGAQGLKGEPGVDGLPGVMGPPGPPGppglpenydeslmvnsmgafr 228
Cdd:NF038329 122 PGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDG--------------------- 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574366  229 gttQPGAKGVPGEKGDAGQKGERGDPGHKGAHGPSGAKGEPGEPGTPGLPGLPGQVGQ----PGGLDGLASANGtkgekg 304
Cdd:NF038329 181 ---EAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQgpdgDPGPTGEDGPQG------ 251

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574366  305 ekgekgmrgrrggtgatgPIGPPGKPGPMGDIGHSGRPGMTGPKGEMGPKGPKGDSG--GREGLKGDKGDRGQDGRDGLP 382
Cdd:NF038329 252 ------------------PDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGqnGKDGLPGKDGKDGQNGKDGLP 313


                 ....
gi 28574366  383 GPPG 386
Cdd:NF038329 314 GKDG 317
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 79-386 5.52e-21

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 96.51  E-value: 5.52e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574366   79 GEKGERGPKgdsirgppgppGPPGPKGETAPYPPFVETTSAGAKYTGECTCNASDILEAIKDNEslreslRGAPGTPGKD 158
Cdd:NF038329 117 GEKGEPGPA-----------GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGE------AGPQGPAGKD 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574366  159 GKPGTPGHTGATGVPGARGARGSEGAQGLKGEPGVDGlpgvmgppgppgppglpenydeslmvnsmgafrgttQPGAKGV 238
Cdd:NF038329 180 GEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDG------------------------------------EAGPAGE 223

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574366  239 PGEKGDAG--QKGERGDPGHKGAHGPSGAKGEPGEPGTPGLPGLPGqvgqPGGLDGLASANGTkgekgekgekgmrgrrg 316
Cdd:NF038329 224 DGPAGPAGdgQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAG----PDGPDGKDGERGP----------------- 282

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574366  317 gtgatgpigppgkpgpmgdIGHSGRPGMTGPKGEMGPKGPKGDSgGREGLKGDKGDRGQDGRDGLPGPPG 386
Cdd:NF038329 283 -------------------VGPAGKDGQNGKDGLPGKDGKDGQN-GKDGLPGKDGKDGQPGKDGLPGKDG 332
Collagen_trimer pfam20010
Collagen trimerization domain; This small domain mediate trimerization in various collagen ...
 488-536 4.88e-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: 4.88e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 28574366   488 AVTFQNIDEMTKKSALNPPGTLAYITEEEALLVRVNKGWQYIALGTLVP 536
Cdd:pfam20010   1 VTVFQNYDTMLQKTHRVPEGTLVYVREREELYIRVRNGWRKIQLGELIP 49
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 142-386 1.02e-16

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: 83.42  E-value: 1.02e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574366  142 ESLRESLRGAPGTpGKDGKPGTPGHTGATGVPGARGARGSEGAQGLKGEPGVDGlpgvmgppgppgppglpenydeslmv 221
Cdd:NF038329 104 EELDEGLQQLKGD-GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQG-------------------------- 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574366  222 nsmgafrgttQPGAKGVPGEKGDAGQKGERGDPGHKGAHGPSGAKGEPGEPGTPGLPGLPGQVGqPGGLDGLASANGTKG 301
Cdd:NF038329 157 ----------ERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAG-PAGPDGEAGPAGEDG 225

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574366  302 EKGEKGEkgmrgrrggtgatgpigppgkpgpmgdiGHSGRPGMTGPKGEMGPKGPKGDSGGreglKGDKGDRGQDGRDGL 381
Cdd:NF038329 226 PAGPAGD----------------------------GQQGPDGDPGPTGEDGPQGPDGPAGK----DGPRGDRGEAGPDGP 273


                 ....*
gi 28574366  382 PGPPG 386
Cdd:NF038329 274 DGKDG 278
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 237-288 8.18e-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: 57.89  E-value: 8.18e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 28574366   237 GVPGEKGDAGQKGERGDPGHKGAHGPSGAKGEPGEPGTPGLPGLPGQVGQPG 288
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPG 52
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 62-191 2.55e-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: 41.04  E-value: 2.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574366   62 PPGQTQYTHERPYRGIKGEKGERGPKGDSIRGPPGPPGPPGPKGETAPYPPFVETTSAGAK----YTGECTCNASDiLEA 137
Cdd:NF038329 202 PAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRgdrgEAGPDGPDGKD-GER 280

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574366  138 IKDNESLRESLRGAPGTPGKDG------KPGTPGHTGATGVPGARGARGSEGAQGLKGEP 191
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 ...
 569-738 3.38e-109

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: 330.06  E-value: 3.38e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574366 569 TPTLRVAALNEPSTGDLQGIRGADFACYRQGRRAGLLGTFKAFLSSRVQNLDTIVRPADRD-LPVVNTRGDVLFNSWKGI 647
Cdd:cd00247   1 QPVLHLVALNTPLSGDMRGIRGADFQCFQQARAAGLKGTFRAFLSSRLQDLYSIVRRADRDsLPIVNLKGEVLFNSWESL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574366 648 FNGQGGFFSQAPRIYSFSGKNVMTDSTWPMKMVWHGSLPNGERSMDTYCDAWHSGDHLKGSFASNLDGHKLLEQKRQSCD 727
Cdd:cd00247  81 FSGSGGQFNPGARIYSFDGRDVLTDPAWPQKMVWHGSDPNGRRLTDSYCEAWRTGDSAVTGQASSLSSGKLLEQKAYSCE 160

                       170
                ....*....|.
gi 28574366 728 SKLIILCVEAL 738
Cdd:cd00247 161 NKLIVLCIENS 171
Endostatin pfam06482
Collagenase NC10 and Endostatin; NC10 stands for Non-helical region 10 and is taken from Swiss: ...
 572-736 3.19e-76

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: 3.19e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574366   572 LRVAALNEPSTGDLQGIRGADFACYRQGRRAGLLGTFKAFLSSRVQNLDTIVRPADRD-LPVVNTRGDVLFNSWKGIFNG 650
Cdd:pfam06482   1 LHLIALNTPQSGDMRGIRGADFLCFQQARAAGLKGTFRAFLSSRLQDLYSIVRKADREnVPIVNLKDEVLFDSWESIFSG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574366   651 QGGFFSQAPRIYSFSGKNVMTDSTWPMKMVWHGSLPNGERSMDTYCDAWHSGDHLKGSFASNLDGHKLLEQKRQSCDSKL 730
Cdd:pfam06482  81 SGGQMKPNVPIYSFDGRDVLRDPAWPQKMVWHGSTSKGHRLTDNYCEAWRTGDQAVTGQASSLQSGKLLQQSPSSCSNSY 160


                  ....*.
gi 28574366   731 IILCVE 736
Cdd:pfam06482 161 IVLCIE 166
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 149-386 3.26e-23

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: 103.45  E-value: 3.26e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574366  149 RGAPGTPGKDGKPGTPGHTGATGVPGARGARGSEGAQGLKGEPGVDGLPGVMGPPGPPGppglpenydeslmvnsmgafr 228
Cdd:NF038329 122 PGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDG--------------------- 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574366  229 gttQPGAKGVPGEKGDAGQKGERGDPGHKGAHGPSGAKGEPGEPGTPGLPGLPGQVGQ----PGGLDGLASANGtkgekg 304
Cdd:NF038329 181 ---EAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQgpdgDPGPTGEDGPQG------ 251

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574366  305 ekgekgmrgrrggtgatgPIGPPGKPGPMGDIGHSGRPGMTGPKGEMGPKGPKGDSG--GREGLKGDKGDRGQDGRDGLP 382
Cdd:NF038329 252 ------------------PDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGqnGKDGLPGKDGKDGQNGKDGLP 313


                 ....
gi 28574366  383 GPPG 386
Cdd:NF038329 314 GKDG 317
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 79-386 5.52e-21

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 96.51  E-value: 5.52e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574366   79 GEKGERGPKgdsirgppgppGPPGPKGETAPYPPFVETTSAGAKYTGECTCNASDILEAIKDNEslreslRGAPGTPGKD 158
Cdd:NF038329 117 GEKGEPGPA-----------GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGE------AGPQGPAGKD 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574366  159 GKPGTPGHTGATGVPGARGARGSEGAQGLKGEPGVDGlpgvmgppgppgppglpenydeslmvnsmgafrgttQPGAKGV 238
Cdd:NF038329 180 GEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDG------------------------------------EAGPAGE 223

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574366  239 PGEKGDAG--QKGERGDPGHKGAHGPSGAKGEPGEPGTPGLPGLPGqvgqPGGLDGLASANGTkgekgekgekgmrgrrg 316
Cdd:NF038329 224 DGPAGPAGdgQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAG----PDGPDGKDGERGP----------------- 282

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574366  317 gtgatgpigppgkpgpmgdIGHSGRPGMTGPKGEMGPKGPKGDSgGREGLKGDKGDRGQDGRDGLPGPPG 386
Cdd:NF038329 283 -------------------VGPAGKDGQNGKDGLPGKDGKDGQN-GKDGLPGKDGKDGQPGKDGLPGKDG 332
Collagen_trimer pfam20010
Collagen trimerization domain; This small domain mediate trimerization in various collagen ...
 488-536 4.88e-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: 4.88e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 28574366   488 AVTFQNIDEMTKKSALNPPGTLAYITEEEALLVRVNKGWQYIALGTLVP 536
Cdd:pfam20010   1 VTVFQNYDTMLQKTHRVPEGTLVYVREREELYIRVRNGWRKIQLGELIP 49
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 142-386 1.02e-16

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: 83.42  E-value: 1.02e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574366  142 ESLRESLRGAPGTpGKDGKPGTPGHTGATGVPGARGARGSEGAQGLKGEPGVDGlpgvmgppgppgppglpenydeslmv 221
Cdd:NF038329 104 EELDEGLQQLKGD-GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQG-------------------------- 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574366  222 nsmgafrgttQPGAKGVPGEKGDAGQKGERGDPGHKGAHGPSGAKGEPGEPGTPGLPGLPGQVGqPGGLDGLASANGTKG 301
Cdd:NF038329 157 ----------ERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAG-PAGPDGEAGPAGEDG 225

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574366  302 EKGEKGEkgmrgrrggtgatgpigppgkpgpmgdiGHSGRPGMTGPKGEMGPKGPKGDSGGreglKGDKGDRGQDGRDGL 381
Cdd:NF038329 226 PAGPAGD----------------------------GQQGPDGDPGPTGEDGPQGPDGPAGK----DGPRGDRGEAGPDGP 273


                 ....*
gi 28574366  382 PGPPG 386
Cdd:NF038329 274 DGKDG 278
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 237-288 8.18e-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: 57.89  E-value: 8.18e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 28574366   237 GVPGEKGDAGQKGERGDPGHKGAHGPSGAKGEPGEPGTPGLPGLPGQVGQPG 288
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPG 52
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 232-288 2.91e-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: 53.65  E-value: 2.91e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 28574366   232 QPGAKGVPGEKGDAGQKGERGDPGHKGahgPSGAKGEPGEPGTPGLPGLPGQVGQPG 288
Cdd:pfam01391   2 PPGPPGPPGPPGPPGPPGPPGPPGPPG---PPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 232-278 6.05e-08

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: 49.80  E-value: 6.05e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 28574366   232 QPGAKGVPGEKGDAGQKGERGDPGHKGAHGPSGAKGEPGEPGTPGLP 278
Cdd:pfam01391  11 PPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 233-281 8.28e-08

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: 49.41  E-value: 8.28e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 28574366   233 PGAKGVPGEKGDAGQKGERGDPGHKGAHGPSGAKGEPGEPGTPGLPGLP 281
Cdd:pfam01391   9 PGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 340-388 2.24e-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: 2.24e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 28574366   340 GRPGMTGPKGEMGPKGPKGDSGGReglkGDKGDRGQDGRDGLPGPPGLP 388
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPP----GPPGPPGEPGPPGPPGPPGPP 45
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 150-193 2.62e-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: 42.10  E-value: 2.62e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 28574366   150 GAPGTPGKDGKPGTPGHTGATGVPGARGARGSEGAQGLKGEPGV 193
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGP 44
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 337-385 1.75e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.78  E-value: 1.75e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 28574366   337 GHSGRPGMTGPKGEMGPKGPKGDSG--GREGLKGDKGDRGQDGRDGLPGPP 385
Cdd:pfam01391   7 GPPGPPGPPGPPGPPGPPGPPGPPGepGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 148-206 2.54e-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: 36.70  E-value: 2.54e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 28574366   148 LRGAPGTPGKDGKPGTPGHTGATGVPGARGARGSEGAQGLKGEPGvdglpgvmgPPGPP 206
Cdd:pfam01391   2 PPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPG---------PPGAP 51
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 62-191 2.55e-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: 41.04  E-value: 2.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574366   62 PPGQTQYTHERPYRGIKGEKGERGPKGDSIRGPPGPPGPPGPKGETAPYPPFVETTSAGAK----YTGECTCNASDiLEA 137
Cdd:NF038329 202 PAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRgdrgEAGPDGPDGKD-GER 280

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574366  138 IKDNESLRESLRGAPGTPGKDG------KPGTPGHTGATGVPGARGARGSEGAQGLKGEP 191
Cdd:NF038329 281 GPVGPAGKDGQNGKDGLPGKDGkdgqngKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
 
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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