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Conserved domains on  [gi|147904870|ref|NP_001081121|]
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collagen type XVIII alpha 1 L homeolog precursor [Xenopus laevis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Endostatin pfam06482
Collagenase NC10 and Endostatin; NC10 stands for Non-helical region 10 and is taken from Swiss: ...
 1133-1301 1.55e-113

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


:

Pssm-ID: 461931  Cd Length: 169  Bit Score: 352.13  E-value: 1.55e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147904870  1133 LHLVALNAPISGSMKSIRGVDFQCFEQARKAGLHGTFRAFLSSRLQDLYSIVRRADRQSVQIVNLRDEVLYDNWDSLFSG 1212
Cdd:pfam06482    1 LHLIALNTPQSGDMRGIRGADFLCFQQARAAGLKGTFRAFLSSRLQDLYSIVRKADRENVPIVNLKDEVLFDSWESIFSG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147904870  1213 SEAQMRSGARILSFDGKDVTTDPTWPQKMVWHGSDAKGRRLTESYCETWRTDESAVTGQASSLTSGKLLEQRPQSCNKNF 1292
Cdd:pfam06482   81 SGGQMKPNVPIYSFDGRDVLRDPAWPQKMVWHGSTSKGHRLTDNYCEAWRTGDQAVTGQASSLQSGKLLQQSPSSCSNSY 160


                   ....*....
gi 147904870  1293 IVLCIENSF 1301
Cdd:pfam06482  161 IVLCIENSY 169
LamG super family cl22861
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 31-219 7.22e-32

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: 123.24  E-value: 7.22e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147904870     31 EVGLLQLIGEP-VPNEITKVFGPDK-TPAYVFDKEANTGQVAQYHLPNPMYRDFSLLFHVQPSTNKAGILFAITDAsQSI 108
Cdd:smart00210    1 GQDLLQVFDLPsLSFAIRQVVGPEPgSPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPKSRGVLFAIYDA-QNV 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147904870    109 VYIGVKLsevkDGKQDII--FYYTEPGSQDSYVaatFNVPSL-VNRWSRFAISVEDEEVVLFMDCDELERVRFERSPDEM 185
Cdd:smart00210   80 RQFGLEV----DGRANTLllRYQGVDGKQHTVS---FRNLPLaDGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGQPP 152

                           170       180       190
                    ....*....|....*....|....*....|....
gi 147904870    186 elEDGSGLFVAQAGGADPDRYQGVIADLKIVANP 219
Cdd:smart00210  153 --IDTDGIEVRGAQAADRKPFQGDLQQLKIVCDP 184
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 620-813 1.33e-27

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: 117.70  E-value: 1.33e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147904870  620 GAQGLPGLPGAKGEQGNPGLPGLQGVKGDSGPPGPEGRQGLDGFPGPEGLRGEKGERGERGETGHDGVGIPGPPGPPGQv 699
Cdd:NF038329  138 GDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDG- 216

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147904870  700 lyVPSDDKSVVGAIPGPEGRQGIAGLPGPRGPKGDQGLDGFPGTHGAKGEKGEPGlmmrPDGtlytdpSKGEKGDQGLRG 779
Cdd:NF038329  217 --EAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAG----PDG------PDGKDGERGPVG 284

                         170       180       190
                  ....*....|....*....|....*....|....
gi 147904870  780 PAGSVGPYGQKGEIGFPGRPGRPGMNGLKGEKGE 813
Cdd:NF038329  285 PAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGK 318
Collagen_trimer pfam20010
Collagen trimerization domain; This small domain mediate trimerization in various collagen ...
 994-1042 3.12e-17

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


:

Pssm-ID: 466257  Cd Length: 49  Bit Score: 76.49  E-value: 3.12e-17
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 147904870   994 ATVLQTHQTMINLAHRLQEGTIVLVQERAELYVRVREGFRRILLGEYTT 1042
Cdd:pfam20010    1 VTVFQNYDTMLQKTHRVPEGTLVYVREREELYIRVRNGWRKIQLGELIP 49
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 286-654 5.75e-15

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: 78.79  E-value: 5.75e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147904870  286 QGIKGEKGDhGEKGERGLTGPKGdsasvspasdSNGEKGQKGEVGVKGSAG-FGYPGPKGQKGDPGtmgprgpagppgps 364
Cdd:NF038329  108 EGLQQLKGD-GEKGEPGPAGPAG----------PAGEQGPRGDRGETGPAGpAGPPGPQGERGEKG-------------- 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147904870  365 ilqksdgtsvrqvtgppgpqgpagPAGKDGEPGDPGEDGKTGEVGPQGFPGTPGDPGQKGEKGDTGvgmrgppglpgppg 444
Cdd:NF038329  163 ------------------------PAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAG-------------- 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147904870  445 ppgpaktdkltfidmegsgysgdlehvkgPPGLPGPPGPPGVPGLPGVPGTFGMNSTGLPGPSGLPGLPGKEGIPGPPGL 524
Cdd:NF038329  205 -----------------------------EQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGP 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147904870  525 PGPPGKDGLPGASGVAGIRGEDGEIGLPGAPGAKGNPGEQGQPGAAGQPGlaglpgpmgprgqpgppgppgpvsrgsaig 604
Cdd:NF038329  256 AGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDG------------------------------ 305

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 147904870  605 fddmeasglgfglREGAQGLPGLPGAKGEQGNPGLPGLQGVKGDSGPPGP 654
Cdd:NF038329  306 -------------QNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 760-871 1.12e-08

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: 59.15  E-value: 1.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147904870  760 DGTLYTDPSKGEKGDQGLRGPAGSVGPYGQKGEIGFPGRPGRPGMNGLKGEKGECASSGSGLRGPPGPPGPPGPPGsvvn 839
Cdd:NF038329  107 DEGLQQLKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEA---- 182

                          90       100       110
                  ....*....|....*....|....*....|..
gi 147904870  840 GDQNIPGAyPGQKGERGFPGPQGDVGPAGPPG 871
Cdd:NF038329  183 GAKGPAGE-KGPQGPRGETGPAGEQGPAGPAG 213
 
Name Accession Description Interval E-value
Endostatin pfam06482
Collagenase NC10 and Endostatin; NC10 stands for Non-helical region 10 and is taken from Swiss: ...
 1133-1301 1.55e-113

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


Pssm-ID: 461931  Cd Length: 169  Bit Score: 352.13  E-value: 1.55e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147904870  1133 LHLVALNAPISGSMKSIRGVDFQCFEQARKAGLHGTFRAFLSSRLQDLYSIVRRADRQSVQIVNLRDEVLYDNWDSLFSG 1212
Cdd:pfam06482    1 LHLIALNTPQSGDMRGIRGADFLCFQQARAAGLKGTFRAFLSSRLQDLYSIVRKADRENVPIVNLKDEVLFDSWESIFSG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147904870  1213 SEAQMRSGARILSFDGKDVTTDPTWPQKMVWHGSDAKGRRLTESYCETWRTDESAVTGQASSLTSGKLLEQRPQSCNKNF 1292
Cdd:pfam06482   81 SGGQMKPNVPIYSFDGRDVLRDPAWPQKMVWHGSTSKGHRLTDNYCEAWRTGDQAVTGQASSLQSGKLLQQSPSSCSNSY 160


                   ....*....
gi 147904870  1293 IVLCIENSF 1301
Cdd:pfam06482  161 IVLCIENSY 169
Endostatin-like cd00247
Endostatin-like domain; the angiogenesis inhibitor endostatin is a C-terminal fragment of ...
 1130-1300 9.55e-111

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: 344.70  E-value: 9.55e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147904870 1130 NPALHLVALNAPISGSMKSIRGVDFQCFEQARKAGLHGTFRAFLSSRLQDLYSIVRRADRQSVQIVNLRDEVLYDNWDSL 1209
Cdd:cd00247     1 QPVLHLVALNTPLSGDMRGIRGADFQCFQQARAAGLKGTFRAFLSSRLQDLYSIVRRADRDSLPIVNLKGEVLFNSWESL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147904870 1210 FSGSEAQMRSGARILSFDGKDVTTDPTWPQKMVWHGSDAKGRRLTESYCETWRTDESAVTGQASSLTSGKLLEQRPQSCN 1289
Cdd:cd00247    81 FSGSGGQFNPGARIYSFDGRDVLTDPAWPQKMVWHGSDPNGRRLTDSYCEAWRTGDSAVTGQASSLSSGKLLEQKAYSCE 160

                         170
                  ....*....|.
gi 147904870 1290 KNFIVLCIENS 1300
Cdd:cd00247   161 NKLIVLCIENS 171
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 31-219 7.22e-32

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


Pssm-ID: 214560  Cd Length: 184  Bit Score: 123.24  E-value: 7.22e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147904870     31 EVGLLQLIGEP-VPNEITKVFGPDK-TPAYVFDKEANTGQVAQYHLPNPMYRDFSLLFHVQPSTNKAGILFAITDAsQSI 108
Cdd:smart00210    1 GQDLLQVFDLPsLSFAIRQVVGPEPgSPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPKSRGVLFAIYDA-QNV 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147904870    109 VYIGVKLsevkDGKQDII--FYYTEPGSQDSYVaatFNVPSL-VNRWSRFAISVEDEEVVLFMDCDELERVRFERSPDEM 185
Cdd:smart00210   80 RQFGLEV----DGRANTLllRYQGVDGKQHTVS---FRNLPLaDGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGQPP 152

                           170       180       190
                    ....*....|....*....|....*....|....
gi 147904870    186 elEDGSGLFVAQAGGADPDRYQGVIADLKIVANP 219
Cdd:smart00210  153 --IDTDGIEVRGAQAADRKPFQGDLQQLKIVCDP 184
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 620-813 1.33e-27

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: 117.70  E-value: 1.33e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147904870  620 GAQGLPGLPGAKGEQGNPGLPGLQGVKGDSGPPGPEGRQGLDGFPGPEGLRGEKGERGERGETGHDGVGIPGPPGPPGQv 699
Cdd:NF038329  138 GDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDG- 216

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147904870  700 lyVPSDDKSVVGAIPGPEGRQGIAGLPGPRGPKGDQGLDGFPGTHGAKGEKGEPGlmmrPDGtlytdpSKGEKGDQGLRG 779
Cdd:NF038329  217 --EAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAG----PDG------PDGKDGERGPVG 284

                         170       180       190
                  ....*....|....*....|....*....|....
gi 147904870  780 PAGSVGPYGQKGEIGFPGRPGRPGMNGLKGEKGE 813
Cdd:NF038329  285 PAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGK 318
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 502-753 1.25e-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: 108.84  E-value: 1.25e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147904870  502 GLPGPSGLPGLPGKEGIPGPPGLPGPPGKDGLPGASGVAG---IRGEDGEIGLPGAPGAKGNPGEQGQPGAAGQPGLAGL 578
Cdd:NF038329  132 GEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGpqgPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGP 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147904870  579 PGPMGPRGQPGPPGPPGPVSRGsaigfddmeasglgfglREGAQGLPGLPGAKGEQGNPGLPGLQGVKGDSGPPGPEGRQ 658
Cdd:NF038329  212 AGPDGEAGPAGEDGPAGPAGDG-----------------QQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPD 274

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147904870  659 GLDGFPGPEGLRGEKGERGERGETGHDgvgipgppgppgqvlyvpsddksvvgaipGPEGRQGIAGLPGPRGPKGDQGLD 738
Cdd:NF038329  275 GKDGERGPVGPAGKDGQNGKDGLPGKD-----------------------------GKDGQNGKDGLPGKDGKDGQPGKD 325

                         250
                  ....*....|....*
gi 147904870  739 GFPGTHGAKGEKGEP 753
Cdd:NF038329  326 GLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 641-871 8.41e-20

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 93.82  E-value: 8.41e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147904870  641 GLQGVKGDS--GPPGPEGRQGLDGFPGPEGLRGEKGERGERGEtghdgvgipgppgppgqvlyvpsddksvvgaiPGPEG 718
Cdd:NF038329  109 GLQQLKGDGekGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGP--------------------------------PGPQG 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147904870  719 RQGIAGLPGPRGPKGDQGLDGFPGTHGAKGEKGEPGlmmrPDGtlytdpSKGEKGDQGLRGPAGSVGPYGQKGEIGFPGR 798
Cdd:NF038329  157 ERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKG----PQG------PRGETGPAGEQGPAGPAGPDGEAGPAGEDGP 226

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 147904870  799 PGRPGmNGLKGEKGEcassgsglrgppgppgppgppgsvvngdqnipgaypgqKGERGFPGPQGDVGPAGPPG 871
Cdd:NF038329  227 AGPAG-DGQQGPDGD--------------------------------------PGPTGEDGPQGPDGPAGKDG 260
Collagen_trimer pfam20010
Collagen trimerization domain; This small domain mediate trimerization in various collagen ...
 994-1042 3.12e-17

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


Pssm-ID: 466257  Cd Length: 49  Bit Score: 76.49  E-value: 3.12e-17
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 147904870   994 ATVLQTHQTMINLAHRLQEGTIVLVQERAELYVRVREGFRRILLGEYTT 1042
Cdd:pfam20010    1 VTVFQNYDTMLQKTHRVPEGTLVYVREREELYIRVRNGWRKIQLGELIP 49
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 286-654 5.75e-15

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 78.79  E-value: 5.75e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147904870  286 QGIKGEKGDhGEKGERGLTGPKGdsasvspasdSNGEKGQKGEVGVKGSAG-FGYPGPKGQKGDPGtmgprgpagppgps 364
Cdd:NF038329  108 EGLQQLKGD-GEKGEPGPAGPAG----------PAGEQGPRGDRGETGPAGpAGPPGPQGERGEKG-------------- 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147904870  365 ilqksdgtsvrqvtgppgpqgpagPAGKDGEPGDPGEDGKTGEVGPQGFPGTPGDPGQKGEKGDTGvgmrgppglpgppg 444
Cdd:NF038329  163 ------------------------PAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAG-------------- 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147904870  445 ppgpaktdkltfidmegsgysgdlehvkgPPGLPGPPGPPGVPGLPGVPGTFGMNSTGLPGPSGLPGLPGKEGIPGPPGL 524
Cdd:NF038329  205 -----------------------------EQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGP 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147904870  525 PGPPGKDGLPGASGVAGIRGEDGEIGLPGAPGAKGNPGEQGQPGAAGQPGlaglpgpmgprgqpgppgppgpvsrgsaig 604
Cdd:NF038329  256 AGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDG------------------------------ 305

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 147904870  605 fddmeasglgfglREGAQGLPGLPGAKGEQGNPGLPGLQGVKGDSGPPGP 654
Cdd:NF038329  306 -------------QNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 284-577 6.99e-15

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 78.79  E-value: 6.99e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147904870  284 GQQGIKGEKGDHGEKGERGLTGPKGDSASVSPAsdsnGEKGQKGEVGVKGSAGfgYPGPKGQKGDPGTMGPRGPAGPPGP 363
Cdd:NF038329  141 GETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ----GPAGKDGEAGAKGPAG--EKGPQGPRGETGPAGEQGPAGPAGP 214

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147904870  364 SILQKSDGtsvrqvtgpPGPQGPAGPAGKDGEPGDPGEDGKTGEVGPQGFPGTPGDPGQKGEKGDTGvgmrgppglpgpp 443
Cdd:NF038329  215 DGEAGPAG---------EDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDG------------- 272

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147904870  444 gppgpaktdkltfidmegsgysgdlehvkgppglpgppgppgvpglpgvpgtfgmnSTGLPGPSGLPGLPGKEGIPGPPg 523
Cdd:NF038329  273 --------------------------------------------------------PDGKDGERGPVGPAGKDGQNGKD- 295

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 147904870  524 lpgppgkdglpGASGVAGIRGEDGEIGLPGAPGAKGNPGEQGQPGAAGQPGLAG 577
Cdd:NF038329  296 -----------GLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 283-577 7.08e-14

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 75.71  E-value: 7.08e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147904870  283 QGQQGIKGEKGDHGEKGERGLTGPKGDSASVSPAsdsnGEKGQKGEVGVKGSAGfgYPGPKGQKGDPGTMGPRGPAGPPG 362
Cdd:NF038329  128 AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEK----GPAGPQGEAGPQGPAG--KDGEAGAKGPAGEKGPQGPRGETG 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147904870  363 PSILQKSDGTSVRQVTGPPGPQGPAGPAGKDGEPGDPGEDGKTGEVGPQGFPGTPGDPGQKGEKGDTGVGmrgppglpgp 442
Cdd:NF038329  202 PAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPD---------- 271

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147904870  443 pgppgpaktdkltfidmegsgysgdlehvkgppglpgppgppgvpglpgvpgtfgmNSTGLPGPSGLPGLPgkegipgpp 522
Cdd:NF038329  272 --------------------------------------------------------GPDGKDGERGPVGPA--------- 286

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 147904870  523 glpgppGKDGLPGASGVAGIRGEDGEIGLPGAPGAKGNPGEQGQPGAAGQPGLAG 577
Cdd:NF038329  287 ------GKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDG 335
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 623-679 2.65e-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: 54.04  E-value: 2.65e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 147904870   623 GLPGLPGAKGEQGNPGLPGLQGVKGDSGPPGPEGRQGLDGFPGPEGLRGEKGERGER 679
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 760-871 1.12e-08

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: 59.15  E-value: 1.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147904870  760 DGTLYTDPSKGEKGDQGLRGPAGSVGPYGQKGEIGFPGRPGRPGMNGLKGEKGECASSGSGLRGPPGPPGPPGPPGsvvn 839
Cdd:NF038329  107 DEGLQQLKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEA---- 182

                          90       100       110
                  ....*....|....*....|....*....|..
gi 147904870  840 GDQNIPGAyPGQKGERGFPGPQGDVGPAGPPG 871
Cdd:NF038329  183 GAKGPAGE-KGPQGPRGETGPAGEQGPAGPAG 213
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 533-579 5.85e-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: 5.85e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 147904870   533 LPGASGVAGIRGEDGEIGLPGAPGAKGNPGEQGQPGAAGQPGLAGLP 579
Cdd:pfam01391    2 PPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPP 48
 
Name Accession Description Interval E-value
Endostatin pfam06482
Collagenase NC10 and Endostatin; NC10 stands for Non-helical region 10 and is taken from Swiss: ...
 1133-1301 1.55e-113

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


Pssm-ID: 461931  Cd Length: 169  Bit Score: 352.13  E-value: 1.55e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147904870  1133 LHLVALNAPISGSMKSIRGVDFQCFEQARKAGLHGTFRAFLSSRLQDLYSIVRRADRQSVQIVNLRDEVLYDNWDSLFSG 1212
Cdd:pfam06482    1 LHLIALNTPQSGDMRGIRGADFLCFQQARAAGLKGTFRAFLSSRLQDLYSIVRKADRENVPIVNLKDEVLFDSWESIFSG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147904870  1213 SEAQMRSGARILSFDGKDVTTDPTWPQKMVWHGSDAKGRRLTESYCETWRTDESAVTGQASSLTSGKLLEQRPQSCNKNF 1292
Cdd:pfam06482   81 SGGQMKPNVPIYSFDGRDVLRDPAWPQKMVWHGSTSKGHRLTDNYCEAWRTGDQAVTGQASSLQSGKLLQQSPSSCSNSY 160


                   ....*....
gi 147904870  1293 IVLCIENSF 1301
Cdd:pfam06482  161 IVLCIENSY 169
Endostatin-like cd00247
Endostatin-like domain; the angiogenesis inhibitor endostatin is a C-terminal fragment of ...
 1130-1300 9.55e-111

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: 344.70  E-value: 9.55e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147904870 1130 NPALHLVALNAPISGSMKSIRGVDFQCFEQARKAGLHGTFRAFLSSRLQDLYSIVRRADRQSVQIVNLRDEVLYDNWDSL 1209
Cdd:cd00247     1 QPVLHLVALNTPLSGDMRGIRGADFQCFQQARAAGLKGTFRAFLSSRLQDLYSIVRRADRDSLPIVNLKGEVLFNSWESL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147904870 1210 FSGSEAQMRSGARILSFDGKDVTTDPTWPQKMVWHGSDAKGRRLTESYCETWRTDESAVTGQASSLTSGKLLEQRPQSCN 1289
Cdd:cd00247    81 FSGSGGQFNPGARIYSFDGRDVLTDPAWPQKMVWHGSDPNGRRLTDSYCEAWRTGDSAVTGQASSLSSGKLLEQKAYSCE 160

                         170
                  ....*....|.
gi 147904870 1290 KNFIVLCIENS 1300
Cdd:cd00247   161 NKLIVLCIENS 171
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 31-219 7.22e-32

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


Pssm-ID: 214560  Cd Length: 184  Bit Score: 123.24  E-value: 7.22e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147904870     31 EVGLLQLIGEP-VPNEITKVFGPDK-TPAYVFDKEANTGQVAQYHLPNPMYRDFSLLFHVQPSTNKAGILFAITDAsQSI 108
Cdd:smart00210    1 GQDLLQVFDLPsLSFAIRQVVGPEPgSPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPKSRGVLFAIYDA-QNV 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147904870    109 VYIGVKLsevkDGKQDII--FYYTEPGSQDSYVaatFNVPSL-VNRWSRFAISVEDEEVVLFMDCDELERVRFERSPDEM 185
Cdd:smart00210   80 RQFGLEV----DGRANTLllRYQGVDGKQHTVS---FRNLPLaDGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGQPP 152

                           170       180       190
                    ....*....|....*....|....*....|....
gi 147904870    186 elEDGSGLFVAQAGGADPDRYQGVIADLKIVANP 219
Cdd:smart00210  153 --IDTDGIEVRGAQAADRKPFQGDLQQLKIVCDP 184
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 620-813 1.33e-27

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: 117.70  E-value: 1.33e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147904870  620 GAQGLPGLPGAKGEQGNPGLPGLQGVKGDSGPPGPEGRQGLDGFPGPEGLRGEKGERGERGETGHDGVGIPGPPGPPGQv 699
Cdd:NF038329  138 GDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDG- 216

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147904870  700 lyVPSDDKSVVGAIPGPEGRQGIAGLPGPRGPKGDQGLDGFPGTHGAKGEKGEPGlmmrPDGtlytdpSKGEKGDQGLRG 779
Cdd:NF038329  217 --EAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAG----PDG------PDGKDGERGPVG 284

                         170       180       190
                  ....*....|....*....|....*....|....
gi 147904870  780 PAGSVGPYGQKGEIGFPGRPGRPGMNGLKGEKGE 813
Cdd:NF038329  285 PAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGK 318
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 502-753 1.25e-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: 108.84  E-value: 1.25e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147904870  502 GLPGPSGLPGLPGKEGIPGPPGLPGPPGKDGLPGASGVAG---IRGEDGEIGLPGAPGAKGNPGEQGQPGAAGQPGLAGL 578
Cdd:NF038329  132 GEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGpqgPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGP 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147904870  579 PGPMGPRGQPGPPGPPGPVSRGsaigfddmeasglgfglREGAQGLPGLPGAKGEQGNPGLPGLQGVKGDSGPPGPEGRQ 658
Cdd:NF038329  212 AGPDGEAGPAGEDGPAGPAGDG-----------------QQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPD 274

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147904870  659 GLDGFPGPEGLRGEKGERGERGETGHDgvgipgppgppgqvlyvpsddksvvgaipGPEGRQGIAGLPGPRGPKGDQGLD 738
Cdd:NF038329  275 GKDGERGPVGPAGKDGQNGKDGLPGKD-----------------------------GKDGQNGKDGLPGKDGKDGQPGKD 325

                         250
                  ....*....|....*
gi 147904870  739 GFPGTHGAKGEKGEP 753
Cdd:NF038329  326 GLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 641-871 8.41e-20

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 93.82  E-value: 8.41e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147904870  641 GLQGVKGDS--GPPGPEGRQGLDGFPGPEGLRGEKGERGERGEtghdgvgipgppgppgqvlyvpsddksvvgaiPGPEG 718
Cdd:NF038329  109 GLQQLKGDGekGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGP--------------------------------PGPQG 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147904870  719 RQGIAGLPGPRGPKGDQGLDGFPGTHGAKGEKGEPGlmmrPDGtlytdpSKGEKGDQGLRGPAGSVGPYGQKGEIGFPGR 798
Cdd:NF038329  157 ERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKG----PQG------PRGETGPAGEQGPAGPAGPDGEAGPAGEDGP 226

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 147904870  799 PGRPGmNGLKGEKGEcassgsglrgppgppgppgppgsvvngdqnipgaypgqKGERGFPGPQGDVGPAGPPG 871
Cdd:NF038329  227 AGPAG-DGQQGPDGD--------------------------------------PGPTGEDGPQGPDGPAGKDG 260
Collagen_trimer pfam20010
Collagen trimerization domain; This small domain mediate trimerization in various collagen ...
 994-1042 3.12e-17

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


Pssm-ID: 466257  Cd Length: 49  Bit Score: 76.49  E-value: 3.12e-17
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 147904870   994 ATVLQTHQTMINLAHRLQEGTIVLVQERAELYVRVREGFRRILLGEYTT 1042
Cdd:pfam20010    1 VTVFQNYDTMLQKTHRVPEGTLVYVREREELYIRVRNGWRKIQLGELIP 49
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 286-654 5.75e-15

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 78.79  E-value: 5.75e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147904870  286 QGIKGEKGDhGEKGERGLTGPKGdsasvspasdSNGEKGQKGEVGVKGSAG-FGYPGPKGQKGDPGtmgprgpagppgps 364
Cdd:NF038329  108 EGLQQLKGD-GEKGEPGPAGPAG----------PAGEQGPRGDRGETGPAGpAGPPGPQGERGEKG-------------- 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147904870  365 ilqksdgtsvrqvtgppgpqgpagPAGKDGEPGDPGEDGKTGEVGPQGFPGTPGDPGQKGEKGDTGvgmrgppglpgppg 444
Cdd:NF038329  163 ------------------------PAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAG-------------- 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147904870  445 ppgpaktdkltfidmegsgysgdlehvkgPPGLPGPPGPPGVPGLPGVPGTFGMNSTGLPGPSGLPGLPGKEGIPGPPGL 524
Cdd:NF038329  205 -----------------------------EQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGP 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147904870  525 PGPPGKDGLPGASGVAGIRGEDGEIGLPGAPGAKGNPGEQGQPGAAGQPGlaglpgpmgprgqpgppgppgpvsrgsaig 604
Cdd:NF038329  256 AGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDG------------------------------ 305

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 147904870  605 fddmeasglgfglREGAQGLPGLPGAKGEQGNPGLPGLQGVKGDSGPPGP 654
Cdd:NF038329  306 -------------QNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 284-577 6.99e-15

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 78.79  E-value: 6.99e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147904870  284 GQQGIKGEKGDHGEKGERGLTGPKGDSASVSPAsdsnGEKGQKGEVGVKGSAGfgYPGPKGQKGDPGTMGPRGPAGPPGP 363
Cdd:NF038329  141 GETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ----GPAGKDGEAGAKGPAG--EKGPQGPRGETGPAGEQGPAGPAGP 214

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147904870  364 SILQKSDGtsvrqvtgpPGPQGPAGPAGKDGEPGDPGEDGKTGEVGPQGFPGTPGDPGQKGEKGDTGvgmrgppglpgpp 443
Cdd:NF038329  215 DGEAGPAG---------EDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDG------------- 272

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147904870  444 gppgpaktdkltfidmegsgysgdlehvkgppglpgppgppgvpglpgvpgtfgmnSTGLPGPSGLPGLPGKEGIPGPPg 523
Cdd:NF038329  273 --------------------------------------------------------PDGKDGERGPVGPAGKDGQNGKD- 295

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 147904870  524 lpgppgkdglpGASGVAGIRGEDGEIGLPGAPGAKGNPGEQGQPGAAGQPGLAG 577
Cdd:NF038329  296 -----------GLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 283-577 7.08e-14

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 75.71  E-value: 7.08e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147904870  283 QGQQGIKGEKGDHGEKGERGLTGPKGDSASVSPAsdsnGEKGQKGEVGVKGSAGfgYPGPKGQKGDPGTMGPRGPAGPPG 362
Cdd:NF038329  128 AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEK----GPAGPQGEAGPQGPAG--KDGEAGAKGPAGEKGPQGPRGETG 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147904870  363 PSILQKSDGTSVRQVTGPPGPQGPAGPAGKDGEPGDPGEDGKTGEVGPQGFPGTPGDPGQKGEKGDTGVGmrgppglpgp 442
Cdd:NF038329  202 PAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPD---------- 271

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147904870  443 pgppgpaktdkltfidmegsgysgdlehvkgppglpgppgppgvpglpgvpgtfgmNSTGLPGPSGLPGLPgkegipgpp 522
Cdd:NF038329  272 --------------------------------------------------------GPDGKDGERGPVGPA--------- 286

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 147904870  523 glpgppGKDGLPGASGVAGIRGEDGEIGLPGAPGAKGNPGEQGQPGAAGQPGLAG 577
Cdd:NF038329  287 ------GKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDG 335
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 623-679 2.65e-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: 54.04  E-value: 2.65e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 147904870   623 GLPGLPGAKGEQGNPGLPGLQGVKGDSGPPGPEGRQGLDGFPGPEGLRGEKGERGER 679
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 620-676 4.08e-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: 4.08e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 147904870   620 GAQGLPGLPGAKGEQGNPGLPGLQGVKGDSGPPGPEGRQGLDGFPGPEGLRGEKGER 676
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 626-681 6.85e-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: 52.88  E-value: 6.85e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 147904870   626 GLPGAKGEQGNPGLPGLQGVKGDSGPPGPEGRQGLDGFPGPEGLRGEKGERGERGE 681
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 760-871 1.12e-08

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: 59.15  E-value: 1.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147904870  760 DGTLYTDPSKGEKGDQGLRGPAGSVGPYGQKGEIGFPGRPGRPGMNGLKGEKGECASSGSGLRGPPGPPGPPGPPGsvvn 839
Cdd:NF038329  107 DEGLQQLKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEA---- 182

                          90       100       110
                  ....*....|....*....|....*....|..
gi 147904870  840 GDQNIPGAyPGQKGERGFPGPQGDVGPAGPPG 871
Cdd:NF038329  183 GAKGPAGE-KGPQGPRGETGPAGEQGPAGPAG 213
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 533-579 5.85e-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: 5.85e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 147904870   533 LPGASGVAGIRGEDGEIGLPGAPGAKGNPGEQGQPGAAGQPGLAGLP 579
Cdd:pfam01391    2 PPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPP 48
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 714-754 1.59e-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: 40.55  E-value: 1.59e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 147904870   714 PGPEGRQGIAGLPGPRGPKGDQGLDGFPGTHGAKGEKGEPG 754
Cdd:pfam01391   12 PGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPG 52
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 665-753 3.05e-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: 3.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147904870   665 GPEGLRGEKGERGERGEtghdgvgipgppgppgqvlyvpsddksvvgaiPGPEGRQGIAGLPGPRGPKGDQGLDGFPGTH 744
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGP--------------------------------PGPPGPPGPPGPPGEPGPPGPPGPPGPPGPP 48


                   ....*....
gi 147904870   745 GAKGEKGEP 753
Cdd:pfam01391   49 GAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 508-573 4.56e-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: 39.40  E-value: 4.56e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 147904870   508 GLPGLPGkegipgppgLPGPPGKDGLPGASGVAGIRGEDGEIGLPGAPGAKGNPGEQGQPGAAGQP 573
Cdd:pfam01391    1 GPPGPPG---------PPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 715-786 5.34e-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: 39.40  E-value: 5.34e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 147904870   715 GPEGRQGIAGLPGPRGPKGDQgldGFPGTHGAKGEKGEPGlmmrpdgtlytdpSKGEKGDQGLRGPAGSVGP 786
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPP---GPPGPPGPPGEPGPPG-------------PPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 394-430 2.04e-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: 37.47  E-value: 2.04e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 147904870   394 GEPGDPGEDGKTGEVGPQGFPGTPGDPGQKGEKGDTG 430
Cdd:pfam01391   19 GPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 770-813 5.62e-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: 5.62e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 147904870   770 GEKGDQGLRGPAGSVGPYGQKGEIGFPGRPGRPGMNGLKGEKGE 813
Cdd:pfam01391    4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGP 47
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 773-870 8.09e-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: 35.93  E-value: 8.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147904870   773 GDQGLRGPAGSVGPYGQKGEIGFPGRPGRPGMNGLkgekgecassgsglrgppgppgppgppgsvvngdqnipgayPGQK 852
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGP-----------------------------------------PGPP 39

                           90
                   ....*....|....*...
gi 147904870   853 GERGFPGPQGDVGPAGPP 870
Cdd:pfam01391   40 GPPGPPGPPGAPGAPGPP 57
 
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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