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Conserved domains on  [gi|767952615|ref|XP_011515188|]
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collagen alpha-1(XXII) chain isoform X4 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 36-190 5.47e-43

Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains.


The actual alignment was detected with superfamily member cd01475:

Pssm-ID: 469594 [Multi-domain]  Cd Length: 224  Bit Score: 156.78  E-value: 5.47e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615   36 HYDLVFLLDTSSSVGKEDFEKVRQWVANLVDTFE-----------------------------EEVKAAARRLAYHGGNT 86
Cdd:cd01475     2 PTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDvgpdatrvglvqysstvkqefplgrfkskADLKRAVRRMEYLETGT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615   87 NTGDALRYITARSFSPHAGGRPRDRAYKQVAILLTDGRSQDLVLDAAAAAHRAGIRIFAVGVGEALKEELEEIASEPKSA 166
Cdd:cd01475    82 MTGLAIQYAMNNAFSEAEGARPGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLAD 161

                         170       180
                  ....*....|....*....|....
gi 767952615  167 HVFHVSDFNAIDKIRGKLRRRLCE 190
Cdd:cd01475   162 HVFYVEDFSTIEELTKKFQGKICV 185
LamG super family cl22861
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 210-397 4.61e-33

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: 126.70  E-value: 4.61e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615    210 GTKEITGFDLMDL-FSVKEILGKRenGAQSSYvRMGSFPVV-QSTEDVFPQGLPDEYAFVTTFRFRKTSRkedWYIWQVI 287
Cdd:smart00210    1 GQDLLQVFDLPSLsFAIRQVVGPE--PGSPAY-RLGDPALVpQPTRDLFPSGLPEDFSLLTTFRQTPKSR---GVLFAIY 74

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615    288 DQYSIPQVSIRLDGENKAVEYNAVGAMKDAVRVVFRGSrvnDLFDRDWHKMALSIQAQNVSLHIDCALVQTLPIEER--E 365
Cdd:smart00210   75 DAQNVRQFGLEVDGRANTLLLRYQGVDGKQHTVSFRNL---PLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPgqP 151

                           170       180       190
                    ....*....|....*....|....*....|..
gi 767952615    366 NIDIQGKTVIGKRLYDSVPIDFDLQRIVIYCD 397
Cdd:smart00210  152 PIDTDGIEVRGAQAADRKPFQGDLQQLKIVCD 183
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 452-674 1.19e-28

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: 121.17  E-value: 1.19e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615  452 GEKGEMGVAGPMGLPGPKGDIGAIGPVGAPGPKGEKGDVGI----GPFG----QGEKGEKGSLGLPGPPGRDGSKGMRGE 523
Cdd:NF038329  120 GEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEkgpaGPQGeagpQGPAGKDGEAGAKGPAGEKGPQGPRGE 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615  524 PGELGEPGLPGEVGMRGPQGPPGLPGPPGRVGaPGLQGERGEKGTRGEKGERGLDGFPGKPGDTGQQGRPGPSGVAGPQG 603
Cdd:NF038329  200 TGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDG 278

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767952615  604 EKGDVGPAGPPGvpgsvvqQEGLKGEQGAPGPRGHQGAPGPPGARGPIGPEGRDGPPGLQGLRGKKGDMGP 674
Cdd:NF038329  279 ERGPVGPAGKDG-------QNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 769-1048 2.33e-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.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 99.21  E-value: 2.33e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615  769 GEKGEAGLPGAPGFPGVRGEKGDQGEKGELGLPGLKGDRGEKGEagpagppglpgttslftphprmPGEQGPKGEKGDPG 848
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGE----------------------KGPAGPQGEAGPQG 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615  849 LPGEPGLQGrpgelgpqgptgppgakgqegahgapgaagnpgapghvgapgpsgppgsvgAPGLRGTPGKDGERGEKGAA 928
Cdd:NF038329  175 PAGKDGEAG---------------------------------------------------AKGPAGEKGPQGPRGETGPA 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615  929 GEEGSPGPVGPRGDPGAPGLPGPPGKGKDGEPGLRGSPGLPGPLGTKGDRGAPGIPGSPGSRGDPGIGVAGPPGPSGPPG 1008
Cdd:NF038329  204 GEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPV 283

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 767952615 1009 DK----GSPGSRGLPGFPGPQGPAGRDGAPGNPGERGPPGKPGL 1048
Cdd:NF038329  284 GPagkdGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGL 327
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1121-1337 3.99e-18

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: 89.19  E-value: 3.99e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615 1121 QGERGADGEVGQKGDQGHPGVPGFMGPPGNPGPPGADGIAGAAGPPGIQGSPGKEGPPGPQGPSGLPGIPGEEGKEGRDG 1200
Cdd:NF038329  131 AGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAG 210

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615 1201 KPGPPGEPGKAGEPGLPGPEGA--RGPPGFKGHTGDSGAPGPRGESGAMGLPGQEGLPGKDGDTGPtgpqgpqgpRGPPG 1278
Cdd:NF038329  211 PAGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK---------DGERG 281

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767952615 1279 KNGSPGSPGEPGPSGTPGQKGSKGENGSPGLPGFLGPRGPPGEPGEKGVPGKEGVPGKP 1337
Cdd:NF038329  282 PVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1239-1535 6.71e-13

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


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 72.63  E-value: 6.71e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615 1239 GPRGESGAMGLPGQEGLPGKDGDTGPTGPQGPQGPRGPPGKNGSPGSPGEPGPSGTPGQKGSKGENGSPGLPGFLGPRGP 1318
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615 1319 PGEPGEKGVPGKEGVPGKPGEPGFKGERGDPGIKGDKGPPGGkgqpgdpgipGHKGHTGLMGPQGLPGENGPVGPPGPPG 1398
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPD----------GDPGPTGEDGPQGPDGPAGKDGPRGDRG 266

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615 1399 QPGFPGLRGESpsmetlrrliqeelgkqletrlayllaqmppaymkssqgrpgppgppgkdglpGRAGPMGEPGRPGQGG 1478
Cdd:NF038329  267 EAGPDGPDGKD-----------------------------------------------------GERGPVGPAGKDGQNG 293

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767952615 1479 LEGPSGPIGPKGERGAKGDPGAPGvglrgemGPPGIPGQPGEPGYAKDGLPGIPGPQ 1535
Cdd:NF038329  294 KDGLPGKDGKDGQNGKDGLPGKDG-------KDGQPGKDGLPGKDGKDGQPGKPAPK 343
 
Name Accession Description Interval E-value
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 36-190 5.47e-43

VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and matrix-matrix interactions thereby providing tissue integrity. Some members of the matrilin family are expressed specifically in developing cartilage rudiments. The matrilin family consists of at least four members. All the members of the matrilin family contain VWA domains, EGF-like domains and a heptad repeat coiled-coiled domain at the carboxy terminus which is responsible for the oligomerization of the matrilins. The VWA domains have been shown to be essential for matrilin network formation by interacting with matrix ligands.


Pssm-ID: 238752 [Multi-domain]  Cd Length: 224  Bit Score: 156.78  E-value: 5.47e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615   36 HYDLVFLLDTSSSVGKEDFEKVRQWVANLVDTFE-----------------------------EEVKAAARRLAYHGGNT 86
Cdd:cd01475     2 PTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDvgpdatrvglvqysstvkqefplgrfkskADLKRAVRRMEYLETGT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615   87 NTGDALRYITARSFSPHAGGRPRDRAYKQVAILLTDGRSQDLVLDAAAAAHRAGIRIFAVGVGEALKEELEEIASEPKSA 166
Cdd:cd01475    82 MTGLAIQYAMNNAFSEAEGARPGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLAD 161

                         170       180
                  ....*....|....*....|....
gi 767952615  167 HVFHVSDFNAIDKIRGKLRRRLCE 190
Cdd:cd01475   162 HVFYVEDFSTIEELTKKFQGKICV 185
VWA pfam00092
von Willebrand factor type A domain;
38-183 7.33e-37

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 137.41  E-value: 7.33e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615    38 DLVFLLDTSSSVGKEDFEKVRQWVANLVDTFE-----------------------------EEVKAAARRLAYHGGNT-N 87
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDigpdgtrvglvqyssdvrtefplndysskEELLSAVDNLRYLGGGTtN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615    88 TGDALRYITARSFSPHAGGRPRdraYKQVAILLTDGRSQDL-VLDAAAAAHRAGIRIFAVGVGEALKEELEEIASEPKSA 166
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPG---APKVVVLLTDGRSQDGdPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEG 157

                          170
                   ....*....|....*..
gi 767952615   167 HVFHVSDFNAIDKIRGK 183
Cdd:pfam00092  158 HVFTVSDFEALEDLQDQ 174
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 210-397 4.61e-33

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


Pssm-ID: 214560  Cd Length: 184  Bit Score: 126.70  E-value: 4.61e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615    210 GTKEITGFDLMDL-FSVKEILGKRenGAQSSYvRMGSFPVV-QSTEDVFPQGLPDEYAFVTTFRFRKTSRkedWYIWQVI 287
Cdd:smart00210    1 GQDLLQVFDLPSLsFAIRQVVGPE--PGSPAY-RLGDPALVpQPTRDLFPSGLPEDFSLLTTFRQTPKSR---GVLFAIY 74

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615    288 DQYSIPQVSIRLDGENKAVEYNAVGAMKDAVRVVFRGSrvnDLFDRDWHKMALSIQAQNVSLHIDCALVQTLPIEER--E 365
Cdd:smart00210   75 DAQNVRQFGLEVDGRANTLLLRYQGVDGKQHTVSFRNL---PLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPgqP 151

                           170       180       190
                    ....*....|....*....|....*....|..
gi 767952615    366 NIDIQGKTVIGKRLYDSVPIDFDLQRIVIYCD 397
Cdd:smart00210  152 PIDTDGIEVRGAQAADRKPFQGDLQQLKIVCD 183
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 452-674 1.19e-28

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: 121.17  E-value: 1.19e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615  452 GEKGEMGVAGPMGLPGPKGDIGAIGPVGAPGPKGEKGDVGI----GPFG----QGEKGEKGSLGLPGPPGRDGSKGMRGE 523
Cdd:NF038329  120 GEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEkgpaGPQGeagpQGPAGKDGEAGAKGPAGEKGPQGPRGE 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615  524 PGELGEPGLPGEVGMRGPQGPPGLPGPPGRVGaPGLQGERGEKGTRGEKGERGLDGFPGKPGDTGQQGRPGPSGVAGPQG 603
Cdd:NF038329  200 TGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDG 278

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767952615  604 EKGDVGPAGPPGvpgsvvqQEGLKGEQGAPGPRGHQGAPGPPGARGPIGPEGRDGPPGLQGLRGKKGDMGP 674
Cdd:NF038329  279 ERGPVGPAGKDG-------QNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 38-180 5.41e-27

von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 109.08  E-value: 5.41e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615     38 DLVFLLDTSSSVGKEDFEKVRQWVANLVDTFE-----------------------------EEVKAAARRLAYH-GGNTN 87
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDigpdgdrvglvtfsddarvlfplndsrskDALLEALASLSYKlGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615     88 TGDALRYITARSFSPHAGGRPRDRaykQVAILLTDGRSQDL---VLDAAAAAHRAGIRIFAVGVGEA-LKEELEEIASEP 163
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAP---KVVILITDGESNDGpkdLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLASAP 157

                           170
                    ....*....|....*..
gi 767952615    164 KSAHVFHVSDFNAIDKI 180
Cdd:smart00327  158 GGVYVFLPELLDLLIDL 174
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 501-793 5.66e-26

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: 113.08  E-value: 5.66e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615  501 GEKGSLGLPGPPGRDGSKGMRGEPGELGEPGLPGEVGMRgpqgppglpGPPGRVGAPGLQGERGEKGTRGEKGERGLDGF 580
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQ---------GERGEKGPAGPQGEAGPQGPAGKDGEAGAKGP 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615  581 PGKPGDTGQQGRPGPSGVAGPQGEKG-DVGPAGPPGVPGSVVQQEGLKGEQGAPGPRGHQGAPGPPGARGPIGPEGRDGP 659
Cdd:NF038329  188 AGEKGPQGPRGETGPAGEQGPAGPAGpDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGE 267

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615  660 PGLQGLRGKKGDMGPPGipgllglqgppgppgvpgppgpggspglpgeigfpgkpgppgptgppgkdgpngppgppgTKG 739
Cdd:NF038329  268 AGPDGPDGKDGERGPVG------------------------------------------------------------PAG 287

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767952615  740 EPGERGEDGLPGKPGLRGEIGEQGLagrPGEKGEAGLPGAPGFPGVRGEKGDQG 793
Cdd:NF038329  288 KDGQNGKDGLPGKDGKDGQNGKDGL---PGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 769-1048 2.33e-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: 99.21  E-value: 2.33e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615  769 GEKGEAGLPGAPGFPGVRGEKGDQGEKGELGLPGLKGDRGEKGEagpagppglpgttslftphprmPGEQGPKGEKGDPG 848
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGE----------------------KGPAGPQGEAGPQG 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615  849 LPGEPGLQGrpgelgpqgptgppgakgqegahgapgaagnpgapghvgapgpsgppgsvgAPGLRGTPGKDGERGEKGAA 928
Cdd:NF038329  175 PAGKDGEAG---------------------------------------------------AKGPAGEKGPQGPRGETGPA 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615  929 GEEGSPGPVGPRGDPGAPGLPGPPGKGKDGEPGLRGSPGLPGPLGTKGDRGAPGIPGSPGSRGDPGIGVAGPPGPSGPPG 1008
Cdd:NF038329  204 GEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPV 283

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 767952615 1009 DK----GSPGSRGLPGFPGPQGPAGRDGAPGNPGERGPPGKPGL 1048
Cdd:NF038329  284 GPagkdGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGL 327
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 450-660 1.43e-19

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: 93.43  E-value: 1.43e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615  450 PAGEKGEMGVAGPMGLPGPKGDIGAIGPVGAPGPKGEKGDVG----IGPFG-QGEKGEKGSLGLPGPPGRDGS--KGMRG 522
Cdd:NF038329  160 EKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGpageQGPAGpAGPDGEAGPAGEDGPAGPAGDgqQGPDG 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615  523 EPGELGEPGLPGEVGMRGPQGPPGLPGPPGRVGAPGLQGERGEKGTRGEKGERGLDGFPGKPGDTGQQGRPGPSGVAGpq 602
Cdd:NF038329  240 DPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDG-- 317

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767952615  603 gekgdvgpagppgvpgsvvqQEGLKGEQGAPGPRGHQGAPGPPGARGPIGPEGRDGPP 660
Cdd:NF038329  318 --------------------KDGQPGKDGLPGKDGKDGQPGKPAPKTPEVPQKPDTAP 355
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 624-994 1.83e-19

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: 93.43  E-value: 1.83e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615  624 EGLKGEQGAPGPRGHQGAPGPPGARGPIGPEGRDGPPGLQGLRGKKGDMGPPGipgllglqgppgppgvpgppgpggspg 703
Cdd:NF038329  116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQG--------------------------- 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615  704 lpgeigfpgkpgppgptgppgkdgpngppgppgtkgEPGERGEDGLPGKPGLRGEIGEQGLAGRPGEKGEAGLPGAPGFP 783
Cdd:NF038329  169 ------------------------------------EAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPA 212

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615  784 GVRGEKGDQGEKGELGLPGlKGDRGEKGEagpagppglpgttslftphprmPGEQGPKGEKGDPGLPGEPGLQGRPGElg 863
Cdd:NF038329  213 GPDGEAGPAGEDGPAGPAG-DGQQGPDGD----------------------PGPTGEDGPQGPDGPAGKDGPRGDRGE-- 267

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615  864 pqgptgppgakgqegahgapgaagnpgapghvgapgpsgppgsvgaPGLRGTPGKDGERGEKGAAGEEGSPGPVGPrgdp 943
Cdd:NF038329  268 ----------------------------------------------AGPDGPDGKDGERGPVGPAGKDGQNGKDGL---- 297

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767952615  944 gapglpgppgKGKDGEPGLRGSPGLPGPLGTKGDRGAPGIPGSPGSRGDPG 994
Cdd:NF038329  298 ----------PGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1121-1337 3.99e-18

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: 89.19  E-value: 3.99e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615 1121 QGERGADGEVGQKGDQGHPGVPGFMGPPGNPGPPGADGIAGAAGPPGIQGSPGKEGPPGPQGPSGLPGIPGEEGKEGRDG 1200
Cdd:NF038329  131 AGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAG 210

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615 1201 KPGPPGEPGKAGEPGLPGPEGA--RGPPGFKGHTGDSGAPGPRGESGAMGLPGQEGLPGKDGDTGPtgpqgpqgpRGPPG 1278
Cdd:NF038329  211 PAGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK---------DGERG 281

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767952615 1279 KNGSPGSPGEPGPSGTPGQKGSKGENGSPGLPGFLGPRGPPGEPGEKGVPGKEGVPGKP 1337
Cdd:NF038329  282 PVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1121-1350 1.87e-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: 83.80  E-value: 1.87e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615 1121 QGERGADGEVGQKGDQGHPGVPGFMGPPGNPGPPGADGIAGAAGPPGIQGSpgkegppgpqgpsglpgiPGEEGKEGRDG 1200
Cdd:NF038329  119 KGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGE------------------AGPQGPAGKDG 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615 1201 KPGPPGEPGKAGEPGLPGPEGARGPPGFKGHTGDSGAPGPRGESGAMGLPGQeGLPGKDGDTGPTGPQGPQGPRGPPGKN 1280
Cdd:NF038329  181 EAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKD 259

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615 1281 GSPGSPGEPGPSGTPGQKGSKGENGSPGLPGFLGPRGPPGEPGEKGVPGKEGVPGKPGEPGFKGERGDPG 1350
Cdd:NF038329  260 GPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPG 329
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 919-1219 1.52e-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: 81.10  E-value: 1.52e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615  919 DGERGEKGAAGEEGSPGPVGPRGdpgapglpgppgkgKDGEPGLRGSPGLPGPLGTKGDRGAPGIPGSPGSRGDPGigva 998
Cdd:NF038329  116 DGEKGEPGPAGPAGPAGEQGPRG--------------DRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAG---- 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615  999 gppgpsgppgDKGSPGSRGLPGFPGPQGPAGRDGAPGNPGERGPPGKPGLSSLLSPgdinllakdvcndcppGPPGLPGL 1078
Cdd:NF038329  178 ----------KDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGE----------------DGPAGPAG 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615 1079 PGFKGDKGVPGKPGREGTEGKKGEAGPPGLPGPPGIAGPQGSQGERGADGEVGQKGDQGHPGvpgfmgppgnpgppgadg 1158
Cdd:NF038329  232 DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNG------------------ 293

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767952615 1159 iagAAGPPGiqgspgkegPPGPQGPSGLPGIPGEEGKEGRDGKPGPPGEPGKAGEPGLPGP 1219
Cdd:NF038329  294 ---KDGLPG---------KDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1191-1384 4.54e-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: 79.56  E-value: 4.54e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615 1191 GEEGKEGRDGKPGPPGEPGKAGEPGLPGPEGARGPPGFKGHTGDSGAPGPRGESGAMGLPGQEGLPGKDGDTGPTGPQGP 1270
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615 1271 QGPRGPPGKNGSPGSPGEPGPSGTPGQKGSKG-----ENGSPGLPGflgPRGPPGEPGEKGVPGKEGVPGKPGEPGFKGE 1345
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGpagdgQQGPDGDPG---PTGEDGPQGPDGPAGKDGPRGDRGEAGPDGP 273

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 767952615 1346 RGDPGIKGDKGPPGGKGQPGDPGIPGHKGHTGLMGPQGL 1384
Cdd:NF038329  274 DGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGL 312
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1239-1535 6.71e-13

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 72.63  E-value: 6.71e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615 1239 GPRGESGAMGLPGQEGLPGKDGDTGPTGPQGPQGPRGPPGKNGSPGSPGEPGPSGTPGQKGSKGENGSPGLPGFLGPRGP 1318
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615 1319 PGEPGEKGVPGKEGVPGKPGEPGFKGERGDPGIKGDKGPPGGkgqpgdpgipGHKGHTGLMGPQGLPGENGPVGPPGPPG 1398
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPD----------GDPGPTGEDGPQGPDGPAGKDGPRGDRG 266

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615 1399 QPGFPGLRGESpsmetlrrliqeelgkqletrlayllaqmppaymkssqgrpgppgppgkdglpGRAGPMGEPGRPGQGG 1478
Cdd:NF038329  267 EAGPDGPDGKD-----------------------------------------------------GERGPVGPAGKDGQNG 293

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767952615 1479 LEGPSGPIGPKGERGAKGDPGAPGvglrgemGPPGIPGQPGEPGYAKDGLPGIPGPQ 1535
Cdd:NF038329  294 KDGLPGKDGKDGQNGKDGLPGKDG-------KDGQPGKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1212-1544 7.83e-12

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: 69.55  E-value: 7.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615 1212 GEPGLPGPEGARGPPGFKGHTGDSGAPGPRGESGAMGLPGQEGLPGKDGDTGPTgpqgpqgprgppgknGSPGSPGEPGP 1291
Cdd:NF038329  120 GEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ---------------GPAGKDGEAGA 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615 1292 SGTPGQKGSKGENGSPGlpgflgprgppgepgEKGVPGKEGVPGKPGEPGFKGERGDPGIKGDKGPPGGkgqpgdpgipG 1371
Cdd:NF038329  185 KGPAGEKGPQGPRGETG---------------PAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPD----------G 239

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615 1372 HKGHTGLMGPQGLPGENGPVGPPGPPGQPGFPGLRGESpsmetlrrliqeelgkqletrlayllaqmppaymkssqgrpg 1451
Cdd:NF038329  240 DPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKD------------------------------------------ 277

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615 1452 ppgppgkdglpGRAGPMGEPGRPGQGGLEGPSGPIGPKGERGAKGDPGAPGvglrgemgppgipgqpgepgyaKDGLPGI 1531
Cdd:NF038329  278 -----------GERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDG----------------------KDGQPGK 324

                         330
                  ....*....|...
gi 767952615 1532 PGPQGETGPAGHP 1544
Cdd:NF038329  325 DGLPGKDGKDGQP 337
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 2-180 6.06e-10

vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and metabolism];


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 61.88  E-value: 6.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615    2 AGLRGNAVAGLLWMLLLWSGGGGCQAQRAGCKSVHYDLVFLLDTSSSVGKED-FEKVRQWVANLVDTFEEE--------- 71
Cdd:COG1240    58 LLALLLAALLLLLAVLLLLLALALAPLALARPQRGRDVVLVVDASGSMAAENrLEAAKGALLDFLDDYRPRdrvglvafg 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615   72 ------------VKAAARRLAY--HGGNTNTGDALRYITARsfsphagGRPRDRAYKQVAILLTDGR---SQDLVLDAAA 134
Cdd:COG1240   138 geaevllpltrdREALKRALDElpPGGGTPLGDALALALEL-------LKRADPARRKVIVLLTDGRdnaGRIDPLEAAE 210

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 767952615  135 AAHRAGIRIFAVGVG-EALKEE-LEEIASEpKSAHVFHVSDFNAIDKI 180
Cdd:COG1240   211 LAAAAGIRIYTIGVGtEAVDEGlLREIAEA-TGGRYFRADDLSELAAI 257
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 748-802 4.45e-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: 4.45e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 767952615   748 GLPGKPGLRGEIGEQGLAGRPGEKGEAGLPGAPGFPGVRGEKGDQGEKGELGLPG 802
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
482-676 1.63e-04

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 46.18  E-value: 1.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615  482 GPKGEKGDVGIGPFGQGekGEKGSLGLPGPPGRDGSKGMRGEPGELGEPGLPGEVGMRGPQGPPGLPGPPGRVGAPGLQG 561
Cdd:COG5164     2 GLYGPGKTGPSDPGGVT--TPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615  562 ERGEKGTRGEKGERGLDGFPGKPGDTGQQGRPGPSGVAGPQGEKG-----DVGPAGPPGVPGSVVQQEGLKGEQGAPGPR 636
Cdd:COG5164    80 GTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGsttppSGGSTTPPGDGGSTPPGPGSTGPGGSTTPP 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 767952615  637 GHQGA---PGPPGARGPIGPEGRDGPP--GLQGLRGKKGDMGPPG 676
Cdd:COG5164   160 GDGGSttpPGPGGSTTPPDDGGSTTPPnkGETGTDIPTGGTPRQG 204
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1212-1264 2.02e-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: 2.02e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 767952615  1212 GEPGLPGPEGARGPPGFKGHTGDSGAPGPRGESGAMGLPGQEGLPGKDGDTGP 1264
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGA 53
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 625-677 2.91e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.17  E-value: 2.91e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 767952615   625 GLKGEQGAPGPRGHQGAPGPPGARGPIGPEGRDGPPGLQGLRGKKGDMGPPGI 677
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGA 53
 
Name Accession Description Interval E-value
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 36-190 5.47e-43

VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and matrix-matrix interactions thereby providing tissue integrity. Some members of the matrilin family are expressed specifically in developing cartilage rudiments. The matrilin family consists of at least four members. All the members of the matrilin family contain VWA domains, EGF-like domains and a heptad repeat coiled-coiled domain at the carboxy terminus which is responsible for the oligomerization of the matrilins. The VWA domains have been shown to be essential for matrilin network formation by interacting with matrix ligands.


Pssm-ID: 238752 [Multi-domain]  Cd Length: 224  Bit Score: 156.78  E-value: 5.47e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615   36 HYDLVFLLDTSSSVGKEDFEKVRQWVANLVDTFE-----------------------------EEVKAAARRLAYHGGNT 86
Cdd:cd01475     2 PTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDvgpdatrvglvqysstvkqefplgrfkskADLKRAVRRMEYLETGT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615   87 NTGDALRYITARSFSPHAGGRPRDRAYKQVAILLTDGRSQDLVLDAAAAAHRAGIRIFAVGVGEALKEELEEIASEPKSA 166
Cdd:cd01475    82 MTGLAIQYAMNNAFSEAEGARPGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLAD 161

                         170       180
                  ....*....|....*....|....
gi 767952615  167 HVFHVSDFNAIDKIRGKLRRRLCE 190
Cdd:cd01475   162 HVFYVEDFSTIEELTKKFQGKICV 185
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 38-174 9.86e-39

von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This domain has a variety of functions including: intermolecular adhesion, cell migration, signalling, transcription, and DNA repair. In integrins these domains form heterodimers while in vWF it forms homodimers and multimers. There are different interaction surfaces of this domain as seen by its complexes with collagen with either integrin or human vWFA. In integrins collagen binding occurs via the metal ion-dependent adhesion site (MIDAS) and involves three surface loops located on the upper surface of the molecule. In human vWFA, collagen binding is thought to occur on the bottom of the molecule and does not involve the vestigial MIDAS motif.


Pssm-ID: 238749 [Multi-domain]  Cd Length: 164  Bit Score: 142.37  E-value: 9.86e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615   38 DLVFLLDTSSSVGKEDFEKVRQWVANLVDTFE-----------------------------EEVKAAARRLAYHGGNTNT 88
Cdd:cd01472     2 DIVFLVDGSESIGLSNFNLVKDFVKRVVERLDigpdgvrvgvvqysddprtefylntyrskDDVLEAVKNLRYIGGGTNT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615   89 GDALRYITARSFSPHAGGRPrdrAYKQVAILLTDGRSQDLVLDAAAAAHRAGIRIFAVGVGEALKEELEEIASEPKSAHV 168
Cdd:cd01472    82 GKALKYVRENLFTEASGSRE---GVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKELYV 158


                  ....*.
gi 767952615  169 FHVSDF 174
Cdd:cd01472   159 FNVADF 164
VWA pfam00092
von Willebrand factor type A domain;
38-183 7.33e-37

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 137.41  E-value: 7.33e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615    38 DLVFLLDTSSSVGKEDFEKVRQWVANLVDTFE-----------------------------EEVKAAARRLAYHGGNT-N 87
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDigpdgtrvglvqyssdvrtefplndysskEELLSAVDNLRYLGGGTtN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615    88 TGDALRYITARSFSPHAGGRPRdraYKQVAILLTDGRSQDL-VLDAAAAAHRAGIRIFAVGVGEALKEELEEIASEPKSA 166
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPG---APKVVVLLTDGRSQDGdPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEG 157

                          170
                   ....*....|....*..
gi 767952615   167 HVFHVSDFNAIDKIRGK 183
Cdd:pfam00092  158 HVFTVSDFEALEDLQDQ 174
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 38-174 6.20e-36

Collagen: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions.


Pssm-ID: 238759 [Multi-domain]  Cd Length: 164  Bit Score: 134.34  E-value: 6.20e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615   38 DLVFLLDTSSSVGKEDFEKVRQWVANLVDTFE-----------------------------EEVKAAARRLAYHGGNTNT 88
Cdd:cd01482     2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEigpdgvqvglvqysddprtefdlnaytskEDVLAAIKNLPYKGGNTRT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615   89 GDALRYITARSFSPHAGGRPRDRaykQVAILLTDGRSQDLVLDAAAAAHRAGIRIFAVGVGEALKEELEEIASEPKSAHV 168
Cdd:cd01482    82 GKALTHVREKNFTPDAGARPGVP---KVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHV 158


                  ....*.
gi 767952615  169 FHVSDF 174
Cdd:cd01482   159 FNVADF 164
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 210-397 4.61e-33

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


Pssm-ID: 214560  Cd Length: 184  Bit Score: 126.70  E-value: 4.61e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615    210 GTKEITGFDLMDL-FSVKEILGKRenGAQSSYvRMGSFPVV-QSTEDVFPQGLPDEYAFVTTFRFRKTSRkedWYIWQVI 287
Cdd:smart00210    1 GQDLLQVFDLPSLsFAIRQVVGPE--PGSPAY-RLGDPALVpQPTRDLFPSGLPEDFSLLTTFRQTPKSR---GVLFAIY 74

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615    288 DQYSIPQVSIRLDGENKAVEYNAVGAMKDAVRVVFRGSrvnDLFDRDWHKMALSIQAQNVSLHIDCALVQTLPIEER--E 365
Cdd:smart00210   75 DAQNVRQFGLEVDGRANTLLLRYQGVDGKQHTVSFRNL---PLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPgqP 151

                           170       180       190
                    ....*....|....*....|....*....|..
gi 767952615    366 NIDIQGKTVIGKRLYDSVPIDFDLQRIVIYCD 397
Cdd:smart00210  152 PIDTDGIEVRGAQAADRKPFQGDLQQLKIVCD 183
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 37-169 5.98e-32

Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains


Pssm-ID: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 122.79  E-value: 5.98e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615   37 YDLVFLLDTSSSVGKEDFEKVRQWVANLVDTFE-----------------------------EEVKAAARRLAYHGGN-T 86
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDigpdktrvglvqysddvrvefslndykskDDLLKAVKNLKYLGGGgT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615   87 NTGDALRYITARSFSPhaggRPRDRAYKQVAILLTDGRSQDL--VLDAAAAAHRAGIRIFAVGVGEALKEELEEIASEPK 164
Cdd:cd01450    81 NTGKALQYALEQLFSE----SNARENVPKVIIVLTDGRSDDGgdPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPS 156


                  ....*
gi 767952615  165 SAHVF 169
Cdd:cd01450   157 ERHVF 161
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 452-674 1.19e-28

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: 121.17  E-value: 1.19e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615  452 GEKGEMGVAGPMGLPGPKGDIGAIGPVGAPGPKGEKGDVGI----GPFG----QGEKGEKGSLGLPGPPGRDGSKGMRGE 523
Cdd:NF038329  120 GEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEkgpaGPQGeagpQGPAGKDGEAGAKGPAGEKGPQGPRGE 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615  524 PGELGEPGLPGEVGMRGPQGPPGLPGPPGRVGaPGLQGERGEKGTRGEKGERGLDGFPGKPGDTGQQGRPGPSGVAGPQG 603
Cdd:NF038329  200 TGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDG 278

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767952615  604 EKGDVGPAGPPGvpgsvvqQEGLKGEQGAPGPRGHQGAPGPPGARGPIGPEGRDGPPGLQGLRGKKGDMGP 674
Cdd:NF038329  279 ERGPVGPAGKDG-------QNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 38-180 5.41e-27

von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 109.08  E-value: 5.41e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615     38 DLVFLLDTSSSVGKEDFEKVRQWVANLVDTFE-----------------------------EEVKAAARRLAYH-GGNTN 87
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDigpdgdrvglvtfsddarvlfplndsrskDALLEALASLSYKlGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615     88 TGDALRYITARSFSPHAGGRPRDRaykQVAILLTDGRSQDL---VLDAAAAAHRAGIRIFAVGVGEA-LKEELEEIASEP 163
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAP---KVVILITDGESNDGpkdLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLASAP 157

                           170
                    ....*....|....*..
gi 767952615    164 KSAHVFHVSDFNAIDKI 180
Cdd:smart00327  158 GGVYVFLPELLDLLIDL 174
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 501-793 5.66e-26

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: 113.08  E-value: 5.66e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615  501 GEKGSLGLPGPPGRDGSKGMRGEPGELGEPGLPGEVGMRgpqgppglpGPPGRVGAPGLQGERGEKGTRGEKGERGLDGF 580
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQ---------GERGEKGPAGPQGEAGPQGPAGKDGEAGAKGP 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615  581 PGKPGDTGQQGRPGPSGVAGPQGEKG-DVGPAGPPGVPGSVVQQEGLKGEQGAPGPRGHQGAPGPPGARGPIGPEGRDGP 659
Cdd:NF038329  188 AGEKGPQGPRGETGPAGEQGPAGPAGpDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGE 267

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615  660 PGLQGLRGKKGDMGPPGipgllglqgppgppgvpgppgpggspglpgeigfpgkpgppgptgppgkdgpngppgppgTKG 739
Cdd:NF038329  268 AGPDGPDGKDGERGPVG------------------------------------------------------------PAG 287

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767952615  740 EPGERGEDGLPGKPGLRGEIGEQGLagrPGEKGEAGLPGAPGFPGVRGEKGDQG 793
Cdd:NF038329  288 KDGQNGKDGLPGKDGKDGQNGKDGL---PGKDGKDGQPGKDGLPGKDGKDGQPG 338
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 38-180 2.27e-21

Integrins are a class of adhesion receptors that link the extracellular matrix to the cytoskeleton and cooperate with growth factor receptors to promote celll survival, cell cycle progression and cell migration. Integrins consist of an alpha and a beta sub-unit. Each sub-unit has a large extracellular portion, a single transmembrane segment and a short cytoplasmic domain. The N-terminal domains of the alpha and beta subunits associate to form the integrin headpiece, which contains the ligand binding site, whereas the C-terminal segments traverse the plasma membrane and mediate interaction with the cytoskeleton and with signalling proteins.The VWA domains present in the alpha subunits of integrins seem to be a chordate specific radiation of the gene family being found only in vertebrates. They mediate protein-protein interactions.


Pssm-ID: 238746 [Multi-domain]  Cd Length: 177  Bit Score: 93.19  E-value: 2.27e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615   38 DLVFLLDTSSSVGKEDFEKVRQWVANLVDTFE-----------------------------EEVKAAARRLAYHGGNTNT 88
Cdd:cd01469     2 DIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDigptktqfglvqysesfrteftlneyrtkEEPLSLVKHISQLLGLTNT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615   89 GDALRYITARSFSPHAGGRprdRAYKQVAILLTDGRSQD--LVLDAAAAAHRAGIRIFAVGVGEALK-----EELEEIAS 161
Cdd:cd01469    82 ATAIQYVVTELFSESNGAR---KDATKVLVVITDGESHDdpLLKDVIPQAEREGIIRYAIGVGGHFQrensrEELKTIAS 158

                         170
                  ....*....|....*....
gi 767952615  162 EPKSAHVFHVSDFNAIDKI 180
Cdd:cd01469   159 KPPEEHFFNVTDFAALKDI 177
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 769-1048 2.33e-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: 99.21  E-value: 2.33e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615  769 GEKGEAGLPGAPGFPGVRGEKGDQGEKGELGLPGLKGDRGEKGEagpagppglpgttslftphprmPGEQGPKGEKGDPG 848
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGE----------------------KGPAGPQGEAGPQG 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615  849 LPGEPGLQGrpgelgpqgptgppgakgqegahgapgaagnpgapghvgapgpsgppgsvgAPGLRGTPGKDGERGEKGAA 928
Cdd:NF038329  175 PAGKDGEAG---------------------------------------------------AKGPAGEKGPQGPRGETGPA 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615  929 GEEGSPGPVGPRGDPGAPGLPGPPGKGKDGEPGLRGSPGLPGPLGTKGDRGAPGIPGSPGSRGDPGIGVAGPPGPSGPPG 1008
Cdd:NF038329  204 GEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPV 283

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 767952615 1009 DK----GSPGSRGLPGFPGPQGPAGRDGAPGNPGERGPPGKPGL 1048
Cdd:NF038329  284 GPagkdGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGL 327
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 38-174 2.50e-21

VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions.


Pssm-ID: 238758  Cd Length: 165  Bit Score: 92.39  E-value: 2.50e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615   38 DLVFLLDTSSSVGKEDFEKVRQWVANLVDTFE-----------------------------EEVKAAARRLAYHGGNT-N 87
Cdd:cd01481     2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDvgpdkirvavvqfsdtprpefylnthstkADVLGAVRRLRLRGGSQlN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615   88 TGDALRYITARSFSPHAGGRPRDrAYKQVAILLTDGRSQDLVLDAAAAAHRAGIRIFAVGVGEALKEELEEIASEPKsaH 167
Cdd:cd01481    82 TGSALDYVVKNLFTKSAGSRIEE-GVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPS--F 158


                  ....*..
gi 767952615  168 VFHVSDF 174
Cdd:cd01481   159 VFQVSDF 165
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 450-660 1.43e-19

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: 93.43  E-value: 1.43e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615  450 PAGEKGEMGVAGPMGLPGPKGDIGAIGPVGAPGPKGEKGDVG----IGPFG-QGEKGEKGSLGLPGPPGRDGS--KGMRG 522
Cdd:NF038329  160 EKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGpageQGPAGpAGPDGEAGPAGEDGPAGPAGDgqQGPDG 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615  523 EPGELGEPGLPGEVGMRGPQGPPGLPGPPGRVGAPGLQGERGEKGTRGEKGERGLDGFPGKPGDTGQQGRPGPSGVAGpq 602
Cdd:NF038329  240 DPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDG-- 317

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767952615  603 gekgdvgpagppgvpgsvvqQEGLKGEQGAPGPRGHQGAPGPPGARGPIGPEGRDGPP 660
Cdd:NF038329  318 --------------------KDGQPGKDGLPGKDGKDGQPGKPAPKTPEVPQKPDTAP 355
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 624-994 1.83e-19

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: 93.43  E-value: 1.83e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615  624 EGLKGEQGAPGPRGHQGAPGPPGARGPIGPEGRDGPPGLQGLRGKKGDMGPPGipgllglqgppgppgvpgppgpggspg 703
Cdd:NF038329  116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQG--------------------------- 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615  704 lpgeigfpgkpgppgptgppgkdgpngppgppgtkgEPGERGEDGLPGKPGLRGEIGEQGLAGRPGEKGEAGLPGAPGFP 783
Cdd:NF038329  169 ------------------------------------EAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPA 212

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615  784 GVRGEKGDQGEKGELGLPGlKGDRGEKGEagpagppglpgttslftphprmPGEQGPKGEKGDPGLPGEPGLQGRPGElg 863
Cdd:NF038329  213 GPDGEAGPAGEDGPAGPAG-DGQQGPDGD----------------------PGPTGEDGPQGPDGPAGKDGPRGDRGE-- 267

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615  864 pqgptgppgakgqegahgapgaagnpgapghvgapgpsgppgsvgaPGLRGTPGKDGERGEKGAAGEEGSPGPVGPrgdp 943
Cdd:NF038329  268 ----------------------------------------------AGPDGPDGKDGERGPVGPAGKDGQNGKDGL---- 297

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767952615  944 gapglpgppgKGKDGEPGLRGSPGLPGPLGTKGDRGAPGIPGSPGSRGDPG 994
Cdd:NF038329  298 ----------PGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 37-169 1.08e-18

Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains.


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 84.92  E-value: 1.08e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615   37 YDLVFLLDTSSSVGKEDFEKVRQWVANLVDTFE-----------------------------EEVKAAARRL-AYHGGNT 86
Cdd:cd00198     1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSasppgdrvglvtfgsnarvvlplttdtdkADLLEAIDALkKGLGGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615   87 NTGDALRYItARSFSphaggRPRDRAYKQVAILLTDGRSQD---LVLDAAAAAHRAGIRIFAVGVG-EALKEELEEIASE 162
Cdd:cd00198    81 NIGAALRLA-LELLK-----SAKRPNARRVIILLTDGEPNDgpeLLAEAARELRKLGITVYTIGIGdDANEDELKEIADK 154


                  ....*..
gi 767952615  163 PKSAHVF 169
Cdd:cd00198   155 TTGGAVF 161
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1121-1337 3.99e-18

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: 89.19  E-value: 3.99e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615 1121 QGERGADGEVGQKGDQGHPGVPGFMGPPGNPGPPGADGIAGAAGPPGIQGSPGKEGPPGPQGPSGLPGIPGEEGKEGRDG 1200
Cdd:NF038329  131 AGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAG 210

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615 1201 KPGPPGEPGKAGEPGLPGPEGA--RGPPGFKGHTGDSGAPGPRGESGAMGLPGQEGLPGKDGDTGPtgpqgpqgpRGPPG 1278
Cdd:NF038329  211 PAGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK---------DGERG 281

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767952615 1279 KNGSPGSPGEPGPSGTPGQKGSKGENGSPGLPGFLGPRGPPGEPGEKGVPGKEGVPGKP 1337
Cdd:NF038329  282 PVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1121-1350 1.87e-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: 83.80  E-value: 1.87e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615 1121 QGERGADGEVGQKGDQGHPGVPGFMGPPGNPGPPGADGIAGAAGPPGIQGSpgkegppgpqgpsglpgiPGEEGKEGRDG 1200
Cdd:NF038329  119 KGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGE------------------AGPQGPAGKDG 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615 1201 KPGPPGEPGKAGEPGLPGPEGARGPPGFKGHTGDSGAPGPRGESGAMGLPGQeGLPGKDGDTGPTGPQGPQGPRGPPGKN 1280
Cdd:NF038329  181 EAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKD 259

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615 1281 GSPGSPGEPGPSGTPGQKGSKGENGSPGLPGFLGPRGPPGEPGEKGVPGKEGVPGKPGEPGFKGERGDPG 1350
Cdd:NF038329  260 GPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPG 329
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 919-1219 1.52e-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: 81.10  E-value: 1.52e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615  919 DGERGEKGAAGEEGSPGPVGPRGdpgapglpgppgkgKDGEPGLRGSPGLPGPLGTKGDRGAPGIPGSPGSRGDPGigva 998
Cdd:NF038329  116 DGEKGEPGPAGPAGPAGEQGPRG--------------DRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAG---- 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615  999 gppgpsgppgDKGSPGSRGLPGFPGPQGPAGRDGAPGNPGERGPPGKPGLSSLLSPgdinllakdvcndcppGPPGLPGL 1078
Cdd:NF038329  178 ----------KDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGE----------------DGPAGPAG 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615 1079 PGFKGDKGVPGKPGREGTEGKKGEAGPPGLPGPPGIAGPQGSQGERGADGEVGQKGDQGHPGvpgfmgppgnpgppgadg 1158
Cdd:NF038329  232 DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNG------------------ 293

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767952615 1159 iagAAGPPGiqgspgkegPPGPQGPSGLPGIPGEEGKEGRDGKPGPPGEPGKAGEPGLPGP 1219
Cdd:NF038329  294 ---KDGLPG---------KDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1191-1384 4.54e-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: 79.56  E-value: 4.54e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615 1191 GEEGKEGRDGKPGPPGEPGKAGEPGLPGPEGARGPPGFKGHTGDSGAPGPRGESGAMGLPGQEGLPGKDGDTGPTGPQGP 1270
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615 1271 QGPRGPPGKNGSPGSPGEPGPSGTPGQKGSKG-----ENGSPGLPGflgPRGPPGEPGEKGVPGKEGVPGKPGEPGFKGE 1345
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGpagdgQQGPDGDPG---PTGEDGPQGPDGPAGKDGPRGDRGEAGPDGP 273

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 767952615 1346 RGDPGIKGDKGPPGGKGQPGDPGIPGHKGHTGLMGPQGL 1384
Cdd:NF038329  274 DGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGL 312
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 38-168 4.88e-15

VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions.


Pssm-ID: 238757 [Multi-domain]  Cd Length: 186  Bit Score: 75.11  E-value: 4.88e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615   38 DLVFLLDTSSSVGKEDFEKVRQWVANLVDTFE------------------------------------EEVKAAARRLAY 81
Cdd:cd01480     4 DITFVLDSSESVGLQNFDITKNFVKRVAERFLkdyyrkdpagswrvgvvqysdqqeveagflrdirnyTSLKEAVDNLEY 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615   82 HGGNTNTGDALRYITARSF-SPHAGGrprdrayKQVAILLTDGRSQ----DLVLDAAAAAHRAGIRIFAVGVGEALKEEL 156
Cdd:cd01480    84 IGGGTFTDCALKYATEQLLeGSHQKE-------NKFLLVITDGHSDgspdGGIEKAVNEADHLGIKIFFVAVGSQNEEPL 156

                         170
                  ....*....|..
gi 767952615  157 EEIASEPKSAHV 168
Cdd:cd01480   157 SRIACDGKSALY 168
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 38-169 4.37e-13

VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have diverse functions in cell-cell and cell-extracellular matrix interactions. Because of their involvement in many biologically important adhesion processes, integrins are conserved across a wide range of multicellular animals. Integrins from invertebrates have been identified from six phyla. There are no data to date to suggest any immunological functions for the invertebrate integrins. The members of this sub-group have the conserved MIDAS motif that is charateristic of this domain suggesting the involvement of the integrins in the recognition and binding of multi-ligands.


Pssm-ID: 238753 [Multi-domain]  Cd Length: 163  Bit Score: 68.58  E-value: 4.37e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615   38 DLVFLLDTSSSVgKEDFEKVRQWVANLVD--------------TF-----------------EEEVKAAARRLAYHGGNT 86
Cdd:cd01476     2 DLLFVLDSSGSV-RGKFEKYKKYIERIVEgleigptatrvaliTYsgrgrqrvrfnlpkhndGEELLEKVDNLRFIGGTT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615   87 NTGDALRYiTARSFSPHAGGRPRdraYKQVAILLTDGRSQDLVLDAAAAAHR-AGIRIFAVGVGE---ALKEELEEIASE 162
Cdd:cd01476    81 ATGAAIEV-ALQQLDPSEGRREG---IPKVVVVLTDGRSHDDPEKQARILRAvPNIETFAVGTGDpgtVDTEELHSITGN 156


                  ....*..
gi 767952615  163 PKsaHVF 169
Cdd:cd01476   157 ED--HIF 161
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1239-1535 6.71e-13

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 72.63  E-value: 6.71e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615 1239 GPRGESGAMGLPGQEGLPGKDGDTGPTGPQGPQGPRGPPGKNGSPGSPGEPGPSGTPGQKGSKGENGSPGLPGFLGPRGP 1318
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615 1319 PGEPGEKGVPGKEGVPGKPGEPGFKGERGDPGIKGDKGPPGGkgqpgdpgipGHKGHTGLMGPQGLPGENGPVGPPGPPG 1398
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPD----------GDPGPTGEDGPQGPDGPAGKDGPRGDRG 266

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615 1399 QPGFPGLRGESpsmetlrrliqeelgkqletrlayllaqmppaymkssqgrpgppgppgkdglpGRAGPMGEPGRPGQGG 1478
Cdd:NF038329  267 EAGPDGPDGKD-----------------------------------------------------GERGPVGPAGKDGQNG 293

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767952615 1479 LEGPSGPIGPKGERGAKGDPGAPGvglrgemGPPGIPGQPGEPGYAKDGLPGIPGPQ 1535
Cdd:NF038329  294 KDGLPGKDGKDGQNGKDGLPGKDG-------KDGQPGKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1212-1544 7.83e-12

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: 69.55  E-value: 7.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615 1212 GEPGLPGPEGARGPPGFKGHTGDSGAPGPRGESGAMGLPGQEGLPGKDGDTGPTgpqgpqgprgppgknGSPGSPGEPGP 1291
Cdd:NF038329  120 GEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ---------------GPAGKDGEAGA 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615 1292 SGTPGQKGSKGENGSPGlpgflgprgppgepgEKGVPGKEGVPGKPGEPGFKGERGDPGIKGDKGPPGGkgqpgdpgipG 1371
Cdd:NF038329  185 KGPAGEKGPQGPRGETG---------------PAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPD----------G 239

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615 1372 HKGHTGLMGPQGLPGENGPVGPPGPPGQPGFPGLRGESpsmetlrrliqeelgkqletrlayllaqmppaymkssqgrpg 1451
Cdd:NF038329  240 DPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKD------------------------------------------ 277

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615 1452 ppgppgkdglpGRAGPMGEPGRPGQGGLEGPSGPIGPKGERGAKGDPGAPGvglrgemgppgipgqpgepgyaKDGLPGI 1531
Cdd:NF038329  278 -----------GERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDG----------------------KDGQPGK 324

                         330
                  ....*....|...
gi 767952615 1532 PGPQGETGPAGHP 1544
Cdd:NF038329  325 DGLPGKDGKDGQP 337
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 2-180 6.06e-10

vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and metabolism];


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 61.88  E-value: 6.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615    2 AGLRGNAVAGLLWMLLLWSGGGGCQAQRAGCKSVHYDLVFLLDTSSSVGKED-FEKVRQWVANLVDTFEEE--------- 71
Cdd:COG1240    58 LLALLLAALLLLLAVLLLLLALALAPLALARPQRGRDVVLVVDASGSMAAENrLEAAKGALLDFLDDYRPRdrvglvafg 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615   72 ------------VKAAARRLAY--HGGNTNTGDALRYITARsfsphagGRPRDRAYKQVAILLTDGR---SQDLVLDAAA 134
Cdd:COG1240   138 geaevllpltrdREALKRALDElpPGGGTPLGDALALALEL-------LKRADPARRKVIVLLTDGRdnaGRIDPLEAAE 210

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 767952615  135 AAHRAGIRIFAVGVG-EALKEE-LEEIASEpKSAHVFHVSDFNAIDKI 180
Cdd:COG1240   211 LAAAAGIRIYTIGVGtEAVDEGlLREIAEA-TGGRYFRADDLSELAAI 257
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 38-188 7.53e-09

Secreted protein containing bacterial Ig-like domain and vWFA domain [General function prediction only];


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 58.96  E-value: 7.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615   38 DLVFLLDTSSSVGKEDFEKVRQWVANLVD-----------TFE---------------EEVKAAARRLaYHGGNTNTGDA 91
Cdd:COG2304    93 NLVFVIDVSGSMSGDKLELAKEAAKLLVDqlrpgdrvsivTFAgdarvllpptpatdrAKILAAIDRL-QAGGGTALGAG 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615   92 LRYITARSFSPHAGGRPRdraykqVAILLTDGR------SQDLVLDAAAAAHRAGIRIFAVGVGEALKEE-LEEIASEPK 164
Cdd:COG2304   172 LELAYELARKHFIPGRVN------RVILLTDGDanvgitDPEELLKLAEEAREEGITLTTLGVGSDYNEDlLERLADAGG 245

                         170       180
                  ....*....|....*....|....
gi 767952615  165 SAHvFHVSDFNAIDKIRGKLRRRL 188
Cdd:COG2304   246 GNY-YYIDDPEEAEKVFVREFSRI 268
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 36-180 4.97e-07

ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, the causative agent of anthrax. ATR is the cellular receptor for the anthrax protective antigen and facilitates entry of the toxin into cells. The VWA domain in ATR contains the toxin binding site and mediates interaction with protective antigen. The binding is mediated by divalent cations that binds to the MIDAS motif. These proteins are a family of vertebrate ECM receptors expressed by endothelial cells.


Pssm-ID: 238751 [Multi-domain]  Cd Length: 185  Bit Score: 51.74  E-value: 4.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615   36 HYDLVFLLDTSSSVGKEDFEkVRQWVANLVDTF--------------------------EEEVKAAAR-RLAYHGGNTNT 88
Cdd:cd01474     4 HFDLYFVLDKSGSVAANWIE-IYDFVEQLVDRFnspglrfsfitfstratkilpltddsSAIIKGLEVlKKVTPSGQTYI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615   89 GDALRYITARSFSPHAGGRPRDRaykqVAILLTDGR-SQDLVLDAAAAAHRA---GIRIFAVGVGEALKEELEEIASEPK 164
Cdd:cd01474    83 HEGLENANEQIFNRNGGGRETVS----VIIALTDGQlLLNGHKYPEHEAKLSrklGAIVYCVGVTDFLKSQLINIADSKE 158

                         170
                  ....*....|....*..
gi 767952615  165 saHVFHVSD-FNAIDKI 180
Cdd:cd01474   159 --YVFPVTSgFQALSGI 173
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
40-180 1.55e-06

Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 50.31  E-value: 1.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615   40 VFLLDTSSSVGKEDFEKVRQWVANLVDTFEEEVKAAAR------------RLAYH--------------GGNTNTGDALR 93
Cdd:COG4245     9 YLLLDTSGSMSGEPIEALNEGLQALIDELRQDPYALETvevsvitfdgeaKVLLPltdledfqppdlsaSGGTPLGAALE 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615   94 YITARSFSPHAGGRP-RDRAYKQVAILLTDGRSQDL-------VLDAAAAAHRAGirIFAVGVG-EALKEELEEIASEPK 164
Cdd:COG4245    89 LLLDLIERRVQKYTAeGKGDWRPVVFLITDGEPTDSdweaalqRLKDGEAAKKAN--IFAIGVGpDADTEVLKQLTDPVR 166

                         170
                  ....*....|....*.
gi 767952615  165 sahVFHVSDFNAIDKI 180
Cdd:COG4245   167 ---ALDALDGLDFREF 179
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 38-162 7.95e-06

Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain [Function unknown];


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 49.29  E-value: 7.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615   38 DLVFLLDTSSSVGKEDFEKVRQWVANLVD-----------------------TFEEEVKAAARRLA--YHGGNTNTGDAL 92
Cdd:COG2425   120 PVVLCVDTSGSMAGSKEAAAKAAALALLRalrpnrrfgvilfdtevvedlplTADDGLEDAIEFLSglFAGGGTDIAPAL 199

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767952615   93 RYitarsfsphAGGRPRDRAYKQ-VAILLTDGRSQDLVLD--AAAAAHRAGIRIFAVGVGEALKEELEEIASE 162
Cdd:COG2425   200 RA---------ALELLEEPDYRNaDIVLITDGEAGVSPEEllREVRAKESGVRLFTVAIGDAGNPGLLEALAD 263
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 38-155 2.94e-05

Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a target cell. In association with invasion, T. gondii sequentially discharges three sets of secretory organelles beginning with the micronemes, which contain adhesive proteins involved in parasite attachment to a host cell. Deployed as protein complexes, several micronemal proteins possess vertebrate-derived adhesive sequences that function in binding receptors. The VWA domain likely mediates the protein-protein interactions of these with their interacting partners.


Pssm-ID: 238748 [Multi-domain]  Cd Length: 186  Bit Score: 46.61  E-value: 2.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615   38 DLVFLLDTSSSVGKED-FEKVRQWVANLVD--------------TFEEEVK--------------------AAARRLAYH 82
Cdd:cd01471     2 DLYLLVDGSGSIGYSNwVTHVVPFLHTFVQnlnispdeinlylvTFSTNAKelirlsspnstnkdlalnaiRALLSLYYP 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767952615   83 GGNTNTGDALRYITARSFSpHAGGRPRdraYKQVAILLTDGRSQDL--VLDAAAAAHRAGIRIFAVGVGEALKEE 155
Cdd:cd01471    82 NGSTNTTSALLVVEKHLFD-TRGNREN---APQLVIIMTDGIPDSKfrTLKEARKLRERGVIIAVLGVGQGVNHE 152
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 748-802 4.45e-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: 4.45e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 767952615   748 GLPGKPGLRGEIGEQGLAGRPGEKGEAGLPGAPGFPGVRGEKGDQGEKGELGLPG 802
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 743-797 4.96e-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: 4.96e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 767952615   743 ERGEDGLPGKPGLRGEIGEQGLAGRPGEKGEAGLPGAPGFPGVRGEKGDQGEKGE 797
Cdd:pfam01391    2 PPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
482-676 1.63e-04

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 46.18  E-value: 1.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615  482 GPKGEKGDVGIGPFGQGekGEKGSLGLPGPPGRDGSKGMRGEPGELGEPGLPGEVGMRGPQGPPGLPGPPGRVGAPGLQG 561
Cdd:COG5164     2 GLYGPGKTGPSDPGGVT--TPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615  562 ERGEKGTRGEKGERGLDGFPGKPGDTGQQGRPGPSGVAGPQGEKG-----DVGPAGPPGVPGSVVQQEGLKGEQGAPGPR 636
Cdd:COG5164    80 GTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGsttppSGGSTTPPGDGGSTPPGPGSTGPGGSTTPP 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 767952615  637 GHQGA---PGPPGARGPIGPEGRDGPP--GLQGLRGKKGDMGPPG 676
Cdd:COG5164   160 GDGGSttpPGPGGSTTPPDDGGSTTPPnkGETGTDIPTGGTPRQG 204
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1212-1264 2.02e-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: 2.02e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 767952615  1212 GEPGLPGPEGARGPPGFKGHTGDSGAPGPRGESGAMGLPGQEGLPGKDGDTGP 1264
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGA 53
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 625-677 2.91e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.17  E-value: 2.91e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 767952615   625 GLKGEQGAPGPRGHQGAPGPPGARGPIGPEGRDGPPGLQGLRGKKGDMGPPGI 677
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGA 53
VWA_2 pfam13519
von Willebrand factor type A domain;
39-120 5.77e-04

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 40.74  E-value: 5.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615    39 LVFLLDTSSSVGKED-----FEKVRQWVANLVD----------TFEEEVK-------------AAARRLAYHGGNTNTGD 90
Cdd:pfam13519    1 LVFVLDTSGSMRNGDygptrLEAAKDAVLALLKslpgdrvglvTFGDGPEvlipltkdrakilRALRRLEPKGGGTNLAA 80

                           90       100       110
                   ....*....|....*....|....*....|
gi 767952615    91 ALRYitARSFSPHaggrpRDRAYKQVAILL 120
Cdd:pfam13519   81 ALQL--ARAALKH-----RRKNQPRRIVLI 103
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1211-1258 6.51e-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: 6.51e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 767952615  1211 AGEPGLPGPEGARGPPGFKGHTGDSGAPGPRGESGAMGLPGQEGLPGK 1258
Cdd:pfam01391    9 PGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 982-1046 1.13e-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: 38.63  E-value: 1.13e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767952615   982 GIPGSPGSRGDPGigvagppgPSGPPGDKGSPGSRGLPGFPGPQGPAGRDGAPGNPGERGPPGKP 1046
Cdd:pfam01391    1 GPPGPPGPPGPPG--------PPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 763-813 1.98e-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: 37.86  E-value: 1.98e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 767952615   763 GLAGRPGEKGEAGLPGAPGFPGVRGEKGDQGEKGELGLPGLKGDRGEKGEA 813
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAP 51
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1281-1350 2.64e-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: 2.64e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615  1281 GSPGSPGEPGPSGTPGQKGSKGENGSPGLPGFlgprgppgepgekgvPGKEGVPGKPGEPGFKGERGDPG 1350
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGE---------------PGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 556-606 2.91e-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: 2.91e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 767952615   556 APGLQGERGEKGTRGEKGERGLDGFPGKPGDTGQQGRPGPSGVAGPQGEKG 606
Cdd:pfam01391    5 PPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 39-160 2.98e-03

VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. Not much is known about the function of the VWA domain in these proteins. The members do have a conserved MIDAS motif. The biochemical function however is not known.


Pssm-ID: 238742 [Multi-domain]  Cd Length: 170  Bit Score: 40.33  E-value: 2.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952615   39 LVFLLDTSSSVGKEDFEKVRQWVANLVDTFEE--------------------------EVKAAARRLAyHGGNTN--TGD 90
Cdd:cd01465     3 LVFVIDRSGSMDGPKLPLVKSALKLLVDQLRPddrlaivtydgaaetvlpatpvrdkaAILAAIDRLT-AGGSTAggAGI 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767952615   91 ALRYITA-RSFSPHAGGRprdraykqvAILLTDG------RSQDLVLDAAAAAHRAGIRIFAVGVGEALKEEL-EEIA 160
Cdd:cd01465    82 QLGYQEAqKHFVPGGVNR---------ILLATDGdfnvgeTDPDELARLVAQKRESGITLSTLGFGDNYNEDLmEAIA 150
 
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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