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Conserved domains on  [gi|767952611|ref|XP_011515186|]
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collagen alpha-1(XXII) chain isoform X2 [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 ...
 36-219 3.91e-60

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: 206.08  E-value: 3.91e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611   36 HYDLVFLLDTSSSVGKEDFEKVRQWVANLVDTFEVGPDRTRVGVVRYSDRPTTAFELGLFGSQEEVKAAARRLAYHGGNT 115
Cdd:cd01475     2 PTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611  116 NTGDALRYITARSFSPHAGGRPRDRAYKQVAILLTDGRSQDLVLDAAAAAHRAGIRIFAVGVGEALKEELEEIASEPKSA 195
Cdd:cd01475    82 MTGLAIQYAMNNAFSEAEGARPGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLAD 161

                         170       180
                  ....*....|....*....|....
gi 767952611  196 HVFHVSDFNAIDKIRGKLRRRLCE 219
Cdd:cd01475   162 HVFYVEDFSTIEELTKKFQGKICV 185
LamG super family cl22861
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 239-426 6.05e-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: 126.32  E-value: 6.05e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611    239 GTKEITGFDLMDL-FSVKEILGKRenGAQSSYvRMGSFPVV-QSTEDVFPQGLPDEYAFVTTFRFRKTSRkedWYIWQVI 316
Cdd:smart00210    1 GQDLLQVFDLPSLsFAIRQVVGPE--PGSPAY-RLGDPALVpQPTRDLFPSGLPEDFSLLTTFRQTPKSR---GVLFAIY 74

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611    317 DQYSIPQVSIRLDGENKAVEYNAVGAMKDAVRVVFRGSrvnDLFDRDWHKMALSIQAQNVSLHIDCALVQTLPIEER--E 394
Cdd:smart00210   75 DAQNVRQFGLEVDGRANTLLLRYQGVDGKQHTVSFRNL---PLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPgqP 151

                           170       180       190
                    ....*....|....*....|....*....|..
gi 767952611    395 NIDIQGKTVIGKRLYDSVPIDFDLQRIVIYCD 426
Cdd:smart00210  152 PIDTDGIEVRGAQAADRKPFQGDLQQLKIVCD 183
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 479-690 1.72e-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: 120.78  E-value: 1.72e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611  479 PAGEKGEMGVAGPMGLPGPKGDIGAIGPVGAPGPKGEKGDVGSLGLPGPPGRDGSKGMRGEPGELGEPGLPGEVGMRGPQ 558
Cdd:NF038329  139 DRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEA 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611  559 GPPGLPGPPGRVGaPGLQGERGEKGTRGEKGERGLDGFPGKPGDTGQQGRPGPSGVAGPQGEKGDVGPAGPPGvpgsvvq 638
Cdd:NF038329  219 GPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDG------- 290

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767952611  639 QEGLKGEQGAPGPRGHQGAPGPPGARGPIGPEGRDGPPGLQGLRGKKGDMGP 690
Cdd:NF038329  291 QNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 785-1064 1.01e-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: 100.36  E-value: 1.01e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611  785 GEKGEAGLPGAPGFPGVRGEKGDQGEKGELGLPGLKGDRGEKGEagpagppglpgttslftphprmPGEQGPKGEKGDPG 864
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGE----------------------KGPAGPQGEAGPQG 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611  865 LPGEPGLQGrpgelgpqgptgppgakgqegahgapgaagnpgapghvgapgpsgppgsvgAPGLRGTPGKDGERGEKGAA 944
Cdd:NF038329  175 PAGKDGEAG---------------------------------------------------AKGPAGEKGPQGPRGETGPA 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611  945 GEEGSPGPVGPRGDPGAPGLPGPPGKGKDGEPGLRGSPGLPGPLGTKGDRGAPGIPGSPGSRGDPGIGVAGPPGPSGPPG 1024
Cdd:NF038329  204 GEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPV 283

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 767952611 1025 DK----GSPGSRGLPGFPGPQGPAGRDGAPGNPGERGPPGKPGL 1064
Cdd:NF038329  284 GPagkdGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGL 327
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1137-1353 2.65e-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: 89.58  E-value: 2.65e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611 1137 QGERGADGEVGQKGDQGHPGVPGFMGPPGNPGPPGADGIAGAAGPPGIQGSPGKEGPPGPQGPSGLPGIPGEEGKEGRDG 1216
Cdd:NF038329  131 AGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAG 210

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611 1217 KPGPPGEPGKAGEPGLPGPEGA--RGPPGFKGHTGDSGAPGPRGESGAMGLPGQEGLPGKDGDTGPtgpqgpqgpRGPPG 1294
Cdd:NF038329  211 PAGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK---------DGERG 281

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767952611 1295 KNGSPGSPGEPGPSGTPGQKGSKGENGSPGLPGFLGPRGPPGEPGEKGVPGKEGVPGKP 1353
Cdd:NF038329  282 PVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1255-1551 4.18e-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: 73.40  E-value: 4.18e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611 1255 GPRGESGAMGLPGQEGLPGKDGDTGPTGPQGPQGPRGPPGKNGSPGSPGEPGPSGTPGQKGSKGENGSPGLPGFLGPRGP 1334
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611 1335 PGEPGEKGVPGKEGVPGKPGEPGFKGERGDPGIKGDKGPPGGkgqpgdpgipGHKGHTGLMGPQGLPGENGPVGPPGPPG 1414
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPD----------GDPGPTGEDGPQGPDGPAGKDGPRGDRG 266

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611 1415 QPGFPGLRGESpsmetlrrliqeelgkqletrlayllaqmppaymkssqgrpgppgppgkdglpGRAGPMGEPGRPGQGG 1494
Cdd:NF038329  267 EAGPDGPDGKD-----------------------------------------------------GERGPVGPAGKDGQNG 293

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767952611 1495 LEGPSGPIGPKGERGAKGDPGAPGvglrgemGPPGIPGQPGEPGYAKDGLPGIPGPQ 1551
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 ...
 36-219 3.91e-60

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: 206.08  E-value: 3.91e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611   36 HYDLVFLLDTSSSVGKEDFEKVRQWVANLVDTFEVGPDRTRVGVVRYSDRPTTAFELGLFGSQEEVKAAARRLAYHGGNT 115
Cdd:cd01475     2 PTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611  116 NTGDALRYITARSFSPHAGGRPRDRAYKQVAILLTDGRSQDLVLDAAAAAHRAGIRIFAVGVGEALKEELEEIASEPKSA 195
Cdd:cd01475    82 MTGLAIQYAMNNAFSEAEGARPGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLAD 161

                         170       180
                  ....*....|....*....|....
gi 767952611  196 HVFHVSDFNAIDKIRGKLRRRLCE 219
Cdd:cd01475   162 HVFYVEDFSTIEELTKKFQGKICV 185
VWA pfam00092
von Willebrand factor type A domain;
38-212 5.28e-54

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 186.33  E-value: 5.28e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611    38 DLVFLLDTSSSVGKEDFEKVRQWVANLVDTFEVGPDRTRVGVVRYSDRPTTAFELGLFGSQEEVKAAARRLAYHGGNT-N 116
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTtN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611   117 TGDALRYITARSFSPHAGGRPRdraYKQVAILLTDGRSQDL-VLDAAAAAHRAGIRIFAVGVGEALKEELEEIASEPKSA 195
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPG---APKVVVLLTDGRSQDGdPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEG 157

                          170
                   ....*....|....*..
gi 767952611   196 HVFHVSDFNAIDKIRGK 212
Cdd:pfam00092  158 HVFTVSDFEALEDLQDQ 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 38-209 3.03e-42

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: 152.99  E-value: 3.03e-42
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611     38 DLVFLLDTSSSVGKEDFEKVRQWVANLVDTFEVGPDRTRVGVVRYSDRPTTAFELGLFGSQEEVKAAARRLAYH-GGNTN 116
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611    117 TGDALRYITARSFSPHAGGRPRDRaykQVAILLTDGRSQDL---VLDAAAAAHRAGIRIFAVGVGEA-LKEELEEIASEP 192
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAP---KVVILITDGESNDGpkdLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLASAP 157

                           170
                    ....*....|....*..
gi 767952611    193 KSAHVFHVSDFNAIDKI 209
Cdd:smart00327  158 GGVYVFLPELLDLLIDL 174
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 239-426 6.05e-33

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


Pssm-ID: 214560  Cd Length: 184  Bit Score: 126.32  E-value: 6.05e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611    239 GTKEITGFDLMDL-FSVKEILGKRenGAQSSYvRMGSFPVV-QSTEDVFPQGLPDEYAFVTTFRFRKTSRkedWYIWQVI 316
Cdd:smart00210    1 GQDLLQVFDLPSLsFAIRQVVGPE--PGSPAY-RLGDPALVpQPTRDLFPSGLPEDFSLLTTFRQTPKSR---GVLFAIY 74

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611    317 DQYSIPQVSIRLDGENKAVEYNAVGAMKDAVRVVFRGSrvnDLFDRDWHKMALSIQAQNVSLHIDCALVQTLPIEER--E 394
Cdd:smart00210   75 DAQNVRQFGLEVDGRANTLLLRYQGVDGKQHTVSFRNL---PLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPgqP 151

                           170       180       190
                    ....*....|....*....|....*....|..
gi 767952611    395 NIDIQGKTVIGKRLYDSVPIDFDLQRIVIYCD 426
Cdd:smart00210  152 PIDTDGIEVRGAQAADRKPFQGDLQQLKIVCD 183
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 479-690 1.72e-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: 120.78  E-value: 1.72e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611  479 PAGEKGEMGVAGPMGLPGPKGDIGAIGPVGAPGPKGEKGDVGSLGLPGPPGRDGSKGMRGEPGELGEPGLPGEVGMRGPQ 558
Cdd:NF038329  139 DRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEA 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611  559 GPPGLPGPPGRVGaPGLQGERGEKGTRGEKGERGLDGFPGKPGDTGQQGRPGPSGVAGPQGEKGDVGPAGPPGvpgsvvq 638
Cdd:NF038329  219 GPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDG------- 290

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767952611  639 QEGLKGEQGAPGPRGHQGAPGPPGARGPIGPEGRDGPPGLQGLRGKKGDMGP 690
Cdd:NF038329  291 QNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 481-809 2.35e-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: 120.40  E-value: 2.35e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611  481 GEKGEMGVAGPMGLPGPKGDIGAIGPVGAPGPKGEKGDVGSLGLPGPPGRDGSKGMRGEPGELGEpglpgevgmrgpqgp 560
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGE--------------- 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611  561 pglpgppgrvgaPGLQGERGEKGTRGEKGERGLDGFPGKPGDTGQQGRPGPSGVAGPQGEKGDvgpagppgvpgsvvqqe 640
Cdd:NF038329  182 ------------AGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD----------------- 232

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611  641 GLKGEQGAPGPRGHQGAPGPPGARGPIGPEGRDGPPGLQGLRGKKGDMGPPGipgllglqgppgppgvpgppgpggspgl 720
Cdd:NF038329  233 GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVG---------------------------- 284

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611  721 pgeigfpgkpgppgptgppgkdgpngppgppgTKGEPGERGEDGLPGKPGLRGEIGEQGLagrPGEKGEAGLPGAPGFPG 800
Cdd:NF038329  285 --------------------------------PAGKDGQNGKDGLPGKDGKDGQNGKDGL---PGKDGKDGQPGKDGLPG 329


                  ....*....
gi 767952611  801 VRGEKGDQG 809
Cdd:NF038329  330 KDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 785-1064 1.01e-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: 100.36  E-value: 1.01e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611  785 GEKGEAGLPGAPGFPGVRGEKGDQGEKGELGLPGLKGDRGEKGEagpagppglpgttslftphprmPGEQGPKGEKGDPG 864
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGE----------------------KGPAGPQGEAGPQG 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611  865 LPGEPGLQGrpgelgpqgptgppgakgqegahgapgaagnpgapghvgapgpsgppgsvgAPGLRGTPGKDGERGEKGAA 944
Cdd:NF038329  175 PAGKDGEAG---------------------------------------------------AKGPAGEKGPQGPRGETGPA 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611  945 GEEGSPGPVGPRGDPGAPGLPGPPGKGKDGEPGLRGSPGLPGPLGTKGDRGAPGIPGSPGSRGDPGIGVAGPPGPSGPPG 1024
Cdd:NF038329  204 GEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPV 283

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 767952611 1025 DK----GSPGSRGLPGFPGPQGPAGRDGAPGNPGERGPPGKPGL 1064
Cdd:NF038329  284 GPagkdGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGL 327
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 640-1010 5.87e-20

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 94.97  E-value: 5.87e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611  640 EGLKGEQGAPGPRGHQGAPGPPGARGPIGPEGRDGPPGLQGLRGKKGDMGPPGipgllglqgppgppgvpgppgpggspg 719
Cdd:NF038329  116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQG--------------------------- 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611  720 lpgeigfpgkpgppgptgppgkdgpngppgppgtkgEPGERGEDGLPGKPGLRGEIGEQGLAGRPGEKGEAGLPGAPGFP 799
Cdd:NF038329  169 ------------------------------------EAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPA 212

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611  800 GVRGEKGDQGEKGELGLPGlKGDRGEKGEagpagppglpgttslftphprmPGEQGPKGEKGDPGLPGEPGLQGRPGElg 879
Cdd:NF038329  213 GPDGEAGPAGEDGPAGPAG-DGQQGPDGD----------------------PGPTGEDGPQGPDGPAGKDGPRGDRGE-- 267

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611  880 pqgptgppgakgqegahgapgaagnpgapghvgapgpsgppgsvgaPGLRGTPGKDGERGEKGAAGEEGSPGPVGPrgdp 959
Cdd:NF038329  268 ----------------------------------------------AGPDGPDGKDGERGPVGPAGKDGQNGKDGL---- 297

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767952611  960 gapglpgppgKGKDGEPGLRGSPGLPGPLGTKGDRGAPGIPGSPGSRGDPG 1010
Cdd:NF038329  298 ----------PGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1137-1353 2.65e-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: 89.58  E-value: 2.65e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611 1137 QGERGADGEVGQKGDQGHPGVPGFMGPPGNPGPPGADGIAGAAGPPGIQGSPGKEGPPGPQGPSGLPGIPGEEGKEGRDG 1216
Cdd:NF038329  131 AGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAG 210

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611 1217 KPGPPGEPGKAGEPGLPGPEGA--RGPPGFKGHTGDSGAPGPRGESGAMGLPGQEGLPGKDGDTGPtgpqgpqgpRGPPG 1294
Cdd:NF038329  211 PAGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK---------DGERG 281

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767952611 1295 KNGSPGSPGEPGPSGTPGQKGSKGENGSPGLPGFLGPRGPPGEPGEKGVPGKEGVPGKP 1353
Cdd:NF038329  282 PVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1137-1366 1.21e-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: 84.57  E-value: 1.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611 1137 QGERGADGEVGQKGDQGHPGVPGFMGPPGNPGPPGADGIAGAAGPPGIQGSpgkegppgpqgpsglpgiPGEEGKEGRDG 1216
Cdd:NF038329  119 KGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGE------------------AGPQGPAGKDG 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611 1217 KPGPPGEPGKAGEPGLPGPEGARGPPGFKGHTGDSGAPGPRGESGAMGLPGQeGLPGKDGDTGPTGPQGPQGPRGPPGKN 1296
Cdd:NF038329  181 EAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKD 259

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611 1297 GSPGSPGEPGPSGTPGQKGSKGENGSPGLPGFLGPRGPPGEPGEKGVPGKEGVPGKPGEPGFKGERGDPG 1366
Cdd:NF038329  260 GPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPG 329
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 2-209 1.63e-16

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: 81.52  E-value: 1.63e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611    2 AGLRGNAVAGLLWMLLLWSGGGGCQAQRAGCKSVHYDLVFLLDTSSSVGKED-FEKVRQWVANLVDTFevgPDRTRVGVV 80
Cdd:COG1240    58 LLALLLAALLLLLAVLLLLLALALAPLALARPQRGRDVVLVVDASGSMAAENrLEAAKGALLDFLDDY---RPRDRVGLV 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611   81 RYSDRPTTAFELGlfGSQEEVKAAARRLAYhGGNTNTGDALRYITARsfsphagGRPRDRAYKQVAILLTDGR---SQDL 157
Cdd:COG1240   135 AFGGEAEVLLPLT--RDREALKRALDELPP-GGGTPLGDALALALEL-------LKRADPARRKVIVLLTDGRdnaGRID 204

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767952611  158 VLDAAAAAHRAGIRIFAVGVG-EALKEE-LEEIASEpKSAHVFHVSDFNAIDKI 209
Cdd:COG1240   205 PLEAAELAAAAGIRIYTIGVGtEAVDEGlLREIAEA-TGGRYFRADDLSELAAI 257
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 935-1235 8.82e-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: 81.88  E-value: 8.82e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611  935 DGERGEKGAAGEEGSPGPVGPRGdpgapglpgppgkgKDGEPGLRGSPGLPGPLGTKGDRGAPGIPGSPGSRGDPGigva 1014
Cdd:NF038329  116 DGEKGEPGPAGPAGPAGEQGPRG--------------DRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAG---- 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611 1015 gppgpsgppgDKGSPGSRGLPGFPGPQGPAGRDGAPGNPGERGPPGKPGLSSLLSPgdinllakdvcndcppGPPGLPGL 1094
Cdd:NF038329  178 ----------KDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGE----------------DGPAGPAG 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611 1095 PGFKGDKGVPGKPGREGTEGKKGEAGPPGLPGPPGIAGPQGSQGERGADGEVGQKGDQGHPGvpgfmgppgnpgppgadg 1174
Cdd:NF038329  232 DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNG------------------ 293

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767952611 1175 iagAAGPPGiqgspgkegPPGPQGPSGLPGIPGEEGKEGRDGKPGPPGEPGKAGEPGLPGP 1235
Cdd:NF038329  294 ---KDGLPG---------KDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1207-1400 2.98e-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: 80.33  E-value: 2.98e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611 1207 GEEGKEGRDGKPGPPGEPGKAGEPGLPGPEGARGPPGFKGHTGDSGAPGPRGESGAMGLPGQEGLPGKDGDTGPTGPQGP 1286
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611 1287 QGPRGPPGKNGSPGSPGEPGPSGTPGQKGSKG-----ENGSPGLPGflgPRGPPGEPGEKGVPGKEGVPGKPGEPGFKGE 1361
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGpagdgQQGPDGDPG---PTGEDGPQGPDGPAGKDGPRGDRGEAGPDGP 273

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 767952611 1362 RGDPGIKGDKGPPGGKGQPGDPGIPGHKGHTGLMGPQGL 1400
Cdd:NF038329  274 DGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGL 312
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1255-1551 4.18e-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: 73.40  E-value: 4.18e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611 1255 GPRGESGAMGLPGQEGLPGKDGDTGPTGPQGPQGPRGPPGKNGSPGSPGEPGPSGTPGQKGSKGENGSPGLPGFLGPRGP 1334
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611 1335 PGEPGEKGVPGKEGVPGKPGEPGFKGERGDPGIKGDKGPPGGkgqpgdpgipGHKGHTGLMGPQGLPGENGPVGPPGPPG 1414
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPD----------GDPGPTGEDGPQGPDGPAGKDGPRGDRG 266

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611 1415 QPGFPGLRGESpsmetlrrliqeelgkqletrlayllaqmppaymkssqgrpgppgppgkdglpGRAGPMGEPGRPGQGG 1494
Cdd:NF038329  267 EAGPDGPDGKD-----------------------------------------------------GERGPVGPAGKDGQNG 293

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767952611 1495 LEGPSGPIGPKGERGAKGDPGAPGvglrgemGPPGIPGQPGEPGYAKDGLPGIPGPQ 1551
Cdd:NF038329  294 KDGLPGKDGKDGQNGKDGLPGKDG-------KDGQPGKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1228-1560 4.04e-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: 70.32  E-value: 4.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611 1228 GEPGLPGPEGARGPPGFKGHTGDSGAPGPRGESGAMGLPGQEGLPGKDGDTGPTgpqgpqgprgppgknGSPGSPGEPGP 1307
Cdd:NF038329  120 GEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ---------------GPAGKDGEAGA 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611 1308 SGTPGQKGSKGENGSPGlpgflgprgppgepgEKGVPGKEGVPGKPGEPGFKGERGDPGIKGDKGPPGGkgqpgdpgipG 1387
Cdd:NF038329  185 KGPAGEKGPQGPRGETG---------------PAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPD----------G 239

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611 1388 HKGHTGLMGPQGLPGENGPVGPPGPPGQPGFPGLRGESpsmetlrrliqeelgkqletrlayllaqmppaymkssqgrpg 1467
Cdd:NF038329  240 DPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKD------------------------------------------ 277

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611 1468 ppgppgkdglpGRAGPMGEPGRPGQGGLEGPSGPIGPKGERGAKGDPGAPGvglrgemgppgipgqpgepgyaKDGLPGI 1547
Cdd:NF038329  278 -----------GERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDG----------------------KDGQPGK 324

                         330
                  ....*....|...
gi 767952611 1548 PGPQGETGPAGHP 1560
Cdd:NF038329  325 DGLPGKDGKDGQP 337
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
505-692 2.85e-06

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 51.95  E-value: 2.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611  505 GPVGAPGPKGEKGDVGSLGLPGPPGRDGSKGMRGEPGELGEPGLPGEVGMRGPQGPPGLPGPPGRVGAPGLQGERGEKGT 584
Cdd:COG5164     7 GKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQN 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611  585 RGEKGERGLDGFPGKPGDTGQQGRPGPSGVAGPQGEKG-----DVGPAGPPGVPGSVVQQEGLKGEQGAPGPRGHQGA-- 657
Cdd:COG5164    87 QGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGsttppSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGStt 166

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 767952611  658 -PGPPGARGPIGPEGRDGPP--GLQGLRGKKGDMGPPG 692
Cdd:COG5164   167 pPGPGGSTTPPDDGGSTTPPnkGETGTDIPTGGTPRQG 204
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 764-818 2.78e-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: 43.25  E-value: 2.78e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 767952611   764 GLPGKPGLRGEIGEQGLAGRPGEKGEAGLPGAPGFPGVRGEKGDQGEKGELGLPG 818
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1228-1280 1.27e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 41.33  E-value: 1.27e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 767952611  1228 GEPGLPGPEGARGPPGFKGHTGDSGAPGPRGESGAMGLPGQEGLPGKDGDTGP 1280
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGA 53
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 484-540 1.58e-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: 40.94  E-value: 1.58e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 767952611   484 GEMGVAGPMGLPGPKGDIGAIGPVGAPGPKGEKGDVGSLGLPGPPGRDGSKGMRGEP 540
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
 
Name Accession Description Interval E-value
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 36-219 3.91e-60

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: 206.08  E-value: 3.91e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611   36 HYDLVFLLDTSSSVGKEDFEKVRQWVANLVDTFEVGPDRTRVGVVRYSDRPTTAFELGLFGSQEEVKAAARRLAYHGGNT 115
Cdd:cd01475     2 PTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611  116 NTGDALRYITARSFSPHAGGRPRDRAYKQVAILLTDGRSQDLVLDAAAAAHRAGIRIFAVGVGEALKEELEEIASEPKSA 195
Cdd:cd01475    82 MTGLAIQYAMNNAFSEAEGARPGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLAD 161

                         170       180
                  ....*....|....*....|....
gi 767952611  196 HVFHVSDFNAIDKIRGKLRRRLCE 219
Cdd:cd01475   162 HVFYVEDFSTIEELTKKFQGKICV 185
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 38-203 1.81e-55

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: 190.13  E-value: 1.81e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611   38 DLVFLLDTSSSVGKEDFEKVRQWVANLVDTFEVGPDRTRVGVVRYSDRPTTAFELGLFGSQEEVKAAARRLAYHGGNTNT 117
Cdd:cd01472     2 DIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTNT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611  118 GDALRYITARSFSPHAGGRPrdrAYKQVAILLTDGRSQDLVLDAAAAAHRAGIRIFAVGVGEALKEELEEIASEPKSAHV 197
Cdd:cd01472    82 GKALKYVRENLFTEASGSRE---GVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKELYV 158


                  ....*.
gi 767952611  198 FHVSDF 203
Cdd:cd01472   159 FNVADF 164
VWA pfam00092
von Willebrand factor type A domain;
38-212 5.28e-54

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 186.33  E-value: 5.28e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611    38 DLVFLLDTSSSVGKEDFEKVRQWVANLVDTFEVGPDRTRVGVVRYSDRPTTAFELGLFGSQEEVKAAARRLAYHGGNT-N 116
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTtN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611   117 TGDALRYITARSFSPHAGGRPRdraYKQVAILLTDGRSQDL-VLDAAAAAHRAGIRIFAVGVGEALKEELEEIASEPKSA 195
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPG---APKVVVLLTDGRSQDGdPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEG 157

                          170
                   ....*....|....*..
gi 767952611   196 HVFHVSDFNAIDKIRGK 212
Cdd:pfam00092  158 HVFTVSDFEALEDLQDQ 174
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 38-203 4.38e-53

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: 183.26  E-value: 4.38e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611   38 DLVFLLDTSSSVGKEDFEKVRQWVANLVDTFEVGPDRTRVGVVRYSDRPTTAFELGLFGSQEEVKAAARRLAYHGGNTNT 117
Cdd:cd01482     2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTRT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611  118 GDALRYITARSFSPHAGGRPRDRaykQVAILLTDGRSQDLVLDAAAAAHRAGIRIFAVGVGEALKEELEEIASEPKSAHV 197
Cdd:cd01482    82 GKALTHVREKNFTPDAGARPGVP---KVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHV 158


                  ....*.
gi 767952611  198 FHVSDF 203
Cdd:cd01482   159 FNVADF 164
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 37-198 1.56e-48

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: 170.16  E-value: 1.56e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611   37 YDLVFLLDTSSSVGKEDFEKVRQWVANLVDTFEVGPDRTRVGVVRYSDRPTTAFELGLFGSQEEVKAAARRLAYHGGN-T 115
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGgT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611  116 NTGDALRYITARSFSPhaggRPRDRAYKQVAILLTDGRSQDL--VLDAAAAAHRAGIRIFAVGVGEALKEELEEIASEPK 193
Cdd:cd01450    81 NTGKALQYALEQLFSE----SNARENVPKVIIVLTDGRSDDGgdPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPS 156


                  ....*
gi 767952611  194 SAHVF 198
Cdd:cd01450   157 ERHVF 161
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 38-209 3.03e-42

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: 152.99  E-value: 3.03e-42
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611     38 DLVFLLDTSSSVGKEDFEKVRQWVANLVDTFEVGPDRTRVGVVRYSDRPTTAFELGLFGSQEEVKAAARRLAYH-GGNTN 116
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611    117 TGDALRYITARSFSPHAGGRPRDRaykQVAILLTDGRSQDL---VLDAAAAAHRAGIRIFAVGVGEA-LKEELEEIASEP 192
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAP---KVVILITDGESNDGpkdLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLASAP 157

                           170
                    ....*....|....*..
gi 767952611    193 KSAHVFHVSDFNAIDKI 209
Cdd:smart00327  158 GGVYVFLPELLDLLIDL 174
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 38-203 5.13e-38

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: 140.15  E-value: 5.13e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611   38 DLVFLLDTSSSVGKEDFEKVRQWVANLVDTFEVGPDRTRVGVVRYSDRPTTAFELGLFGSQEEVKAAARRLAYHGGN-TN 116
Cdd:cd01481     2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSqLN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611  117 TGDALRYITARSFSPHAGGRPRDrAYKQVAILLTDGRSQDLVLDAAAAAHRAGIRIFAVGVGEALKEELEEIASEPKsaH 196
Cdd:cd01481    82 TGSALDYVVKNLFTKSAGSRIEE-GVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPS--F 158


                  ....*..
gi 767952611  197 VFHVSDF 203
Cdd:cd01481   159 VFQVSDF 165
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 38-209 4.31e-34

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: 129.40  E-value: 4.31e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611   38 DLVFLLDTSSSVGKEDFEKVRQWVANLVDTFEVGPDRTRVGVVRYSDRPTTAFELGLFGSQEEVKAAARRLAYHGGNTNT 117
Cdd:cd01469     2 DIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTNT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611  118 GDALRYITARSFSPHAGGRprdRAYKQVAILLTDGRSQD--LVLDAAAAAHRAGIRIFAVGVGEALK-----EELEEIAS 190
Cdd:cd01469    82 ATAIQYVVTELFSESNGAR---KDATKVLVVITDGESHDdpLLKDVIPQAEREGIIRYAIGVGGHFQrensrEELKTIAS 158

                         170
                  ....*....|....*....
gi 767952611  191 EPKSAHVFHVSDFNAIDKI 209
Cdd:cd01469   159 KPPEEHFFNVTDFAALKDI 177
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 239-426 6.05e-33

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


Pssm-ID: 214560  Cd Length: 184  Bit Score: 126.32  E-value: 6.05e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611    239 GTKEITGFDLMDL-FSVKEILGKRenGAQSSYvRMGSFPVV-QSTEDVFPQGLPDEYAFVTTFRFRKTSRkedWYIWQVI 316
Cdd:smart00210    1 GQDLLQVFDLPSLsFAIRQVVGPE--PGSPAY-RLGDPALVpQPTRDLFPSGLPEDFSLLTTFRQTPKSR---GVLFAIY 74

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611    317 DQYSIPQVSIRLDGENKAVEYNAVGAMKDAVRVVFRGSrvnDLFDRDWHKMALSIQAQNVSLHIDCALVQTLPIEER--E 394
Cdd:smart00210   75 DAQNVRQFGLEVDGRANTLLLRYQGVDGKQHTVSFRNL---PLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPgqP 151

                           170       180       190
                    ....*....|....*....|....*....|..
gi 767952611    395 NIDIQGKTVIGKRLYDSVPIDFDLQRIVIYCD 426
Cdd:smart00210  152 PIDTDGIEVRGAQAADRKPFQGDLQQLKIVCD 183
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 37-198 9.02e-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: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 122.29  E-value: 9.02e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611   37 YDLVFLLDTSSSVGKEDFEKVRQWVANLVDTFEVGPDRTRVGVVRYSDRPTTAFELGLFGSQEEVKAAARRL-AYHGGNT 115
Cdd:cd00198     1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALkKGLGGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611  116 NTGDALRYItARSFSphaggRPRDRAYKQVAILLTDGRSQD---LVLDAAAAAHRAGIRIFAVGVG-EALKEELEEIASE 191
Cdd:cd00198    81 NIGAALRLA-LELLK-----SAKRPNARRVIILLTDGEPNDgpeLLAEAARELRKLGITVYTIGIGdDANEDELKEIADK 154


                  ....*..
gi 767952611  192 PKSAHVF 198
Cdd:cd00198   155 TTGGAVF 161
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 479-690 1.72e-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: 120.78  E-value: 1.72e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611  479 PAGEKGEMGVAGPMGLPGPKGDIGAIGPVGAPGPKGEKGDVGSLGLPGPPGRDGSKGMRGEPGELGEPGLPGEVGMRGPQ 558
Cdd:NF038329  139 DRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEA 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611  559 GPPGLPGPPGRVGaPGLQGERGEKGTRGEKGERGLDGFPGKPGDTGQQGRPGPSGVAGPQGEKGDVGPAGPPGvpgsvvq 638
Cdd:NF038329  219 GPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDG------- 290

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767952611  639 QEGLKGEQGAPGPRGHQGAPGPPGARGPIGPEGRDGPPGLQGLRGKKGDMGP 690
Cdd:NF038329  291 QNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 481-809 2.35e-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: 120.40  E-value: 2.35e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611  481 GEKGEMGVAGPMGLPGPKGDIGAIGPVGAPGPKGEKGDVGSLGLPGPPGRDGSKGMRGEPGELGEpglpgevgmrgpqgp 560
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGE--------------- 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611  561 pglpgppgrvgaPGLQGERGEKGTRGEKGERGLDGFPGKPGDTGQQGRPGPSGVAGPQGEKGDvgpagppgvpgsvvqqe 640
Cdd:NF038329  182 ------------AGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD----------------- 232

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611  641 GLKGEQGAPGPRGHQGAPGPPGARGPIGPEGRDGPPGLQGLRGKKGDMGPPGipgllglqgppgppgvpgppgpggspgl 720
Cdd:NF038329  233 GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVG---------------------------- 284

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611  721 pgeigfpgkpgppgptgppgkdgpngppgppgTKGEPGERGEDGLPGKPGLRGEIGEQGLagrPGEKGEAGLPGAPGFPG 800
Cdd:NF038329  285 --------------------------------PAGKDGQNGKDGLPGKDGKDGQNGKDGL---PGKDGKDGQPGKDGLPG 329


                  ....*....
gi 767952611  801 VRGEKGDQG 809
Cdd:NF038329  330 KDGKDGQPG 338
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 38-197 1.92e-24

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: 102.08  E-value: 1.92e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611   38 DLVFLLDTSSSVGKEDFEKVRQWVANLVDTFEVG------PDRTRVGVVRYSDRPTTAF-ELGLFGSQEEVKAAARRLAY 110
Cdd:cd01480     4 DITFVLDSSESVGLQNFDITKNFVKRVAERFLKDyyrkdpAGSWRVGVVQYSDQQEVEAgFLRDIRNYTSLKEAVDNLEY 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611  111 HGGNTNTGDALRYITARSF-SPHAGGrprdrayKQVAILLTDGRSQ----DLVLDAAAAAHRAGIRIFAVGVGEALKEEL 185
Cdd:cd01480    84 IGGGTFTDCALKYATEQLLeGSHQKE-------NKFLLVITDGHSDgspdGGIEKAVNEADHLGIKIFFVAVGSQNEEPL 156

                         170
                  ....*....|..
gi 767952611  186 EEIASEPKSAHV 197
Cdd:cd01480   157 SRIACDGKSALY 168
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 38-198 3.06e-24

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: 100.94  E-value: 3.06e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611   38 DLVFLLDTSSSVgKEDFEKVRQWVANLVDTFEVGPDRTRVGVVRYSDRPTT--AFELGLFGSQEEVKAAARRLAYHGGNT 115
Cdd:cd01476     2 DLLFVLDSSGSV-RGKFEKYKKYIERIVEGLEIGPTATRVALITYSGRGRQrvRFNLPKHNDGEELLEKVDNLRFIGGTT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611  116 NTGDALRYiTARSFSPHAGGRPRdraYKQVAILLTDGRSQDLVLDAAAAAHR-AGIRIFAVGVGE---ALKEELEEIASE 191
Cdd:cd01476    81 ATGAAIEV-ALQQLDPSEGRREG---IPKVVVVLTDGRSHDDPEKQARILRAvPNIETFAVGTGDpgtVDTEELHSITGN 156


                  ....*..
gi 767952611  192 PKsaHVF 198
Cdd:cd01476   157 ED--HIF 161
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 785-1064 1.01e-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: 100.36  E-value: 1.01e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611  785 GEKGEAGLPGAPGFPGVRGEKGDQGEKGELGLPGLKGDRGEKGEagpagppglpgttslftphprmPGEQGPKGEKGDPG 864
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGE----------------------KGPAGPQGEAGPQG 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611  865 LPGEPGLQGrpgelgpqgptgppgakgqegahgapgaagnpgapghvgapgpsgppgsvgAPGLRGTPGKDGERGEKGAA 944
Cdd:NF038329  175 PAGKDGEAG---------------------------------------------------AKGPAGEKGPQGPRGETGPA 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611  945 GEEGSPGPVGPRGDPGAPGLPGPPGKGKDGEPGLRGSPGLPGPLGTKGDRGAPGIPGSPGSRGDPGIGVAGPPGPSGPPG 1024
Cdd:NF038329  204 GEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPV 283

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 767952611 1025 DK----GSPGSRGLPGFPGPQGPAGRDGAPGNPGERGPPGKPGL 1064
Cdd:NF038329  284 GPagkdGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGL 327
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 640-1010 5.87e-20

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 94.97  E-value: 5.87e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611  640 EGLKGEQGAPGPRGHQGAPGPPGARGPIGPEGRDGPPGLQGLRGKKGDMGPPGipgllglqgppgppgvpgppgpggspg 719
Cdd:NF038329  116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQG--------------------------- 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611  720 lpgeigfpgkpgppgptgppgkdgpngppgppgtkgEPGERGEDGLPGKPGLRGEIGEQGLAGRPGEKGEAGLPGAPGFP 799
Cdd:NF038329  169 ------------------------------------EAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPA 212

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611  800 GVRGEKGDQGEKGELGLPGlKGDRGEKGEagpagppglpgttslftphprmPGEQGPKGEKGDPGLPGEPGLQGRPGElg 879
Cdd:NF038329  213 GPDGEAGPAGEDGPAGPAG-DGQQGPDGD----------------------PGPTGEDGPQGPDGPAGKDGPRGDRGE-- 267

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611  880 pqgptgppgakgqegahgapgaagnpgapghvgapgpsgppgsvgaPGLRGTPGKDGERGEKGAAGEEGSPGPVGPrgdp 959
Cdd:NF038329  268 ----------------------------------------------AGPDGPDGKDGERGPVGPAGKDGQNGKDGL---- 297

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767952611  960 gapglpgppgKGKDGEPGLRGSPGLPGPLGTKGDRGAPGIPGSPGSRGDPG 1010
Cdd:NF038329  298 ----------PGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1137-1353 2.65e-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: 89.58  E-value: 2.65e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611 1137 QGERGADGEVGQKGDQGHPGVPGFMGPPGNPGPPGADGIAGAAGPPGIQGSPGKEGPPGPQGPSGLPGIPGEEGKEGRDG 1216
Cdd:NF038329  131 AGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAG 210

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611 1217 KPGPPGEPGKAGEPGLPGPEGA--RGPPGFKGHTGDSGAPGPRGESGAMGLPGQEGLPGKDGDTGPtgpqgpqgpRGPPG 1294
Cdd:NF038329  211 PAGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK---------DGERG 281

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767952611 1295 KNGSPGSPGEPGPSGTPGQKGSKGENGSPGLPGFLGPRGPPGEPGEKGVPGKEGVPGKP 1353
Cdd:NF038329  282 PVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1137-1366 1.21e-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: 84.57  E-value: 1.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611 1137 QGERGADGEVGQKGDQGHPGVPGFMGPPGNPGPPGADGIAGAAGPPGIQGSpgkegppgpqgpsglpgiPGEEGKEGRDG 1216
Cdd:NF038329  119 KGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGE------------------AGPQGPAGKDG 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611 1217 KPGPPGEPGKAGEPGLPGPEGARGPPGFKGHTGDSGAPGPRGESGAMGLPGQeGLPGKDGDTGPTGPQGPQGPRGPPGKN 1296
Cdd:NF038329  181 EAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKD 259

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611 1297 GSPGSPGEPGPSGTPGQKGSKGENGSPGLPGFLGPRGPPGEPGEKGVPGKEGVPGKPGEPGFKGERGDPG 1366
Cdd:NF038329  260 GPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPG 329
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 2-209 1.63e-16

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: 81.52  E-value: 1.63e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611    2 AGLRGNAVAGLLWMLLLWSGGGGCQAQRAGCKSVHYDLVFLLDTSSSVGKED-FEKVRQWVANLVDTFevgPDRTRVGVV 80
Cdd:COG1240    58 LLALLLAALLLLLAVLLLLLALALAPLALARPQRGRDVVLVVDASGSMAAENrLEAAKGALLDFLDDY---RPRDRVGLV 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611   81 RYSDRPTTAFELGlfGSQEEVKAAARRLAYhGGNTNTGDALRYITARsfsphagGRPRDRAYKQVAILLTDGR---SQDL 157
Cdd:COG1240   135 AFGGEAEVLLPLT--RDREALKRALDELPP-GGGTPLGDALALALEL-------LKRADPARRKVIVLLTDGRdnaGRID 204

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767952611  158 VLDAAAAAHRAGIRIFAVGVG-EALKEE-LEEIASEpKSAHVFHVSDFNAIDKI 209
Cdd:COG1240   205 PLEAAELAAAAGIRIYTIGVGtEAVDEGlLREIAEA-TGGRYFRADDLSELAAI 257
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 38-217 4.87e-16

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 80.53  E-value: 4.87e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611   38 DLVFLLDTSSSVGKEDFEKVRQWVANLVDTFevgPDRTRVGVVRYSDRPTTAFELGLFGSQEEVKAAARRLaYHGGNTNT 117
Cdd:COG2304    93 NLVFVIDVSGSMSGDKLELAKEAAKLLVDQL---RPGDRVSIVTFAGDARVLLPPTPATDRAKILAAIDRL-QAGGGTAL 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611  118 GDALRYITARSFSPHAGGRPRdraykqVAILLTDGR------SQDLVLDAAAAAHRAGIRIFAVGVGEALKEE-LEEIAS 190
Cdd:COG2304   169 GAGLELAYELARKHFIPGRVN------RVILLTDGDanvgitDPEELLKLAEEAREEGITLTTLGVGSDYNEDlLERLAD 242

                         170       180
                  ....*....|....*....|....*..
gi 767952611  191 EPKSAHvFHVSDFNAIDKIRGKLRRRL 217
Cdd:COG2304   243 AGGGNY-YYIDDPEEAEKVFVREFSRI 268
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 935-1235 8.82e-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: 81.88  E-value: 8.82e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611  935 DGERGEKGAAGEEGSPGPVGPRGdpgapglpgppgkgKDGEPGLRGSPGLPGPLGTKGDRGAPGIPGSPGSRGDPGigva 1014
Cdd:NF038329  116 DGEKGEPGPAGPAGPAGEQGPRG--------------DRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAG---- 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611 1015 gppgpsgppgDKGSPGSRGLPGFPGPQGPAGRDGAPGNPGERGPPGKPGLSSLLSPgdinllakdvcndcppGPPGLPGL 1094
Cdd:NF038329  178 ----------KDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGE----------------DGPAGPAG 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611 1095 PGFKGDKGVPGKPGREGTEGKKGEAGPPGLPGPPGIAGPQGSQGERGADGEVGQKGDQGHPGvpgfmgppgnpgppgadg 1174
Cdd:NF038329  232 DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNG------------------ 293

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767952611 1175 iagAAGPPGiqgspgkegPPGPQGPSGLPGIPGEEGKEGRDGKPGPPGEPGKAGEPGLPGP 1235
Cdd:NF038329  294 ---KDGLPG---------KDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1207-1400 2.98e-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: 80.33  E-value: 2.98e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611 1207 GEEGKEGRDGKPGPPGEPGKAGEPGLPGPEGARGPPGFKGHTGDSGAPGPRGESGAMGLPGQEGLPGKDGDTGPTGPQGP 1286
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611 1287 QGPRGPPGKNGSPGSPGEPGPSGTPGQKGSKG-----ENGSPGLPGflgPRGPPGEPGEKGVPGKEGVPGKPGEPGFKGE 1361
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGpagdgQQGPDGDPG---PTGEDGPQGPDGPAGKDGPRGDRGEAGPDGP 273

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 767952611 1362 RGDPGIKGDKGPPGGKGQPGDPGIPGHKGHTGLMGPQGL 1400
Cdd:NF038329  274 DGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGL 312
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 36-209 3.85e-14

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: 72.54  E-value: 3.85e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611   36 HYDLVFLLDTSSSVGKEDFEkVRQWVANLVDTFeVGPDrTRVGVVRYSDRPTTAFELGLFGSQEEVKAAARRLAYHGGNT 115
Cdd:cd01474     4 HFDLYFVLDKSGSVAANWIE-IYDFVEQLVDRF-NSPG-LRFSFITFSTRATKILPLTDDSSAIIKGLEVLKKVTPSGQT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611  116 NTGDALRYITARSFSPHAGGRPRDRaykqVAILLTDGR-SQDLVLDAAAAAHRA---GIRIFAVGVGEALKEELEEIASE 191
Cdd:cd01474    81 YIHEGLENANEQIFNRNGGGRETVS----VIIALTDGQlLLNGHKYPEHEAKLSrklGAIVYCVGVTDFLKSQLINIADS 156

                         170
                  ....*....|....*....
gi 767952611  192 PKsaHVFHVSD-FNAIDKI 209
Cdd:cd01474   157 KE--YVFPVTSgFQALSGI 173
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 38-184 2.27e-13

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: 70.11  E-value: 2.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611   38 DLVFLLDTSSSVGKED-FEKVRQWVANLVDTFEVGPDRTRVGVVRYSDRPTTAFELGLFGSQEE-----VKAAARRLAYH 111
Cdd:cd01471     2 DLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPNSTNKdlalnAIRALLSLYYP 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767952611  112 GGNTNTGDALRYITARSFSpHAGGRPRdraYKQVAILLTDGRSQDL--VLDAAAAAHRAGIRIFAVGVGEALKEE 184
Cdd:cd01471    82 NGSTNTTSALLVVEKHLFD-TRGNREN---APQLVIIMTDGIPDSKfrTLKEARKLRERGVIIAVLGVGQGVNHE 152
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1255-1551 4.18e-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: 73.40  E-value: 4.18e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611 1255 GPRGESGAMGLPGQEGLPGKDGDTGPTGPQGPQGPRGPPGKNGSPGSPGEPGPSGTPGQKGSKGENGSPGLPGFLGPRGP 1334
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611 1335 PGEPGEKGVPGKEGVPGKPGEPGFKGERGDPGIKGDKGPPGGkgqpgdpgipGHKGHTGLMGPQGLPGENGPVGPPGPPG 1414
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPD----------GDPGPTGEDGPQGPDGPAGKDGPRGDRG 266

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611 1415 QPGFPGLRGESpsmetlrrliqeelgkqletrlayllaqmppaymkssqgrpgppgppgkdglpGRAGPMGEPGRPGQGG 1494
Cdd:NF038329  267 EAGPDGPDGKD-----------------------------------------------------GERGPVGPAGKDGQNG 293

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767952611 1495 LEGPSGPIGPKGERGAKGDPGAPGvglrgemGPPGIPGQPGEPGYAKDGLPGIPGPQ 1551
Cdd:NF038329  294 KDGLPGKDGKDGQNGKDGLPGKDG-------KDGQPGKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1228-1560 4.04e-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: 70.32  E-value: 4.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611 1228 GEPGLPGPEGARGPPGFKGHTGDSGAPGPRGESGAMGLPGQEGLPGKDGDTGPTgpqgpqgprgppgknGSPGSPGEPGP 1307
Cdd:NF038329  120 GEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ---------------GPAGKDGEAGA 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611 1308 SGTPGQKGSKGENGSPGlpgflgprgppgepgEKGVPGKEGVPGKPGEPGFKGERGDPGIKGDKGPPGGkgqpgdpgipG 1387
Cdd:NF038329  185 KGPAGEKGPQGPRGETG---------------PAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPD----------G 239

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611 1388 HKGHTGLMGPQGLPGENGPVGPPGPPGQPGFPGLRGESpsmetlrrliqeelgkqletrlayllaqmppaymkssqgrpg 1467
Cdd:NF038329  240 DPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKD------------------------------------------ 277

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611 1468 ppgppgkdglpGRAGPMGEPGRPGQGGLEGPSGPIGPKGERGAKGDPGAPGvglrgemgppgipgqpgepgyaKDGLPGI 1547
Cdd:NF038329  278 -----------GERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDG----------------------KDGQPGK 324

                         330
                  ....*....|...
gi 767952611 1548 PGPQGETGPAGHP 1560
Cdd:NF038329  325 DGLPGKDGKDGQP 337
VWA_2 pfam13519
von Willebrand factor type A domain;
39-149 1.40e-11

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 62.69  E-value: 1.40e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611    39 LVFLLDTSSSVGKED-----FEKVRQWVANLVDTFevgpDRTRVGVVRYSDRPTTafELGLFGSQEEVKAAARRLAYHGG 113
Cdd:pfam13519    1 LVFVLDTSGSMRNGDygptrLEAAKDAVLALLKSL----PGDRVGLVTFGDGPEV--LIPLTKDRAKILRALRRLEPKGG 74

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 767952611   114 NTNTGDALRYitARSFSPHaggrpRDRAYKQVAILL 149
Cdd:pfam13519   75 GTNLAAALQL--ARAALKH-----RRKNQPRRIVLI 103
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 38-191 2.14e-10

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 63.16  E-value: 2.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611   38 DLVFLLDTSSSVGKEDFEKVRQWVANLVDTFEvgPDRtRVGVVRYSDRPTTAFELglfGSQEEVKAAARRLA--YHGGNT 115
Cdd:COG2425   120 PVVLCVDTSGSMAGSKEAAAKAAALALLRALR--PNR-RFGVILFDTEVVEDLPL---TADDGLEDAIEFLSglFAGGGT 193

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767952611  116 NTGDALRYitarsfsphAGGRPRDRAYKQ-VAILLTDGRSQDLVLD--AAAAAHRAGIRIFAVGVGEALKEELEEIASE 191
Cdd:COG2425   194 DIAPALRA---------ALELLEEPDYRNaDIVLITDGEAGVSPEEllREVRAKESGVRLFTVAIGDAGNPGLLEALAD 263
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
40-209 1.57e-09

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 59.17  E-value: 1.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611   40 VFLLDTSSSVGKEDFEKVRQWVANLVDTFEVGP---DRTRVGVVRYSDRPTTAFELglfgsQEEVKAAARRLAYHGGnTN 116
Cdd:COG4245     9 YLLLDTSGSMSGEPIEALNEGLQALIDELRQDPyalETVEVSVITFDGEAKVLLPL-----TDLEDFQPPDLSASGG-TP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611  117 TGDALRYITARSFSPHAGGRP-RDRAYKQVAILLTDGRSQDL-------VLDAAAAAHRAGirIFAVGVG-EALKEELEE 187
Cdd:COG4245    83 LGAALELLLDLIERRVQKYTAeGKGDWRPVVFLITDGEPTDSdweaalqRLKDGEAAKKAN--IFAIGVGpDADTEVLKQ 160

                         170       180
                  ....*....|....*....|..
gi 767952611  188 IASEPKsahVFHVSDFNAIDKI 209
Cdd:COG4245   161 LTDPVR---ALDALDGLDFREF 179
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 39-189 1.92e-08

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: 55.36  E-value: 1.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611   39 LVFLLDTSSSVGKEDFEKVRQWVANLVDTFEvgpDRTRVGVVRYSDRPTTAFELGLFGSQEEVKAAARRLAyHGGNTN-- 116
Cdd:cd01465     3 LVFVIDRSGSMDGPKLPLVKSALKLLVDQLR---PDDRLAIVTYDGAAETVLPATPVRDKAAILAAIDRLT-AGGSTAgg 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611  117 TGDALRYITA-RSFSPHAGGRprdraykqvAILLTDG------RSQDLVLDAAAAAHRAGIRIFAVGVGEALKEEL-EEI 188
Cdd:cd01465    79 AGIQLGYQEAqKHFVPGGVNR---------ILLATDGdfnvgeTDPDELARLVAQKRESGITLSTLGFGDNYNEDLmEAI 149


                  .
gi 767952611  189 A 189
Cdd:cd01465   150 A 150
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 42-202 1.05e-07

Complement factors B and C2 are two critical proteases for complement activation. They both contain three CCP or Sushi domains, a trypsin-type serine protease domain and a single VWA domain with a conserved metal ion dependent adhesion site referred commonly as the MIDAS motif. Orthologues of these molecules are found from echinoderms to chordates. During complement activation, the CCP domains are cleaved off, resulting in the formation of an active protease that cleaves and activates complement C3. Complement C2 is in the classical pathway and complement B is in the alternative pathway. The interaction of C2 with C4 and of factor B with C3b are both dependent on Mg2+ binding sites within the VWA domains and the VWA domain of factor B has been shown to mediate the binding of C3. This is consistent with the common inferred function of VWA domains as magnesium-dependent protein interaction domains.


Pssm-ID: 238747 [Multi-domain]  Cd Length: 198  Bit Score: 53.83  E-value: 1.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611   42 LLDTSSSVGKEDFEKVRQWVANLVD---TFEVGPdrtRVGVVRYSDRPTTAFELGLFGSQeEVKAAARRLA---Y--HGG 113
Cdd:cd01470     6 ALDASDSIGEEDFDEAKNAIKTLIEkisSYEVSP---RYEIISYASDPKEIVSIRDFNSN-DADDVIKRLEdfnYddHGD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611  114 N--TNTGDALRYITARSFSPHAGGRPRDRAYKQVAILLTDGRS----------QDLVLDAAAAAHRAGIR-----IFAVG 176
Cdd:cd01470    82 KtgTNTAAALKKVYERMALEKVRNKEAFNETRHVIILFTDGKSnmggsplptvDKIKNLVYKNNKSDNPRedyldVYVFG 161

                         170       180
                  ....*....|....*....|....*...
gi 767952611  177 VG-EALKEELEEIASE-PKSAHVFHVSD 202
Cdd:cd01470   162 VGdDVNKEELNDLASKkDNERHFFKLKD 189
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
505-692 2.85e-06

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 51.95  E-value: 2.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611  505 GPVGAPGPKGEKGDVGSLGLPGPPGRDGSKGMRGEPGELGEPGLPGEVGMRGPQGPPGLPGPPGRVGAPGLQGERGEKGT 584
Cdd:COG5164     7 GKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQN 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611  585 RGEKGERGLDGFPGKPGDTGQQGRPGPSGVAGPQGEKG-----DVGPAGPPGVPGSVVQQEGLKGEQGAPGPRGHQGA-- 657
Cdd:COG5164    87 QGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGsttppSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGStt 166

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 767952611  658 -PGPPGARGPIGPEGRDGPP--GLQGLRGKKGDMGPPG 692
Cdd:COG5164   167 pPGPGGSTTPPDDGGSTTPPnkGETGTDIPTGGTPRQG 204
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 764-818 2.78e-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: 43.25  E-value: 2.78e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 767952611   764 GLPGKPGLRGEIGEQGLAGRPGEKGEAGLPGAPGFPGVRGEKGDQGEKGELGLPG 818
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 759-813 3.00e-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: 42.87  E-value: 3.00e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 767952611   759 ERGEDGLPGKPGLRGEIGEQGLAGRPGEKGEAGLPGAPGFPGVRGEKGDQGEKGE 813
Cdd:pfam01391    2 PPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 37-189 1.10e-04

CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an important phenomenon in parasite invasion and in malaria associated pathology.CTRP encodes a protein containing a putative signal sequence followed by a long extracellular region of 1990 amino acids, a transmembrane domain, and a short cytoplasmic segment. The extracellular region of CTRP contains two separated adhesive domains. The first domain contains six 210-amino acid-long homologous VWA domain repeats. The second domain contains seven repeats of 87-60 amino acids in length, which share similarities with the thrombospondin type 1 domain found in a variety of adhesive molecules. Finally, CTRP also contains consensus motifs found in the superfamily of haematopoietin receptors. The VWA domains in these proteins likely mediate protein-protein interactions.


Pssm-ID: 238750 [Multi-domain]  Cd Length: 192  Bit Score: 45.00  E-value: 1.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611   37 YDLVFLLDTSSSVGKEDFEK-VRQWVANLVDTFEVGPDRTRVGVVRYSD--RPTTAFE----------LGLFGSQEEVKA 103
Cdd:cd01473     1 YDLTLILDESASIGYSNWRKdVIPFTEKIINNLNISKDKVHVGILLFAEknRDVVPFSdeerydknelLKKINDLKNSYR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611  104 AarrlayhGGNTNTGDALRYITARSFspHAGGRpRDRAYKqVAILLTDG----RSQDLVLDAAAAAHRAGIRIFAVGVGE 179
Cdd:cd01473    81 S-------GGETYIVEALKYGLKNYT--KHGNR-RKDAPK-VTMLFTDGndtsASKKELQDISLLYKEENVKLLVVGVGA 149

                         170
                  ....*....|
gi 767952611  180 ALKEELEEIA 189
Cdd:cd01473   150 ASENKLKLLA 159
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1228-1280 1.27e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 41.33  E-value: 1.27e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 767952611  1228 GEPGLPGPEGARGPPGFKGHTGDSGAPGPRGESGAMGLPGQEGLPGKDGDTGP 1280
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGA 53
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 484-540 1.58e-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: 40.94  E-value: 1.58e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 767952611   484 GEMGVAGPMGLPGPKGDIGAIGPVGAPGPKGEKGDVGSLGLPGPPGRDGSKGMRGEP 540
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 641-693 1.83e-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: 40.94  E-value: 1.83e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 767952611   641 GLKGEQGAPGPRGHQGAPGPPGARGPIGPEGRDGPPGLQGLRGKKGDMGPPGI 693
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGA 53
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 493-552 3.68e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.78  E-value: 3.68e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611   493 GLPGPKGDIGAIGPVGAPGPKGEKGDVGslgLPGPPGRDGSKGMRGEPGELGEPGLPGEV 552
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPG---PPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1227-1274 4.14e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.78  E-value: 4.14e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 767952611  1227 AGEPGLPGPEGARGPPGFKGHTGDSGAPGPRGESGAMGLPGQEGLPGK 1274
Cdd:pfam01391    9 PGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 998-1062 6.91e-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: 39.01  E-value: 6.91e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767952611   998 GIPGSPGSRGDPGigvagppgPSGPPGDKGSPGSRGLPGFPGPQGPAGRDGAPGNPGERGPPGKP 1062
Cdd:pfam01391    1 GPPGPPGPPGPPG--------PPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 779-829 1.34e-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: 38.24  E-value: 1.34e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 767952611   779 GLAGRPGEKGEAGLPGAPGFPGVRGEKGDQGEKGELGLPGLKGDRGEKGEA 829
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAP 51
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1297-1366 1.55e-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: 38.24  E-value: 1.55e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952611  1297 GSPGSPGEPGPSGTPGQKGSKGENGSPGLPGFlgprgppgepgekgvPGKEGVPGKPGEPGFKGERGDPG 1366
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGE---------------PGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 572-622 1.91e-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: 37.86  E-value: 1.91e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 767952611   572 APGLQGERGEKGTRGEKGERGLDGFPGKPGDTGQQGRPGPSGVAGPQGEKG 622
Cdd:pfam01391    5 PPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1249-1320 9.68e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 35.93  E-value: 9.68e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767952611  1249 GDSGAPGPRGESGAMGLPGQEGLPGKDGDTGPtgpqgpqgprgppgkNGSPGSPGEPGPSGTPGQKGSKGEN 1320
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGE---------------PGPPGPPGPPGPPGPPGAPGAPGPP 57
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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