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Conserved domains on  [gi|40805823|ref|NP_690848|]
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collagen alpha-1(XXII) chain precursor [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 3.89e-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: 3.89e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823   36 HYDLVFLLDTSSSVGKEDFEKVRQWVANLVDTFEVGPDRTRVGVVRYSDRPTTAFELGLFGSQEEVKAAARRLAYHGGNT 115
Cdd:cd01475    2 PTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823  116 NTGDALRYITARSFSPHAGGRPRDRAYKQVAILLTDGRSQDLVLDAAAAAHRAGIRIFAVGVGEALKEELEEIASEPKSA 195
Cdd:cd01475   82 MTGLAIQYAMNNAFSEAEGARPGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLAD 161
                        170       180
                 ....*....|....*....|....
gi 40805823  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 4.33e-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: 127.09  E-value: 4.33e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823     239 GTKEITGFDLMDL-FSVKEILGKRenGAQSSYvRMGSFPVV-QSTEDVFPQGLPDEYAFVTTFRFRKTSRkedWYIWQVI 316
Cdd:smart00210    1 GQDLLQVFDLPSLsFAIRQVVGPE--PGSPAY-RLGDPALVpQPTRDLFPSGLPEDFSLLTTFRQTPKSR---GVLFAIY 74
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823     317 DQYSIPQVSIRLDGENKAVEYNAVGAMKDAVRVVFRGSrvnDLFDRDWHKMALSIQAQNVSLHIDCALVQTLPIEER--E 394
Cdd:smart00210   75 DAQNVRQFGLEVDGRANTLLLRYQGVDGKQHTVSFRNL---PLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPgqP 151
                           170       180       190
                    ....*....|....*....|....*....|..
gi 40805823     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 ...
481-703 5.31e-29

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: 122.32  E-value: 5.31e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823   481 GEKGEMGVAGPMGLPGPKGDIGAIGPVGAPGPKGEKGDVGI----GPFG----QGEKGEKGSLGLPGPPGRDGSKGMRGE 552
Cdd:NF038329  120 GEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEkgpaGPQGeagpQGPAGKDGEAGAKGPAGEKGPQGPRGE 199
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823   553 PGELGEPGLPGEVGMRGPQGPPGLPGPPGRVGaPGLQGERGEKGTRGEKGERGLDGFPGKPGDTGQQGRPGPSGVAGPQG 632
Cdd:NF038329  200 TGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDG 278
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 40805823   633 EKGDVGPAGPPGvpgsvvqQEGLKGEQGAPGPRGHQGAPGPPGARGPIGPEGRDGPPGLQGLRGKKGDMGP 703
Cdd:NF038329  279 ERGPVGPAGKDG-------QNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
798-1097 8.70e-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.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 94.20  E-value: 8.70e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823   798 GEKGEAGLPGAPGFPGVRGEKGDQGEKGELGLPGLKGDRGEKGEagpagppglpgttslftphprmPGEQGPKGEKGDPG 877
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGE----------------------KGPAGPQGEAGPQG 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823   878 LPGEPGLQGrpgelgpqgptgppgakgqegahgapgaagnpgapghvgapgpsgppgsvgAPGLRGTPGKDGERGEKGAA 957
Cdd:NF038329  175 PAGKDGEAG---------------------------------------------------AKGPAGEKGPQGPRGETGPA 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823   958 GEEGSPGPVGPRGDPGAPGLPGPPGKGKDGEPGLRGSPGLPGPLGTKAACGKVrgsencalGGQCVKGDRGAPGIPGSPG 1037
Cdd:NF038329  204 GEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPA--------GKDGPRGDRGEAGPDGPDG 275
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823  1038 SRGDPGigvagppgPSGPPGDKGSPGSRGLPGFPGPQGPAGRDGAPGNPGERGPPGKPGL 1097
Cdd:NF038329  276 KDGERG--------PVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGL 327
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
1170-1386 2.62e-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: 2.62e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823  1170 QGERGADGEVGQKGDQGHPGVPGFMGPPGNPGPPGADGIAGAAGPPGIQGSPGKEGPPGPQGPSGLPGIPGEEGKEGRDG 1249
Cdd:NF038329  131 AGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAG 210
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823  1250 KPGPPGEPGKAGEPGLPGPEGA--RGPPGFKGHTGDSGAPGPRGESGAMGLPGQEGLPGKDGDTGPtgpqgpqgpRGPPG 1327
Cdd:NF038329  211 PAGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK---------DGERG 281
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 40805823  1328 KNGSPGSPGEPGPSGTPGQKGSKGENGSPGLPGFLGPRGPPGEPGEKGVPGKEGVPGKP 1386
Cdd:NF038329  282 PVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
1288-1584 4.07e-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: 4.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823  1288 GPRGESGAMGLPGQEGLPGKDGDTGPTGPQGPQGPRGPPGKNGSPGSPGEPGPSGTPGQKGSKGENGSPGLPGFLGPRGP 1367
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823  1368 PGEPGEKGVPGKEGVPGKPGEPGFKGERGDPGIKGDKGPPGGkgqpgdpgipGHKGHTGLMGPQGLPGENGPVGPPGPPG 1447
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPD----------GDPGPTGEDGPQGPDGPAGKDGPRGDRG 266
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823  1448 QPGFPGLRGESpsmetlrrliqeelgkqletrlayllaqmppaymkssqgrpgppgppgkdglpGRAGPMGEPGRPGQGG 1527
Cdd:NF038329  267 EAGPDGPDGKD-----------------------------------------------------GERGPVGPAGKDGQNG 293
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 40805823  1528 LEGPSGPIGPKGERGAKGDPGAPGvglrgemGPPGIPGQPGEPGYAKDGLPGIPGPQ 1584
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 3.89e-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: 3.89e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823   36 HYDLVFLLDTSSSVGKEDFEKVRQWVANLVDTFEVGPDRTRVGVVRYSDRPTTAFELGLFGSQEEVKAAARRLAYHGGNT 115
Cdd:cd01475    2 PTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823  116 NTGDALRYITARSFSPHAGGRPRDRAYKQVAILLTDGRSQDLVLDAAAAAHRAGIRIFAVGVGEALKEELEEIASEPKSA 195
Cdd:cd01475   82 MTGLAIQYAMNNAFSEAEGARPGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLAD 161
                        170       180
                 ....*....|....*....|....
gi 40805823  196 HVFHVSDFNAIDKIRGKLRRRLCE 219
Cdd:cd01475  162 HVFYVEDFSTIEELTKKFQGKICV 185
VWA pfam00092
von Willebrand factor type A domain;
38-212 5.39e-54

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 186.33  E-value: 5.39e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823     38 DLVFLLDTSSSVGKEDFEKVRQWVANLVDTFEVGPDRTRVGVVRYSDRPTTAFELGLFGSQEEVKAAARRLAYHGGNT-N 116
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTtN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823    117 TGDALRYITARSFSPHAGGRPRdraYKQVAILLTDGRSQDL-VLDAAAAAHRAGIRIFAVGVGEALKEELEEIASEPKSA 195
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPG---APKVVVLLTDGRSQDGdPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEG 157
                          170
                   ....*....|....*..
gi 40805823    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 3.13e-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: 3.13e-42
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823      38 DLVFLLDTSSSVGKEDFEKVRQWVANLVDTFEVGPDRTRVGVVRYSDRPTTAFELGLFGSQEEVKAAARRLAYH-GGNTN 116
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTN 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823     117 TGDALRYITARSFSPHAGGRPRDRaykQVAILLTDGRSQDL---VLDAAAAAHRAGIRIFAVGVGEA-LKEELEEIASEP 192
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAP---KVVILITDGESNDGpkdLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLASAP 157
                           170
                    ....*....|....*..
gi 40805823     193 KSAHVFHVSDFNAIDKI 209
Cdd:smart00327  158 GGVYVFLPELLDLLIDL 174
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
239-426 4.33e-33

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


Pssm-ID: 214560  Cd Length: 184  Bit Score: 127.09  E-value: 4.33e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823     239 GTKEITGFDLMDL-FSVKEILGKRenGAQSSYvRMGSFPVV-QSTEDVFPQGLPDEYAFVTTFRFRKTSRkedWYIWQVI 316
Cdd:smart00210    1 GQDLLQVFDLPSLsFAIRQVVGPE--PGSPAY-RLGDPALVpQPTRDLFPSGLPEDFSLLTTFRQTPKSR---GVLFAIY 74
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823     317 DQYSIPQVSIRLDGENKAVEYNAVGAMKDAVRVVFRGSrvnDLFDRDWHKMALSIQAQNVSLHIDCALVQTLPIEER--E 394
Cdd:smart00210   75 DAQNVRQFGLEVDGRANTLLLRYQGVDGKQHTVSFRNL---PLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPgqP 151
                           170       180       190
                    ....*....|....*....|....*....|..
gi 40805823     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 ...
481-703 5.31e-29

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: 122.32  E-value: 5.31e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823   481 GEKGEMGVAGPMGLPGPKGDIGAIGPVGAPGPKGEKGDVGI----GPFG----QGEKGEKGSLGLPGPPGRDGSKGMRGE 552
Cdd:NF038329  120 GEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEkgpaGPQGeagpQGPAGKDGEAGAKGPAGEKGPQGPRGE 199
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823   553 PGELGEPGLPGEVGMRGPQGPPGLPGPPGRVGaPGLQGERGEKGTRGEKGERGLDGFPGKPGDTGQQGRPGPSGVAGPQG 632
Cdd:NF038329  200 TGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDG 278
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 40805823   633 EKGDVGPAGPPGvpgsvvqQEGLKGEQGAPGPRGHQGAPGPPGARGPIGPEGRDGPPGLQGLRGKKGDMGP 703
Cdd:NF038329  279 ERGPVGPAGKDG-------QNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
530-822 2.18e-26

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 114.23  E-value: 2.18e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823   530 GEKGSLGLPGPPGRDGSKGMRGEPGELGEPGLPGEVGMRgpqgppglpGPPGRVGAPGLQGERGEKGTRGEKGERGLDGF 609
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQ---------GERGEKGPAGPQGEAGPQGPAGKDGEAGAKGP 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823   610 PGKPGDTGQQGRPGPSGVAGPQGEKG-DVGPAGPPGVPGSVVQQEGLKGEQGAPGPRGHQGAPGPPGARGPIGPEGRDGP 688
Cdd:NF038329  188 AGEKGPQGPRGETGPAGEQGPAGPAGpDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGE 267
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823   689 PGLQGLRGKKGDMGPPGipgllglqgppgppgvpgppgpggspglpgeigfpgkpgppgptgppgkdgpngppgppgTKG 768
Cdd:NF038329  268 AGPDGPDGKDGERGPVG------------------------------------------------------------PAG 287
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 40805823   769 EPGERGEDGLPGKPGLRGEIGEQGLagrPGEKGEAGLPGAPGFPGVRGEKGDQG 822
Cdd:NF038329  288 KDGQNGKDGLPGKDGKDGQNGKDGL---PGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
479-689 7.01e-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: 94.59  E-value: 7.01e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823   479 PAGEKGEMGVAGPMGLPGPKGDIGAIGPVGAPGPKGEKGDVG----IGPFG-QGEKGEKGSLGLPGPPGRDGS--KGMRG 551
Cdd:NF038329  160 EKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGpageQGPAGpAGPDGEAGPAGEDGPAGPAGDgqQGPDG 239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823   552 EPGELGEPGLPGEVGMRGPQGPPGLPGPPGRVGAPGLQGERGEKGTRGEKGERGLDGFPGKPGDTGQQGRPGPSGVAGpq 631
Cdd:NF038329  240 DPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDG-- 317
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 40805823   632 gekgdvgpagppgvpgsvvqQEGLKGEQGAPGPRGHQGAPGPPGARGPIGPEGRDGPP 689
Cdd:NF038329  318 --------------------KDGQPGKDGLPGKDGKDGQPGKPAPKTPEVPQKPDTAP 355
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
798-1097 8.70e-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: 94.20  E-value: 8.70e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823   798 GEKGEAGLPGAPGFPGVRGEKGDQGEKGELGLPGLKGDRGEKGEagpagppglpgttslftphprmPGEQGPKGEKGDPG 877
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGE----------------------KGPAGPQGEAGPQG 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823   878 LPGEPGLQGrpgelgpqgptgppgakgqegahgapgaagnpgapghvgapgpsgppgsvgAPGLRGTPGKDGERGEKGAA 957
Cdd:NF038329  175 PAGKDGEAG---------------------------------------------------AKGPAGEKGPQGPRGETGPA 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823   958 GEEGSPGPVGPRGDPGAPGLPGPPGKGKDGEPGLRGSPGLPGPLGTKAACGKVrgsencalGGQCVKGDRGAPGIPGSPG 1037
Cdd:NF038329  204 GEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPA--------GKDGPRGDRGEAGPDGPDG 275
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823  1038 SRGDPGigvagppgPSGPPGDKGSPGSRGLPGFPGPQGPAGRDGAPGNPGERGPPGKPGL 1097
Cdd:NF038329  276 KDGERG--------PVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGL 327
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
653-889 1.80e-19

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 93.43  E-value: 1.80e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823   653 EGLKGEQGAPGPRGHQGAPGPPGARGPIGPEGRDGPPGLQGLRGKKGDMGPPGIPGLLGLQGPPGPPGVPGPPGPGGSPG 732
Cdd:NF038329  116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823   733 LPGEiGFPGKPGPPGPTGPPGKDGPNGPPGPPGTKGEPGERGEDGLPGKPGLRGEIGEQGLAGRPGEKGEAGLPGAPGFP 812
Cdd:NF038329  196 PRGE-TGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPD 274
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823   813 GVRGEK------GDQGEKGELGLPGLKGDRGEKGEagpagppglpgttslftphPRMPGEQGPKGEKGDPGLPGEPGLQG 886
Cdd:NF038329  275 GKDGERgpvgpaGKDGQNGKDGLPGKDGKDGQNGK-------------------DGLPGKDGKDGQPGKDGLPGKDGKDG 335

                  ...
gi 40805823   887 RPG 889
Cdd:NF038329  336 QPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
1170-1386 2.62e-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: 2.62e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823  1170 QGERGADGEVGQKGDQGHPGVPGFMGPPGNPGPPGADGIAGAAGPPGIQGSPGKEGPPGPQGPSGLPGIPGEEGKEGRDG 1249
Cdd:NF038329  131 AGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAG 210
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823  1250 KPGPPGEPGKAGEPGLPGPEGA--RGPPGFKGHTGDSGAPGPRGESGAMGLPGQEGLPGKDGDTGPtgpqgpqgpRGPPG 1327
Cdd:NF038329  211 PAGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK---------DGERG 281
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 40805823  1328 KNGSPGSPGEPGPSGTPGQKGSKGENGSPGLPGFLGPRGPPGEPGEKGVPGKEGVPGKP 1386
Cdd:NF038329  282 PVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
2-209 1.17e-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: 81.91  E-value: 1.17e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823    2 AGLRGNAVAGLLWMLLLWSGGGGCQAQRAGCKSVHYDLVFLLDTSSSVGKED-FEKVRQWVANLVDTFevgPDRTRVGVV 80
Cdd:COG1240   58 LLALLLAALLLLLAVLLLLLALALAPLALARPQRGRDVVLVVDASGSMAAENrLEAAKGALLDFLDDY---RPRDRVGLV 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823   81 RYSDRPTTAFELGlfGSQEEVKAAARRLAYhGGNTNTGDALRYITARsfsphagGRPRDRAYKQVAILLTDGR---SQDL 157
Cdd:COG1240  135 AFGGEAEVLLPLT--RDREALKRALDELPP-GGGTPLGDALALALEL-------LKRADPARRKVIVLLTDGRdnaGRID 204
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 40805823  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 ...
1170-1399 1.24e-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: 1.24e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823  1170 QGERGADGEVGQKGDQGHPGVPGFMGPPGNPGPPGADGIAGAAGPPGIQGSpgkegppgpqgpsglpgiPGEEGKEGRDG 1249
Cdd:NF038329  119 KGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGE------------------AGPQGPAGKDG 180
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823  1250 KPGPPGEPGKAGEPGLPGPEGARGPPGFKGHTGDSGAPGPRGESGAMGLPGQeGLPGKDGDTGPTGPQGPQGPRGPPGKN 1329
Cdd:NF038329  181 EAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKD 259
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823  1330 GSPGSPGEPGPSGTPGQKGSKGENGSPGLPGFLGPRGPPGEPGEKGVPGKEGVPGKPGEPGFKGERGDPG 1399
Cdd:NF038329  260 GPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPG 329
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
1240-1433 3.08e-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: 3.08e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823  1240 GEEGKEGRDGKPGPPGEPGKAGEPGLPGPEGARGPPGFKGHTGDSGAPGPRGESGAMGLPGQEGLPGKDGDTGPTGPQGP 1319
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823  1320 QGPRGPPGKNGSPGSPGEPGPSGTPGQKGSKG-----ENGSPGLPGflgPRGPPGEPGEKGVPGKEGVPGKPGEPGFKGE 1394
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGpagdgQQGPDGDPG---PTGEDGPQGPDGPAGKDGPRGDRGEAGPDGP 273
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 40805823  1395 RGDPGIKGDKGPPGGKGQPGDPGIPGHKGHTGLMGPQGL 1433
Cdd:NF038329  274 DGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGL 312
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
1288-1584 4.07e-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: 4.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823  1288 GPRGESGAMGLPGQEGLPGKDGDTGPTGPQGPQGPRGPPGKNGSPGSPGEPGPSGTPGQKGSKGENGSPGLPGFLGPRGP 1367
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823  1368 PGEPGEKGVPGKEGVPGKPGEPGFKGERGDPGIKGDKGPPGGkgqpgdpgipGHKGHTGLMGPQGLPGENGPVGPPGPPG 1447
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPD----------GDPGPTGEDGPQGPDGPAGKDGPRGDRG 266
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823  1448 QPGFPGLRGESpsmetlrrliqeelgkqletrlayllaqmppaymkssqgrpgppgppgkdglpGRAGPMGEPGRPGQGG 1527
Cdd:NF038329  267 EAGPDGPDGKD-----------------------------------------------------GERGPVGPAGKDGQNG 293
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 40805823  1528 LEGPSGPIGPKGERGAKGDPGAPGvglrgemGPPGIPGQPGEPGYAKDGLPGIPGPQ 1584
Cdd:NF038329  294 KDGLPGKDGKDGQNGKDGLPGKDG-------KDGQPGKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
948-1268 1.21e-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: 71.86  E-value: 1.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823   948 DGERGEKGAAGEEGSPGPVGPRGdpgapglpgppgkgKDGEPGLRGSPGLPGPLGTKAACGkvrgsencALGGQCVKGDR 1027
Cdd:NF038329  116 DGEKGEPGPAGPAGPAGEQGPRG--------------DRGETGPAGPAGPPGPQGERGEKG--------PAGPQGEAGPQ 173
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823  1028 GAPGIPGSPGSRGDPGigvagppgpsgppgDKGSPGSRGLPGFPGPQGPAGRDGAPGNPGERGPPGKPGLSSLLSPGDIN 1107
Cdd:NF038329  174 GPAGKDGEAGAKGPAG--------------EKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDG 239
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823  1108 LLAKDvcndcppgppglpglpGFKGDKGVPGKPGREGTEGKKGEAGPPGLPGPPGIagpqgsQGERGADGEVGQKGDQGH 1187
Cdd:NF038329  240 DPGPT----------------GEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGE------RGPVGPAGKDGQNGKDGL 297
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823  1188 PGvpgfmgppgnpgppgadgiagaagppgiqgspgkegPPGPQGPSGLPGIPGEEGKEGRDGKPGPPGEPGKAGEPGLPG 1267
Cdd:NF038329  298 PG------------------------------------KDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPA 341

                  .
gi 40805823  1268 P 1268
Cdd:NF038329  342 P 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
1261-1593 4.06e-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: 4.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823  1261 GEPGLPGPEGARGPPGFKGHTGDSGAPGPRGESGAMGLPGQEGLPGKDGDTGPTgpqgpqgprgppgknGSPGSPGEPGP 1340
Cdd:NF038329  120 GEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ---------------GPAGKDGEAGA 184
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823  1341 SGTPGQKGSKGENGSPGlpgflgprgppgepgEKGVPGKEGVPGKPGEPGFKGERGDPGIKGDKGPPGGkgqpgdpgipG 1420
Cdd:NF038329  185 KGPAGEKGPQGPRGETG---------------PAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPD----------G 239
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823  1421 HKGHTGLMGPQGLPGENGPVGPPGPPGQPGFPGLRGESpsmetlrrliqeelgkqletrlayllaqmppaymkssqgrpg 1500
Cdd:NF038329  240 DPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKD------------------------------------------ 277
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823  1501 ppgppgkdglpGRAGPMGEPGRPGQGGLEGPSGPIGPKGERGAKGDPGAPGvglrgemgppgipgqpgepgyaKDGLPGI 1580
Cdd:NF038329  278 -----------GERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDG----------------------KDGQPGK 324
                         330
                  ....*....|...
gi 40805823  1581 PGPQGETGPAGHP 1593
Cdd:NF038329  325 DGLPGKDGKDGQP 337
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
777-831 2.38e-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: 2.38e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 40805823    777 GLPGKPGLRGEIGEQGLAGRPGEKGEAGLPGAPGFPGVRGEKGDQGEKGELGLPG 831
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
511-705 9.99e-05

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 46.95  E-value: 9.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823  511 GPKGEKGDVGIGPFGQGekGEKGSLGLPGPPGRDGSKGMRGEPGELGEPGLPGEVGMRGPQGPPGLPGPPGRVGAPGLQG 590
Cdd:COG5164    2 GLYGPGKTGPSDPGGVT--TPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823  591 ERGEKGTRGEKGERGLDGFPGKPGDTGQQGRPGPSGVAGPQGEKG-----DVGPAGPPGVPGSVVQQEGLKGEQGAPGPR 665
Cdd:COG5164   80 GTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGsttppSGGSTTPPGDGGSTPPGPGSTGPGGSTTPP 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 40805823  666 GHQGA---PGPPGARGPIGPEGRDGPP--GLQGLRGKKGDMGPPG 705
Cdd:COG5164  160 GDGGSttpPGPGGSTTPPDDGGSTTPPnkGETGTDIPTGGTPRQG 204
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1261-1313 1.10e-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: 1.10e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 40805823   1261 GEPGLPGPEGARGPPGFKGHTGDSGAPGPRGESGAMGLPGQEGLPGKDGDTGP 1313
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGA 53
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
654-706 1.57e-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: 1.57e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 40805823    654 GLKGEQGAPGPRGHQGAPGPPGARGPIGPEGRDGPPGLQGLRGKKGDMGPPGI 706
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGA 53
 
Name Accession Description Interval E-value
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
36-219 3.89e-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: 3.89e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823   36 HYDLVFLLDTSSSVGKEDFEKVRQWVANLVDTFEVGPDRTRVGVVRYSDRPTTAFELGLFGSQEEVKAAARRLAYHGGNT 115
Cdd:cd01475    2 PTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823  116 NTGDALRYITARSFSPHAGGRPRDRAYKQVAILLTDGRSQDLVLDAAAAAHRAGIRIFAVGVGEALKEELEEIASEPKSA 195
Cdd:cd01475   82 MTGLAIQYAMNNAFSEAEGARPGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLAD 161
                        170       180
                 ....*....|....*....|....
gi 40805823  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 1.83e-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: 1.83e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823   38 DLVFLLDTSSSVGKEDFEKVRQWVANLVDTFEVGPDRTRVGVVRYSDRPTTAFELGLFGSQEEVKAAARRLAYHGGNTNT 117
Cdd:cd01472    2 DIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTNT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823  118 GDALRYITARSFSPHAGGRPrdrAYKQVAILLTDGRSQDLVLDAAAAAHRAGIRIFAVGVGEALKEELEEIASEPKSAHV 197
Cdd:cd01472   82 GKALKYVRENLFTEASGSRE---GVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKELYV 158

                 ....*.
gi 40805823  198 FHVSDF 203
Cdd:cd01472  159 FNVADF 164
VWA pfam00092
von Willebrand factor type A domain;
38-212 5.39e-54

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 186.33  E-value: 5.39e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823     38 DLVFLLDTSSSVGKEDFEKVRQWVANLVDTFEVGPDRTRVGVVRYSDRPTTAFELGLFGSQEEVKAAARRLAYHGGNT-N 116
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTtN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823    117 TGDALRYITARSFSPHAGGRPRdraYKQVAILLTDGRSQDL-VLDAAAAAHRAGIRIFAVGVGEALKEELEEIASEPKSA 195
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPG---APKVVVLLTDGRSQDGdPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEG 157
                          170
                   ....*....|....*..
gi 40805823    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 4.02e-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: 183.64  E-value: 4.02e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823   38 DLVFLLDTSSSVGKEDFEKVRQWVANLVDTFEVGPDRTRVGVVRYSDRPTTAFELGLFGSQEEVKAAARRLAYHGGNTNT 117
Cdd:cd01482    2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTRT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823  118 GDALRYITARSFSPHAGGRPRDRaykQVAILLTDGRSQDLVLDAAAAAHRAGIRIFAVGVGEALKEELEEIASEPKSAHV 197
Cdd:cd01482   82 GKALTHVREKNFTPDAGARPGVP---KVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHV 158

                 ....*.
gi 40805823  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 40805823   37 YDLVFLLDTSSSVGKEDFEKVRQWVANLVDTFEVGPDRTRVGVVRYSDRPTTAFELGLFGSQEEVKAAARRLAYHGGN-T 115
Cdd:cd01450    1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGgT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823  116 NTGDALRYITARSFSPhaggRPRDRAYKQVAILLTDGRSQDL--VLDAAAAAHRAGIRIFAVGVGEALKEELEEIASEPK 193
Cdd:cd01450   81 NTGKALQYALEQLFSE----SNARENVPKVIIVLTDGRSDDGgdPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPS 156

                 ....*
gi 40805823  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 3.13e-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: 3.13e-42
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823      38 DLVFLLDTSSSVGKEDFEKVRQWVANLVDTFEVGPDRTRVGVVRYSDRPTTAFELGLFGSQEEVKAAARRLAYH-GGNTN 116
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTN 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823     117 TGDALRYITARSFSPHAGGRPRDRaykQVAILLTDGRSQDL---VLDAAAAAHRAGIRIFAVGVGEA-LKEELEEIASEP 192
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAP---KVVILITDGESNDGpkdLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLASAP 157
                           170
                    ....*....|....*..
gi 40805823     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 5.29e-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: 5.29e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823   38 DLVFLLDTSSSVGKEDFEKVRQWVANLVDTFEVGPDRTRVGVVRYSDRPTTAFELGLFGSQEEVKAAARRLAYHGGN-TN 116
Cdd:cd01481    2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSqLN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823  117 TGDALRYITARSFSPHAGGRPRDrAYKQVAILLTDGRSQDLVLDAAAAAHRAGIRIFAVGVGEALKEELEEIASEPKsaH 196
Cdd:cd01481   82 TGSALDYVVKNLFTKSAGSRIEE-GVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPS--F 158

                 ....*..
gi 40805823  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 4.41e-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: 4.41e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823   38 DLVFLLDTSSSVGKEDFEKVRQWVANLVDTFEVGPDRTRVGVVRYSDRPTTAFELGLFGSQEEVKAAARRLAYHGGNTNT 117
Cdd:cd01469    2 DIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTNT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823  118 GDALRYITARSFSPHAGGRprdRAYKQVAILLTDGRSQD--LVLDAAAAAHRAGIRIFAVGVGEALK-----EELEEIAS 190
Cdd:cd01469   82 ATAIQYVVTELFSESNGAR---KDATKVLVVITDGESHDdpLLKDVIPQAEREGIIRYAIGVGGHFQrensrEELKTIAS 158
                        170
                 ....*....|....*....
gi 40805823  191 EPKSAHVFHVSDFNAIDKI 209
Cdd:cd01469  159 KPPEEHFFNVTDFAALKDI 177
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
239-426 4.33e-33

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


Pssm-ID: 214560  Cd Length: 184  Bit Score: 127.09  E-value: 4.33e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823     239 GTKEITGFDLMDL-FSVKEILGKRenGAQSSYvRMGSFPVV-QSTEDVFPQGLPDEYAFVTTFRFRKTSRkedWYIWQVI 316
Cdd:smart00210    1 GQDLLQVFDLPSLsFAIRQVVGPE--PGSPAY-RLGDPALVpQPTRDLFPSGLPEDFSLLTTFRQTPKSR---GVLFAIY 74
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823     317 DQYSIPQVSIRLDGENKAVEYNAVGAMKDAVRVVFRGSrvnDLFDRDWHKMALSIQAQNVSLHIDCALVQTLPIEER--E 394
Cdd:smart00210   75 DAQNVRQFGLEVDGRANTLLLRYQGVDGKQHTVSFRNL---PLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPgqP 151
                           170       180       190
                    ....*....|....*....|....*....|..
gi 40805823     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 9.22e-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: 9.22e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823   37 YDLVFLLDTSSSVGKEDFEKVRQWVANLVDTFEVGPDRTRVGVVRYSDRPTTAFELGLFGSQEEVKAAARRL-AYHGGNT 115
Cdd:cd00198    1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALkKGLGGGT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823  116 NTGDALRYItARSFSphaggRPRDRAYKQVAILLTDGRSQD---LVLDAAAAAHRAGIRIFAVGVG-EALKEELEEIASE 191
Cdd:cd00198   81 NIGAALRLA-LELLK-----SAKRPNARRVIILLTDGEPNDgpeLLAEAARELRKLGITVYTIGIGdDANEDELKEIADK 154

                 ....*..
gi 40805823  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 ...
481-703 5.31e-29

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: 122.32  E-value: 5.31e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823   481 GEKGEMGVAGPMGLPGPKGDIGAIGPVGAPGPKGEKGDVGI----GPFG----QGEKGEKGSLGLPGPPGRDGSKGMRGE 552
Cdd:NF038329  120 GEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEkgpaGPQGeagpQGPAGKDGEAGAKGPAGEKGPQGPRGE 199
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823   553 PGELGEPGLPGEVGMRGPQGPPGLPGPPGRVGaPGLQGERGEKGTRGEKGERGLDGFPGKPGDTGQQGRPGPSGVAGPQG 632
Cdd:NF038329  200 TGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDG 278
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 40805823   633 EKGDVGPAGPPGvpgsvvqQEGLKGEQGAPGPRGHQGAPGPPGARGPIGPEGRDGPPGLQGLRGKKGDMGP 703
Cdd:NF038329  279 ERGPVGPAGKDG-------QNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
530-822 2.18e-26

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 114.23  E-value: 2.18e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823   530 GEKGSLGLPGPPGRDGSKGMRGEPGELGEPGLPGEVGMRgpqgppglpGPPGRVGAPGLQGERGEKGTRGEKGERGLDGF 609
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQ---------GERGEKGPAGPQGEAGPQGPAGKDGEAGAKGP 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823   610 PGKPGDTGQQGRPGPSGVAGPQGEKG-DVGPAGPPGVPGSVVQQEGLKGEQGAPGPRGHQGAPGPPGARGPIGPEGRDGP 688
Cdd:NF038329  188 AGEKGPQGPRGETGPAGEQGPAGPAGpDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGE 267
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823   689 PGLQGLRGKKGDMGPPGipgllglqgppgppgvpgppgpggspglpgeigfpgkpgppgptgppgkdgpngppgppgTKG 768
Cdd:NF038329  268 AGPDGPDGKDGERGPVG------------------------------------------------------------PAG 287
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 40805823   769 EPGERGEDGLPGKPGLRGEIGEQGLagrPGEKGEAGLPGAPGFPGVRGEKGDQG 822
Cdd:NF038329  288 KDGQNGKDGLPGKDGKDGQNGKDGL---PGKDGKDGQPGKDGLPGKDGKDGQPG 338
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
38-197 1.95e-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: 1.95e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823   38 DLVFLLDTSSSVGKEDFEKVRQWVANLVDTFEVG------PDRTRVGVVRYSDRPTTAF-ELGLFGSQEEVKAAARRLAY 110
Cdd:cd01480    4 DITFVLDSSESVGLQNFDITKNFVKRVAERFLKDyyrkdpAGSWRVGVVQYSDQQEVEAgFLRDIRNYTSLKEAVDNLEY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823  111 HGGNTNTGDALRYITARSF-SPHAGGrprdrayKQVAILLTDGRSQ----DLVLDAAAAAHRAGIRIFAVGVGEALKEEL 185
Cdd:cd01480   84 IGGGTFTDCALKYATEQLLeGSHQKE-------NKFLLVITDGHSDgspdGGIEKAVNEADHLGIKIFFVAVGSQNEEPL 156
                        170
                 ....*....|..
gi 40805823  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 3.16e-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: 3.16e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823   38 DLVFLLDTSSSVgKEDFEKVRQWVANLVDTFEVGPDRTRVGVVRYSDRPTT--AFELGLFGSQEEVKAAARRLAYHGGNT 115
Cdd:cd01476    2 DLLFVLDSSGSV-RGKFEKYKKYIERIVEGLEIGPTATRVALITYSGRGRQrvRFNLPKHNDGEELLEKVDNLRFIGGTT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823  116 NTGDALRYiTARSFSPHAGGRPRdraYKQVAILLTDGRSQDLVLDAAAAAHR-AGIRIFAVGVGE---ALKEELEEIASE 191
Cdd:cd01476   81 ATGAAIEV-ALQQLDPSEGRREG---IPKVVVVLTDGRSHDDPEKQARILRAvPNIETFAVGTGDpgtVDTEELHSITGN 156

                 ....*..
gi 40805823  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 ...
479-689 7.01e-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: 94.59  E-value: 7.01e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823   479 PAGEKGEMGVAGPMGLPGPKGDIGAIGPVGAPGPKGEKGDVG----IGPFG-QGEKGEKGSLGLPGPPGRDGS--KGMRG 551
Cdd:NF038329  160 EKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGpageQGPAGpAGPDGEAGPAGEDGPAGPAGDgqQGPDG 239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823   552 EPGELGEPGLPGEVGMRGPQGPPGLPGPPGRVGAPGLQGERGEKGTRGEKGERGLDGFPGKPGDTGQQGRPGPSGVAGpq 631
Cdd:NF038329  240 DPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDG-- 317
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 40805823   632 gekgdvgpagppgvpgsvvqQEGLKGEQGAPGPRGHQGAPGPPGARGPIGPEGRDGPP 689
Cdd:NF038329  318 --------------------KDGQPGKDGLPGKDGKDGQPGKPAPKTPEVPQKPDTAP 355
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
798-1097 8.70e-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: 94.20  E-value: 8.70e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823   798 GEKGEAGLPGAPGFPGVRGEKGDQGEKGELGLPGLKGDRGEKGEagpagppglpgttslftphprmPGEQGPKGEKGDPG 877
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGE----------------------KGPAGPQGEAGPQG 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823   878 LPGEPGLQGrpgelgpqgptgppgakgqegahgapgaagnpgapghvgapgpsgppgsvgAPGLRGTPGKDGERGEKGAA 957
Cdd:NF038329  175 PAGKDGEAG---------------------------------------------------AKGPAGEKGPQGPRGETGPA 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823   958 GEEGSPGPVGPRGDPGAPGLPGPPGKGKDGEPGLRGSPGLPGPLGTKAACGKVrgsencalGGQCVKGDRGAPGIPGSPG 1037
Cdd:NF038329  204 GEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPA--------GKDGPRGDRGEAGPDGPDG 275
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823  1038 SRGDPGigvagppgPSGPPGDKGSPGSRGLPGFPGPQGPAGRDGAPGNPGERGPPGKPGL 1097
Cdd:NF038329  276 KDGERG--------PVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGL 327
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
653-889 1.80e-19

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 93.43  E-value: 1.80e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823   653 EGLKGEQGAPGPRGHQGAPGPPGARGPIGPEGRDGPPGLQGLRGKKGDMGPPGIPGLLGLQGPPGPPGVPGPPGPGGSPG 732
Cdd:NF038329  116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823   733 LPGEiGFPGKPGPPGPTGPPGKDGPNGPPGPPGTKGEPGERGEDGLPGKPGLRGEIGEQGLAGRPGEKGEAGLPGAPGFP 812
Cdd:NF038329  196 PRGE-TGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPD 274
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823   813 GVRGEK------GDQGEKGELGLPGLKGDRGEKGEagpagppglpgttslftphPRMPGEQGPKGEKGDPGLPGEPGLQG 886
Cdd:NF038329  275 GKDGERgpvgpaGKDGQNGKDGLPGKDGKDGQNGK-------------------DGLPGKDGKDGQPGKDGLPGKDGKDG 335

                  ...
gi 40805823   887 RPG 889
Cdd:NF038329  336 QPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
1170-1386 2.62e-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: 2.62e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823  1170 QGERGADGEVGQKGDQGHPGVPGFMGPPGNPGPPGADGIAGAAGPPGIQGSPGKEGPPGPQGPSGLPGIPGEEGKEGRDG 1249
Cdd:NF038329  131 AGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAG 210
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823  1250 KPGPPGEPGKAGEPGLPGPEGA--RGPPGFKGHTGDSGAPGPRGESGAMGLPGQEGLPGKDGDTGPtgpqgpqgpRGPPG 1327
Cdd:NF038329  211 PAGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK---------DGERG 281
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 40805823  1328 KNGSPGSPGEPGPSGTPGQKGSKGENGSPGLPGFLGPRGPPGEPGEKGVPGKEGVPGKP 1386
Cdd:NF038329  282 PVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
2-209 1.17e-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: 81.91  E-value: 1.17e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823    2 AGLRGNAVAGLLWMLLLWSGGGGCQAQRAGCKSVHYDLVFLLDTSSSVGKED-FEKVRQWVANLVDTFevgPDRTRVGVV 80
Cdd:COG1240   58 LLALLLAALLLLLAVLLLLLALALAPLALARPQRGRDVVLVVDASGSMAAENrLEAAKGALLDFLDDY---RPRDRVGLV 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823   81 RYSDRPTTAFELGlfGSQEEVKAAARRLAYhGGNTNTGDALRYITARsfsphagGRPRDRAYKQVAILLTDGR---SQDL 157
Cdd:COG1240  135 AFGGEAEVLLPLT--RDREALKRALDELPP-GGGTPLGDALALALEL-------LKRADPARRKVIVLLTDGRdnaGRID 204
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 40805823  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 ...
1170-1399 1.24e-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: 1.24e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823  1170 QGERGADGEVGQKGDQGHPGVPGFMGPPGNPGPPGADGIAGAAGPPGIQGSpgkegppgpqgpsglpgiPGEEGKEGRDG 1249
Cdd:NF038329  119 KGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGE------------------AGPQGPAGKDG 180
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823  1250 KPGPPGEPGKAGEPGLPGPEGARGPPGFKGHTGDSGAPGPRGESGAMGLPGQeGLPGKDGDTGPTGPQGPQGPRGPPGKN 1329
Cdd:NF038329  181 EAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKD 259
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823  1330 GSPGSPGEPGPSGTPGQKGSKGENGSPGLPGFLGPRGPPGEPGEKGVPGKEGVPGKPGEPGFKGERGDPG 1399
Cdd:NF038329  260 GPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPG 329
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
38-217 3.77e-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: 80.92  E-value: 3.77e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823   38 DLVFLLDTSSSVGKEDFEKVRQWVANLVDTFevgPDRTRVGVVRYSDRPTTAFELGLFGSQEEVKAAARRLaYHGGNTNT 117
Cdd:COG2304   93 NLVFVIDVSGSMSGDKLELAKEAAKLLVDQL---RPGDRVSIVTFAGDARVLLPPTPATDRAKILAAIDRL-QAGGGTAL 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823  118 GDALRYITARSFSPHAGGRPRdraykqVAILLTDGR------SQDLVLDAAAAAHRAGIRIFAVGVGEALKEE-LEEIAS 190
Cdd:COG2304  169 GAGLELAYELARKHFIPGRVN------RVILLTDGDanvgitDPEELLKLAEEAREEGITLTTLGVGSDYNEDlLERLAD 242
                        170       180
                 ....*....|....*....|....*..
gi 40805823  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 ...
1240-1433 3.08e-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: 3.08e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823  1240 GEEGKEGRDGKPGPPGEPGKAGEPGLPGPEGARGPPGFKGHTGDSGAPGPRGESGAMGLPGQEGLPGKDGDTGPTGPQGP 1319
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823  1320 QGPRGPPGKNGSPGSPGEPGPSGTPGQKGSKG-----ENGSPGLPGflgPRGPPGEPGEKGVPGKEGVPGKPGEPGFKGE 1394
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGpagdgQQGPDGDPG---PTGEDGPQGPDGPAGKDGPRGDRGEAGPDGP 273
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 40805823  1395 RGDPGIKGDKGPPGGKGQPGDPGIPGHKGHTGLMGPQGL 1433
Cdd:NF038329  274 DGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGL 312
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
36-209 3.94e-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: 3.94e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823   36 HYDLVFLLDTSSSVGKEDFEkVRQWVANLVDTFeVGPDrTRVGVVRYSDRPTTAFELGLFGSQEEVKAAARRLAYHGGNT 115
Cdd:cd01474    4 HFDLYFVLDKSGSVAANWIE-IYDFVEQLVDRF-NSPG-LRFSFITFSTRATKILPLTDDSSAIIKGLEVLKKVTPSGQT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823  116 NTGDALRYITARSFSPHAGGRPRDRaykqVAILLTDGR-SQDLVLDAAAAAHRA---GIRIFAVGVGEALKEELEEIASE 191
Cdd:cd01474   81 YIHEGLENANEQIFNRNGGGRETVS----VIIALTDGQlLLNGHKYPEHEAKLSrklGAIVYCVGVTDFLKSQLINIADS 156
                        170
                 ....*....|....*....
gi 40805823  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 2.32e-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: 2.32e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823   38 DLVFLLDTSSSVGKED-FEKVRQWVANLVDTFEVGPDRTRVGVVRYSDRPTTAFELGLFGSQEE-----VKAAARRLAYH 111
Cdd:cd01471    2 DLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPNSTNKdlalnAIRALLSLYYP 81
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 40805823  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 ...
1288-1584 4.07e-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: 4.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823  1288 GPRGESGAMGLPGQEGLPGKDGDTGPTGPQGPQGPRGPPGKNGSPGSPGEPGPSGTPGQKGSKGENGSPGLPGFLGPRGP 1367
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823  1368 PGEPGEKGVPGKEGVPGKPGEPGFKGERGDPGIKGDKGPPGGkgqpgdpgipGHKGHTGLMGPQGLPGENGPVGPPGPPG 1447
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPD----------GDPGPTGEDGPQGPDGPAGKDGPRGDRG 266
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823  1448 QPGFPGLRGESpsmetlrrliqeelgkqletrlayllaqmppaymkssqgrpgppgppgkdglpGRAGPMGEPGRPGQGG 1527
Cdd:NF038329  267 EAGPDGPDGKD-----------------------------------------------------GERGPVGPAGKDGQNG 293
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 40805823  1528 LEGPSGPIGPKGERGAKGDPGAPGvglrgemGPPGIPGQPGEPGYAKDGLPGIPGPQ 1584
Cdd:NF038329  294 KDGLPGKDGKDGQNGKDGLPGKDG-------KDGQPGKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
948-1268 1.21e-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: 71.86  E-value: 1.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823   948 DGERGEKGAAGEEGSPGPVGPRGdpgapglpgppgkgKDGEPGLRGSPGLPGPLGTKAACGkvrgsencALGGQCVKGDR 1027
Cdd:NF038329  116 DGEKGEPGPAGPAGPAGEQGPRG--------------DRGETGPAGPAGPPGPQGERGEKG--------PAGPQGEAGPQ 173
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823  1028 GAPGIPGSPGSRGDPGigvagppgpsgppgDKGSPGSRGLPGFPGPQGPAGRDGAPGNPGERGPPGKPGLSSLLSPGDIN 1107
Cdd:NF038329  174 GPAGKDGEAGAKGPAG--------------EKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDG 239
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823  1108 LLAKDvcndcppgppglpglpGFKGDKGVPGKPGREGTEGKKGEAGPPGLPGPPGIagpqgsQGERGADGEVGQKGDQGH 1187
Cdd:NF038329  240 DPGPT----------------GEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGE------RGPVGPAGKDGQNGKDGL 297
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823  1188 PGvpgfmgppgnpgppgadgiagaagppgiqgspgkegPPGPQGPSGLPGIPGEEGKEGRDGKPGPPGEPGKAGEPGLPG 1267
Cdd:NF038329  298 PG------------------------------------KDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPA 341

                  .
gi 40805823  1268 P 1268
Cdd:NF038329  342 P 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
1261-1593 4.06e-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: 4.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823  1261 GEPGLPGPEGARGPPGFKGHTGDSGAPGPRGESGAMGLPGQEGLPGKDGDTGPTgpqgpqgprgppgknGSPGSPGEPGP 1340
Cdd:NF038329  120 GEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ---------------GPAGKDGEAGA 184
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823  1341 SGTPGQKGSKGENGSPGlpgflgprgppgepgEKGVPGKEGVPGKPGEPGFKGERGDPGIKGDKGPPGGkgqpgdpgipG 1420
Cdd:NF038329  185 KGPAGEKGPQGPRGETG---------------PAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPD----------G 239
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823  1421 HKGHTGLMGPQGLPGENGPVGPPGPPGQPGFPGLRGESpsmetlrrliqeelgkqletrlayllaqmppaymkssqgrpg 1500
Cdd:NF038329  240 DPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKD------------------------------------------ 277
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823  1501 ppgppgkdglpGRAGPMGEPGRPGQGGLEGPSGPIGPKGERGAKGDPGAPGvglrgemgppgipgqpgepgyaKDGLPGI 1580
Cdd:NF038329  278 -----------GERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDG----------------------KDGQPGK 324
                         330
                  ....*....|...
gi 40805823  1581 PGPQGETGPAGHP 1593
Cdd:NF038329  325 DGLPGKDGKDGQP 337
VWA_2 pfam13519
von Willebrand factor type A domain;
39-149 1.43e-11

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 62.69  E-value: 1.43e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823     39 LVFLLDTSSSVGKED-----FEKVRQWVANLVDTFevgpDRTRVGVVRYSDRPTTafELGLFGSQEEVKAAARRLAYHGG 113
Cdd:pfam13519    1 LVFVLDTSGSMRNGDygptrLEAAKDAVLALLKSL----PGDRVGLVTFGDGPEV--LIPLTKDRAKILRALRRLEPKGG 74
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 40805823    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 1.63e-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: 63.55  E-value: 1.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823   38 DLVFLLDTSSSVGKEDFEKVRQWVANLVDTFEvgPDRtRVGVVRYSDRPTTAFELglfGSQEEVKAAARRLA--YHGGNT 115
Cdd:COG2425  120 PVVLCVDTSGSMAGSKEAAAKAAALALLRALR--PNR-RFGVILFDTEVVEDLPL---TADDGLEDAIEFLSglFAGGGT 193
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 40805823  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 1.60e-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: 1.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823   40 VFLLDTSSSVGKEDFEKVRQWVANLVDTFEVGP---DRTRVGVVRYSDRPTTAFELglfgsQEEVKAAARRLAYHGGnTN 116
Cdd:COG4245    9 YLLLDTSGSMSGEPIEALNEGLQALIDELRQDPyalETVEVSVITFDGEAKVLLPL-----TDLEDFQPPDLSASGG-TP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823  117 TGDALRYITARSFSPHAGGRP-RDRAYKQVAILLTDGRSQDL-------VLDAAAAAHRAGirIFAVGVG-EALKEELEE 187
Cdd:COG4245   83 LGAALELLLDLIERRVQKYTAeGKGDWRPVVFLITDGEPTDSdweaalqRLKDGEAAKKAN--IFAIGVGpDADTEVLKQ 160
                        170       180
                 ....*....|....*....|..
gi 40805823  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 1.82e-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: 55.74  E-value: 1.82e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823   39 LVFLLDTSSSVGKEDFEKVRQWVANLVDTFEvgpDRTRVGVVRYSDRPTTAFELGLFGSQEEVKAAARRLAyHGGNTN-- 116
Cdd:cd01465    3 LVFVIDRSGSMDGPKLPLVKSALKLLVDQLR---PDDRLAIVTYDGAAETVLPATPVRDKAAILAAIDRLT-AGGSTAgg 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823  117 TGDALRYITA-RSFSPHAGGRprdraykqvAILLTDG------RSQDLVLDAAAAAHRAGIRIFAVGVGEALKEEL-EEI 188
Cdd:cd01465   79 AGIQLGYQEAqKHFVPGGVNR---------ILLATDGdfnvgeTDPDELARLVAQKRESGITLSTLGFGDNYNEDLmEAI 149

                 .
gi 40805823  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 1.06e-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: 1.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823   42 LLDTSSSVGKEDFEKVRQWVANLVD---TFEVGPdrtRVGVVRYSDRPTTAFELGLFGSQeEVKAAARRLA---Y--HGG 113
Cdd:cd01470    6 ALDASDSIGEEDFDEAKNAIKTLIEkisSYEVSP---RYEIISYASDPKEIVSIRDFNSN-DADDVIKRLEdfnYddHGD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823  114 N--TNTGDALRYITARSFSPHAGGRPRDRAYKQVAILLTDGRS----------QDLVLDAAAAAHRAGIR-----IFAVG 176
Cdd:cd01470   82 KtgTNTAAALKKVYERMALEKVRNKEAFNETRHVIILFTDGKSnmggsplptvDKIKNLVYKNNKSDNPRedyldVYVFG 161
                        170       180
                 ....*....|....*....|....*...
gi 40805823  177 VG-EALKEELEEIASE-PKSAHVFHVSD 202
Cdd:cd01470  162 VGdDVNKEELNDLASKkDNERHFFKLKD 189
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
777-831 2.38e-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: 2.38e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 40805823    777 GLPGKPGLRGEIGEQGLAGRPGEKGEAGLPGAPGFPGVRGEKGDQGEKGELGLPG 831
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
772-826 2.60e-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: 2.60e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 40805823    772 ERGEDGLPGKPGLRGEIGEQGLAGRPGEKGEAGLPGAPGFPGVRGEKGDQGEKGE 826
Cdd:pfam01391    2 PPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
511-705 9.99e-05

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 46.95  E-value: 9.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823  511 GPKGEKGDVGIGPFGQGekGEKGSLGLPGPPGRDGSKGMRGEPGELGEPGLPGEVGMRGPQGPPGLPGPPGRVGAPGLQG 590
Cdd:COG5164    2 GLYGPGKTGPSDPGGVT--TPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823  591 ERGEKGTRGEKGERGLDGFPGKPGDTGQQGRPGPSGVAGPQGEKG-----DVGPAGPPGVPGSVVQQEGLKGEQGAPGPR 665
Cdd:COG5164   80 GTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGsttppSGGSTTPPGDGGSTPPGPGSTGPGGSTTPP 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 40805823  666 GHQGA---PGPPGARGPIGPEGRDGPP--GLQGLRGKKGDMGPPG 705
Cdd:COG5164  160 GDGGSttpPGPGGSTTPPDDGGSTTPPnkGETGTDIPTGGTPRQG 204
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1261-1313 1.10e-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: 1.10e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 40805823   1261 GEPGLPGPEGARGPPGFKGHTGDSGAPGPRGESGAMGLPGQEGLPGKDGDTGP 1313
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGA 53
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
37-189 1.12e-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: 1.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823   37 YDLVFLLDTSSSVGKEDFEK-VRQWVANLVDTFEVGPDRTRVGVVRYSD--RPTTAFE----------LGLFGSQEEVKA 103
Cdd:cd01473    1 YDLTLILDESASIGYSNWRKdVIPFTEKIINNLNISKDKVHVGILLFAEknRDVVPFSdeerydknelLKKINDLKNSYR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823  104 AarrlayhGGNTNTGDALRYITARSFspHAGGRpRDRAYKqVAILLTDG----RSQDLVLDAAAAAHRAGIRIFAVGVGE 179
Cdd:cd01473   81 S-------GGETYIVEALKYGLKNYT--KHGNR-RKDAPK-VTMLFTDGndtsASKKELQDISLLYKEENVKLLVVGVGA 149
                        170
                 ....*....|
gi 40805823  180 ALKEELEEIA 189
Cdd:cd01473  150 ASENKLKLLA 159
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
654-706 1.57e-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: 1.57e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 40805823    654 GLKGEQGAPGPRGHQGAPGPPGARGPIGPEGRDGPPGLQGLRGKKGDMGPPGI 706
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGA 53
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1260-1307 3.62e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.17  E-value: 3.62e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 40805823   1260 AGEPGLPGPEGARGPPGFKGHTGDSGAPGPRGESGAMGLPGQEGLPGK 1307
Cdd:pfam01391    9 PGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1031-1095 5.85e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.40  E-value: 5.85e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 40805823   1031 GIPGSPGSRGDPGigvagppgPSGPPGDKGSPGSRGLPGFPGPQGPAGRDGAPGNPGERGPPGKP 1095
Cdd:pfam01391    1 GPPGPPGPPGPPG--------PPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
792-842 1.14e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 38.63  E-value: 1.14e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 40805823    792 GLAGRPGEKGEAGLPGAPGFPGVRGEKGDQGEKGELGLPGLKGDRGEKGEA 842
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAP 51
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1330-1399 1.30e-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: 1.30e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40805823   1330 GSPGSPGEPGPSGTPGQKGSKGENGSPGLPGFlgprgppgepgekgvPGKEGVPGKPGEPGFKGERGDPG 1399
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGE---------------PGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
585-635 1.69e-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: 1.69e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 40805823    585 APGLQGERGEKGTRGEKGERGLDGFPGKPGDTGQQGRPGPSGVAGPQGEKG 635
Cdd:pfam01391    5 PPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1282-1353 8.12e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 36.32  E-value: 8.12e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 40805823   1282 GDSGAPGPRGESGAMGLPGQEGLPGKDGDTGPtgpqgpqgprgppgkNGSPGSPGEPGPSGTPGQKGSKGEN 1353
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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