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Conserved domains on  [gi|1062879461|ref|XP_017914092|]
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PREDICTED: collagen alpha-1(XXII) chain [Capra hircus]

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 ...
 45-228 1.89e-58

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: 201.07  E-value: 1.89e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461   45 HYDLVFVLDSSSSVGKENFEKVRQWVANLVDTFEVGPERTRVGVVHYSDRPATAFELGRFGSRAAVRAAARQLAYHGGHT 124
Cdd:cd01475      2 PTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGT 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461  125 HTGDALRFITRHSFAPRAGGRPGDRAFKQVAILLTDGRSQDLVLPAATAARRAGIRIFAVGVGEALREELEEIASEPTAA 204
Cdd:cd01475     82 MTGLAIQYAMNNAFSEAEGARPGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLAD 161

                          170       180
                   ....*....|....*....|....
gi 1062879461  205 HVFHVSDFDAIDKIRGKLRRRLCE 228
Cdd:cd01475    162 HVFYVEDFSTIEELTKKFQGKICV 185
LamG super family cl22861
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 248-435 2.00e-36

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: 136.33  E-value: 2.00e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461   248 GTKEITGFDLMDL-FSVKTLLGERenGAQSSYvRMGSFPVV-QRTEDVFPQGLPDEYAFVTTFRLRKSSRredWYIWQVI 325
Cdd:smart00210    1 GQDLLQVFDLPSLsFAIRQVVGPE--PGSPAY-RLGDPALVpQPTRDLFPSGLPEDFSLLTTFRQTPKSR---GVLFAIY 74

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461   326 DQYGIPQVSIRLDGENKAVEYSAVGAMKDAVRVVFRGPrvhDLFDRDWHKVALSVQAQHASLYVDCALVQTLPLEER--E 403
Cdd:smart00210   75 DAQNVRQFGLEVDGRANTLLLRYQGVDGKQHTVSFRNL---PLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPgqP 151

                           170       180       190
                    ....*....|....*....|....*....|..
gi 1062879461   404 NIDIQGKTAIGKRLYDSVPVDFDLQRVVIYCD 435
Cdd:smart00210  152 PIDTDGIEVRGAQAADRKPFQGDLQQLKIVCD 183
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1118-1386 2.50e-27

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


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 117.31  E-value: 2.50e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461 1118 KGDKGLPGKPGREGTEGKKGDAGPRGLPGPPGIAGPQGSKGEHGADGETGQKGDQGHPGvpgfmgppgdpgppgadgiag 1197
Cdd:NF038329   119 KGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAG--------------------- 177

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461 1198 aagppgIQGPPGKEGPpgpqgpsglpgiPGEEGKEGRDGKPGPPGEQGKTGEPGLPGPEGARGPPGFKGHTGDSGppgpr 1277
Cdd:NF038329   178 ------KDGEAGAKGP------------AGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQ----- 234

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461 1278 gepgaTGPPGREGSPGKDGDTGPTGPQGPQGLRGLPGKSGSPGSPGEPGTPGSPGQKGTKGENGSPGLPGFLGPRGPQGE 1357
Cdd:NF038329   235 -----QGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGK 309

                          250       260
                   ....*....|....*....|....*....
gi 1062879461 1358 PGEKGVPGKEGAPGKPGEPGLRGERGDPG 1386
Cdd:NF038329   310 DGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 503-829 9.16e-22

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


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 100.36  E-value: 9.16e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461  503 GPKGDVGATGPAGAPGPkgekgdtgrgpfvQGEKGEKGSLGLPGPPGRDGSKGMRGEPGEPGELGLPGEVGLRgsqgppg 582
Cdd:NF038329   117 GEKGEPGPAGPAGPAGE-------------QGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPA------- 176

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461  583 lpgppgpigapglhGERGEKGAQGEKGERGLDGFPGKQGEAGEQGRPGPPGEPGPQGEKGAVGPAGPPGLPGsvVQREGL 662
Cdd:NF038329   177 --------------GKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQ--QGPDGD 240

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461  663 KGKQGApgpqghqgppgppgapglMGPEGKDGPPGLQGLRGKRGEAGPPGVPgllgqqgppgppgvpgppgpggppglpg 742
Cdd:NF038329   241 PGPTGE------------------DGPQGPDGPAGKDGPRGDRGEAGPDGPD---------------------------- 274

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461  743 eigfpGKPGAPGQVGPPGKDGPngppglpgpkgdpgdRGEDGLPGQRGPRGEAGEQGLagrPGEKGEAGLPGFPGLPGER 822
Cdd:NF038329   275 -----GKDGERGPVGPAGKDGQ---------------NGKDGLPGKDGKDGQNGKDGL---PGKDGKDGQPGKDGLPGKD 331


                   ....*..
gi 1062879461  823 GEKGDQG 829
Cdd:NF038329   332 GKDGQPG 338
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1289-1571 1.13e-17

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: 87.65  E-value: 1.13e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461 1289 EGSPGKDGDTGPTGPQGPQGLRGLPGKSGSPGSPGEPGTPGSPGQKGTKGENGSPGLpgfLGPRGPQGEPGEKGVPGKEG 1368
Cdd:NF038329   116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGP---QGPAGKDGEAGAKGPAGEKG 192

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461 1369 APGKPGEPGLRGERGDPGIKGDKGPPGGKGQPGDPGIPGhKGHTGLMGPQGPPGENGPAGPPGPPGQPGFPGLRGESpsm 1448
Cdd:NF038329   193 PQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEA--- 268

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461 1449 dvlrrliqeelekqletklayllaqmpsahtkssqgrpgppGPPGKDGLPGRAGPVGEPGRPGQGGLEGPSGPVGPKGER 1528
Cdd:NF038329   269 -----------------------------------------GPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQN 307

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1062879461 1529 GAKGDPGAPGvglrgemGPPGIPGQPGEPGYAKDGLPGSPGPQ 1571
Cdd:NF038329   308 GKDGLPGKDG-------KDGQPGKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 871-1176 2.27e-10

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: 64.93  E-value: 2.27e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461  871 PGEPGPRGEKGDPGTPGEPGSPGHPGELGPRGPIGPPGAKGQEGAQGTPGAAGspgapglvgPPGPsgpPGSVGPPGSRG 950
Cdd:NF038329   122 PGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQG---------PAGK---DGEAGAKGPAG 189

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461  951 PPGKDGERGEKGAAGEEGSPGPAGPRGNPGSPGPPGPPGRGKDGDPGLRGPPGLPGPMGTKGDRGAPGIPGSPGNRGEPG 1030
Cdd:NF038329   190 EKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAG 269

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461 1031 mavagppgpsgppgekgppgsrgppgfpgpqgpagQDGVPGNPGERGPPGKPGpssvlspgdvnllvKDVCNdcppgppg 1110
Cdd:NF038329   270 -----------------------------------PDGPDGKDGERGPVGPAG--------------KDGQN-------- 292

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1062879461 1111 lpglpgfkGDKGLPGKPGREGTEGKKGdagprglpgppgIAGPQGSKGEHGADGETGQKGDQGHPG 1176
Cdd:NF038329   293 --------GKDGLPGKDGKDGQNGKDG------------LPGKDGKDGQPGKDGLPGKDGKDGQPG 338
 
Name Accession Description Interval E-value
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 45-228 1.89e-58

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: 201.07  E-value: 1.89e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461   45 HYDLVFVLDSSSSVGKENFEKVRQWVANLVDTFEVGPERTRVGVVHYSDRPATAFELGRFGSRAAVRAAARQLAYHGGHT 124
Cdd:cd01475      2 PTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGT 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461  125 HTGDALRFITRHSFAPRAGGRPGDRAFKQVAILLTDGRSQDLVLPAATAARRAGIRIFAVGVGEALREELEEIASEPTAA 204
Cdd:cd01475     82 MTGLAIQYAMNNAFSEAEGARPGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLAD 161

                          170       180
                   ....*....|....*....|....
gi 1062879461  205 HVFHVSDFDAIDKIRGKLRRRLCE 228
Cdd:cd01475    162 HVFYVEDFSTIEELTKKFQGKICV 185
VWA pfam00092
von Willebrand factor type A domain;
47-221 2.94e-53

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 184.40  E-value: 2.94e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461   47 DLVFVLDSSSSVGKENFEKVRQWVANLVDTFEVGPERTRVGVVHYSDRPATAFELGRFGSRAAVRAAARQLAY-HGGHTH 125
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYlGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461  126 TGDALRFITRHSFAPRAGGRPGdraFKQVAILLTDGRSQDL-VLPAATAARRAGIRIFAVGVGEALREELEEIASEPTAA 204
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPG---APKVVVLLTDGRSQDGdPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEG 157

                          170
                   ....*....|....*..
gi 1062879461  205 HVFHVSDFDAIDKIRGK 221
Cdd:pfam00092  158 HVFTVSDFEALEDLQDQ 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 47-218 1.84e-40

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: 147.60  E-value: 1.84e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461    47 DLVFVLDSSSSVGKENFEKVRQWVANLVDTFEVGPERTRVGVVHYSDRPATAFELGRFGSRAAVRAAARQLAYH-GGHTH 125
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461   126 TGDALRFITRHSFAPRAGGRPGdraFKQVAILLTDGRSQDL---VLPAATAARRAGIRIFAVGVGEA-LREELEEIASEP 201
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRG---APKVVILITDGESNDGpkdLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLASAP 157

                           170
                    ....*....|....*..
gi 1062879461   202 TAAHVFHVSDFDAIDKI 218
Cdd:smart00327  158 GGVYVFLPELLDLLIDL 174
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 248-435 2.00e-36

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


Pssm-ID: 214560  Cd Length: 184  Bit Score: 136.33  E-value: 2.00e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461   248 GTKEITGFDLMDL-FSVKTLLGERenGAQSSYvRMGSFPVV-QRTEDVFPQGLPDEYAFVTTFRLRKSSRredWYIWQVI 325
Cdd:smart00210    1 GQDLLQVFDLPSLsFAIRQVVGPE--PGSPAY-RLGDPALVpQPTRDLFPSGLPEDFSLLTTFRQTPKSR---GVLFAIY 74

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461   326 DQYGIPQVSIRLDGENKAVEYSAVGAMKDAVRVVFRGPrvhDLFDRDWHKVALSVQAQHASLYVDCALVQTLPLEER--E 403
Cdd:smart00210   75 DAQNVRQFGLEVDGRANTLLLRYQGVDGKQHTVSFRNL---PLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPgqP 151

                           170       180       190
                    ....*....|....*....|....*....|..
gi 1062879461   404 NIDIQGKTAIGKRLYDSVPVDFDLQRVVIYCD 435
Cdd:smart00210  152 PIDTDGIEVRGAQAADRKPFQGDLQQLKIVCD 183
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1118-1386 2.50e-27

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 117.31  E-value: 2.50e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461 1118 KGDKGLPGKPGREGTEGKKGDAGPRGLPGPPGIAGPQGSKGEHGADGETGQKGDQGHPGvpgfmgppgdpgppgadgiag 1197
Cdd:NF038329   119 KGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAG--------------------- 177

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461 1198 aagppgIQGPPGKEGPpgpqgpsglpgiPGEEGKEGRDGKPGPPGEQGKTGEPGLPGPEGARGPPGFKGHTGDSGppgpr 1277
Cdd:NF038329   178 ------KDGEAGAKGP------------AGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQ----- 234

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461 1278 gepgaTGPPGREGSPGKDGDTGPTGPQGPQGLRGLPGKSGSPGSPGEPGTPGSPGQKGTKGENGSPGLPGFLGPRGPQGE 1357
Cdd:NF038329   235 -----QGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGK 309

                          250       260
                   ....*....|....*....|....*....
gi 1062879461 1358 PGEKGVPGKEGAPGKPGEPGLRGERGDPG 1386
Cdd:NF038329   310 DGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1117-1373 4.32e-24

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 107.30  E-value: 4.32e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461 1117 FKGDKGLPGKPGREGTEGKKGDAGPRGLPGPPGIAGPQGSKGEHGADGETGQKGDQGHPGVPGFMGPPGDPGPPGADGIA 1196
Cdd:NF038329   115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461 1197 GAAGPPGIQGPPGKEGPPGPQgpsglpgipGEEGKEGRDGKPGPPGeQGKTGEPGLPGPEGARGPpgfkghtgdsgppgp 1276
Cdd:NF038329   195 GPRGETGPAGEQGPAGPAGPD---------GEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGP--------------- 249

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461 1277 rgepgaTGPPGREGSPGKDGDTGPTGPQGPQGLRGLPGKSGSPGSPGEPGTPGSPGQKGTKGENGSPGLPGFLGPRGPQG 1356
Cdd:NF038329   250 ------QGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPG 323

                          250
                   ....*....|....*..
gi 1062879461 1357 EPGEKGVPGKEGAPGKP 1373
Cdd:NF038329   324 KDGLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 503-829 9.16e-22

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 100.36  E-value: 9.16e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461  503 GPKGDVGATGPAGAPGPkgekgdtgrgpfvQGEKGEKGSLGLPGPPGRDGSKGMRGEPGEPGELGLPGEVGLRgsqgppg 582
Cdd:NF038329   117 GEKGEPGPAGPAGPAGE-------------QGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPA------- 176

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461  583 lpgppgpigapglhGERGEKGAQGEKGERGLDGFPGKQGEAGEQGRPGPPGEPGPQGEKGAVGPAGPPGLPGsvVQREGL 662
Cdd:NF038329   177 --------------GKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQ--QGPDGD 240

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461  663 KGKQGApgpqghqgppgppgapglMGPEGKDGPPGLQGLRGKRGEAGPPGVPgllgqqgppgppgvpgppgpggppglpg 742
Cdd:NF038329   241 PGPTGE------------------DGPQGPDGPAGKDGPRGDRGEAGPDGPD---------------------------- 274

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461  743 eigfpGKPGAPGQVGPPGKDGPngppglpgpkgdpgdRGEDGLPGQRGPRGEAGEQGLagrPGEKGEAGLPGFPGLPGER 822
Cdd:NF038329   275 -----GKDGERGPVGPAGKDGQ---------------NGKDGLPGKDGKDGQNGKDGL---PGKDGKDGQPGKDGLPGKD 331


                   ....*..
gi 1062879461  823 GEKGDQG 829
Cdd:NF038329   332 GKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 486-816 1.08e-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: 96.90  E-value: 1.08e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461  486 PPGEKGEKGFDGPVGLPGPKGDVGATGPAGAPGPKGEKGDTG-RGPfvQGEKGEKGSLGLPGPPGRDGSKGMRGEPGEPG 564
Cdd:NF038329   127 PAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGeAGP--QGPAGKDGEAGAKGPAGEKGPQGPRGETGPAG 204

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461  565 ELGLPGEVGLRGSQGPPGLPGPPGPIGAPGlHGERGEKGAQGEKGERGLDGFPGKQGEageqgrpgppgepgpqgekgav 644
Cdd:NF038329   205 EQGPAGPAGPDGEAGPAGEDGPAGPAGDGQ-QGPDGDPGPTGEDGPQGPDGPAGKDGP---------------------- 261

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461  645 gpagppglpgsvvqreglkgkqgapgpqghqgppgppgapglmgpEGKDGPPGLQGLRGKRGEAGPPGVpgllgqqgppg 724
Cdd:NF038329   262 ---------------------------------------------RGDRGEAGPDGPDGKDGERGPVGP----------- 285

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461  725 ppgvpgppgpggppglpgeigfPGKPGAPGQVGPPGKDGPngppglpgpkgdpgdRGEDGLPGQRGPRGEAGEQGLAGRP 804
Cdd:NF038329   286 ----------------------AGKDGQNGKDGLPGKDGK---------------DGQNGKDGLPGKDGKDGQPGKDGLP 328

                          330
                   ....*....|..
gi 1062879461  805 GEKGEAGLPGFP 816
Cdd:NF038329   329 GKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 488-712 1.42e-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: 90.35  E-value: 1.42e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461  488 GEKGEKGFDGPVGLPGPKGDVGATGPAGAPGPKGEKGDTGRgPFVQGEKGEKGSLGLPGPPGRDGSKGMRGEPGEPGELG 567
Cdd:NF038329   120 GEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGE-KGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRG 198

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461  568 LPGEVGLRGSQGPPGLPGPPGPIGAPGLHGE--RGEKGAQGEKGERGLDGFPGKQGEAGEQGRPGPPGEPGPQGEKGavg 645
Cdd:NF038329   199 ETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPagDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG--- 275

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461  646 pagppglpgsvvqREGLKGKQGAPGPQGHQGPPGPPGAPGLMGPEGKDGPPGLQ---GLRGKRGEAGPPG 712
Cdd:NF038329   276 -------------KDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDgkdGQPGKDGLPGKDG 332
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1289-1571 1.13e-17

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: 87.65  E-value: 1.13e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461 1289 EGSPGKDGDTGPTGPQGPQGLRGLPGKSGSPGSPGEPGTPGSPGQKGTKGENGSPGLpgfLGPRGPQGEPGEKGVPGKEG 1368
Cdd:NF038329   116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGP---QGPAGKDGEAGAKGPAGEKG 192

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461 1369 APGKPGEPGLRGERGDPGIKGDKGPPGGKGQPGDPGIPGhKGHTGLMGPQGPPGENGPAGPPGPPGQPGFPGLRGESpsm 1448
Cdd:NF038329   193 PQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEA--- 268

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461 1449 dvlrrliqeelekqletklayllaqmpsahtkssqgrpgppGPPGKDGLPGRAGPVGEPGRPGQGGLEGPSGPVGPKGER 1528
Cdd:NF038329   269 -----------------------------------------GPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQN 307

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1062879461 1529 GAKGDPGAPGvglrgemGPPGIPGQPGEPGYAKDGLPGSPGPQ 1571
Cdd:NF038329   308 GKDGLPGKDG-------KDGQPGKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 691-923 1.19e-17

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: 87.65  E-value: 1.19e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461  691 GKDGPPGLQGLRGKRGEAGPPGvpgllgqqgppgppgvpgPPGPGGPPGLPGEIGFPGKPGAPGQVGPPGKDGPNGPPGL 770
Cdd:NF038329   126 GPAGPAGEQGPRGDRGETGPAG------------------PAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGP 187

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461  771 PGPKGDPGDRGEDGLPGQRGPRGEAGEQGLAGRPGEKGEAGLPGfPGLPGERGEKGDQGEKGALGLPGLKGDQGAKGEVG 850
Cdd:NF038329   188 AGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRG 266

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1062879461  851 PPGPPGLPgttslftphprmpGEPGPRGEKGDPGTPGEPGSPGHPGELGPRGPIGPPGAKGQEGAQGTPGAAG 923
Cdd:NF038329   267 EAGPDGPD-------------GKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDG 326
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 660-897 1.08e-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: 1.08e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461  660 EGLKGKQGAPGPQGHQGPPGPPGAPGLMGPEGKDGPPGLQGLRGKRGEAGPPGVPGLLGQQGPPGPPGVPGPPGPGGPPG 739
Cdd:NF038329   116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461  740 LPGEIGFPGKPGAPGQVGPPGKDGPNGPPGLPGPKGDPG-----DRGEDGLPGQRGPRGEAGEQGLAGRPGEKGEAGLPG 814
Cdd:NF038329   196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQqgpdgDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461  815 FPGLPGERGEKGDQGEKGALGLPGLKGDQGAKGEvgppgppglpgttslftphprmPGEPGPRGEKGDPGTPGEPGSPGH 894
Cdd:NF038329   276 KDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGK----------------------DGLPGKDGKDGQPGKDGLPGKDGK 333


                   ...
gi 1062879461  895 PGE 897
Cdd:NF038329   334 DGQ 336
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1232-1585 1.75e-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: 84.19  E-value: 1.75e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461 1232 EGRDGKPGPPGEQGKTGEPGLPGPEGARGPPGFKGHTGDSGPPGPRGEPGATGPPGREGSPGKDGDTGPTGPQGPQGLRG 1311
Cdd:NF038329   116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461 1312 LPGKSGSPGSPGEPGTPGSPGQKGTKGENGSPGLPGfLGPRGPQGEPGEKGVPGKEGAPGKPGEPGLRGERGDPGIkgdk 1391
Cdd:NF038329   196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGP---- 270

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461 1392 gppggkgqpgdpgiPGHKGHTGlmgpqgppgengpagppgppgqpgfpglrgespsmdvlrrliqeelekqletklayll 1471
Cdd:NF038329   271 --------------DGPDGKDG---------------------------------------------------------- 278

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461 1472 aqmpsahtkssqgrpgppgppgkdglpgRAGPVGEPGRPGQGGLEGPSGPVGPKGERGAKGDPGAPGvglrgemgppgip 1551
Cdd:NF038329   279 ----------------------------ERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDG------------- 317

                          330       340       350
                   ....*....|....*....|....*....|....
gi 1062879461 1552 gqpgepgyaKDGLPGSPGPQGEtgpaghpgpPGP 1585
Cdd:NF038329   318 ---------KDGQPGKDGLPGK---------DGK 333
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 47-218 2.83e-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: 80.75  E-value: 2.83e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461   47 DLVFVLDSSSSVGKEN-FEKVRQWVANLVDTFevgPERTRVGVVHYSDRPATAFELGRfgSRAAVRAAARQLAYhGGHTH 125
Cdd:COG1240     94 DVVLVVDASGSMAAENrLEAAKGALLDFLDDY---RPRDRVGLVAFGGEAEVLLPLTR--DREALKRALDELPP-GGGTP 167

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461  126 TGDALRfITRHSFAPRAGGRpgdrafKQVAILLTDGR---SQDLVLPAATAARRAGIRIFAVGVG-EALREE-LEEIASE 200
Cdd:COG1240    168 LGDALA-LALELLKRADPAR------RKVIVLLTDGRdnaGRIDPLEAAELAAAAGIRIYTIGVGtEAVDEGlLREIAEA 240

                          170
                   ....*....|....*...
gi 1062879461  201 pTAAHVFHVSDFDAIDKI 218
Cdd:COG1240    241 -TGGRYFRADDLSELAAI 257
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 606-844 4.67e-15

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 79.56  E-value: 4.67e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461  606 GEKGERGLDGFPGKQGEAgeqgrpgppgepGPQGEKGAVGPAGPPGLPGSVVQReGLKGKQGAPGPQGHQGPPGPPGAPG 685
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQ------------GPRGDRGETGPAGPAGPPGPQGER-GEKGPAGPQGEAGPQGPAGKDGEAG 183

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461  686 LMGPEGKDGPPGLQGLRGKRGEAGPPGvPGLLGQQGPPGPPGVPGPPGPGGPPGLPGEIGFPGKPGAPGQVGPPGKDgpn 765
Cdd:NF038329   184 AKGPAGEKGPQGPRGETGPAGEQGPAG-PAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKD--- 259

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1062879461  766 gppglpgpkGDPGDRGEDGLPGQRGPRGEAGEQGLAGRPGEKGEAGLPGFPGLPGERGEKGDQGEKGALGLPGLKGDQG 844
Cdd:NF038329   260 ---------GPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPG 329
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1012-1333 4.55e-11

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: 66.85  E-value: 4.55e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461 1012 GDRGAPGIPGSPGNRGEPGmaVAGPPGPSGPPGEKGPPGSRGPPGFPGPQGPAGQDGVPGNPGERGPPGKPGPSSVLSPG 1091
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQG--PRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461 1092 DVNLLVKDVCNDCPPGPPGLPGLPGFKGDKGLPGKPGReGTEGKKgdagprGLPGPPGIAGPQGSKGEHGADGETGQKGD 1171
Cdd:NF038329   195 GPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPD------GDPGPTGEDGPQGPDGPAGKDGPRGDRGE 267

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461 1172 QGHpgvpgfmgppgdpgppgadgiagaagppgiqgppgkegppgpqgpsglpgiPGEEGKEGRDGKPGPPGEQGKTGEPG 1251
Cdd:NF038329   268 AGP---------------------------------------------------DGPDGKDGERGPVGPAGKDGQNGKDG 296

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461 1252 LPGPEGARGPPGFKGHTGDSGPPGPRGEPGATGPPGREGSPGKDGDTGPTGPQGPQglrglpgksgspGSPGEPGTPGSP 1331
Cdd:NF038329   297 LPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPEVPQKPD------------TAPHTPKTPQIP 364


                   ..
gi 1062879461 1332 GQ 1333
Cdd:NF038329   365 GQ 366
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 871-1176 2.27e-10

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: 64.93  E-value: 2.27e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461  871 PGEPGPRGEKGDPGTPGEPGSPGHPGELGPRGPIGPPGAKGQEGAQGTPGAAGspgapglvgPPGPsgpPGSVGPPGSRG 950
Cdd:NF038329   122 PGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQG---------PAGK---DGEAGAKGPAG 189

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461  951 PPGKDGERGEKGAAGEEGSPGPAGPRGNPGSPGPPGPPGRGKDGDPGLRGPPGLPGPMGTKGDRGAPGIPGSPGNRGEPG 1030
Cdd:NF038329   190 EKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAG 269

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461 1031 mavagppgpsgppgekgppgsrgppgfpgpqgpagQDGVPGNPGERGPPGKPGpssvlspgdvnllvKDVCNdcppgppg 1110
Cdd:NF038329   270 -----------------------------------PDGPDGKDGERGPVGPAG--------------KDGQN-------- 292

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1062879461 1111 lpglpgfkGDKGLPGKPGREGTEGKKGdagprglpgppgIAGPQGSKGEHGADGETGQKGDQGHPG 1176
Cdd:NF038329   293 --------GKDGLPGKDGKDGQNGKDG------------LPGKDGKDGQPGKDGLPGKDGKDGQPG 338
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1284-1340 7.82e-08

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 50.18  E-value: 7.82e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1062879461 1284 GPPGREGSPGKDGDTGPTGPQGPQGLRGLPGKSGSPGSPGEPGTPGSPGQKGTKGEN 1340
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
1227-1413 1.67e-07

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 55.81  E-value: 1.67e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461 1227 GEEGKEGRDGKPGPPGEQGKTGEPGLPGPEGARGPPGFKGHTGDSGPPGPRGEPGATGPPGREGSPGKDGDTGPTGPQGP 1306
Cdd:COG5164     34 GSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDD 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461 1307 QGLRGLPGKSGSP-----GSPGEPGTPGS-PGQKGTKGENGSPGLPGFLGPRGPQGEPGEKGVPGKEGA--PGKPGEPGL 1378
Cdd:COG5164    114 GGATGPPDDGGSTtppsgGSTTPPGDGGStPPGPGSTGPGGSTTPPGDGGSTTPPGPGGSTTPPDDGGSttPPNKGETGT 193

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1062879461 1379 RGERGDPGIKGDKGPPGGKGQPGDPGIPGHKGHTG 1413
Cdd:COG5164    194 DIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKT 228
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 784-838 3.99e-06

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: 45.56  E-value: 3.99e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1062879461  784 GLPGQRGPRGEAGEQGLAGRPGEKGEAGLPGFPGLPGERGEKGDQGEKGALGLPG 838
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
PHA03169 PHA03169
hypothetical protein; Provisional
 1228-1381 2.55e-04

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 45.35  E-value: 2.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461 1228 EEGKEGRDGKPGPPGEQGKTGEPGLPGPEGARGppGFKGHTGDSGPPGPRGEPGATGPPGREG--SPGKDGDTGPTGPQG 1305
Cdd:PHA03169    85 EERGQGGPSGSGSESVGSPTPSPSGSAEELASG--LSPENTSGSSPESPASHSPPPSPPSHPGphEPAPPESHNPSPNQQ 162

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1062879461 1306 PQGLRGLPGKSGSpgSPGEPGTPGSPGQKGTKGENGSPGLPGflGPRGPQGEPGEKGVPGKEGAPGKPGEPGLRGE 1381
Cdd:PHA03169   163 PSSFLQPSHEDSP--EEPEPPTSEPEPDSPGPPQSETPTSSP--PPQSPPDEPGEPQSPTPQQAPSPNTQQAVEHE 234
 
Name Accession Description Interval E-value
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 45-228 1.89e-58

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: 201.07  E-value: 1.89e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461   45 HYDLVFVLDSSSSVGKENFEKVRQWVANLVDTFEVGPERTRVGVVHYSDRPATAFELGRFGSRAAVRAAARQLAYHGGHT 124
Cdd:cd01475      2 PTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGT 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461  125 HTGDALRFITRHSFAPRAGGRPGDRAFKQVAILLTDGRSQDLVLPAATAARRAGIRIFAVGVGEALREELEEIASEPTAA 204
Cdd:cd01475     82 MTGLAIQYAMNNAFSEAEGARPGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLAD 161

                          170       180
                   ....*....|....*....|....
gi 1062879461  205 HVFHVSDFDAIDKIRGKLRRRLCE 228
Cdd:cd01475    162 HVFYVEDFSTIEELTKKFQGKICV 185
VWA pfam00092
von Willebrand factor type A domain;
47-221 2.94e-53

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 184.40  E-value: 2.94e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461   47 DLVFVLDSSSSVGKENFEKVRQWVANLVDTFEVGPERTRVGVVHYSDRPATAFELGRFGSRAAVRAAARQLAY-HGGHTH 125
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYlGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461  126 TGDALRFITRHSFAPRAGGRPGdraFKQVAILLTDGRSQDL-VLPAATAARRAGIRIFAVGVGEALREELEEIASEPTAA 204
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPG---APKVVVLLTDGRSQDGdPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEG 157

                          170
                   ....*....|....*..
gi 1062879461  205 HVFHVSDFDAIDKIRGK 221
Cdd:pfam00092  158 HVFTVSDFEALEDLQDQ 174
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 47-212 2.58e-52

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: 181.33  E-value: 2.58e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461   47 DLVFVLDSSSSVGKENFEKVRQWVANLVDTFEVGPERTRVGVVHYSDRPATAFELGRFGSRAAVRAAARQLAYHGGHTHT 126
Cdd:cd01482      2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTRT 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461  127 GDALRFITRHSFAPRAGGRPGdraFKQVAILLTDGRSQDLVLPAATAARRAGIRIFAVGVGEALREELEEIASEPTAAHV 206
Cdd:cd01482     82 GKALTHVREKNFTPDAGARPG---VPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHV 158


                   ....*.
gi 1062879461  207 FHVSDF 212
Cdd:cd01482    159 FNVADF 164
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 47-212 3.85e-52

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: 180.89  E-value: 3.85e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461   47 DLVFVLDSSSSVGKENFEKVRQWVANLVDTFEVGPERTRVGVVHYSDRPATAFELGRFGSRAAVRAAARQLAYHGGHTHT 126
Cdd:cd01472      2 DIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTNT 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461  127 GDALRFITRHSFAPRAGGRPGdraFKQVAILLTDGRSQDLVLPAATAARRAGIRIFAVGVGEALREELEEIASEPTAAHV 206
Cdd:cd01472     82 GKALKYVRENLFTEASGSREG---VPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKELYV 158


                   ....*.
gi 1062879461  207 FHVSDF 212
Cdd:cd01472    159 FNVADF 164
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 46-207 1.26e-45

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: 162.08  E-value: 1.26e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461   46 YDLVFVLDSSSSVGKENFEKVRQWVANLVDTFEVGPERTRVGVVHYSDRPATAFELGRFGSRAAVRAAARQLAYHGG-HT 124
Cdd:cd01450      1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGgGT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461  125 HTGDALRFITRHSFAPRAgGRPGDRafkQVAILLTDGRSQDL--VLPAATAARRAGIRIFAVGVGEALREELEEIASEPT 202
Cdd:cd01450     81 NTGKALQYALEQLFSESN-ARENVP---KVIIVLTDGRSDDGgdPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPS 156


                   ....*
gi 1062879461  203 AAHVF 207
Cdd:cd01450    157 ERHVF 161
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 47-218 1.84e-40

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: 147.60  E-value: 1.84e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461    47 DLVFVLDSSSSVGKENFEKVRQWVANLVDTFEVGPERTRVGVVHYSDRPATAFELGRFGSRAAVRAAARQLAYH-GGHTH 125
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461   126 TGDALRFITRHSFAPRAGGRPGdraFKQVAILLTDGRSQDL---VLPAATAARRAGIRIFAVGVGEA-LREELEEIASEP 201
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRG---APKVVILITDGESNDGpkdLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLASAP 157

                           170
                    ....*....|....*..
gi 1062879461   202 TAAHVFHVSDFDAIDKI 218
Cdd:smart00327  158 GGVYVFLPELLDLLIDL 174
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 248-435 2.00e-36

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


Pssm-ID: 214560  Cd Length: 184  Bit Score: 136.33  E-value: 2.00e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461   248 GTKEITGFDLMDL-FSVKTLLGERenGAQSSYvRMGSFPVV-QRTEDVFPQGLPDEYAFVTTFRLRKSSRredWYIWQVI 325
Cdd:smart00210    1 GQDLLQVFDLPSLsFAIRQVVGPE--PGSPAY-RLGDPALVpQPTRDLFPSGLPEDFSLLTTFRQTPKSR---GVLFAIY 74

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461   326 DQYGIPQVSIRLDGENKAVEYSAVGAMKDAVRVVFRGPrvhDLFDRDWHKVALSVQAQHASLYVDCALVQTLPLEER--E 403
Cdd:smart00210   75 DAQNVRQFGLEVDGRANTLLLRYQGVDGKQHTVSFRNL---PLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPgqP 151

                           170       180       190
                    ....*....|....*....|....*....|..
gi 1062879461   404 NIDIQGKTAIGKRLYDSVPVDFDLQRVVIYCD 435
Cdd:smart00210  152 PIDTDGIEVRGAQAADRKPFQGDLQQLKIVCD 183
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 47-212 3.27e-33

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: 126.67  E-value: 3.27e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461   47 DLVFVLDSSSSVGKENFEKVRQWVANLVDTFEVGPERTRVGVVHYSDRPATAFELGRFGSRAAVRAAARQLAYHGGH-TH 125
Cdd:cd01481      2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSqLN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461  126 TGDALRFITRHSFAPRAGGRPGDrAFKQVAILLTDGRSQDLVLPAATAARRAGIRIFAVGVGEALREELEEIASEPTaaH 205
Cdd:cd01481     82 TGSALDYVVKNLFTKSAGSRIEE-GVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPS--F 158


                   ....*..
gi 1062879461  206 VFHVSDF 212
Cdd:cd01481    159 VFQVSDF 165
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 47-218 2.15e-32

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: 124.78  E-value: 2.15e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461   47 DLVFVLDSSSSVGKENFEKVRQWVANLVDTFEVGPERTRVGVVHYSDRPATAFELGRFGSRAAVRAAARQLAYHGGHTHT 126
Cdd:cd01469      2 DIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTNT 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461  127 GDALRFITRHSFAPRAGGRPGdrAFKqVAILLTDGRSQD-----LVLPaatAARRAGIRIFAVGVG-----EALREELEE 196
Cdd:cd01469     82 ATAIQYVVTELFSESNGARKD--ATK-VLVVITDGESHDdpllkDVIP---QAEREGIIRYAIGVGghfqrENSREELKT 155

                          170       180
                   ....*....|....*....|..
gi 1062879461  197 IASEPTAAHVFHVSDFDAIDKI 218
Cdd:cd01469    156 IASKPPEEHFFNVTDFAALKDI 177
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 46-207 4.52e-30

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: 117.28  E-value: 4.52e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461   46 YDLVFVLDSSSSVGKENFEKVRQWVANLVDTFEVGPERTRVGVVHYSDRPATAFELGRFGSRAAVRAAARQL-AYHGGHT 124
Cdd:cd00198      1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALkKGLGGGT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461  125 HTGDALRFITRHSFAPRAGGRpgdrafKQVAILLTDGRSQD---LVLPAATAARRAGIRIFAVGVG-EALREELEEIASE 200
Cdd:cd00198     81 NIGAALRLALELLKSAKRPNA------RRVIILLTDGEPNDgpeLLAEAARELRKLGITVYTIGIGdDANEDELKEIADK 154


                   ....*..
gi 1062879461  201 PTAAHVF 207
Cdd:cd00198    155 TTGGAVF 161
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1118-1386 2.50e-27

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 117.31  E-value: 2.50e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461 1118 KGDKGLPGKPGREGTEGKKGDAGPRGLPGPPGIAGPQGSKGEHGADGETGQKGDQGHPGvpgfmgppgdpgppgadgiag 1197
Cdd:NF038329   119 KGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAG--------------------- 177

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461 1198 aagppgIQGPPGKEGPpgpqgpsglpgiPGEEGKEGRDGKPGPPGEQGKTGEPGLPGPEGARGPPGFKGHTGDSGppgpr 1277
Cdd:NF038329   178 ------KDGEAGAKGP------------AGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQ----- 234

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461 1278 gepgaTGPPGREGSPGKDGDTGPTGPQGPQGLRGLPGKSGSPGSPGEPGTPGSPGQKGTKGENGSPGLPGFLGPRGPQGE 1357
Cdd:NF038329   235 -----QGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGK 309

                          250       260
                   ....*....|....*....|....*....
gi 1062879461 1358 PGEKGVPGKEGAPGKPGEPGLRGERGDPG 1386
Cdd:NF038329   310 DGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 47-207 3.39e-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: 100.55  E-value: 3.39e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461   47 DLVFVLDSSSSVgKENFEKVRQWVANLVDTFEVGPERTRVGVVHYS--DRPATAFELGRFGSRAAVRAAARQLAYHGGHT 124
Cdd:cd01476      2 DLLFVLDSSGSV-RGKFEKYKKYIERIVEGLEIGPTATRVALITYSgrGRQRVRFNLPKHNDGEELLEKVDNLRFIGGTT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461  125 HTGDALRFITRHsFAPRAGGRPGdraFKQVAILLTDGRSQDLVLPAATAARR-AGIRIFAVGVGE---ALREELEEIASE 200
Cdd:cd01476     81 ATGAAIEVALQQ-LDPSEGRREG---IPKVVVVLTDGRSHDDPEKQARILRAvPNIETFAVGTGDpgtVDTEELHSITGN 156


                   ....*..
gi 1062879461  201 PTaaHVF 207
Cdd:cd01476    157 ED--HIF 161
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1117-1373 4.32e-24

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 107.30  E-value: 4.32e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461 1117 FKGDKGLPGKPGREGTEGKKGDAGPRGLPGPPGIAGPQGSKGEHGADGETGQKGDQGHPGVPGFMGPPGDPGPPGADGIA 1196
Cdd:NF038329   115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461 1197 GAAGPPGIQGPPGKEGPPGPQgpsglpgipGEEGKEGRDGKPGPPGeQGKTGEPGLPGPEGARGPpgfkghtgdsgppgp 1276
Cdd:NF038329   195 GPRGETGPAGEQGPAGPAGPD---------GEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGP--------------- 249

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461 1277 rgepgaTGPPGREGSPGKDGDTGPTGPQGPQGLRGLPGKSGSPGSPGEPGTPGSPGQKGTKGENGSPGLPGFLGPRGPQG 1356
Cdd:NF038329   250 ------QGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPG 323

                          250
                   ....*....|....*..
gi 1062879461 1357 EPGEKGVPGKEGAPGKP 1373
Cdd:NF038329   324 KDGLPGKDGKDGQPGKP 340
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 47-206 4.51e-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: 100.92  E-value: 4.51e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461   47 DLVFVLDSSSSVGKENFEKVRQWVANLVDTFEVG------PERTRVGVVHYSDRPATAFELGRFGSRAAVRAAARQ-LAY 119
Cdd:cd01480      4 DITFVLDSSESVGLQNFDITKNFVKRVAERFLKDyyrkdpAGSWRVGVVQYSDQQEVEAGFLRDIRNYTSLKEAVDnLEY 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461  120 HGGHTHTGDALRFITRHSFAPRAGGRpgdrafKQVAILLTDGRSQ----DLVLPAATAARRAGIRIFAVGVGEALREELE 195
Cdd:cd01480     84 IGGGTFTDCALKYATEQLLEGSHQKE------NKFLLVITDGHSDgspdGGIEKAVNEADHLGIKIFFVAVGSQNEEPLS 157

                          170
                   ....*....|.
gi 1062879461  196 EIASEPTAAHV 206
Cdd:cd01480    158 RIACDGKSALY 168
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 503-829 9.16e-22

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 100.36  E-value: 9.16e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461  503 GPKGDVGATGPAGAPGPkgekgdtgrgpfvQGEKGEKGSLGLPGPPGRDGSKGMRGEPGEPGELGLPGEVGLRgsqgppg 582
Cdd:NF038329   117 GEKGEPGPAGPAGPAGE-------------QGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPA------- 176

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461  583 lpgppgpigapglhGERGEKGAQGEKGERGLDGFPGKQGEAGEQGRPGPPGEPGPQGEKGAVGPAGPPGLPGsvVQREGL 662
Cdd:NF038329   177 --------------GKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQ--QGPDGD 240

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461  663 KGKQGApgpqghqgppgppgapglMGPEGKDGPPGLQGLRGKRGEAGPPGVPgllgqqgppgppgvpgppgpggppglpg 742
Cdd:NF038329   241 PGPTGE------------------DGPQGPDGPAGKDGPRGDRGEAGPDGPD---------------------------- 274

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461  743 eigfpGKPGAPGQVGPPGKDGPngppglpgpkgdpgdRGEDGLPGQRGPRGEAGEQGLagrPGEKGEAGLPGFPGLPGER 822
Cdd:NF038329   275 -----GKDGERGPVGPAGKDGQ---------------NGKDGLPGKDGKDGQNGKDGL---PGKDGKDGQPGKDGLPGKD 331


                   ....*..
gi 1062879461  823 GEKGDQG 829
Cdd:NF038329   332 GKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 486-816 1.08e-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: 96.90  E-value: 1.08e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461  486 PPGEKGEKGFDGPVGLPGPKGDVGATGPAGAPGPKGEKGDTG-RGPfvQGEKGEKGSLGLPGPPGRDGSKGMRGEPGEPG 564
Cdd:NF038329   127 PAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGeAGP--QGPAGKDGEAGAKGPAGEKGPQGPRGETGPAG 204

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461  565 ELGLPGEVGLRGSQGPPGLPGPPGPIGAPGlHGERGEKGAQGEKGERGLDGFPGKQGEageqgrpgppgepgpqgekgav 644
Cdd:NF038329   205 EQGPAGPAGPDGEAGPAGEDGPAGPAGDGQ-QGPDGDPGPTGEDGPQGPDGPAGKDGP---------------------- 261

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461  645 gpagppglpgsvvqreglkgkqgapgpqghqgppgppgapglmgpEGKDGPPGLQGLRGKRGEAGPPGVpgllgqqgppg 724
Cdd:NF038329   262 ---------------------------------------------RGDRGEAGPDGPDGKDGERGPVGP----------- 285

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461  725 ppgvpgppgpggppglpgeigfPGKPGAPGQVGPPGKDGPngppglpgpkgdpgdRGEDGLPGQRGPRGEAGEQGLAGRP 804
Cdd:NF038329   286 ----------------------AGKDGQNGKDGLPGKDGK---------------DGQNGKDGLPGKDGKDGQPGKDGLP 328

                          330
                   ....*....|..
gi 1062879461  805 GEKGEAGLPGFP 816
Cdd:NF038329   329 GKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 488-712 1.42e-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: 90.35  E-value: 1.42e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461  488 GEKGEKGFDGPVGLPGPKGDVGATGPAGAPGPKGEKGDTGRgPFVQGEKGEKGSLGLPGPPGRDGSKGMRGEPGEPGELG 567
Cdd:NF038329   120 GEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGE-KGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRG 198

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461  568 LPGEVGLRGSQGPPGLPGPPGPIGAPGLHGE--RGEKGAQGEKGERGLDGFPGKQGEAGEQGRPGPPGEPGPQGEKGavg 645
Cdd:NF038329   199 ETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPagDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG--- 275

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461  646 pagppglpgsvvqREGLKGKQGAPGPQGHQGPPGPPGAPGLMGPEGKDGPPGLQ---GLRGKRGEAGPPG 712
Cdd:NF038329   276 -------------KDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDgkdGQPGKDGLPGKDG 332
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1289-1571 1.13e-17

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: 87.65  E-value: 1.13e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461 1289 EGSPGKDGDTGPTGPQGPQGLRGLPGKSGSPGSPGEPGTPGSPGQKGTKGENGSPGLpgfLGPRGPQGEPGEKGVPGKEG 1368
Cdd:NF038329   116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGP---QGPAGKDGEAGAKGPAGEKG 192

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461 1369 APGKPGEPGLRGERGDPGIKGDKGPPGGKGQPGDPGIPGhKGHTGLMGPQGPPGENGPAGPPGPPGQPGFPGLRGESpsm 1448
Cdd:NF038329   193 PQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEA--- 268

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461 1449 dvlrrliqeelekqletklayllaqmpsahtkssqgrpgppGPPGKDGLPGRAGPVGEPGRPGQGGLEGPSGPVGPKGER 1528
Cdd:NF038329   269 -----------------------------------------GPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQN 307

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1062879461 1529 GAKGDPGAPGvglrgemGPPGIPGQPGEPGYAKDGLPGSPGPQ 1571
Cdd:NF038329   308 GKDGLPGKDG-------KDGQPGKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 691-923 1.19e-17

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: 87.65  E-value: 1.19e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461  691 GKDGPPGLQGLRGKRGEAGPPGvpgllgqqgppgppgvpgPPGPGGPPGLPGEIGFPGKPGAPGQVGPPGKDGPNGPPGL 770
Cdd:NF038329   126 GPAGPAGEQGPRGDRGETGPAG------------------PAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGP 187

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461  771 PGPKGDPGDRGEDGLPGQRGPRGEAGEQGLAGRPGEKGEAGLPGfPGLPGERGEKGDQGEKGALGLPGLKGDQGAKGEVG 850
Cdd:NF038329   188 AGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRG 266

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1062879461  851 PPGPPGLPgttslftphprmpGEPGPRGEKGDPGTPGEPGSPGHPGELGPRGPIGPPGAKGQEGAQGTPGAAG 923
Cdd:NF038329   267 EAGPDGPD-------------GKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDG 326
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 660-897 1.08e-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: 1.08e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461  660 EGLKGKQGAPGPQGHQGPPGPPGAPGLMGPEGKDGPPGLQGLRGKRGEAGPPGVPGLLGQQGPPGPPGVPGPPGPGGPPG 739
Cdd:NF038329   116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461  740 LPGEIGFPGKPGAPGQVGPPGKDGPNGPPGLPGPKGDPG-----DRGEDGLPGQRGPRGEAGEQGLAGRPGEKGEAGLPG 814
Cdd:NF038329   196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQqgpdgDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461  815 FPGLPGERGEKGDQGEKGALGLPGLKGDQGAKGEvgppgppglpgttslftphprmPGEPGPRGEKGDPGTPGEPGSPGH 894
Cdd:NF038329   276 KDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGK----------------------DGLPGKDGKDGQPGKDGLPGKDGK 333


                   ...
gi 1062879461  895 PGE 897
Cdd:NF038329   334 DGQ 336
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1232-1585 1.75e-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: 84.19  E-value: 1.75e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461 1232 EGRDGKPGPPGEQGKTGEPGLPGPEGARGPPGFKGHTGDSGPPGPRGEPGATGPPGREGSPGKDGDTGPTGPQGPQGLRG 1311
Cdd:NF038329   116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461 1312 LPGKSGSPGSPGEPGTPGSPGQKGTKGENGSPGLPGfLGPRGPQGEPGEKGVPGKEGAPGKPGEPGLRGERGDPGIkgdk 1391
Cdd:NF038329   196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGP---- 270

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461 1392 gppggkgqpgdpgiPGHKGHTGlmgpqgppgengpagppgppgqpgfpglrgespsmdvlrrliqeelekqletklayll 1471
Cdd:NF038329   271 --------------DGPDGKDG---------------------------------------------------------- 278

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461 1472 aqmpsahtkssqgrpgppgppgkdglpgRAGPVGEPGRPGQGGLEGPSGPVGPKGERGAKGDPGAPGvglrgemgppgip 1551
Cdd:NF038329   279 ----------------------------ERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDG------------- 317

                          330       340       350
                   ....*....|....*....|....*....|....
gi 1062879461 1552 gqpgepgyaKDGLPGSPGPQGEtgpaghpgpPGP 1585
Cdd:NF038329   318 ---------KDGQPGKDGLPGK---------DGK 333
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 47-218 2.83e-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: 80.75  E-value: 2.83e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461   47 DLVFVLDSSSSVGKEN-FEKVRQWVANLVDTFevgPERTRVGVVHYSDRPATAFELGRfgSRAAVRAAARQLAYhGGHTH 125
Cdd:COG1240     94 DVVLVVDASGSMAAENrLEAAKGALLDFLDDY---RPRDRVGLVAFGGEAEVLLPLTR--DREALKRALDELPP-GGGTP 167

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461  126 TGDALRfITRHSFAPRAGGRpgdrafKQVAILLTDGR---SQDLVLPAATAARRAGIRIFAVGVG-EALREE-LEEIASE 200
Cdd:COG1240    168 LGDALA-LALELLKRADPAR------RKVIVLLTDGRdnaGRIDPLEAAELAAAAGIRIYTIGVGtEAVDEGlLREIAEA 240

                          170
                   ....*....|....*...
gi 1062879461  201 pTAAHVFHVSDFDAIDKI 218
Cdd:COG1240    241 -TGGRYFRADDLSELAAI 257
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 45-218 3.67e-16

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: 78.32  E-value: 3.67e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461   45 HYDLVFVLDSSSSVGKENFEkVRQWVANLVDTFeVGPErTRVGVVHYSDRPATAFELGRFGSRAAVRAAARQLAYHGGHT 124
Cdd:cd01474      4 HFDLYFVLDKSGSVAANWIE-IYDFVEQLVDRF-NSPG-LRFSFITFSTRATKILPLTDDSSAIIKGLEVLKKVTPSGQT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461  125 HTGDALRFITRHSFAPRAGGRpgdrAFKQVAILLTDGRSQDLV----LPAATAARRAGIRIFAVGVGEALREELEEIASE 200
Cdd:cd01474     81 YIHEGLENANEQIFNRNGGGR----ETVSVIIALTDGQLLLNGhkypEHEAKLSRKLGAIVYCVGVTDFLKSQLINIADS 156

                          170
                   ....*....|....*....
gi 1062879461  201 PTaaHVFHVSD-FDAIDKI 218
Cdd:cd01474    157 KE--YVFPVTSgFQALSGI 173
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 606-844 4.67e-15

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 79.56  E-value: 4.67e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461  606 GEKGERGLDGFPGKQGEAgeqgrpgppgepGPQGEKGAVGPAGPPGLPGSVVQReGLKGKQGAPGPQGHQGPPGPPGAPG 685
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQ------------GPRGDRGETGPAGPAGPPGPQGER-GEKGPAGPQGEAGPQGPAGKDGEAG 183

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461  686 LMGPEGKDGPPGLQGLRGKRGEAGPPGvPGLLGQQGPPGPPGVPGPPGPGGPPGLPGEIGFPGKPGAPGQVGPPGKDgpn 765
Cdd:NF038329   184 AKGPAGEKGPQGPRGETGPAGEQGPAG-PAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKD--- 259

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1062879461  766 gppglpgpkGDPGDRGEDGLPGQRGPRGEAGEQGLAGRPGEKGEAGLPGFPGLPGERGEKGDQGEKGALGLPGLKGDQG 844
Cdd:NF038329   260 ---------GPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPG 329
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 47-187 5.04e-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: 69.34  E-value: 5.04e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461   47 DLVFVLDSSSSVGKEN-FEKVRQWVANLVDTFEVGPERTRVGVVHYSDRPATAFELGRFGSRAAVRAAA-----RQLAYH 120
Cdd:cd01471      2 DLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPNSTNKDLALNairalLSLYYP 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1062879461  121 GGHTHTGDALRFITRHSFAPRaGGRPGdraFKQVAILLTDGRSQDL--VLPAATAARRAGIRIFAVGVG 187
Cdd:cd01471     82 NGSTNTTSALLVVEKHLFDTR-GNREN---APQLVIIMTDGIPDSKfrTLKEARKLRERGVIIAVLGVG 146
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 47-226 3.12e-11

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 66.28  E-value: 3.12e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461   47 DLVFVLDSSSSVGKENFEKVRQWVANLVDTFevgPERTRVGVVHYSDRPATAFELGRFGSRAAVRAAARQLaYHGGHTHT 126
Cdd:COG2304     93 NLVFVIDVSGSMSGDKLELAKEAAKLLVDQL---RPGDRVSIVTFAGDARVLLPPTPATDRAKILAAIDRL-QAGGGTAL 168

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461  127 GDALRFITRHsfaPRAGGRPGdrAFKQVaILLTDGR------SQDLVLPAATAARRAGIRIFAVGVGEALREELEEIASE 200
Cdd:COG2304    169 GAGLELAYEL---ARKHFIPG--RVNRV-ILLTDGDanvgitDPEELLKLAEEAREEGITLTTLGVGSDYNEDLLERLAD 242

                          170       180
                   ....*....|....*....|....*.
gi 1062879461  201 PTAAHVFHVSDFDAIDKIRGKLRRRL 226
Cdd:COG2304    243 AGGGNYYYIDDPEEAEKVFVREFSRI 268
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1012-1333 4.55e-11

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: 66.85  E-value: 4.55e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461 1012 GDRGAPGIPGSPGNRGEPGmaVAGPPGPSGPPGEKGPPGSRGPPGFPGPQGPAGQDGVPGNPGERGPPGKPGPSSVLSPG 1091
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQG--PRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461 1092 DVNLLVKDVCNDCPPGPPGLPGLPGFKGDKGLPGKPGReGTEGKKgdagprGLPGPPGIAGPQGSKGEHGADGETGQKGD 1171
Cdd:NF038329   195 GPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPD------GDPGPTGEDGPQGPDGPAGKDGPRGDRGE 267

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461 1172 QGHpgvpgfmgppgdpgppgadgiagaagppgiqgppgkegppgpqgpsglpgiPGEEGKEGRDGKPGPPGEQGKTGEPG 1251
Cdd:NF038329   268 AGP---------------------------------------------------DGPDGKDGERGPVGPAGKDGQNGKDG 296

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461 1252 LPGPEGARGPPGFKGHTGDSGPPGPRGEPGATGPPGREGSPGKDGDTGPTGPQGPQglrglpgksgspGSPGEPGTPGSP 1331
Cdd:NF038329   297 LPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPEVPQKPD------------TAPHTPKTPQIP 364


                   ..
gi 1062879461 1332 GQ 1333
Cdd:NF038329   365 GQ 366
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 871-1176 2.27e-10

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: 64.93  E-value: 2.27e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461  871 PGEPGPRGEKGDPGTPGEPGSPGHPGELGPRGPIGPPGAKGQEGAQGTPGAAGspgapglvgPPGPsgpPGSVGPPGSRG 950
Cdd:NF038329   122 PGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQG---------PAGK---DGEAGAKGPAG 189

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461  951 PPGKDGERGEKGAAGEEGSPGPAGPRGNPGSPGPPGPPGRGKDGDPGLRGPPGLPGPMGTKGDRGAPGIPGSPGNRGEPG 1030
Cdd:NF038329   190 EKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAG 269

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461 1031 mavagppgpsgppgekgppgsrgppgfpgpqgpagQDGVPGNPGERGPPGKPGpssvlspgdvnllvKDVCNdcppgppg 1110
Cdd:NF038329   270 -----------------------------------PDGPDGKDGERGPVGPAG--------------KDGQN-------- 292

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1062879461 1111 lpglpgfkGDKGLPGKPGREGTEGKKGdagprglpgppgIAGPQGSKGEHGADGETGQKGDQGHPG 1176
Cdd:NF038329   293 --------GKDGLPGKDGKDGQNGKDG------------LPGKDGKDGQPGKDGLPGKDGKDGQPG 338
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
49-218 4.17e-09

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 58.01  E-value: 4.17e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461   49 VFVLDSSSSVGKENFEKVRQWVANLVDTFEVGP---ERTRVGVVHYSDR--------PATAFELGRFGSraavraaarql 117
Cdd:COG4245      9 YLLLDTSGSMSGEPIEALNEGLQALIDELRQDPyalETVEVSVITFDGEakvllpltDLEDFQPPDLSA----------- 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461  118 ayhGGHTHTGDALRFITRHSFAPRAGGRP-GDRAFKQVAILLTDGRSQDLVLPAATAA-----RRAGIRIFAVGVG-EAL 190
Cdd:COG4245     78 ---SGGTPLGAALELLLDLIERRVQKYTAeGKGDWRPVVFLITDGEPTDSDWEAALQRlkdgeAAKKANIFAIGVGpDAD 154

                          170       180
                   ....*....|....*....|....*...
gi 1062879461  191 REELEEIASEptaAHVFHVSDFDAIDKI 218
Cdd:COG4245    155 TEVLKQLTDP---VRALDALDGLDFREF 179
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1284-1340 7.82e-08

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 50.18  E-value: 7.82e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1062879461 1284 GPPGREGSPGKDGDTGPTGPQGPQGLRGLPGKSGSPGSPGEPGTPGSPGQKGTKGEN 1340
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
1227-1413 1.67e-07

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 55.81  E-value: 1.67e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461 1227 GEEGKEGRDGKPGPPGEQGKTGEPGLPGPEGARGPPGFKGHTGDSGPPGPRGEPGATGPPGREGSPGKDGDTGPTGPQGP 1306
Cdd:COG5164     34 GSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDD 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461 1307 QGLRGLPGKSGSP-----GSPGEPGTPGS-PGQKGTKGENGSPGLPGFLGPRGPQGEPGEKGVPGKEGA--PGKPGEPGL 1378
Cdd:COG5164    114 GGATGPPDDGGSTtppsgGSTTPPGDGGStPPGPGSTGPGGSTTPPGDGGSTTPPGPGGSTTPPDDGGSttPPNKGETGT 193

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1062879461 1379 RGERGDPGIKGDKGPPGGKGQPGDPGIPGHKGHTG 1413
Cdd:COG5164    194 DIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKT 228
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
1152-1376 1.91e-07

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 55.81  E-value: 1.91e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461 1152 GPQGSKGEhGADGETGQKGDQGHPGVPGFMGPPGDPGPPGADGIAGAAGPPGIQGPPGKEGPPGPQGPSGLPGIPGEEGK 1231
Cdd:COG5164      2 GLYGPGKT-GPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461 1232 EGRDGKPGPPGEQGKTGEPGLPGPEGARGPPGFKGHTG--DSGPPGPRGEPGATGPPGREGS-PGKDGDTGPTG---PQG 1305
Cdd:COG5164     81 TTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGppDDGGSTTPPSGGSTTPPGDGGStPPGPGSTGPGGsttPPG 160

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1062879461 1306 PQGLRGLPGKSGSPGSPGEPG--TPGSPGQKGTKGENGSPGLPGFLGPRGPQGEPGEKGVPGKEGAPGKPGEP 1376
Cdd:COG5164    161 DGGSTTPPGPGGSTTPPDDGGstTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTGPKDQ 233
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1317-1373 4.06e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 48.26  E-value: 4.06e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1062879461 1317 GSPGSPGEPGTPGSPGQKGTKGENGSPGLPGFLGPRGPQGEPGEKGVPGKEGAPGKP 1373
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1305-1360 6.13e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 47.87  E-value: 6.13e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1062879461 1305 GPQGLRGLPGKSGSPGSPGEPGTPGSPGQKGTKGENGSPGLPGFLGPRGPQGEPGE 1360
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1320-1376 6.89e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 47.49  E-value: 6.89e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1062879461 1320 GSPGEPGTPGSPGQKGTKGENGSPGLPGFLGPRGPQGEPGEKGVPGKEGAPGKPGEP 1376
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1314-1370 8.98e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 47.49  E-value: 8.98e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1062879461 1314 GKSGSPGSPGEPGTPGSPGQKGTKGENGSPGLPGFLGPRGPQGEPGEKGVPGKEGAP 1370
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1323-1377 2.44e-06

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: 45.95  E-value: 2.44e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1062879461 1323 GEPGTPGSPGQKGTKGENGSPGLPGFLGPRGPQGEPGEKGVPGKEGAPGKPGEPG 1377
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 784-838 3.99e-06

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: 45.56  E-value: 3.99e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1062879461  784 GLPGQRGPRGEAGEQGLAGRPGEKGEAGLPGFPGLPGERGEKGDQGEKGALGLPG 838
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 780-833 8.25e-06

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: 44.79  E-value: 8.25e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1062879461  780 RGEDGLPGQRGPRGEAGEQGLAGRPGEKGEAGLPGFPGLPGERGEKGDQGEKGA 833
Cdd:pfam01391    3 PGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 47-200 1.11e-05

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 48.91  E-value: 1.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461   47 DLVFVLDSSSSVGKENFEKVRQWVANLVDTFEvgpERTRVGVVHYSDRPATAFELGRFGSRAAVRAAARQLAYHGGhTHT 126
Cdd:COG2425    120 PVVLCVDTSGSMAGSKEAAAKAAALALLRALR---PNRRFGVILFDTEVVEDLPLTADDGLEDAIEFLSGLFAGGG-TDI 195

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1062879461  127 GDALRFITRHSFAPRAGGRpgdrafkqVAILLTDGRSQDLVLP--AATAARRAGIRIFAVGVGEALREELEEIASE 200
Cdd:COG2425    196 APALRAALELLEEPDYRNA--------DIVLITDGEAGVSPEEllREVRAKESGVRLFTVAIGDAGNPGLLEALAD 263
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
1119-1373 4.10e-05

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 48.10  E-value: 4.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461 1119 GDKGLPGKPGREGTEGKKGDAGPRGLPGPPGIAGPQGSKGEHGADGETGQKGDQGHPGVPGFMGPPGDPGPPGADGIAGA 1198
Cdd:COG5164     22 GSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGGTRPAGNTGGTTP 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461 1199 AGPPGIQGPPGKEGPPGPQGPSGLPGIP--GEEGKEGRDGK-PGPPGEQGKTGEPGLPGPEGARGPPGFKGHTGdsgppg 1275
Cdd:COG5164    102 AGDGGATGPPDDGGATGPPDDGGSTTPPsgGSTTPPGDGGStPPGPGSTGPGGSTTPPGDGGSTTPPGPGGSTT------ 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461 1276 pRGEPGATGPPGREGSPGKDGDTGPTGPQGPQGLRGLPGKSGSPGSPgepgtpgsPGQKGTKGENGSPGLPGFLGPRGPQ 1355
Cdd:COG5164    176 -PPDDGGSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPP--------DDRGGKTGPKDQRPKTNPIERRGPE 246

                          250
                   ....*....|....*...
gi 1062879461 1356 GEPGEKGVPGKEGAPGKP 1373
Cdd:COG5164    247 RPEAAALPAELTALEAEN 264
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 47-221 8.30e-05

VWA BatA type: 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. Members of this subgroup are bacterial in origin. They are typified by the presence of a MIDAS motif.


Pssm-ID: 238744 [Multi-domain]  Cd Length: 180  Bit Score: 45.01  E-value: 8.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461   47 DLVFVLDSSSS------VGKENFEKVRQWVANLVDtfevGPERTRVGVVHYSDRPATAFELGRFGSRAAVRAAARQLAYH 120
Cdd:cd01467      4 DIMIALDVSGSmlaqdfVKPSRLEAAKEVLSDFID----RRENDRIGLVVFAGAAFTQAPLTLDRESLKELLEDIKIGLA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461  121 GGHTHTGDALRFITRHSFAPRAGGRpgdrafkqVAILLTDGRSQDLVLPAATAARRA---GIRIFAVGVGEALREELEEI 197
Cdd:cd01467     80 GQGTAIGDAIGLAIKRLKNSEAKER--------VIVLLTDGENNAGEIDPATAAELAknkGVRIYTIGVGKSGSGPKPDG 151

                          170       180
                   ....*....|....*....|....
gi 1062879461  198 ASEPtaahvfhvsDFDAIDKIRGK 221
Cdd:cd01467    152 STIL---------DEDSLVEIADK 166
VWA_2 pfam13519
von Willebrand factor type A domain;
48-146 1.59e-04

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 42.28  E-value: 1.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461   48 LVFVLDSSSS-----VGKENFEKVRQWVANLVDTFEvgpeRTRVGVVHYSDRPATAFELGRfgSRAAVRAAARQLAYHGG 122
Cdd:pfam13519    1 LVFVLDTSGSmrngdYGPTRLEAAKDAVLALLKSLP----GDRVGLVTFGDGPEVLIPLTK--DRAKILRALRRLEPKGG 74

                           90       100
                   ....*....|....*....|....
gi 1062879461  123 HTHTGDALRFITRHSFAPRAGGRP 146
Cdd:pfam13519   75 GTNLAAALQLARAALKHRRKNQPR 98
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 48-207 1.61e-04

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: 44.19  E-value: 1.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461   48 LVFVLDSSSSVGKENFEKVRQWVANLVDTFEvgpERTRVGVVHYSDRPATAFELGRFGSRAAVRAAARQLAyHGGHTHTG 127
Cdd:cd01465      3 LVFVIDRSGSMDGPKLPLVKSALKLLVDQLR---PDDRLAIVTYDGAAETVLPATPVRDKAAILAAIDRLT-AGGSTAGG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461  128 D----ALRFITRHsFAPRAGGRpgdrafkqvAILLTDG------RSQDLVLPAATAARRAGIRIFAVGVGEALREELEE- 196
Cdd:cd01465     79 AgiqlGYQEAQKH-FVPGGVNR---------ILLATDGdfnvgeTDPDELARLVAQKRESGITLSTLGFGDNYNEDLMEa 148

                          170       180
                   ....*....|....*....|..
gi 1062879461  197 -----------IASEPTAAHVF 207
Cdd:cd01465    149 iadagngntayIDNLAEARKVF 170
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 51-213 2.08e-04

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: 44.20  E-value: 2.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461   51 VLDSSSSVGKENFEKVRQWVANLVD---TFEVGPertRVGVVHYSDRPATAFELGRFGSRAAVR--AAARQLAY--HGGH 123
Cdd:cd01470      6 ALDASDSIGEEDFDEAKNAIKTLIEkisSYEVSP---RYEIISYASDPKEIVSIRDFNSNDADDviKRLEDFNYddHGDK 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461  124 --THTGDALRFITRHSFAPRAGGRPGDRAFKQVAILLTDGRS-------------QDLVL--PAATAARRAGIRIFAVGV 186
Cdd:cd01470     83 tgTNTAAALKKVYERMALEKVRNKEAFNETRHVIILFTDGKSnmggsplptvdkiKNLVYknNKSDNPREDYLDVYVFGV 162

                          170       180
                   ....*....|....*....|....*....
gi 1062879461  187 G-EALREELEEIASE-PTAAHVFHVSDFD 213
Cdd:cd01470    163 GdDVNKEELNDLASKkDNERHFFKLKDYE 191
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 793-846 2.19e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.55  E-value: 2.19e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1062879461  793 GEAGEQGLAGRPGEKGEAGLPGFPGLPGERGEKGDQGEKGALGLPGLKGDQGAK 846
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAP 54
PHA03169 PHA03169
hypothetical protein; Provisional
 1228-1381 2.55e-04

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 45.35  E-value: 2.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062879461 1228 EEGKEGRDGKPGPPGEQGKTGEPGLPGPEGARGppGFKGHTGDSGPPGPRGEPGATGPPGREG--SPGKDGDTGPTGPQG 1305
Cdd:PHA03169    85 EERGQGGPSGSGSESVGSPTPSPSGSAEELASG--LSPENTSGSSPESPASHSPPPSPPSHPGphEPAPPESHNPSPNQQ 162

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1062879461 1306 PQGLRGLPGKSGSpgSPGEPGTPGSPGQKGTKGENGSPGLPGflGPRGPQGEPGEKGVPGKEGAPGKPGEPGLRGE 1381
Cdd:PHA03169   163 PSSFLQPSHEDSP--EEPEPPTSEPEPDSPGPPQSETPTSSP--PPQSPPDEPGEPQSPTPQQAPSPNTQQAVEHE 234
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1341-1386 4.68e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.78  E-value: 4.68e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1062879461 1341 GSPGLPGFLGPRGPQGEPGEKGVPGKEGAPGKPGEPGLRGERGDPG 1386
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPG 46
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1251-1325 9.23e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.01  E-value: 9.23e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1062879461 1251 GLPGPEGARGPPGfkghtgdsgppgprgepgATGPPGREGSPGKDGDTGPTGPQGPQGLRGLPGKSGSPGSPGEP 1325
Cdd:pfam01391    1 GPPGPPGPPGPPG------------------PPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 494-565 9.98e-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: 38.63  E-value: 9.98e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1062879461  494 GFDGPVGLPGPKGDVGATGPAGAPGPKGEKGDTGRgpfvqgekgekgslglPGPPGRDGSKGMRGEPGEPGE 565
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGP----------------PGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 799-849 6.75e-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: 6.75e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1062879461  799 GLAGRPGEKGEAGLPGFPGLPGERGEKGDQGEKGALGLPGLKGDQGAKGEV 849
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAP 51
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 486-527 8.80e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 35.93  E-value: 8.80e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1062879461  486 PPGEKGEKGFDGPVGLPGPKGDVGATGPAGAPGPKGEKGDTG 527
Cdd:pfam01391   14 PPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
 
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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