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Conserved domains on  [gi|767945419|ref|XP_011513665|]
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collagen alpha-1(XXVIII) chain isoform X4 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 272-582 4.41e-31

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: 126.94  E-value: 4.41e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419 272 GNAQKGEAGERGPGGIPGYKGDKGERGECGKPGIKGDKGSPGPYGPKGPRGIQgitgppgdpgpkgfqgnkgepgppgpy 351
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQ--------------------------- 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419 352 gspgapgiGQQGIKGERGQEGRPGAPGPigVGEPGQPGPRGPEGVPGERGLPGEgfPGPKGEKGSEGPTGPQGLQGLSIK 431
Cdd:NF038329 168 --------GEAGPQGPAGKDGEAGAKGP--AGEKGPQGPRGETGPAGEQGPAGP--AGPDGEAGPAGEDGPAGPAGDGQQ 235

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419 432 GEKGDIGPVGPQGPMGIPGigsqgeqgiqgpigppgpqgpagqgLPGSKGEVGQMGPTGPRGPVG-IGVQGPKGEPGSIG 510
Cdd:NF038329 236 GPDGDPGPTGEDGPQGPDG-------------------------PAGKDGPRGDRGEAGPDGPDGkDGERGPVGPAGKDG 290

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767945419 511 LPGQPGVPGEDGAAGKKGEAGLPgargpegppgkgqpgpkgdeGKKGSKGNQGQRGLPGPEGPKGEPGIMGP 582
Cdd:NF038329 291 QNGKDGLPGKDGKDGQNGKDGLP--------------------GKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 47-209 3.59e-27

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: 108.15  E-value: 3.59e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419  47 IDIVFIVDSSESSKIALFDKQKDFVDSLSDKIfqltpgRSLEYDIKLAALQFSSSVQIDPPFSSWKDLQTFKQKVKSMNL 126
Cdd:cd01450    1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKL------DIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKY 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419 127 I-GQGTFSYYAISNATRLL--KREGRKDGVKVVLLMTDGIDHpKNPDVQSISEDARISGISFITIALSTvVNEAKLRLIS 203
Cdd:cd01450   75 LgGGGTNTGKALQYALEQLfsESNARENVPKVIIVLTDGRSD-DGGDPKEAAAKLKDEGIKVFVVGVGP-ADEEELREIA 152


                 ....*.
gi 767945419 204 GDSSSE 209
Cdd:cd01450  153 SCPSER 158
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 554-612 1.72e-05

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


:

Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.87  E-value: 1.72e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767945419  554 GKKGSKGNQGQRGLPGPEGPKGEPGIMGPFGMPGTsiPGPPGPKGDRGGPGIPGFKGEP 612
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGP--PGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 591-636 7.88e-05

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


:

Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.94  E-value: 7.88e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 767945419  591 PGPPGPKGDRGGPGIPGFKGEPGLsiRGPKGVQGPRGPVGAPGLKG 636
Cdd:pfam01391   6 PGPPGPPGPPGPPGPPGPPGPPGP--PGEPGPPGPPGPPGPPGPPG 49
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 272-582 4.41e-31

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: 126.94  E-value: 4.41e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419 272 GNAQKGEAGERGPGGIPGYKGDKGERGECGKPGIKGDKGSPGPYGPKGPRGIQgitgppgdpgpkgfqgnkgepgppgpy 351
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQ--------------------------- 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419 352 gspgapgiGQQGIKGERGQEGRPGAPGPigVGEPGQPGPRGPEGVPGERGLPGEgfPGPKGEKGSEGPTGPQGLQGLSIK 431
Cdd:NF038329 168 --------GEAGPQGPAGKDGEAGAKGP--AGEKGPQGPRGETGPAGEQGPAGP--AGPDGEAGPAGEDGPAGPAGDGQQ 235

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419 432 GEKGDIGPVGPQGPMGIPGigsqgeqgiqgpigppgpqgpagqgLPGSKGEVGQMGPTGPRGPVG-IGVQGPKGEPGSIG 510
Cdd:NF038329 236 GPDGDPGPTGEDGPQGPDG-------------------------PAGKDGPRGDRGEAGPDGPDGkDGERGPVGPAGKDG 290

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767945419 511 LPGQPGVPGEDGAAGKKGEAGLPgargpegppgkgqpgpkgdeGKKGSKGNQGQRGLPGPEGPKGEPGIMGP 582
Cdd:NF038329 291 QNGKDGLPGKDGKDGQNGKDGLP--------------------GKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 423-637 1.86e-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: 116.16  E-value: 1.86e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419 423 QGLQGLSIKGEKGDIGPVGPQGPMGIPGI-GSQGEQGIQGPIGPPGPQGPagqglPGSKGEVGQMGPTGPRGPVgiGVQG 501
Cdd:NF038329 108 EGLQQLKGDGEKGEPGPAGPAGPAGEQGPrGDRGETGPAGPAGPPGPQGE-----RGEKGPAGPQGEAGPQGPA--GKDG 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419 502 PKGEPGSIGLPGQPGVPGEDGAAGKKGEAGLPGARGPEGPPGKGQPGPKGDEGKKGSKGNQGQRGLPGPEGPKGEPGIMG 581
Cdd:NF038329 181 EAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDG 260

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767945419 582 PFGMPG-TSIPGPPGPKGDRGGPGIPGFKGEPGLsiRGPKGVQGPRGPVGAPGLKGD 637
Cdd:NF038329 261 PRGDRGeAGPDGPDGKDGERGPVGPAGKDGQNGK--DGLPGKDGKDGQNGKDGLPGK 315
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 47-209 3.59e-27

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: 108.15  E-value: 3.59e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419  47 IDIVFIVDSSESSKIALFDKQKDFVDSLSDKIfqltpgRSLEYDIKLAALQFSSSVQIDPPFSSWKDLQTFKQKVKSMNL 126
Cdd:cd01450    1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKL------DIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKY 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419 127 I-GQGTFSYYAISNATRLL--KREGRKDGVKVVLLMTDGIDHpKNPDVQSISEDARISGISFITIALSTvVNEAKLRLIS 203
Cdd:cd01450   75 LgGGGTNTGKALQYALEQLfsESNARENVPKVIIVLTDGRSD-DGGDPKEAAAKLKDEGIKVFVVGVGP-ADEEELREIA 152


                 ....*.
gi 767945419 204 GDSSSE 209
Cdd:cd01450  153 SCPSER 158
VWA pfam00092
von Willebrand factor type A domain;
48-226 6.05e-25

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 101.97  E-value: 6.05e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419   48 DIVFIVDSSESSKIALFDKQKDFVDSLSDkifQLTPGrslEYDIKLAALQFSSSVQIDPPFSSWKDLQTFKQKVKSMNLI 127
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVE---SLDIG---PDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419  128 GQGTFSY-YAISNATRLL---KREGRKDGVKVVLLMTDGidHPKNPDVQSISEDARISGISFITIALSTVVNEAkLRLIS 203
Cdd:pfam00092  75 GGGTTNTgKALKYALENLfssAAGARPGAPKVVVLLTDG--RSQDGDPEEVARELKSAGVTVFAVGVGNADDEE-LRKIA 151

                         170       180
                  ....*....|....*....|...
gi 767945419  204 GDSSSEPTLLLSDPTLVDKIQDR 226
Cdd:pfam00092 152 SEPGEGHVFTVSDFEALEDLQDQ 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 48-227 4.74e-23

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: 96.75  E-value: 4.74e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419    48 DIVFIVDSSESSKIALFDKQKDFVDSLsdkifqLTPGRSLEYDIKLAALQFSSSVQIDPPFSSWKDLQTFKQKVKSMNLI 127
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKL------VEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYK 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419   128 -GQGTFSYYAISNATRLLKRE---GRKDGVKVVLLMTDGIDHPKNPDVQSISEDARISGISFITIALSTVVNEAKLRLIS 203
Cdd:smart00327  75 lGGGTNLGAALQYALENLFSKsagSRRGAPKVVILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVGNDVDEEELKKLA 154

                          170       180
                   ....*....|....*....|....
gi 767945419   204 GDSSSEPTLLlsdPTLVDKIQDRL 227
Cdd:smart00327 155 SAPGGVYVFL---PELLDLLIDLL 175
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 257-533 8.73e-23

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: 101.91  E-value: 8.73e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419 257 GNPGIKGERGPKGNPGNAQK-GEAGERGPGGIPGYKGDKGERGECGKPGIKGDKGSPGPYGPKGPRGIQGITGPPGDPGP 335
Cdd:NF038329 120 GEPGPAGPAGPAGEQGPRGDrGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGE 199

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419 336 KGFQGNKGEPGPPGPYgspgapgigqqgikGERGQEGRPGAPGPIGVGEPGQPGPRGPEGVPGERGLPGEgfPGPKGEKG 415
Cdd:NF038329 200 TGPAGEQGPAGPAGPD--------------GEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGP--AGKDGPRG 263

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419 416 SEGPTGPQGLqglsiKGEKGDIGPVGPQGPmgipgigsqgeqgiqgpigppgpqgpagqglPGSKGEVGQMGPTGPRGPv 495
Cdd:NF038329 264 DRGEAGPDGP-----DGKDGERGPVGPAGK-------------------------------DGQNGKDGLPGKDGKDGQ- 306

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 767945419 496 gigvQGPKGEPGSIGLPGQPGVPGEDGAAGKKGEAGLP 533
Cdd:NF038329 307 ----NGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 257-445 3.22e-13

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 72.25  E-value: 3.22e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419 257 GNPGIKGERGPKGNPGNAQKGEAGERGPGGIPGYKGDKGERGECGKPGIKGDKGSPGPYGPKGPRGIQGITGPPGDPGPK 336
Cdd:NF038329 210 GPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKD 289

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419 337 GFQGNKgepgppgpygspgapgiGQQGIKGERGQEGRPGAPGPigVGEPGQPGPRGPEGVPGERGLPGEgfPGPKGEKGS 416
Cdd:NF038329 290 GQNGKD-----------------GLPGKDGKDGQNGKDGLPGK--DGKDGQPGKDGLPGKDGKDGQPGK--PAPKTPEVP 348

                        170       180       190
                 ....*....|....*....|....*....|
gi 767945419 417 EGP-TGPQGLQGLSIKGEKGDIGPvGPQGP 445
Cdd:NF038329 349 QKPdTAPHTPKTPQIPGQSKDVTP-APQNP 377
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 47-203 1.11e-12

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: 68.81  E-value: 1.11e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419  47 IDIVFIVDSSES----SKIalfDKQKDFVDSLSDkifQLTPGRsleydiKLAALQFSSSVQIDPPFSSwkDLQTFKQKVK 122
Cdd:COG1240   93 RDVVLVVDASGSmaaeNRL---EAAKGALLDFLD---DYRPRD------RVGLVAFGGEAEVLLPLTR--DREALKRALD 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419 123 SMNlIGQGTFSYYAISNATRLLKREgRKDGVKVVLLMTDGIDHPKNPDVQSISEDARISGISFITIALST-VVNEAKLRL 201
Cdd:COG1240  159 ELP-PGGGTPLGDALALALELLKRA-DPARRKVIVLLTDGRDNAGRIDPLEAAELAAAAGIRIYTIGVGTeAVDEGLLRE 236


                 ..
gi 767945419 202 IS 203
Cdd:COG1240  237 IA 238
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
257-510 2.28e-06

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 50.80  E-value: 2.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419 257 GNPGIKGERGPKGNPG-NAQKGEAGERGPGGIPGYKGDKGERGECGKPGIKGDKGSPGPYGPKGPRGIQGITGPPGDPGP 335
Cdd:COG5164   19 TPAGSQGSTKPAQNQGsTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGGTRPAGNTGG 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419 336 KGFQGNKGEPGPPGPYGSPGAPGIGQQGIKGERGQEGRPGAPG--PIGVGEPGQPGPRGPEGVPGERGLPGEGfpGPKGE 413
Cdd:COG5164   99 TTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGstPPGPGSTGPGGSTTPPGDGGSTTPPGPG--GSTTP 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419 414 KGSEGPTGPQGLQGLSIKGEKGDIGPVGPQGPMGIPGIGSQGEQGIQGPIGPPGPQGPAGQGLPGSKGEVGQMGPTGPRG 493
Cdd:COG5164  177 PDDGGSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTGPKDQRPKTNPIERRGPERPEAAALPAE 256

                        250
                 ....*....|....*..
gi 767945419 494 PVGIGVQGPKGEPGSIG 510
Cdd:COG5164  257 LTALEAENRAANPEPAT 273
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 360-419 1.04e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 43.25  E-value: 1.04e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419  360 GQQGIKGERGQEGRPGAPGPIgvGEPGQPGPRGPEGVPGERGLPgeGFPGPKGEKGSEGP 419
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPP--GPPGPPGPPGEPGPPGPPGPP--GPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 554-612 1.72e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.87  E-value: 1.72e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767945419  554 GKKGSKGNQGQRGLPGPEGPKGEPGIMGPFGMPGTsiPGPPGPKGDRGGPGIPGFKGEP 612
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGP--PGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 591-636 7.88e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.94  E-value: 7.88e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 767945419  591 PGPPGPKGDRGGPGIPGFKGEPGLsiRGPKGVQGPRGPVGAPGLKG 636
Cdd:pfam01391   6 PGPPGPPGPPGPPGPPGPPGPPGP--PGEPGPPGPPGPPGPPGPPG 49
PHA03169 PHA03169
hypothetical protein; Provisional
 256-420 4.72e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 39.95  E-value: 4.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419 256 HGNPGIKGERGPKGN-------PGNAQKGEAGERGPGGIPGYKGDKGERGECGKPGIKGDKGSPGPYGPKGPRGIQGitg 328
Cdd:PHA03169  81 HGEKEERGQGGPSGSgsesvgsPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNP--- 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419 329 PPGDPGPKGFQGNKGEPGPPGPYGSPGAPGIGQQGIKGERGQEGRPGAPGPIGVGEPGQPGPRGPEGVPGERGLPGEGFP 408
Cdd:PHA03169 158 SPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQAPSPNTQQAVEHEDEP 237

                        170
                 ....*....|..
gi 767945419 409 GPKGEKGSEGPT 420
Cdd:PHA03169 238 TEPEREGPPFPG 249
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 272-582 4.41e-31

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: 126.94  E-value: 4.41e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419 272 GNAQKGEAGERGPGGIPGYKGDKGERGECGKPGIKGDKGSPGPYGPKGPRGIQgitgppgdpgpkgfqgnkgepgppgpy 351
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQ--------------------------- 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419 352 gspgapgiGQQGIKGERGQEGRPGAPGPigVGEPGQPGPRGPEGVPGERGLPGEgfPGPKGEKGSEGPTGPQGLQGLSIK 431
Cdd:NF038329 168 --------GEAGPQGPAGKDGEAGAKGP--AGEKGPQGPRGETGPAGEQGPAGP--AGPDGEAGPAGEDGPAGPAGDGQQ 235

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419 432 GEKGDIGPVGPQGPMGIPGigsqgeqgiqgpigppgpqgpagqgLPGSKGEVGQMGPTGPRGPVG-IGVQGPKGEPGSIG 510
Cdd:NF038329 236 GPDGDPGPTGEDGPQGPDG-------------------------PAGKDGPRGDRGEAGPDGPDGkDGERGPVGPAGKDG 290

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767945419 511 LPGQPGVPGEDGAAGKKGEAGLPgargpegppgkgqpgpkgdeGKKGSKGNQGQRGLPGPEGPKGEPGIMGP 582
Cdd:NF038329 291 QNGKDGLPGKDGKDGQNGKDGLP--------------------GKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 423-637 1.86e-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: 116.16  E-value: 1.86e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419 423 QGLQGLSIKGEKGDIGPVGPQGPMGIPGI-GSQGEQGIQGPIGPPGPQGPagqglPGSKGEVGQMGPTGPRGPVgiGVQG 501
Cdd:NF038329 108 EGLQQLKGDGEKGEPGPAGPAGPAGEQGPrGDRGETGPAGPAGPPGPQGE-----RGEKGPAGPQGEAGPQGPA--GKDG 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419 502 PKGEPGSIGLPGQPGVPGEDGAAGKKGEAGLPGARGPEGPPGKGQPGPKGDEGKKGSKGNQGQRGLPGPEGPKGEPGIMG 581
Cdd:NF038329 181 EAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDG 260

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767945419 582 PFGMPG-TSIPGPPGPKGDRGGPGIPGFKGEPGLsiRGPKGVQGPRGPVGAPGLKGD 637
Cdd:NF038329 261 PRGDRGeAGPDGPDGKDGERGPVGPAGKDGQNGK--DGLPGKDGKDGQNGKDGLPGK 315
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 47-209 3.59e-27

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: 108.15  E-value: 3.59e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419  47 IDIVFIVDSSESSKIALFDKQKDFVDSLSDKIfqltpgRSLEYDIKLAALQFSSSVQIDPPFSSWKDLQTFKQKVKSMNL 126
Cdd:cd01450    1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKL------DIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKY 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419 127 I-GQGTFSYYAISNATRLL--KREGRKDGVKVVLLMTDGIDHpKNPDVQSISEDARISGISFITIALSTvVNEAKLRLIS 203
Cdd:cd01450   75 LgGGGTNTGKALQYALEQLfsESNARENVPKVIIVLTDGRSD-DGGDPKEAAAKLKDEGIKVFVVGVGP-ADEEELREIA 152


                 ....*.
gi 767945419 204 GDSSSE 209
Cdd:cd01450  153 SCPSER 158
VWA pfam00092
von Willebrand factor type A domain;
48-226 6.05e-25

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 101.97  E-value: 6.05e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419   48 DIVFIVDSSESSKIALFDKQKDFVDSLSDkifQLTPGrslEYDIKLAALQFSSSVQIDPPFSSWKDLQTFKQKVKSMNLI 127
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVE---SLDIG---PDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419  128 GQGTFSY-YAISNATRLL---KREGRKDGVKVVLLMTDGidHPKNPDVQSISEDARISGISFITIALSTVVNEAkLRLIS 203
Cdd:pfam00092  75 GGGTTNTgKALKYALENLfssAAGARPGAPKVVVLLTDG--RSQDGDPEEVARELKSAGVTVFAVGVGNADDEE-LRKIA 151

                         170       180
                  ....*....|....*....|...
gi 767945419  204 GDSSSEPTLLLSDPTLVDKIQDR 226
Cdd:pfam00092 152 SEPGEGHVFTVSDFEALEDLQDQ 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 48-227 4.74e-23

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: 96.75  E-value: 4.74e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419    48 DIVFIVDSSESSKIALFDKQKDFVDSLsdkifqLTPGRSLEYDIKLAALQFSSSVQIDPPFSSWKDLQTFKQKVKSMNLI 127
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKL------VEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYK 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419   128 -GQGTFSYYAISNATRLLKRE---GRKDGVKVVLLMTDGIDHPKNPDVQSISEDARISGISFITIALSTVVNEAKLRLIS 203
Cdd:smart00327  75 lGGGTNLGAALQYALENLFSKsagSRRGAPKVVILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVGNDVDEEELKKLA 154

                          170       180
                   ....*....|....*....|....
gi 767945419   204 GDSSSEPTLLlsdPTLVDKIQDRL 227
Cdd:smart00327 155 SAPGGVYVFL---PELLDLLIDLL 175
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 257-533 8.73e-23

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: 101.91  E-value: 8.73e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419 257 GNPGIKGERGPKGNPGNAQK-GEAGERGPGGIPGYKGDKGERGECGKPGIKGDKGSPGPYGPKGPRGIQGITGPPGDPGP 335
Cdd:NF038329 120 GEPGPAGPAGPAGEQGPRGDrGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGE 199

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419 336 KGFQGNKGEPGPPGPYgspgapgigqqgikGERGQEGRPGAPGPIGVGEPGQPGPRGPEGVPGERGLPGEgfPGPKGEKG 415
Cdd:NF038329 200 TGPAGEQGPAGPAGPD--------------GEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGP--AGKDGPRG 263

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419 416 SEGPTGPQGLqglsiKGEKGDIGPVGPQGPmgipgigsqgeqgiqgpigppgpqgpagqglPGSKGEVGQMGPTGPRGPv 495
Cdd:NF038329 264 DRGEAGPDGP-----DGKDGERGPVGPAGK-------------------------------DGQNGKDGLPGKDGKDGQ- 306

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 767945419 496 gigvQGPKGEPGSIGLPGQPGVPGEDGAAGKKGEAGLP 533
Cdd:NF038329 307 ----NGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 47-208 1.12e-22

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: 95.33  E-value: 1.12e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419  47 IDIVFIVDSSESSKIALFDKQKDFVDSLSDKIfqltpgRSLEYDIKLAALQFSSSVQIDPPFSSWKDLQTFKQKVKSMNL 126
Cdd:cd00198    1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSL------SASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKK 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419 127 IGQGTFSYY-AISNATRLLKREGRKDGVKVVLLMTDGIDHPKNPDVQSISEDARISGISFITIALSTVVNEAKLRLISGD 205
Cdd:cd00198   75 GLGGGTNIGaALRLALELLKSAKRPNARRVIILLTDGEPNDGPELLAEAARELRKLGITVYTIGIGDDANEDELKEIADK 154


                 ...
gi 767945419 206 SSS 208
Cdd:cd00198  155 TTG 157
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 45-208 2.88e-19

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: 86.29  E-value: 2.88e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419  45 CFIDIVFIVDSSESSKIALFDKQKDFVDSLSDKI--FQLTPGRSLeyDIKLAALQFSSSVQIDPPF-SSWKDLQTFKQKV 121
Cdd:cd01480    1 GPVDITFVLDSSESVGLQNFDITKNFVKRVAERFlkDYYRKDPAG--SWRVGVVQYSDQQEVEAGFlRDIRNYTSLKEAV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419 122 KSMNLIGQGTFSYYAISNATRLLKREGRKDGVKVVLLMTDGiDHPKNPD--VQSISEDARISGISFITIALSTVVNEaKL 199
Cdd:cd01480   79 DNLEYIGGGTFTDCALKYATEQLLEGSHQKENKFLLVITDG-HSDGSPDggIEKAVNEADHLGIKIFFVAVGSQNEE-PL 156


                 ....*....
gi 767945419 200 RLISGDSSS 208
Cdd:cd01480  157 SRIACDGKS 165
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 47-209 1.21e-16

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: 78.04  E-value: 1.21e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419  47 IDIVFIVDSSESSKIALFDKQKDFVDSLSDkifQLTPGRSleyDIKLAALQFSSSVQIDPPFSSWKDLQTFKQKVKSMNL 126
Cdd:cd01472    1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVE---RLDIGPD---GVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRY 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419 127 IGQGTFSYYAISNATRLL--KREGRKDGV-KVVLLMTDGidhpKNPDvqSISEDA---RISGISFITIALSTVVNEaKLR 200
Cdd:cd01472   75 IGGGTNTGKALKYVRENLftEASGSREGVpKVLVVITDG----KSQD--DVEEPAvelKQAGIEVFAVGVKNADEE-ELK 147


                 ....*....
gi 767945419 201 LISGDSSSE 209
Cdd:cd01472  148 QIASDPKEL 156
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 48-205 6.00e-14

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: 70.12  E-value: 6.00e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419  48 DIVFIVDSSESSKiALFDKQKDFVDSLSDKIfQLTPgrslEYDiKLAALQFSSSVQ--IDPPFSSWKDLQTFKQKVKSMN 125
Cdd:cd01476    2 DLLFVLDSSGSVR-GKFEKYKKYIERIVEGL-EIGP----TAT-RVALITYSGRGRqrVRFNLPKHNDGEELLEKVDNLR 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419 126 LIGQGTFSYYAISNATRLLKR-EGRKDGV-KVVLLMTDGIDHpknPDVQSISEDARiSGISFITIALST----VVNEAKL 199
Cdd:cd01476   75 FIGGTTATGAAIEVALQQLDPsEGRREGIpKVVVVLTDGRSH---DDPEKQARILR-AVPNIETFAVGTgdpgTVDTEEL 150


                 ....*.
gi 767945419 200 RLISGD 205
Cdd:cd01476  151 HSITGN 156
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 257-445 3.22e-13

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 72.25  E-value: 3.22e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419 257 GNPGIKGERGPKGNPGNAQKGEAGERGPGGIPGYKGDKGERGECGKPGIKGDKGSPGPYGPKGPRGIQGITGPPGDPGPK 336
Cdd:NF038329 210 GPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKD 289

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419 337 GFQGNKgepgppgpygspgapgiGQQGIKGERGQEGRPGAPGPigVGEPGQPGPRGPEGVPGERGLPGEgfPGPKGEKGS 416
Cdd:NF038329 290 GQNGKD-----------------GLPGKDGKDGQNGKDGLPGK--DGKDGQPGKDGLPGKDGKDGQPGK--PAPKTPEVP 348

                        170       180       190
                 ....*....|....*....|....*....|
gi 767945419 417 EGP-TGPQGLQGLSIKGEKGDIGPvGPQGP 445
Cdd:NF038329 349 QKPdTAPHTPKTPQIPGQSKDVTP-APQNP 377
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 47-203 1.11e-12

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: 68.81  E-value: 1.11e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419  47 IDIVFIVDSSES----SKIalfDKQKDFVDSLSDkifQLTPGRsleydiKLAALQFSSSVQIDPPFSSwkDLQTFKQKVK 122
Cdd:COG1240   93 RDVVLVVDASGSmaaeNRL---EAAKGALLDFLD---DYRPRD------RVGLVAFGGEAEVLLPLTR--DREALKRALD 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419 123 SMNlIGQGTFSYYAISNATRLLKREgRKDGVKVVLLMTDGIDHPKNPDVQSISEDARISGISFITIALST-VVNEAKLRL 201
Cdd:COG1240  159 ELP-PGGGTPLGDALALALELLKRA-DPARRKVIVLLTDGRDNAGRIDPLEAAELAAAAGIRIYTIGVGTeAVDEGLLRE 236


                 ..
gi 767945419 202 IS 203
Cdd:COG1240  237 IA 238
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 47-243 1.40e-12

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: 67.80  E-value: 1.40e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419  47 IDIVFIVDSSESSKIALFDKQKDFVDSLSDKIfqltpgrsleyDIKLAA-----LQFSSSVQIDPPFSSWKDLQTFKQKV 121
Cdd:cd01475    3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSL-----------DVGPDAtrvglVQYSSTVKQEFPLGRFKSKADLKRAV 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419 122 KSMNLIGQGTFSYYAISNATRLL------KREGRKDGVKVVLLMTDGidHPKNpDVQSISEDARISGISFITIALSTVVn 195
Cdd:cd01475   72 RRMEYLETGTMTGLAIQYAMNNAfseaegARPGSERVPRVGIVVTDG--RPQD-DVSEVAAKARALGIEMFAVGVGRAD- 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 767945419 196 EAKLRLISGDSSSEPTLLLSDPTLVDKIQDRLDilfEKKCE-RKICECE 243
Cdd:cd01475  148 EEELREIASEPLADHVFYVEDFSTIEELTKKFQ---GKICVvPDLCATL 193
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 47-216 5.40e-10

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: 58.91  E-value: 5.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419  47 IDIVFIVDSSESSKIALFDKQKDFVDSLSDKiFQLTPGrsleyDIKLAALQFSSSVQIDPPFSSWKDLQTFKQKVKSMNL 126
Cdd:cd01469    1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKK-LDIGPT-----KTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQ 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419 127 IGQGTFSYYAISNATRLLKRE---GRKDGVKVVLLMTDGIDH--PKNPDVQSISEDARIsgISFItIAL------STVVN 195
Cdd:cd01469   75 LLGLTNTATAIQYVVTELFSEsngARKDATKVLVVITDGESHddPLLKDVIPQAEREGI--IRYA-IGVgghfqrENSRE 151

                        170       180
                 ....*....|....*....|.
gi 767945419 196 EakLRLISGDSSSEPTLLLSD 216
Cdd:cd01469  152 E--LKTIASKPPEEHFFNVTD 170
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 47-209 7.88e-09

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: 55.85  E-value: 7.88e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419  47 IDIVFIVDSSESSKIA-LFDKQKDFVDSLSDKIfQLTPGrsleyDIKLAALQFSSSV--QID--PPFSSWKDLQTFK-QK 120
Cdd:cd01471    1 LDLYLLVDGSGSIGYSnWVTHVVPFLHTFVQNL-NISPD-----EINLYLVTFSTNAkeLIRlsSPNSTNKDLALNAiRA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419 121 VKSMNLIGQGTFSYYAISNATRLLK--REGRKDGVKVVLLMTDGIdhpKNPDVQSISEDARIS--GISFITIALSTVVNE 196
Cdd:cd01471   75 LLSLYYPNGSTNTTSALLVVEKHLFdtRGNRENAPQLVIIMTDGI---PDSKFRTLKEARKLRerGVIIAVLGVGQGVNH 151

                        170
                 ....*....|...
gi 767945419 197 AKLRLISGDSSSE 209
Cdd:cd01471  152 EENRSLVGCDPDD 164
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 48-203 5.01e-08

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 54.69  E-value: 5.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419  48 DIVFIVDSSES---SKIAlfdkqkdFVDSLSDKIFQ-LTPGRsleydiKLAALQFSSSVQIDPPFSSWKDLQTFKQKVKS 123
Cdd:COG2425  120 PVVLCVDTSGSmagSKEA-------AAKAAALALLRaLRPNR------RFGVILFDTEVVEDLPLTADDGLEDAIEFLSG 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419 124 MNLIGqGTFSYYAISNATRLLKREGRKDgvKVVLLMTDGIDHpkNPDVQSISE-DARISGISFITIALSTVVNEAKLRLI 202
Cdd:COG2425  187 LFAGG-GTDIAPALRAALELLEEPDYRN--ADIVLITDGEAG--VSPEELLREvRAKESGVRLFTVAIGDAGNPGLLEAL 261


                 .
gi 767945419 203 S 203
Cdd:COG2425  262 A 262
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 48-208 1.84e-06

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: 48.44  E-value: 1.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419  48 DIVFIVDSSESSKIALFDKQKDFVDSLSdKIFQLTPGRsleydIKLAALQFSSSVQIDPPFSSWKDLQTFKQKVKSMNLI 127
Cdd:cd01482    2 DIVFLVDGSWSIGRSNFNLVRSFLSSVV-EAFEIGPDG-----VQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYK 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419 128 GQGTFSYYAISNA--TRLLKREG-RKDGVKVVLLMTDGidhPKNPDVQSISEDARISGISFITIALSTVVnEAKLRLISG 204
Cdd:cd01482   76 GGNTRTGKALTHVreKNFTPDAGaRPGVPKVVILITDG---KSQDDVELPARVLRNLGVNVFAVGVKDAD-ESELKMIAS 151


                 ....
gi 767945419 205 DSSS 208
Cdd:cd01482  152 KPSE 155
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
257-510 2.28e-06

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 50.80  E-value: 2.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419 257 GNPGIKGERGPKGNPG-NAQKGEAGERGPGGIPGYKGDKGERGECGKPGIKGDKGSPGPYGPKGPRGIQGITGPPGDPGP 335
Cdd:COG5164   19 TPAGSQGSTKPAQNQGsTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGGTRPAGNTGG 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419 336 KGFQGNKGEPGPPGPYGSPGAPGIGQQGIKGERGQEGRPGAPG--PIGVGEPGQPGPRGPEGVPGERGLPGEGfpGPKGE 413
Cdd:COG5164   99 TTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGstPPGPGSTGPGGSTTPPGDGGSTTPPGPG--GSTTP 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419 414 KGSEGPTGPQGLQGLSIKGEKGDIGPVGPQGPMGIPGIGSQGEQGIQGPIGPPGPQGPAGQGLPGSKGEVGQMGPTGPRG 493
Cdd:COG5164  177 PDDGGSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTGPKDQRPKTNPIERRGPERPEAAALPAE 256

                        250
                 ....*....|....*..
gi 767945419 494 PVGIGVQGPKGEPGSIG 510
Cdd:COG5164  257 LTALEAENRAANPEPAT 273
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 360-419 1.04e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 43.25  E-value: 1.04e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419  360 GQQGIKGERGQEGRPGAPGPIgvGEPGQPGPRGPEGVPGERGLPgeGFPGPKGEKGSEGP 419
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPP--GPPGPPGPPGEPGPPGPPGPP--GPPGPPGAPGAPGP 56
VWA_2 pfam13519
von Willebrand factor type A domain;
49-158 1.13e-05

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 44.59  E-value: 1.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419   49 IVFIVDSSES-----SKIALFDKQKDFVDSLsdkiFQLTPGRsleydiKLAALQFSSSVQIDPPFSswKDLQTFKQKVKS 123
Cdd:pfam13519   1 LVFVLDTSGSmrngdYGPTRLEAAKDAVLAL----LKSLPGD------RVGLVTFGDGPEVLIPLT--KDRAKILRALRR 68

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 767945419  124 MNLIGQGTFSYYAISNATRLLKREGRKDGVKVVLL 158
Cdd:pfam13519  69 LEPKGGGTNLAAALQLARAALKHRRKNQPRRIVLI 103
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 554-612 1.72e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.87  E-value: 1.72e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767945419  554 GKKGSKGNQGQRGLPGPEGPKGEPGIMGPFGMPGTsiPGPPGPKGDRGGPGIPGFKGEP 612
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGP--PGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 369-422 2.13e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.48  E-value: 2.13e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767945419  369 GQEGRPGAPGPIG-VGEPGQPGPRGPEGVPGERGLPGE-GFPGPKGEKGSEGPTGP 422
Cdd:pfam01391   1 GPPGPPGPPGPPGpPGPPGPPGPPGPPGPPGEPGPPGPpGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 481-536 2.33e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.48  E-value: 2.33e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767945419  481 GEVGQMGPTGPRGPVGI-GVQGPKGEPGSIGLPGQPGVPGEDGAAGKKGEAGLPGAR 536
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPpGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 591-636 7.88e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.94  E-value: 7.88e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 767945419  591 PGPPGPKGDRGGPGIPGFKGEPGLsiRGPKGVQGPRGPVGAPGLKG 636
Cdd:pfam01391   6 PGPPGPPGPPGPPGPPGPPGPPGP--PGEPGPPGPPGPPGPPGPPG 49
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 48-204 8.74e-05

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


Pssm-ID: 238750 [Multi-domain]  Cd Length: 192  Bit Score: 43.85  E-value: 8.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419  48 DIVFIVDssESSKIALFDKQKDFVDSLSDKIFQLTPGrslEYDIKLAALQFSSSVQIDPPFS---SWKDLQTFKQKVKSM 124
Cdd:cd01473    2 DLTLILD--ESASIGYSNWRKDVIPFTEKIINNLNIS---KDKVHVGILLFAEKNRDVVPFSdeeRYDKNELLKKINDLK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419 125 NLIGQGTFSY------YAISNATRLLKRegRKDGVKVVLLMTDGID-HPKNPDVQSISEDARISGISFITIALSTvVNEA 197
Cdd:cd01473   77 NSYRSGGETYivealkYGLKNYTKHGNR--RKDAPKVTMLFTDGNDtSASKKELQDISLLYKEENVKLLVVGVGA-ASEN 153


                 ....*..
gi 767945419 198 KLRLISG 204
Cdd:cd01473  154 KLKLLAG 160
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 383-442 2.01e-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: 2.01e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419  383 GEPGQPGPRGPEGVPGERGLPGEgfPGPKGEKGSEGPTGPQGLqglsiKGEKGDIGPVGP 442
Cdd:pfam01391   4 GPPGPPGPPGPPGPPGPPGPPGP--PGPPGEPGPPGPPGPPGP-----PGPPGAPGAPGP 56
VWA_3 pfam13768
von Willebrand factor type A domain;
47-203 3.61e-04

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 41.61  E-value: 3.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419   47 IDIVFIVDSSESSKialfDKQKDFVDSLSDKIFQLTPGrsleydIKLAALQFSSSVQidPPFSSWK-----DLQTFKQKV 121
Cdd:pfam13768   1 GDVVIVVDVSSSMS----GEPKLQKDALSVALRQLPTG------DKFAVLGFGTLPR--PLFPGWRvvsprSLQEAFQFI 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419  122 KSMNLIGQGTFSYYAISNATRLLKREGRkdgVKVVLLMTDGIDHPKNPDVQSISEDARiSGISFITIALSTVVNEAKLRL 201
Cdd:pfam13768  69 KTLQPPLGGSDLLGALKEAVRAPASPGY---IRHVLLLTDGSPMQGETRVSDLISRAP-GKIRFFAYGLGASISAPMLQL 144


                  ..
gi 767945419  202 IS 203
Cdd:pfam13768 145 LA 146
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 566-632 3.88e-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: 3.88e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767945419  566 GLPGPEGPKGEPGIMGPfgmpgtsiPGPPGPKGDRGGPGIPGFKGEPGLSirGPKGVQGPRGPVGAP 632
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGP--------PGPPGPPGPPGPPGEPGPPGPPGPP--GPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 277-325 5.53e-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: 5.53e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 767945419  277 GEAGERGPGGIPGYKGDKGERGECGKPGIKGDKGSPGPYGPKGPRGIQG 325
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPG 49
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 263-321 7.88e-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: 37.86  E-value: 7.88e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767945419  263 GERGPKGNPGnaQKGEAGERGPGGIPGYKGDKGERGECGKPGIKGDKGSPGPYGPKGPR 321
Cdd:pfam01391   1 GPPGPPGPPG--PPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
478-638 8.30e-04

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 42.71  E-value: 8.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419 478 GSKGEVGQMGPTGPRGPVG-------IGVQGPKGEPGSIGLPGQPGVPGEDGAAGKKGEAGLPGARgpEGPPGKGQPGPK 550
Cdd:COG5164   16 GVTTPAGSQGSTKPAQNQGstrpagnTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGT--TPAQNQGGTRPA 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419 551 GDEGKKGSKGNQGQRGLPGPEGPKGEPGIMGPFGMPGTSIPGPPGPKGDR-GGPGIPGFKGepGLSIRGPKGVQGPRGPV 629
Cdd:COG5164   94 GNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTpPGPGSTGPGG--STTPPGDGGSTTPPGPG 171


                 ....*....
gi 767945419 630 GAPGLKGDG 638
Cdd:COG5164  172 GSTTPPDDG 180
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 48-128 1.92e-03

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: 39.61  E-value: 1.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419  48 DIVFIVDSSESSKIALFDKQKDFVDSLsdkIFQLTPGRSLeydIKLAALQFSSSVQIDPPFSSWKDLQTFKQKVKSMNLI 127
Cdd:cd01481    2 DIVFLIDGSDNVGSGNFPAIRDFIERI---VQSLDVGPDK---IRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLR 75


                 .
gi 767945419 128 G 128
Cdd:cd01481   76 G 76
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 487-538 2.72e-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: 2.72e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767945419  487 GPTGPRGPVGIgvQGPKGEPGSIGLPGQPGVPGEDGAAGKKGEAGLPGARGP 538
Cdd:pfam01391   1 GPPGPPGPPGP--PGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGA 50
PHA03169 PHA03169
hypothetical protein; Provisional
 256-420 4.72e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 39.95  E-value: 4.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419 256 HGNPGIKGERGPKGN-------PGNAQKGEAGERGPGGIPGYKGDKGERGECGKPGIKGDKGSPGPYGPKGPRGIQGitg 328
Cdd:PHA03169  81 HGEKEERGQGGPSGSgsesvgsPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNP--- 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945419 329 PPGDPGPKGFQGNKGEPGPPGPYGSPGAPGIGQQGIKGERGQEGRPGAPGPIGVGEPGQPGPRGPEGVPGERGLPGEGFP 408
Cdd:PHA03169 158 SPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQAPSPNTQQAVEHEDEP 237

                        170
                 ....*....|..
gi 767945419 409 GPKGEKGSEGPT 420
Cdd:PHA03169 238 TEPEREGPPFPG 249
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 280-330 7.60e-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: 35.16  E-value: 7.60e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767945419  280 GERGPGGIPGYKGDKGERGECGKPGIKGDKGSPGPYGPKGPRGIQGITGPP 330
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAP 51
 
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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