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Conserved domains on  [gi|2065167|emb|CAA72402|]
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collagen type XIV, partial [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
6-170 1.81e-92

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: 285.72  E-value: 1.81e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065167    6 ADLVFMVDGSWSIGDENFNKIISFLYSTVGALNkIGTDGTQVAMVQFTDDPRTEFKLNAYKTKETLLDAIKHISYKGGNT 85
Cdd:cd01482   1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFE-IGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNT 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065167   86 KTGKAIKYVRDTLFTAESGTRRGIPKVIVVITDGRSQDDVNKISREMQLDGYSIFAIGVADADYSELVSIGSKPSARHVF 165
Cdd:cd01482  80 RTGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHVF 159

                ....*
gi 2065167  166 FVDDF 170
Cdd:cd01482 160 NVADF 164
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
204-399 3.45e-54

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


:

Pssm-ID: 214560  Cd Length: 184  Bit Score: 184.87  E-value: 3.45e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065167     204 GFKMMEMFGLVEKDFSSVEGVSMEPGtfnvFPCYQLHKDALVSQPTRYLHPEGLPSDYTISFLFRIlpdTPQEPFALWEI 283
Cdd:smart00210   1 GQDLLQVFDLPSLSFAIRQVVGPEPG----SPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQ---TPKSRGVLFAI 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065167     284 LNKNSDPLVGVILDNGGKTLTYFNYDQSGDFQTVTFEGpeiRKIFYGSFHKLHIVVSETLVKVVIDCKQVGEKAMNASA- 362
Cdd:smart00210  74 YDAQNVRQFGLEVDGRANTLLLRYQGVDGKQHTVSFRN---LPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGq 150
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 2065167     363 -NITSDGVEVLGKMVRSRGPggnsAPFQLQMFDIVCST 399
Cdd:smart00210 151 pPIDTDGIEVRGAQAADRKP----FQGDLQQLKIVCDP 184
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
453-583 4.44e-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: 84.57  E-value: 4.44e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065167   453 QQGEPGPKGPDGPRGEiglpgpqgppgpqgpsglsiQGMPGMPGEKGEKGDTGLPGPQGIPGGVGSPGRDGSPGQRGLPG 532
Cdd:NF038329 118 EKGEPGPAGPAGPAGE--------------------QGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAG 177
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 2065167   533 KDGSSGPPGPPGPIGIPGTPGVPGITGSMGPQGALGPPGVPGAKGERGERG 583
Cdd:NF038329 178 KDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAG 228
 
Name Accession Description Interval E-value
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
6-170 1.81e-92

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: 285.72  E-value: 1.81e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065167    6 ADLVFMVDGSWSIGDENFNKIISFLYSTVGALNkIGTDGTQVAMVQFTDDPRTEFKLNAYKTKETLLDAIKHISYKGGNT 85
Cdd:cd01482   1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFE-IGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNT 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065167   86 KTGKAIKYVRDTLFTAESGTRRGIPKVIVVITDGRSQDDVNKISREMQLDGYSIFAIGVADADYSELVSIGSKPSARHVF 165
Cdd:cd01482  80 RTGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHVF 159

                ....*
gi 2065167  166 FVDDF 170
Cdd:cd01482 160 NVADF 164
VWA pfam00092
von Willebrand factor type A domain;
7-179 1.39e-67

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 220.61  E-value: 1.39e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065167      7 DLVFMVDGSWSIGDENFNKIISFLYSTVGALNkIGTDGTQVAMVQFTDDPRTEFKLNAYKTKETLLDAIKHISYKGGNTK 86
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLD-IGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065167     87 -TGKAIKYVRDTLFTAESGTRRGIPKVIVVITDGRSQD-DVNKISREMQLDGYSIFAIGVADADYSELVSIGSKPSARHV 164
Cdd:pfam00092  80 nTGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGHV 159
                         170
                  ....*....|....*
gi 2065167    165 FFVDDFDAFKKIEDE 179
Cdd:pfam00092 160 FTVSDFEALEDLQDQ 174
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
204-399 3.45e-54

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


Pssm-ID: 214560  Cd Length: 184  Bit Score: 184.87  E-value: 3.45e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065167     204 GFKMMEMFGLVEKDFSSVEGVSMEPGtfnvFPCYQLHKDALVSQPTRYLHPEGLPSDYTISFLFRIlpdTPQEPFALWEI 283
Cdd:smart00210   1 GQDLLQVFDLPSLSFAIRQVVGPEPG----SPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQ---TPKSRGVLFAI 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065167     284 LNKNSDPLVGVILDNGGKTLTYFNYDQSGDFQTVTFEGpeiRKIFYGSFHKLHIVVSETLVKVVIDCKQVGEKAMNASA- 362
Cdd:smart00210  74 YDAQNVRQFGLEVDGRANTLLLRYQGVDGKQHTVSFRN---LPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGq 150
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 2065167     363 -NITSDGVEVLGKMVRSRGPggnsAPFQLQMFDIVCST 399
Cdd:smart00210 151 pPIDTDGIEVRGAQAADRKP----FQGDLQQLKIVCDP 184
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
7-173 4.41e-50

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: 173.02  E-value: 4.41e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065167       7 DLVFMVDGSWSIGDENFNKIISFLYSTVGALNkIGTDGTQVAMVQFTDDPRTEFKLNAYKTKETLLDAIKHISYK-GGNT 85
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLD-IGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGT 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065167      86 KTGKAIKYVRDTLFTAESGTRRGIPKVIVVITDGRSQD---DVNKISREMQLDGYSIFAIGV-ADADYSELVSIGSKPSA 161
Cdd:smart00327  80 NLGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVgNDVDEEELKKLASAPGG 159
                          170
                   ....*....|..
gi 2065167     162 RHVFFVDDFDAF 173
Cdd:smart00327 160 VYVFLPELLDLL 171
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
453-583 4.44e-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: 84.57  E-value: 4.44e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065167   453 QQGEPGPKGPDGPRGEiglpgpqgppgpqgpsglsiQGMPGMPGEKGEKGDTGLPGPQGIPGGVGSPGRDGSPGQRGLPG 532
Cdd:NF038329 118 EKGEPGPAGPAGPAGE--------------------QGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAG 177
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 2065167   533 KDGSSGPPGPPGPIGIPGTPGVPGITGSMGPQGALGPPGVPGAKGERGERG 583
Cdd:NF038329 178 KDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAG 228
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
453-583 2.10e-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: 82.26  E-value: 2.10e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065167   453 QQGEPGPKGPDGPRGEiglpgpqgppgpqgpsglsiQGMPGMPGEKGEKGDTGLPGPQGIPGGVGSPGRDGSPGQRGLPG 532
Cdd:NF038329 166 PQGEAGPQGPAGKDGE--------------------AGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDG 225
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 2065167   533 KDGSSGPPGPPGPIGipgtpgvPGITGSMGPQGALGPPGVPGAKGERGERG 583
Cdd:NF038329 226 PAGPAGDGQQGPDGD-------PGPTGEDGPQGPDGPAGKDGPRGDRGEAG 269
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
454-584 3.37e-16

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 81.88  E-value: 3.37e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065167   454 QGEPGPKGPDGPRGEiglpgpqgppgpqgPSGLSIQGMPGMPGEKGEKGDTGLPGPQGIPGGVGSPGRDGSPGQRGLPGK 533
Cdd:NF038329 125 AGPAGPAGEQGPRGD--------------RGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGE 190
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 2065167   534 DGSSGPPGPPGPIGIPGTPGVPGITGSMGPQGALGPPGVPGaKGERGERGD 584
Cdd:NF038329 191 KGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGD 240
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
454-583 2.65e-12

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 69.55  E-value: 2.65e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065167   454 QGEPGPKGPDGPRGEI-GLPGPQGPPGPQGPSGLSIQGMPGMPGE--KGEKGDTGLPGPQGIP---GGVGSPGRDGSPGQ 527
Cdd:NF038329 185 KGPAGEKGPQGPRGETgPAGEQGPAGPAGPDGEAGPAGEDGPAGPagDGQQGPDGDPGPTGEDgpqGPDGPAGKDGPRGD 264
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 2065167   528 RGLPGKDgssgppgppgpigipgtpgvpGITGSMGPQGALGPPGVPGAKGERGERG 583
Cdd:NF038329 265 RGEAGPD---------------------GPDGKDGERGPVGPAGKDGQNGKDGLPG 299
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
455-576 1.01e-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: 67.62  E-value: 1.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065167   455 GEPGPKGPDGPRGEIGLPGPQGPPGPQGPSGLSIQGMPGMPGEKGEKGDTGLPGPQGIPGG------VGSPGRDGSPGQR 528
Cdd:NF038329 216 GEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKdgergpVGPAGKDGQNGKD 295
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 2065167   529 GLPGKDGSSGPPGPPGPIGIPGTPGVPGITGSMGPQGALGPPGVPGAK 576
Cdd:NF038329 296 GLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
6-176 1.69e-09

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: 59.18  E-value: 1.69e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065167    6 ADLVFMVDGSWSIGDEN-FNKIISFLYSTVGALNKigtdGTQVAMVQFTDDPRTEFKLNayKTKETLLDAIKHISYKGGn 84
Cdd:COG1240  93 RDVVLVVDASGSMAAENrLEAAKGALLDFLDDYRP----RDRVGLVAFGGEAEVLLPLT--RDREALKRALDELPPGGG- 165
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065167   85 TKTGKAIKYVRDTLFTAESGTRrgipKVIVVITDGR---SQDDVNKISREMQLDGYSIFAIGVADADYSE--LVSIGSKP 159
Cdd:COG1240 166 TPLGDALALALELLKRADPARR----KVIVLLTDGRdnaGRIDPLEAAELAAAAGIRIYTIGVGTEAVDEglLREIAEAT 241
                       170
                ....*....|....*..
gi 2065167  160 SARHvFFVDDFDAFKKI 176
Cdd:COG1240 242 GGRY-FRADDLSELAAI 257
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
489-532 9.97e-09

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: 51.73  E-value: 9.97e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2065167    489 QGMPGMPGEKGEKGDTGLPGPQGIPGGVGSPGRDGSPGQRGLPG 532
Cdd:pfam01391   3 PGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPG 46
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
453-533 1.64e-06

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: 51.06  E-value: 1.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065167   453 QQGEPGPKGPDGPRGEIGLPGPQGPPGPqgpsglsiQGMPGMPGEKGEKGDTGLPGPQGIPGGVGSPGRDGSPGQRGLPG 532
Cdd:NF038329 267 EAGPDGPDGKDGERGPVGPAGKDGQNGK--------DGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338

                 .
gi 2065167   533 K 533
Cdd:NF038329 339 K 339
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
5-171 4.29e-04

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 43.80  E-value: 4.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065167     5 KADLVFMVDGSWSIGDENF-NKIISFLYSTVGALNkIGTDGTQVAMVQFTDDPRTEFKL--NAYKTKETLLDAIKHISyK 81
Cdd:PTZ00441  42 EVDLYLLVDGSGSIGYHNWiTHVIPMLMGLIQQLN-LSDDAINLYMSLFSNNTTELIRLgsGASKDKEQALIIVKSLR-K 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065167    82 G----GNTKTGKAIKYVRDTLftAESGTRRGIPKVIVVITDG--RSQDDVNKISREMQLDGYSIFAIGVA---DADYSEL 152
Cdd:PTZ00441 120 TylpyGKTNMTDALLEVRKHL--NDRVNRENAIQLVILMTDGipNSKYRALEESRKLKDRNVKLAVIGIGqgiNHQFNRL 197
                        170
                 ....*....|....*....
gi 2065167   153 VsIGSKPSARHVFFVDDFD 171
Cdd:PTZ00441 198 L-AGCRPREGKCKFYSDAD 215
 
Name Accession Description Interval E-value
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
6-170 1.81e-92

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: 285.72  E-value: 1.81e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065167    6 ADLVFMVDGSWSIGDENFNKIISFLYSTVGALNkIGTDGTQVAMVQFTDDPRTEFKLNAYKTKETLLDAIKHISYKGGNT 85
Cdd:cd01482   1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFE-IGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNT 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065167   86 KTGKAIKYVRDTLFTAESGTRRGIPKVIVVITDGRSQDDVNKISREMQLDGYSIFAIGVADADYSELVSIGSKPSARHVF 165
Cdd:cd01482  80 RTGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHVF 159

                ....*
gi 2065167  166 FVDDF 170
Cdd:cd01482 160 NVADF 164
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
6-170 4.78e-77

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: 245.22  E-value: 4.78e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065167    6 ADLVFMVDGSWSIGDENFNKIISFLYSTVGALNkIGTDGTQVAMVQFTDDPRTEFKLNAYKTKETLLDAIKHISYKGGNT 85
Cdd:cd01472   1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLD-IGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGT 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065167   86 KTGKAIKYVRDTLFTAESGTRRGIPKVIVVITDGRSQDDVNKISREMQLDGYSIFAIGVADADYSELVSIGSKPSARHVF 165
Cdd:cd01472  80 NTGKALKYVRENLFTEASGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKELYVF 159

                ....*
gi 2065167  166 FVDDF 170
Cdd:cd01472 160 NVADF 164
VWA pfam00092
von Willebrand factor type A domain;
7-179 1.39e-67

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 220.61  E-value: 1.39e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065167      7 DLVFMVDGSWSIGDENFNKIISFLYSTVGALNkIGTDGTQVAMVQFTDDPRTEFKLNAYKTKETLLDAIKHISYKGGNTK 86
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLD-IGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065167     87 -TGKAIKYVRDTLFTAESGTRRGIPKVIVVITDGRSQD-DVNKISREMQLDGYSIFAIGVADADYSELVSIGSKPSARHV 164
Cdd:pfam00092  80 nTGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGHV 159
                         170
                  ....*....|....*
gi 2065167    165 FFVDDFDAFKKIEDE 179
Cdd:pfam00092 160 FTVSDFEALEDLQDQ 174
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
204-399 3.45e-54

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


Pssm-ID: 214560  Cd Length: 184  Bit Score: 184.87  E-value: 3.45e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065167     204 GFKMMEMFGLVEKDFSSVEGVSMEPGtfnvFPCYQLHKDALVSQPTRYLHPEGLPSDYTISFLFRIlpdTPQEPFALWEI 283
Cdd:smart00210   1 GQDLLQVFDLPSLSFAIRQVVGPEPG----SPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQ---TPKSRGVLFAI 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065167     284 LNKNSDPLVGVILDNGGKTLTYFNYDQSGDFQTVTFEGpeiRKIFYGSFHKLHIVVSETLVKVVIDCKQVGEKAMNASA- 362
Cdd:smart00210  74 YDAQNVRQFGLEVDGRANTLLLRYQGVDGKQHTVSFRN---LPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGq 150
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 2065167     363 -NITSDGVEVLGKMVRSRGPggnsAPFQLQMFDIVCST 399
Cdd:smart00210 151 pPIDTDGIEVRGAQAADRKP----FQGDLQQLKIVCDP 184
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
6-165 4.28e-54

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: 183.65  E-value: 4.28e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065167    6 ADLVFMVDGSWSIGDENFNKIISFLYSTVGALNkIGTDGTQVAMVQFTDDPRTEFKLNAYKTKETLLDAIKHISYKGGN- 84
Cdd:cd01450   1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLD-IGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGg 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065167   85 TKTGKAIKYVRDTLFTaESGTRRGIPKVIVVITDGRSQD--DVNKISREMQLDGYSIFAIGVADADYSELVSIGSKPSAR 162
Cdd:cd01450  80 TNTGKALQYALEQLFS-ESNARENVPKVIIVLTDGRSDDggDPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPSER 158

                ...
gi 2065167  163 HVF 165
Cdd:cd01450 159 HVF 161
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
7-173 4.41e-50

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: 173.02  E-value: 4.41e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065167       7 DLVFMVDGSWSIGDENFNKIISFLYSTVGALNkIGTDGTQVAMVQFTDDPRTEFKLNAYKTKETLLDAIKHISYK-GGNT 85
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLD-IGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGT 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065167      86 KTGKAIKYVRDTLFTAESGTRRGIPKVIVVITDGRSQD---DVNKISREMQLDGYSIFAIGV-ADADYSELVSIGSKPSA 161
Cdd:smart00327  80 NLGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVgNDVDEEELKKLASAPGG 159
                          170
                   ....*....|..
gi 2065167     162 RHVFFVDDFDAF 173
Cdd:smart00327 160 VYVFLPELLDLL 171
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
6-189 1.96e-47

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: 167.56  E-value: 1.96e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065167    6 ADLVFMVDGSWSIGDENFNKIISFLYSTVGALNkIGTDGTQVAMVQFTDDPRTEFKLNAYKTKETLLDAIKHISYKGGNT 85
Cdd:cd01475   3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLD-VGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGT 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065167   86 KTGKAIKYVRDTLFTAESGTRRG---IPKVIVVITDGRSQDDVNKISREMQLDGYSIFAIGVADADYSELVSIGSKPSAR 162
Cdd:cd01475  82 MTGLAIQYAMNNAFSEAEGARPGserVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLAD 161
                       170       180
                ....*....|....*....|....*..
gi 2065167  163 HVFFVDDFDAFKKIEDELITFVCETAS 189
Cdd:cd01475 162 HVFYVEDFSTIEELTKKFQGKICVVPD 188
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
6-170 3.93e-44

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: 156.33  E-value: 3.93e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065167    6 ADLVFMVDGSWSIGDENFNKIISFLYSTVGALNkIGTDGTQVAMVQFTDDPRTEFKLNAYKTKETLLDAIKHISYKGGN- 84
Cdd:cd01481   1 KDIVFLIDGSDNVGSGNFPAIRDFIERIVQSLD-VGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSq 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065167   85 TKTGKAIKYVRDTLFTAESGTR--RGIPKVIVVITDGRSQDDVNKISREMQLDGYSIFAIGVADADYSELVSIGSKPSar 162
Cdd:cd01481  80 LNTGSALDYVVKNLFTKSAGSRieEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPS-- 157

                ....*...
gi 2065167  163 HVFFVDDF 170
Cdd:cd01481 158 FVFQVSDF 165
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
7-176 6.65e-44

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: 155.98  E-value: 6.65e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065167    7 DLVFMVDGSWSIGDENFNKIISFLYSTVGALnKIGTDGTQVAMVQFTDDPRTEFKLNAYKTKETLLDAIKHISYKGGNTK 86
Cdd:cd01469   2 DIVFVLDGSGSIYPDDFQKVKNFLSTVMKKL-DIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065167   87 TGKAIKYVRDTLFTAESGTRRGIPKVIVVITDGRSQDD--VNKISREMQLDGYSIFAIGVADA-----DYSELVSIGSKP 159
Cdd:cd01469  81 TATAIQYVVTELFSESNGARKDATKVLVVITDGESHDDplLKDVIPQAEREGIIRYAIGVGGHfqrenSREELKTIASKP 160
                       170
                ....*....|....*..
gi 2065167  160 SARHVFFVDDFDAFKKI 176
Cdd:cd01469 161 PEEHFFNVTDFAALKDI 177
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
6-165 1.57e-28

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: 111.89  E-value: 1.57e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065167    6 ADLVFMVDGSWSIGDENFNKIISFLYSTVGALnKIGTDGTQVAMVQFTDDPRTEFKLNAYKTKETLLDAIKHISYK-GGN 84
Cdd:cd00198   1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSL-SASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGlGGG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065167   85 TKTGKAIKYVRDTLFtaeSGTRRGIPKVIVVITDGRSQDD---VNKISREMQLDGYSIFAIGV-ADADYSELVSIGSKPS 160
Cdd:cd00198  80 TNIGAALRLALELLK---SAKRPNARRVIILLTDGEPNDGpelLAEAARELRKLGITVYTIGIgDDANEDELKEIADKTT 156

                ....*
gi 2065167  161 ARHVF 165
Cdd:cd00198 157 GGAVF 161
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
6-166 4.01e-27

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: 107.87  E-value: 4.01e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065167    6 ADLVFMVDGSWSIGDEnFNKIISFLYSTVGALnKIGTDGTQVAMVQFTDDPRT--EFKLNAYKTKETLLDAIKHISYKGG 83
Cdd:cd01476   1 LDLLFVLDSSGSVRGK-FEKYKKYIERIVEGL-EIGPTATRVALITYSGRGRQrvRFNLPKHNDGEELLEKVDNLRFIGG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065167   84 NTKTGKAIKYVRDtLFTAESGTRRGIPKVIVVITDGRSQDDVNKISREMQ-LDGYSIFAIGVAD---ADYSELVSIGSKP 159
Cdd:cd01476  79 TTATGAAIEVALQ-QLDPSEGRREGIPKVVVVLTDGRSHDDPEKQARILRaVPNIETFAVGTGDpgtVDTEELHSITGNE 157

                ....*..
gi 2065167  160 saRHVFF 166
Cdd:cd01476 158 --DHIFT 162
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
7-144 2.09e-17

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: 80.89  E-value: 2.09e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065167    7 DLVFMVDGSWSIGDEN-FNKIISFLYSTVGALNkIGTDGTQVAMVQFTDDPRTEFKLNAYKT--KETLLDAIKH---ISY 80
Cdd:cd01471   2 DLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLN-ISPDEINLYLVTFSTNAKELIRLSSPNStnKDLALNAIRAllsLYY 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2065167   81 KGGNTKTGKAIKYVRDTLFTAEsGTRRGIPKVIVVITDGRSQDDVN--KISREMQLDGYSIFAIGV 144
Cdd:cd01471  81 PNGSTNTTSALLVVEKHLFDTR-GNRENAPQLVIIMTDGIPDSKFRtlKEARKLRERGVIIAVLGV 145
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
453-583 4.44e-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: 84.57  E-value: 4.44e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065167   453 QQGEPGPKGPDGPRGEiglpgpqgppgpqgpsglsiQGMPGMPGEKGEKGDTGLPGPQGIPGGVGSPGRDGSPGQRGLPG 532
Cdd:NF038329 118 EKGEPGPAGPAGPAGE--------------------QGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAG 177
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 2065167   533 KDGSSGPPGPPGPIGIPGTPGVPGITGSMGPQGALGPPGVPGAKGERGERG 583
Cdd:NF038329 178 KDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAG 228
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
453-583 2.10e-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: 82.26  E-value: 2.10e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065167   453 QQGEPGPKGPDGPRGEiglpgpqgppgpqgpsglsiQGMPGMPGEKGEKGDTGLPGPQGIPGGVGSPGRDGSPGQRGLPG 532
Cdd:NF038329 166 PQGEAGPQGPAGKDGE--------------------AGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDG 225
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 2065167   533 KDGSSGPPGPPGPIGipgtpgvPGITGSMGPQGALGPPGVPGAKGERGERG 583
Cdd:NF038329 226 PAGPAGDGQQGPDGD-------PGPTGEDGPQGPDGPAGKDGPRGDRGEAG 269
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
454-584 3.37e-16

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 81.88  E-value: 3.37e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065167   454 QGEPGPKGPDGPRGEiglpgpqgppgpqgPSGLSIQGMPGMPGEKGEKGDTGLPGPQGIPGGVGSPGRDGSPGQRGLPGK 533
Cdd:NF038329 125 AGPAGPAGEQGPRGD--------------RGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGE 190
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 2065167   534 DGSSGPPGPPGPIGIPGTPGVPGITGSMGPQGALGPPGVPGaKGERGERGD 584
Cdd:NF038329 191 KGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGD 240
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
6-185 5.49e-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: 76.78  E-value: 5.49e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065167    6 ADLVFMVDGSWSIGDeNFNKIISFLYSTVGALNKigtDGTQVAMVQFTDDPRTEFKLNAYKTKETL-LDAIKHISyKGGN 84
Cdd:cd01474   5 FDLYFVLDKSGSVAA-NWIEIYDFVEQLVDRFNS---PGLRFSFITFSTRATKILPLTDDSSAIIKgLEVLKKVT-PSGQ 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065167   85 TKTGKAIKYVRDTLFTAESGTRRgIPKVIVVITDGRSQDDV-------NKISREMqldGYSIFAIGVADADYSELVSIGS 157
Cdd:cd01474  80 TYIHEGLENANEQIFNRNGGGRE-TVSVIIALTDGQLLLNGhkypeheAKLSRKL---GAIVYCVGVTDFLKSQLINIAD 155
                       170       180
                ....*....|....*....|....*....
gi 2065167  158 KPSarHVFFVDD-FDAFKKIEDELITFVC 185
Cdd:cd01474 156 SKE--YVFPVTSgFQALSGIIESVVKKAC 182
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
6-169 7.76e-15

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


Pssm-ID: 238757 [Multi-domain]  Cd Length: 186  Bit Score: 73.57  E-value: 7.76e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065167    6 ADLVFMVDGSWSIGDENFN-------KIISFLYSTvgALNKIGTDGTQVAMVQFTDDPRTEF-KLNAYKTKETLLDAIKH 77
Cdd:cd01480   3 VDITFVLDSSESVGLQNFDitknfvkRVAERFLKD--YYRKDPAGSWRVGVVQYSDQQEVEAgFLRDIRNYTSLKEAVDN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065167   78 ISYKGGNTKTGKAIKYVRDTLFTAESGTRRgipKVIVVITDGRSQ---DDVNKIS-REMQLDGYSIFAIGVADADYSELV 153
Cdd:cd01480  81 LEYIGGGTFTDCALKYATEQLLEGSHQKEN---KFLLVITDGHSDgspDGGIEKAvNEADHLGIKIFFVAVGSQNEEPLS 157
                       170       180
                ....*....|....*....|....*.
gi 2065167  154 SIGSKPSARHV----------FFVDD 169
Cdd:cd01480 158 RIACDGKSALYrenfaellwsFFIDD 183
VWA_2 pfam13519
von Willebrand factor type A domain;
8-116 1.23e-12

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 64.62  E-value: 1.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065167      8 LVFMVDGSWSIGDE-----NFNKIISFLYSTVGALNkigtdGTQVAMVQFTDDPRTEFKLNayKTKETLLDAIKHISYKG 82
Cdd:pfam13519   1 LVFVLDTSGSMRNGdygptRLEAAKDAVLALLKSLP-----GDRVGLVTFGDGPEVLIPLT--KDRAKILRALRRLEPKG 73
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2065167     83 GNTKTGKAIKYVRDTLFTAesgtRRGIPKVIVVI 116
Cdd:pfam13519  74 GGTNLAAALQLARAALKHR----RKNQPRRIVLI 103
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
454-583 2.65e-12

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 69.55  E-value: 2.65e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065167   454 QGEPGPKGPDGPRGEI-GLPGPQGPPGPQGPSGLSIQGMPGMPGE--KGEKGDTGLPGPQGIP---GGVGSPGRDGSPGQ 527
Cdd:NF038329 185 KGPAGEKGPQGPRGETgPAGEQGPAGPAGPDGEAGPAGEDGPAGPagDGQQGPDGDPGPTGEDgpqGPDGPAGKDGPRGD 264
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 2065167   528 RGLPGKDgssgppgppgpigipgtpgvpGITGSMGPQGALGPPGVPGAKGERGERG 583
Cdd:NF038329 265 RGEAGPD---------------------GPDGKDGERGPVGPAGKDGQNGKDGLPG 299
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
455-576 1.01e-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: 67.62  E-value: 1.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065167   455 GEPGPKGPDGPRGEIGLPGPQGPPGPQGPSGLSIQGMPGMPGEKGEKGDTGLPGPQGIPGG------VGSPGRDGSPGQR 528
Cdd:NF038329 216 GEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKdgergpVGPAGKDGQNGKD 295
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 2065167   529 GLPGKDGSSGPPGPPGPIGIPGTPGVPGITGSMGPQGALGPPGVPGAK 576
Cdd:NF038329 296 GLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
6-176 1.69e-09

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: 59.18  E-value: 1.69e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065167    6 ADLVFMVDGSWSIGDEN-FNKIISFLYSTVGALNKigtdGTQVAMVQFTDDPRTEFKLNayKTKETLLDAIKHISYKGGn 84
Cdd:COG1240  93 RDVVLVVDASGSMAAENrLEAAKGALLDFLDDYRP----RDRVGLVAFGGEAEVLLPLT--RDREALKRALDELPPGGG- 165
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065167   85 TKTGKAIKYVRDTLFTAESGTRrgipKVIVVITDGR---SQDDVNKISREMQLDGYSIFAIGVADADYSE--LVSIGSKP 159
Cdd:COG1240 166 TPLGDALALALELLKRADPARR----KVIVLLTDGRdnaGRIDPLEAAELAAAAGIRIYTIGVGTEAVDEglLREIAEAT 241
                       170
                ....*....|....*..
gi 2065167  160 SARHvFFVDDFDAFKKI 176
Cdd:COG1240 242 GGRY-FRADDLSELAAI 257
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
489-532 9.97e-09

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: 51.73  E-value: 9.97e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2065167    489 QGMPGMPGEKGEKGDTGLPGPQGIPGGVGSPGRDGSPGQRGLPG 532
Cdd:pfam01391   3 PGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPG 46
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
490-575 2.53e-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: 50.96  E-value: 2.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065167    490 GMPGMPGEKGEKGDTGLPGPQGIPGGVGSPGRDGSPGQRglpgkdgssgppgppgpigipgtpgvpgitGSMGPQGALGP 569
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPP------------------------------GPPGPPGPPGA 50

                  ....*.
gi 2065167    570 PGVPGA 575
Cdd:pfam01391  51 PGAPGP 56
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
7-155 8.91e-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: 54.30  E-value: 8.91e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065167    7 DLVFMVDGSWSIGDENFNKIISFLYSTVGALNkigtDGTQVAMVQFTDDPRTEFKLNAYKTKETLLDAIKHISYKGGnTK 86
Cdd:COG2425 120 PVVLCVDTSGSMAGSKEAAAKAAALALLRALR----PNRRFGVILFDTEVVEDLPLTADDGLEDAIEFLSGLFAGGG-TD 194
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2065167   87 TGKAIKYVRDTLftAESGTRRgipKVIVVITDGRSQDDVNKISREM--QLDGYSIFAIGVADADYSELVSI 155
Cdd:COG2425 195 IAPALRAALELL--EEPDYRN---ADIVLITDGEAGVSPEELLREVraKESGVRLFTVAIGDAGNPGLLEA 260
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
502-579 1.14e-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: 1.14e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2065167    502 GDTGLPGPQGIPGGVGSPGRDGSPGQRGLPGKDgssgppgppgpigipgtpgvpGITGSMGPQGALGPPGVPGAKGER 579
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEP---------------------GPPGPPGPPGPPGPPGAPGAPGPP 57
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
453-533 1.64e-06

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: 51.06  E-value: 1.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065167   453 QQGEPGPKGPDGPRGEIGLPGPQGPPGPqgpsglsiQGMPGMPGEKGEKGDTGLPGPQGIPGGVGSPGRDGSPGQRGLPG 532
Cdd:NF038329 267 EAGPDGPDGKDGERGPVGPAGKDGQNGK--------DGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338

                 .
gi 2065167   533 K 533
Cdd:NF038329 339 K 339
vWA_F09G8-8_type cd01477
VWA F09G8.8 type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
7-165 6.41e-05

VWA F09G8.8 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. The members of this subgroup lack the MIDAS motif. This subgroup is found only in C. elegans and the members identified thus far are always found fused to a C-Lectin type domain. Biochemical function thus far has not be attributed to any of the members of this subgroup.


Pssm-ID: 238754 [Multi-domain]  Cd Length: 193  Bit Score: 44.72  E-value: 6.41e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065167    7 DLVFMVDGSWSIGDENFNKIISFLYSTVGALNKIGTD-----GTQVAMVQFTDDPRTEFKLNAYKTKETLLDAIKHI--- 78
Cdd:cd01477  21 DIVFVVDNSKGMTQGGLWQVRATISSLFGSSSQIGTDyddprSTRVGLVTYNSNATVVADLNDLQSFDDLYSQIQGSltd 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065167   79 --SYKGGNTKTGkaIKYVRDTLFTAESGTRRGIPKVIVVIT---DGRSQDDVNKISREMQLDGYSIfaIGVA---DADYS 150
Cdd:cd01477 101 vsSTNASYLDTG--LQAAEQMLAAGKRTSRENYKKVVIVFAsdyNDEGSNDPRPIAARLKSTGIAI--ITVAftqDESSN 176
                       170
                ....*....|....*
gi 2065167  151 ELVSIGSKPSARHVF 165
Cdd:cd01477 177 LLDKLGKIASPGMNF 191
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
508-583 2.39e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.40  E-value: 2.39e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2065167    508 GPQGIPGGVGSPGRDGSPGQRglpgkdgssgppGPpgpigipgtpgvPGITGSMGPQGALGPPGVPGAKGERGERG 583
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPP------------GP------------PGPPGPPGEPGPPGPPGPPGPPGPPGAPG 52
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
5-171 4.29e-04

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 43.80  E-value: 4.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065167     5 KADLVFMVDGSWSIGDENF-NKIISFLYSTVGALNkIGTDGTQVAMVQFTDDPRTEFKL--NAYKTKETLLDAIKHISyK 81
Cdd:PTZ00441  42 EVDLYLLVDGSGSIGYHNWiTHVIPMLMGLIQQLN-LSDDAINLYMSLFSNNTTELIRLgsGASKDKEQALIIVKSLR-K 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065167    82 G----GNTKTGKAIKYVRDTLftAESGTRRGIPKVIVVITDG--RSQDDVNKISREMQLDGYSIFAIGVA---DADYSEL 152
Cdd:PTZ00441 120 TylpyGKTNMTDALLEVRKHL--NDRVNRENAIQLVILMTDGipNSKYRALEESRKLKDRNVKLAVIGIGqgiNHQFNRL 197
                        170
                 ....*....|....*....
gi 2065167   153 VsIGSKPSARHVFFVDDFD 171
Cdd:PTZ00441 198 L-AGCRPREGKCKFYSDAD 215
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
7-134 6.28e-04

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


Pssm-ID: 238750 [Multi-domain]  Cd Length: 192  Bit Score: 41.53  E-value: 6.28e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065167    7 DLVFMVDGSWSIGDENFNK-IISFLYSTVGALNkIGTDGTQVAM----------VQFTDDPRTEfklnayktKETLLDAI 75
Cdd:cd01473   2 DLTLILDESASIGYSNWRKdVIPFTEKIINNLN-ISKDKVHVGIllfaeknrdvVPFSDEERYD--------KNELLKKI 72
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2065167   76 KHI--SYK-GGNTKTGKAIKYVRDTlFTAESGTRRGIPKVIVVITDGRSQDDVNKISREMQL 134
Cdd:cd01473  73 NDLknSYRsGGETYIVEALKYGLKN-YTKHGNRRKDAPKVTMLFTDGNDTSASKKELQDISL 133
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
12-178 7.99e-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: 41.50  E-value: 7.99e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065167   12 VDGSWSIGDENFNKiisFLYSTVGALNKIGTDGT--QVAMVQFTDDPR-----TEFKLNAYKTKETLLDAIKHISYKGGN 84
Cdd:cd01470   7 LDASDSIGEEDFDE---AKNAIKTLIEKISSYEVspRYEIISYASDPKeivsiRDFNSNDADDVIKRLEDFNYDDHGDKT 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065167   85 -TKTGKAIKYVRDTLFTAESGTRRG---IPKVIVVITDGRS-------------QDDVNK-----ISREMQLDGYsIFAI 142
Cdd:cd01470  84 gTNTAAALKKVYERMALEKVRNKEAfneTRHVIILFTDGKSnmggsplptvdkiKNLVYKnnksdNPREDYLDVY-VFGV 162
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 2065167  143 GvADADYSELVSIGS-KPSARHVFFVDDFDAFKKIED 178
Cdd:cd01470 163 G-DDVNKEELNDLASkKDNERHFFKLKDYEDLQEVFD 198
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
82-176 2.56e-03

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 39.91  E-value: 2.56e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065167   82 GGNTKTGKAIKYVRDTLfTAESGTRRGIPK-----VIVVITDGRSQDD-----VNKISREMQLDGYSIFAIGV-ADADYS 150
Cdd:COG4245  78 SGGTPLGAALELLLDLI-ERRVQKYTAEGKgdwrpVVFLITDGEPTDSdweaaLQRLKDGEAAKKANIFAIGVgPDADTE 156
                        90       100
                ....*....|....*....|....*.
gi 2065167  151 ELVSIGskpSARHVFFVDDFDAFKKI 176
Cdd:COG4245 157 VLKQLT---DPVRALDALDGLDFREF 179
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
555-584 8.63e-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: 8.63e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 2065167    555 PGITGSMGPQGALGPPGVPGAKGERGERGD 584
Cdd:pfam01391   3 PGPPGPPGPPGPPGPPGPPGPPGPPGPPGE 32
 
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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