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Conserved domains on  [gi|18780273|ref|NP_110447|]
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collagen alpha-1(XXI) chain isoform a precursor [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 34-254 1.78e-58

Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains.


The actual alignment was detected with superfamily member cd01475:

Pssm-ID: 469594 [Multi-domain]  Cd Length: 224  Bit Score: 199.92  E-value: 1.78e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273  34 APTDLVFILDGSYSVGPENFEIVKKWLVNITKNFDIGPKFIQVGVVQYSDYPVLEIPLGSYDSGEHLTAAVESILYLGGN 113
Cdd:cd01475   1 GPTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273 114 TKTGKAIQFALDYLFA------KSSRFLTKIAVVLTDGKSQDDVKDAAQAARDSKITLFAIGVGSETEDaELRAIANKPS 187
Cdd:cd01475  81 TMTGLAIQYAMNNAFSeaegarPGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEE-ELREIASEPL 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18780273 188 STYVFYVEDYIAISKIREVMKQKLCE-ESVCPTripvAARDERGFDILLGLDVNKKVKKRIQLSPKKI 254
Cdd:cd01475 160 ADHVFYVEDFSTIEELTKKFQGKICVvPDLCAT----LSHVCQQVCISTPGSYLCACTEGYALLEDNK 223
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 511-746 1.73e-37

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: 146.59  E-value: 1.73e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273  511 DGDKGDRGLPGFPGLHGMPGSKGEMGAKGDKGSPGfygkkgakgEKGNAGFPGLPGPAGEPGRHGKDGLMGSPGFKGEAG 590
Cdd:NF038329 116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAG---------PPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKG 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273  591 SPGAPGQDGTRGEPGIPGFPGNRGLMGQKGEIGPPGQQGKKGAPGmpglMGSNGSPGQPGTPGSKGSKGEPGIQGMPGAS 670
Cdd:NF038329 187 PAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG----DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPR 262

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18780273  671 GLKGEPGATGSPGEPGYMGLPGIQGKKGDKGNQGEKGIQGQKGENGRQGIPGQQGIQGHHGAKGERGEKGEPGVRG 746
Cdd:NF038329 263 GDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
LamG super family cl22861
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 230-412 9.77e-23

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.


The actual alignment was detected with superfamily member smart00210:

Pssm-ID: 473984  Cd Length: 184  Bit Score: 96.66  E-value: 9.77e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273    230 GFDILLGLD---VNKKVKKRIQLSPKKiKGYEVTSKVDLSELTSNVFPEGLPPSYVFVSTQRFKVKKIWDLWRILTIDGR 306
Cdd:smart00210   1 GQDLLQVFDlpsLSFAIRQVVGPEPGS-PAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPKSRGVLFAIYDAQNV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273    307 PQIAVTLNGVDKILLFTTTSVINGSQVVTFANPQvktLFDEGWHQIRLLVTEQDVTLYIDDQQIENKPLHPVLG--ILIN 384
Cdd:smart00210  80 RQFGLEVDGRANTLLLRYQGVDGKQHTVSFRNLP---LADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGQppIDTD 156

                          170       180
                   ....*....|....*....|....*...
gi 18780273    385 GQTQIGKYSGKEETVQFDVQKLRIYCDP 412
Cdd:smart00210 157 GIEVRGAQAADRKPFQGDLQQLKIVCDP 184
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 452-508 1.05e-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: 54.81  E-value: 1.05e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 18780273   452 GLQGPKGDPGLPGNPGYPGQPGQDGKPGYQGIAGTPGVPGSPGIQGARGLPGYKGEP 508
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 692-934 1.90e-07

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: 54.53  E-value: 1.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273  692 GIQGKKGDkGNQGEKGIQGQKGENGRQGIPGQQGIQGHHGAKGERGEKGEPGVRGAIGSKGESGVDGLMGPAGPKGQPGD 771
Cdd:NF038329 109 GLQQLKGD-GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGP 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273  772 PGPQgppgldgkpgrefseqfirqvctdviraqlpvllqsgrirncdhclsqhgspgipgppgpiGPEGPRGLPGLPGRD 851
Cdd:NF038329 188 AGEK-------------------------------------------------------------GPQGPRGETGPAGEQ 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273  852 GVPGLVGVPGRPGVRGLKGLPGR-----NGEKGSQGfgypgeqGPPGPPGPEGPPGISKEGPPGDPGLPGKDGDHGKPGI 926
Cdd:NF038329 207 GPAGPAGPDGEAGPAGEDGPAGPagdgqQGPDGDPG-------PTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGE 279


                 ....*...
gi 18780273  927 QGQPGPPG 934
Cdd:NF038329 280 RGPVGPAG 287
 
Name Accession Description Interval E-value
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 34-254 1.78e-58

VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and matrix-matrix interactions thereby providing tissue integrity. Some members of the matrilin family are expressed specifically in developing cartilage rudiments. The matrilin family consists of at least four members. All the members of the matrilin family contain VWA domains, EGF-like domains and a heptad repeat coiled-coiled domain at the carboxy terminus which is responsible for the oligomerization of the matrilins. The VWA domains have been shown to be essential for matrilin network formation by interacting with matrix ligands.


Pssm-ID: 238752 [Multi-domain]  Cd Length: 224  Bit Score: 199.92  E-value: 1.78e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273  34 APTDLVFILDGSYSVGPENFEIVKKWLVNITKNFDIGPKFIQVGVVQYSDYPVLEIPLGSYDSGEHLTAAVESILYLGGN 113
Cdd:cd01475   1 GPTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273 114 TKTGKAIQFALDYLFA------KSSRFLTKIAVVLTDGKSQDDVKDAAQAARDSKITLFAIGVGSETEDaELRAIANKPS 187
Cdd:cd01475  81 TMTGLAIQYAMNNAFSeaegarPGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEE-ELREIASEPL 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18780273 188 STYVFYVEDYIAISKIREVMKQKLCE-ESVCPTripvAARDERGFDILLGLDVNKKVKKRIQLSPKKI 254
Cdd:cd01475 160 ADHVFYVEDFSTIEELTKKFQGKICVvPDLCAT----LSHVCQQVCISTPGSYLCACTEGYALLEDNK 223
VWA pfam00092
von Willebrand factor type A domain;
37-205 1.73e-54

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 186.71  E-value: 1.73e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273    37 DLVFILDGSYSVGPENFEIVKKWLVNITKNFDIGPKFIQVGVVQYSDYPVLEIPLGSYDSGEHLTAAVESILYLGGNTK- 115
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTn 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273   116 TGKAIQFALDYLFAKSSRF---LTKIAVVLTDGKSQD-DVKDAAQAARDSKITLFAIGVGSETeDAELRAIANKPSSTYV 191
Cdd:pfam00092  81 TGKALKYALENLFSSAAGArpgAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNAD-DEELRKIASEPGEGHV 159

                         170
                  ....*....|....
gi 18780273   192 FYVEDYIAISKIRE 205
Cdd:pfam00092 160 FTVSDFEALEDLQD 173
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 37-203 5.25e-45

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: 159.93  E-value: 5.25e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273     37 DLVFILDGSYSVGPENFEIVKKWLVNITKNFDIGPKFIQVGVVQYSDYPVLEIPLGSYDSGEHLTAAVESILY-LGGNTK 115
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYkLGGGTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273    116 TGKAIQFALDYLFAK---SSRFLTKIAVVLTDGKSQD---DVKDAAQAARDSKITLFAIGVGSETEDAELRAIANKPSST 189
Cdd:smart00327  81 LGAALQYALENLFSKsagSRRGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDVDEEELKKLASAPGGV 160

                          170
                   ....*....|....
gi 18780273    190 YVFYVEDYIAISKI 203
Cdd:smart00327 161 YVFLPELLDLLIDL 174
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 511-746 1.73e-37

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: 146.59  E-value: 1.73e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273  511 DGDKGDRGLPGFPGLHGMPGSKGEMGAKGDKGSPGfygkkgakgEKGNAGFPGLPGPAGEPGRHGKDGLMGSPGFKGEAG 590
Cdd:NF038329 116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAG---------PPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKG 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273  591 SPGAPGQDGTRGEPGIPGFPGNRGLMGQKGEIGPPGQQGKKGAPGmpglMGSNGSPGQPGTPGSKGSKGEPGIQGMPGAS 670
Cdd:NF038329 187 PAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG----DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPR 262

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18780273  671 GLKGEPGATGSPGEPGYMGLPGIQGKKGDKGNQGEKGIQGQKGENGRQGIPGQQGIQGHHGAKGERGEKGEPGVRG 746
Cdd:NF038329 263 GDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 447-655 2.90e-35

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: 140.04  E-value: 2.90e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273  447 PPGKPGLQGPKGDPGLPGNPGYPGQPGQDGKPGYQGIAGTPGVPGSPGIQGARGLPGYKGEPGRDGDKGDRGLPG---FP 523
Cdd:NF038329 127 PAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGpagEQ 206

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273  524 GLHGMPGSKGEMGAKGDKGSPGfygkKGAKGEKGNAGFPGLPGPAGEPGRHGKDGLMGSPGFKGEAGSPGAPGQDGTRGE 603
Cdd:NF038329 207 GPAGPAGPDGEAGPAGEDGPAG----PAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGP 282

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18780273  604 PGIPG---------FPGNRGLMGQKGEIGPPGQQGKKGAPGMPGLMGSNGSPGQPGTPGSK 655
Cdd:NF038329 283 VGPAGkdgqngkdgLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 598-933 1.66e-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: 116.93  E-value: 1.66e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273  598 DGTRGEPGIPGFPGNRGLMGQKG---EIGPPGQQGKKGAPGMPGLMGSNGSPGQPGTPGSKGSKGEPGIQGMPGASGLKG 674
Cdd:NF038329 116 DGEKGEPGPAGPAGPAGEQGPRGdrgETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273  675 EPGATGSPGEPGYMGLPGIQGKKGDKGNQGEKGIQGQkGENGRQGIPGQQGIQGhhgAKGERGEKGEPGVRGAIGSKGES 754
Cdd:NF038329 196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDG---PQGPDGPAGKDGPRGDRGEAGPD 271

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273  755 GVDGLMGPAGPkgqpgdpgpqgppgldgkpgrefseqfirqvctdviraqlpvllqsgrirncdhclsqhgspgipgppg 834
Cdd:NF038329 272 GPDGKDGERGP--------------------------------------------------------------------- 282

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273  835 pigpegprglPGLPGRDGVPGLVGVPGRPGVRG---LKGLPGRNGEKGSQGfgypgeqgppgppgpegppgiskegppgd 911
Cdd:NF038329 283 ----------VGPAGKDGQNGKDGLPGKDGKDGqngKDGLPGKDGKDGQPG----------------------------- 323

                        330       340
                 ....*....|....*....|..
gi 18780273  912 pglpgKDGDHGKPGIQGQPGPP 933
Cdd:NF038329 324 -----KDGLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 608-934 1.04e-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: 105.37  E-value: 1.04e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273  608 GFPGNRGLMGQKGEIGPPGQQGKKGAPGMPGLMGSNGSPGQPGTPGSKGSKGEPGIQGMPGASGLKGEPGATGSPGEPGY 687
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273  688 MGLPGIQGKKGDKGNQGEKGIQGQKGENGRQGIPGQqGIQGHHGAKGERGEKGEPGVRGAIGSKGESGVDGLMGPAGPKg 767
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPD- 274

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273  768 qpgdpgpqgppgldgkpgrefseqfirqvctdviraqlpvllqsgrirncdhclsqhgspgipgppgpigpegprglpgl 847
Cdd:NF038329     --------------------------------------------------------------------------------

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273  848 pGRDGVPGLVGVPGRPGVRGLKGLPGRNGEKGSQGfgypgeqgppgppgpegppgiskegppgDPGLPGKDGDHGKPGIQ 927
Cdd:NF038329 275 -GKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNG----------------------------KDGLPGKDGKDGQPGKD 325


                 ....*..
gi 18780273  928 GQPGPPG 934
Cdd:NF038329 326 GLPGKDG 332
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 230-412 9.77e-23

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


Pssm-ID: 214560  Cd Length: 184  Bit Score: 96.66  E-value: 9.77e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273    230 GFDILLGLD---VNKKVKKRIQLSPKKiKGYEVTSKVDLSELTSNVFPEGLPPSYVFVSTQRFKVKKIWDLWRILTIDGR 306
Cdd:smart00210   1 GQDLLQVFDlpsLSFAIRQVVGPEPGS-PAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPKSRGVLFAIYDAQNV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273    307 PQIAVTLNGVDKILLFTTTSVINGSQVVTFANPQvktLFDEGWHQIRLLVTEQDVTLYIDDQQIENKPLHPVLG--ILIN 384
Cdd:smart00210  80 RQFGLEVDGRANTLLLRYQGVDGKQHTVSFRNLP---LADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGQppIDTD 156

                          170       180
                   ....*....|....*....|....*...
gi 18780273    385 GQTQIGKYSGKEETVQFDVQKLRIYCDP 412
Cdd:smart00210 157 GIEVRGAQAADRKPFQGDLQQLKIVCDP 184
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 32-209 3.71e-17

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: 82.29  E-value: 3.71e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273  32 RTAPTDLVFILDGSYSVGPEN-FEIVKKWLVNITKNFdigPKFIQVGVVQYSDYPVLEIPLGSydSGEHLTAAVESiLYL 110
Cdd:COG1240  89 PQRGRDVVLVVDASGSMAAENrLEAAKGALLDFLDDY---RPRDRVGLVAFGGEAEVLLPLTR--DREALKRALDE-LPP 162

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273 111 GGNTKTGKAIQFALDyLFAKSSRFLTKIAVVLTDGK---SQDDVKDAAQAARDSKITLFAIGVGSETED-AELRAIANKP 186
Cdd:COG1240 163 GGGTPLGDALALALE-LLKRADPARRKVIVLLTDGRdnaGRIDPLEAAELAAAAGIRIYTIGVGTEAVDeGLLREIAEAT 241

                       170       180
                ....*....|....*....|...
gi 18780273 187 SSTYvFYVEDyiaISKIREVMKQ 209
Cdd:COG1240 242 GGRY-FRADD---LSELAAIYRE 260
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 452-508 1.05e-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: 54.81  E-value: 1.05e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 18780273   452 GLQGPKGDPGLPGNPGYPGQPGQDGKPGYQGIAGTPGVPGSPGIQGARGLPGYKGEP 508
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 587-649 3.45e-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: 53.65  E-value: 3.45e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18780273   587 GEAGSPGAPGQDGTRGEPGIPGFPGNRglmGQKGEIGPPGQQGKKGAPGMPglmGSNGSPGQP 649
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPP---GPPGEPGPPGPPGPPGPPGPP---GAPGAPGPP 57
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 692-934 1.90e-07

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: 54.53  E-value: 1.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273  692 GIQGKKGDkGNQGEKGIQGQKGENGRQGIPGQQGIQGHHGAKGERGEKGEPGVRGAIGSKGESGVDGLMGPAGPKGQPGD 771
Cdd:NF038329 109 GLQQLKGD-GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGP 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273  772 PGPQgppgldgkpgrefseqfirqvctdviraqlpvllqsgrirncdhclsqhgspgipgppgpiGPEGPRGLPGLPGRD 851
Cdd:NF038329 188 AGEK-------------------------------------------------------------GPQGPRGETGPAGEQ 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273  852 GVPGLVGVPGRPGVRGLKGLPGR-----NGEKGSQGfgypgeqGPPGPPGPEGPPGISKEGPPGDPGLPGKDGDHGKPGI 926
Cdd:NF038329 207 GPAGPAGPDGEAGPAGEDGPAGPagdgqQGPDGDPG-------PTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGE 279


                 ....*...
gi 18780273  927 QGQPGPPG 934
Cdd:NF038329 280 RGPVGPAG 287
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
 588-731 2.55e-07

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 54.69  E-value: 2.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273  588 EAGSPGAPGQdgtrGEPGIPGFPGnrGLMGQKGEIGPPGQQGKKGAPGMPGLMGSNGSPGQPG--------------TPG 653
Cdd:PRK14959 369 ESLRPSGGGA----SAPSGSAAEG--PASGGAATIPTPGTQGPQGTAPAAGMTPSSAAPATPApsaapsprvpwddaPPA 442

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273  654 SKGSKGEP-GIQGMPGASGLKGEPGATGS-PGEPGYMGLPGIQGKKGDKGNQGEKGI----QGQKGENGRQGIPGQQGiQ 727
Cdd:PRK14959 443 PPRSGIPPrPAPRMPEASPVPGAPDSVASaSDAPPTLGDPSDTAEHTPSGPRTWDGFlefcQGRNGQGGRLATVLRQA-T 521


                 ....
gi 18780273  728 GHHG 731
Cdd:PRK14959 522 PEHA 525
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 476-752 1.15e-05

dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a skin-specific glycoprotein that may play a regulatory role in the crosstalk between barrier dysfunction and inflammation, and therefore play a role in inflammatory diseases such as psoriasis. Dermokine is one of the most highly expressed proteins in differentiating keratinocytes, found mainly in the spinous and granular layers of the epidermis, but also in the epithelia of the small intestine, macrophages of the lung, and endothelial cells of the lung. Mouse dermokine has been reported to be encoded by 22 exons, and its expression leads to alpha, beta, and gamma transcripts.


Pssm-ID: 411053 [Multi-domain]  Cd Length: 495  Bit Score: 49.23  E-value: 1.15e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273 476 GKPGYQGIAGTPGVPGSPGIQGARGLPGYKGEPGRDGDKGDRglPGFPGLHGMPGSKGEMGAKGDKGSPGFygkkgakge 555
Cdd:cd21118  70 GEEGGSTLGSRGDVFEHRLGEAARSLGNAGNEIGRQAEDIIR--HGVDAVHNSWQGSGGHGAYGSQGGPGV--------- 138

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273 556 KGNAGFPGLPGPAGEPGRHGKDGLMGSpgfKGEAGSPGAPGQD-GTRGEPGIPGFPGNRGLMGQKGEIGPPGQQGKKG-- 632
Cdd:cd21118 139 QGHGIPGGTGGPWASGGNYGTNSLGGS---VGQGGNGGPLNYGtNSQGAVAQPGYGTVRGNNQNSGCTNPPPSGSHESfs 215

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273 633 -----------------APGMPGLMGSNGSPGQPGTPGSKGSKGEPGIQGMPGASGLKGEP-GATGSPGEPGYMGLPGIQ 694
Cdd:cd21118 216 nsggssssgssgsqgshGSNGQGSSGSSGGQGNGGNNGSSSSNSGNSGGSNGGSSGNSGSGsGGSSSGGSNGWGGSSSSG 295

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 18780273 695 GKKGDKGNQGEKgiQGQKGENGRQgiPGQQGIQGHHGAKGERGEKGEPGVRGAIGSKG 752
Cdd:cd21118 296 GSGGSGGGNKPE--CNNPGNDVRM--AGGGGSQGSKESSGSHGSNGGNGQAEAVGGLN 349
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
 563-686 1.05e-03

PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];


Pssm-ID: 444064 [Multi-domain]  Cd Length: 548  Bit Score: 42.74  E-value: 1.05e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273 563 GLPGPAGEPGRHGKDGLMGSPGFKGEAGSPGAPgQDGTRGEPGIPGFPGNRGLMGQKGEIGPPGQQGKKGAPGMPGLMGS 642
Cdd:COG5180 340 GVPEAASDAGQPPSAYPPAEEAVPGKPLEQGAP-RPGSSGGDGAPFQPPNGAPQPGLGRRGAPGPPMGAGDLVQAALDGG 418

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 18780273 643 NGSPGQPGTPGSKGSKGEPGIQGMPGASGLKGEPGATGSPGEPG 686
Cdd:COG5180 419 GRETASLGGAAGGAGQGPKADFVPGDAESVSGPAGLADQAGAAA 462
 
Name Accession Description Interval E-value
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 34-254 1.78e-58

VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and matrix-matrix interactions thereby providing tissue integrity. Some members of the matrilin family are expressed specifically in developing cartilage rudiments. The matrilin family consists of at least four members. All the members of the matrilin family contain VWA domains, EGF-like domains and a heptad repeat coiled-coiled domain at the carboxy terminus which is responsible for the oligomerization of the matrilins. The VWA domains have been shown to be essential for matrilin network formation by interacting with matrix ligands.


Pssm-ID: 238752 [Multi-domain]  Cd Length: 224  Bit Score: 199.92  E-value: 1.78e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273  34 APTDLVFILDGSYSVGPENFEIVKKWLVNITKNFDIGPKFIQVGVVQYSDYPVLEIPLGSYDSGEHLTAAVESILYLGGN 113
Cdd:cd01475   1 GPTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273 114 TKTGKAIQFALDYLFA------KSSRFLTKIAVVLTDGKSQDDVKDAAQAARDSKITLFAIGVGSETEDaELRAIANKPS 187
Cdd:cd01475  81 TMTGLAIQYAMNNAFSeaegarPGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEE-ELREIASEPL 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18780273 188 STYVFYVEDYIAISKIREVMKQKLCE-ESVCPTripvAARDERGFDILLGLDVNKKVKKRIQLSPKKI 254
Cdd:cd01475 160 ADHVFYVEDFSTIEELTKKFQGKICVvPDLCAT----LSHVCQQVCISTPGSYLCACTEGYALLEDNK 223
VWA pfam00092
von Willebrand factor type A domain;
37-205 1.73e-54

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 186.71  E-value: 1.73e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273    37 DLVFILDGSYSVGPENFEIVKKWLVNITKNFDIGPKFIQVGVVQYSDYPVLEIPLGSYDSGEHLTAAVESILYLGGNTK- 115
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTn 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273   116 TGKAIQFALDYLFAKSSRF---LTKIAVVLTDGKSQD-DVKDAAQAARDSKITLFAIGVGSETeDAELRAIANKPSSTYV 191
Cdd:pfam00092  81 TGKALKYALENLFSSAAGArpgAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNAD-DEELRKIASEPGEGHV 159

                         170
                  ....*....|....
gi 18780273   192 FYVEDYIAISKIRE 205
Cdd:pfam00092 160 FTVSDFEALEDLQD 173
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 36-192 1.84e-52

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: 180.57  E-value: 1.84e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273  36 TDLVFILDGSYSVGPENFEIVKKWLVNITKNFDIGPKFIQVGVVQYSDYPVLEIPLGSYDSGEHLTAAVESILYLGGN-T 114
Cdd:cd01450   1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGgT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273 115 KTGKAIQFALDYLFAKSSRFL--TKIAVVLTDGKSQD--DVKDAAQAARDSKITLFAIGVGSETEDaELRAIANKPSSTY 190
Cdd:cd01450  81 NTGKALQYALEQLFSESNAREnvPKVIIVLTDGRSDDggDPKEAAAKLKDEGIKVFVVGVGPADEE-ELREIASCPSERH 159


                ..
gi 18780273 191 VF 192
Cdd:cd01450 160 VF 161
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 36-197 2.60e-51

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: 177.48  E-value: 2.60e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273  36 TDLVFILDGSYSVGPENFEIVKKWLVNITKNFDIGPKFIQVGVVQYSDYPVLEIPLGSYDSGEHLTAAVESILYLGGNTK 115
Cdd:cd01482   1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273 116 TGKAIQFALDYLFAKSSRF---LTKIAVVLTDGKSQDDVKDAAQAARDSKITLFAIGVGSETEdAELRAIANKPSSTYVF 192
Cdd:cd01482  81 TGKALTHVREKNFTPDAGArpgVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADE-SELKMIASKPSETHVF 159


                ....*
gi 18780273 193 YVEDY 197
Cdd:cd01482 160 NVADF 164
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 36-196 2.79e-51

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: 177.42  E-value: 2.79e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273  36 TDLVFILDGSYSVGPENFEIVKKWLVNITKNFDIGPKFIQVGVVQYSDYPVLEIPLGSYDSGEHLTAAVESILYLGGNTK 115
Cdd:cd01472   1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273 116 TGKAIQFALDYLFAKSSRFLT---KIAVVLTDGKSQDDVKDAAQAARDSKITLFAIGVGSETEDaELRAIANKPSSTYVF 192
Cdd:cd01472  81 TGKALKYVRENLFTEASGSREgvpKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEE-ELKQIASDPKELYVF 159


                ....
gi 18780273 193 YVED 196
Cdd:cd01472 160 NVAD 163
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 37-203 5.25e-45

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: 159.93  E-value: 5.25e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273     37 DLVFILDGSYSVGPENFEIVKKWLVNITKNFDIGPKFIQVGVVQYSDYPVLEIPLGSYDSGEHLTAAVESILY-LGGNTK 115
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYkLGGGTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273    116 TGKAIQFALDYLFAK---SSRFLTKIAVVLTDGKSQD---DVKDAAQAARDSKITLFAIGVGSETEDAELRAIANKPSST 189
Cdd:smart00327  81 LGAALQYALENLFSKsagSRRGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDVDEEELKKLASAPGGV 160

                          170
                   ....*....|....
gi 18780273    190 YVFYVEDYIAISKI 203
Cdd:smart00327 161 YVFLPELLDLLIDL 174
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 36-203 9.01e-41

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: 147.89  E-value: 9.01e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273  36 TDLVFILDGSYSVGPENFEIVKKWLVNITKNFDIGPKFIQVGVVQYSDYPVLEIPLGSYDSGEHLTAAVESILYLGGNTK 115
Cdd:cd01469   1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273 116 TGKAIQFALDYLFAKSS---RFLTKIAVVLTDGKSQDD--VKDAAQAARDSKITLFAIGVG----SETEDAELRAIANKP 186
Cdd:cd01469  81 TATAIQYVVTELFSESNgarKDATKVLVVITDGESHDDplLKDVIPQAEREGIIRYAIGVGghfqRENSREELKTIASKP 160

                       170
                ....*....|....*..
gi 18780273 187 SSTYVFYVEDYIAISKI 203
Cdd:cd01469 161 PEEHFFNVTDFAALKDI 177
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 511-746 1.73e-37

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: 146.59  E-value: 1.73e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273  511 DGDKGDRGLPGFPGLHGMPGSKGEMGAKGDKGSPGfygkkgakgEKGNAGFPGLPGPAGEPGRHGKDGLMGSPGFKGEAG 590
Cdd:NF038329 116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAG---------PPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKG 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273  591 SPGAPGQDGTRGEPGIPGFPGNRGLMGQKGEIGPPGQQGKKGAPGmpglMGSNGSPGQPGTPGSKGSKGEPGIQGMPGAS 670
Cdd:NF038329 187 PAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG----DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPR 262

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18780273  671 GLKGEPGATGSPGEPGYMGLPGIQGKKGDKGNQGEKGIQGQKGENGRQGIPGQQGIQGHHGAKGERGEKGEPGVRG 746
Cdd:NF038329 263 GDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 447-655 2.90e-35

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: 140.04  E-value: 2.90e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273  447 PPGKPGLQGPKGDPGLPGNPGYPGQPGQDGKPGYQGIAGTPGVPGSPGIQGARGLPGYKGEPGRDGDKGDRGLPG---FP 523
Cdd:NF038329 127 PAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGpagEQ 206

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273  524 GLHGMPGSKGEMGAKGDKGSPGfygkKGAKGEKGNAGFPGLPGPAGEPGRHGKDGLMGSPGFKGEAGSPGAPGQDGTRGE 603
Cdd:NF038329 207 GPAGPAGPDGEAGPAGEDGPAG----PAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGP 282

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18780273  604 PGIPG---------FPGNRGLMGQKGEIGPPGQQGKKGAPGMPGLMGSNGSPGQPGTPGSK 655
Cdd:NF038329 283 VGPAGkdgqngkdgLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 37-192 5.88e-32

Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains.


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 122.29  E-value: 5.88e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273  37 DLVFILDGSYSVGPENFEIVKKWLVNITKNFDIGPKFIQVGVVQYSDYPVLEIPLGSYDSGEHLTAAVESILY-LGGNTK 115
Cdd:cd00198   2 DIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKgLGGGTN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273 116 TGKAIQFALDYLFAKSSRFLTKIAVVLTDGKSQDD---VKDAAQAARDSKITLFAIGVGSETEDAELRAIANKPSSTYVF 192
Cdd:cd00198  82 IGAALRLALELLKSAKRPNARRVIILLTDGEPNDGpelLAEAARELRKLGITVYTIGIGDDANEDELKEIADKTTGGAVF 161
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 37-197 1.09e-30

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: 118.58  E-value: 1.09e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273  37 DLVFILDGSYSVGPENFEIVKKWLVNITKNFDIGPKFIQVGVVQYSDYPVLEIPLGSYDSGEHLTAAVESILYLGGN-TK 115
Cdd:cd01481   2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSqLN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273 116 TGKAIQFALDYLFAKS--SRF---LTKIAVVLTDGKSQDDVKDAAQAARDSKITLFAIGVGSeTEDAELRAIANKPSstY 190
Cdd:cd01481  82 TGSALDYVVKNLFTKSagSRIeegVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARN-ADLAELQQIAFDPS--F 158


                ....*..
gi 18780273 191 VFYVEDY 197
Cdd:cd01481 159 VFQVSDF 165
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 598-933 1.66e-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: 116.93  E-value: 1.66e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273  598 DGTRGEPGIPGFPGNRGLMGQKG---EIGPPGQQGKKGAPGMPGLMGSNGSPGQPGTPGSKGSKGEPGIQGMPGASGLKG 674
Cdd:NF038329 116 DGEKGEPGPAGPAGPAGEQGPRGdrgETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273  675 EPGATGSPGEPGYMGLPGIQGKKGDKGNQGEKGIQGQkGENGRQGIPGQQGIQGhhgAKGERGEKGEPGVRGAIGSKGES 754
Cdd:NF038329 196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDG---PQGPDGPAGKDGPRGDRGEAGPD 271

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273  755 GVDGLMGPAGPkgqpgdpgpqgppgldgkpgrefseqfirqvctdviraqlpvllqsgrirncdhclsqhgspgipgppg 834
Cdd:NF038329 272 GPDGKDGERGP--------------------------------------------------------------------- 282

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273  835 pigpegprglPGLPGRDGVPGLVGVPGRPGVRG---LKGLPGRNGEKGSQGfgypgeqgppgppgpegppgiskegppgd 911
Cdd:NF038329 283 ----------VGPAGKDGQNGKDGLPGKDGKDGqngKDGLPGKDGKDGQPG----------------------------- 323

                        330       340
                 ....*....|....*....|..
gi 18780273  912 pglpgKDGDHGKPGIQGQPGPP 933
Cdd:NF038329 324 -----KDGLPGKDGKDGQPGKP 340
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 37-190 7.97e-26

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: 104.79  E-value: 7.97e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273  37 DLVFILDGSYSVGPEnFEIVKKWLVNITKNFDIGPKFIQVGVVQYSDYP--VLEIPLGSYDSGEHLTAAVESILYLGGNT 114
Cdd:cd01476   2 DLLFVLDSSGSVRGK-FEKYKKYIERIVEGLEIGPTATRVALITYSGRGrqRVRFNLPKHNDGEELLEKVDNLRFIGGTT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273 115 KTGKAIQFALDYLFAKSSRF--LTKIAVVLTDGKSQDDVKDAAQAARDSK-ITLFAIGVG--SETEDAELRAIANKPSST 189
Cdd:cd01476  81 ATGAAIEVALQQLDPSEGRRegIPKVVVVLTDGRSHDDPEKQARILRAVPnIETFAVGTGdpGTVDTEELHSITGNEDHI 160


                .
gi 18780273 190 Y 190
Cdd:cd01476 161 F 161
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 35-189 8.57e-25

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


Pssm-ID: 238757 [Multi-domain]  Cd Length: 186  Bit Score: 102.46  E-value: 8.57e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273  35 PTDLVFILDGSYSVGPENFEIVKKWLVNITKNF------DIGPKFIQVGVVQYSDYPVLE-IPLGSYDSGEHLTAAVESI 107
Cdd:cd01480   2 PVDITFVLDSSESVGLQNFDITKNFVKRVAERFlkdyyrKDPAGSWRVGVVQYSDQQEVEaGFLRDIRNYTSLKEAVDNL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273 108 LYLGGNTKTGKAIQFALDYLFAKSSRFLTKIAVVLTDGKSQ----DDVKDAAQAARDSKITLFAIGVGSETEDaELRAIA 183
Cdd:cd01480  82 EYIGGGTFTDCALKYATEQLLEGSHQKENKFLLVITDGHSDgspdGGIEKAVNEADHLGIKIFFVAVGSQNEE-PLSRIA 160


                ....*.
gi 18780273 184 NKPSST 189
Cdd:cd01480 161 CDGKSA 166
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 608-934 1.04e-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: 105.37  E-value: 1.04e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273  608 GFPGNRGLMGQKGEIGPPGQQGKKGAPGMPGLMGSNGSPGQPGTPGSKGSKGEPGIQGMPGASGLKGEPGATGSPGEPGY 687
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273  688 MGLPGIQGKKGDKGNQGEKGIQGQKGENGRQGIPGQqGIQGHHGAKGERGEKGEPGVRGAIGSKGESGVDGLMGPAGPKg 767
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPD- 274

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273  768 qpgdpgpqgppgldgkpgrefseqfirqvctdviraqlpvllqsgrirncdhclsqhgspgipgppgpigpegprglpgl 847
Cdd:NF038329     --------------------------------------------------------------------------------

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273  848 pGRDGVPGLVGVPGRPGVRGLKGLPGRNGEKGSQGfgypgeqgppgppgpegppgiskegppgDPGLPGKDGDHGKPGIQ 927
Cdd:NF038329 275 -GKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNG----------------------------KDGLPGKDGKDGQPGKD 325


                 ....*..
gi 18780273  928 GQPGPPG 934
Cdd:NF038329 326 GLPGKDG 332
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 230-412 9.77e-23

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


Pssm-ID: 214560  Cd Length: 184  Bit Score: 96.66  E-value: 9.77e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273    230 GFDILLGLD---VNKKVKKRIQLSPKKiKGYEVTSKVDLSELTSNVFPEGLPPSYVFVSTQRFKVKKIWDLWRILTIDGR 306
Cdd:smart00210   1 GQDLLQVFDlpsLSFAIRQVVGPEPGS-PAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPKSRGVLFAIYDAQNV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273    307 PQIAVTLNGVDKILLFTTTSVINGSQVVTFANPQvktLFDEGWHQIRLLVTEQDVTLYIDDQQIENKPLHPVLG--ILIN 384
Cdd:smart00210  80 RQFGLEVDGRANTLLLRYQGVDGKQHTVSFRNLP---LADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGQppIDTD 156

                          170       180
                   ....*....|....*....|....*...
gi 18780273    385 GQTQIGKYSGKEETVQFDVQKLRIYCDP 412
Cdd:smart00210 157 GIEVRGAQAADRKPFQGDLQQLKIVCDP 184
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 32-209 3.71e-17

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: 82.29  E-value: 3.71e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273  32 RTAPTDLVFILDGSYSVGPEN-FEIVKKWLVNITKNFdigPKFIQVGVVQYSDYPVLEIPLGSydSGEHLTAAVESiLYL 110
Cdd:COG1240  89 PQRGRDVVLVVDASGSMAAENrLEAAKGALLDFLDDY---RPRDRVGLVAFGGEAEVLLPLTR--DREALKRALDE-LPP 162

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273 111 GGNTKTGKAIQFALDyLFAKSSRFLTKIAVVLTDGK---SQDDVKDAAQAARDSKITLFAIGVGSETED-AELRAIANKP 186
Cdd:COG1240 163 GGGTPLGDALALALE-LLKRADPARRKVIVLLTDGRdnaGRIDPLEAAELAAAAGIRIYTIGVGTEAVDeGLLREIAEAT 241

                       170       180
                ....*....|....*....|...
gi 18780273 187 SSTYvFYVEDyiaISKIREVMKQ 209
Cdd:COG1240 242 GGRY-FRADD---LSELAAIYRE 260
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 37-189 5.10e-14

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: 71.26  E-value: 5.10e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273  37 DLVFILDGSYSVGPEN-FEIVKKWLVNITKNFDIGPKFIQVGVVQYSDYPVLEIPLGSY-----DSGEHLTAAVESILYL 110
Cdd:cd01471   2 DLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPnstnkDLALNAIRALLSLYYP 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273 111 GGNTKTGKAIQFALDYLF-AKSSR-FLTKIAVVLTDGKSQDDVK--DAAQAARDSKITLFAIGVGSETEDAELRAIANKP 186
Cdd:cd01471  82 NGSTNTTSALLVVEKHLFdTRGNReNAPQLVIIMTDGIPDSKFRtlKEARKLRERGVIIAVLGVGQGVNHEENRSLVGCD 161


                ...
gi 18780273 187 SST 189
Cdd:cd01471 162 PDD 164
VWA_2 pfam13519
von Willebrand factor type A domain;
38-142 1.36e-12

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 64.62  E-value: 1.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273    38 LVFILDGSYS-----VGPENFEIVKKWLVNITKNFDIGpkfiQVGVVQYSDYPVLEIPLGsyDSGEHLTAAVESILYLGG 112
Cdd:pfam13519   1 LVFVLDTSGSmrngdYGPTRLEAAKDAVLALLKSLPGD----RVGLVTFGDGPEVLIPLT--KDRAKILRALRRLEPKGG 74

                          90       100       110
                  ....*....|....*....|....*....|
gi 18780273   113 NTKTGKAIQFALDYLFAKSSRfLTKIAVVL 142
Cdd:pfam13519  75 GTNLAAALQLARAALKHRRKN-QPRRIVLI 103
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 452-508 1.05e-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: 54.81  E-value: 1.05e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 18780273   452 GLQGPKGDPGLPGNPGYPGQPGQDGKPGYQGIAGTPGVPGSPGIQGARGLPGYKGEP 508
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 447-502 2.59e-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: 54.04  E-value: 2.59e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 18780273   447 PPGKPGLQGPKGDPGLPGNPGYPGQPGQDGKPGYQGIAGTPGVPGSPGIQGARGLP 502
Cdd:pfam01391   2 PPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 455-509 3.13e-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: 53.65  E-value: 3.13e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 18780273   455 GPKGDPGLPGNPGYPGQPGQDGKPGYQGIAGTPGVPGSPGIQGARGLPGYKGEPG 509
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 587-649 3.45e-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: 53.65  E-value: 3.45e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18780273   587 GEAGSPGAPGQDGTRGEPGIPGFPGNRglmGQKGEIGPPGQQGKKGAPGMPglmGSNGSPGQP 649
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPP---GPPGEPGPPGPPGPPGPPGPP---GAPGAPGPP 57
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 562-765 3.99e-09

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 60.41  E-value: 3.99e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273   562 PGLPGPAGEPGrhgkdGLMGSPG----FKGEAGSPGAPgqdgtRGEPGIPGFPGNRGLMGQKGEIGPPGQQG-KKGAPGM 636
Cdd:pfam09606 101 PMGPGPGGPMG-----QQMGGPGtasnLLASLGRPQMP-----MGGAGFPSQMSRVGRMQPGGQAGGMMQPSsGQPGSGT 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273   637 PGLMGSNGSPGQPGTPGSKGSKGEPGIQGMPGASGLKG-----EPGATGSPGEPGYMGLPGIQGKKGDKG---NQGEKGI 708
Cdd:pfam09606 171 PNQMGPNGGPGQGQAGGMNGGQQGPMGGQMPPQMGVPGmpgpaDAGAQMGQQAQANGGMNPQQMGGAPNQvamQQQQPQQ 250

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 18780273   709 QGQKGENGRQGIPGQQGIQGHHGAKGErgekGEPGVRGAIGSKGESGVDGLMGPAGP 765
Cdd:pfam09606 251 QGQQSQLGMGINQMQQMPQGVGGGAGQ----GGPGQPMGPPGQQPGAMPNVMSIGDQ 303
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 629-685 4.76e-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: 53.27  E-value: 4.76e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 18780273   629 GKKGAPGMPGLMGSNGSPGQPGTPGSKGSKGEPGIQGMPGASGLKGEPGATGSPGEP 685
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 37-212 5.05e-09

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: 56.94  E-value: 5.05e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273  37 DLVFILDGSYSVGPENFEI-VKKWLVNITKNFDIGPKFIQVGVVQYSDYPVLEIPLG---SYDSGEhLTAAVESI---LY 109
Cdd:cd01473   2 DLTLILDESASIGYSNWRKdVIPFTEKIINNLNISKDKVHVGILLFAEKNRDVVPFSdeeRYDKNE-LLKKINDLknsYR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273 110 LGGNTKTGKAIQFALDYLFAKSSRFLT--KIAVVLTDG----KSQDDVKDAAQAARDSKITLFAIGVGsETEDAELRAIA 183
Cdd:cd01473  81 SGGETYIVEALKYGLKNYTKHGNRRKDapKVTMLFTDGndtsASKKELQDISLLYKEENVKLLVVGVG-AASENKLKLLA 159

                       170       180       190
                ....*....|....*....|....*....|..
gi 18780273 184 --NKPSSTYVFYVE-DYIAISKIREVMKQKLC 212
Cdd:cd01473 160 gcDINNDNCPNVIKtEWNNLNGISKFLTDKIC 191
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 632-686 6.45e-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: 52.88  E-value: 6.45e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 18780273   632 GAPGMPGLMGSNGSPGQPGTPGSKGSKGEPGIQGMPGASGLKGEPGATGSPGEPG 686
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 599-653 6.77e-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: 52.50  E-value: 6.77e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 18780273   599 GTRGEPGIPGFPGNRGLMGQKGEIGPPGQQGKKGAPGMPGLMGSNGSPGQPGTPG 653
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Glutenin_hmw pfam03157
High molecular weight glutenin subunit; Members of this family include high molecular weight ...
 439-725 6.93e-09

High molecular weight glutenin subunit; Members of this family include high molecular weight subunits of glutenin. This group of gluten proteins is thought to be largely responsible for the elastic properties of gluten, and hence, doughs. Indeed, glutenin high molecular weight subunits are classified as elastomeric proteins, because the glutenin network can withstand significant deformations without breaking, and return to the original conformation when the stress is removed. Elastomeric proteins differ considerably in amino acid sequence, but they are all polymers whose subunits consist of elastomeric domains, composed of repeated motifs, and non-elastic domains that mediate cross-linking between the subunits. The elastomeric domain motifs are all rich in glycine residues in addition to other hydrophobic residues. High molecular weight glutenin subunits have an extensive central elastomeric domain, flanked by two terminal non-elastic domains that form disulphide cross-links. The central elastomeric domain is characterized by the following three repeated motifs: PGQGQQ, GYYPTS[P/L]QQ, GQQ. It possesses overlapping beta-turns within and between the repeated motifs, and assumes a regular helical secondary structure with a diameter of approx. 1.9 nm and a pitch of approx. 1.5 nm.


Pssm-ID: 367362 [Multi-domain]  Cd Length: 786  Bit Score: 59.96  E-value: 6.93e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273   439 STPAPCICPPGKPGLQGPKGDPGLPGN-PGYPGQPGQdGKPGY------QGIAGTPG-VPGSPGIQGARGLPGYKGEPGR 510
Cdd:pfam03157 373 SQQQPQQGQQPEQGQQGQQQGQGQQGQqPGQGQQPGQ-GQPGYyptspqQSGQGQPGyYPTSPQQSGQGQQPGQGQQPGQ 451

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273   511 dGDKGDRGLPGfPGLHGMPGSKGEMGAKGDKGSPGFYGKKgakgekgnagfPGLPGPAGEPGRHGKDGlMGSPGFKgeAG 590
Cdd:pfam03157 452 -EQPGQGQQPG-QGQQGQQPGQPEQGQQPGQGQPGYYPTS-----------PQQSGQGQQLGQWQQQG-QGQPGYY--PT 515

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273   591 SPGAPGQDGTRGEPGIPGFPGNRGLMGQ--KGEIGPPGQQGKKGAPGM-PGLMGSNGSPGQPGTPGSKGSKGEPGiQGMP 667
Cdd:pfam03157 516 SPLQPGQGQPGYYPTSPQQPGQGQQLGQlqQPTQGQQGQQSGQGQQGQqPGQGQQGQQPGQGQQGQQPGQGQQPG-QGQP 594

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273   668 G-------ASGLKGEPGATGSPGE--PGYMGLPGIQGKKGDKG---NQGEKGIQGQKGENGRQGIPGQQG 725
Cdd:pfam03157 595 GyyptspqQSGQGQQPGQWQQPGQgqPGYYPTSSLQLGQGQQGyypTSPQQPGQGQQPGQWQQSGQGQQG 664
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 581-637 7.25e-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: 52.50  E-value: 7.25e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 18780273   581 GSPGFKGEAGSPGAPGQDGTRGEPGIPGFPGNRGLMGQKGEIGPPGQQGKKGAPGMP 637
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 638-692 9.82e-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: 52.11  E-value: 9.82e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 18780273   638 GLMGSNGSPGQPGTPGSKGSKGEPGIQGMPGASGLKGEPGATGSPGEPGYMGLPG 692
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 39-197 1.05e-08

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: 56.14  E-value: 1.05e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273  39 VFI-LDGSYSVGPENFEIVKKWLVN-ITK--NFDIGPKFiqvGVVQYSDYPVLEIPLGSYDSG------EHLTAAVESIL 108
Cdd:cd01470   3 IYIaLDASDSIGEEDFDEAKNAIKTlIEKisSYEVSPRY---EIISYASDPKEIVSIRDFNSNdaddviKRLEDFNYDDH 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273 109 YLGGNTKTGKAIQFALDYLF----AKSSRFLT--KIAVVLTDGKSQ---------DDVKD------AAQAARDSKITLFA 167
Cdd:cd01470  80 GDKTGTNTAAALKKVYERMAlekvRNKEAFNEtrHVIILFTDGKSNmggsplptvDKIKNlvyknnKSDNPREDYLDVYV 159

                       170       180       190
                ....*....|....*....|....*....|.
gi 18780273 168 IGVGSETEDAELRAIAN-KPSSTYVFYVEDY 197
Cdd:cd01470 160 FGVGDDVNKEELNDLASkKDNERHFFKLKDY 190
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 644-698 1.10e-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: 52.11  E-value: 1.10e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 18780273   644 GSPGQPGTPGSKGSKGEPGIQGMPGASGLKGEPGATGSPGEPGYMGLPGIQGKKG 698
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 488-544 1.67e-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: 51.73  E-value: 1.67e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 18780273   488 GVPGSPGIQGARGLPGYKGEPGRDGDKGDRGLPGFPGLHGMPGSKGEMGAKGDKGSP 544
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 647-701 2.05e-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: 51.34  E-value: 2.05e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 18780273   647 GQPGTPGSKGSKGEPGIQGMPGASGLKGEPGATGSPGEPGYMGLPGIQGKKGDKG 701
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 527-595 2.67e-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: 2.67e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18780273   527 GMPGSKGEMGAKGDKGSPGfygkkgakgekgNAGFPGLPGPAGEPGRHGKDGLMGSPGFKGEAGSPGAP 595
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPG------------PPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
35-184 2.67e-08

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 54.93  E-value: 2.67e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273  35 PTDLVFILDGSYSVGPENFEIVKKWLVNITKNFDIGPKF---IQVGVVQYSDYPVLEIPLGSYDSgehltaAVESILYLG 111
Cdd:COG4245   5 RLPVYLLLDTSGSMSGEPIEALNEGLQALIDELRQDPYAletVEVSVITFDGEAKVLLPLTDLED------FQPPDLSAS 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273 112 GNTKTGKAIQFALDyLFAKSSRFLTK--------IAVVLTDGKSQD-DVKDAAQAARD----SKITLFAIGVGSETEDAE 178
Cdd:COG4245  79 GGTPLGAALELLLD-LIERRVQKYTAegkgdwrpVVFLITDGEPTDsDWEAALQRLKDgeaaKKANIFAIGVGPDADTEV 157


                ....*.
gi 18780273 179 LRAIAN 184
Cdd:COG4245 158 LKQLTD 163
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 626-682 2.88e-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: 2.88e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 18780273   626 GQQGKKGAPGMPGLMGSNGSPGQPGTPGSKGSKGEPGIQGMPGASGLKGEPGATGSP 682
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 563-627 3.06e-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: 3.06e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18780273   563 GLPGPAGEPGrhgkdglmgSPGFKGEAGSPGAPGQDGTRGEPGIPGFPGNRGLMGQKGEIGPPGQ 627
Cdd:pfam01391   1 GPPGPPGPPG---------PPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 674-728 8.15e-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: 49.80  E-value: 8.15e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 18780273   674 GEPGATGSPGEPGYMGLPGIQGKKGDKGNQGEKGIQGQKGENGRQGIPGQQGIQG 728
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 641-696 8.15e-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: 49.80  E-value: 8.15e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 18780273   641 GSNGSPGQPGTPGSKGSKGEPGIQGMPGASGLKGEPGATGSPGEPGYMGLPGIQGK 696
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 37-214 8.57e-08

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: 53.28  E-value: 8.57e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273  37 DLVFILDGSYSVG---PENFEIVKkwlvnitknfDIGPKFI----QVGVVQYSDYPVLEIPLGSYDSGEHLTAAVESILY 109
Cdd:cd01474   6 DLYFVLDKSGSVAanwIEIYDFVE----------QLVDRFNspglRFSFITFSTRATKILPLTDDSSAIIKGLEVLKKVT 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273 110 LGGNTKTGKAIQFALDYLFAKS--SRFLTKIAVVLTDGKSQDDV-KDA---AQAARDSKITLFAIGVgSETEDAELRAIA 183
Cdd:cd01474  76 PSGQTYIHEGLENANEQIFNRNggGRETVSVIIALTDGQLLLNGhKYPeheAKLSRKLGAIVYCVGV-TDFLKSQLINIA 154

                       170       180       190
                ....*....|....*....|....*....|..
gi 18780273 184 NKPSstYVFYVED-YIAISKIREVMKQKLCEE 214
Cdd:cd01474 155 DSKE--YVFPVTSgFQALSGIIESVVKKACIE 184
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 596-656 9.08e-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: 49.41  E-value: 9.08e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18780273   596 GQDGTRGEPGIPGFPgnrglmGQKGEIGPPGQQGKKGAPGMPGLMGSNGSPGQPGTPGSKG 656
Cdd:pfam01391   1 GPPGPPGPPGPPGPP------GPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 656-711 9.82e-08

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 49.41  E-value: 9.82e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 18780273   656 GSKGEPGIQGMPGASGLKGEPGATGSPGEPGYMGLPGIQGKKGDKGNQGEKGIQGQ 711
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 38-206 1.35e-07

VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. Not much is known about the function of the VWA domain in these proteins. The members do have a conserved MIDAS motif. The biochemical function however is not known.


Pssm-ID: 238742 [Multi-domain]  Cd Length: 170  Bit Score: 52.28  E-value: 1.35e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273  38 LVFILDGSYSVGPENFEIVKKWLVNITKNfdIGPKFIqVGVVQYSDYPVLEIPLGSYDSGEHLTAAVESiLYLGGNTKTG 117
Cdd:cd01465   3 LVFVIDRSGSMDGPKLPLVKSALKLLVDQ--LRPDDR-LAIVTYDGAAETVLPATPVRDKAAILAAIDR-LTAGGSTAGG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273 118 KAIQFALDYLF-AKSSRFLTKIaVVLTDGK------SQDDVKDAAQAARDSKITLFAIGVGSETEDAELRAIANKPSSTY 190
Cdd:cd01465  79 AGIQLGYQEAQkHFVPGGVNRI-LLATDGDfnvgetDPDELARLVAQKRESGITLSTLGFGDNYNEDLMEAIADAGNGNT 157

                       170
                ....*....|....*..
gi 18780273 191 vfyveDYIA-ISKIREV 206
Cdd:cd01465 158 -----AYIDnLAEARKV 169
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 692-934 1.90e-07

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: 54.53  E-value: 1.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273  692 GIQGKKGDkGNQGEKGIQGQKGENGRQGIPGQQGIQGHHGAKGERGEKGEPGVRGAIGSKGESGVDGLMGPAGPKGQPGD 771
Cdd:NF038329 109 GLQQLKGD-GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGP 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273  772 PGPQgppgldgkpgrefseqfirqvctdviraqlpvllqsgrirncdhclsqhgspgipgppgpiGPEGPRGLPGLPGRD 851
Cdd:NF038329 188 AGEK-------------------------------------------------------------GPQGPRGETGPAGEQ 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273  852 GVPGLVGVPGRPGVRGLKGLPGR-----NGEKGSQGfgypgeqGPPGPPGPEGPPGISKEGPPGDPGLPGKDGDHGKPGI 926
Cdd:NF038329 207 GPAGPAGPDGEAGPAGEDGPAGPagdgqQGPDGDPG-------PTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGE 279


                 ....*...
gi 18780273  927 QGQPGPPG 934
Cdd:NF038329 280 RGPVGPAG 287
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 611-667 2.01e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 48.64  E-value: 2.01e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 18780273   611 GNRGLMGQKGEIGPPGQQGKKGAPGMPGLMGSNGSPGQPGTPGSKGSKGEPGIQGMP 667
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
 588-731 2.55e-07

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 54.69  E-value: 2.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273  588 EAGSPGAPGQdgtrGEPGIPGFPGnrGLMGQKGEIGPPGQQGKKGAPGMPGLMGSNGSPGQPG--------------TPG 653
Cdd:PRK14959 369 ESLRPSGGGA----SAPSGSAAEG--PASGGAATIPTPGTQGPQGTAPAAGMTPSSAAPATPApsaapsprvpwddaPPA 442

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273  654 SKGSKGEP-GIQGMPGASGLKGEPGATGS-PGEPGYMGLPGIQGKKGDKGNQGEKGI----QGQKGENGRQGIPGQQGiQ 727
Cdd:PRK14959 443 PPRSGIPPrPAPRMPEASPVPGAPDSVASaSDAPPTLGDPSDTAEHTPSGPRTWDGFlefcQGRNGQGGRLATVLRQA-T 521


                 ....
gi 18780273  728 GHHG 731
Cdd:PRK14959 522 PEHA 525
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 470-524 4.76e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 47.49  E-value: 4.76e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 18780273   470 GQPGQDGKPGYQGIAGTPGVPGSPGIQGARGLPGYKGEPGRDGDKGDRGLPGFPG 524
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 476-530 8.08e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 46.72  E-value: 8.08e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 18780273   476 GKPGYQGIAGTPGVPGSPGIQGARGLPGYKGEPGRDGDKGDRGLPGFPGLHGMPG 530
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 650-705 1.13e-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: 46.33  E-value: 1.13e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 18780273   650 GTPGSKGSKGEPGIQGMPGASGLKGEPGATGSPGEPGYMGLPGIQGKKGDKGNQGE 705
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 533-613 5.26e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 44.41  E-value: 5.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273   533 GEMGAKGDKGSPGFygkkgakgekgnagfPGLPGPAGEPgrhgkdglmGSPGFKGEAGSPGAPGQDGTRGEPGIPGFPGN 612
Cdd:pfam01391   1 GPPGPPGPPGPPGP---------------PGPPGPPGPP---------GPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56


                  .
gi 18780273   613 R 613
Cdd:pfam01391  57 P 57
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 476-752 1.15e-05

dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a skin-specific glycoprotein that may play a regulatory role in the crosstalk between barrier dysfunction and inflammation, and therefore play a role in inflammatory diseases such as psoriasis. Dermokine is one of the most highly expressed proteins in differentiating keratinocytes, found mainly in the spinous and granular layers of the epidermis, but also in the epithelia of the small intestine, macrophages of the lung, and endothelial cells of the lung. Mouse dermokine has been reported to be encoded by 22 exons, and its expression leads to alpha, beta, and gamma transcripts.


Pssm-ID: 411053 [Multi-domain]  Cd Length: 495  Bit Score: 49.23  E-value: 1.15e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273 476 GKPGYQGIAGTPGVPGSPGIQGARGLPGYKGEPGRDGDKGDRglPGFPGLHGMPGSKGEMGAKGDKGSPGFygkkgakge 555
Cdd:cd21118  70 GEEGGSTLGSRGDVFEHRLGEAARSLGNAGNEIGRQAEDIIR--HGVDAVHNSWQGSGGHGAYGSQGGPGV--------- 138

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273 556 KGNAGFPGLPGPAGEPGRHGKDGLMGSpgfKGEAGSPGAPGQD-GTRGEPGIPGFPGNRGLMGQKGEIGPPGQQGKKG-- 632
Cdd:cd21118 139 QGHGIPGGTGGPWASGGNYGTNSLGGS---VGQGGNGGPLNYGtNSQGAVAQPGYGTVRGNNQNSGCTNPPPSGSHESfs 215

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273 633 -----------------APGMPGLMGSNGSPGQPGTPGSKGSKGEPGIQGMPGASGLKGEP-GATGSPGEPGYMGLPGIQ 694
Cdd:cd21118 216 nsggssssgssgsqgshGSNGQGSSGSSGGQGNGGNNGSSSSNSGNSGGSNGGSSGNSGSGsGGSSSGGSNGWGGSSSSG 295

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 18780273 695 GKKGDKGNQGEKgiQGQKGENGRQgiPGQQGIQGHHGAKGERGEKGEPGVRGAIGSKG 752
Cdd:cd21118 296 GSGGSGGGNKPE--CNNPGNDVRM--AGGGGSQGSKESSGSHGSNGGNGQAEAVGGLN 349
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 506-572 1.24e-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: 43.64  E-value: 1.24e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18780273   506 GEPGRDGDKGDRGLPGFPGLHGMPGSKGEMGAKGDKGSPGfygkkgakgekgNAGFPGLPGPAGEPG 572
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPG------------PPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 683-738 1.89e-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: 1.89e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 18780273   683 GEPGYMGLPGIQGKKGDKGNQGEKGIQGQKGENGRQGIPGQQGIQGHHGAKGERGE 738
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 566-766 2.58e-05

dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a skin-specific glycoprotein that may play a regulatory role in the crosstalk between barrier dysfunction and inflammation, and therefore play a role in inflammatory diseases such as psoriasis. Dermokine is one of the most highly expressed proteins in differentiating keratinocytes, found mainly in the spinous and granular layers of the epidermis, but also in the epithelia of the small intestine, macrophages of the lung, and endothelial cells of the lung. Mouse dermokine has been reported to be encoded by 22 exons, and its expression leads to alpha, beta, and gamma transcripts.


Pssm-ID: 411053 [Multi-domain]  Cd Length: 495  Bit Score: 48.07  E-value: 2.58e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273 566 GPAGEPGRHGKDGLMGSPGFKGEaGSPGAPGQDGTRGepGIPGFPGNRGLMGQKGEIGPPGQ----QGKKGAPGMPGLMG 641
Cdd:cd21118 119 NSWQGSGGHGAYGSQGGPGVQGH-GIPGGTGGPWASG--GNYGTNSLGGSVGQGGNGGPLNYgtnsQGAVAQPGYGTVRG 195

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273 642 SNGSPGQPGTPGSkGSKGEPGIQGMPGASGLKGEPGATGSPGEpgymglpGIQGKKGDKGNQGEKGIQGQKGENGRQGIP 721
Cdd:cd21118 196 NNQNSGCTNPPPS-GSHESFSNSGGSSSSGSSGSQGSHGSNGQ-------GSSGSSGGQGNGGNNGSSSSNSGNSGGSNG 267

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 18780273 722 GQQGIQGHHGAKGERGEKGEPGVRGAIGSKGESGVDGLMGPAGPK 766
Cdd:cd21118 268 GSSGNSGSGSGGSSSGGSNGWGGSSSSGGSGGSGGGNKPECNNPG 312
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 713-766 3.68e-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: 42.10  E-value: 3.68e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 18780273   713 GENGRQGIPGQQGIQGHHGAKGERGEKGEPGVRGAIGSKGESGVDGLMGPAGPK 766
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAP 54
vWA_subfamily cd01464
VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 107-183 7.25e-05

VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. Members of this subgroup have no assigned function. This subfamily is typified by the presence of a conserved MIDAS motif.


Pssm-ID: 238741 [Multi-domain]  Cd Length: 176  Bit Score: 44.25  E-value: 7.25e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273 107 ILYLGGNTKTGKAIQFALDYLFAKSSRFLTK-------IAVVLTDGKSQDDVKDAAQA---ARDSKITLFAIGVGSETED 176
Cdd:cd01464  72 RLTASGGTSMGAALELALDCIDRRVQRYRADqkgdwrpWVFLLTDGEPTDDLTAAIERikeARDSKGRIVACAVGPKADL 151


                ....*..
gi 18780273 177 AELRAIA 183
Cdd:cd01464 152 DTLKQIT 158
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 452-686 2.90e-04

dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a skin-specific glycoprotein that may play a regulatory role in the crosstalk between barrier dysfunction and inflammation, and therefore play a role in inflammatory diseases such as psoriasis. Dermokine is one of the most highly expressed proteins in differentiating keratinocytes, found mainly in the spinous and granular layers of the epidermis, but also in the epithelia of the small intestine, macrophages of the lung, and endothelial cells of the lung. Mouse dermokine has been reported to be encoded by 22 exons, and its expression leads to alpha, beta, and gamma transcripts.


Pssm-ID: 411053 [Multi-domain]  Cd Length: 495  Bit Score: 44.61  E-value: 2.90e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273 452 GLQGPKGDPGLPGNPGYPGQPGQDGKPGYQGIAGTPGVPGSPG----------IQGARGLPGYKGEPGRDGDKGDRGLPG 521
Cdd:cd21118 128 GAYGSQGGPGVQGHGIPGGTGGPWASGGNYGTNSLGGSVGQGGnggplnygtnSQGAVAQPGYGTVRGNNQNSGCTNPPP 207

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273 522 fPGLHGMPGSKGEMGAKGDKGSPGFYGKKGakgekgnAGFPGLPGPAGEPGRHGKDGLMGSPGFKGEAGSPGAPGQDGTR 601
Cdd:cd21118 208 -SGSHESFSNSGGSSSSGSSGSQGSHGSNG-------QGSSGSSGGQGNGGNNGSSSSNSGNSGGSNGGSSGNSGSGSGG 279

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273 602 GEPGipgfpGNRGLMGQKGEIGPPGQQGKKG-APGMPGlmGSNGSPGQPGTPGSKGSKGEPGIQGMPGASGLKGEPGATG 680
Cdd:cd21118 280 SSSG-----GSNGWGGSSSSGGSGGSGGGNKpECNNPG--NDVRMAGGGGSQGSKESSGSHGSNGGNGQAEAVGGLNTLN 352


                ....*.
gi 18780273 681 SPGEPG 686
Cdd:cd21118 353 SDASTL 358
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 488-725 4.41e-04

dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a skin-specific glycoprotein that may play a regulatory role in the crosstalk between barrier dysfunction and inflammation, and therefore play a role in inflammatory diseases such as psoriasis. Dermokine is one of the most highly expressed proteins in differentiating keratinocytes, found mainly in the spinous and granular layers of the epidermis, but also in the epithelia of the small intestine, macrophages of the lung, and endothelial cells of the lung. Mouse dermokine has been reported to be encoded by 22 exons, and its expression leads to alpha, beta, and gamma transcripts.


Pssm-ID: 411053 [Multi-domain]  Cd Length: 495  Bit Score: 43.83  E-value: 4.41e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273 488 GVPGSpGIQGARGLPGYKGEPGRDGdKGDRGLPGfpGLHGMPGSKGEMGAKGDKGSPGFygkkgakgEKGNAGFPGLPGP 567
Cdd:cd21118 123 GSGGH-GAYGSQGGPGVQGHGIPGG-TGGPWASG--GNYGTNSLGGSVGQGGNGGPLNY--------GTNSQGAVAQPGY 190

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273 568 AGEPGRHGKDGLMGSPGFKGEAGS--PGAPGQDGTRGEPGIPGFPGnRGLMGQKGEIGPPGQQGKKGAPGMP------GL 639
Cdd:cd21118 191 GTVRGNNQNSGCTNPPPSGSHESFsnSGGSSSSGSSGSQGSHGSNG-QGSSGSSGGQGNGGNNGSSSSNSGNsggsngGS 269

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273 640 MGSNGSP-GQPGTPGSKGSKGEPGIQGMPGASGLKG-EPGATG-SPGEPGYMGLPGIQGKKGDKGNQGEKGIQGQKGENG 716
Cdd:cd21118 270 SGNSGSGsGGSSSGGSNGWGGSSSSGGSGGSGGGNKpECNNPGnDVRMAGGGGSQGSKESSGSHGSNGGNGQAEAVGGLN 349


                ....*....
gi 18780273 717 RQGIPGQQG 725
Cdd:cd21118 350 TLNSDASTL 358
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
 563-686 1.05e-03

PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];


Pssm-ID: 444064 [Multi-domain]  Cd Length: 548  Bit Score: 42.74  E-value: 1.05e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273 563 GLPGPAGEPGRHGKDGLMGSPGFKGEAGSPGAPgQDGTRGEPGIPGFPGNRGLMGQKGEIGPPGQQGKKGAPGMPGLMGS 642
Cdd:COG5180 340 GVPEAASDAGQPPSAYPPAEEAVPGKPLEQGAP-RPGSSGGDGAPFQPPNGAPQPGLGRRGAPGPPMGAGDLVQAALDGG 418

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 18780273 643 NGSPGQPGTPGSKGSKGEPGIQGMPGASGLKGEPGATGSPGEPG 686
Cdd:COG5180 419 GRETASLGGAAGGAGQGPKADFVPGDAESVSGPAGLADQAGAAA 462
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 37-173 1.17e-03

VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses. In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. Members of this subgroup are bacterial in origin. They are typified by the presence of a MIDAS motif.


Pssm-ID: 238744 [Multi-domain]  Cd Length: 180  Bit Score: 40.78  E-value: 1.17e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273  37 DLVFILDGSYSVGPENFeiVKKWLVNITKnfDIGPKFI------QVGVVQYSDYPVLEIPL-GSYDSGEHLTAAVEsILY 109
Cdd:cd01467   4 DIMIALDVSGSMLAQDF--VKPSRLEAAK--EVLSDFIdrrendRIGLVVFAGAAFTQAPLtLDRESLKELLEDIK-IGL 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18780273 110 LGGNTKTGKAIQFALDYLfaKSSRFLTKIAVVLTDGKSQDDVKDAAQAARDSK---ITLFAIGVGSE 173
Cdd:cd01467  79 AGQGTAIGDAIGLAIKRL--KNSEAKERVIVLLTDGENNAGEIDPATAAELAKnkgVRIYTIGVGKS 143
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 497-545 5.14e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 35.93  E-value: 5.14e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 18780273   497 GARGLPGYKGEPGRDGDKGDRGLPGFPGLHGMPGSKGEMGAKGDKGSPG 545
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPG 49
Glutenin_hmw pfam03157
High molecular weight glutenin subunit; Members of this family include high molecular weight ...
 618-753 6.43e-03

High molecular weight glutenin subunit; Members of this family include high molecular weight subunits of glutenin. This group of gluten proteins is thought to be largely responsible for the elastic properties of gluten, and hence, doughs. Indeed, glutenin high molecular weight subunits are classified as elastomeric proteins, because the glutenin network can withstand significant deformations without breaking, and return to the original conformation when the stress is removed. Elastomeric proteins differ considerably in amino acid sequence, but they are all polymers whose subunits consist of elastomeric domains, composed of repeated motifs, and non-elastic domains that mediate cross-linking between the subunits. The elastomeric domain motifs are all rich in glycine residues in addition to other hydrophobic residues. High molecular weight glutenin subunits have an extensive central elastomeric domain, flanked by two terminal non-elastic domains that form disulphide cross-links. The central elastomeric domain is characterized by the following three repeated motifs: PGQGQQ, GYYPTS[P/L]QQ, GQQ. It possesses overlapping beta-turns within and between the repeated motifs, and assumes a regular helical secondary structure with a diameter of approx. 1.9 nm and a pitch of approx. 1.5 nm.


Pssm-ID: 367362 [Multi-domain]  Cd Length: 786  Bit Score: 40.32  E-value: 6.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18780273   618 QKGEIGPPGQQGKKGAPGMPGLMGSNGSPGQ------PGTPGSKGSKGEPGIQGMPGasglKGEPGATGSPGEPGYMGLP 691
Cdd:pfam03157 130 RPGQGQQPGQGQQWYYPTSPQQPGQWQQPGQgqqgyyPTSPQQSGQRQQPGQGQQLR----QGQQGQQSGQGQPGYYPTS 205

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18780273   692 GIQGKKGDKGNQGEKGIQGQKGENGRQGIPGQQGIQGHHGAKGERGEKGEPGVRGAIGSKGE 753
Cdd:pfam03157 206 SQQPGQLQQTGQGQQGQQPERGQQGQQPGQGQQPGQGQQGQQPGQPQQLGQGQQGYYPISPQ 267
 
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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