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Conserved domains on  [gi|578811997|ref|XP_006715286|]
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collagen alpha-1(XXI) chain isoform X2 [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 1.67e-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: 1.67e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997  34 APTDLVFILDGSYSVGPENFEIVKKWLVNITKNFDIGPKFIQVGVVQYSDYPVLEIPLGSYDSGEHLTAAVESILYLGGN 113
Cdd:cd01475    1 GPTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 114 TKTGKAIQFALDYLFA------KSSRFLTKIAVVLTDGKSQDDVKDAAQAARDSKITLFAIGVGSETEDaELRAIANKPS 187
Cdd:cd01475   81 TMTGLAIQYAMNNAFSeaegarPGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEE-ELREIASEPL 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578811997 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 ...
 447-677 6.46e-40

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: 153.91  E-value: 6.46e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 447 PPGKPGLQGPKGDPGLPGNPGYPGQPGQDGKPGYQGIAGTPGVPGSPGIQGARGLPGYKGEPGRDGDKGDRGLpgfPGLH 526
Cdd:NF038329 127 PAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGE---TGPA 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 527 GMPGSKGEMGAKGDKGSpgfygkkgakgekgnAGFPGLPGPAGEpGRHGKDGLMGSPGFKGEAGSPGAPGQDGTRGEPGI 606
Cdd:NF038329 204 GEQGPAGPAGPDGEAGP---------------AGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGE 267

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578811997 607 PGFPGNRGLMGQKGEIGPPGQQGKKGAPGMPGLMGSNGSPGQPGTPGSKGSKGEPGIQGMPGASGLKGEPG 677
Cdd:NF038329 268 AGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 574-921 1.63e-27

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


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 116.93  E-value: 1.63e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 574 HGKDGLMGSPGFKGEAGSPGAPGQDGTRGEPGIPGFPGNRGLMGQKGEIGPPGQQGKKGAPGMPGLMGSNGSPGQPGTPG 653
Cdd:NF038329 113 LKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKG 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 654 SKGSKGEPGIQGMPGASGLKGEPGATGSPGEPGYMGLPGiqgkkgqKGENGRQGIPGQQGIQGhhgAKGERGEKGEPGVR 733
Cdd:NF038329 193 PQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-------DGQQGPDGDPGPTGEDG---PQGPDGPAGKDGPR 262

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 734 GAIGSKGESGVDGLMGPAGPkgqpgdpgpqgppgldgkpgrefseqfirqvctdviraqlpvllqsgrirncdhclsqhg 813
Cdd:NF038329 263 GDRGEAGPDGPDGKDGERGP------------------------------------------------------------ 282

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 814 spgipgppgpigpegprglPGLPGRDGVPGLVGVPGRPGVRG---LKGLPGRNGEKGSQGfgypgeqgppgppgpegppg 890
Cdd:NF038329 283 -------------------VGPAGKDGQNGKDGLPGKDGKDGqngKDGLPGKDGKDGQPG-------------------- 323

                        330       340       350
                 ....*....|....*....|....*....|.
gi 578811997 891 iskegppgdpglpgKDGDHGKPGIQGQPGPP 921
Cdd:NF038329 324 --------------KDGLPGKDGKDGQPGKP 340
LamG super family cl22861
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 230-412 9.63e-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: 9.63e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997   230 GFDILLGLD---VNKKVKKRIQLSPKKiKGYEVTSKVDLSELTSNVFPEGLPPSYVFVSTQRFKVKKIWDLWRILTIDGR 306
Cdd:smart00210   1 GQDLLQVFDlpsLSFAIRQVVGPEPGS-PAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPKSRGVLFAIYDAQNV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997   307 PQIAVTLNGVDKILLFTTTSVINGSQVVTFANPQvktLFDEGWHQIRLLVTEQDVTLYIDDQQIENKPLHPVLG--ILIN 384
Cdd:smart00210  80 RQFGLEVDGRANTLLLRYQGVDGKQHTVSFRNLP---LADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGQppIDTD 156

                          170       180
                   ....*....|....*....|....*...
gi 578811997   385 GQTQIGKYSGKEETVQFDVQKLRIYCDP 412
Cdd:smart00210 157 GIEVRGAQAADRKPFQGDLQQLKIVCDP 184
 
Name Accession Description Interval E-value
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 34-254 1.67e-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: 1.67e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997  34 APTDLVFILDGSYSVGPENFEIVKKWLVNITKNFDIGPKFIQVGVVQYSDYPVLEIPLGSYDSGEHLTAAVESILYLGGN 113
Cdd:cd01475    1 GPTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 114 TKTGKAIQFALDYLFA------KSSRFLTKIAVVLTDGKSQDDVKDAAQAARDSKITLFAIGVGSETEDaELRAIANKPS 187
Cdd:cd01475   81 TMTGLAIQYAMNNAFSeaegarPGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEE-ELREIASEPL 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578811997 188 STYVFYVEDYIAISKIREVMKQKLCE-ESVCPTripvAARDERGFDILLGLDVNKKVKKRIQLSPKKI 254
Cdd:cd01475  160 ADHVFYVEDFSTIEELTKKFQGKICVvPDLCAT----LSHVCQQVCISTPGSYLCACTEGYALLEDNK 223
VWA pfam00092
von Willebrand factor type A domain;
37-205 1.65e-54

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 186.71  E-value: 1.65e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997   37 DLVFILDGSYSVGPENFEIVKKWLVNITKNFDIGPKFIQVGVVQYSDYPVLEIPLGSYDSGEHLTAAVESILYLGGNTK- 115
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTn 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997  116 TGKAIQFALDYLFAKSSRF---LTKIAVVLTDGKSQD-DVKDAAQAARDSKITLFAIGVGSETeDAELRAIANKPSSTYV 191
Cdd:pfam00092  81 TGKALKYALENLFSSAAGArpgAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNAD-DEELRKIASEPGEGHV 159

                         170
                  ....*....|....
gi 578811997  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 5.14e-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: 5.14e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997    37 DLVFILDGSYSVGPENFEIVKKWLVNITKNFDIGPKFIQVGVVQYSDYPVLEIPLGSYDSGEHLTAAVESILY-LGGNTK 115
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYkLGGGTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997   116 TGKAIQFALDYLFAK---SSRFLTKIAVVLTDGKSQD---DVKDAAQAARDSKITLFAIGVGSETEDAELRAIANKPSST 189
Cdd:smart00327  81 LGAALQYALENLFSKsagSRRGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDVDEEELKKLASAPGGV 160

                          170
                   ....*....|....
gi 578811997   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 ...
 447-677 6.46e-40

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: 153.91  E-value: 6.46e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 447 PPGKPGLQGPKGDPGLPGNPGYPGQPGQDGKPGYQGIAGTPGVPGSPGIQGARGLPGYKGEPGRDGDKGDRGLpgfPGLH 526
Cdd:NF038329 127 PAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGE---TGPA 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 527 GMPGSKGEMGAKGDKGSpgfygkkgakgekgnAGFPGLPGPAGEpGRHGKDGLMGSPGFKGEAGSPGAPGQDGTRGEPGI 606
Cdd:NF038329 204 GEQGPAGPAGPDGEAGP---------------AGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGE 267

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578811997 607 PGFPGNRGLMGQKGEIGPPGQQGKKGAPGMPGLMGSNGSPGQPGTPGSKGSKGEPGIQGMPGASGLKGEPG 677
Cdd:NF038329 268 AGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 511-760 6.94e-36

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: 141.97  E-value: 6.94e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 511 DGDKGDRGLPGFPGLHGMPGSKGEMGAKGDkgspgfygkkgakgekgnagfpglPGPAGEPGRHGKDGLMGSPGFKGEAG 590
Cdd:NF038329 116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGP------------------------AGPAGPPGPQGERGEKGPAGPQGEAG 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 591 SPGAPGQDGTRGEPGIPGFPGNRGLMGQKGEIGPPGQQGKKGAPGMPGLMGSNGSPGQPGtPGSKGSKGEPGIQGMPGAS 670
Cdd:NF038329 172 PQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQ 250

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 671 GLKGEPGATGSPGEPGYMGLPGIQGKKGQKGENGRQGIPGQQGIQGHHGAKGERGEKGEPGVRGAIGSKGESGVDGLMGP 750
Cdd:NF038329 251 GPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGK 330

                        250
                 ....*....|
gi 578811997 751 AGPKGQPGDP 760
Cdd:NF038329 331 DGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 574-921 1.63e-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: 1.63e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 574 HGKDGLMGSPGFKGEAGSPGAPGQDGTRGEPGIPGFPGNRGLMGQKGEIGPPGQQGKKGAPGMPGLMGSNGSPGQPGTPG 653
Cdd:NF038329 113 LKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKG 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 654 SKGSKGEPGIQGMPGASGLKGEPGATGSPGEPGYMGLPGiqgkkgqKGENGRQGIPGQQGIQGhhgAKGERGEKGEPGVR 733
Cdd:NF038329 193 PQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-------DGQQGPDGDPGPTGEDG---PQGPDGPAGKDGPR 262

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 734 GAIGSKGESGVDGLMGPAGPkgqpgdpgpqgppgldgkpgrefseqfirqvctdviraqlpvllqsgrirncdhclsqhg 813
Cdd:NF038329 263 GDRGEAGPDGPDGKDGERGP------------------------------------------------------------ 282

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 814 spgipgppgpigpegprglPGLPGRDGVPGLVGVPGRPGVRG---LKGLPGRNGEKGSQGfgypgeqgppgppgpegppg 890
Cdd:NF038329 283 -------------------VGPAGKDGQNGKDGLPGKDGKDGqngKDGLPGKDGKDGQPG-------------------- 323

                        330       340       350
                 ....*....|....*....|....*....|.
gi 578811997 891 iskegppgdpglpgKDGDHGKPGIQGQPGPP 921
Cdd:NF038329 324 --------------KDGLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 598-922 6.82e-25

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: 108.84  E-value: 6.82e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 598 DGTRGEPGIPGFPGNRGLMGQKG---EIGPPGQQGKKGAPGMPGLMGSNGSPGQPGTPGSKGSKGEPGIQGMPGASGLKG 674
Cdd:NF038329 116 DGEKGEPGPAGPAGPAGEQGPRGdrgETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 675 EPGATGSPGEPGYMGLPGIQGKKGQKGENGRQGIPGQqGIQGHHGAKGERGEKGEPGVRGAIGSKGESGVDGLMGPAGPK 754
Cdd:NF038329 196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPD 274

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 755 gqpgdpgpqgppgldgkpgrefseqfirqvctdviraqlpvllqsgrirncdhclsqhgspgipgppgpigpegprglpg 834
Cdd:NF038329     --------------------------------------------------------------------------------

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 835 lpGRDGVPGLVGVPGRPGVRGLKGLPGRNGEKGSQGfgypgeqgppgppgpegppgiskegppgDPGLPGKDGDHGKPGI 914
Cdd:NF038329 275 --GKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNG----------------------------KDGLPGKDGKDGQPGK 324


                 ....*...
gi 578811997 915 QGQPGPPG 922
Cdd:NF038329 325 DGLPGKDG 332
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 447-607 1.23e-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: 104.99  E-value: 1.23e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 447 PPGKPGLQGPKGDPGLPGNPGYPGQPGQDGKPGYQGIAGTPGVPGSPGIQGARGLPGY-----KGEPGRDGDKGDRGLPG 521
Cdd:NF038329 175 PAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgqqgpDGDPGPTGEDGPQGPDG 254

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 522 FPGLHGMPGSKGEMGAKGDKGSPGFYGKKGAKGEKGNAGFPGLPGPAGEPGRHGKDGLMGSPGFKGEAGSPGAPGQDGTR 601
Cdd:NF038329 255 PAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKD 334


                 ....*.
gi 578811997 602 GEPGIP 607
Cdd:NF038329 335 GQPGKP 340
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 230-412 9.63e-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: 9.63e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997   230 GFDILLGLD---VNKKVKKRIQLSPKKiKGYEVTSKVDLSELTSNVFPEGLPPSYVFVSTQRFKVKKIWDLWRILTIDGR 306
Cdd:smart00210   1 GQDLLQVFDlpsLSFAIRQVVGPEPGS-PAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPKSRGVLFAIYDAQNV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997   307 PQIAVTLNGVDKILLFTTTSVINGSQVVTFANPQvktLFDEGWHQIRLLVTEQDVTLYIDDQQIENKPLHPVLG--ILIN 384
Cdd:smart00210  80 RQFGLEVDGRANTLLLRYQGVDGKQHTVSFRNLP---LADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGQppIDTD 156

                          170       180
                   ....*....|....*....|....*...
gi 578811997   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 3.65e-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: 3.65e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997  32 RTAPTDLVFILDGSYSVGPEN-FEIVKKWLVNITKNFdigPKFIQVGVVQYSDYPVLEIPLGSydSGEHLTAAVESiLYL 110
Cdd:COG1240   89 PQRGRDVVLVVDASGSMAAENrLEAAKGALLDFLDDY---RPRDRVGLVAFGGEAEVLLPLTR--DREALKRALDE-LPP 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 111 GGNTKTGKAIQFALDyLFAKSSRFLTKIAVVLTDGK---SQDDVKDAAQAARDSKITLFAIGVGSETED-AELRAIANKP 186
Cdd:COG1240  163 GGGTPLGDALALALE-LLKRADPARRKVIVLLTDGRdnaGRIDPLEAAELAAAAGIRIYTIGVGTEAVDeGLLREIAEAT 241

                        170       180
                 ....*....|....*....|...
gi 578811997 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 8.56e-10

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: 55.19  E-value: 8.56e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578811997  452 GLQGPKGDPGLPGNPGYPGQPGQDGKPGYQGIAGTPGVPGSPGIQGARGLPGYKGEP 508
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 656-711 9.24e-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: 9.24e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 578811997  656 GSKGEPGIQGMPGASGLKGEPGATGSPGEPGYMGLPGIQGKKGQKGENGRQGIPGQ 711
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 668-922 2.93e-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: 54.14  E-value: 2.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 668 GASGLKGEpgatGSPGEPGYMGLPGIQGKKGQKGENGRQGIPGQQGIQGHHGAKGERGEKGEPGVRGAIGSKGESGVDGL 747
Cdd:NF038329 109 GLQQLKGD----GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGA 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 748 MGPAGPKgqpgdpgpqgppgldgkpgrefseqfirqvctdviraqlpvllqsgrirncdhclsqhgspgipgppgpiGPE 827
Cdd:NF038329 185 KGPAGEK----------------------------------------------------------------------GPQ 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 828 GPRGLPGLPGRDGVPGLVGVPGRPGVRGLKGLPGR-----NGEKGSQGfgypgeqGPPGPPGPEGPPGISKEGPPGDPGL 902
Cdd:NF038329 195 GPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPagdgqQGPDGDPG-------PTGEDGPQGPDGPAGKDGPRGDRGE 267

                        250       260
                 ....*....|....*....|
gi 578811997 903 PGKDGDHGKPGIQGQPGPPG 922
Cdd:NF038329 268 AGPDGPDGKDGERGPVGPAG 287
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 476-740 3.86e-06

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: 50.38  E-value: 3.86e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 476 GKPGYQGIAGTPGVPGSPGIQGARGLPGYKGEPGRDGDKGDRglPGFPGLHGMPGSKGEMGAKGDKGSPGFygkkgakge 555
Cdd:cd21118   70 GEEGGSTLGSRGDVFEHRLGEAARSLGNAGNEIGRQAEDIIR--HGVDAVHNSWQGSGGHGAYGSQGGPGV--------- 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 556 KGNAGFPGLPGPAGEPGRHGKDGLMGSpgfKGEAGSPGAPGQD-GTRGEPGIPGFPGNRGLMGQKGEIGPPGQQGKKG-- 632
Cdd:cd21118  139 QGHGIPGGTGGPWASGGNYGTNSLGGS---VGQGGNGGPLNYGtNSQGAVAQPGYGTVRGNNQNSGCTNPPPSGSHESfs 215

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 633 -----------------APGMPGLMGSNGSPGQPGTPGSKGSKGEPGIQGMPGASGLKGEP-GATGSPGEPGYMGLPGIQ 694
Cdd:cd21118  216 nsggssssgssgsqgshGSNGQGSSGSSGGQGNGGNNGSSSSNSGNSGGSNGGSSGNSGSGsGGSSSGGSNGWGGSSSSG 295

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 578811997 695 GKKGQKGENGRQ--------GIPGQQGIQGHHGAKGERGEKGEPGVRGAIGSKG 740
Cdd:cd21118  296 GSGGSGGGNKPEcnnpgndvRMAGGGGSQGSKESSGSHGSNGGNGQAEAVGGLN 349
PHA03169 PHA03169
hypothetical protein; Provisional
 570-753 1.42e-05

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 48.43  E-value: 1.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 570 EPGRHGKDGLMGSpgfkgeaGSPGAPGQDGTRGEPGIPGFPGNRGLMG----QKGEIGPPGQQGKKGAPGMPGlmgsNGS 645
Cdd:PHA03169  77 EESRHGEKEERGQ-------GGPSGSGSESVGSPTPSPSGSAEELASGlspeNTSGSSPESPASHSPPPSPPS----HPG 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 646 PGQPGTPGSKGSKGEPGiqgmpGASGLKGEPGATGSPGEPGyMGLPGIQGKKGQKGENGRQGIPGQQGIQghhgakgERG 725
Cdd:PHA03169 146 PHEPAPPESHNPSPNQQ-----PSSFLQPSHEDSPEEPEPP-TSEPEPDSPGPPQSETPTSSPPPQSPPD-------EPG 212

                        170       180
                 ....*....|....*....|....*...
gi 578811997 726 EKGEPGVRGAIGSKGESGVDGLMGPAGP 753
Cdd:PHA03169 213 EPQSPTPQQAPSPNTQQAVEHEDEPTEP 240
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 447-514 1.45e-04

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: 45.28  E-value: 1.45e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578811997 447 PPGKPGLQGPKGDPGLPGNPG------YPGQPGQDGKPGYQGIAGTPGVPGSPGIQGARGLPGYKGEPGRDGDK 514
Cdd:NF038329 270 PDGPDGKDGERGPVGPAGKDGqngkdgLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
 563-686 1.11e-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: 1.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 563 GLPGPAGEPGRHGKDGLMGSPGFKGEAGSPGAPgQDGTRGEPGIPGFPGNRGLMGQKGEIGPPGQQGKKGAPGMPGLMGS 642
Cdd:COG5180  340 GVPEAASDAGQPPSAYPPAEEAVPGKPLEQGAP-RPGSSGGDGAPFQPPNGAPQPGLGRRGAPGPPMGAGDLVQAALDGG 418

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 578811997 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 1.67e-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: 1.67e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997  34 APTDLVFILDGSYSVGPENFEIVKKWLVNITKNFDIGPKFIQVGVVQYSDYPVLEIPLGSYDSGEHLTAAVESILYLGGN 113
Cdd:cd01475    1 GPTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 114 TKTGKAIQFALDYLFA------KSSRFLTKIAVVLTDGKSQDDVKDAAQAARDSKITLFAIGVGSETEDaELRAIANKPS 187
Cdd:cd01475   81 TMTGLAIQYAMNNAFSeaegarPGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEE-ELREIASEPL 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578811997 188 STYVFYVEDYIAISKIREVMKQKLCE-ESVCPTripvAARDERGFDILLGLDVNKKVKKRIQLSPKKI 254
Cdd:cd01475  160 ADHVFYVEDFSTIEELTKKFQGKICVvPDLCAT----LSHVCQQVCISTPGSYLCACTEGYALLEDNK 223
VWA pfam00092
von Willebrand factor type A domain;
37-205 1.65e-54

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 186.71  E-value: 1.65e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997   37 DLVFILDGSYSVGPENFEIVKKWLVNITKNFDIGPKFIQVGVVQYSDYPVLEIPLGSYDSGEHLTAAVESILYLGGNTK- 115
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTn 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997  116 TGKAIQFALDYLFAKSSRF---LTKIAVVLTDGKSQD-DVKDAAQAARDSKITLFAIGVGSETeDAELRAIANKPSSTYV 191
Cdd:pfam00092  81 TGKALKYALENLFSSAAGArpgAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNAD-DEELRKIASEPGEGHV 159

                         170
                  ....*....|....
gi 578811997  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 1.76e-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: 1.76e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997  36 TDLVFILDGSYSVGPENFEIVKKWLVNITKNFDIGPKFIQVGVVQYSDYPVLEIPLGSYDSGEHLTAAVESILYLGGN-T 114
Cdd:cd01450    1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGgT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 115 KTGKAIQFALDYLFAKSSRFL--TKIAVVLTDGKSQD--DVKDAAQAARDSKITLFAIGVGSETEDaELRAIANKPSSTY 190
Cdd:cd01450   81 NTGKALQYALEQLFSESNAREnvPKVIIVLTDGRSDDggDPKEAAAKLKDEGIKVFVVGVGPADEE-ELREIASCPSERH 159


                 ..
gi 578811997 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 2.18e-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: 2.18e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997  36 TDLVFILDGSYSVGPENFEIVKKWLVNITKNFDIGPKFIQVGVVQYSDYPVLEIPLGSYDSGEHLTAAVESILYLGGNTK 115
Cdd:cd01482    1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 116 TGKAIQFALDYLFAKSSRF---LTKIAVVLTDGKSQDDVKDAAQAARDSKITLFAIGVGSETEdAELRAIANKPSSTYVF 192
Cdd:cd01482   81 TGKALTHVREKNFTPDAGArpgVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADE-SELKMIASKPSETHVF 159


                 ....*
gi 578811997 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 2.69e-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: 2.69e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997  36 TDLVFILDGSYSVGPENFEIVKKWLVNITKNFDIGPKFIQVGVVQYSDYPVLEIPLGSYDSGEHLTAAVESILYLGGNTK 115
Cdd:cd01472    1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 116 TGKAIQFALDYLFAKSSRFLT---KIAVVLTDGKSQDDVKDAAQAARDSKITLFAIGVGSETEDaELRAIANKPSSTYVF 192
Cdd:cd01472   81 TGKALKYVRENLFTEASGSREgvpKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEE-ELKQIASDPKELYVF 159


                 ....
gi 578811997 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 5.14e-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: 5.14e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997    37 DLVFILDGSYSVGPENFEIVKKWLVNITKNFDIGPKFIQVGVVQYSDYPVLEIPLGSYDSGEHLTAAVESILY-LGGNTK 115
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYkLGGGTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997   116 TGKAIQFALDYLFAK---SSRFLTKIAVVLTDGKSQD---DVKDAAQAARDSKITLFAIGVGSETEDAELRAIANKPSST 189
Cdd:smart00327  81 LGAALQYALENLFSKsagSRRGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDVDEEELKKLASAPGGV 160

                          170
                   ....*....|....
gi 578811997   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 8.86e-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: 8.86e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997  36 TDLVFILDGSYSVGPENFEIVKKWLVNITKNFDIGPKFIQVGVVQYSDYPVLEIPLGSYDSGEHLTAAVESILYLGGNTK 115
Cdd:cd01469    1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 116 TGKAIQFALDYLFAKSS---RFLTKIAVVLTDGKSQDD--VKDAAQAARDSKITLFAIGVG----SETEDAELRAIANKP 186
Cdd:cd01469   81 TATAIQYVVTELFSESNgarKDATKVLVVITDGESHDDplLKDVIPQAEREGIIRYAIGVGghfqRENSREELKTIASKP 160

                        170
                 ....*....|....*..
gi 578811997 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 ...
 447-677 6.46e-40

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: 153.91  E-value: 6.46e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 447 PPGKPGLQGPKGDPGLPGNPGYPGQPGQDGKPGYQGIAGTPGVPGSPGIQGARGLPGYKGEPGRDGDKGDRGLpgfPGLH 526
Cdd:NF038329 127 PAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGE---TGPA 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 527 GMPGSKGEMGAKGDKGSpgfygkkgakgekgnAGFPGLPGPAGEpGRHGKDGLMGSPGFKGEAGSPGAPGQDGTRGEPGI 606
Cdd:NF038329 204 GEQGPAGPAGPDGEAGP---------------AGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGE 267

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578811997 607 PGFPGNRGLMGQKGEIGPPGQQGKKGAPGMPGLMGSNGSPGQPGTPGSKGSKGEPGIQGMPGASGLKGEPG 677
Cdd:NF038329 268 AGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 511-760 6.94e-36

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: 141.97  E-value: 6.94e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 511 DGDKGDRGLPGFPGLHGMPGSKGEMGAKGDkgspgfygkkgakgekgnagfpglPGPAGEPGRHGKDGLMGSPGFKGEAG 590
Cdd:NF038329 116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGP------------------------AGPAGPPGPQGERGEKGPAGPQGEAG 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 591 SPGAPGQDGTRGEPGIPGFPGNRGLMGQKGEIGPPGQQGKKGAPGMPGLMGSNGSPGQPGtPGSKGSKGEPGIQGMPGAS 670
Cdd:NF038329 172 PQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQ 250

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 671 GLKGEPGATGSPGEPGYMGLPGIQGKKGQKGENGRQGIPGQQGIQGHHGAKGERGEKGEPGVRGAIGSKGESGVDGLMGP 750
Cdd:NF038329 251 GPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGK 330

                        250
                 ....*....|
gi 578811997 751 AGPKGQPGDP 760
Cdd:NF038329 331 DGKDGQPGKP 340
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 37-192 5.80e-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: 5.80e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997  37 DLVFILDGSYSVGPENFEIVKKWLVNITKNFDIGPKFIQVGVVQYSDYPVLEIPLGSYDSGEHLTAAVESILY-LGGNTK 115
Cdd:cd00198    2 DIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKgLGGGTN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 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 1.04e-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: 1.04e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997  37 DLVFILDGSYSVGPENFEIVKKWLVNITKNFDIGPKFIQVGVVQYSDYPVLEIPLGSYDSGEHLTAAVESILYLGGN-TK 115
Cdd:cd01481    2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSqLN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 116 TGKAIQFALDYLFAKS--SRF---LTKIAVVLTDGKSQDDVKDAAQAARDSKITLFAIGVGSeTEDAELRAIANKPSstY 190
Cdd:cd01481   82 TGSALDYVVKNLFTKSagSRIeegVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARN-ADLAELQQIAFDPS--F 158


                 ....*..
gi 578811997 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 ...
 574-921 1.63e-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: 1.63e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 574 HGKDGLMGSPGFKGEAGSPGAPGQDGTRGEPGIPGFPGNRGLMGQKGEIGPPGQQGKKGAPGMPGLMGSNGSPGQPGTPG 653
Cdd:NF038329 113 LKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKG 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 654 SKGSKGEPGIQGMPGASGLKGEPGATGSPGEPGYMGLPGiqgkkgqKGENGRQGIPGQQGIQGhhgAKGERGEKGEPGVR 733
Cdd:NF038329 193 PQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-------DGQQGPDGDPGPTGEDG---PQGPDGPAGKDGPR 262

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 734 GAIGSKGESGVDGLMGPAGPkgqpgdpgpqgppgldgkpgrefseqfirqvctdviraqlpvllqsgrirncdhclsqhg 813
Cdd:NF038329 263 GDRGEAGPDGPDGKDGERGP------------------------------------------------------------ 282

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 814 spgipgppgpigpegprglPGLPGRDGVPGLVGVPGRPGVRG---LKGLPGRNGEKGSQGfgypgeqgppgppgpegppg 890
Cdd:NF038329 283 -------------------VGPAGKDGQNGKDGLPGKDGKDGqngKDGLPGKDGKDGQPG-------------------- 323

                        330       340       350
                 ....*....|....*....|....*....|.
gi 578811997 891 iskegppgdpglpgKDGDHGKPGIQGQPGPP 921
Cdd:NF038329 324 --------------KDGLPGKDGKDGQPGKP 340
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 37-190 7.86e-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: 7.86e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997  37 DLVFILDGSYSVGPEnFEIVKKWLVNITKNFDIGPKFIQVGVVQYSDYP--VLEIPLGSYDSGEHLTAAVESILYLGGNT 114
Cdd:cd01476    2 DLLFVLDSSGSVRGK-FEKYKKYIERIVEGLEIGPTATRVALITYSGRGrqRVRFNLPKHNDGEELLEKVDNLRFIGGTT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 115 KTGKAIQFALDYLFAKSSRF--LTKIAVVLTDGKSQDDVKDAAQAARDSK-ITLFAIGVG--SETEDAELRAIANKPSST 189
Cdd:cd01476   81 ATGAAIEVALQQLDPSEGRRegIPKVVVVLTDGRSHDDPEKQARILRAVPnIETFAVGTGdpGTVDTEELHSITGNEDHI 160


                 .
gi 578811997 190 Y 190
Cdd:cd01476  161 F 161
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 598-922 6.82e-25

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: 108.84  E-value: 6.82e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 598 DGTRGEPGIPGFPGNRGLMGQKG---EIGPPGQQGKKGAPGMPGLMGSNGSPGQPGTPGSKGSKGEPGIQGMPGASGLKG 674
Cdd:NF038329 116 DGEKGEPGPAGPAGPAGEQGPRGdrgETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 675 EPGATGSPGEPGYMGLPGIQGKKGQKGENGRQGIPGQqGIQGHHGAKGERGEKGEPGVRGAIGSKGESGVDGLMGPAGPK 754
Cdd:NF038329 196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPD 274

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 755 gqpgdpgpqgppgldgkpgrefseqfirqvctdviraqlpvllqsgrirncdhclsqhgspgipgppgpigpegprglpg 834
Cdd:NF038329     --------------------------------------------------------------------------------

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 835 lpGRDGVPGLVGVPGRPGVRGLKGLPGRNGEKGSQGfgypgeqgppgppgpegppgiskegppgDPGLPGKDGDHGKPGI 914
Cdd:NF038329 275 --GKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNG----------------------------KDGLPGKDGKDGQPGK 324


                 ....*...
gi 578811997 915 QGQPGPPG 922
Cdd:NF038329 325 DGLPGKDG 332
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 35-189 8.45e-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: 8.45e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997  35 PTDLVFILDGSYSVGPENFEIVKKWLVNITKNF------DIGPKFIQVGVVQYSDYPVLE-IPLGSYDSGEHLTAAVESI 107
Cdd:cd01480    2 PVDITFVLDSSESVGLQNFDITKNFVKRVAERFlkdyyrKDPAGSWRVGVVQYSDQQEVEaGFLRDIRNYTSLKEAVDNL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 108 LYLGGNTKTGKAIQFALDYLFAKSSRFLTKIAVVLTDGKSQ----DDVKDAAQAARDSKITLFAIGVGSETEDaELRAIA 183
Cdd:cd01480   82 EYIGGGTFTDCALKYATEQLLEGSHQKENKFLLVITDGHSDgspdGGIEKAVNEADHLGIKIFFVAVGSQNEE-PLSRIA 160


                 ....*.
gi 578811997 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 ...
 447-607 1.23e-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: 104.99  E-value: 1.23e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 447 PPGKPGLQGPKGDPGLPGNPGYPGQPGQDGKPGYQGIAGTPGVPGSPGIQGARGLPGY-----KGEPGRDGDKGDRGLPG 521
Cdd:NF038329 175 PAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgqqgpDGDPGPTGEDGPQGPDG 254

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 522 FPGLHGMPGSKGEMGAKGDKGSPGFYGKKGAKGEKGNAGFPGLPGPAGEPGRHGKDGLMGSPGFKGEAGSPGAPGQDGTR 601
Cdd:NF038329 255 PAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKD 334


                 ....*.
gi 578811997 602 GEPGIP 607
Cdd:NF038329 335 GQPGKP 340
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 230-412 9.63e-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: 9.63e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997   230 GFDILLGLD---VNKKVKKRIQLSPKKiKGYEVTSKVDLSELTSNVFPEGLPPSYVFVSTQRFKVKKIWDLWRILTIDGR 306
Cdd:smart00210   1 GQDLLQVFDlpsLSFAIRQVVGPEPGS-PAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPKSRGVLFAIYDAQNV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997   307 PQIAVTLNGVDKILLFTTTSVINGSQVVTFANPQvktLFDEGWHQIRLLVTEQDVTLYIDDQQIENKPLHPVLG--ILIN 384
Cdd:smart00210  80 RQFGLEVDGRANTLLLRYQGVDGKQHTVSFRNLP---LADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGQppIDTD 156

                          170       180
                   ....*....|....*....|....*...
gi 578811997   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 3.65e-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: 3.65e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997  32 RTAPTDLVFILDGSYSVGPEN-FEIVKKWLVNITKNFdigPKFIQVGVVQYSDYPVLEIPLGSydSGEHLTAAVESiLYL 110
Cdd:COG1240   89 PQRGRDVVLVVDASGSMAAENrLEAAKGALLDFLDDY---RPRDRVGLVAFGGEAEVLLPLTR--DREALKRALDE-LPP 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 111 GGNTKTGKAIQFALDyLFAKSSRFLTKIAVVLTDGK---SQDDVKDAAQAARDSKITLFAIGVGSETED-AELRAIANKP 186
Cdd:COG1240  163 GGGTPLGDALALALE-LLKRADPARRKVIVLLTDGRdnaGRIDPLEAAELAAAAGIRIYTIGVGTEAVDeGLLREIAEAT 241

                        170       180
                 ....*....|....*....|...
gi 578811997 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 5.03e-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: 5.03e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997  37 DLVFILDGSYSVGPEN-FEIVKKWLVNITKNFDIGPKFIQVGVVQYSDYPVLEIPLGSY-----DSGEHLTAAVESILYL 110
Cdd:cd01471    2 DLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPnstnkDLALNAIRALLSLYYP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 111 GGNTKTGKAIQFALDYLF-AKSSR-FLTKIAVVLTDGKSQDDVK--DAAQAARDSKITLFAIGVGSETEDAELRAIANKP 186
Cdd:cd01471   82 NGSTNTTSALLVVEKHLFdTRGNReNAPQLVIIMTDGIPDSKFRtlKEARKLRERGVIIAVLGVGQGVNHEENRSLVGCD 161


                 ...
gi 578811997 187 SST 189
Cdd:cd01471  162 PDD 164
VWA_2 pfam13519
von Willebrand factor type A domain;
38-142 1.34e-12

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 64.62  E-value: 1.34e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997   38 LVFILDGSYS-----VGPENFEIVKKWLVNITKNFDIGpkfiQVGVVQYSDYPVLEIPLGsyDSGEHLTAAVESILYLGG 112
Cdd:pfam13519   1 LVFVLDTSGSmrngdYGPTRLEAAKDAVLALLKSLPGD----RVGLVTFGDGPEVLIPLT--KDRAKILRALRRLEPKGG 74

                          90       100       110
                  ....*....|....*....|....*....|
gi 578811997  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 8.56e-10

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: 55.19  E-value: 8.56e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578811997  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 2.15e-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: 2.15e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 578811997  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 2.61e-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: 2.61e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 578811997  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 2.85e-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: 2.85e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578811997  587 GEAGSPGAPGQDGTRGEPGIPGFPGNRglmGQKGEIGPPGQQGKKGAPGMPglmGSNGSPGQP 649
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPP---GPPGEPGPPGPPGPPGPPGPP---GAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 629-685 3.94e-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: 3.94e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578811997  629 GKKGAPGMPGLMGSNGSPGQPGTPGSKGSKGEPGIQGMPGASGLKGEPGATGSPGEP 685
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 644-699 4.39e-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: 4.39e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 578811997  644 GSPGQPGTPGSKGSKGEPGIQGMPGASGLKGEPGATGSPGEPGYMGLPGIQGKKGQ 699
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 37-212 4.98e-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: 4.98e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997  37 DLVFILDGSYSVGPENFEI-VKKWLVNITKNFDIGPKFIQVGVVQYSDYPVLEIPLG---SYDSGEhLTAAVESI---LY 109
Cdd:cd01473    2 DLTLILDESASIGYSNWRKdVIPFTEKIINNLNISKDKVHVGILLFAEKNRDVVPFSdeeRYDKNE-LLKKINDLknsYR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 110 LGGNTKTGKAIQFALDYLFAKSSRFLT--KIAVVLTDG----KSQDDVKDAAQAARDSKITLFAIGVGsETEDAELRAIA 183
Cdd:cd01473   81 SGGETYIVEALKYGLKNYTKHGNRRKDapKVTMLFTDGndtsASKKELQDISLLYKEENVKLLVVGVG-AASENKLKLLA 159

                        170       180       190
                 ....*....|....*....|....*....|..
gi 578811997 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 ...
 599-653 5.39e-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: 5.39e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 578811997  599 GTRGEPGIPGFPGNRGLMGQKGEIGPPGQQGKKGAPGMPGLMGSNGSPGQPGTPG 653
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 632-686 5.44e-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: 5.44e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 578811997  632 GAPGMPGLMGSNGSPGQPGTPGSKGSKGEPGIQGMPGASGLKGEPGATGSPGEPG 686
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 562-749 5.53e-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: 60.02  E-value: 5.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997  562 PGLPGPAGEPGrhgkdGLMGSPG----FKGEAGSPGAPgqdgtRGEPGIPGFPGNRGLMGQKGEIGPPGQQG-KKGAPGM 636
Cdd:pfam09606 101 PMGPGPGGPMG-----QQMGGPGtasnLLASLGRPQMP-----MGGAGFPSQMSRVGRMQPGGQAGGMMQPSsGQPGSGT 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997  637 PGLMGSNGSPGQPGTPGSKGSKGEPGIQGMPGASGLKG-----EPGATGSPGEPGYMGLPGIQGKKGQKGENGRQGIPGQ 711
Cdd:pfam09606 171 PNQMGPNGGPGQGQAGGMNGGQQGPMGGQMPPQMGVPGmpgpaDAGAQMGQQAQANGGMNPQQMGGAPNQVAMQQQQPQQ 250

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 578811997  712 QGIQGHHGAKGERGEKGEPGVRGAIGSKGESGVDGLMG 749
Cdd:pfam09606 251 QGQQSQLGMGINQMQQMPQGVGGGAGQGGPGQPMGPPG 288
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 581-637 5.95e-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: 5.95e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578811997  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 7.97e-09

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 52.50  E-value: 7.97e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 578811997  638 GLMGSNGSPGQPGTPGSKGSKGEPGIQGMPGASGLKGEPGATGSPGEPGYMGLPG 692
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 656-711 9.24e-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: 9.24e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 578811997  656 GSKGEPGIQGMPGASGLKGEPGATGSPGEPGYMGLPGIQGKKGQKGENGRQGIPGQ 711
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 39-197 1.04e-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: 1.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997  39 VFI-LDGSYSVGPENFEIVKKWLVN-ITK--NFDIGPKFiqvGVVQYSDYPVLEIPLGSYDSG------EHLTAAVESIL 108
Cdd:cd01470    3 IYIaLDASDSIGEEDFDEAKNAIKTlIEKisSYEVSPRY---EIISYASDPKEIVSIRDFNSNdaddviKRLEDFNYDDH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 109 YLGGNTKTGKAIQFALDYLF----AKSSRFLT--KIAVVLTDGKSQ---------DDVKD------AAQAARDSKITLFA 167
Cdd:cd01470   80 GDKTGTNTAAALKKVYERMAlekvRNKEAFNEtrHVIILFTDGKSNmggsplptvDKIKNlvyknnKSDNPREDYLDVYV 159

                        170       180       190
                 ....*....|....*....|....*....|.
gi 578811997 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 ...
 647-703 1.13e-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: 1.13e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578811997  647 GQPGTPGSKGSKGEPGIQGMPGASGLKGEPGATGSPGEPGYMGLPGIQGKKGQKGEN 703
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 488-544 1.43e-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: 1.43e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578811997  488 GVPGSPGIQGARGLPGYKGEPGRDGDKGDRGLPGFPGLHGMPGSKGEMGAKGDKGSP 544
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 527-595 2.21e-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: 2.21e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578811997  527 GMPGSKGEMGAKGDKGSPGfygkkgakgekgNAGFPGLPGPAGEPGRHGKDGLMGSPGFKGEAGSPGAP 595
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPG------------PPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 626-682 2.34e-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: 2.34e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578811997  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 2.48e-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: 2.48e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578811997  563 GLPGPAGEPGrhgkdglmgSPGFKGEAGSPGAPGQDGTRGEPGIPGFPGNRGLMGQKGEIGPPGQ 627
Cdd:pfam01391   1 GPPGPPGPPG---------PPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
35-184 2.63e-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: 2.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997  35 PTDLVFILDGSYSVGPENFEIVKKWLVNITKNFDIGPKF---IQVGVVQYSDYPVLEIPLGSYDSgehltaAVESILYLG 111
Cdd:COG4245    5 RLPVYLLLDTSGSMSGEPIEALNEGLQALIDELRQDPYAletVEVSVITFDGEAKVLLPLTDLED------FQPPDLSAS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 112 GNTKTGKAIQFALDyLFAKSSRFLTK--------IAVVLTDGKSQD-DVKDAAQAARD----SKITLFAIGVGSETEDAE 178
Cdd:COG4245   79 GGTPLGAALELLLD-LIERRVQKYTAegkgdwrpVVFLITDGEPTDsDWEAALQRLKDgeaaKKANIFAIGVGPDADTEV 157


                 ....*.
gi 578811997 179 LRAIAN 184
Cdd:COG4245  158 LKQLTD 163
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 596-656 7.29e-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: 7.29e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578811997  596 GQDGTRGEPGIPGFPgnrglmGQKGEIGPPGQQGKKGAPGMPGLMGSNGSPGQPGTPGSKG 656
Cdd:pfam01391   1 GPPGPPGPPGPPGPP------GPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 37-214 8.45e-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: 8.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997  37 DLVFILDGSYSVG---PENFEIVKkwlvnitknfDIGPKFI----QVGVVQYSDYPVLEIPLGSYDSGEHLTAAVESILY 109
Cdd:cd01474    6 DLYFVLDKSGSVAanwIEIYDFVE----------QLVDRFNspglRFSFITFSTRATKILPLTDDSSAIIKGLEVLKKVT 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 110 LGGNTKTGKAIQFALDYLFAKS--SRFLTKIAVVLTDGKSQDDV-KDA---AQAARDSKITLFAIGVgSETEDAELRAIA 183
Cdd:cd01474   76 PSGQTYIHEGLENANEQIFNRNggGRETVSVIIALTDGQLLLNGhKYPeheAKLSRKLGAIVYCVGV-TDFLKSQLINIA 154

                        170       180       190
                 ....*....|....*....|....*....|..
gi 578811997 184 NKPSstYVFYVED-YIAISKIREVMKQKLCEE 214
Cdd:cd01474  155 DSKE--YVFPVTSgFQALSGIIESVVKKACIE 184
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 38-206 1.21e-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: 1.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997  38 LVFILDGSYSVGPENFEIVKKWLVNITKNfdIGPKFIqVGVVQYSDYPVLEIPLGSYDSGEHLTAAVESiLYLGGNTKTG 117
Cdd:cd01465    3 LVFVIDRSGSMDGPKLPLVKSALKLLVDQ--LRPDDR-LAIVTYDGAAETVLPATPVRDKAAILAAIDR-LTAGGSTAGG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 118 KAIQFALDYLF-AKSSRFLTKIaVVLTDGK------SQDDVKDAAQAARDSKITLFAIGVGSETEDAELRAIANKPSSTY 190
Cdd:cd01465   79 AGIQLGYQEAQkHFVPGGVNRI-LLATDGDfnvgetDPDELARLVAQKRESGITLSTLGFGDNYNEDLMEAIADAGNGNT 157

                        170
                 ....*....|....*..
gi 578811997 191 vfyveDYIA-ISKIREV 206
Cdd:cd01465  158 -----AYIDnLAEARKV 169
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 611-667 1.65e-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: 1.65e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578811997  611 GNRGLMGQKGEIGPPGQQGKKGAPGMPGLMGSNGSPGQPGTPGSKGSKGEPGIQGMP 667
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 668-922 2.93e-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: 54.14  E-value: 2.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 668 GASGLKGEpgatGSPGEPGYMGLPGIQGKKGQKGENGRQGIPGQQGIQGHHGAKGERGEKGEPGVRGAIGSKGESGVDGL 747
Cdd:NF038329 109 GLQQLKGD----GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGA 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 748 MGPAGPKgqpgdpgpqgppgldgkpgrefseqfirqvctdviraqlpvllqsgrirncdhclsqhgspgipgppgpiGPE 827
Cdd:NF038329 185 KGPAGEK----------------------------------------------------------------------GPQ 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 828 GPRGLPGLPGRDGVPGLVGVPGRPGVRGLKGLPGR-----NGEKGSQGfgypgeqGPPGPPGPEGPPGISKEGPPGDPGL 902
Cdd:NF038329 195 GPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPagdgqQGPDGDPG-------PTGEDGPQGPDGPAGKDGPRGDRGE 267

                        250       260
                 ....*....|....*....|
gi 578811997 903 PGKDGDHGKPGIQGQPGPPG 922
Cdd:NF038329 268 AGPDGPDGKDGERGPVGPAG 287
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 470-524 4.01e-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: 47.49  E-value: 4.01e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 578811997  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 6.55e-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: 47.10  E-value: 6.55e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 578811997  476 GKPGYQGIAGTPGVPGSPGIQGARGLPGYKGEPGRDGDKGDRGLPGFPGLHGMPG 530
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 674-730 1.48e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 45.95  E-value: 1.48e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578811997  674 GEPGATGSPGEPGYMGLPGIQGKKGQKGENGRQGIPGQQGIQGHHGAKGERGEKGEP 730
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 476-740 3.86e-06

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: 50.38  E-value: 3.86e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 476 GKPGYQGIAGTPGVPGSPGIQGARGLPGYKGEPGRDGDKGDRglPGFPGLHGMPGSKGEMGAKGDKGSPGFygkkgakge 555
Cdd:cd21118   70 GEEGGSTLGSRGDVFEHRLGEAARSLGNAGNEIGRQAEDIIR--HGVDAVHNSWQGSGGHGAYGSQGGPGV--------- 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 556 KGNAGFPGLPGPAGEPGRHGKDGLMGSpgfKGEAGSPGAPGQD-GTRGEPGIPGFPGNRGLMGQKGEIGPPGQQGKKG-- 632
Cdd:cd21118  139 QGHGIPGGTGGPWASGGNYGTNSLGGS---VGQGGNGGPLNYGtNSQGAVAQPGYGTVRGNNQNSGCTNPPPSGSHESfs 215

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 633 -----------------APGMPGLMGSNGSPGQPGTPGSKGSKGEPGIQGMPGASGLKGEP-GATGSPGEPGYMGLPGIQ 694
Cdd:cd21118  216 nsggssssgssgsqgshGSNGQGSSGSSGGQGNGGNNGSSSSNSGNSGGSNGGSSGNSGSGsGGSSSGGSNGWGGSSSSG 295

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 578811997 695 GKKGQKGENGRQ--------GIPGQQGIQGHHGAKGERGEKGEPGVRGAIGSKG 740
Cdd:cd21118  296 GSGGSGGGNKPEcnnpgndvRMAGGGGSQGSKESSGSHGSNGGNGQAEAVGGLN 349
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 533-613 4.15e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 44.79  E-value: 4.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997  533 GEMGAKGDKGSPGFygkkgakgekgnagfPGLPGPAGEPgrhgkdglmGSPGFKGEAGSPGAPGQDGTRGEPGIPGFPGN 612
Cdd:pfam01391   1 GPPGPPGPPGPPGP---------------PGPPGPPGPP---------GPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56


                  .
gi 578811997  613 R 613
Cdd:pfam01391  57 P 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 506-572 1.06e-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: 1.06e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578811997  506 GEPGRDGDKGDRGLPGFPGLHGMPGSKGEMGAKGDKGSPGfygkkgakgekgNAGFPGLPGPAGEPG 572
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPG------------PPGPPGPPGAPGAPG 55
PHA03169 PHA03169
hypothetical protein; Provisional
 570-753 1.42e-05

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 48.43  E-value: 1.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 570 EPGRHGKDGLMGSpgfkgeaGSPGAPGQDGTRGEPGIPGFPGNRGLMG----QKGEIGPPGQQGKKGAPGMPGlmgsNGS 645
Cdd:PHA03169  77 EESRHGEKEERGQ-------GGPSGSGSESVGSPTPSPSGSAEELASGlspeNTSGSSPESPASHSPPPSPPS----HPG 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 646 PGQPGTPGSKGSKGEPGiqgmpGASGLKGEPGATGSPGEPGyMGLPGIQGKKGQKGENGRQGIPGQQGIQghhgakgERG 725
Cdd:PHA03169 146 PHEPAPPESHNPSPNQQ-----PSSFLQPSHEDSPEEPEPP-TSEPEPDSPGPPQSETPTSSPPPQSPPD-------EPG 212

                        170       180
                 ....*....|....*....|....*...
gi 578811997 726 EKGEPGVRGAIGSKGESGVDGLMGPAGP 753
Cdd:PHA03169 213 EPQSPTPQQAPSPNTQQAVEHEDEPTEP 240
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
 588-719 2.22e-05

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 48.14  E-value: 2.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 588 EAGSPGAPGQdgtrGEPGIPGFPGnrGLMGQKGEIGPPGQQGKKGAPGMPGLMGSNGSPGQPG--------------TPG 653
Cdd:PRK14959 369 ESLRPSGGGA----SAPSGSAAEG--PASGGAATIPTPGTQGPQGTAPAAGMTPSSAAPATPApsaapsprvpwddaPPA 442

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 654 SKGSKGEP-GIQGMPGASGLKGEPGATGS-PGEPGYMGLPG----------------IQGKKGQKGENGRQGIPGQQGiQ 715
Cdd:PRK14959 443 PPRSGIPPrPAPRMPEASPVPGAPDSVASaSDAPPTLGDPSdtaehtpsgprtwdgfLEFCQGRNGQGGRLATVLRQA-T 521


                 ....
gi 578811997 716 GHHG 719
Cdd:PRK14959 522 PEHA 525
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 488-715 2.59e-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: 2.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 488 GVPGSpGIQGARGLPGYKGEPGRDGdKGDRGLPGfpGLHGMPGSKGEMGAKGDKGSPGFygkkgakgEKGNAGFPGLPGP 567
Cdd:cd21118  123 GSGGH-GAYGSQGGPGVQGHGIPGG-TGGPWASG--GNYGTNSLGGSVGQGGNGGPLNY--------GTNSQGAVAQPGY 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 568 AGEPGRHGKDGLMGSPGFKGEAGS--PGAPGQDGTRGEPGIPGFPGnRGLMGQKGEIGPPGQQGKKGAPGMPGLMGSNGS 645
Cdd:cd21118  191 GTVRGNNQNSGCTNPPPSGSHESFsnSGGSSSSGSSGSQGSHGSNG-QGSSGSSGGQGNGGNNGSSSSNSGNSGGSNGGS 269

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 646 PGQPGTPGSKGSKGepGIQGMPGASGLKGEPGA--------------TGSPGEPGYMGLPGIQGKKGQKGENGRQGIPGQ 711
Cdd:cd21118  270 SGNSGSGSGGSSSG--GSNGWGGSSSSGGSGGSgggnkpecnnpgndVRMAGGGGSQGSKESSGSHGSNGGNGQAEAVGG 347


                 ....
gi 578811997 712 QGIQ 715
Cdd:cd21118  348 LNTL 351
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 701-754 3.16e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.48  E-value: 3.16e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 578811997  701 GENGRQGIPGQQGIQGHHGAKGERGEKGEPGVRGAIGSKGESGVDGLMGPAGPK 754
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 7.14e-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: 7.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 107 ILYLGGNTKTGKAIQFALDYLFAKSSRFLTK-------IAVVLTDGKSQDDVKDAAQA---ARDSKITLFAIGVGSETED 176
Cdd:cd01464   72 RLTASGGTSMGAALELALDCIDRRVQRYRADqkgdwrpWVFLLTDGEPTDDLTAAIERikeARDSKGRIVACAVGPKADL 151


                 ....*..
gi 578811997 177 AELRAIA 183
Cdd:cd01464  152 DTLKQIT 158
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 447-514 1.45e-04

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: 45.28  E-value: 1.45e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578811997 447 PPGKPGLQGPKGDPGLPGNPG------YPGQPGQDGKPGYQGIAGTPGVPGSPGIQGARGLPGYKGEPGRDGDK 514
Cdd:NF038329 270 PDGPDGKDGERGPVGPAGKDGqngkdgLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 452-686 2.11e-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: 44.99  E-value: 2.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 452 GLQGPKGDPGLPGNPGYPGQPGQDGKPGYQGIAGTPGVPGSPG----------IQGARGLPGYKGEPGRDGDKGDRGLPG 521
Cdd:cd21118  128 GAYGSQGGPGVQGHGIPGGTGGPWASGGNYGTNSLGGSVGQGGnggplnygtnSQGAVAQPGYGTVRGNNQNSGCTNPPP 207

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 522 fPGLHGMPGSKGEMGAKGDKGSPGFYGKKGakgekgnAGFPGLPGPAGEPGRHGKDGLMGSPGFKGEAGSPGAPGQDGTR 601
Cdd:cd21118  208 -SGSHESFSNSGGSSSSGSSGSQGSHGSNG-------QGSSGSSGGQGNGGNNGSSSSNSGNSGGSNGGSSGNSGSGSGG 279

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 602 GEPGipgfpGNRGLMGQKGEIGPPGQQGKKG-APGMPGlmGSNGSPGQPGTPGSKGSKGEPGIQGMPGASGLKGEPGATG 680
Cdd:cd21118  280 SSSG-----GSNGWGGSSSSGGSGGSGGGNKpECNNPG--NDVRMAGGGGSQGSKESSGSHGSNGGNGQAEAVGGLNTLN 352


                 ....*.
gi 578811997 681 SPGEPG 686
Cdd:cd21118  353 SDASTL 358
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 566-754 4.50e-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: 4.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 566 GPAGEPGRHGKDGLMGSPGFKGEaGSPGAPGQDGTRGepGIPGFPGNRGLMGQKGEIGPPGQ----QGKKGAPGMPGLMG 641
Cdd:cd21118  119 NSWQGSGGHGAYGSQGGPGVQGH-GIPGGTGGPWASG--GNYGTNSLGGSVGQGGNGGPLNYgtnsQGAVAQPGYGTVRG 195

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 642 SNGSPGQPGTPGSkGSKGEPGIQGMPGASGLKGEPGATGSPGEpGYMGLPGIQGKKGQKGE------NGRQGIPGQQGIQ 715
Cdd:cd21118  196 NNQNSGCTNPPPS-GSHESFSNSGGSSSSGSSGSQGSHGSNGQ-GSSGSSGGQGNGGNNGSsssnsgNSGGSNGGSSGNS 273

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 578811997 716 GHHGAKGERGEKGEPGVRGAIGSKGESGVDGLMGPAGPK 754
Cdd:cd21118  274 GSGSGGSSSGGSNGWGGSSSSGGSGGSGGGNKPECNNPG 312
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 37-173 1.05e-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: 41.16  E-value: 1.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997  37 DLVFILDGSYSVGPENFeiVKKWLVNITKnfDIGPKFI------QVGVVQYSDYPVLEIPL-GSYDSGEHLTAAVEsILY 109
Cdd:cd01467    4 DIMIALDVSGSMLAQDF--VKPSRLEAAK--EVLSDFIdrrendRIGLVVFAGAAFTQAPLtLDRESLKELLEDIK-IGL 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578811997 110 LGGNTKTGKAIQFALDYLfaKSSRFLTKIAVVLTDGKSQDDVKDAAQAARDSK---ITLFAIGVGSE 173
Cdd:cd01467   79 AGQGTAIGDAIGLAIKRL--KNSEAKERVIVLLTDGENNAGEIDPATAAELAKnkgVRIYTIGVGKS 143
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
 563-686 1.11e-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: 1.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811997 563 GLPGPAGEPGRHGKDGLMGSPGFKGEAGSPGAPgQDGTRGEPGIPGFPGNRGLMGQKGEIGPPGQQGKKGAPGMPGLMGS 642
Cdd:COG5180  340 GVPEAASDAGQPPSAYPPAEEAVPGKPLEQGAP-RPGSSGGDGAPFQPPNGAPQPGLGRRGAPGPPMGAGDLVQAALDGG 418

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 578811997 643 NGSPGQPGTPGSKGSKGEPGIQGMPGASGLKGEPGATGSPGEPG 686
Cdd:COG5180  419 GRETASLGGAAGGAGQGPKADFVPGDAESVSGPAGLADQAGAAA 462
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 497-545 4.29e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 36.32  E-value: 4.29e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 578811997  497 GARGLPGYKGEPGRDGDKGDRGLPGFPGLHGMPGSKGEMGAKGDKGSPG 545
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPG 49
 
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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