collagen alpha-1(XXI) chain isoform X1 [Macaca mulatta]
Protein Classification
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 | 2.20e-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: 199.53 E-value: 2.20e-58
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| gly_rich_SclB super family | cl45768 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
511-746 | 1.59e-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. The actual alignment was detected with superfamily member NF038329: Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 143.89 E-value: 1.59e-36
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| LamG super family | cl22861 | Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
230-412 | 1.05e-22 | ||||
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: 96.27 E-value: 1.05e-22
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| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
452-508 | 1.33e-09 | ||||
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins. : Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 54.81 E-value: 1.33e-09
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| Name | Accession | Description | Interval | E-value | ||||||
| vWA_Matrilin | cd01475 | VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ... |
34-254 | 2.20e-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: 199.53 E-value: 2.20e-58
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| VWA | pfam00092 | von Willebrand factor type A domain; |
37-205 | 2.70e-54 | ||||||
von Willebrand factor type A domain; Pssm-ID: 459670 [Multi-domain] Cd Length: 174 Bit Score: 186.33 E-value: 2.70e-54
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| VWA | smart00327 | von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ... |
37-203 | 5.15e-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: 5.15e-45
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| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
511-746 | 1.59e-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: 143.89 E-value: 1.59e-36
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| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
447-655 | 4.99e-35 | ||||||
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats. Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 139.27 E-value: 4.99e-35
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| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
598-933 | 1.60e-26 | ||||||
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: 113.85 E-value: 1.60e-26
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| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
608-934 | 8.20e-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: 102.68 E-value: 8.20e-23
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| TSPN | smart00210 | Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ... |
230-412 | 1.05e-22 | ||||||
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of thrombospondin Pssm-ID: 214560 Cd Length: 184 Bit Score: 96.27 E-value: 1.05e-22
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| ChlD | COG1240 | vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ... |
32-209 | 7.98e-18 | ||||||
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: 84.60 E-value: 7.98e-18
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| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
452-508 | 1.33e-09 | ||||||
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins. Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 54.81 E-value: 1.33e-09
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| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
629-685 | 4.32e-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: 4.32e-09
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| PRK14959 | PRK14959 | DNA polymerase III subunits gamma and tau; Provisional |
588-731 | 9.13e-07 | ||||||
DNA polymerase III subunits gamma and tau; Provisional Pssm-ID: 184923 [Multi-domain] Cd Length: 624 Bit Score: 52.76 E-value: 9.13e-07
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| dermokine | cd21118 | dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ... |
476-755 | 2.41e-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: 2.41e-05
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| PBP1 | COG5180 | PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ... |
563-686 | 3.04e-03 | ||||||
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; Pssm-ID: 444064 [Multi-domain] Cd Length: 548 Bit Score: 41.20 E-value: 3.04e-03
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| Name | Accession | Description | Interval | E-value | ||||||
| vWA_Matrilin | cd01475 | VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ... |
34-254 | 2.20e-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: 199.53 E-value: 2.20e-58
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| VWA | pfam00092 | von Willebrand factor type A domain; |
37-205 | 2.70e-54 | ||||||
von Willebrand factor type A domain; Pssm-ID: 459670 [Multi-domain] Cd Length: 174 Bit Score: 186.33 E-value: 2.70e-54
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| vWFA_subfamily_ECM | cd01450 | Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ... |
36-192 | 2.35e-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: 180.18 E-value: 2.35e-52
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| vWA_collagen_alphaI-XII-like | cd01482 | Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ... |
36-197 | 6.34e-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: 176.32 E-value: 6.34e-51
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| vWA_collagen | cd01472 | von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ... |
36-196 | 9.96e-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: 175.88 E-value: 9.96e-51
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| VWA | smart00327 | von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ... |
37-203 | 5.15e-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: 5.15e-45
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| vWA_integrins_alpha_subunit | cd01469 | Integrins are a class of adhesion receptors that link the extracellular matrix to the ... |
36-203 | 4.95e-40 | ||||||
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: 145.96 E-value: 4.95e-40
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| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
511-746 | 1.59e-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: 143.89 E-value: 1.59e-36
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| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
447-655 | 4.99e-35 | ||||||
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats. Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 139.27 E-value: 4.99e-35
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| vWFA | cd00198 | Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ... |
37-192 | 6.54e-33 | ||||||
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: 124.99 E-value: 6.54e-33
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| vWA_collagen_alpha3-VI-like | cd01481 | VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ... |
37-197 | 5.90e-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: 116.65 E-value: 5.90e-30
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| VWA_integrin_invertebrates | cd01476 | VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ... |
37-190 | 1.48e-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: 106.71 E-value: 1.48e-26
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| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
598-933 | 1.60e-26 | ||||||
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: 113.85 E-value: 1.60e-26
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| vWA_collagen_alpha_1-VI-type | cd01480 | VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ... |
35-189 | 2.18e-24 | ||||||
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions. Pssm-ID: 238757 [Multi-domain] Cd Length: 186 Bit Score: 101.31 E-value: 2.18e-24
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| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
608-934 | 8.20e-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: 102.68 E-value: 8.20e-23
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| TSPN | smart00210 | Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ... |
230-412 | 1.05e-22 | ||||||
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of thrombospondin Pssm-ID: 214560 Cd Length: 184 Bit Score: 96.27 E-value: 1.05e-22
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| ChlD | COG1240 | vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ... |
32-209 | 7.98e-18 | ||||||
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: 84.60 E-value: 7.98e-18
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| vWA_micronemal_protein | cd01471 | Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ... |
37-189 | 2.96e-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: 72.03 E-value: 2.96e-14
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| VWA_2 | pfam13519 | von Willebrand factor type A domain; |
38-142 | 4.43e-13 | ||||||
von Willebrand factor type A domain; Pssm-ID: 463909 [Multi-domain] Cd Length: 103 Bit Score: 66.16 E-value: 4.43e-13
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| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
452-508 | 1.33e-09 | ||||||
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins. Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 54.81 E-value: 1.33e-09
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| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
447-502 | 3.38e-09 | ||||||
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins. Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 53.65 E-value: 3.38e-09
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| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
455-509 | 3.91e-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: 3.91e-09
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| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
629-685 | 4.32e-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: 4.32e-09
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| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
587-649 | 4.71e-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: 4.71e-09
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| vWA_complement_factors | cd01470 | Complement factors B and C2 are two critical proteases for complement activation. They both ... |
39-197 | 6.27e-09 | ||||||
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: 56.91 E-value: 6.27e-09
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| Med15 | pfam09606 | ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ... |
562-761 | 7.58e-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: 59.64 E-value: 7.58e-09
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| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
599-653 | 8.57e-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: 8.57e-09
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| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
581-637 | 9.08e-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: 9.08e-09
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| Glutenin_hmw | pfam03157 | High molecular weight glutenin subunit; Members of this family include high molecular weight ... |
439-725 | 9.42e-09 | ||||||
High molecular weight glutenin subunit; Members of this family include high molecular weight subunits of glutenin. This group of gluten proteins is thought to be largely responsible for the elastic properties of gluten, and hence, doughs. Indeed, glutenin high molecular weight subunits are classified as elastomeric proteins, because the glutenin network can withstand significant deformations without breaking, and return to the original conformation when the stress is removed. Elastomeric proteins differ considerably in amino acid sequence, but they are all polymers whose subunits consist of elastomeric domains, composed of repeated motifs, and non-elastic domains that mediate cross-linking between the subunits. The elastomeric domain motifs are all rich in glycine residues in addition to other hydrophobic residues. High molecular weight glutenin subunits have an extensive central elastomeric domain, flanked by two terminal non-elastic domains that form disulphide cross-links. The central elastomeric domain is characterized by the following three repeated motifs: PGQGQQ, GYYPTS[P/L]QQ, GQQ. It possesses overlapping beta-turns within and between the repeated motifs, and assumes a regular helical secondary structure with a diameter of approx. 1.9 nm and a pitch of approx. 1.5 nm. Pssm-ID: 367362 [Multi-domain] Cd Length: 786 Bit Score: 59.19 E-value: 9.42e-09
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| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
644-698 | 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
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| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
632-686 | 1.51e-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: 1.51e-08
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| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
638-692 | 1.57e-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: 1.57e-08
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| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
488-544 | 2.19e-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: 2.19e-08
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| TerY | COG4245 | Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown]; |
35-184 | 2.48e-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: 2.48e-08
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| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
527-595 | 3.54e-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: 50.57 E-value: 3.54e-08
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| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
563-627 | 3.99e-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: 50.57 E-value: 3.99e-08
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| vWA_ATR | cd01474 | ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ... |
37-214 | 4.02e-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: 54.05 E-value: 4.02e-08
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| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
647-701 | 4.90e-08 | ||||||
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins. Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 50.18 E-value: 4.90e-08
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| vWA_CTRP | cd01473 | CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ... |
37-212 | 5.94e-08 | ||||||
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: 53.86 E-value: 5.94e-08
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| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
596-656 | 1.17e-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: 49.03 E-value: 1.17e-07
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| vWA_subgroup | cd01465 | VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ... |
38-206 | 1.43e-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: 1.43e-07
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| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
674-728 | 2.24e-07 | ||||||
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins. Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 48.26 E-value: 2.24e-07
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| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
611-667 | 2.49e-07 | ||||||
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins. Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 48.26 E-value: 2.49e-07
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| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
656-711 | 2.67e-07 | ||||||
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins. Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 48.26 E-value: 2.67e-07
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| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
470-524 | 6.08e-07 | ||||||
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins. Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 47.10 E-value: 6.08e-07
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| PRK14959 | PRK14959 | DNA polymerase III subunits gamma and tau; Provisional |
588-731 | 9.13e-07 | ||||||
DNA polymerase III subunits gamma and tau; Provisional Pssm-ID: 184923 [Multi-domain] Cd Length: 624 Bit Score: 52.76 E-value: 9.13e-07
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| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
476-530 | 9.64e-07 | ||||||
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins. Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 46.72 E-value: 9.64e-07
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| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
650-705 | 2.73e-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: 45.18 E-value: 2.73e-06
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| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
533-613 | 7.27e-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: 44.02 E-value: 7.27e-06
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| vWA_subfamily | cd01464 | VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood ... |
107-183 | 1.53e-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: 46.56 E-value: 1.53e-05
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| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
506-572 | 1.64e-05 | ||||||
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins. Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 43.25 E-value: 1.64e-05
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| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
707-763 | 2.34e-05 | ||||||
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins. Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 42.87 E-value: 2.34e-05
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| dermokine | cd21118 | dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ... |
476-755 | 2.41e-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: 2.41e-05
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| dermokine | cd21118 | dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ... |
566-766 | 2.41e-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: 2.41e-05
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| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
683-738 | 4.57e-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: 41.71 E-value: 4.57e-05
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| dermokine | cd21118 | dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ... |
452-686 | 2.87e-04 | ||||||
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a skin-specific glycoprotein that may play a regulatory role in the crosstalk between barrier dysfunction and inflammation, and therefore play a role in inflammatory diseases such as psoriasis. Dermokine is one of the most highly expressed proteins in differentiating keratinocytes, found mainly in the spinous and granular layers of the epidermis, but also in the epithelia of the small intestine, macrophages of the lung, and endothelial cells of the lung. Mouse dermokine has been reported to be encoded by 22 exons, and its expression leads to alpha, beta, and gamma transcripts. Pssm-ID: 411053 [Multi-domain] Cd Length: 495 Bit Score: 44.61 E-value: 2.87e-04
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| NorD | COG4548 | Nitric oxide reductase activation protein [Inorganic ion transport and metabolism]; |
97-176 | 5.25e-04 | ||||||
Nitric oxide reductase activation protein [Inorganic ion transport and metabolism]; Pssm-ID: 443612 [Multi-domain] Cd Length: 439 Bit Score: 43.55 E-value: 5.25e-04
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| vWA_BatA_type | cd01467 | VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ... |
37-173 | 1.06e-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: 1.06e-03
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| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
716-765 | 2.18e-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: 37.09 E-value: 2.18e-03
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| PBP1 | COG5180 | PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ... |
563-686 | 3.04e-03 | ||||||
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; Pssm-ID: 444064 [Multi-domain] Cd Length: 548 Bit Score: 41.20 E-value: 3.04e-03
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| vWA_norD_type | cd01454 | norD type: Denitrifying bacteria contain both membrane bound and periplasmic nitrate ... |
89-173 | 4.48e-03 | ||||||
norD type: Denitrifying bacteria contain both membrane bound and periplasmic nitrate reductases. Denitrification plays a major role in completing the nitrogen cycle by converting nitrate or nitrite to nitrogen gas. The pathway for microbial denitrification has been established as NO3- ------> NO2- ------> NO -------> N2O ---------> N2. This reaction generally occurs under oxygen limiting conditions. Genetic and biochemical studies have shown that the first srep of the biochemical pathway is catalyzed by periplasmic nitrate reductases. This family is widely present in proteobacteria and firmicutes. This version of the domain is also present in some archaeal members. The function of the vWA domain in this sub-group is not known. Members of this subgroup have a conserved MIDAS motif. Pssm-ID: 238731 [Multi-domain] Cd Length: 174 Bit Score: 39.23 E-value: 4.48e-03
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| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
497-545 | 5.96e-03 | ||||||
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins. Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 35.93 E-value: 5.96e-03
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