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disintegrin MDC9
List of domain hits
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Name | Accession | Description | Interval | E-value | ||||
ZnMc_adamalysin_II_like | cd04269 | Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ... |
212-404 | 6.39e-94 | ||||
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom zinc endopeptidase. This subfamily contains other snake venom metalloproteinases, as well as membrane-anchored metalloproteases belonging to the ADAM family. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions. : Pssm-ID: 239797 [Multi-domain] Cd Length: 194 Bit Score: 292.60 E-value: 6.39e-94
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ACR | smart00608 | ADAM Cysteine-Rich Domain; |
500-636 | 4.28e-59 | ||||
ADAM Cysteine-Rich Domain; : Pssm-ID: 214743 Cd Length: 137 Bit Score: 197.20 E-value: 4.28e-59
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Pep_M12B_propep | pfam01562 | Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
44-163 | 1.55e-42 | ||||
Reprolysin family propeptide; This region is the propeptide for members of peptidase family M12B. The propeptide contains a sequence motif similar to the "cysteine switch" of the matrixins. This motif is found at the C terminus of the alignment but is not well aligned. : Pssm-ID: 460254 Cd Length: 128 Bit Score: 150.93 E-value: 1.55e-42
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Disintegrin | pfam00200 | Disintegrin; |
423-496 | 1.41e-36 | ||||
Disintegrin; : Pssm-ID: 459709 Cd Length: 74 Bit Score: 131.98 E-value: 1.41e-36
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Drf_FH1 | pfam06346 | Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ... |
747-802 | 1.24e-09 | ||||
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs). It consists of low complexity repeats of around 12 residues. : Pssm-ID: 461881 [Multi-domain] Cd Length: 157 Bit Score: 57.57 E-value: 1.24e-09
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EGF_2 | pfam07974 | EGF-like domain; This family contains EGF domains found in a variety of extracellular proteins. |
650-673 | 7.93e-03 | ||||
EGF-like domain; This family contains EGF domains found in a variety of extracellular proteins. : Pssm-ID: 400365 Cd Length: 26 Bit Score: 34.63 E-value: 7.93e-03
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Name | Accession | Description | Interval | E-value | ||||
ZnMc_adamalysin_II_like | cd04269 | Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ... |
212-404 | 6.39e-94 | ||||
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom zinc endopeptidase. This subfamily contains other snake venom metalloproteinases, as well as membrane-anchored metalloproteases belonging to the ADAM family. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions. Pssm-ID: 239797 [Multi-domain] Cd Length: 194 Bit Score: 292.60 E-value: 6.39e-94
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Reprolysin | pfam01421 | Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ... |
212-406 | 2.24e-93 | ||||
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis. Members of this family are also known as adamalysins. Most members of this family are snake venom endopeptidases, but there are also some mammalian proteins such as Swiss:P78325, and fertilin. Fertilin and closely related proteins appear to not have some active site residues and may not be active enzymes. Pssm-ID: 426256 [Multi-domain] Cd Length: 200 Bit Score: 291.51 E-value: 2.24e-93
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ACR | smart00608 | ADAM Cysteine-Rich Domain; |
500-636 | 4.28e-59 | ||||
ADAM Cysteine-Rich Domain; Pssm-ID: 214743 Cd Length: 137 Bit Score: 197.20 E-value: 4.28e-59
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ADAM_CR | pfam08516 | ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ... |
501-605 | 1.14e-47 | ||||
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell surface and extracellular matrix (ECM) in order to alter cell behaviour. It has been shown that the cysteine-rich domain of ADAM13 regulates the protein's metalloprotease activity. Pssm-ID: 462504 Cd Length: 105 Bit Score: 164.33 E-value: 1.14e-47
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Pep_M12B_propep | pfam01562 | Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
44-163 | 1.55e-42 | ||||
Reprolysin family propeptide; This region is the propeptide for members of peptidase family M12B. The propeptide contains a sequence motif similar to the "cysteine switch" of the matrixins. This motif is found at the C terminus of the alignment but is not well aligned. Pssm-ID: 460254 Cd Length: 128 Bit Score: 150.93 E-value: 1.55e-42
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Disintegrin | pfam00200 | Disintegrin; |
423-496 | 1.41e-36 | ||||
Disintegrin; Pssm-ID: 459709 Cd Length: 74 Bit Score: 131.98 E-value: 1.41e-36
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DISIN | smart00050 | Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ... |
423-498 | 3.15e-35 | ||||
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to integrin receptors. They contain a 'RGD' sequence, identical to the recognition site of many adhesion proteins. Molecules containing both disintegrin and metalloprotease domains are known as ADAMs. Pssm-ID: 214490 Cd Length: 75 Bit Score: 128.19 E-value: 3.15e-35
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Drf_FH1 | pfam06346 | Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ... |
747-802 | 1.24e-09 | ||||
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs). It consists of low complexity repeats of around 12 residues. Pssm-ID: 461881 [Multi-domain] Cd Length: 157 Bit Score: 57.57 E-value: 1.24e-09
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PHA03378 | PHA03378 | EBNA-3B; Provisional |
748-810 | 6.95e-06 | ||||
EBNA-3B; Provisional Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 50.07 E-value: 6.95e-06
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SPT5 | COG5164 | Transcription elongation factor SPT5 [Transcription]; |
742-811 | 9.40e-06 | ||||
Transcription elongation factor SPT5 [Transcription]; Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 49.26 E-value: 9.40e-06
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EGF_2 | pfam07974 | EGF-like domain; This family contains EGF domains found in a variety of extracellular proteins. |
650-673 | 7.93e-03 | ||||
EGF-like domain; This family contains EGF domains found in a variety of extracellular proteins. Pssm-ID: 400365 Cd Length: 26 Bit Score: 34.63 E-value: 7.93e-03
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Name | Accession | Description | Interval | E-value | ||||
ZnMc_adamalysin_II_like | cd04269 | Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ... |
212-404 | 6.39e-94 | ||||
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom zinc endopeptidase. This subfamily contains other snake venom metalloproteinases, as well as membrane-anchored metalloproteases belonging to the ADAM family. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions. Pssm-ID: 239797 [Multi-domain] Cd Length: 194 Bit Score: 292.60 E-value: 6.39e-94
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Reprolysin | pfam01421 | Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ... |
212-406 | 2.24e-93 | ||||
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis. Members of this family are also known as adamalysins. Most members of this family are snake venom endopeptidases, but there are also some mammalian proteins such as Swiss:P78325, and fertilin. Fertilin and closely related proteins appear to not have some active site residues and may not be active enzymes. Pssm-ID: 426256 [Multi-domain] Cd Length: 200 Bit Score: 291.51 E-value: 2.24e-93
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ACR | smart00608 | ADAM Cysteine-Rich Domain; |
500-636 | 4.28e-59 | ||||
ADAM Cysteine-Rich Domain; Pssm-ID: 214743 Cd Length: 137 Bit Score: 197.20 E-value: 4.28e-59
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ADAM_CR | pfam08516 | ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ... |
501-605 | 1.14e-47 | ||||
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell surface and extracellular matrix (ECM) in order to alter cell behaviour. It has been shown that the cysteine-rich domain of ADAM13 regulates the protein's metalloprotease activity. Pssm-ID: 462504 Cd Length: 105 Bit Score: 164.33 E-value: 1.14e-47
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Pep_M12B_propep | pfam01562 | Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
44-163 | 1.55e-42 | ||||
Reprolysin family propeptide; This region is the propeptide for members of peptidase family M12B. The propeptide contains a sequence motif similar to the "cysteine switch" of the matrixins. This motif is found at the C terminus of the alignment but is not well aligned. Pssm-ID: 460254 Cd Length: 128 Bit Score: 150.93 E-value: 1.55e-42
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Disintegrin | pfam00200 | Disintegrin; |
423-496 | 1.41e-36 | ||||
Disintegrin; Pssm-ID: 459709 Cd Length: 74 Bit Score: 131.98 E-value: 1.41e-36
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DISIN | smart00050 | Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ... |
423-498 | 3.15e-35 | ||||
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to integrin receptors. They contain a 'RGD' sequence, identical to the recognition site of many adhesion proteins. Molecules containing both disintegrin and metalloprotease domains are known as ADAMs. Pssm-ID: 214490 Cd Length: 75 Bit Score: 128.19 E-value: 3.15e-35
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ZnMc_ADAM_like | cd04267 | Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ... |
212-387 | 9.67e-30 | ||||
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ADAM family of metalloproteases contains proteolytic domains from snake venoms, proteases from the mammalian reproductive tract, and the tumor necrosis factor alpha convertase, TACE. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions. Pssm-ID: 239795 Cd Length: 192 Bit Score: 116.75 E-value: 9.67e-30
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ZnMc_ADAMTS_like | cd04273 | Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ... |
212-403 | 7.38e-28 | ||||
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions. This particular subfamily represents domain architectures that combine ADAM-like metalloproteinases with thrombospondin type-1 repeats. ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) proteinases are inhibited by TIMPs (tissue inhibitors of metalloproteinases), and they play roles in coagulation, angiogenesis, development and progression of arthritis. They hydrolyze the von Willebrand factor precursor and various components of the extracellular matrix. Pssm-ID: 239801 Cd Length: 207 Bit Score: 111.95 E-value: 7.38e-28
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Reprolysin_3 | pfam13582 | Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
237-358 | 6.51e-19 | ||||
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the characteriztic binding motif HExxGHxxGxxH of Reprolysin-like peptidases of family M12B. Pssm-ID: 463926 [Multi-domain] Cd Length: 122 Bit Score: 83.19 E-value: 6.51e-19
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Reprolysin_5 | pfam13688 | Metallo-peptidase family M12; |
211-383 | 9.21e-18 | ||||
Metallo-peptidase family M12; Pssm-ID: 372673 Cd Length: 191 Bit Score: 82.08 E-value: 9.21e-18
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ZnMc_salivary_gland_MPs | cd04272 | Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ... |
213-402 | 2.58e-15 | ||||
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary glands of arthropods. Pssm-ID: 239800 Cd Length: 220 Bit Score: 75.85 E-value: 2.58e-15
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ZnMc | cd00203 | Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ... |
212-393 | 5.17e-13 | ||||
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major branches, the astacin-like proteases and the adamalysin/reprolysin-like proteases. Both branches have wide phylogenetic distribution, and contain sub-families, which are involved in vertebrate development and disease. Pssm-ID: 238124 [Multi-domain] Cd Length: 167 Bit Score: 67.93 E-value: 5.17e-13
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Drf_FH1 | pfam06346 | Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ... |
747-802 | 1.24e-09 | ||||
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs). It consists of low complexity repeats of around 12 residues. Pssm-ID: 461881 [Multi-domain] Cd Length: 157 Bit Score: 57.57 E-value: 1.24e-09
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Reprolysin_2 | pfam13574 | Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
234-386 | 2.55e-09 | ||||
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the characteriztic binding motif HExxGHxxGxxH of Reprolysin-like peptidases of family M12B. Pssm-ID: 372637 Cd Length: 193 Bit Score: 57.64 E-value: 2.55e-09
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Reprolysin_4 | pfam13583 | Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
212-390 | 1.76e-08 | ||||
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the characteriztic binding motif HExxGHxxGxxH of Reprolysin-like peptidases of family M12B. Pssm-ID: 404471 Cd Length: 203 Bit Score: 55.32 E-value: 1.76e-08
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ZnMc_TACE_like | cd04270 | Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ... |
216-401 | 2.05e-06 | ||||
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha converting enzyme, releases soluble TNF-alpha from transmembrane pro-TNF-alpha. Pssm-ID: 239798 [Multi-domain] Cd Length: 244 Bit Score: 50.06 E-value: 2.05e-06
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PHA03378 | PHA03378 | EBNA-3B; Provisional |
748-810 | 6.95e-06 | ||||
EBNA-3B; Provisional Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 50.07 E-value: 6.95e-06
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SPT5 | COG5164 | Transcription elongation factor SPT5 [Transcription]; |
742-811 | 9.40e-06 | ||||
Transcription elongation factor SPT5 [Transcription]; Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 49.26 E-value: 9.40e-06
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ZnMc_ADAM_fungal | cd04271 | Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ... |
281-386 | 9.60e-06 | ||||
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A Disintegrin And Metalloprotease) family of metalloproteases are integral membrane proteases acting on a variety of extracellular targets. They are involved in shedding soluble peptides or proteins from the cell surface. This subfamily contains fungal ADAMs, whose precise function has yet to be determined. Pssm-ID: 239799 [Multi-domain] Cd Length: 228 Bit Score: 47.80 E-value: 9.60e-06
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PHA03378 | PHA03378 | EBNA-3B; Provisional |
747-805 | 1.57e-05 | ||||
EBNA-3B; Provisional Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 48.91 E-value: 1.57e-05
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Pro-rich | pfam15240 | Proline-rich protein; This family includes several eukaryotic proline-rich proteins. |
732-811 | 2.65e-05 | ||||
Proline-rich protein; This family includes several eukaryotic proline-rich proteins. Pssm-ID: 464580 [Multi-domain] Cd Length: 167 Bit Score: 45.41 E-value: 2.65e-05
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SPT5 | COG5164 | Transcription elongation factor SPT5 [Transcription]; |
732-810 | 3.17e-05 | ||||
Transcription elongation factor SPT5 [Transcription]; Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 47.33 E-value: 3.17e-05
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PHA03378 | PHA03378 | EBNA-3B; Provisional |
741-814 | 1.58e-04 | ||||
EBNA-3B; Provisional Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 45.44 E-value: 1.58e-04
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SPT5 | COG5164 | Transcription elongation factor SPT5 [Transcription]; |
750-811 | 1.76e-04 | ||||
Transcription elongation factor SPT5 [Transcription]; Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 45.02 E-value: 1.76e-04
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Pro-rich | pfam15240 | Proline-rich protein; This family includes several eukaryotic proline-rich proteins. |
740-797 | 2.58e-04 | ||||
Proline-rich protein; This family includes several eukaryotic proline-rich proteins. Pssm-ID: 464580 [Multi-domain] Cd Length: 167 Bit Score: 42.33 E-value: 2.58e-04
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SPT5 | COG5164 | Transcription elongation factor SPT5 [Transcription]; |
747-811 | 3.47e-04 | ||||
Transcription elongation factor SPT5 [Transcription]; Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 44.25 E-value: 3.47e-04
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PHA03307 | PHA03307 | transcriptional regulator ICP4; Provisional |
731-806 | 4.76e-04 | ||||
transcriptional regulator ICP4; Provisional Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 44.01 E-value: 4.76e-04
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Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
747-794 | 4.84e-04 | ||||
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins. Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 38.63 E-value: 4.84e-04
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PHA03378 | PHA03378 | EBNA-3B; Provisional |
728-802 | 6.09e-04 | ||||
EBNA-3B; Provisional Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 43.52 E-value: 6.09e-04
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Drf_FH1 | pfam06346 | Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ... |
747-809 | 7.08e-04 | ||||
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs). It consists of low complexity repeats of around 12 residues. Pssm-ID: 461881 [Multi-domain] Cd Length: 157 Bit Score: 41.01 E-value: 7.08e-04
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ZnMc_MMP_like | cd04268 | Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ... |
287-357 | 7.42e-04 | ||||
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix metalloproteinases (MMPs), serralysins, and the astacin_like family of proteases. Pssm-ID: 239796 [Multi-domain] Cd Length: 165 Bit Score: 40.94 E-value: 7.42e-04
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Pro-rich | pfam15240 | Proline-rich protein; This family includes several eukaryotic proline-rich proteins. |
747-810 | 7.90e-04 | ||||
Proline-rich protein; This family includes several eukaryotic proline-rich proteins. Pssm-ID: 464580 [Multi-domain] Cd Length: 167 Bit Score: 41.18 E-value: 7.90e-04
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Pro-rich | pfam15240 | Proline-rich protein; This family includes several eukaryotic proline-rich proteins. |
746-810 | 9.81e-04 | ||||
Proline-rich protein; This family includes several eukaryotic proline-rich proteins. Pssm-ID: 464580 [Multi-domain] Cd Length: 167 Bit Score: 40.79 E-value: 9.81e-04
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PBP1 | COG5180 | PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ... |
723-811 | 1.62e-03 | ||||
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; Pssm-ID: 444064 [Multi-domain] Cd Length: 548 Bit Score: 41.97 E-value: 1.62e-03
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Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
755-794 | 2.06e-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: 2.06e-03
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PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
730-810 | 3.57e-03 | ||||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 41.08 E-value: 3.57e-03
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Peptidase_M54 | cd11375 | Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ... |
345-392 | 5.87e-03 | ||||
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 (archaemetzincin or archaelysin) is a zinc-dependent aminopeptidase that contains the consensus zinc-binding sequence HEXXHXXGXXH/D and a conserved Met residue at the active site, and is thus classified as a metzincin. Archaemetzincins, first identified in archaea, are also found in bacteria and eukaryotes, including two human members, archaemetzincin-1 and -2 (AMZ1 and AMZ2). AMZ1 is mainly found in the liver and heart while AMZ2 is primarily expressed in testis and heart; both have been reported to degrade synthetic substrates and peptides. The Peptidase M54 family contains an extended metzincin concensus sequence of HEXXHXXGX3CX4CXMX17CXXC such that a second zinc ion is bound to four cysteines, thus resembling a zinc finger. Phylogenetic analysis of this family reveals a complex evolutionary process involving a series of lateral gene transfer, gene loss and genetic duplication events. Pssm-ID: 213029 Cd Length: 173 Bit Score: 38.43 E-value: 5.87e-03
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Drf_FH1 | pfam06346 | Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ... |
747-793 | 6.75e-03 | ||||
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs). It consists of low complexity repeats of around 12 residues. Pssm-ID: 461881 [Multi-domain] Cd Length: 157 Bit Score: 38.31 E-value: 6.75e-03
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Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
755-795 | 7.49e-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: 35.55 E-value: 7.49e-03
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EGF_2 | pfam07974 | EGF-like domain; This family contains EGF domains found in a variety of extracellular proteins. |
650-673 | 7.93e-03 | ||||
EGF-like domain; This family contains EGF domains found in a variety of extracellular proteins. Pssm-ID: 400365 Cd Length: 26 Bit Score: 34.63 E-value: 7.93e-03
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FAP | pfam07174 | Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment ... |
747-809 | 8.02e-03 | ||||
Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment proteins (FAP). Family members are rich in alanine and proline, are approximately 300 long, and seem to be restricted to mycobacteria. These proteins contain a fibronectin-binding motif that allows mycobacteria to bind to fibronectin in the extracellular matrix. Pssm-ID: 429334 Cd Length: 301 Bit Score: 39.14 E-value: 8.02e-03
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