hypothetical protein A2617_02920 [Candidatus Daviesbacteria bacterium RIFOXYD1_FULL_41_10]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| TGc | smart00460 | Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish ... |
420-489 | 2.01e-10 | ||||
Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish covalent links between proteins. A subset of transglutaminase homologues appear to catalyse the reverse reaction, the hydrolysis of peptide bonds. Proteins with this domain are both extracellular and intracellular, and it is likely that the eukaryotic intracellular proteins are involved in signalling events. : Pssm-ID: 214673 Cd Length: 68 Bit Score: 57.39 E-value: 2.01e-10
|
||||||||
| vWFA | cd00198 | Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ... |
654-811 | 3.09e-06 | ||||
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: 47.95 E-value: 3.09e-06
|
||||||||
| Lipoprotein_20 super family | cl08141 | YfhG lipoprotein; This family includes the YfhG protein from E. coli. Members of this family ... |
51-214 | 4.84e-03 | ||||
YfhG lipoprotein; This family includes the YfhG protein from E. coli. Members of this family have an N-terminal lipoprotein attachment site. The members of this family are functionally uncharacterized. The actual alignment was detected with superfamily member PRK10722: Pssm-ID: 447579 Cd Length: 247 Bit Score: 39.59 E-value: 4.84e-03
|
||||||||
| Name | Accession | Description | Interval | E-value | ||||
| TGc | smart00460 | Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish ... |
420-489 | 2.01e-10 | ||||
Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish covalent links between proteins. A subset of transglutaminase homologues appear to catalyse the reverse reaction, the hydrolysis of peptide bonds. Proteins with this domain are both extracellular and intracellular, and it is likely that the eukaryotic intracellular proteins are involved in signalling events. Pssm-ID: 214673 Cd Length: 68 Bit Score: 57.39 E-value: 2.01e-10
|
||||||||
| Transglut_core | pfam01841 | Transglutaminase-like superfamily; This family includes animal transglutaminases and other ... |
382-487 | 1.02e-09 | ||||
Transglutaminase-like superfamily; This family includes animal transglutaminases and other bacterial proteins of unknown function. Sequence conservation in this superfamily primarily involves three motifs that centre around conserved cysteine, histidine, and aspartate residues that form the catalytic triad in the structurally characterized transglutaminase, the human blood clotting factor XIIIa'. On the basis of the experimentally demonstrated activity of the Methanobacterium phage pseudomurein endoisopeptidase, it is proposed that many, if not all, microbial homologs of the transglutaminases are proteases and that the eukaryotic transglutaminases have evolved from an ancestral protease. Pssm-ID: 376628 [Multi-domain] Cd Length: 108 Bit Score: 56.64 E-value: 1.02e-09
|
||||||||
| YebA | COG1305 | Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, ... |
378-488 | 2.00e-09 | ||||
Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440916 [Multi-domain] Cd Length: 174 Bit Score: 57.71 E-value: 2.00e-09
|
||||||||
| vWFA | cd00198 | Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ... |
654-811 | 3.09e-06 | ||||
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: 47.95 E-value: 3.09e-06
|
||||||||
| PRK10722 | PRK10722 | two-component system QseEF-associated lipoprotein QseG; |
51-214 | 4.84e-03 | ||||
two-component system QseEF-associated lipoprotein QseG; Pssm-ID: 236745 Cd Length: 247 Bit Score: 39.59 E-value: 4.84e-03
|
||||||||
| Name | Accession | Description | Interval | E-value | ||||
| TGc | smart00460 | Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish ... |
420-489 | 2.01e-10 | ||||
Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish covalent links between proteins. A subset of transglutaminase homologues appear to catalyse the reverse reaction, the hydrolysis of peptide bonds. Proteins with this domain are both extracellular and intracellular, and it is likely that the eukaryotic intracellular proteins are involved in signalling events. Pssm-ID: 214673 Cd Length: 68 Bit Score: 57.39 E-value: 2.01e-10
|
||||||||
| Transglut_core | pfam01841 | Transglutaminase-like superfamily; This family includes animal transglutaminases and other ... |
382-487 | 1.02e-09 | ||||
Transglutaminase-like superfamily; This family includes animal transglutaminases and other bacterial proteins of unknown function. Sequence conservation in this superfamily primarily involves three motifs that centre around conserved cysteine, histidine, and aspartate residues that form the catalytic triad in the structurally characterized transglutaminase, the human blood clotting factor XIIIa'. On the basis of the experimentally demonstrated activity of the Methanobacterium phage pseudomurein endoisopeptidase, it is proposed that many, if not all, microbial homologs of the transglutaminases are proteases and that the eukaryotic transglutaminases have evolved from an ancestral protease. Pssm-ID: 376628 [Multi-domain] Cd Length: 108 Bit Score: 56.64 E-value: 1.02e-09
|
||||||||
| YebA | COG1305 | Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, ... |
378-488 | 2.00e-09 | ||||
Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440916 [Multi-domain] Cd Length: 174 Bit Score: 57.71 E-value: 2.00e-09
|
||||||||
| vWFA | cd00198 | Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ... |
654-811 | 3.09e-06 | ||||
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: 47.95 E-value: 3.09e-06
|
||||||||
| PRK10722 | PRK10722 | two-component system QseEF-associated lipoprotein QseG; |
51-214 | 4.84e-03 | ||||
two-component system QseEF-associated lipoprotein QseG; Pssm-ID: 236745 Cd Length: 247 Bit Score: 39.59 E-value: 4.84e-03
|
||||||||
| Blast search parameters | ||||
|
