probable ribonuclease ZC3H12C isoform 2 [Mus musculus]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| PIN_Zc3h12-like | cd18729 | PRORP-like PIN domain of ribonuclease Zc3h12a and related proteins; Zc3h12a (zinc finger ... |
249-379 | 1.95e-100 | |||||
PRORP-like PIN domain of ribonuclease Zc3h12a and related proteins; Zc3h12a (zinc finger CCCH-type containing 12A, also known as MCPIP1/MCP induced protein 1 and Regnase-1) is a critical regulator of inflammatory response, with additional roles in defense against viruses and various stresses, cellular differentiation, and apoptosis. This subfamily also includes three less-studied mammalian homologs: Zc3h12b-d/Regnase-2-4. It belongs to the Zc3h12a-N4BP1-like PIN subfamily of the PRORP-Zc3h12a-like PIN family, the latter of which additionally includes human PRORP, also known as proteinaceous RNase P and mitochondrial RNase P protein subunit 3 (MRPP3), and Arabidopsis thaliana PRORP1-3. The PIN (PilT N terminus) domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members, additional metal coordinating residues can be found while some others lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. : Pssm-ID: 350296 Cd Length: 131 Bit Score: 308.14 E-value: 1.95e-100
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| Regnase_1_C | pfam18561 | Endoribonuclease Regnase 1/ ZC3H12 C-terminal domain; This is the C-terminal domain found in ... |
836-879 | 1.58e-22 | |||||
Endoribonuclease Regnase 1/ ZC3H12 C-terminal domain; This is the C-terminal domain found in regnase-1, an RNase that directly cleaves mRNAs of inflammatory genes such as IL-6 and IL-12p40, and negatively regulates cellular inflammatory responses. The C-terminal domain is composed of three alpha helices and resembles ubiquitin associated protein 1 in structure. : Pssm-ID: 465803 Cd Length: 44 Bit Score: 90.93 E-value: 1.58e-22
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| UBA_6 | pfam18039 | UBA-like domain; This entry represents a UBA-like domain found at the N-terminus of ... |
163-204 | 4.56e-17 | |||||
UBA-like domain; This entry represents a UBA-like domain found at the N-terminus of ribonuclease ZC3 proteins. : Pssm-ID: 407876 Cd Length: 42 Bit Score: 75.52 E-value: 4.56e-17
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| zf-CCCH_2 | pfam14608 | RNA-binding, Nab2-type zinc finger; This is an unusual zinc-finger family, and is represented ... |
416-434 | 3.10e-04 | |||||
RNA-binding, Nab2-type zinc finger; This is an unusual zinc-finger family, and is represented by fingers 5-7 of Nab2. Nab2 ZnF5-7 are zinc-fingers of the type C-x8-C-x5-C-x3-H. Nab2 ZnFs function in the generation of export-competent mRNPs. Mab2 is a conserved polyadenosine-RNA-binding Zn finger protein required for both mRNA export and polyadenylation regulation and becomes attached to the mRNP after splicing and during or immediately after polyadenylation. The three ZnFs, 5-7, have almost identical folds and, most unusually, associate with one another to form a single coherent structural unit. ZnF5-7 bind to eight consecutive adenines, and chemical shift perturbations identify residues on each finger that interact with RNA. : Pssm-ID: 464217 Cd Length: 19 Bit Score: 38.65 E-value: 3.10e-04
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| Peptidase_S21 super family | cl25932 | Assemblin (Peptidase family S21); |
500-743 | 3.11e-04 | |||||
Assemblin (Peptidase family S21); The actual alignment was detected with superfamily member PHA03160: Pssm-ID: 330753 Cd Length: 499 Bit Score: 44.31 E-value: 3.11e-04
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| Name | Accession | Description | Interval | E-value | |||||
| PIN_Zc3h12-like | cd18729 | PRORP-like PIN domain of ribonuclease Zc3h12a and related proteins; Zc3h12a (zinc finger ... |
249-379 | 1.95e-100 | |||||
PRORP-like PIN domain of ribonuclease Zc3h12a and related proteins; Zc3h12a (zinc finger CCCH-type containing 12A, also known as MCPIP1/MCP induced protein 1 and Regnase-1) is a critical regulator of inflammatory response, with additional roles in defense against viruses and various stresses, cellular differentiation, and apoptosis. This subfamily also includes three less-studied mammalian homologs: Zc3h12b-d/Regnase-2-4. It belongs to the Zc3h12a-N4BP1-like PIN subfamily of the PRORP-Zc3h12a-like PIN family, the latter of which additionally includes human PRORP, also known as proteinaceous RNase P and mitochondrial RNase P protein subunit 3 (MRPP3), and Arabidopsis thaliana PRORP1-3. The PIN (PilT N terminus) domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members, additional metal coordinating residues can be found while some others lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. Pssm-ID: 350296 Cd Length: 131 Bit Score: 308.14 E-value: 1.95e-100
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| RNase_Zc3h12a | pfam11977 | Zc3h12a-like Ribonuclease NYN domain; This domain is found in the Zc3h12a protein which has ... |
245-401 | 6.95e-84 | |||||
Zc3h12a-like Ribonuclease NYN domain; This domain is found in the Zc3h12a protein which has shown to be a ribonuclease that controls the stability of a set of inflammatory genes. It has been suggested that this domain belongs to the PIN domain superfamily. This domain has also been identified as part of the NYN domain family. Pssm-ID: 403256 Cd Length: 154 Bit Score: 265.34 E-value: 6.95e-84
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| Regnase_1_C | pfam18561 | Endoribonuclease Regnase 1/ ZC3H12 C-terminal domain; This is the C-terminal domain found in ... |
836-879 | 1.58e-22 | |||||
Endoribonuclease Regnase 1/ ZC3H12 C-terminal domain; This is the C-terminal domain found in regnase-1, an RNase that directly cleaves mRNAs of inflammatory genes such as IL-6 and IL-12p40, and negatively regulates cellular inflammatory responses. The C-terminal domain is composed of three alpha helices and resembles ubiquitin associated protein 1 in structure. Pssm-ID: 465803 Cd Length: 44 Bit Score: 90.93 E-value: 1.58e-22
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| UBA_6 | pfam18039 | UBA-like domain; This entry represents a UBA-like domain found at the N-terminus of ... |
163-204 | 4.56e-17 | |||||
UBA-like domain; This entry represents a UBA-like domain found at the N-terminus of ribonuclease ZC3 proteins. Pssm-ID: 407876 Cd Length: 42 Bit Score: 75.52 E-value: 4.56e-17
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| zf-CCCH_2 | pfam14608 | RNA-binding, Nab2-type zinc finger; This is an unusual zinc-finger family, and is represented ... |
416-434 | 3.10e-04 | |||||
RNA-binding, Nab2-type zinc finger; This is an unusual zinc-finger family, and is represented by fingers 5-7 of Nab2. Nab2 ZnF5-7 are zinc-fingers of the type C-x8-C-x5-C-x3-H. Nab2 ZnFs function in the generation of export-competent mRNPs. Mab2 is a conserved polyadenosine-RNA-binding Zn finger protein required for both mRNA export and polyadenylation regulation and becomes attached to the mRNP after splicing and during or immediately after polyadenylation. The three ZnFs, 5-7, have almost identical folds and, most unusually, associate with one another to form a single coherent structural unit. ZnF5-7 bind to eight consecutive adenines, and chemical shift perturbations identify residues on each finger that interact with RNA. Pssm-ID: 464217 Cd Length: 19 Bit Score: 38.65 E-value: 3.10e-04
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| PHA03160 | PHA03160 | hypothetical protein; Provisional |
500-743 | 3.11e-04 | |||||
hypothetical protein; Provisional Pssm-ID: 165431 Cd Length: 499 Bit Score: 44.31 E-value: 3.11e-04
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| Name | Accession | Description | Interval | E-value | |||||
| PIN_Zc3h12-like | cd18729 | PRORP-like PIN domain of ribonuclease Zc3h12a and related proteins; Zc3h12a (zinc finger ... |
249-379 | 1.95e-100 | |||||
PRORP-like PIN domain of ribonuclease Zc3h12a and related proteins; Zc3h12a (zinc finger CCCH-type containing 12A, also known as MCPIP1/MCP induced protein 1 and Regnase-1) is a critical regulator of inflammatory response, with additional roles in defense against viruses and various stresses, cellular differentiation, and apoptosis. This subfamily also includes three less-studied mammalian homologs: Zc3h12b-d/Regnase-2-4. It belongs to the Zc3h12a-N4BP1-like PIN subfamily of the PRORP-Zc3h12a-like PIN family, the latter of which additionally includes human PRORP, also known as proteinaceous RNase P and mitochondrial RNase P protein subunit 3 (MRPP3), and Arabidopsis thaliana PRORP1-3. The PIN (PilT N terminus) domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members, additional metal coordinating residues can be found while some others lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. Pssm-ID: 350296 Cd Length: 131 Bit Score: 308.14 E-value: 1.95e-100
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| RNase_Zc3h12a | pfam11977 | Zc3h12a-like Ribonuclease NYN domain; This domain is found in the Zc3h12a protein which has ... |
245-401 | 6.95e-84 | |||||
Zc3h12a-like Ribonuclease NYN domain; This domain is found in the Zc3h12a protein which has shown to be a ribonuclease that controls the stability of a set of inflammatory genes. It has been suggested that this domain belongs to the PIN domain superfamily. This domain has also been identified as part of the NYN domain family. Pssm-ID: 403256 Cd Length: 154 Bit Score: 265.34 E-value: 6.95e-84
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| PIN_Zc3h12a-N4BP1-like | cd18719 | PRORP-like PIN domain of ribonuclease Zc3h12a, NEDD4-binding partner-1, and related proteins; ... |
249-378 | 6.28e-73 | |||||
PRORP-like PIN domain of ribonuclease Zc3h12a, NEDD4-binding partner-1, and related proteins; Zc3h12a (zinc finger CCCH-type containing 12A, also known as MCPIP1/MCP induced protein 1 and Regnase-1) is a critical regulator of inflammatory response, with additional roles in defense against viruses and various stresses, cellular differentiation, and apoptosis. This subfamily also includes Caenorhabditis elegans REGE-1 (REGnasE-1), which also functions as a cytoplasmic endonuclease. Additionally, it includes three less-studied mammalian homologs: Zc3h12b-d/Regnase-2-4, as well as N4BP1 (NEDD4-binding partner-1), NYNRIN (NYN domain and retroviral integrase containing, also known as CGIN1/Cousin of GIN1), and KHNYN (KH and NYN domain containing) protein. N4BP1, CGIN1, and KHNYN proteins are probably of retroviral origin. This subfamily belongs to the PRORP-Zc3h12a-like PIN family which in addition includes human PRORP, also known as proteinaceous RNase P and mitochondrial RNase P protein subunit 3 (MRPP3), and Arabidopsis thaliana PRORP1-3. The PIN (PilT N terminus) domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members, additional metal coordinating residues can be found while some others lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. Pssm-ID: 350286 Cd Length: 127 Bit Score: 235.17 E-value: 6.28e-73
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| PIN_N4BP1-like | cd18728 | PRORP-like PIN domain of NEDD4 binding protein 1 and related proteins; NEDD4-binding partner-1 ... |
249-378 | 3.99e-53 | |||||
PRORP-like PIN domain of NEDD4 binding protein 1 and related proteins; NEDD4-binding partner-1 (N4BP1) interacts with and is a substrate of NEDD4 ubiquitin ligase (neural precursor cell expressed, developmentally down-regulated 4, E3 ubiquitin protein ligase). It is also an inhibitor of the E3 ubiquitin-protein ligase ITCH, a NEDD4 structurally related E3. This subfamily additionally includes NYNRIN (NYN domain and retroviral integrase containing, also known as CGIN1/Cousin of GIN1), and KHNYN (KH and NYN domain containing) protein. N4BP1, CGIN1, and KHNYN proteins are probably of retroviral origin. This subfamily belongs to the Zc3h12a-N4BP1-like PIN subfamily of the PRORP-Zc3h12a-like PIN family, the latter of which additionally includes human PRORP, also known as proteinaceous RNase P and mitochondrial RNase P protein subunit 3 (MRPP3), and Arabidopsis thaliana PRORP1-3. The PIN (PilT N terminus) domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members, additional metal coordinating residues can be found while some others lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. Pssm-ID: 350295 Cd Length: 127 Bit Score: 180.77 E-value: 3.99e-53
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| PIN_PRORP-Zc3h12a-like | cd18671 | PIN domain of protein-only RNase P (PRORP), ribonuclease Zc3h12a, and related proteins; PRORPs ... |
249-378 | 1.85e-47 | |||||
PIN domain of protein-only RNase P (PRORP), ribonuclease Zc3h12a, and related proteins; PRORPs catalyze the maturation of the 5' end of precursor tRNAs in eukaryotes. This family includes human PRORP, also known as proteinaceous RNase P and mitochondrial RNase P protein subunit 3 (MRPP3), and Arabidopsis thaliana PRORP1-3, PRORP1 localizes to the chloroplast and the mitochondria, and PRORP2 and PRORP3 localize to the nucleus. Zc3h12a (zinc finger CCCH-type containing 12A, also known as MCPIP1/MCP induced protein 1 and Regnase-1) is a critical regulator of inflammatory response, with additional roles in defense against viruses and various stresses, cellular differentiation, and apoptosis. This PIN_PRORP-Zc3h12a-like family also includes Caenorhabditis elegans REGE-1 (REGnasE-1), which also functions as a cytoplasmic endonuclease. Additionally, it includes three less-studied mammalian homologs: Zc3h12b-d/Regnase-2-4, as well as N4BP1 (NEDD4-binding partner-1), NYNRIN (NYN domain and retroviral integrase containing, also known as CGIN1/Cousin of GIN1), and KHNYN (KH and NYN domain containing) protein. N4BP1, CGIN1, and KHNYN proteins are probably of retroviral origin. The PIN (PilT N terminus) domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members, additional metal coordinating residues can be found while some others lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. Pssm-ID: 350238 Cd Length: 126 Bit Score: 164.73 E-value: 1.85e-47
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| Regnase_1_C | pfam18561 | Endoribonuclease Regnase 1/ ZC3H12 C-terminal domain; This is the C-terminal domain found in ... |
836-879 | 1.58e-22 | |||||
Endoribonuclease Regnase 1/ ZC3H12 C-terminal domain; This is the C-terminal domain found in regnase-1, an RNase that directly cleaves mRNAs of inflammatory genes such as IL-6 and IL-12p40, and negatively regulates cellular inflammatory responses. The C-terminal domain is composed of three alpha helices and resembles ubiquitin associated protein 1 in structure. Pssm-ID: 465803 Cd Length: 44 Bit Score: 90.93 E-value: 1.58e-22
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| UBA_6 | pfam18039 | UBA-like domain; This entry represents a UBA-like domain found at the N-terminus of ... |
163-204 | 4.56e-17 | |||||
UBA-like domain; This entry represents a UBA-like domain found at the N-terminus of ribonuclease ZC3 proteins. Pssm-ID: 407876 Cd Length: 42 Bit Score: 75.52 E-value: 4.56e-17
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| zf-CCCH_2 | pfam14608 | RNA-binding, Nab2-type zinc finger; This is an unusual zinc-finger family, and is represented ... |
416-434 | 3.10e-04 | |||||
RNA-binding, Nab2-type zinc finger; This is an unusual zinc-finger family, and is represented by fingers 5-7 of Nab2. Nab2 ZnF5-7 are zinc-fingers of the type C-x8-C-x5-C-x3-H. Nab2 ZnFs function in the generation of export-competent mRNPs. Mab2 is a conserved polyadenosine-RNA-binding Zn finger protein required for both mRNA export and polyadenylation regulation and becomes attached to the mRNP after splicing and during or immediately after polyadenylation. The three ZnFs, 5-7, have almost identical folds and, most unusually, associate with one another to form a single coherent structural unit. ZnF5-7 bind to eight consecutive adenines, and chemical shift perturbations identify residues on each finger that interact with RNA. Pssm-ID: 464217 Cd Length: 19 Bit Score: 38.65 E-value: 3.10e-04
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| PHA03160 | PHA03160 | hypothetical protein; Provisional |
500-743 | 3.11e-04 | |||||
hypothetical protein; Provisional Pssm-ID: 165431 Cd Length: 499 Bit Score: 44.31 E-value: 3.11e-04
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| PIN_PRORP | cd18718 | PIN domain of protein-only RNase P (PRORP) and related proteins; PRORPs catalyze the ... |
249-359 | 4.43e-03 | |||||
PIN domain of protein-only RNase P (PRORP) and related proteins; PRORPs catalyze the maturation of the 5' end of precursor tRNAs in eukaryotes. This family includes human PRORP, also known as proteinaceous RNase P and mitochondrial RNase P protein subunit 3 (MRPP3), and Arabidopsis thaliana PRORP1-3, PRORP1 localizes to the chloroplast and the mitochondria, and PRORP2 and PRORP3 localize to the nucleus. This subfamily belongs to the PRORP-Zc3h12a-like PIN family which in addition includes Zc3h12a (also known as MCPIP1/MCP induced protein 1 and Regnase-1), Caenorhabditis elegans REGE-1 (REGnasE-1), Zc3h12b-d (also known as Regnase-2-4), N4BP1, and NYNRIN (also known as CGIN1). The PIN (PilT N terminus) domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members, additional metal coordinating residues can be found while some others lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. Pssm-ID: 350285 Cd Length: 124 Bit Score: 37.93 E-value: 4.43e-03
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| Blast search parameters | ||||
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