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Conserved domains on  [gi|193202326|ref|NP_491985|]
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Endoribonuclease rege-1 [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RNase_Zc3h12a pfam11977
Zc3h12a-like Ribonuclease NYN domain; This domain is found in the Zc3h12a protein which has ...
 224-377 1.45e-78

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: 246.08  E-value: 1.45e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202326  224 SLRAVVVDGSNVAMLHGRKEVFSCAGLRECLNYFLERGHPEVLIFIPQYRREQprsDSPITDQHILQEIERH--IIYTPS 301
Cdd:pfam11977   1 GLRPIVIDGSNVAMSHGRQKKFSVRGLAIAVDYFVKRGHEEITVFVPQWRKEA---DEKITDQHELLELERLglIVFTPS 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 193202326  302 RNVNGRRVVCHDDRYILRTAELKDAVIVSNDEYRDLTRENPAWRKIVEERLLMFTFVEDKFMPPDDPSGRHGPRIE 377
Cdd:pfam11977  78 RTLDGKRIVSYDDRFILKLAEETDGVIVSNDNFRDLADENPEWIDIVEERLLMYTFVGDKFMPPDDPLGRVGPSLE 153
UBA_6 super family cl39454
UBA-like domain; This entry represents a UBA-like domain found at the N-terminus of ...
 118-158 1.02e-09

UBA-like domain; This entry represents a UBA-like domain found at the N-terminus of ribonuclease ZC3 proteins.


The actual alignment was detected with superfamily member pfam18039:

Pssm-ID: 407876  Cd Length: 42  Bit Score: 53.95  E-value: 1.02e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 193202326  118 PEVVEFATKLGYSTEQLSHVLNTIGVDSRMDDVLSELVKMG 158
Cdd:pfam18039   2 KERVDFALKLGYSEEQVQAVLQKLGPEADTDKVLGELIKLG 42
Regnase_1_C super family cl39881
Endoribonuclease Regnase 1/ ZC3H12 C-terminal domain; This is the C-terminal domain found in ...
 586-627 1.10e-05

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.


The actual alignment was detected with superfamily member pfam18561:

Pssm-ID: 465803  Cd Length: 44  Bit Score: 42.78  E-value: 1.10e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 193202326  586 AEVRSRVHFHLCNIFPHDFVESVMAANPEEVNAPVLCELIIR 627
Cdd:pfam18561   1 QDEREKVYINLCGIFPPHLVRAVMARNPHLLDPQQLAAEILA 42
 
Name Accession Description Interval E-value
RNase_Zc3h12a pfam11977
Zc3h12a-like Ribonuclease NYN domain; This domain is found in the Zc3h12a protein which has ...
 224-377 1.45e-78

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: 246.08  E-value: 1.45e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202326  224 SLRAVVVDGSNVAMLHGRKEVFSCAGLRECLNYFLERGHPEVLIFIPQYRREQprsDSPITDQHILQEIERH--IIYTPS 301
Cdd:pfam11977   1 GLRPIVIDGSNVAMSHGRQKKFSVRGLAIAVDYFVKRGHEEITVFVPQWRKEA---DEKITDQHELLELERLglIVFTPS 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 193202326  302 RNVNGRRVVCHDDRYILRTAELKDAVIVSNDEYRDLTRENPAWRKIVEERLLMFTFVEDKFMPPDDPSGRHGPRIE 377
Cdd:pfam11977  78 RTLDGKRIVSYDDRFILKLAEETDGVIVSNDNFRDLADENPEWIDIVEERLLMYTFVGDKFMPPDDPLGRVGPSLE 153
PIN_Zc3h12-like cd18729
PRORP-like PIN domain of ribonuclease Zc3h12a and related proteins; Zc3h12a (zinc finger ...
 228-356 4.67e-69

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: 220.32  E-value: 4.67e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202326 228 VVVDGSNVAMLHGRKEVFSCAGLRECLNYFLERGHPEVLIFIPQYRREQPRSDSPITDQHILQEIE--RHIIYTPSRNVN 305
Cdd:cd18729    1 IVIDGSNVAMSHGNKEVFSCRGIQLAVDWFRERGHRDITVFVPSWRKEQPRPDAPITDQEILRELEkeKILVFTPSRRVG 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 193202326 306 GRRVVCHDDRYILRTAELKDAVIVSNDEYRDLTRENPAWRKIVEERLLMFT 356
Cdd:cd18729   81 GKRVVCYDDRFILKLAYESDGIVVSNDNYRDLQNEKPEWKKFIEERLLMYS 131
UBA_6 pfam18039
UBA-like domain; This entry represents a UBA-like domain found at the N-terminus of ...
 118-158 1.02e-09

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: 53.95  E-value: 1.02e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 193202326  118 PEVVEFATKLGYSTEQLSHVLNTIGVDSRMDDVLSELVKMG 158
Cdd:pfam18039   2 KERVDFALKLGYSEEQVQAVLQKLGPEADTDKVLGELIKLG 42
Regnase_1_C pfam18561
Endoribonuclease Regnase 1/ ZC3H12 C-terminal domain; This is the C-terminal domain found in ...
 586-627 1.10e-05

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: 42.78  E-value: 1.10e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 193202326  586 AEVRSRVHFHLCNIFPHDFVESVMAANPEEVNAPVLCELIIR 627
Cdd:pfam18561   1 QDEREKVYINLCGIFPPHLVRAVMARNPHLLDPQQLAAEILA 42
 
Name Accession Description Interval E-value
RNase_Zc3h12a pfam11977
Zc3h12a-like Ribonuclease NYN domain; This domain is found in the Zc3h12a protein which has ...
 224-377 1.45e-78

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: 246.08  E-value: 1.45e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202326  224 SLRAVVVDGSNVAMLHGRKEVFSCAGLRECLNYFLERGHPEVLIFIPQYRREQprsDSPITDQHILQEIERH--IIYTPS 301
Cdd:pfam11977   1 GLRPIVIDGSNVAMSHGRQKKFSVRGLAIAVDYFVKRGHEEITVFVPQWRKEA---DEKITDQHELLELERLglIVFTPS 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 193202326  302 RNVNGRRVVCHDDRYILRTAELKDAVIVSNDEYRDLTRENPAWRKIVEERLLMFTFVEDKFMPPDDPSGRHGPRIE 377
Cdd:pfam11977  78 RTLDGKRIVSYDDRFILKLAEETDGVIVSNDNFRDLADENPEWIDIVEERLLMYTFVGDKFMPPDDPLGRVGPSLE 153
PIN_Zc3h12-like cd18729
PRORP-like PIN domain of ribonuclease Zc3h12a and related proteins; Zc3h12a (zinc finger ...
 228-356 4.67e-69

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: 220.32  E-value: 4.67e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202326 228 VVVDGSNVAMLHGRKEVFSCAGLRECLNYFLERGHPEVLIFIPQYRREQPRSDSPITDQHILQEIE--RHIIYTPSRNVN 305
Cdd:cd18729    1 IVIDGSNVAMSHGNKEVFSCRGIQLAVDWFRERGHRDITVFVPSWRKEQPRPDAPITDQEILRELEkeKILVFTPSRRVG 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 193202326 306 GRRVVCHDDRYILRTAELKDAVIVSNDEYRDLTRENPAWRKIVEERLLMFT 356
Cdd:cd18729   81 GKRVVCYDDRFILKLAYESDGIVVSNDNYRDLQNEKPEWKKFIEERLLMYS 131
PIN_Zc3h12a-N4BP1-like cd18719
PRORP-like PIN domain of ribonuclease Zc3h12a, NEDD4-binding partner-1, and related proteins; ...
 228-355 2.85e-68

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: 218.23  E-value: 2.85e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202326 228 VVVDGSNVAMLHGRKEVFSCAGLRECLNYFLERGHpEVLIFIPQYRREQPRSdsPITDQHILQEIER--HIIYTPSRNVN 305
Cdd:cd18719    1 VVIDGSNVAMSHGNGKVFSCKGIQICVRYFLERGH-EVTAFVPQFRLESPNP--NSTDQDILEELERlgILVFTPSRRVP 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 193202326 306 GRRVVCHDDRYILRTAELKDAVIVSNDEYRDLTRENPAWRKIVEERLLMF 355
Cdd:cd18719   78 GKRISSYDDRFILQLAEETDGVIVSNDNFRDLLNENPDWREIIEERLLPF 127
PIN_N4BP1-like cd18728
PRORP-like PIN domain of NEDD4 binding protein 1 and related proteins; NEDD4-binding partner-1 ...
 228-355 1.53e-40

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: 143.79  E-value: 1.53e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202326 228 VVVDGSNVAMLHGRKEVFSCAGLRECLNYFLERGHPEVLIFIPQYRReqpRSDSPITDQHILQEIE--RHIIYTPSRNVN 305
Cdd:cd18728    1 IVIDGSNVAMVHGLQHFFSCRGIAIAVEYFWKRGHRNITVFVPQWRT---KRDPNVTEQHFLTQLQelGILSLTPSRMVL 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 193202326 306 GRRVVCHDDRYILRTAELKDAVIVSNDEYRDLTRENPAWRKIVEERLLMF 355
Cdd:cd18728   78 GKRIASHDDRFLLHLAEKTGGIIVTNDNFREFVNESPSWREIIKERLLQY 127
PIN_PRORP-Zc3h12a-like cd18671
PIN domain of protein-only RNase P (PRORP), ribonuclease Zc3h12a, and related proteins; PRORPs ...
 228-355 1.81e-31

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: 118.89  E-value: 1.81e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202326 228 VVVDGSNVAMLHGRKEVFSCAGLRECLNYFLERGHPE--VLIFIPQYRREQPRSdSPITDQHILQEIERH--IIYTPSrn 303
Cdd:cd18671    1 AVIDGANVGLSHQNKESFSCRQLLLAVNWFLERSHNNtdPLVFLHKWRVEQPRP-VPPTDRHLLEEWEKKgiLYATPP-- 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 193202326 304 vngrrvVCHDDRYILRTAELKDAVIVSNDEYRDLTRE---NPAWRKIVEERLLMF 355
Cdd:cd18671   78 ------GSNDDWYWLYAAYESKCLLVTNDEMRDHQFEllgRQFFKRWKEEHQVRY 126
UBA_6 pfam18039
UBA-like domain; This entry represents a UBA-like domain found at the N-terminus of ...
 118-158 1.02e-09

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: 53.95  E-value: 1.02e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 193202326  118 PEVVEFATKLGYSTEQLSHVLNTIGVDSRMDDVLSELVKMG 158
Cdd:pfam18039   2 KERVDFALKLGYSEEQVQAVLQKLGPEADTDKVLGELIKLG 42
PIN_PRORP cd18718
PIN domain of protein-only RNase P (PRORP) and related proteins; PRORPs catalyze the ...
 228-336 3.24e-07

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: 49.49  E-value: 3.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202326 228 VVVDGSNVAMLHGRK-EVFSCAGLRECLNYFLERGHPeVLIFIPQYRREQPRSDSPitDQHILQEiERHIIYTPsrnvNG 306
Cdd:cd18718    1 VVIDGLNVAYYGQNFpGGFNAQQLLAVVEHLQKQNKK-VLVLGRKHMLKWSRWSPS--AMKLIEK-NASLFFTP----NG 72

                         90       100       110
                 ....*....|....*....|....*....|...
gi 193202326 307 rrvvCHDDRYILrTAELK---DAVIVSNDEYRD 336
Cdd:cd18718   73 ----SNDDPFWL-YAALKsgpKTLFVSNDLMRD 100
Regnase_1_C pfam18561
Endoribonuclease Regnase 1/ ZC3H12 C-terminal domain; This is the C-terminal domain found in ...
 586-627 1.10e-05

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: 42.78  E-value: 1.10e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 193202326  586 AEVRSRVHFHLCNIFPHDFVESVMAANPEEVNAPVLCELIIR 627
Cdd:pfam18561   1 QDEREKVYINLCGIFPPHLVRAVMARNPHLLDPQQLAAEILA 42
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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