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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866338 249 IVIDGSNVAMSHGNKEVFSCRGIKLAVDWFLERGHKDITVFVPAWRKEQSRPDALITDQEILRKLEKEKILVFTPSRRVQ 328
Cdd:cd18729     1 IVIDGSNVAMSHGNKEVFSCRGIQLAVDWFRERGHRDITVFVPSWRKEQPRPDAPITDQEILRELEKEKILVFTPSRRVG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1622866338 329 GRRVVCYDDRFIVKLAFESDGIIVSNDNYRDLANEKPEWKKFIDERLLMYS 379
Cdd:cd18729    81 GKRVVCYDDRFILKLAYESDGIVVSNDNYRDLQNEKPEWKKFIEERLLMYS 131

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

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1622866338 163 YQTKLEFALKLGYSEEQVQLVLNKLGTDALINDILGELVKLG 204
Cdd:pfam18039   1 YKERVDFALKLGYSEEQVQAVLQKLGPEADTDKVLGELIKLG 42

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.

                          10
                  ....*....|....*....
gi 1622866338 416 PCPYGKKCTYGHKCKYYHP 434
Cdd:pfam14608   1 PCRFGGNCTFGPKCPFSHP 19

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866338 249 IVIDGSNVAMSHGNKEVFSCRGIKLAVDWFLERGHKDITVFVPAWRKEQSRPDALITDQEILRKLEKEKILVFTPSRRVQ 328
Cdd:cd18729     1 IVIDGSNVAMSHGNKEVFSCRGIQLAVDWFRERGHRDITVFVPSWRKEQPRPDAPITDQEILRELEKEKILVFTPSRRVG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1622866338 329 GRRVVCYDDRFIVKLAFESDGIIVSNDNYRDLANEKPEWKKFIDERLLMYS 379
Cdd:cd18729    81 GKRVVCYDDRFILKLAYESDGIVVSNDNYRDLQNEKPEWKKFIEERLLMYS 131

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.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1622866338 836 QDNREKIYINLCNIFPPDLVRIVMKRNPHMTDAQQLAAAILVEK 879
Cdd:pfam18561   1 QDEREKVYINLCGIFPPHLVRAVMARNPHLLDPQQLAAEILAEK 44

hypothetical protein; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866338 533 PQST--TSLSNGLPSGVHFPpqdqRPqGQYPPMMmatKNHGTLMPYEQYPKCD-SPVDIGYysMLNAYSNLSLSGPRSPE 609
Cdd:PHA03160  260 PKSTflSMLQNNLDNFKQHP----RP-ACFPPYF---PPQGAYMPYELYNHPPyLGDNIGY--MLPNGSYVPAIFPSRPN 329

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866338 610 RRFSLDTDyrissvasDCSSEGSMSCgssdsyvgYNDRSYVSSPDPQLEENLK---------CQHMHPHSRLNPQPFLQN 680
Cdd:PHA03160  330 KRKREDFD--------DCVFPGESSL--------YKDVLNLTKNISQLQDDLKdlkqaainqPNRIIPHHFSNPYSFDPG 393

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622866338 681 fHDPLTRVQSYSHEEPKFHHKPPL------PHLALHLQHPAVGArsscPGDYPSPPSSAHSKAPHLGRS 743
Cdd:PHA03160  394 -HAPFFRYAPYGAPKNDHHLLPPLacsqqlPMQPLHVQQAPMQA----PHVAPPPMQPPHVQQPRVLPS 457

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866338 249 IVIDGSNVAMSHGNKEVFSCRGIKLAVDWFLERGHKDITVFVPAWRKEQSRPDALITDQEILRKLEKEKILVFTPSRRVQ 328
Cdd:cd18729     1 IVIDGSNVAMSHGNKEVFSCRGIQLAVDWFRERGHRDITVFVPSWRKEQPRPDAPITDQEILRELEKEKILVFTPSRRVG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1622866338 329 GRRVVCYDDRFIVKLAFESDGIIVSNDNYRDLANEKPEWKKFIDERLLMYS 379
Cdd:cd18729    81 GKRVVCYDDRFILKLAYESDGIVVSNDNYRDLQNEKPEWKKFIEERLLMYS 131

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866338 249 IVIDGSNVAMSHGNKEVFSCRGIKLAVDWFLERGHkDITVFVPAWRKEQSRPDalITDQEILRKLEKEKILVFTPSRRVQ 328
Cdd:cd18719     1 VVIDGSNVAMSHGNGKVFSCKGIQICVRYFLERGH-EVTAFVPQFRLESPNPN--STDQDILEELERLGILVFTPSRRVP 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1622866338 329 GRRVVCYDDRFIVKLAFESDGIIVSNDNYRDLANEKPEWKKFIDERLLMY 378
Cdd:cd18719    78 GKRISSYDDRFILQLAEETDGVIVSNDNFRDLLNENPDWREIIEERLLPF 127

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866338 249 IVIDGSNVAMSHGNKEVFSCRGIKLAVDWFLERGH--KDITVFVPAWRKEQSRPDAlITDQEILRKLEKEKILVFTPSrr 326
Cdd:cd18671     1 AVIDGANVGLSHQNKESFSCRQLLLAVNWFLERSHnnTDPLVFLHKWRVEQPRPVP-PTDRHLLEEWEKKGILYATPP-- 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622866338 327 vqgrrvVCYDDRFIVKLAFESDGIIVSNDNYRDLANE---KPEWKKFIDERLLMY 378
Cdd:cd18671    78 ------GSNDDWYWLYAAYESKCLLVTNDEMRDHQFEllgRQFFKRWKEEHQVRY 126

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

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1622866338 163 YQTKLEFALKLGYSEEQVQLVLNKLGTDALINDILGELVKLG 204
Cdd:pfam18039   1 YKERVDFALKLGYSEEQVQAVLQKLGPEADTDKVLGELIKLG 42

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.

                          10
                  ....*....|....*....
gi 1622866338 416 PCPYGKKCTYGHKCKYYHP 434
Cdd:pfam14608   1 PCRFGGNCTFGPKCPFSHP 19