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 568965377  95 IVIDGSNVAMSHGNKEAFSCRGIRLAVDWFRDRGHTYIKVFVPSWRKEPSRSDTPIREQHVLEELERQAVLVYTPSRKVN 174
Cdd:cd18729    1 IVIDGSNVAMSHGNKEVFSCRGIQLAVDWFRERGHRDITVFVPSWRKEQPRPDAPITDQEILRELEKEKILVFTPSRRVG 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568965377 175 GKRVVCYDDRYIVKVAYEKDGIIVSNDNYRDLQNENPEWKWFIEQRLLMFS 225
Cdd:cd18729   81 GKRVVCYDDRFILKLAYESDGIVVSNDNYRDLQNEKPEWKKFIEERLLMYS 131

large tegument protein UL36; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965377  233 PPDDPLGRRGPTLSNFLSKKPRPPEPSwqhcpygkkctygvkcRFYHPERPHHGQLSVADELRAKTRAWLGGGAEEPRTP 312
Cdd:PHA03247 2604 DRGDPRGPAPPSPLPPDTHAPDPPPPS----------------PSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRA 2667

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965377  313 SARSRPTTARLLPQEPgehdLPPAPQPAVLAALNrsfarltFSDTAASGVVSQSRGPDWMPtGVPTSWAPPSLRAGSAAT 392
Cdd:PHA03247 2668 RRLGRAAQASSPPQRP----RRRAARPTVGSLTS-------LADPPPPPPTPEPAPHALVS-ATPLPPGPAAARQASPAL 2735

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965377  393 IGLPGMRSlrTPNNPLSPGDLGSPICPQArlserhrsrdmhSDLPPQRRPLEDPWALLPSSYCYLNHSVWSESAWGEDIF 472
Cdd:PHA03247 2736 PAAPAPPA--VPAGPATPGGPARPARPPT------------TAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSP 2801

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568965377  473 RGPSESAQPVANGGGTRPVHCSFFPPD-------QDHPVMASGPPLSDMAL 516
Cdd:PHA03247 2802 WDPADPPAAVLAPAAALPPAASPAGPLppptsaqPTAPPPPPGPPPPSLPL 2852

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 568965377  95 IVIDGSNVAMSHGNKEAFSCRGIRLAVDWFRDRGHTYIKVFVPSWRKEPSRSDTPIREQHVLEELERQAVLVYTPSRKVN 174
Cdd:cd18729    1 IVIDGSNVAMSHGNKEVFSCRGIQLAVDWFRERGHRDITVFVPSWRKEQPRPDAPITDQEILRELEKEKILVFTPSRRVG 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568965377 175 GKRVVCYDDRYIVKVAYEKDGIIVSNDNYRDLQNENPEWKWFIEQRLLMFS 225
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 568965377    3 HRSKMEFFQKLGYSQEDVVRVLGKLGDSALVNDVLQELIQTG 44
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 568965377  263 CPYGKKCTYGVKCRFYHP 280
Cdd:pfam14608   2 CRFGGNCTFGPKCPFSHP 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 568965377  95 IVIDGSNVAMSHGNKEAFSCRGIRLAVDWFRDRGHTYIKVFVPSWRKEPSRSDTPIREQHVLEELERQAVLVYTPSRKVN 174
Cdd:cd18729    1 IVIDGSNVAMSHGNKEVFSCRGIQLAVDWFRERGHRDITVFVPSWRKEQPRPDAPITDQEILRELEKEKILVFTPSRRVG 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568965377 175 GKRVVCYDDRYIVKVAYEKDGIIVSNDNYRDLQNENPEWKWFIEQRLLMFS 225
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 568965377  95 IVIDGSNVAMSHGNKEAFSCRGIRLAVDWFRDRGHTyIKVFVPSWRKEPSRSdtPIREQHVLEELERQAVLVYTPSRKVN 174
Cdd:cd18719    1 VVIDGSNVAMSHGNGKVFSCKGIQICVRYFLERGHE-VTAFVPQFRLESPNP--NSTDQDILEELERLGILVFTPSRRVP 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 568965377 175 GKRVVCYDDRYIVKVAYEKDGIIVSNDNYRDLQNENPEWKWFIEQRLLMF 224
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 568965377  95 IVIDGSNVAMSHGNKEAFSCRGIRLAVDWFRDRGH--TYIKVFVPSWRKEPSRSdTPIREQHVLEELERQAVLVYTPSrk 172
Cdd:cd18671    1 AVIDGANVGLSHQNKESFSCRQLLLAVNWFLERSHnnTDPLVFLHKWRVEQPRP-VPPTDRHLLEEWEKKGILYATPP-- 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568965377 173 vngkrvVCYDDRYIVKVAYEKDGIIVSNDNYRDLQNE---NPEWKWFIEQRLLMF 224
Cdd:cd18671   78 ------GSNDDWYWLYAAYESKCLLVTNDEMRDHQFEllgRQFFKRWKEEHQVRY 126

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965377  95 IVIDGSNVAMSHGNK-EAFSCRGIRLAVDWFRDRGHtyiKVFVPSwRKepSRSDTPIREQHVLEELERQAVLVYTPsrkv 173
Cdd:cd18718    1 VVIDGLNVAYYGQNFpGGFNAQQLLAVVEHLQKQNK---KVLVLG-RK--HMLKWSRWSPSAMKLIEKNASLFFTP---- 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568965377 174 NGkrvvCYDDRYIV--KVAYEKDGIIVSNDNYRD--------LQNENPEWKW 215
Cdd:cd18718   71 NG----SNDDPFWLyaALKSGPKTLFVSNDLMRDhkfqlldeLQRLFKKWQE 118

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 568965377  263 CPYGKKCTYGVKCRFYHP 280
Cdd:pfam14608   2 CRFGGNCTFGPKCPFSHP 19