Mut7-C ubiquitin; This member of the ubiquitin superfamily is found at the N-terminus of Mut7-C like RNAses, suggestive of an RNA-binding role.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495917276    1 MVTATFRFYEELNDFLAPAQRRRDLSCPCARAATVKHMIEALGVPHTEVELILVNGESSPFERIVCDGDRIAVYPKFESF 80
Cdd:pfam14451   1 MPTATFRFYAELNDFLPRARRQRTAARAFDGGATVKHMIEALGVPHTEVGLILVNGESVPFSHIPADGDRVAVYPVFEAL 80

                  .
gi 495917276   81 D 81
Cdd:pfam14451  81 D 81

Mut7-C RNAse domain; RNAse domain of the PIN fold with an inserted Zinc Ribbon at the C terminus.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495917276   96 IRFVADAHLGGLAHLLRMTGFDTLYDNHFEDSEIARIASDEKRIVLTRDRELLKRRGITHGCYVRAIRSSLQVREIFSRL 175
Cdd:pfam01927   1 PRFLLDAMLGKLARYLRMLGYDTLYDNDYEDDELLRIAAKEGRILLTRDRGLLKRRELTHGVYVRSLDPEEQLREVIARL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495917276  176 DLARSARP-FSLCLDCNVPLRRIGKTDVDGRVPEGVFERHEHFVTCPHCQRVFWEGSHWRKMRTLV 240
Cdd:pfam01927  81 GLALSLKPeFSRCLLCNGPLRPVEKEEVAGRVPPKVYERYDEFWRCPGCGRVYWEGSHWRRMRELL 146

uncharacterized subgroup of the Mut7-C-like family of the PIN domain superfamily; The Mut7-C-like family of the PIN domain superfamily includes the C-terminal domain of Caenorhabditis elegans Mut-7 (also known as exonuclease 3'-5' domain-containing protein 3 homolog). Mut-7 is involved in RNA interference (RNAi) and transposon silencing in C. elegans. The Mut7-C PIN domain family is recognized as a genuine PIN domain, however it is not included it in the CDD PIN domain superfamily hierarchical model as it is lacks a core strand and helix (H3 and S3). The PIN (PilT N terminus) domain belongs to a large nuclease superfamily, and were originally named for their sequence similarity to the N-terminal domain of an annotated pili biogenesis protein, PilT, a domain fusion between a PIN-domain and a PilT ATPase domain. 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. Other PIN domain families are: the FEN-like PIN domain family which includes the PIN domains of Flap endonuclease-1 (FEN1), Exonuclease-1 (EXO1), Mkt1, Gap endonuclease 1 (GEN1), and Xeroderma pigmentosum complementation group G (XPG) nuclease, 5'-3' exonucleases of DNA polymerase I and bacteriophage T4- and T5-5' nucleases; the VapC-like PIN domain family which includes toxins of prokaryotic toxin/antitoxin operons FitAB and VapBC, as well as, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and, rRNA-processing protein Fcf1; the LabA-like PIN domain family which includes the PIN domains of Synechococcus elongatus LabA (low-amplitude and bright); the PRORP-Zc3h12a-like PIN domain family which includes the PIN domains of of RNase P (PRORP), ribonuclease Zc3h12a; and Bacillus subtilis YacP/Rae1-like PIN domains.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495917276  98 FVADAHLGGLAHLLRMTGFDTLYDNHFEDSEIARIASDEKRIVLTRDRELLKRRGITHGCYV 159
Cdd:cd18771    1 FLLDVHLGTLARLLRLLGFDTAYDNTYADATLAALADAEDRILLSRDRGLLKRRGIRRGAFV 62

ubiquitin-like (Ubl) domain found in small archaeal modifier protein (SAMP2); Ubiquitin-like small archaeal modifier protein 2 (SAMP2) shows a beta-grasp fold of Ub, suggesting that this archaeal Ubl molecule is more closely related to eukaryotic Ub and Ubls than to its prokaryotic counterpart. Several Ub-like structural features such as an N-terminal single lysine residue and di-glycine motif at the C-terminus, spatially isolated, implicate formation of a poly-SAMPylated chainpoly-SAMPylation. SAMP2 can form covalent conjugates with its protein targets through an isopeptide linkage via their C-terminal diglycine motif in a streamlined archaeal E1-dependent pathway. It also forms homo-conjugates through the intermolecular isopeptide bond between the C-terminal Gly and the Lys58 side chain, a feature that likely resembles polyubiquitination. SAMP2 is involved in sulfur transfer during tRNA thiolation much like Urm1. This family also includes uncharacterized proteins such as Methanothermococcus thermolithotrophicus Mth1743, Pyrococcus furiosus PF1061 and others, all closely related to proteins MoaD.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 495917276  31 RAATVKHMIEALGVPHTEVeLILVNGESSPFERIVCDGDRIAVYP 75
Cdd:cd17506   19 GGATVRDLLRTLSLPPEEV-IVVVNGEVVPEDDPLKDGDIIRLIP 62

Mut7-C RNAse domain; RNAse domain of the PIN fold with an inserted Zinc Ribbon at the C terminus.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495917276   96 IRFVADAHLGGLAHLLRMTGFDTLYDNHFEDSEIARIASDEKRIVLTRDRELLKRRGITHGCYVRAIRSSLQVREIFSRL 175
Cdd:pfam01927   1 PRFLLDAMLGKLARYLRMLGYDTLYDNDYEDDELLRIAAKEGRILLTRDRGLLKRRELTHGVYVRSLDPEEQLREVIARL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495917276  176 DLARSARP-FSLCLDCNVPLRRIGKTDVDGRVPEGVFERHEHFVTCPHCQRVFWEGSHWRKMRTLV 240
Cdd:pfam01927  81 GLALSLKPeFSRCLLCNGPLRPVEKEEVAGRVPPKVYERYDEFWRCPGCGRVYWEGSHWRRMRELL 146

uncharacterized subgroup of the Mut7-C-like family of the PIN domain superfamily; The Mut7-C-like family of the PIN domain superfamily includes the C-terminal domain of Caenorhabditis elegans Mut-7 (also known as exonuclease 3'-5' domain-containing protein 3 homolog). Mut-7 is involved in RNA interference (RNAi) and transposon silencing in C. elegans. The Mut7-C PIN domain family is recognized as a genuine PIN domain, however it is not included it in the CDD PIN domain superfamily hierarchical model as it is lacks a core strand and helix (H3 and S3). The PIN (PilT N terminus) domain belongs to a large nuclease superfamily, and were originally named for their sequence similarity to the N-terminal domain of an annotated pili biogenesis protein, PilT, a domain fusion between a PIN-domain and a PilT ATPase domain. 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. Other PIN domain families are: the FEN-like PIN domain family which includes the PIN domains of Flap endonuclease-1 (FEN1), Exonuclease-1 (EXO1), Mkt1, Gap endonuclease 1 (GEN1), and Xeroderma pigmentosum complementation group G (XPG) nuclease, 5'-3' exonucleases of DNA polymerase I and bacteriophage T4- and T5-5' nucleases; the VapC-like PIN domain family which includes toxins of prokaryotic toxin/antitoxin operons FitAB and VapBC, as well as, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and, rRNA-processing protein Fcf1; the LabA-like PIN domain family which includes the PIN domains of Synechococcus elongatus LabA (low-amplitude and bright); the PRORP-Zc3h12a-like PIN domain family which includes the PIN domains of of RNase P (PRORP), ribonuclease Zc3h12a; and Bacillus subtilis YacP/Rae1-like PIN domains.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495917276  98 FVADAHLGGLAHLLRMTGFDTLYDNHFEDSEIARIASDEKRIVLTRDRELLKRRGITHGCYV 159
Cdd:cd18771    1 FLLDVHLGTLARLLRLLGFDTAYDNTYADATLAALADAEDRILLSRDRGLLKRRGIRRGAFV 62

Predicted nuclease, contains PIN domain, potential toxin-antitoxin system component [General function prediction only];

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495917276  96 IRFVADAHLG-GLAHLLRMTGFDTLY-----DNHFEDSEIARIASDEKRIVLTRDR---ELLKRRGITH 155
Cdd:COG4634    1 MKFLLDENLSpRLVEWLREAGHDVLHvrdlgLPGASDEEILEYARREGRIIVTKDKdfgELLALSGAPP 69

ThiS family; ThiS (thiaminS) is a 66 aa protein involved in sulphur transfer. ThiS is coded in the thiCEFSGH operon in E. coli. This family of proteins have two conserved Glycines at the COOH terminus. Thiocarboxylate is formed at the last G in the activation process. Sulphur is transferred from ThiI to ThiS in a reaction catalyzed by IscS. MoaD, a protein involved sulphur transfer in molybdopterin synthesis, is about the same length and shows limited sequence similarity to ThiS. Both have the conserved GG at the COOH end.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 495917276   32 AATVKHMIEALGVPHTEVE---LILVNGESSPFER---IVCDGDRIAVYP 75
Cdd:pfam02597  20 GATVAELLEALGLRYPELRervAVAVNGEIVPRLWldtPLKDGDEVAIIP 69

ubiquitin-like (Ubl) domain found in small archaeal modifier protein (SAMP2); Ubiquitin-like small archaeal modifier protein 2 (SAMP2) shows a beta-grasp fold of Ub, suggesting that this archaeal Ubl molecule is more closely related to eukaryotic Ub and Ubls than to its prokaryotic counterpart. Several Ub-like structural features such as an N-terminal single lysine residue and di-glycine motif at the C-terminus, spatially isolated, implicate formation of a poly-SAMPylated chainpoly-SAMPylation. SAMP2 can form covalent conjugates with its protein targets through an isopeptide linkage via their C-terminal diglycine motif in a streamlined archaeal E1-dependent pathway. It also forms homo-conjugates through the intermolecular isopeptide bond between the C-terminal Gly and the Lys58 side chain, a feature that likely resembles polyubiquitination. SAMP2 is involved in sulfur transfer during tRNA thiolation much like Urm1. This family also includes uncharacterized proteins such as Methanothermococcus thermolithotrophicus Mth1743, Pyrococcus furiosus PF1061 and others, all closely related to proteins MoaD.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 495917276  31 RAATVKHMIEALGVPHTEVeLILVNGESSPFERIVCDGDRIAVYP 75
Cdd:cd17506   19 GGATVRDLLRTLSLPPEEV-IVVVNGEVVPEDDPLKDGDIIRLIP 62