NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|488373628|ref|WP_002443013|]
View 

ribonuclease Z [Staphylococcus caprae]

Protein Classification

ribonuclease Z( domain architecture ID 10021201)

ribonuclease Z is a tRNA 3-prime endonuclease that is involved in the maturation of tRNA, such as processing of tRNAs that lack an encoded CCA motif at the 3' end, to prepare for the addition of the motif by tRNA nucleotidyltransferase

CATH:  3.60.15.10
EC:  3.1.26.11
Gene Ontology:  GO:0042781|GO:0046872
PubMed:  17597585|11471246|17363966|12032089
SCOP:  3001057

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 2-306 5.64e-132

ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of endonuclease or exonuclease activity, and differs in different species. Member of this family are ribonuclease Z, a tRNA 3-prime endonuclease that processes tRNAs to prepare for addition of CCA. In species where all tRNA sequences already have the CCA tail, such as E. coli, the need for such an enzyme is unclear. Protein similar to the E. coli enzyme, matched by TIGRFAMs model TIGR02649, are designated ribonuclease BN. [Transcription, RNA processing]


:

Pssm-ID: 274246 [Multi-domain]  Cd Length: 299  Bit Score: 376.56  E-value: 5.64e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373628    2 EVTFFGTSAGLPTKERNTQSIALNLEpysNSVWLFDVGEGTQHQILHHSIKLGKVDHIFITHMHGDHIFGLPGLLTSRSF 81
Cdd:TIGR02651   1 EITFLGTGGGVPTKERNLPSIALKLN---GELWLFDCGEGTQRQMLRSGISPMKIDRIFITHLHGDHILGLPGLLSTMSF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373628   82 QGGEnKPLTLIGPKGIQNYIETSLKLSESHLNYPITYIEINQQFT-YHHEGFTVKAELLNHGITSYGYRIEAPTTPGTID 160
Cdd:TIGR02651  78 QGRK-EPLTIYGPPGIKEFIETSLRVSYTYLNYPIKIHEIEEGGLvFEDDGFKVEAFPLDHSIPSLGYRFEEKDRPGKFD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373628  161 VEALKAIGLNPGPKYQEVKVQDTFEH-NGLMYQSSDFKGAAKPGPVVAIFGDTKPCDNEYILAQDADVMIHESTYIEGEK 239
Cdd:TIGR02651 157 REKAKELGIPPGPLYGKLKRGETVTLiDGRIIDPEDVLGPPRKGRKIAYTGDTRPCEEVIEFAKNADLLIHEATFLDEDK 236

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488373628  240 TLANNYHHSHIDDVFDLIKNANVRKSLITHISNRYNIEEVEsIYEALNNQsdvPNFYFVKDFDTYKI 306
Cdd:TIGR02651 237 KLAKEYGHSTAAQAAEIAKEANVKRLILTHISPRYSDEEEL-LEEAKKIF---PNTYIAEDFMEIEI 299
 
Name Accession Description Interval E-value
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 2-306 5.64e-132

ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of endonuclease or exonuclease activity, and differs in different species. Member of this family are ribonuclease Z, a tRNA 3-prime endonuclease that processes tRNAs to prepare for addition of CCA. In species where all tRNA sequences already have the CCA tail, such as E. coli, the need for such an enzyme is unclear. Protein similar to the E. coli enzyme, matched by TIGRFAMs model TIGR02649, are designated ribonuclease BN. [Transcription, RNA processing]


Pssm-ID: 274246 [Multi-domain]  Cd Length: 299  Bit Score: 376.56  E-value: 5.64e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373628    2 EVTFFGTSAGLPTKERNTQSIALNLEpysNSVWLFDVGEGTQHQILHHSIKLGKVDHIFITHMHGDHIFGLPGLLTSRSF 81
Cdd:TIGR02651   1 EITFLGTGGGVPTKERNLPSIALKLN---GELWLFDCGEGTQRQMLRSGISPMKIDRIFITHLHGDHILGLPGLLSTMSF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373628   82 QGGEnKPLTLIGPKGIQNYIETSLKLSESHLNYPITYIEINQQFT-YHHEGFTVKAELLNHGITSYGYRIEAPTTPGTID 160
Cdd:TIGR02651  78 QGRK-EPLTIYGPPGIKEFIETSLRVSYTYLNYPIKIHEIEEGGLvFEDDGFKVEAFPLDHSIPSLGYRFEEKDRPGKFD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373628  161 VEALKAIGLNPGPKYQEVKVQDTFEH-NGLMYQSSDFKGAAKPGPVVAIFGDTKPCDNEYILAQDADVMIHESTYIEGEK 239
Cdd:TIGR02651 157 REKAKELGIPPGPLYGKLKRGETVTLiDGRIIDPEDVLGPPRKGRKIAYTGDTRPCEEVIEFAKNADLLIHEATFLDEDK 236

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488373628  240 TLANNYHHSHIDDVFDLIKNANVRKSLITHISNRYNIEEVEsIYEALNNQsdvPNFYFVKDFDTYKI 306
Cdd:TIGR02651 237 KLAKEYGHSTAAQAAEIAKEANVKRLILTHISPRYSDEEEL-LEEAKKIF---PNTYIAEDFMEIEI 299
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 3-304 7.76e-103

Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as tRNase Z or 3' tRNase) catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors. Escherichia coli zinc phosphodiesterase (ZiPD, also known as ecoZ, tRNase Z, or RNase BN) is a 3' tRNA-processing endonuclease, encoded by the elaC gene. Two forms of RNase Z exist in eukaryotes, one long (ELAC2) and one short form (ELAC1), the former may have resulted from a duplication of the shorter enzyme; this subgroup includes the short form (ELAC1). Only the short form exists in bacteria. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293803 [Multi-domain]  Cd Length: 247  Bit Score: 300.91  E-value: 7.76e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373628   3 VTFFGTSAGLPTKERNTQSIALNLEpysNSVWLFDVGEGTQHQILHHSIKLGKVDHIFITHMHGDHIFGLPGLLTSRSFQ 82
Cdd:cd07717    1 LTFLGTGSAVPTPERNLSSIALRLE---GELWLFDCGEGTQRQLLRAGLSPSKIDRIFITHLHGDHILGLPGLLSTMSLL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373628  83 GGEnKPLTLIGPKGIQNYIETSLKLSESHLNYPITYIEIN--QQFTYHHEGFTVKAELLNHGITSYGYRIEApttpgtid 160
Cdd:cd07717   78 GRT-EPLTIYGPKGLKEFLETLLRLSASRLPYPIEVHELEpdPGLVFEDDGFTVTAFPLDHRVPCFGYRFEE-------- 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373628 161 vealkaiglnpgpkyqevkvqdtfehnglmyqssdfkgaakpGPVVAIFGDTKPCDNEYILAQDADVMIHESTYIEGEKT 240
Cdd:cd07717  149 ------------------------------------------GRKIAYLGDTRPCEGLVELAKGADLLIHEATFLDDDAE 186

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488373628 241 LANNYHHSHIDDVFDLIKNANVRKSLITHISNRY-NIEEVESiyEAlnnQSDVPNFYFVKDFDTY 304
Cdd:cd07717  187 KAKETGHSTAKQAAEIAKKAGVKKLVLTHFSARYkDPEELLK--EA---RAVFPNTILAEDFMTI 246
PRK00055 PRK00055
ribonuclease Z; Reviewed
 1-306 3.46e-94

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 279.76  E-value: 3.46e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373628   1 MEVTFFGTSAGLPTKERNTQSIALNLEpysNSVWLFDVGEGTQHQILHHSIKLGKVDHIFITHMHGDHIFGLPGLLTSRS 80
Cdd:PRK00055   2 MELTFLGTGSGVPTPTRNVSSILLRLG---GELFLFDCGEGTQRQLLKTGIKPRKIDKIFITHLHGDHIFGLPGLLSTRS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373628  81 FQGGEnKPLTLIGPKGIQNYIETSLKLSeshlnypityieinqqftyhhegftvkaellnhgiTSYGYRIEAPTTPGTID 160
Cdd:PRK00055  79 LSGRT-EPLTIYGPKGIKEFVETLLRAS-----------------------------------GSLGYRIAEKDKPGKLD 122

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373628 161 VEALKAIGLNPGPKYQEVKVQDTFE-HNGLMYQSSDFKGAAKPGPVVAIFGDTKPCDNEYILAQDADVMIHESTYIEGEK 239
Cdd:PRK00055 123 AEKLKALGVPPGPLFGKLKRGEDVTlEDGRIINPADVLGPPRKGRKVAYCGDTRPCEALVELAKGADLLVHEATFGDEDE 202

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488373628 240 TLANNYHHSHIDDVFDLIKNANVRKSLITHISNRYNIEEVESIYEAlnnQSDVPNFYFVKDFDTYKI 306
Cdd:PRK00055 203 ELAKEYGHSTARQAAEIAKEAGVKRLILTHFSPRYTGDPEELLKEA---REIFPNTELAEDLMRVEV 266
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
1-306 1.34e-87

Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 262.05  E-value: 1.34e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373628   1 MEVTFFGTSAGLPTKERNTQSIALNLEpysNSVWLFDVGEGTQHQILHHSIKLGKVDHIFITHMHGDHIFGLPGLLTSRS 80
Cdd:COG1234    1 MKLTFLGTGGAVPTPGRATSSYLLEAG---GERLLIDCGEGTQRQLLRAGLDPRDIDAIFITHLHGDHIAGLPGLLSTRS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373628  81 FQGGEnKPLTLIGPKGIQNYIETSLKLSESHLNYPITYIEINQQFTYHHEGFTVKAELLNHGITSYGYRIEApttpgtid 160
Cdd:COG1234   78 LAGRE-KPLTIYGPPGTKEFLEALLKASGTDLDFPLEFHEIEPGEVFEIGGFTVTAFPLDHPVPAYGYRFEE-------- 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373628 161 vealkaiglnpgpkyqevkvqdtfehnglmyqssdfkgaakPGPVVAIFGDTKPCDNEYILAQDADVMIHESTYIEGEKT 240
Cdd:COG1234  149 -----------------------------------------PGRSLVYSGDTRPCEALVELAKGADLLIHEATFLDEEAE 187

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488373628 241 LANNYHHSHIDDVFDLIKNANVRKSLITHISNRYN-----IEEVESIYEAlnnqsdvpNFYFVKDFDTYKI 306
Cdd:COG1234  188 LAKETGHSTAKEAAELAAEAGVKRLVLTHFSPRYDdpeelLAEARAVFPG--------PVELAEDGMVIEL 250
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 31-134 1.63e-08

Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins contain this domain. These proteins include thiolesterases, members of the glyoxalase II family, that catalyse the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid and a competence protein that is essential for natural transformation in Neisseria gonorrhoeae and could be a transporter involved in DNA uptake. Except for the competence protein these proteins bind two zinc ions per molecule as cofactor.


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 53.33  E-value: 1.63e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373628    31 NSVWLFDVGEGTQHQILHHSIKLG--KVDHIFITHMHGDHIFGLPGLLtsrsfqggENKPLTLIGPKGIQNYIETSLKL- 107
Cdd:smart00849   9 GGAILIDTGPGEAEDLLAELKKLGpkKIDAIILTHGHPDHIGGLPELL--------EAPGAPVYAPEGTAELLKDLLALl 80

                           90       100       110
                   ....*....|....*....|....*....|.
gi 488373628   108 ----SESHLNYPITYIEINQQFTYHHEGFTV 134
Cdd:smart00849  81 gelgAEAEPAPPDRTLKDGDELDLGGGELEV 111
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 35-154 3.16e-07

Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and is related to pfam00753.


Pssm-ID: 432732 [Multi-domain]  Cd Length: 196  Bit Score: 50.00  E-value: 3.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373628   35 LFDVGEGTQHQIL--HHSIKLG--KVDHIFITHMHGDHIFGLPGLLtsrsfqggENKPLTLIGPKGIQNYIETSLKL--S 108
Cdd:pfam12706   4 LIDPGPDLRQQALpaLQPGRLRddPIDAVLLTHDHYDHLAGLLDLR--------EGRPRPLYAPLGVLAHLRRNFPYlfL 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 488373628  109 ESHLNYPITYIEINQQFTYHHEGFTVKA---------ELLNHGITSYGYRIEAPT 154
Cdd:pfam12706  76 LEHYGVRVHEIDWGESFTVGDGGLTVTAtparhgsprGLDPNPGDTLGFRIEGPG 130
 
Name Accession Description Interval E-value
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 2-306 5.64e-132

ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of endonuclease or exonuclease activity, and differs in different species. Member of this family are ribonuclease Z, a tRNA 3-prime endonuclease that processes tRNAs to prepare for addition of CCA. In species where all tRNA sequences already have the CCA tail, such as E. coli, the need for such an enzyme is unclear. Protein similar to the E. coli enzyme, matched by TIGRFAMs model TIGR02649, are designated ribonuclease BN. [Transcription, RNA processing]


Pssm-ID: 274246 [Multi-domain]  Cd Length: 299  Bit Score: 376.56  E-value: 5.64e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373628    2 EVTFFGTSAGLPTKERNTQSIALNLEpysNSVWLFDVGEGTQHQILHHSIKLGKVDHIFITHMHGDHIFGLPGLLTSRSF 81
Cdd:TIGR02651   1 EITFLGTGGGVPTKERNLPSIALKLN---GELWLFDCGEGTQRQMLRSGISPMKIDRIFITHLHGDHILGLPGLLSTMSF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373628   82 QGGEnKPLTLIGPKGIQNYIETSLKLSESHLNYPITYIEINQQFT-YHHEGFTVKAELLNHGITSYGYRIEAPTTPGTID 160
Cdd:TIGR02651  78 QGRK-EPLTIYGPPGIKEFIETSLRVSYTYLNYPIKIHEIEEGGLvFEDDGFKVEAFPLDHSIPSLGYRFEEKDRPGKFD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373628  161 VEALKAIGLNPGPKYQEVKVQDTFEH-NGLMYQSSDFKGAAKPGPVVAIFGDTKPCDNEYILAQDADVMIHESTYIEGEK 239
Cdd:TIGR02651 157 REKAKELGIPPGPLYGKLKRGETVTLiDGRIIDPEDVLGPPRKGRKIAYTGDTRPCEEVIEFAKNADLLIHEATFLDEDK 236

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488373628  240 TLANNYHHSHIDDVFDLIKNANVRKSLITHISNRYNIEEVEsIYEALNNQsdvPNFYFVKDFDTYKI 306
Cdd:TIGR02651 237 KLAKEYGHSTAAQAAEIAKEANVKRLILTHISPRYSDEEEL-LEEAKKIF---PNTYIAEDFMEIEI 299
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 3-304 7.76e-103

Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as tRNase Z or 3' tRNase) catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors. Escherichia coli zinc phosphodiesterase (ZiPD, also known as ecoZ, tRNase Z, or RNase BN) is a 3' tRNA-processing endonuclease, encoded by the elaC gene. Two forms of RNase Z exist in eukaryotes, one long (ELAC2) and one short form (ELAC1), the former may have resulted from a duplication of the shorter enzyme; this subgroup includes the short form (ELAC1). Only the short form exists in bacteria. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293803 [Multi-domain]  Cd Length: 247  Bit Score: 300.91  E-value: 7.76e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373628   3 VTFFGTSAGLPTKERNTQSIALNLEpysNSVWLFDVGEGTQHQILHHSIKLGKVDHIFITHMHGDHIFGLPGLLTSRSFQ 82
Cdd:cd07717    1 LTFLGTGSAVPTPERNLSSIALRLE---GELWLFDCGEGTQRQLLRAGLSPSKIDRIFITHLHGDHILGLPGLLSTMSLL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373628  83 GGEnKPLTLIGPKGIQNYIETSLKLSESHLNYPITYIEIN--QQFTYHHEGFTVKAELLNHGITSYGYRIEApttpgtid 160
Cdd:cd07717   78 GRT-EPLTIYGPKGLKEFLETLLRLSASRLPYPIEVHELEpdPGLVFEDDGFTVTAFPLDHRVPCFGYRFEE-------- 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373628 161 vealkaiglnpgpkyqevkvqdtfehnglmyqssdfkgaakpGPVVAIFGDTKPCDNEYILAQDADVMIHESTYIEGEKT 240
Cdd:cd07717  149 ------------------------------------------GRKIAYLGDTRPCEGLVELAKGADLLIHEATFLDDDAE 186

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488373628 241 LANNYHHSHIDDVFDLIKNANVRKSLITHISNRY-NIEEVESiyEAlnnQSDVPNFYFVKDFDTY 304
Cdd:cd07717  187 KAKETGHSTAKQAAEIAKKAGVKKLVLTHFSARYkDPEELLK--EA---RAVFPNTILAEDFMTI 246
PRK00055 PRK00055
ribonuclease Z; Reviewed
 1-306 3.46e-94

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 279.76  E-value: 3.46e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373628   1 MEVTFFGTSAGLPTKERNTQSIALNLEpysNSVWLFDVGEGTQHQILHHSIKLGKVDHIFITHMHGDHIFGLPGLLTSRS 80
Cdd:PRK00055   2 MELTFLGTGSGVPTPTRNVSSILLRLG---GELFLFDCGEGTQRQLLKTGIKPRKIDKIFITHLHGDHIFGLPGLLSTRS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373628  81 FQGGEnKPLTLIGPKGIQNYIETSLKLSeshlnypityieinqqftyhhegftvkaellnhgiTSYGYRIEAPTTPGTID 160
Cdd:PRK00055  79 LSGRT-EPLTIYGPKGIKEFVETLLRAS-----------------------------------GSLGYRIAEKDKPGKLD 122

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373628 161 VEALKAIGLNPGPKYQEVKVQDTFE-HNGLMYQSSDFKGAAKPGPVVAIFGDTKPCDNEYILAQDADVMIHESTYIEGEK 239
Cdd:PRK00055 123 AEKLKALGVPPGPLFGKLKRGEDVTlEDGRIINPADVLGPPRKGRKVAYCGDTRPCEALVELAKGADLLVHEATFGDEDE 202

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488373628 240 TLANNYHHSHIDDVFDLIKNANVRKSLITHISNRYNIEEVESIYEAlnnQSDVPNFYFVKDFDTYKI 306
Cdd:PRK00055 203 ELAKEYGHSTARQAAEIAKEAGVKRLILTHFSPRYTGDPEELLKEA---REIFPNTELAEDLMRVEV 266
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
1-306 1.34e-87

Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 262.05  E-value: 1.34e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373628   1 MEVTFFGTSAGLPTKERNTQSIALNLEpysNSVWLFDVGEGTQHQILHHSIKLGKVDHIFITHMHGDHIFGLPGLLTSRS 80
Cdd:COG1234    1 MKLTFLGTGGAVPTPGRATSSYLLEAG---GERLLIDCGEGTQRQLLRAGLDPRDIDAIFITHLHGDHIAGLPGLLSTRS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373628  81 FQGGEnKPLTLIGPKGIQNYIETSLKLSESHLNYPITYIEINQQFTYHHEGFTVKAELLNHGITSYGYRIEApttpgtid 160
Cdd:COG1234   78 LAGRE-KPLTIYGPPGTKEFLEALLKASGTDLDFPLEFHEIEPGEVFEIGGFTVTAFPLDHPVPAYGYRFEE-------- 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373628 161 vealkaiglnpgpkyqevkvqdtfehnglmyqssdfkgaakPGPVVAIFGDTKPCDNEYILAQDADVMIHESTYIEGEKT 240
Cdd:COG1234  149 -----------------------------------------PGRSLVYSGDTRPCEALVELAKGADLLIHEATFLDEEAE 187

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488373628 241 LANNYHHSHIDDVFDLIKNANVRKSLITHISNRYN-----IEEVESIYEAlnnqsdvpNFYFVKDFDTYKI 306
Cdd:COG1234  188 LAKETGHSTAKEAAELAAEAGVKRLVLTHFSPRYDdpeelLAEARAVFPG--------PVELAEDGMVIEL 250
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 3-232 1.66e-48

Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as tRNase Z or 3' tRNase) catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors. Two forms of RNase Z exist in eukaryotes, one long (ELAC2) and one short form (ELAC1), the former may have resulted from a duplication of the shorter enzyme. Only the short form exists in bacteria. It includes the C-terminus of human ELAC2 and Escherichia coli zinc phosphodiesterase (ZiPD, also known as ecoZ, tRNase Z, or RNase BN) is a 3' tRNA-processing endonuclease, encoded by the elaC gene. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293830 [Multi-domain]  Cd Length: 180  Bit Score: 159.74  E-value: 1.66e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373628   3 VTFFGTSAGLPTKERNTQSIALNLEpysNSVWLFDVGEGTQHQILHHSIKLGKVDHIFITHMHGDHIFGLPGLLTSRsFQ 82
Cdd:cd16272    1 LTFLGTGGAVPSLTRNTSSYLLETG---GTRILLDCGEGTVYRLLKAGVDPDKLDAIFLSHFHLDHIGGLPTLLFAR-RY 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373628  83 GGENKPLTLIGPKGIQNYIETSLKLSE--SHLNYPITYIEINQ-QFTYHHEGFTVKAELLNHGITSYGYRIEApttpgti 159
Cdd:cd16272   77 GGRKKPLTIYGPKGIKEFLEKLLNFPVeiLPLGFPLEIEELEEgGEVLELGDLKVEAFPVKHSVESLGYRIEA------- 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488373628 160 dvealkaiglnpgpkyqevkvqdtfehnglmyqssdfkgaakPGPVVAIFGDTKPCDNEYILAQDADVMIHES 232
Cdd:cd16272  150 ------------------------------------------EGKSIVYSGDTGPCENLVELAKGADLLIHEC 180
RNaseZ_ELAC1_ELAC2-C-term-like_MBL-fold cd07718
Ribonuclease Z ELAC1, C-terminus of ELAC2, and related proteins; MBL-fold metallo-hydrolase ...
 3-233 1.26e-30

Ribonuclease Z ELAC1, C-terminus of ELAC2, and related proteins; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as tRNase Z or 3' tRNase) catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors. Two forms of RNase Z exist in eukaryotes, one long (ELAC2) and one short form (ELAC1), the former may have resulted from a duplication of the shorter enzyme; this eukaryotic subgroup includes short forms (ELAC1) and the C-terminus of long forms including human ELAC2. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293804 [Multi-domain]  Cd Length: 204  Bit Score: 114.18  E-value: 1.26e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373628   3 VTFFGTSAGLPTKERNTQSIALNLePYSNSVwLFDVGEGTQHQILHH-----------SIKLgkvdhIFITHMHGDHIFG 71
Cdd:cd07718    1 VVFLGTGSAIPSKYRNVSGILLRI-PGDGSI-LLDCGEGTLGQLRRHygpeeadevlrNLKC-----IFISHLHADHHLG 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373628  72 LPGLLTSRS-FQGGENKPLTLIGPKGIQNYIETSLKLsESHLNYPITYIEINQQFTYHHEGFTVKAELLNhgitsygyri 150
Cdd:cd07718   74 LIRLLAERKkLFKPPSPPLYVVAPRQLRRWLREYSSL-EDLGLHDISFISNRVSQSLPESDDPLSRDLLS---------- 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373628 151 eapttpgtidvEALKAIGLNpgpKYQEVKVQDTFEHNGLMYQSSD-FKgaakpgpvVAIFGDTKPCDNEYILAQDADVMI 229
Cdd:cd07718  143 -----------NLLEELGLK---SIETVPVIHCPDAYGIVLTHEDgWK--------IVYSGDTRPCEALVEAGKGADLLI 200


                 ....
gi 488373628 230 HEST 233
Cdd:cd07718  201 HEAT 204
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 2-230 3.47e-30

Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold metallo-hydrolase domain; Arylsulfatase (also known as aryl-sulfate sulfohydrolase, EC 3.1.6.1). Pseudoalteromonas carrageenovora arylsulfatase AtsA may function as a glycosulfohydrolase involved with desulfation of sulfated polysaccharides, which catalyzes hydrolysis of the arylsulfate ester bond, producing the aryl compounds and inorganic sulfate. CD also includes some sequences annotated as ribonucleases. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily.


Pssm-ID: 293805 [Multi-domain]  Cd Length: 193  Bit Score: 112.61  E-value: 3.47e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373628   2 EVTFFGTSAGLPTKERNTQSIALNLEpysNSVWLFDVGEGTQHQILHHSIKLGKVDHIFITHMHGDHIFGLPGLLTSRSF 81
Cdd:cd07719    1 RVTLLGTGGPIPDPDRAGPSTLVVVG---GRVYLVDAGSGVVRRLAQAGLPLGDLDAVFLTHLHSDHVADLPALLLTAWL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373628  82 QGGEnKPLTLIGPKGIQNYIETSLKLSE--------------SHLNYPITYIEINQQFTYHH-EGFTVKAELLNHGIT-- 144
Cdd:cd07719   78 AGRK-TPLPVYGPPGTRALVDGLLAAYAldidyrarigdegrPDPGALVEVHEIAAGGVVYEdDGVKVTAFLVDHGPVpp 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373628 145 SYGYRIEApttpgtidvealkaiglnpgpkyqevkvqdtfehnglmyqssdfkgaakPGPVVAIFGDTKPCDNEYILAQD 224
Cdd:cd07719  157 ALAYRFDT-------------------------------------------------PGRSVVFSGDTGPSENLIELAKG 187


                 ....*.
gi 488373628 225 ADVMIH 230
Cdd:cd07719  188 ADLLVH 193
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 1-306 1.37e-25

Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism];


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 102.28  E-value: 1.37e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373628   1 MEVTFFGTSAGLPT----------------KERNTQSIALNLEpysNSVWLFDVGEGTQHQILHHSIKLGKVDHIFITHM 64
Cdd:COG1235    1 MKVTFLGSGSSGGVpqigcdcpvcastdprYGRTRSSILVEAD---GTRLLIDAGPDLREQLLRLGLDPSKIDAILLTHE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373628  65 HGDHIFGLPGLltsRSFQGgeNKPLTLIGPKGIQNYIETSLKLSESHLNYPITYIEINQQFTYHHEGFTVKAELLNHG-I 143
Cdd:COG1235   78 HADHIAGLDDL---RPRYG--PNPIPVYATPGTLEALERRFPYLFAPYPGKLEFHEIEPGEPFEIGGLTVTPFPVPHDaG 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373628 144 TSYGYRIEApttpgtidvealkaiglnpgpkyqevkvqdtfehnglmyqssdfkgaakPGPVVAIFGDTKPCDNEYI-LA 222
Cdd:COG1235  153 DPVGYRIED-------------------------------------------------GGKKLAYATDTGYIPEEVLeLL 183

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373628 223 QDADVMIHESTYIEGEKTlannyhHSHIDDVFDLIKNANVRKSLITHISNRYNIEEVEsiYEALNNQSDVPNFYFVKDFD 302
Cdd:COG1235  184 RGADLLILDATYDDPEPG------HLSNEEALELLARLGPKRLVLTHLSPDNNDHELD--YDELEAALLPAGVEVAYDGM 255


                 ....
gi 488373628 303 TYKI 306
Cdd:COG1235  256 EIEL 259
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 56-238 1.44e-16

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293826 [Multi-domain]  Cd Length: 194  Bit Score: 76.14  E-value: 1.44e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373628  56 VDHIFITHMHGDHIFGLPGLLTSRSFQGGENKPLTLIGPKGIQNYIETSLKLSESHLN-----YPITYIEINQQFTYHHE 130
Cdd:cd07740   50 IDAIFITHLHGDHFGGLPFFLLDAQFVAKRTRPLTIAGPPGLRERLRRAMEALFPGSSkvprrFDLEVIELEPGEPTTLG 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373628 131 GFTVKAELLNH--GITSYGYRIEApttpgtidvealkaiglnpgpkyqevkvqdtfehnglmyqssdfkgaakPGPVVAI 208
Cdd:cd07740  130 GVTVTAFPVVHpsGALPLALRLEA-------------------------------------------------AGRVLAY 160

                        170       180       190
                 ....*....|....*....|....*....|
gi 488373628 209 FGDTKPCDNEYILAQDADVMIHESTYIEGE 238
Cdd:cd07740  161 SGDTEWTDALVPLARGADLFICECYFFEKK 190
PRK02126 PRK02126
ribonuclease Z; Provisional
 35-285 9.01e-16

ribonuclease Z; Provisional


Pssm-ID: 235006 [Multi-domain]  Cd Length: 334  Bit Score: 76.49  E-value: 9.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373628  35 LFDVGEgtqhqiLHH--SIKLGKVDHIFITHMHGDHIFGLPGLLtsRSFQgGENKPLTLIGPKGIQNYIETSLK-----L 107
Cdd:PRK02126  31 LFDLGD------LHHlpPRELLRISHIFVSHTHMDHFIGFDRLL--RHCL-GRPRRLRLFGPPGFADQVEHKLAgytwnL 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373628 108 SEshlNYPITY----IEIN----QQFTYH-HEGF---------------------TVKAELLNHGITSYGYRIEAPTTPG 157
Cdd:PRK02126 102 VE---NYPTTFrvheVELHdgriRRALFScRRAFareaeeelslpdgvlldepwfRVRAAFLDHGIPCLAFALEEKAHIN 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373628 158 tIDVEALKAIGLNPGPKYQEVK----------------VQDTFEHNGLMYQSSDFKGA---AKPGPVVAIFGDTKPcDNE 218
Cdd:PRK02126 179 -IDKNRLAELGLPPGPWLRELKhavlrgepddtpirvlWRDGGGEHERVRPLGELKERvlrIEPGQKIGYVTDIGY-TEE 256

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488373628 219 YI-----LAQDADVMIHESTYIEGEKTLANNYHHSHIDDVFDLIKNANVRKSLITHISNRYN------IEEVESIYEA 285
Cdd:PRK02126 257 NLariveLAAGVDLLFIEAVFLDEDAEKARRKNHLTARQAGRLAREAGVKRLLPFHFSPRYQgrgaelYREARAAFAG 334
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 35-154 8.90e-14

uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as tRNase Z or 3' tRNase) catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors. Two forms of RNase Z exist in eukaryotes, one long (ELAC2) and one short form (ELAC1), the former may have resulted from a duplication of the shorter enzyme. Only the short form exists in bacteria. Members of this bacterial subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293802 [Multi-domain]  Cd Length: 175  Bit Score: 68.24  E-value: 8.90e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373628  35 LFDVGEGTQHQILHHsIKLGKVDHIFITHMHGDHIFGLPGLLTSRSF--QGGENKPLTLIGPKGIQNYIETSLKLSEShl 112
Cdd:cd07716   31 LLDCGSGVLSRLQRY-IDPEDLDAVVLSHLHPDHCADLGVLQYARRYhpRGARKPPLPLYGPAGPAERLAALYGLEDV-- 107

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 488373628 113 nypITYIEINQQFTYHHEGFTVKAELLNHGITSYGYRIEAPT 154
Cdd:cd07716  108 ---FDFHPIEPGEPLEIGPFTITFFRTVHPVPCYAMRIEDGG 146
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 1-151 1.08e-11

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily.Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry. Some members of this subgroup are named as octanoyltransferase (also known as lipoate-protein ligase B).


Pssm-ID: 293837 [Multi-domain]  Cd Length: 193  Bit Score: 62.49  E-value: 1.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373628   1 MEVTFFGT--SAGLPT-------------KERNTQSIALnLEpYSNSVWLFDVGEGTQHQILHHSIKlgKVDHIFITHMH 65
Cdd:cd16279    1 MKLTFLGTgtSSGVPVigcdcgvcdssdpKNRRLRSSIL-IE-TGGKNILIDTGPDFRQQALRAGIR--KLDAVLLTHAH 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373628  66 GDHIFGLPGLltsRSFQGGENKPLTLIGPKGIQNYIETSLKLSESHLNYPITY------IEINQQFTYhhEGFTVKAELL 139
Cdd:cd16279   77 ADHIHGLDDL---RPFNRLQQRPIPVYASEETLDDLKRRFPYFFAATGGGGVPkldlhiIEPDEPFTI--GGLEITPLPV 151

                        170
                 ....*....|...
gi 488373628 140 NHG-ITSYGYRIE 151
Cdd:cd16279  152 LHGkLPSLGFRFG 164
TaR3-like_MBL-fold cd07715
MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold ...
 58-238 2.57e-10

MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold metallo-hydrolase domain; Myxococcus xanthus Tar3 may function as an ammonium regulator/effector protein involved in biosynthesis of the antibiotic TA. Some are members of this subgroup are annotated as ribonucleases. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293801 [Multi-domain]  Cd Length: 212  Bit Score: 59.05  E-value: 2.57e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373628  58 HIFITHMHGDHIFGLPglltsrsFqggeNKPL-------TLIGPKGIQNYIETSLKLSESHLNYPITYIEINQQFTYHH- 129
Cdd:cd07715   60 HLLLSHTHWDHIQGFP-------F----FAPAydpgnriHIYGPHKDGGSLEEVLRRQMSPPYFPVPLEELLAAIEFHDl 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373628 130 --------EGFTVKAELLNHGITSYGYRIEAPTtpgtidvealKAIglnpgpkyqeVKVQDTfEHNGLMYQSsdfkgaak 201
Cdd:cd07715  129 epgepfsiGGVTVTTIPLNHPGGALGYRIEEDG----------KSV----------VYATDT-EHYPDDGES-------- 179

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 488373628 202 pgpvvaifgdtkpcDNEYI-LAQDADVMIHESTYIEGE 238
Cdd:cd07715  180 --------------DEALLeFARGADLLIHDAQYTDEE 203
class_II_PDE_MBL-fold cd07735
class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium ...
 1-151 2.05e-09

class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium discoideum PDE1 and PDE7, and related proteins; MBL-fold metallo-hydrolase domain; Cyclic nucleotide phosphodiesterases (PDEs) decompose the second messengers cyclic adenosine and guanosine 3',5'-monophosphate (cAMP and cGMP, respectively). Saccharomyces cerevisiae PDE1 and Dictyostelium discoideum PDE1 and PDE7, have dual cAMP/cGMP specificity. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293821  Cd Length: 259  Bit Score: 57.22  E-value: 2.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373628   1 MEVTFFGTSAGLPtkERNTQSIALNlEPYSNSVWLFDVG--------EGTQHQILHHSIKLG-----KVDHIFITHMHGD 67
Cdd:cd07735    1 FELVVLGCSGGPD--EGNTSSFLLD-PAGSDGDILLDAGtgvgalslEEMFNDILFPSQKAAyelyqRIRHYLITHAHLD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373628  68 HIFGLPglLTSRSFQGGENKPLTLIGPK----GIQNYI--------ETSLKLSESHLnypITYIEINQQFTYHHEGFTVK 135
Cdd:cd07735   78 HIAGLP--LLSPNDGGQRGSPKTIYGLPetidALKKHIfnwviwpdFTSIPSGKYPY---LRLEPIEPEYPIALTGLSVT 152

                        170
                 ....*....|....*..
gi 488373628 136 AELLNHG-ITSYGYRIE 151
Cdd:cd07735  153 AFPVSHGvPVSTAFLIR 169
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 31-134 1.63e-08

Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins contain this domain. These proteins include thiolesterases, members of the glyoxalase II family, that catalyse the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid and a competence protein that is essential for natural transformation in Neisseria gonorrhoeae and could be a transporter involved in DNA uptake. Except for the competence protein these proteins bind two zinc ions per molecule as cofactor.


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 53.33  E-value: 1.63e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373628    31 NSVWLFDVGEGTQHQILHHSIKLG--KVDHIFITHMHGDHIFGLPGLLtsrsfqggENKPLTLIGPKGIQNYIETSLKL- 107
Cdd:smart00849   9 GGAILIDTGPGEAEDLLAELKKLGpkKIDAIILTHGHPDHIGGLPELL--------EAPGAPVYAPEGTAELLKDLLALl 80

                           90       100       110
                   ....*....|....*....|....*....|.
gi 488373628   108 ----SESHLNYPITYIEINQQFTYHHEGFTV 134
Cdd:smart00849  81 gelgAEAEPAPPDRTLKDGDELDLGGGELEV 111
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 35-154 3.16e-07

Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and is related to pfam00753.


Pssm-ID: 432732 [Multi-domain]  Cd Length: 196  Bit Score: 50.00  E-value: 3.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373628   35 LFDVGEGTQHQIL--HHSIKLG--KVDHIFITHMHGDHIFGLPGLLtsrsfqggENKPLTLIGPKGIQNYIETSLKL--S 108
Cdd:pfam12706   4 LIDPGPDLRQQALpaLQPGRLRddPIDAVLLTHDHYDHLAGLLDLR--------EGRPRPLYAPLGVLAHLRRNFPYlfL 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 488373628  109 ESHLNYPITYIEINQQFTYHHEGFTVKA---------ELLNHGITSYGYRIEAPT 154
Cdd:pfam12706  76 LEHYGVRVHEIDWGESFTVGDGGLTVTAtparhgsprGLDPNPGDTLGFRIEGPG 130
metallo-hydrolase-like_MBL-fold cd07741
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 37-269 1.94e-06

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293827 [Multi-domain]  Cd Length: 212  Bit Score: 47.57  E-value: 1.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373628  37 DVGEGTQHQILHHSIKLGKVDHIFITHMHGDHIFGLPGLLTSRSfQGGENKPLTLIGPKGIqnyIETSLKLSESHLNYPI 116
Cdd:cd07741   35 DPGPGALVRMCRPKLDPTKLDAIILSHRHLDHSNDANVLIEAMT-EGGFKKRGTLLAPEDA---LNGEPVVLLYYHRRKL 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373628 117 TYIEINQQFT-YHHEGFTVKA-ELLNHGITSYGYRIEApttpgtidvealkaiglnpgpkyqevkvqdtfehnglmyqss 194
Cdd:cd07741  111 EEIEILEEGDeYELGGIKIEAtRHKHSDPTTYGFIFRT------------------------------------------ 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488373628 195 dfkgaakPGPVVAIFGDTKPCDNEYILAQDADVMIHESTYIEGEKtlanNYHHSHIDDVFDLIKNANVRKSLITH 269
Cdd:cd07741  149 -------SDKKIGYISDTRYFEELIEYYSNCDVLIINVTRPRPRK----GVDHLSVEDVEKILKEIKPKLAILTH 212
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 31-76 3.25e-06

mainly hydrolytic enzymes and related proteins which carry out various biological functions; MBL-fold metallohydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases which can catalyze the hydrolysis of a wide range of beta-lactam antibiotics, hydroxyacylglutathione hydrolases (also called glyoxalase II) which hydrolyze S-d-lactoylglutathione to d-lactate in the second step of the glycoxlase system, AHL lactonases which catalyze the hydrolysis and opening of the homoserine lactone rings of acyl homoserine lactones (AHLs), persulfide dioxygenase which catalyze the oxidation of glutathione persulfide to glutathione and persulfite in the mitochondria, flavodiiron proteins which catalyze the reduction of oxygen and/or nitric oxide to water or nitrous oxide respectively, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J which has both 5'-3' exoribonucleolytic and endonucleolytic activity and ribonuclease Z which catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors, cyclic nucleotide phosphodiesterases which decompose cyclic adenosine and guanosine 3', 5'-monophosphate (cAMP and cGMP) respectively, insecticide hydrolases, and proteins required for natural transformation competence. The diversity of biological roles is reflected in variations in the active site metallo-chemistry, for example classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, human persulfide dioxygenase ETHE1 is a mono-iron binding member of the superfamily; Arabidopsis thaliana hydroxyacylglutathione hydrolases incorporates iron, manganese, and zinc in its dinuclear metal binding site, and flavodiiron proteins contains a diiron site.


Pssm-ID: 293792 [Multi-domain]  Cd Length: 188  Bit Score: 46.90  E-value: 3.25e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 488373628  31 NSVWLFDVGEGTQHQILHHSIKLG-KVDHIFITHMHGDHIFGLPGLL 76
Cdd:cd06262   20 GEAILIDPGAGALEKILEAIEELGlKIKAILLTHGHFDHIGGLAELK 66
Lactamase_B_4 pfam13691
tRNase Z endonuclease; This is family of tRNase Z enzymes, that are closely related ...
 35-71 4.42e-06

tRNase Z endonuclease; This is family of tRNase Z enzymes, that are closely related structurally to the Lactamase_B family members. tRNase Z is the endonuclease that is involved in tRNA 3'-end maturation through removal of the 3'-trailer sequences from tRNA precursors. The fission yeast Schizosaccharomyces pombe contains two candidate tRNase Zs encoded by two essential genes. The first, Swiss:Q10155, is targeted to the nucleus and has an SV40 nuclear localization signal at its N-terminus, consisting of four consecutive arginine and lysine residues between residues 208 and 211 (KKRK) that is critical for the NLS function. The second, Swiss:P87168, is targeted to the mitochondria, with an N-terminal mitochondrial targeting signal within the first 38 residues.


Pssm-ID: 404562 [Multi-domain]  Cd Length: 63  Bit Score: 43.35  E-value: 4.42e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 488373628   35 LF-DVGEGTQHQILHHSIKLGKVDHIFITHMHGDHIFG 71
Cdd:pfam13691  25 LFgNVGEGTQRALNEQKVRLSKLEDIFLTGKVSWSNIG 62
RNaseZ_ELAC2-N-term-like_MBL-fold cd16296
Ribonuclease Z, N-terminus of human ELAC2 and related proteins; MBL-fold metallo-hydrolase ...
 34-76 7.05e-06

Ribonuclease Z, N-terminus of human ELAC2 and related proteins; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as tRNase Z or 3' tRNase) catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors. Two forms of RNase Z exist in eukaryotes, one long (ELAC2) and one short form (ELAC1), the former may have resulted from a duplication of the shorter enzyme. This eukaryotic subgroup includes the N-terminus of human ELAC2 and related proteins. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293854 [Multi-domain]  Cd Length: 175  Bit Score: 45.72  E-value: 7.05e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 488373628  34 WLFDVGEGTQHQILHHSIKLGKVDHIFITHMHGDHIFGLPGLL 76
Cdd:cd16296   24 YLFNCGEGVQRLMQEHKLKVARLDNIFLTRMHWSNVGGLSGMI 66
PhnP-like_MBL-fold cd07736
phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase ...
 1-151 7.61e-06

phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase domain; Escherichia coli PhnP catalyzes the hydrolysis of 5-phospho-D-ribose-1,2-cyclic phosphate to D-ribose-1,5-bisphosphate, a step in the C-P lyase pathway. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293822 [Multi-domain]  Cd Length: 186  Bit Score: 45.69  E-value: 7.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373628   1 MEVTFFGT--SAGLP----------------TKERNTQSIALNLEpysNSVWLFDVGegtqHQILHHSIKLGKVDHIFIT 62
Cdd:cd07736    1 MKLTFLGTgdAGGVPvygcdcsacqrarqdpSYRRRPCSALIEVD---GERILLDAG----LTDLAERFPPGSIDAILLT 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373628  63 HMHGDHIFGLpglltsRSFQGGENKPLTLIGPKGIQNYieTSLKLseshlnYP--ITYIEINQQF-TYHHEGFTVKAELL 139
Cdd:cd07736   74 HFHMDHVQGL------FHLRWGVGDPIPVYGPPDPQGC--ADLFK------HPgiLDFQPLVAPFqSFELGGLKITPLPL 139

                        170
                 ....*....|..
gi 488373628 140 NHGITSYGYRIE 151
Cdd:cd07736  140 NHSKPTFGYLLE 151
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
35-153 8.09e-06

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 45.82  E-value: 8.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373628   35 LFDVGEGTQHQILHHSIKLG----KVDHIFITHMHGDHIFGLPGLLTSRSFQGGENKPLTLIGPKGIQNYIETSLKLSES 110
Cdd:pfam00753  19 LIDTGGSAEAALLLLLAALGlgpkDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARELLDEELGLAASRLGLPGP 98

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 488373628  111 HLNYPITYIEINQQFTYHHEGFTVKAELLnHGITSYGYRIEAP 153
Cdd:pfam00753  99 PVVPLPPDVVLEEGDGILGGGLGLLVTHG-PGHGPGHVVVYYG 140
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 33-72 2.43e-05

Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold metallo hydrolase domain; Pseudomonas pseudoalcaligenes OPHC2 is a thermostable organophosphorus hydrolase which a broad substrate activity spectrum: it hydrolyzes various phosphotriesters, esters, and a lactone. This subgroup also includes Pseudomonas oleovorans PoOPH which exhibits high lactonase and esterase activities, and latent PTE activity. However, double mutations His250Ile/Ile263Trp switch PoOPH into an efficient and thermostable PTE. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293806 [Multi-domain]  Cd Length: 251  Bit Score: 44.85  E-value: 2.43e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 488373628  33 VWLFDVGEGTQHQI----LHHS-----IKLGKVDHIFITHMHGDHIFGL 72
Cdd:cd07720   60 LILVDTGAGGLFGPtagkLLANlaaagIDPEDIDDVLLTHLHPDHIGGL 108
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 1-168 7.01e-05

L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and metabolism];


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 43.37  E-value: 7.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373628   1 MEVTFFGTSaglptkerntqSIALNLEpysNSVWLFD---VGEGTQHQILHHSIK-LGKVDHIFITHMHGDHiFGLPGLl 76
Cdd:COG2220    4 MKITWLGHA-----------TFLIETG---GKRILIDpvfSGRASPVNPLPLDPEdLPKIDAVLVTHDHYDH-LDDATL- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373628  77 tsRSFQggeNKPLTLIGPKGIQNYIEtSLKLSEshlnypITYIEINQQFTyhHEGFTVKAELLNHGI--------TSYGY 148
Cdd:COG2220   68 --RALK---RTGATVVAPLGVAAWLR-AWGFPR------VTELDWGESVE--LGGLTVTAVPARHSSgrpdrnggLWVGF 133

                        170       180
                 ....*....|....*....|....*
gi 488373628 149 RIEAPTT----PG-TIDVEALKAIG 168
Cdd:COG2220  134 VIETDGKtiyhAGdTGYFPEMKEIG 158
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 33-72 7.88e-05

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily.Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry. Some members of this subgroup are annotated as GumP protein.


Pssm-ID: 293816 [Multi-domain]  Cd Length: 250  Bit Score: 43.41  E-value: 7.88e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 488373628  33 VWLFDVGEGTQHQILHHSIKLGKVDHIFITHMHGDHIFGL 72
Cdd:cd07730   61 PVPLEVEEDVAEQLAAGGIDPEDIDAVILSHLHWDHIGGL 100
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 30-75 3.84e-04

Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];


Pssm-ID: 440257 [Multi-domain]  Cd Length: 215  Bit Score: 40.83  E-value: 3.84e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 488373628  30 SNSVWLFDVG-EGTQHQILHHSIK-LGK-VDHIFITHMHGDHIFGLPGL 75
Cdd:COG0491   23 GDGAVLIDTGlGPADAEALLAALAaLGLdIKAVLLTHLHPDHVGGLAAL 71
PDE1 COG5212
cAMP phosphodiesterase [Signal transduction mechanisms];
53-151 4.18e-04

cAMP phosphodiesterase [Signal transduction mechanisms];


Pssm-ID: 444071 [Multi-domain]  Cd Length: 300  Bit Score: 41.48  E-value: 4.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373628  53 LGKVDHIFITHMHGDHIFGLPGLLTSRSfqggenkPLTLIGPKG----IQNYIET-------SLKLSESHLNYpITYIEI 121
Cdd:COG5212   70 LEHIKGYLISHAHLDHIAGLPILSPDDS-------PKTIYALPEtidaLRNHYFNwviwpdfTDIGSAPHLPK-YRYVPL 141

                         90       100       110
                 ....*....|....*....|....*....|..
gi 488373628 122 N--QQFTYHHEGFTVKAELLNHGITSYGYRIE 151
Cdd:COG5212  142 KpgQTFPLGGTGLRVTAFPLSHSVPSSAFLIE 173
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 34-97 4.50e-04

Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, and related proteins; MBL-fold metallo hydrolase domain; This subgroup includes Methanocaldococcus jannaschii 7,8-dihydropterin-6-methyl-4-(beta-D-ribofuranosyl)-aminobenzene-5'-phosphate synthase (EC 2.5.1.15), a folate biosynthetic enzyme also known as dihydropteroate synthase and 7,8 dihydropteroate synthase. Thermoanaerobacter tengcongensis Tflp is a ferredoxin-like member. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293799  Cd Length: 269  Bit Score: 41.07  E-value: 4.50e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488373628  34 WLFDVGegtQHQILHH-----SIKLGKVDHIFITHMHGDHIFGLPGLLtsrsfqgGENKPLTLIGPKGI 97
Cdd:cd07713   32 ILFDTG---QSGVLLHnakklGIDLSDIDAVVLSHGHYDHTGGLKALL-------ELNPKAPVYAHPDA 90
CPSF3-like_MBL-fold cd16292
cleavage and polyadenylation specificity factor (CPSF) subunit 3 and related proteins; ...
 50-83 6.71e-04

cleavage and polyadenylation specificity factor (CPSF) subunit 3 and related proteins; MBL-fold metallo-hydrolase domain; CPSF3 (also known as cleavage and polyadenylation specificity factor 73 kDa subunit/CPSF-73) functions as a 3' endonuclease in 3' end processing of pre-mRNAs during cleavage/polyadenylation, and in 3' end processing of metazoan histone pre-mRNAs. This subgroup also contains the yeast homolog of CPSF-73, Ysh1/Brr5 which has roles in mRNA and snoRNA synthesis. In addition to this MBL-fold metallo-hydrolase domain, members of this subgroup contain a beta-CASP (named for metallo-beta-lactamase, CPSF, Artemis, Snm1, Pso2) domain, and a RMMBL domain (RNA-metabolizing metallo-beta-lactamase). Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293850  Cd Length: 194  Bit Score: 39.88  E-value: 6.71e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 488373628  50 SIKLGKVDHIFITHMHGDHIFGLPGLLTSRSFQG 83
Cdd:cd16292   47 EIDLSEIDLLLITHFHLDHCGALPYFLQKTNFKG 80
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 34-76 1.78e-03

DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 441904 [Multi-domain]  Cd Length: 253  Bit Score: 39.07  E-value: 1.78e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 488373628  34 WLFDVGEGTQHQILHHsIKLGKVDHIFITHMHGDHIFGLPGLL 76
Cdd:COG2333   32 PSFDAGERVVLPYLRA-LGIRRLDLLVLTHPDADHIGGLAAVL 73
metallo-hydrolase-like_MBL-fold cd07739
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 58-76 2.53e-03

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293825 [Multi-domain]  Cd Length: 201  Bit Score: 38.25  E-value: 2.53e-03
                         10
                 ....*....|....*....
gi 488373628  58 HIFITHMHGDHIFGLPGLL 76
Cdd:cd07739   55 TIYITHGHPDHYFGLEVLL 73
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 34-76 4.37e-03

uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold metallo hydrolase domain; Includes functionally uncharacterized human lactamase beta 2. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293808 [Multi-domain]  Cd Length: 188  Bit Score: 37.51  E-value: 4.37e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 488373628  34 WLFDVGEGTQHQI--LHHSIKLGK---VDHIFITHMHGDHIFGLPGLL 76
Cdd:cd07722   30 ILIDTGEGRPSYIplLKSVLDSEGnatISDILLTHWHHDHVGGLPDVL 77
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 30-71 8.72e-03

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily.Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293838 [Multi-domain]  Cd Length: 251  Bit Score: 37.18  E-value: 8.72e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488373628  30 SNSVWLFDVGEG-----------TQHQILHHSIKLG----KVDHIFITHMHGDHIFG 71
Cdd:cd16280   21 WVSAWAIDTGDGlilidalnnneAADLIVDGLEKLGldpaDIKYILITHGHGDHYGG 77
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH