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Conserved domains on  [gi|489743381|ref|WP_003647424|]
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MULTISPECIES: ribonuclease Z [Lactobacillus]

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

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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 ...
 2-305 1.52e-155

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: 436.65  E-value: 1.52e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743381    2 EIQFLGTSAGQPSKSRNVSCTALKLLdelNEVWLFDVGEATQHQILKTNIRPRKVTRIFISHTHGDHIFGLPGFLSSRSF 81
Cdd:TIGR02651   1 EITFLGTGGGVPTKERNLPSIALKLN---GELWLFDCGEGTQRQMLRSGISPMKIDRIFITHLHGDHILGLPGLLSTMSF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743381   82 QGDGGPLTIYGPAGIEQFVQTSLKVSRTRVSYPIKYVVLKEDGLIFENNLFAVYTARLDHRVPSFGFRVVEKPRPGELLM 161
Cdd:TIGR02651  78 QGRKEPLTIYGPPGIKEFIETSLRVSYTYLNYPIKIHEIEEGGLVFEDDGFKVEAFPLDHSIPSLGYRFEEKDRPGKFDR 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743381  162 DKVAEYNVPNGPLLGQLKAGKTITLSDGQKLDGRDFLGKERPGRVVTIIYDTRPTENIGKLADHADVLVHESTFNGDEEK 241
Cdd:TIGR02651 158 EKAKELGIPPGPLYGKLKRGETVTLIDGRIIDPEDVLGPPRKGRKIAYTGDTRPCEEVIEFAKNADLLIHEATFLDEDKK 237

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489743381  242 MAHRYFHSTCLDAARIARDRHVRKLYLTHISARYTGKagKELEHEARKIFKHTRLANDLDSFEI 305
Cdd:TIGR02651 238 LAKEYGHSTAAQAAEIAKEANVKRLILTHISPRYSDE--EELLEEAKKIFPNTYIAEDFMEIEI 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 ...
 2-305 1.52e-155

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: 436.65  E-value: 1.52e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743381    2 EIQFLGTSAGQPSKSRNVSCTALKLLdelNEVWLFDVGEATQHQILKTNIRPRKVTRIFISHTHGDHIFGLPGFLSSRSF 81
Cdd:TIGR02651   1 EITFLGTGGGVPTKERNLPSIALKLN---GELWLFDCGEGTQRQMLRSGISPMKIDRIFITHLHGDHILGLPGLLSTMSF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743381   82 QGDGGPLTIYGPAGIEQFVQTSLKVSRTRVSYPIKYVVLKEDGLIFENNLFAVYTARLDHRVPSFGFRVVEKPRPGELLM 161
Cdd:TIGR02651  78 QGRKEPLTIYGPPGIKEFIETSLRVSYTYLNYPIKIHEIEEGGLVFEDDGFKVEAFPLDHSIPSLGYRFEEKDRPGKFDR 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743381  162 DKVAEYNVPNGPLLGQLKAGKTITLSDGQKLDGRDFLGKERPGRVVTIIYDTRPTENIGKLADHADVLVHESTFNGDEEK 241
Cdd:TIGR02651 158 EKAKELGIPPGPLYGKLKRGETVTLIDGRIIDPEDVLGPPRKGRKIAYTGDTRPCEEVIEFAKNADLLIHEATFLDEDKK 237

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489743381  242 MAHRYFHSTCLDAARIARDRHVRKLYLTHISARYTGKagKELEHEARKIFKHTRLANDLDSFEI 305
Cdd:TIGR02651 238 LAKEYGHSTAAQAAEIAKEANVKRLILTHISPRYSDE--EELLEEAKKIFPNTYIAEDFMEIEI 299
PRK00055 PRK00055
ribonuclease Z; Reviewed
 1-305 3.95e-125

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 358.34  E-value: 3.95e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743381   1 MEIQFLGTSAGQPSKSRNVSCTALKLLDELnevWLFDVGEATQHQILKTNIRPRKVTRIFISHTHGDHIFGLPGFLSSRS 80
Cdd:PRK00055   2 MELTFLGTGSGVPTPTRNVSSILLRLGGEL---FLFDCGEGTQRQLLKTGIKPRKIDKIFITHLHGDHIFGLPGLLSTRS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743381  81 FQGDGGPLTIYGPAGIEQFVQTSLKVSrtrvsypikyvvlkedglifennlfavytarldhrvPSFGFRVVEKPRPGELL 160
Cdd:PRK00055  79 LSGRTEPLTIYGPKGIKEFVETLLRAS------------------------------------GSLGYRIAEKDKPGKLD 122

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743381 161 MDKVAEYNVPNGPLLGQLKAGKTITLSDGQKLDGRDFLGKERPGRVVTIIYDTRPTENIGKLADHADVLVHESTFNGDEE 240
Cdd:PRK00055 123 AEKLKALGVPPGPLFGKLKRGEDVTLEDGRIINPADVLGPPRKGRKVAYCGDTRPCEALVELAKGADLLVHEATFGDEDE 202

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489743381 241 KMAHRYFHSTCLDAARIARDRHVRKLYLTHISARYTGKAgKELEHEARKIFKHTRLANDLDSFEI 305
Cdd:PRK00055 203 ELAKEYGHSTARQAAEIAKEAGVKRLILTHFSPRYTGDP-EELLKEAREIFPNTELAEDLMRVEV 266
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 3-304 2.49e-116

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: 335.19  E-value: 2.49e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743381   3 IQFLGTSAGQPSKSRNVSCTALKLLDElneVWLFDVGEATQHQILKTNIRPRKVTRIFISHTHGDHIFGLPGFLSSRSFQ 82
Cdd:cd07717    1 LTFLGTGSAVPTPERNLSSIALRLEGE---LWLFDCGEGTQRQLLRAGLSPSKIDRIFITHLHGDHILGLPGLLSTMSLL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743381  83 GDGGPLTIYGPAGIEQFVQTSLKVSRTRVSYPIKYVVLKED-GLIFENNLFAVYTARLDHRVPSFGFRVVEkprpgellm 161
Cdd:cd07717   78 GRTEPLTIYGPKGLKEFLETLLRLSASRLPYPIEVHELEPDpGLVFEDDGFTVTAFPLDHRVPCFGYRFEE--------- 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743381 162 dkvaeynvpngpllgqlkagktitlsdgqkldgrdflgkerpGRVVTIIYDTRPTENIGKLADHADVLVHESTFNGDEEK 241
Cdd:cd07717  149 ------------------------------------------GRKIAYLGDTRPCEGLVELAKGADLLIHEATFLDDDAE 186

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489743381 242 MAHRYFHSTCLDAARIARDRHVRKLYLTHISARYTGKAgkELEHEARKIFKHTRLANDLDSFE 304
Cdd:cd07717  187 KAKETGHSTAKQAAEIAKKAGVKKLVLTHFSARYKDPE--ELLKEARAVFPNTILAEDFMTIE 247
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
1-305 1.35e-95

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 282.85  E-value: 1.35e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743381   1 MEIQFLGTSAGQPSKSRNVSCTalkLLDELNEVWLFDVGEATQHQILKTNIRPRKVTRIFISHTHGDHIFGLPGFLSSRS 80
Cdd:COG1234    1 MKLTFLGTGGAVPTPGRATSSY---LLEAGGERLLIDCGEGTQRQLLRAGLDPRDIDAIFITHLHGDHIAGLPGLLSTRS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743381  81 FQGDGGPLTIYGPAGIEQFVQTSLKVSRTRVSYPIKYVVLkEDGLIFENNLFAVYTARLDHRVPSFGFRVVEkprpgell 160
Cdd:COG1234   78 LAGREKPLTIYGPPGTKEFLEALLKASGTDLDFPLEFHEI-EPGEVFEIGGFTVTAFPLDHPVPAYGYRFEE-------- 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743381 161 mdkvaeynvpngpllgqlkagktitlsdgqkldgrdflgkerPGRVVTIIYDTRPTENIGKLADHADVLVHESTFNGDEE 240
Cdd:COG1234  149 ------------------------------------------PGRSLVYSGDTRPCEALVELAKGADLLIHEATFLDEEA 186

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489743381 241 KMAHRYFHSTCLDAARIARDRHVRKLYLTHISARYTGKAgkELEHEARKIFK-HTRLANDLDSFEI 305
Cdd:COG1234  187 ELAKETGHSTAKEAAELAAEAGVKRLVLTHFSPRYDDPE--ELLAEARAVFPgPVELAEDGMVIEL 250
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 31-105 8.32e-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: 51.40  E-value: 8.32e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489743381    31 NEVWLFDVGEATQHQILKT--NIRPRKVTRIFISHTHGDHIFGLPGFLSSRsfqgdggPLTIYGPAGIEQFVQTSLK 105
Cdd:smart00849   9 GGAILIDTGPGEAEDLLAElkKLGPKKIDAIILTHGHPDHIGGLPELLEAP-------GAPVYAPEGTAELLKDLLA 78
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 52-271 2.56e-06

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: 47.30  E-value: 2.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743381   52 RPRKVTRIFISHTHGDHIFGLPGFLSSRsfqgdggPLTIYGPAGIEQFVQTSLKVSRTRVSYPIKYVVLKEDGlifennl 131
Cdd:pfam12706  25 RDDPIDAVLLTHDHYDHLAGLLDLREGR-------PRPLYAPLGVLAHLRRNFPYLFLLEHYGVRVHEIDWGE------- 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743381  132 favytarlDHRVPSFGFRVVEKPRPGellmdkvaeynvpNGPLLGQLKAGKTItlsdGQKLDGrdflgkerPGRVVTIIY 211
Cdd:pfam12706  91 --------SFTVGDGGLTVTATPARH-------------GSPRGLDPNPGDTL----GFRIEG--------PGKRVYYAG 137

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489743381  212 DTRP-TENIGKLADHADVLVHESTFNGDEEKMAHryFHSTCLDAARIARDRHVRKLYLTHI 271
Cdd:pfam12706 138 DTGYfPDEIGERLGGADLLLLDGGAWRDDEMIHM--GHMTPEEAVEAAADLGARRKVLIHI 196
 
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 ...
 2-305 1.52e-155

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: 436.65  E-value: 1.52e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743381    2 EIQFLGTSAGQPSKSRNVSCTALKLLdelNEVWLFDVGEATQHQILKTNIRPRKVTRIFISHTHGDHIFGLPGFLSSRSF 81
Cdd:TIGR02651   1 EITFLGTGGGVPTKERNLPSIALKLN---GELWLFDCGEGTQRQMLRSGISPMKIDRIFITHLHGDHILGLPGLLSTMSF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743381   82 QGDGGPLTIYGPAGIEQFVQTSLKVSRTRVSYPIKYVVLKEDGLIFENNLFAVYTARLDHRVPSFGFRVVEKPRPGELLM 161
Cdd:TIGR02651  78 QGRKEPLTIYGPPGIKEFIETSLRVSYTYLNYPIKIHEIEEGGLVFEDDGFKVEAFPLDHSIPSLGYRFEEKDRPGKFDR 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743381  162 DKVAEYNVPNGPLLGQLKAGKTITLSDGQKLDGRDFLGKERPGRVVTIIYDTRPTENIGKLADHADVLVHESTFNGDEEK 241
Cdd:TIGR02651 158 EKAKELGIPPGPLYGKLKRGETVTLIDGRIIDPEDVLGPPRKGRKIAYTGDTRPCEEVIEFAKNADLLIHEATFLDEDKK 237

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489743381  242 MAHRYFHSTCLDAARIARDRHVRKLYLTHISARYTGKagKELEHEARKIFKHTRLANDLDSFEI 305
Cdd:TIGR02651 238 LAKEYGHSTAAQAAEIAKEANVKRLILTHISPRYSDE--EELLEEAKKIFPNTYIAEDFMEIEI 299
PRK00055 PRK00055
ribonuclease Z; Reviewed
 1-305 3.95e-125

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 358.34  E-value: 3.95e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743381   1 MEIQFLGTSAGQPSKSRNVSCTALKLLDELnevWLFDVGEATQHQILKTNIRPRKVTRIFISHTHGDHIFGLPGFLSSRS 80
Cdd:PRK00055   2 MELTFLGTGSGVPTPTRNVSSILLRLGGEL---FLFDCGEGTQRQLLKTGIKPRKIDKIFITHLHGDHIFGLPGLLSTRS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743381  81 FQGDGGPLTIYGPAGIEQFVQTSLKVSrtrvsypikyvvlkedglifennlfavytarldhrvPSFGFRVVEKPRPGELL 160
Cdd:PRK00055  79 LSGRTEPLTIYGPKGIKEFVETLLRAS------------------------------------GSLGYRIAEKDKPGKLD 122

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743381 161 MDKVAEYNVPNGPLLGQLKAGKTITLSDGQKLDGRDFLGKERPGRVVTIIYDTRPTENIGKLADHADVLVHESTFNGDEE 240
Cdd:PRK00055 123 AEKLKALGVPPGPLFGKLKRGEDVTLEDGRIINPADVLGPPRKGRKVAYCGDTRPCEALVELAKGADLLVHEATFGDEDE 202

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489743381 241 KMAHRYFHSTCLDAARIARDRHVRKLYLTHISARYTGKAgKELEHEARKIFKHTRLANDLDSFEI 305
Cdd:PRK00055 203 ELAKEYGHSTARQAAEIAKEAGVKRLILTHFSPRYTGDP-EELLKEAREIFPNTELAEDLMRVEV 266
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 3-304 2.49e-116

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: 335.19  E-value: 2.49e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743381   3 IQFLGTSAGQPSKSRNVSCTALKLLDElneVWLFDVGEATQHQILKTNIRPRKVTRIFISHTHGDHIFGLPGFLSSRSFQ 82
Cdd:cd07717    1 LTFLGTGSAVPTPERNLSSIALRLEGE---LWLFDCGEGTQRQLLRAGLSPSKIDRIFITHLHGDHILGLPGLLSTMSLL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743381  83 GDGGPLTIYGPAGIEQFVQTSLKVSRTRVSYPIKYVVLKED-GLIFENNLFAVYTARLDHRVPSFGFRVVEkprpgellm 161
Cdd:cd07717   78 GRTEPLTIYGPKGLKEFLETLLRLSASRLPYPIEVHELEPDpGLVFEDDGFTVTAFPLDHRVPCFGYRFEE--------- 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743381 162 dkvaeynvpngpllgqlkagktitlsdgqkldgrdflgkerpGRVVTIIYDTRPTENIGKLADHADVLVHESTFNGDEEK 241
Cdd:cd07717  149 ------------------------------------------GRKIAYLGDTRPCEGLVELAKGADLLIHEATFLDDDAE 186

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489743381 242 MAHRYFHSTCLDAARIARDRHVRKLYLTHISARYTGKAgkELEHEARKIFKHTRLANDLDSFE 304
Cdd:cd07717  187 KAKETGHSTAKQAAEIAKKAGVKKLVLTHFSARYKDPE--ELLKEARAVFPNTILAEDFMTIE 247
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
1-305 1.35e-95

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 282.85  E-value: 1.35e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743381   1 MEIQFLGTSAGQPSKSRNVSCTalkLLDELNEVWLFDVGEATQHQILKTNIRPRKVTRIFISHTHGDHIFGLPGFLSSRS 80
Cdd:COG1234    1 MKLTFLGTGGAVPTPGRATSSY---LLEAGGERLLIDCGEGTQRQLLRAGLDPRDIDAIFITHLHGDHIAGLPGLLSTRS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743381  81 FQGDGGPLTIYGPAGIEQFVQTSLKVSRTRVSYPIKYVVLkEDGLIFENNLFAVYTARLDHRVPSFGFRVVEkprpgell 160
Cdd:COG1234   78 LAGREKPLTIYGPPGTKEFLEALLKASGTDLDFPLEFHEI-EPGEVFEIGGFTVTAFPLDHPVPAYGYRFEE-------- 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743381 161 mdkvaeynvpngpllgqlkagktitlsdgqkldgrdflgkerPGRVVTIIYDTRPTENIGKLADHADVLVHESTFNGDEE 240
Cdd:COG1234  149 ------------------------------------------PGRSLVYSGDTRPCEALVELAKGADLLIHEATFLDEEA 186

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489743381 241 KMAHRYFHSTCLDAARIARDRHVRKLYLTHISARYTGKAgkELEHEARKIFK-HTRLANDLDSFEI 305
Cdd:COG1234  187 ELAKETGHSTAKEAAELAAEAGVKRLVLTHFSPRYDDPE--ELLAEARAVFPgPVELAEDGMVIEL 250
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 3-233 1.15e-46

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: 155.11  E-value: 1.15e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743381   3 IQFLGTSAGQPSKSRNVSCTalkLLDELNEVWLFDVGEATQHQILKTNIRPRKVTRIFISHTHGDHIFGLPGFLSSRSFQ 82
Cdd:cd16272    1 LTFLGTGGAVPSLTRNTSSY---LLETGGTRILLDCGEGTVYRLLKAGVDPDKLDAIFLSHFHLDHIGGLPTLLFARRYG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743381  83 GDGGPLTIYGPAGIEQFVQTSLKVSRTR--VSYPIKYVVLKEDGLIFENNLFAVYTARLDHRVPSFGFRVVEKprpgell 160
Cdd:cd16272   78 GRKKPLTIYGPKGIKEFLEKLLNFPVEIlpLGFPLEIEELEEGGEVLELGDLKVEAFPVKHSVESLGYRIEAE------- 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489743381 161 mdkvaeynvpngpllgqlkaGKTITlsdgqkldgrdFLGkerpgrvvtiiyDTRPTENIGKLADHADVLVHES 233
Cdd:cd16272  151 --------------------GKSIV-----------YSG------------DTGPCENLVELAKGADLLIHEC 180
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 2-231 2.85e-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: 112.99  E-value: 2.85e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743381   2 EIQFLGTSAGQPSKSRNVSCTALKLlDelNEVWLFDVGEATQHQILKTNIRPRKVTRIFISHTHGDHIFGLPGFLSSRSF 81
Cdd:cd07719    1 RVTLLGTGGPIPDPDRAGPSTLVVV-G--GRVYLVDAGSGVVRRLAQAGLPLGDLDAVFLTHLHSDHVADLPALLLTAWL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743381  82 QGDGGPLTIYGPAGIEQFVQTSLKVSRTRVSYPIKYVV--------------LKEDGLIFENNLFAVYTARLDHRV--PS 145
Cdd:cd07719   78 AGRKTPLPVYGPPGTRALVDGLLAAYALDIDYRARIGDegrpdpgalvevheIAAGGVVYEDDGVKVTAFLVDHGPvpPA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743381 146 FGFRVvekprpgellmdkvaEYnvpngpllgqlkAGKTITLSdGqkldgrdflgkerpgrvvtiiyDTRPTENIGKLADH 225
Cdd:cd07719  158 LAYRF---------------DT------------PGRSVVFS-G----------------------DTGPSENLIELAKG 187


                 ....*.
gi 489743381 226 ADVLVH 231
Cdd:cd07719  188 ADLLVH 193
PRK02126 PRK02126
ribonuclease Z; Provisional
 35-293 3.79e-28

ribonuclease Z; Provisional


Pssm-ID: 235006 [Multi-domain]  Cd Length: 334  Bit Score: 110.78  E-value: 3.79e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743381  35 LFDVGEATqhqilktNIRPRKVTR---IFISHTHGDHIFGLPGFLssRSFQGDGGPLTIYGPAGIEQFVQTSLK------ 105
Cdd:PRK02126  31 LFDLGDLH-------HLPPRELLRishIFVSHTHMDHFIGFDRLL--RHCLGRPRRLRLFGPPGFADQVEHKLAgytwnl 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743381 106 -------------------VSRTRVSYPIKYVVLKE------DGLIFENNLFAVYTARLDHRVPSFGFRVVEKPRPGeLL 160
Cdd:PRK02126 102 venypttfrvhevelhdgrIRRALFSCRRAFAREAEeelslpDGVLLDEPWFRVRAAFLDHGIPCLAFALEEKAHIN-ID 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743381 161 MDKVAEYNVPNGPLLGQLK--------AGKTITLsdgQKLDGRDFLGKERPG--------RVVT---IIY--DTRPT-EN 218
Cdd:PRK02126 181 KNRLAELGLPPGPWLRELKhavlrgepDDTPIRV---LWRDGGGEHERVRPLgelkervlRIEPgqkIGYvtDIGYTeEN 257

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489743381 219 IGK---LADHADVLVHESTFNGDEEKMAHRYFHSTCLDAARIARDRHVRKLYLTHISARYTGKaGKELEHEARKIFKH 293
Cdd:PRK02126 258 LARiveLAAGVDLLFIEAVFLDEDAEKARRKNHLTARQAGRLAREAGVKRLLPFHFSPRYQGR-GAELYREARAAFAG 334
RNaseZ_ELAC1_ELAC2-C-term-like_MBL-fold cd07718
Ribonuclease Z ELAC1, C-terminus of ELAC2, and related proteins; MBL-fold metallo-hydrolase ...
 3-234 1.50e-22

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: 93.00  E-value: 1.50e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743381   3 IQFLGTSAGQPSKSRNVSCTALKLLDELNevWLFDVGEATQHQIL------KTNIRPRKVTRIFISHTHGDHIFGLPGFL 76
Cdd:cd07718    1 VVFLGTGSAIPSKYRNVSGILLRIPGDGS--ILLDCGEGTLGQLRrhygpeEADEVLRNLKCIFISHLHADHHLGLIRLL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743381  77 SSRS--FQGDGGPLTIYGPAGIEQFVQTSLKVSRTRVSYPIKYVVLKEDGLIFEN---------------NLFAVYTARL 139
Cdd:cd07718   79 AERKklFKPPSPPLYVVAPRQLRRWLREYSSLEDLGLHDISFISNRVSQSLPESDdplsrdllsnlleelGLKSIETVPV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743381 140 DHRVPSFGFRvvekprpgellmdkvaeynvpngpllgqlkagktITLSDGQKldgrdflgkerpgrvvtIIY--DTRPTE 217
Cdd:cd07718  159 IHCPDAYGIV----------------------------------LTHEDGWK-----------------IVYsgDTRPCE 187

                        250
                 ....*....|....*..
gi 489743381 218 NIGKLADHADVLVHEST 234
Cdd:cd07718  188 ALVEAGKGADLLIHEAT 204
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 1-305 2.80e-21

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 90.72  E-value: 2.80e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743381   1 MEIQFLGTSAGQPS----------------KSRNVSCTalkLLDELNEVWLFDVGEATQHQILKTNIRPRKVTRIFISHT 64
Cdd:COG1235    1 MKVTFLGSGSSGGVpqigcdcpvcastdprYGRTRSSI---LVEADGTRLLIDAGPDLREQLLRLGLDPSKIDAILLTHE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743381  65 HGDHIFGLPGFlssRSFQGDgGPLTIYGPAGIEQFVQTSLKVSRTRVSYPIKYVVLKEDG-LIFENnlFAVYTARLDH-R 142
Cdd:COG1235   78 HADHIAGLDDL---RPRYGP-NPIPVYATPGTLEALERRFPYLFAPYPGKLEFHEIEPGEpFEIGG--LTVTPFPVPHdA 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743381 143 VPSFGFRVvekprpgellmdkvaeynvpngpllgqlkagktitlsdgqkldgrdflgkERPGRVVTIIYDT-RPTENIGK 221
Cdd:COG1235  152 GDPVGYRI--------------------------------------------------EDGGKKLAYATDTgYIPEEVLE 181

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743381 222 LADHADVLVHESTFNGDEEKmahryfHSTCLDAARIARDRHVRKLYLTHISARYTGKAGKELEHEARKIFKHTRLANDLD 301
Cdd:COG1235  182 LLRGADLLILDATYDDPEPG------HLSNEEALELLARLGPKRLVLTHLSPDNNDHELDYDELEAALLPAGVEVAYDGM 255


                 ....
gi 489743381 302 SFEI 305
Cdd:COG1235  256 EIEL 259
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 4-235 3.57e-17

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: 78.07  E-value: 3.57e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743381   4 QFLGTSAGQPSKSRNVSCTALKlldelNEVWLF--DVGEATQHQILKTNIRPRKVTRIFISHTHGDHIFGLPGF-LSSRS 80
Cdd:cd07740    1 TFLGSGDAFGSGGRLNTCFHVA-----SEAGRFliDCGASSLIALKRAGIDPNAIDAIFITHLHGDHFGGLPFFlLDAQF 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743381  81 FQGDGGPLTIYGPAGIEQFVQTSLKV-----SRTRVSYPIKYVVLkEDGLIFENNLFAVYTARLDH--RVPSFGFRVVEk 153
Cdd:cd07740   76 VAKRTRPLTIAGPPGLRERLRRAMEAlfpgsSKVPRRFDLEVIEL-EPGEPTTLGGVTVTAFPVVHpsGALPLALRLEA- 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743381 154 prpgellmdkvaeynvpngpllgqlkAGKTITLSDgqkldgrdflgkerpgrvvtiiyDTRPTENIGKLADHADVLVHES 233
Cdd:cd07740  154 --------------------------AGRVLAYSG-----------------------DTEWTDALVPLARGADLFICEC 184


                 ..
gi 489743381 234 TF 235
Cdd:cd07740  185 YF 186
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 51-150 3.62e-09

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: 55.14  E-value: 3.62e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743381  51 IRPRKVTRIFISHTHGDHIFGLPGFLSSRSFQGDGG---PLTIYGPAGIEQFVQTSLKVSRTRVSYPIkyvvlkEDGLIF 127
Cdd:cd07716   46 IDPEDLDAVVLSHLHPDHCADLGVLQYARRYHPRGArkpPLPLYGPAGPAERLAALYGLEDVFDFHPI------EPGEPL 119

                         90       100
                 ....*....|....*....|...
gi 489743381 128 ENNLFAVYTARLDHRVPSFGFRV 150
Cdd:cd07716  120 EIGPFTITFFRTVHPVPCYAMRI 142
TaR3-like_MBL-fold cd07715
MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold ...
 59-240 3.03e-08

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: 52.88  E-value: 3.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743381  59 IFISHTHGDHIFGLPGF--LSSRSFQgdggpLTIYGPAGIEQFVQTSLkvsRTRVSYP------------IKYVVLKEDG 124
Cdd:cd07715   61 LLLSHTHWDHIQGFPFFapAYDPGNR-----IHIYGPHKDGGSLEEVL---RRQMSPPyfpvpleellaaIEFHDLEPGE 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743381 125 LIFENNlFAVYTARLDHRVPSFGFRVvekprpgellmdkvaeynvpngpllgqlkagktitlsdgqkldgrdflgkERPG 204
Cdd:cd07715  133 PFSIGG-VTVTTIPLNHPGGALGYRI--------------------------------------------------EEDG 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 489743381 205 RVVTIIYDT-------RPTENIGKLADHADVLVHESTFNgDEE 240
Cdd:cd07715  162 KSVVYATDTehypddgESDEALLEFARGADLLIHDAQYT-DEE 203
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 31-105 8.32e-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: 51.40  E-value: 8.32e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489743381    31 NEVWLFDVGEATQHQILKT--NIRPRKVTRIFISHTHGDHIFGLPGFLSSRsfqgdggPLTIYGPAGIEQFVQTSLK 105
Cdd:smart00849   9 GGAILIDTGPGEAEDLLAElkKLGPKKIDAIILTHGHPDHIGGLPELLEAP-------GAPVYAPEGTAELLKDLLA 78
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
34-96 1.67e-06

Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];


Pssm-ID: 440850  Cd Length: 273  Bit Score: 48.34  E-value: 1.67e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489743381  34 WLFDVGEAT--QHQILKTNIRPRKVTRIFISHTHGDHIFGLPGFLSSRSfqgdggPLTIYGPAGI 96
Cdd:COG1237   34 ILFDTGQSDvlLKNAEKLGIDLSDIDAVVLSHGHYDHTGGLPALLELNP------KAPVYAHPDA 92
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 52-271 2.56e-06

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: 47.30  E-value: 2.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743381   52 RPRKVTRIFISHTHGDHIFGLPGFLSSRsfqgdggPLTIYGPAGIEQFVQTSLKVSRTRVSYPIKYVVLKEDGlifennl 131
Cdd:pfam12706  25 RDDPIDAVLLTHDHYDHLAGLLDLREGR-------PRPLYAPLGVLAHLRRNFPYLFLLEHYGVRVHEIDWGE------- 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743381  132 favytarlDHRVPSFGFRVVEKPRPGellmdkvaeynvpNGPLLGQLKAGKTItlsdGQKLDGrdflgkerPGRVVTIIY 211
Cdd:pfam12706  91 --------SFTVGDGGLTVTATPARH-------------GSPRGLDPNPGDTL----GFRIEG--------PGKRVYYAG 137

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489743381  212 DTRP-TENIGKLADHADVLVHESTFNGDEEKMAHryFHSTCLDAARIARDRHVRKLYLTHI 271
Cdd:pfam12706 138 DTGYfPDEIGERLGGADLLLLDGGAWRDDEMIHM--GHMTPEEAVEAAADLGARRKVLIHI 196
PhnP-like_MBL-fold cd07736
phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase ...
 1-93 3.85e-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: 46.46  E-value: 3.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743381   1 MEIQFLGT-SAGQ-----------------PSKSRNvSCTALKLLDelNEVWLFDVGEATQHQILktniRPRKVTRIFIS 62
Cdd:cd07736    1 MKLTFLGTgDAGGvpvygcdcsacqrarqdPSYRRR-PCSALIEVD--GERILLDAGLTDLAERF----PPGSIDAILLT 73

                         90       100       110
                 ....*....|....*....|....*....|.
gi 489743381  63 HTHGDHIFGLpgfLSSRsfQGDGGPLTIYGP 93
Cdd:cd07736   74 HFHMDHVQGL---FHLR--WGVGDPIPVYGP 99
class_II_PDE_MBL-fold cd07735
class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium ...
 1-92 6.63e-06

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: 46.44  E-value: 6.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743381   1 MEIQFLGTSAGqPSKSRnvsCTALkLLDEL--NEVWLFD----VGEATQHQILKTNIRP---------RKVTRIFISHTH 65
Cdd:cd07735    1 FELVVLGCSGG-PDEGN---TSSF-LLDPAgsDGDILLDagtgVGALSLEEMFNDILFPsqkaayelyQRIRHYLITHAH 75

                         90       100
                 ....*....|....*....|....*...
gi 489743381  66 GDHIFGLPgfLSSRSFQGDGG-PLTIYG 92
Cdd:cd07735   76 LDHIAGLP--LLSPNDGGQRGsPKTIYG 101
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 26-76 7.65e-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: 45.74  E-value: 7.65e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489743381  26 LLDELNEVWLFDVGEATQHQILKTNIR-PRKVTRIFISHTHGDHIFGLPGFL 76
Cdd:cd06262   15 VSDEEGEAILIDPGAGALEKILEAIEElGLKIKAILLTHGHFDHIGGLAELK 66
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 1-150 1.64e-05

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: 44.77  E-value: 1.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743381   1 MEIQFLGT--SAG-----------QPSKSRNV-SCTALkLLDELNEVWLFDVGEATQHQILKTNIRprKVTRIFISHTHG 66
Cdd:cd16279    1 MKLTFLGTgtSSGvpvigcdcgvcDSSDPKNRrLRSSI-LIETGGKNILIDTGPDFRQQALRAGIR--KLDAVLLTHAHA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743381  67 DHIFGLPGFlssRSFQGD-GGPLTIYGPAGIEQFVQTSLKVSRTRVSYPIKYVVlkEDGLIFENNLFAVYTA-----RLD 140
Cdd:cd16279   78 DHIHGLDDL---RPFNRLqQRPIPVYASEETLDDLKRRFPYFFAATGGGGVPKL--DLHIIEPDEPFTIGGLeitplPVL 152

                        170
                 ....*....|.
gi 489743381 141 H-RVPSFGFRV 150
Cdd:cd16279  153 HgKLPSLGFRF 163
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
35-128 4.73e-05

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 43.51  E-value: 4.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743381   35 LFDVGEATQHQIL----KTNIRPRKVTRIFISHTHGDHIFGLPGFLSSRSFQGDGGPLTIYGPAGIEQFVQTSLKVSRTR 110
Cdd:pfam00753  19 LIDTGGSAEAALLlllaALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARELLDEELGLAASRLGLPGP 98

                          90
                  ....*....|....*...
gi 489743381  111 VSYPIKYVVLKEDGLIFE 128
Cdd:pfam00753  99 PVVPLPPDVVLEEGDGIL 116
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 33-75 3.58e-04

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: 41.48  E-value: 3.58e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 489743381  33 VWLFDVGEATQHQILKTNIRPRKVTRIFISHTHGDHIFGLPGF 75
Cdd:cd07730   61 PVPLEVEEDVAEQLAAGGIDPEDIDAVILSHLHWDHIGGLSDF 103
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 34-96 6.46e-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: 40.68  E-value: 6.46e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489743381  34 WLFDVGeatQHQILKTN-----IRPRKVTRIFISHTHGDHIFGLPGFLSSRSfqgdggPLTIYGPAGI 96
Cdd:cd07713   32 ILFDTG---QSGVLLHNakklgIDLSDIDAVVLSHGHYDHTGGLKALLELNP------KAPVYAHPDA 90
PDE1 COG5212
cAMP phosphodiesterase [Signal transduction mechanisms];
54-94 1.65e-03

cAMP phosphodiesterase [Signal transduction mechanisms];


Pssm-ID: 444071 [Multi-domain]  Cd Length: 300  Bit Score: 39.56  E-value: 1.65e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 489743381  54 RKVTRIFISHTHGDHIFGLPgFLSsrsfqGDGGPLTIYGPA 94
Cdd:COG5212   71 EHIKGYLISHAHLDHIAGLP-ILS-----PDDSPKTIYALP 105
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 51-72 1.78e-03

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: 39.07  E-value: 1.78e-03
                         10        20
                 ....*....|....*....|..
gi 489743381  51 IRPRKVTRIFISHTHGDHIFGL 72
Cdd:cd07720   87 IDPEDIDDVLLTHLHPDHIGGL 108
arylsulfatase_Sdsa1-like_MBL-fold cd07710
Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and ...
 53-98 2.87e-03

Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and related proteins; MBL-fold metallo-hydrolase domain; Arylsulfatase (also known as aryl-sulfate sulfohydrolase, EC 3.1.6.1). Pseudomonas aeruginosa SdsA1 is a secreted SDS hydrolase that allows the bacterium to use primary sulfates such as the detergent SDS common in commercial personal hygiene products as a sole carbon or sulfur source. Pseudomonas inverting secondary alkylsulfatase 1 (Pisa1) is specific for secondary alkyl sulfates. 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: 293796 [Multi-domain]  Cd Length: 239  Bit Score: 38.64  E-value: 2.87e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 489743381  53 PRKVTRIFISHTHGDHIFGLPGFLSsrsfQGDGGPLTIYGPAGIEQ 98
Cdd:cd07710   54 DKPVKAIIYTHSHPDHFGGAGGFVE----EEDSGKVPIIAPEGFME 95
metallo-hydrolase-like_MBL-fold cd07739
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 54-73 4.95e-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: 37.48  E-value: 4.95e-03
                         10        20
                 ....*....|....*....|
gi 489743381  54 RKVTRIFISHTHGDHIFGLP 73
Cdd:cd07739   51 KTLTTIYITHGHPDHYFGLE 70
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 31-75 5.26e-03

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: 37.36  E-value: 5.26e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 489743381  31 NEVWLFDVG-EATQHQILKTNIRPR--KVTRIFISHTHGDHIFGLPGF 75
Cdd:COG0491   24 DGAVLIDTGlGPADAEALLAALAALglDIKAVLLTHLHPDHVGGLAAL 71
metallo-hydrolase-like_MBL-fold cd07742
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 36-75 6.94e-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: 293828 [Multi-domain]  Cd Length: 249  Bit Score: 37.22  E-value: 6.94e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 489743381  36 FDVGEATQHQILKTNIRPRKVTRIFISHTHGDHIFGLPGF 75
Cdd:cd07742   61 LDEDETAVRQIEALGFDPSDVRHIVLTHLDLDHAGGLADF 100
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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