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Conserved domains on  [gi|488195968|ref|WP_002267176|]
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ribonuclease Z [Streptococcus mutans]

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 ...
 2-309 5.08e-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: 376.94  E-value: 5.08e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968    2 EIQFLGTGAGQPAKARNVSSLVLKLLdelNEIWMFDCGEGTQRQILETTIKPRKIRKIFITHLHGDHVFGLPGFLSSRAF 81
Cdd:TIGR02651   1 EITFLGTGGGVPTKERNLPSIALKLN---GELWLFDCGEGTQRQMLRSGISPMKIDRIFITHLHGDHILGLPGLLSTMSF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968   82 QanDEQTDVDIYGPVGIKHLVMASIRTSGAHLPYHIHFHEFDAKhlGKILETDKFMVYAEKLDHTIFCVGYRVVQKDLEG 161
Cdd:TIGR02651  78 Q--GRKEPLTIYGPPGIKEFIETSLRVSYTYLNYPIKIHEIEEG--GLVFEDDGFKVEAFPLDHSIPSLGYRFEEKDRPG 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968  162 TLDAEKLKAAGLPFGPLFGRVKNGQDVVLEDGTTIIAKDYISAPKKGKVITILGDTRKTDASIRLALGADVLVHESTYSK 241
Cdd:TIGR02651 154 KFDREKAKELGIPPGPLYGKLKRGETVTLIDGRIIDPEDVLGPPRKGRKIAYTGDTRPCEEVIEFAKNADLLIHEATFLD 233

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488195968  242 GDENLARRHGHSTNMEAARVAKAASVKKLLLNHISARFlsHDISRMRDDAQEIFTDVHIVRDLEEVKL 309
Cdd:TIGR02651 234 EDKKLAKEYGHSTAAQAAEIAKEANVKRLILTHISPRY--SDEEELLEEAKKIFPNTYIAEDFMEIEI 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 ...
 2-309 5.08e-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: 376.94  E-value: 5.08e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968    2 EIQFLGTGAGQPAKARNVSSLVLKLLdelNEIWMFDCGEGTQRQILETTIKPRKIRKIFITHLHGDHVFGLPGFLSSRAF 81
Cdd:TIGR02651   1 EITFLGTGGGVPTKERNLPSIALKLN---GELWLFDCGEGTQRQMLRSGISPMKIDRIFITHLHGDHILGLPGLLSTMSF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968   82 QanDEQTDVDIYGPVGIKHLVMASIRTSGAHLPYHIHFHEFDAKhlGKILETDKFMVYAEKLDHTIFCVGYRVVQKDLEG 161
Cdd:TIGR02651  78 Q--GRKEPLTIYGPPGIKEFIETSLRVSYTYLNYPIKIHEIEEG--GLVFEDDGFKVEAFPLDHSIPSLGYRFEEKDRPG 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968  162 TLDAEKLKAAGLPFGPLFGRVKNGQDVVLEDGTTIIAKDYISAPKKGKVITILGDTRKTDASIRLALGADVLVHESTYSK 241
Cdd:TIGR02651 154 KFDREKAKELGIPPGPLYGKLKRGETVTLIDGRIIDPEDVLGPPRKGRKIAYTGDTRPCEEVIEFAKNADLLIHEATFLD 233

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488195968  242 GDENLARRHGHSTNMEAARVAKAASVKKLLLNHISARFlsHDISRMRDDAQEIFTDVHIVRDLEEVKL 309
Cdd:TIGR02651 234 EDKKLAKEYGHSTAAQAAEIAKEANVKRLILTHISPRY--SDEEELLEEAKKIFPNTYIAEDFMEIEI 299
PRK00055 PRK00055
ribonuclease Z; Reviewed
 1-309 6.68e-127

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 362.96  E-value: 6.68e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968   1 MEIQFLGTGAGQPAKARNVSSLVLKLLDELneiWMFDCGEGTQRQILETTIKPRKIRKIFITHLHGDHVFGLPGFLSSRA 80
Cdd:PRK00055   2 MELTFLGTGSGVPTPTRNVSSILLRLGGEL---FLFDCGEGTQRQLLKTGIKPRKIDKIFITHLHGDHIFGLPGLLSTRS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968  81 FQANDEQtdVDIYGPVGIKHLVMASIRTSGahlpyhihfhefdakhlgkiletdkfmvyaekldhtifCVGYRVVQKDLE 160
Cdd:PRK00055  79 LSGRTEP--LTIYGPKGIKEFVETLLRASG--------------------------------------SLGYRIAEKDKP 118

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968 161 GTLDAEKLKAAGLPFGPLFGRVKNGQDVVLEDGTTIIAKDYISAPKKGKVITILGDTRKTDASIRLALGADVLVHESTYS 240
Cdd:PRK00055 119 GKLDAEKLKALGVPPGPLFGKLKRGEDVTLEDGRIINPADVLGPPRKGRKVAYCGDTRPCEALVELAKGADLLVHEATFG 198

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488195968 241 KGDENLARRHGHSTNMEAARVAKAASVKKLLLNHISARfLSHDISRMRDDAQEIFTDVHIVRDLEEVKL 309
Cdd:PRK00055 199 DEDEELAKEYGHSTARQAAEIAKEAGVKRLILTHFSPR-YTGDPEELLKEAREIFPNTELAEDLMRVEV 266
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 3-307 3.27e-110

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: 319.78  E-value: 3.27e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968   3 IQFLGTGAGQPAKARNVSSLVLKLLDElneIWMFDCGEGTQRQILETTIKPRKIRKIFITHLHGDHVFGLPGFLSSRAFQ 82
Cdd:cd07717    1 LTFLGTGSAVPTPERNLSSIALRLEGE---LWLFDCGEGTQRQLLRAGLSPSKIDRIFITHLHGDHILGLPGLLSTMSLL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968  83 ANDEqtDVDIYGPVGIKHLVMASIRTSGAHLPYHIHFHEFDAKhLGKILETDKFMVYAEKLDHTIFCVGYRVVQkdlegt 162
Cdd:cd07717   78 GRTE--PLTIYGPKGLKEFLETLLRLSASRLPYPIEVHELEPD-PGLVFEDDGFTVTAFPLDHRVPCFGYRFEE------ 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968 163 ldaeklkaaglpfgplfgrvkngqdvvledgttiiakdyisapkkGKVITILGDTRKTDASIRLALGADVLVHESTYSKG 242
Cdd:cd07717  149 ---------------------------------------------GRKIAYLGDTRPCEGLVELAKGADLLIHEATFLDD 183

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488195968 243 DENLARRHGHSTNMEAARVAKAASVKKLLLNHISARFlsHDISRMRDDAQEIFTDVHIVRDLEEV 307
Cdd:cd07717  184 DAEKAKETGHSTAKQAAEIAKKAGVKKLVLTHFSARY--KDPEELLKEARAVFPNTILAEDFMTI 246
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
1-309 5.61e-89

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 265.91  E-value: 5.61e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968   1 MEIQFLGTGAGQPAKARNVSSLvlkLLDELNEIWMFDCGEGTQRQILETTIKPRKIRKIFITHLHGDHVFGLPGFLSSRA 80
Cdd:COG1234    1 MKLTFLGTGGAVPTPGRATSSY---LLEAGGERLLIDCGEGTQRQLLRAGLDPRDIDAIFITHLHGDHIAGLPGLLSTRS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968  81 FQANDEqtDVDIYGPVGIKHLVMASIRTSGAHLPYHIHFHEFDAkhlGKILETDKFMVYAEKLDHTIFCVGYRVVQkdle 160
Cdd:COG1234   78 LAGREK--PLTIYGPPGTKEFLEALLKASGTDLDFPLEFHEIEP---GEVFEIGGFTVTAFPLDHPVPAYGYRFEE---- 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968 161 gtldaeklkaaglpfgplfgrvkngqdvvledgttiiakdyisapkKGKVITILGDTRKTDASIRLALGADVLVHESTYS 240
Cdd:COG1234  149 ----------------------------------------------PGRSLVYSGDTRPCEALVELAKGADLLIHEATFL 182

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968 241 KGDENLARRHGHSTNMEAARVAKAASVKKLLLNHISARFLshDISRMRDDAQEIFT-DVHIVRDLEEVKL 309
Cdd:COG1234  183 DEEAELAKETGHSTAKEAAELAAEAGVKRLVLTHFSPRYD--DPEELLAEARAVFPgPVELAEDGMVIEL 250
GntH_guanitoxin NF041257
guanitoxin biosynthesis MBL fold metallo-hydrolase GntH;
1-265 2.55e-14

guanitoxin biosynthesis MBL fold metallo-hydrolase GntH;


Pssm-ID: 469157 [Multi-domain]  Cd Length: 372  Bit Score: 72.73  E-value: 2.55e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968   1 MEIQFLGTGAGQPAKARNVSSLVLKLLDELNEIWMFDCGEGTQRQILETTIKPRKIRKIFITHLHGDHVFGLPGFLSSRA 80
Cdd:NF041257  13 MRITFLGSGPPPPRRGQANTSILVELGNGERDKFFFDIGSGSVANIIALQIPYNLLNKVFITHLHVDHYGDLPYLYPFGA 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968  81 FqaNDEQTDVDIYGP------VGIKHLV------MASIRTSGAHLP----YHIHFHEFD-AKHLGKILETDKFMVYAEKL 143
Cdd:NF041257  93 W--SGRWTPLRVWGPsgrtpeLGTKHMVegmkemLAWDTDAFSGFPigdgYEIEVNEFDfRDENGVVYEENGVTVRSWPR 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968 144 DHTI-FCVGYRvvqkdlegtldaekLKAAGLPFgplfgrvkngqdvvledgttiiakdyisapkkgkVITilGDTRKTDA 222
Cdd:NF041257 171 SHAKdGAVSYR--------------LDWNGLSF----------------------------------VFT--GDGRPNEL 200

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488195968 223 SIRLALGADVLVHE--------STYSKGDENLARR---HGHSTNMEAARVAKAA 265
Cdd:NF041257 201 TVEYAKGADVFIHEcfdtpellSGKYGVPPELARYtidTHHTPPYAAGKVFSLV 254
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 31-111 5.25e-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: 51.79  E-value: 5.25e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968    31 NEIWMFDCGEGTQRQILET--TIKPRKIRKIFITHLHGDHVFGLPGFLssrafqandEQTDVDIYGPVGIKHLVMASIRT 108
Cdd:smart00849   9 GGAILIDTGPGEAEDLLAElkKLGPKKIDAIILTHGHPDHIGGLPELL---------EAPGAPVYAPEGTAELLKDLLAL 79


                   ...
gi 488195968   109 SGA 111
Cdd:smart00849  80 LGE 82
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 36-275 1.68e-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: 47.69  E-value: 1.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968   36 FDCGEGTQRQILET----TIKPRKIRKIFITHLHGDHVFGLPGFLSSRAFqandeqtdvDIYGPVGIkhlvmasirtsGA 111
Cdd:pfam12706   5 IDPGPDLRQQALPAlqpgRLRDDPIDAVLLTHDHYDHLAGLLDLREGRPR---------PLYAPLGV-----------LA 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968  112 HLPyhihfhefdakhlgkiletdKFMVYAEKLDHTifcvGYRVVQKDLEGTLdaeKLKAAGLPFGPLFGRVKNGQDVVLE 191
Cdd:pfam12706  65 HLR--------------------RNFPYLFLLEHY----GVRVHEIDWGESF---TVGDGGLTVTATPARHGSPRGLDPN 117

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968  192 DGTTI---IAKDyisapkkGKVITILGDTRKTDASIRLAL-GADVLVHESTYSkgDENLARRHGHSTNMEAARVAKAASV 267
Cdd:pfam12706 118 PGDTLgfrIEGP-------GKRVYYAGDTGYFPDEIGERLgGADLLLLDGGAW--RDDEMIHMGHMTPEEAVEAAADLGA 188


                  ....*...
gi 488195968  268 KKLLLNHI 275
Cdd:pfam12706 189 RRKVLIHI 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 ...
 2-309 5.08e-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: 376.94  E-value: 5.08e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968    2 EIQFLGTGAGQPAKARNVSSLVLKLLdelNEIWMFDCGEGTQRQILETTIKPRKIRKIFITHLHGDHVFGLPGFLSSRAF 81
Cdd:TIGR02651   1 EITFLGTGGGVPTKERNLPSIALKLN---GELWLFDCGEGTQRQMLRSGISPMKIDRIFITHLHGDHILGLPGLLSTMSF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968   82 QanDEQTDVDIYGPVGIKHLVMASIRTSGAHLPYHIHFHEFDAKhlGKILETDKFMVYAEKLDHTIFCVGYRVVQKDLEG 161
Cdd:TIGR02651  78 Q--GRKEPLTIYGPPGIKEFIETSLRVSYTYLNYPIKIHEIEEG--GLVFEDDGFKVEAFPLDHSIPSLGYRFEEKDRPG 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968  162 TLDAEKLKAAGLPFGPLFGRVKNGQDVVLEDGTTIIAKDYISAPKKGKVITILGDTRKTDASIRLALGADVLVHESTYSK 241
Cdd:TIGR02651 154 KFDREKAKELGIPPGPLYGKLKRGETVTLIDGRIIDPEDVLGPPRKGRKIAYTGDTRPCEEVIEFAKNADLLIHEATFLD 233

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488195968  242 GDENLARRHGHSTNMEAARVAKAASVKKLLLNHISARFlsHDISRMRDDAQEIFTDVHIVRDLEEVKL 309
Cdd:TIGR02651 234 EDKKLAKEYGHSTAAQAAEIAKEANVKRLILTHISPRY--SDEEELLEEAKKIFPNTYIAEDFMEIEI 299
PRK00055 PRK00055
ribonuclease Z; Reviewed
 1-309 6.68e-127

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 362.96  E-value: 6.68e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968   1 MEIQFLGTGAGQPAKARNVSSLVLKLLDELneiWMFDCGEGTQRQILETTIKPRKIRKIFITHLHGDHVFGLPGFLSSRA 80
Cdd:PRK00055   2 MELTFLGTGSGVPTPTRNVSSILLRLGGEL---FLFDCGEGTQRQLLKTGIKPRKIDKIFITHLHGDHIFGLPGLLSTRS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968  81 FQANDEQtdVDIYGPVGIKHLVMASIRTSGahlpyhihfhefdakhlgkiletdkfmvyaekldhtifCVGYRVVQKDLE 160
Cdd:PRK00055  79 LSGRTEP--LTIYGPKGIKEFVETLLRASG--------------------------------------SLGYRIAEKDKP 118

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968 161 GTLDAEKLKAAGLPFGPLFGRVKNGQDVVLEDGTTIIAKDYISAPKKGKVITILGDTRKTDASIRLALGADVLVHESTYS 240
Cdd:PRK00055 119 GKLDAEKLKALGVPPGPLFGKLKRGEDVTLEDGRIINPADVLGPPRKGRKVAYCGDTRPCEALVELAKGADLLVHEATFG 198

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488195968 241 KGDENLARRHGHSTNMEAARVAKAASVKKLLLNHISARfLSHDISRMRDDAQEIFTDVHIVRDLEEVKL 309
Cdd:PRK00055 199 DEDEELAKEYGHSTARQAAEIAKEAGVKRLILTHFSPR-YTGDPEELLKEAREIFPNTELAEDLMRVEV 266
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 3-307 3.27e-110

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: 319.78  E-value: 3.27e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968   3 IQFLGTGAGQPAKARNVSSLVLKLLDElneIWMFDCGEGTQRQILETTIKPRKIRKIFITHLHGDHVFGLPGFLSSRAFQ 82
Cdd:cd07717    1 LTFLGTGSAVPTPERNLSSIALRLEGE---LWLFDCGEGTQRQLLRAGLSPSKIDRIFITHLHGDHILGLPGLLSTMSLL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968  83 ANDEqtDVDIYGPVGIKHLVMASIRTSGAHLPYHIHFHEFDAKhLGKILETDKFMVYAEKLDHTIFCVGYRVVQkdlegt 162
Cdd:cd07717   78 GRTE--PLTIYGPKGLKEFLETLLRLSASRLPYPIEVHELEPD-PGLVFEDDGFTVTAFPLDHRVPCFGYRFEE------ 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968 163 ldaeklkaaglpfgplfgrvkngqdvvledgttiiakdyisapkkGKVITILGDTRKTDASIRLALGADVLVHESTYSKG 242
Cdd:cd07717  149 ---------------------------------------------GRKIAYLGDTRPCEGLVELAKGADLLIHEATFLDD 183

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488195968 243 DENLARRHGHSTNMEAARVAKAASVKKLLLNHISARFlsHDISRMRDDAQEIFTDVHIVRDLEEV 307
Cdd:cd07717  184 DAEKAKETGHSTAKQAAEIAKKAGVKKLVLTHFSARY--KDPEELLKEARAVFPNTILAEDFMTI 246
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
1-309 5.61e-89

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 265.91  E-value: 5.61e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968   1 MEIQFLGTGAGQPAKARNVSSLvlkLLDELNEIWMFDCGEGTQRQILETTIKPRKIRKIFITHLHGDHVFGLPGFLSSRA 80
Cdd:COG1234    1 MKLTFLGTGGAVPTPGRATSSY---LLEAGGERLLIDCGEGTQRQLLRAGLDPRDIDAIFITHLHGDHIAGLPGLLSTRS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968  81 FQANDEqtDVDIYGPVGIKHLVMASIRTSGAHLPYHIHFHEFDAkhlGKILETDKFMVYAEKLDHTIFCVGYRVVQkdle 160
Cdd:COG1234   78 LAGREK--PLTIYGPPGTKEFLEALLKASGTDLDFPLEFHEIEP---GEVFEIGGFTVTAFPLDHPVPAYGYRFEE---- 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968 161 gtldaeklkaaglpfgplfgrvkngqdvvledgttiiakdyisapkKGKVITILGDTRKTDASIRLALGADVLVHESTYS 240
Cdd:COG1234  149 ----------------------------------------------PGRSLVYSGDTRPCEALVELAKGADLLIHEATFL 182

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968 241 KGDENLARRHGHSTNMEAARVAKAASVKKLLLNHISARFLshDISRMRDDAQEIFT-DVHIVRDLEEVKL 309
Cdd:COG1234  183 DEEAELAKETGHSTAKEAAELAAEAGVKRLVLTHFSPRYD--DPEELLAEARAVFPgPVELAEDGMVIEL 250
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 3-237 1.82e-39

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: 136.62  E-value: 1.82e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968   3 IQFLGTGAGQPAKARNVSSLvlkLLDELNEIWMFDCGEGTQRQILETTIKPRKIRKIFITHLHGDHVFGLPGFLSSRafQ 82
Cdd:cd16272    1 LTFLGTGGAVPSLTRNTSSY---LLETGGTRILLDCGEGTVYRLLKAGVDPDKLDAIFLSHFHLDHIGGLPTLLFAR--R 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968  83 ANDEQTDVDIYGPVGIKHLVMA--SIRTSGAHLPYHIHFHEFDakHLGKILETDKFMVYAEKLDHTIFCVGYRvvqkdle 160
Cdd:cd16272   76 YGGRKKPLTIYGPKGIKEFLEKllNFPVEILPLGFPLEIEELE--EGGEVLELGDLKVEAFPVKHSVESLGYR------- 146

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488195968 161 gtldaeklkaaglpfgplfgrvkngqdvvLEDGttiiakdyisapkkGKVITILGDTRKTDASIRLALGADVLVHES 237
Cdd:cd16272  147 -----------------------------IEAE--------------GKSIVYSGDTGPCENLVELAKGADLLIHEC 180
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 2-235 2.80e-31

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: 115.69  E-value: 2.80e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968   2 EIQFLGTGAGQPAKARNVSSLVLKLlDelNEIWMFDCGEGTQRQILETTIKPRKIRKIFITHLHGDHVFGLPGFLSSRAF 81
Cdd:cd07719    1 RVTLLGTGGPIPDPDRAGPSTLVVV-G--GRVYLVDAGSGVVRRLAQAGLPLGDLDAVFLTHLHSDHVADLPALLLTAWL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968  82 QANDeqTDVDIYGPVGIKHLV---------MASIRTSGAH-----LPYHIHFHEFDAKhlGKILETDKFMVYAEKLDHTI 147
Cdd:cd07719   78 AGRK--TPLPVYGPPGTRALVdgllaayalDIDYRARIGDegrpdPGALVEVHEIAAG--GVVYEDDGVKVTAFLVDHGP 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968 148 F--CVGYRVvqkdlegtldaeklkaaglpfgplfgrvkngqdvvledgttiiakDYisapkKGKVITILGDTRKTDASIR 225
Cdd:cd07719  154 VppALAYRF---------------------------------------------DT-----PGRSVVFSGDTGPSENLIE 183

                        250
                 ....*....|
gi 488195968 226 LALGADVLVH 235
Cdd:cd07719  184 LAKGADLLVH 193
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 1-309 2.97e-28

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 109.60  E-value: 2.97e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968   1 MEIQFLGTGAGQ----------------PAKARNVSSLvlkLLDELNEIWMFDCGEGTQRQILETTIKPRKIRKIFITHL 64
Cdd:COG1235    1 MKVTFLGSGSSGgvpqigcdcpvcastdPRYGRTRSSI---LVEADGTRLLIDAGPDLREQLLRLGLDPSKIDAILLTHE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968  65 HGDHVFGLPGFlsSRAFQANdeqtDVDIYGPVGIKHLVMASIRTSGAHLPYHIHFHEFDAkhlGKILETDKFMVYAEKLD 144
Cdd:COG1235   78 HADHIAGLDDL--RPRYGPN----PIPVYATPGTLEALERRFPYLFAPYPGKLEFHEIEP---GEPFEIGGLTVTPFPVP 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968 145 H-TIFCVGYRVvqkdlegtldaeklkaaglpfgplfgrvkngqdvvlEDGttiiakdyisapkkGKVITILGDTRK-TDA 222
Cdd:COG1235  149 HdAGDPVGYRI------------------------------------EDG--------------GKKLAYATDTGYiPEE 178

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968 223 SIRLALGADVLVHESTYSkgdenlARRHGHSTNMEAARVAKAASVKKLLLNHISARFLSHDISRMRDDAQEIFTDVHIVR 302
Cdd:COG1235  179 VLELLRGADLLILDATYD------DPEPGHLSNEEALELLARLGPKRLVLTHLSPDNNDHELDYDELEAALLPAGVEVAY 252


                 ....*..
gi 488195968 303 DLEEVKL 309
Cdd:COG1235  253 DGMEIEL 259
RNaseZ_ELAC1_ELAC2-C-term-like_MBL-fold cd07718
Ribonuclease Z ELAC1, C-terminus of ELAC2, and related proteins; MBL-fold metallo-hydrolase ...
 3-238 2.98e-21

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: 89.53  E-value: 2.98e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968   3 IQFLGTGAGQPAKARNVSSLVLKLLDELNeIwMFDCGEGTQRQIL------ETTIKPRKIRKIFITHLHGDHVFGLPGFL 76
Cdd:cd07718    1 VVFLGTGSAIPSKYRNVSGILLRIPGDGS-I-LLDCGEGTLGQLRrhygpeEADEVLRNLKCIFISHLHADHHLGLIRLL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968  77 SSRAfQANDEQTDvdiygPVgikhLVMAsirtsgahlPYHIHF--HEFDakhlgkilETDKFMVYAEKLDHTIFCVGYRV 154
Cdd:cd07718   79 AERK-KLFKPPSP-----PL----YVVA---------PRQLRRwlREYS--------SLEDLGLHDISFISNRVSQSLPE 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968 155 VQKDLEGTLDAEKLKAAGL-------------PFGplfgrvkngqdVVLEDgttiiakdyisapKKGKVITILGDTRKTD 221
Cdd:cd07718  132 SDDPLSRDLLSNLLEELGLksietvpvihcpdAYG-----------IVLTH-------------EDGWKIVYSGDTRPCE 187

                        250
                 ....*....|....*..
gi 488195968 222 ASIRLALGADVLVHEST 238
Cdd:cd07718  188 ALVEAGKGADLLIHEAT 204
PRK02126 PRK02126
ribonuclease Z; Provisional
 36-295 2.39e-18

ribonuclease Z; Provisional


Pssm-ID: 235006 [Multi-domain]  Cd Length: 334  Bit Score: 83.81  E-value: 2.39e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968  36 FDCGegtqrQIleTTIKPRKIRK---IFITHLHGDHVFGLPGFLssRAFQANDEQtdVDIYGPVGI-------------- 98
Cdd:PRK02126  32 FDLG-----DL--HHLPPRELLRishIFVSHTHMDHFIGFDRLL--RHCLGRPRR--LRLFGPPGFadqvehklagytwn 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968  99 -------------KHLVMASIRTSGAHLPyhihfHEFDAKHL-------GKILETDKFMVYAEKLDHTIFCVGYRVVQKd 158
Cdd:PRK02126 101 lvenypttfrvheVELHDGRIRRALFSCR-----RAFAREAEeelslpdGVLLDEPWFRVRAAFLDHGIPCLAFALEEK- 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968 159 LEGTLDAEKLKAAGLPFGPLFGRVKNGQDVVLEDGTTIIA------KDYISAPKKGKV------------ITILGDTRKT 220
Cdd:PRK02126 175 AHINIDKNRLAELGLPPGPWLRELKHAVLRGEPDDTPIRVlwrdggGEHERVRPLGELkervlriepgqkIGYVTDIGYT 254

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488195968 221 DASIR----LALGADVLVHESTYSKGDENLARRHGHSTNMEAARVAKAASVKKLLLNHISARFLSHDiSRMRDDAQEIF 295
Cdd:PRK02126 255 EENLAriveLAAGVDLLFIEAVFLDEDAEKARRKNHLTARQAGRLAREAGVKRLLPFHFSPRYQGRG-AELYREARAAF 332
GntH_guanitoxin NF041257
guanitoxin biosynthesis MBL fold metallo-hydrolase GntH;
1-265 2.55e-14

guanitoxin biosynthesis MBL fold metallo-hydrolase GntH;


Pssm-ID: 469157 [Multi-domain]  Cd Length: 372  Bit Score: 72.73  E-value: 2.55e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968   1 MEIQFLGTGAGQPAKARNVSSLVLKLLDELNEIWMFDCGEGTQRQILETTIKPRKIRKIFITHLHGDHVFGLPGFLSSRA 80
Cdd:NF041257  13 MRITFLGSGPPPPRRGQANTSILVELGNGERDKFFFDIGSGSVANIIALQIPYNLLNKVFITHLHVDHYGDLPYLYPFGA 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968  81 FqaNDEQTDVDIYGP------VGIKHLV------MASIRTSGAHLP----YHIHFHEFD-AKHLGKILETDKFMVYAEKL 143
Cdd:NF041257  93 W--SGRWTPLRVWGPsgrtpeLGTKHMVegmkemLAWDTDAFSGFPigdgYEIEVNEFDfRDENGVVYEENGVTVRSWPR 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968 144 DHTI-FCVGYRvvqkdlegtldaekLKAAGLPFgplfgrvkngqdvvledgttiiakdyisapkkgkVITilGDTRKTDA 222
Cdd:NF041257 171 SHAKdGAVSYR--------------LDWNGLSF----------------------------------VFT--GDGRPNEL 200

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488195968 223 SIRLALGADVLVHE--------STYSKGDENLARR---HGHSTNMEAARVAKAA 265
Cdd:NF041257 201 TVEYAKGADVFIHEcfdtpellSGKYGVPPELARYtidTHHTPPYAAGKVFSLV 254
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 37-237 7.18e-14

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: 68.82  E-value: 7.18e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968  37 DCGEGTQRQILETTIKPRKIRKIFITHLHGDHVFGLPGFLSSRAFQANdEQTDVDIYGPVGIKHLVMASirtsgahlpyh 116
Cdd:cd07740   31 DCGASSLIALKRAGIDPNAIDAIFITHLHGDHFGGLPFFLLDAQFVAK-RTRPLTIAGPPGLRERLRRA----------- 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968 117 ihfheFDAKHLGKILETDKFmvyaeklDHTifcvgYRVVQKDLEGTLDAEKLKAA----GLPFGPLFGRVKNGqdvvled 192
Cdd:cd07740   99 -----MEALFPGSSKVPRRF-------DLE-----VIELEPGEPTTLGGVTVTAFpvvhPSGALPLALRLEAA------- 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 488195968 193 gttiiakdyisapkkGKVITILGDTRKTDASIRLALGADVLVHES 237
Cdd:cd07740  155 ---------------GRVLAYSGDTEWTDALVPLARGADLFICEC 184
TaR3-like_MBL-fold cd07715
MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold ...
 36-251 3.73e-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: 3.73e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968  36 FDCGEGTQR--QILETTIKPRKIRkIFITHLHGDHVFGLPGFLSsrAFQANdeqTDVDIYGPvgikHLVMASIRT----- 108
Cdd:cd07715   37 LDAGTGIRElgNELMKEGPPGEAH-LLLSHTHWDHIQGFPFFAP--AYDPG---NRIHIYGP----HKDGGSLEEvlrrq 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968 109 --------SGAHLPYHIHFHEFDAkhlGKILETDKFMVYAEKLDHTIFCVGYRVvqkdlegtldaeklkaaglpfgplfg 180
Cdd:cd07715  107 msppyfpvPLEELLAAIEFHDLEP---GEPFSIGGVTVTTIPLNHPGGALGYRI-------------------------- 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488195968 181 rvkngqdvvlEDGttiiakdyisapkkGKVITILGDT-------RKTDASIRLALGADVLVHESTYSkgDENLARRHG 251
Cdd:cd07715  158 ----------EED--------------GKSVVYATDTehypddgESDEALLEFARGADLLIHDAQYT--DEEYPSKRG 209
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 31-111 5.25e-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: 51.79  E-value: 5.25e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968    31 NEIWMFDCGEGTQRQILET--TIKPRKIRKIFITHLHGDHVFGLPGFLssrafqandEQTDVDIYGPVGIKHLVMASIRT 108
Cdd:smart00849   9 GGAILIDTGPGEAEDLLAElkKLGPKKIDAIILTHGHPDHIGGLPELL---------EAPGAPVYAPEGTAELLKDLLAL 79


                   ...
gi 488195968   109 SGA 111
Cdd:smart00849  80 LGE 82
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 35-237 5.89e-08

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: 51.67  E-value: 5.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968  35 MFDCGEGTQRQiLETTIKPRKIRKIFITHLHGDHVFGLPGFLSSRAFQANDEQTD-VDIYGPVGIKHLVMASirtsgAHL 113
Cdd:cd07716   31 LLDCGSGVLSR-LQRYIDPEDLDAVVLSHLHPDHCADLGVLQYARRYHPRGARKPpLPLYGPAGPAERLAAL-----YGL 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968 114 PYHIHFHEFDAkhlGKILETDKFMVYAEKLDHTIFCVGYRVvqkdlegtldaeklkaaglpfgplfgrvkngqdvvlEDG 193
Cdd:cd07716  105 EDVFDFHPIEP---GEPLEIGPFTITFFRTVHPVPCYAMRI------------------------------------EDG 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 488195968 194 ttiiakdyisapkkGKVITILGDTRKTDASIRLALGADVLVHES 237
Cdd:cd07716  146 --------------GKVLVYTGDTGYCDELVEFARGADLLLCEA 175
RNaseZ_ELAC2-N-term-like_MBL-fold cd16296
Ribonuclease Z, N-terminus of human ELAC2 and related proteins; MBL-fold metallo-hydrolase ...
 20-214 8.32e-08

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: 51.11  E-value: 8.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968  20 SSLVLKLLDELNEiWMFDCGEGTQRQILETTIKPRKIRKIFITHLHGDHVFGLPGFLssrafqandeqtdvdiygpVGIK 99
Cdd:cd16296   11 MGAALYVFSEYNR-YLFNCGEGVQRLMQEHKLKVARLDNIFLTRMHWSNVGGLSGMI-------------------LTLK 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968 100 HLVMASIRTSGAHLPYHIhfhefDAKHLGKILETDKFMVYAekldhtIFCvgyRVVQKdlEGTLDAEKLKAAGLPFG--- 176
Cdd:cd16296   71 ETGLPKCVLSGPNKQSPD-----KIGVRRQILERDPSLVVA------FIC---KLHLK--KGNFLVLKAKELGLPVGtaa 134

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 488195968 177 --PLFGRVKNGQDVVLEdGTTIIAKDYISAPKKGKVITIL 214
Cdd:cd16296  135 iaPIIAAVKDGKSITFE-GREILAEELCTPPDPGIVFIVV 173
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 26-159 1.64e-07

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: 50.75  E-value: 1.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968  26 LLDELNEIWMFDCGEGTQRQILETTIK-PRKIRKIFITHLHGDHVFGLPGFLssrafqandEQTDVDIYGPVGIKHLVMA 104
Cdd:cd06262   15 VSDEEGEAILIDPGAGALEKILEAIEElGLKIKAILLTHGHFDHIGGLAELK---------EAPGAPVYIHEADAELLED 85

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488195968 105 SIRTSGAHLPYHIHFHEFDakhlgKILET-DKFMVYAEKLD------HTIFCVGYRVVQKDL 159
Cdd:cd06262   86 PELNLAFFGGGPLPPPEPD-----ILLEDgDTIELGGLELEvihtpgHTPGSVCFYIEEEGV 142
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 36-275 1.68e-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: 47.69  E-value: 1.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968   36 FDCGEGTQRQILET----TIKPRKIRKIFITHLHGDHVFGLPGFLSSRAFqandeqtdvDIYGPVGIkhlvmasirtsGA 111
Cdd:pfam12706   5 IDPGPDLRQQALPAlqpgRLRDDPIDAVLLTHDHYDHLAGLLDLREGRPR---------PLYAPLGV-----------LA 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968  112 HLPyhihfhefdakhlgkiletdKFMVYAEKLDHTifcvGYRVVQKDLEGTLdaeKLKAAGLPFGPLFGRVKNGQDVVLE 191
Cdd:pfam12706  65 HLR--------------------RNFPYLFLLEHY----GVRVHEIDWGESF---TVGDGGLTVTATPARHGSPRGLDPN 117

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968  192 DGTTI---IAKDyisapkkGKVITILGDTRKTDASIRLAL-GADVLVHESTYSkgDENLARRHGHSTNMEAARVAKAASV 267
Cdd:pfam12706 118 PGDTLgfrIEGP-------GKRVYYAGDTGYFPDEIGERLgGADLLLLDGGAW--RDDEMIHMGHMTPEEAVEAAADLGA 188


                  ....*...
gi 488195968  268 KKLLLNHI 275
Cdd:pfam12706 189 RRKVLIHI 196
PhnP-like_MBL-fold cd07736
phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase ...
 1-72 3.28e-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: 46.85  E-value: 3.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968   1 MEIQFLGTGA--GQP---------AKARNVSSLVLK----LLDELNEIWMFDCGEgTQrqiLETTIKPRKIRKIFITHLH 65
Cdd:cd07736    1 MKLTFLGTGDagGVPvygcdcsacQRARQDPSYRRRpcsaLIEVDGERILLDAGL-TD---LAERFPPGSIDAILLTHFH 76


                 ....*..
gi 488195968  66 GDHVFGL 72
Cdd:cd07736   77 MDHVQGL 83
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 1-154 1.77e-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: 1.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968   1 MEIQFLGTGAGQ-------------PAKARNV---SSLVLKLlDELNeiWMFDCGEGTQRQILETTIkpRKIRKIFITHL 64
Cdd:cd16279    1 MKLTFLGTGTSSgvpvigcdcgvcdSSDPKNRrlrSSILIET-GGKN--ILIDTGPDFRQQALRAGI--RKLDAVLLTHA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968  65 HGDHVFGLPGFlssRAFQaNDEQTDVDIYGPvgikHLVMASIRT--------SGAHLPYHIHFHEFDAKHLGKILETDkf 136
Cdd:cd16279   76 HADHIHGLDDL---RPFN-RLQQRPIPVYAS----EETLDDLKRrfpyffaaTGGGGVPKLDLHIIEPDEPFTIGGLE-- 145

                        170
                 ....*....|....*....
gi 488195968 137 mVYAEKLDH-TIFCVGYRV 154
Cdd:cd16279  146 -ITPLPVLHgKLPSLGFRF 163
class_II_PDE_MBL-fold cd07735
class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium ...
 1-154 7.96e-05

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: 43.35  E-value: 7.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968   1 MEIQFLGTGAGQPAkaRNVSSLVLKLLDELNEIwMFDCGEGTQRQILETTIKPR-------------KIRKIFITHLHGD 67
Cdd:cd07735    1 FELVVLGCSGGPDE--GNTSSFLLDPAGSDGDI-LLDAGTGVGALSLEEMFNDIlfpsqkaayelyqRIRHYLITHAHLD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968  68 HVFGLPgfLSSRAFQANDEQTdVDIYgpvGIKHlVMASIRTsgahlpyHI-----------------HFHEFDAKHLGKI 130
Cdd:cd07735   78 HIAGLP--LLSPNDGGQRGSP-KTIY---GLPE-TIDALKK-------HIfnwviwpdftsipsgkyPYLRLEPIEPEYP 143

                        170       180
                 ....*....|....*....|....*
gi 488195968 131 LETDKFMVYAEKLDHT-IFCVGYRV 154
Cdd:cd07735  144 IALTGLSVTAFPVSHGvPVSTAFLI 168
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
35-77 8.36e-05

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 42.74  E-value: 8.36e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 488195968   35 MFDCGEGTQRQILETT----IKPRKIRKIFITHLHGDHVFGLPGFLS 77
Cdd:pfam00753  19 LIDTGGSAEAALLLLLaalgLGPKDIDAVILTHGHFDHIGGLGELAE 65
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 34-113 1.53e-04

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: 41.75  E-value: 1.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968  34 WMFDCGEG------TQRQILETTIKPRkIRKIFITHLHGDHVFGLPGFLSSRAFQA-------NDEQTDVDIYGPVGIKH 100
Cdd:cd07722   30 ILIDTGEGrpsyipLLKSVLDSEGNAT-ISDILLTHWHHDHVGGLPDVLDLLRGPSprvykfpRPEEDEDPDEDGGDIHD 108

                         90
                 ....*....|....
gi 488195968 101 L-VMASIRTSGAHL 113
Cdd:cd07722  109 LqDGQVFKVEGATL 122
arylsulfatase_Sdsa1-like_MBL-fold cd07710
Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and ...
 36-111 6.87e-04

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: 40.18  E-value: 6.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488195968  36 FDCGEGTQ--RQILE---TTIKPRKIRKIFITHLHGDHVFGlpgflsSRAFQANDEQTDVDIYGPVG-IKHLVMASIRTS 109
Cdd:cd07710   32 IDTLESAEaaKAALElfrKHTGDKPVKAIIYTHSHPDHFGG------AGGFVEEEDSGKVPIIAPEGfMEEAVSENVLAG 105


                 ..
gi 488195968 110 GA 111
Cdd:cd07710  106 NA 107
Lactamase_B_4 pfam13691
tRNase Z endonuclease; This is family of tRNase Z enzymes, that are closely related ...
 31-65 1.38e-03

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: 36.41  E-value: 1.38e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 488195968   31 NEIWMF-DCGEGTQRQILETTIKPRKIRKIFITHLH 65
Cdd:pfam13691  21 SKRYLFgNVGEGTQRALNEQKVRLSKLEDIFLTGKV 56
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 51-72 2.58e-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: 38.68  E-value: 2.58e-03
                         10        20
                 ....*....|....*....|..
gi 488195968  51 IKPRKIRKIFITHLHGDHVFGL 72
Cdd:cd07720   87 IDPEDIDDVLLTHLHPDHIGGL 108
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 34-75 3.05e-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. Some members of this subgroup are annotated as GumP protein.


Pssm-ID: 293816 [Multi-domain]  Cd Length: 250  Bit Score: 38.40  E-value: 3.05e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 488195968  34 WMFDCGEGTQRQILETTIKPRKIRKIFITHLHGDHVFGLPGF 75
Cdd:cd07730   62 VPLEVEEDVAEQLAAGGIDPEDIDAVILSHLHWDHIGGLSDF 103
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 44-71 4.64e-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: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 37.55  E-value: 4.64e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 488195968  44 RQILET--TIKPRKIRKIFITHLHGDHVFG 71
Cdd:cd16282   39 RALLAAirKVTDKPVRYVVNTHYHGDHTLG 68
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 31-95 4.80e-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: 37.75  E-value: 4.80e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488195968  31 NEIWMFDCG-EGTQRQILETTIKPR--KIRKIFITHLHGDHVFGLPGFLssrafqandEQTDVDIYGP 95
Cdd:COG0491   24 DGAVLIDTGlGPADAEALLAALAALglDIKAVLLTHLHPDHVGGLAALA---------EAFGAPVYAH 82
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 31-76 5.21e-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: 37.91  E-value: 5.21e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 488195968  31 NEIWMFDCGEGTQRQILETTIKP-------RKIRKIFITHLHGDHVFGLPGFL 76
Cdd:COG2333   21 GKTILIDTGPRPSFDAGERVVLPylralgiRRLDLLVLTHPDADHIGGLAAVL 73
metallo-hydrolase-like_MBL-fold cd07739
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 44-73 5.28e-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: 5.28e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 488195968  44 RQILETTikpRKIRKIFITHLHGDHVFGLP 73
Cdd:cd07739   44 DWIKASG---KTLTTIYITHGHPDHYFGLE 70
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 13-79 6.09e-03

uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized Thermus thermophilus TTHA1429 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: 293811 [Multi-domain]  Cd Length: 184  Bit Score: 36.89  E-value: 6.09e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488195968  13 PAKARNVSSLVLKLLDELNEIwmfDCGEGTQ-------RQILETTIKPRKIRKIFITHLHGDHvFGLPGFLSSR 79
Cdd:cd07725    9 PGPLGHVNVYLLRDGDETTLI---DTGLATEedaealwEGLKELGLKPSDIDRVLLTHHHPDH-IGLAGKLQEK 78
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 51-75 8.95e-03

quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl Homoserine Lactones (also known as AHLs) are signal molecules which coordinate gene expression in quorum sensing, in many Gram-negative bacteria. Quorum-quenching N-acyl-homoserine lactonase (also known as AHL lactonase, N-acyl-L-homoserine lactone hydrolase, EC 3.1.1.81) catalyzes the hydrolysis and opening of the homoserine lactone rings of AHLs, a reaction that can block quorum sensing. These enzymes 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: 293815 [Multi-domain]  Cd Length: 238  Bit Score: 36.81  E-value: 8.95e-03
                         10        20
                 ....*....|....*....|....*
gi 488195968  51 IKPRKIRKIFITHLHGDHVFGLPGF 75
Cdd:cd07729   84 LDPEDIDYVILSHLHFDHAGGLDLF 108
 
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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