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Conserved domains on  [gi|508536759|gb|EOX05135|]
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ribonuclease Z [Escherichia coli KTE225]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 10021199)

MBL fold metallo-hydrolase is most likely a hydrolytic enzyme

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
true_RNase_BN TIGR02649
ribonuclease BN; Members of this protein family are ribonuclease BN of Escherichia coli K-12 ...
 3-305 0e+00

ribonuclease BN; Members of this protein family are ribonuclease BN of Escherichia coli K-12 and closely related proteins believed to be equivalent in function. Note that E. coli appears to lack RNase Z per se, and this protein of E. coli appears orthologous to (but not functionally equivalent to) RNase Z of Bacillus subtilis and various other species. Meanwhile, the yihY gene product of E. coli previously was incorrectly identified as RNase BN. [Transcription, RNA processing]


:

Pssm-ID: 131697  Cd Length: 303  Bit Score: 627.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759    3 LIFLGTSAGVPTRTRNVTAILLNLQHPTQSGLWLFDCGEGTQHQLLHTTFNPGKLDKIFISHLHGDHLFGLPGLLCSRSM 82
Cdd:TIGR02649   1 LIFLGTSAGVPTRTRNVTAILLNLQHPTQSGLWLFDCGEGTQHQLLHTAFNPGKLDKIFISHLHGDHLFGLPGLLCSRSM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759   83 SGIIQPLTIYGPQGIREFVETALRISGSWIDYPLEIVEIGAGEILDDGLRKVTAYPLEHPLECYGYRIEEHDKPGALNAQ 162
Cdd:TIGR02649  81 SGIIQPLTIYGPQGIREFVETALRISGSWTDYPLEIVEIGAGEILDDGLRKVTAYPLEHPLECYGYRIEEHDKPGALNAQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759  163 ALKAAGVPPGPLFQALKAGKTIMLEDGRQINGADYLAAPVPGKALAIFGDTGPCDAALDLAKGVDVMVHEATLDITMEAK 242
Cdd:TIGR02649 161 ALKAAGVPPGPLFQELKAGKTITLEDGRQINGADYLAAPVPGKALAIFGDTGPCDAALDLAKGVDVMVHEATLDITMEAK 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 508536759  243 ANSRGHSSTRQAATLAREAGVGKLIITHVSSRYDDKGCQHLLRECRSIFPATELANDFTVFNV 305
Cdd:TIGR02649 241 ANSRGHSSTRQAATLAREAGVGKLIITHVSSRYDDKGCQHLLRECRSIFPATELANDFTVFNV 303
 
Name Accession Description Interval E-value
true_RNase_BN TIGR02649
ribonuclease BN; Members of this protein family are ribonuclease BN of Escherichia coli K-12 ...
 3-305 0e+00

ribonuclease BN; Members of this protein family are ribonuclease BN of Escherichia coli K-12 and closely related proteins believed to be equivalent in function. Note that E. coli appears to lack RNase Z per se, and this protein of E. coli appears orthologous to (but not functionally equivalent to) RNase Z of Bacillus subtilis and various other species. Meanwhile, the yihY gene product of E. coli previously was incorrectly identified as RNase BN. [Transcription, RNA processing]


Pssm-ID: 131697  Cd Length: 303  Bit Score: 627.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759    3 LIFLGTSAGVPTRTRNVTAILLNLQHPTQSGLWLFDCGEGTQHQLLHTTFNPGKLDKIFISHLHGDHLFGLPGLLCSRSM 82
Cdd:TIGR02649   1 LIFLGTSAGVPTRTRNVTAILLNLQHPTQSGLWLFDCGEGTQHQLLHTAFNPGKLDKIFISHLHGDHLFGLPGLLCSRSM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759   83 SGIIQPLTIYGPQGIREFVETALRISGSWIDYPLEIVEIGAGEILDDGLRKVTAYPLEHPLECYGYRIEEHDKPGALNAQ 162
Cdd:TIGR02649  81 SGIIQPLTIYGPQGIREFVETALRISGSWTDYPLEIVEIGAGEILDDGLRKVTAYPLEHPLECYGYRIEEHDKPGALNAQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759  163 ALKAAGVPPGPLFQALKAGKTIMLEDGRQINGADYLAAPVPGKALAIFGDTGPCDAALDLAKGVDVMVHEATLDITMEAK 242
Cdd:TIGR02649 161 ALKAAGVPPGPLFQELKAGKTITLEDGRQINGADYLAAPVPGKALAIFGDTGPCDAALDLAKGVDVMVHEATLDITMEAK 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 508536759  243 ANSRGHSSTRQAATLAREAGVGKLIITHVSSRYDDKGCQHLLRECRSIFPATELANDFTVFNV 305
Cdd:TIGR02649 241 ANSRGHSSTRQAATLAREAGVGKLIITHVSSRYDDKGCQHLLRECRSIFPATELANDFTVFNV 303
PRK00055 PRK00055
ribonuclease Z; Reviewed
 1-305 9.47e-140

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 395.32  E-value: 9.47e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759   1 MELIFLGTSAGVPTRTRNVTAILLNLQHptqsGLWLFDCGEGTQHQLLHTTFNPGKLDKIFISHLHGDHLFGLPGLLCSR 80
Cdd:PRK00055   2 MELTFLGTGSGVPTPTRNVSSILLRLGG----ELFLFDCGEGTQRQLLKTGIKPRKIDKIFITHLHGDHIFGLPGLLSTR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759  81 SMSGIIQPLTIYGPQGIREFVETALRISGSwidypleiveigageilddglrkvtayplehplecYGYRIEEHDKPGALN 160
Cdd:PRK00055  78 SLSGRTEPLTIYGPKGIKEFVETLLRASGS-----------------------------------LGYRIAEKDKPGKLD 122

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759 161 AQALKAAGVPPGPLFQALKAGKTIMLEDGRQINGADYLAAPVPGKALAIFGDTGPCDAALDLAKGVDVMVHEATLDITME 240
Cdd:PRK00055 123 AEKLKALGVPPGPLFGKLKRGEDVTLEDGRIINPADVLGPPRKGRKVAYCGDTRPCEALVELAKGADLLVHEATFGDEDE 202

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 508536759 241 AKANSRGHSSTRQAATLAREAGVGKLIITHVSSRYDDkGCQHLLRECRSIFPATELANDFTVFNV 305
Cdd:PRK00055 203 ELAKEYGHSTARQAAEIAKEAGVKRLILTHFSPRYTG-DPEELLKEAREIFPNTELAEDLMRVEV 266
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 3-303 3.47e-123

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: 352.52  E-value: 3.47e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759   3 LIFLGTSAGVPTRTRNVTAILLNLQHPtqsgLWLFDCGEGTQHQLLHTTFNPGKLDKIFISHLHGDHLFGLPGLLCSRSM 82
Cdd:cd07717    1 LTFLGTGSAVPTPERNLSSIALRLEGE----LWLFDCGEGTQRQLLRAGLSPSKIDRIFITHLHGDHILGLPGLLSTMSL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759  83 SGIIQPLTIYGPQGIREFVETALRISGSWIDYPLEIVEI--GAGEILDDGLRKVTAYPLEHPLECYGYRIEEhdkpgaln 160
Cdd:cd07717   77 LGRTEPLTIYGPKGLKEFLETLLRLSASRLPYPIEVHELepDPGLVFEDDGFTVTAFPLDHRVPCFGYRFEE-------- 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759 161 aqalkaagvppgplfqalkagktimledgrqingadylaapvpGKALAIFGDTGPCDAALDLAKGVDVMVHEATLDITME 240
Cdd:cd07717  149 -------------------------------------------GRKIAYLGDTRPCEGLVELAKGADLLIHEATFLDDDA 185

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 508536759 241 AKANSRGHSSTRQAATLAREAGVGKLIITHVSSRYDDkgCQHLLRECRSIFPATELANDFTVF 303
Cdd:cd07717  186 EKAKETGHSTAKQAAEIAKKAGVKKLVLTHFSARYKD--PEELLKEARAVFPNTILAEDFMTI 246
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
1-305 5.30e-107

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 311.36  E-value: 5.30e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759   1 MELIFLGTSAGVPTRTRNVTAILLNLQhptqSGLWLFDCGEGTQHQLLHTTFNPGKLDKIFISHLHGDHLFGLPGLLCSR 80
Cdd:COG1234    1 MKLTFLGTGGAVPTPGRATSSYLLEAG----GERLLIDCGEGTQRQLLRAGLDPRDIDAIFITHLHGDHIAGLPGLLSTR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759  81 SMSGIIQPLTIYGPQGIREFVETALRISGSWIDYPLEIVEIGAGEILDDGLRKVTAYPLEHPLECYGYRIEEhdkpgaln 160
Cdd:COG1234   77 SLAGREKPLTIYGPPGTKEFLEALLKASGTDLDFPLEFHEIEPGEVFEIGGFTVTAFPLDHPVPAYGYRFEE-------- 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759 161 aqalkaagvppgplfqalkagktimledgrqingadylaapvPGKALAIFGDTGPCDAALDLAKGVDVMVHEATLDITME 240
Cdd:COG1234  149 ------------------------------------------PGRSLVYSGDTRPCEALVELAKGADLLIHEATFLDEEA 186

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 508536759 241 AKANSRGHSSTRQAATLAREAGVGKLIITHVSSRYDDKgcQHLLRECRSIFPA-TELANDFTVFNV 305
Cdd:COG1234  187 ELAKETGHSTAKEAAELAAEAGVKRLVLTHFSPRYDDP--EELLAEARAVFPGpVELAEDGMVIEL 250
GntH_guanitoxin NF041257
guanitoxin biosynthesis MBL fold metallo-hydrolase GntH;
1-305 8.05e-17

guanitoxin biosynthesis MBL fold metallo-hydrolase GntH;


Pssm-ID: 469157 [Multi-domain]  Cd Length: 372  Bit Score: 79.67  E-value: 8.05e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759   1 MELIFLGTSAGVPTRTRNVTAILLNLQHPTQSGLwLFDCGEGTQHQLLHTTFNPGKLDKIFISHLHGDHLFGLPGLLCSR 80
Cdd:NF041257  13 MRITFLGSGPPPPRRGQANTSILVELGNGERDKF-FFDIGSGSVANIIALQIPYNLLNKVFITHLHVDHYGDLPYLYPFG 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759  81 SMSGIIQPLTIYGPQ------GIREFVEtalrisgswidypleiveigageilddGLRKVTAYPLEHPLECY---GYRIE 151
Cdd:NF041257  92 AWSGRWTPLRVWGPSgrtpelGTKHMVE---------------------------GMKEMLAWDTDAFSGFPigdGYEIE 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759 152 EHDkpgalnaqalkaagvppgplFQALKAGKTIMLEDG------RQINGADylaAPVP------GKALAIFGDTGPCDAA 219
Cdd:NF041257 145 VNE--------------------FDFRDENGVVYEENGvtvrswPRSHAKD---GAVSyrldwnGLSFVFTGDGRPNELT 201

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759 220 LDLAKGVDVMVHEATldITMEAKANSRG-------------HSSTRQAATLAREAGVGKLIITHVSsrYDDKGCQHLLRE 286
Cdd:NF041257 202 VEYAKGADVFIHECF--DTPELLSGKYGvppelarytidthHTPPYAAGKVFSLVQPRLAMATHFF--NDPDTVAEILAE 277

                        330       340
                 ....*....|....*....|
gi 508536759 287 CRSIFPA-TELANDFTVFNV 305
Cdd:NF041257 278 IRAHYDGpLSFGPDLMVVNV 297
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 36-270 2.77e-14

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: 70.03  E-value: 2.77e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759   36 LFDCGEGTQHQLLHTTFNP----GKLDKIFISHLHGDHLFGLPGLLCSRsmsgiiqPLTIYGPQGIREFVETALRISGSW 111
Cdd:pfam12706   4 LIDPGPDLRQQALPALQPGrlrdDPIDAVLLTHDHYDHLAGLLDLREGR-------PRPLYAPLGVLAHLRRNFPYLFLL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759  112 IDYPLEIVEIGAGEI--LDDGLRKVTAYPLEH---------PLECYGYRIEEhdkpgalnaqalkaagvppgplfqalka 180
Cdd:pfam12706  77 EHYGVRVHEIDWGESftVGDGGLTVTATPARHgsprgldpnPGDTLGFRIEG---------------------------- 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759  181 gktimledgrqingadylaapvPGKALAIFGDTGPCDAAL-DLAKGVDVMVHEATLdiTMEAKANSRGHSSTRQAATLAR 259
Cdd:pfam12706 129 ----------------------PGKRVYYAGDTGYFPDEIgERLGGADLLLLDGGA--WRDDEMIHMGHMTPEEAVEAAA 184

                         250
                  ....*....|.
gi 508536759  260 EAGVGKLIITH 270
Cdd:pfam12706 185 DLGARRKVLIH 195
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 30-153 4.47e-10

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: 57.95  E-value: 4.47e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759    30 TQSGLWLFDCGEGTQHQLLHT--TFNPGKLDKIFISHLHGDHLFGLPGLLCsrsmsgiIQPLTIYGPQGIREFVETALRI 107
Cdd:smart00849   7 DDGGAILIDTGPGEAEDLLAElkKLGPKKIDAIILTHGHPDHIGGLPELLE-------APGAPVYAPEGTAELLKDLLAL 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 508536759   108 SGS---WIDYPLEIVEIGAGEILDDGLRKVTAYPLE-HPLECYGYRIEEH 153
Cdd:smart00849  80 LGElgaEAEPAPPDRTLKDGDELDLGGGELEVIHTPgHTPGSIVLYLPEG 129
 
Name Accession Description Interval E-value
true_RNase_BN TIGR02649
ribonuclease BN; Members of this protein family are ribonuclease BN of Escherichia coli K-12 ...
 3-305 0e+00

ribonuclease BN; Members of this protein family are ribonuclease BN of Escherichia coli K-12 and closely related proteins believed to be equivalent in function. Note that E. coli appears to lack RNase Z per se, and this protein of E. coli appears orthologous to (but not functionally equivalent to) RNase Z of Bacillus subtilis and various other species. Meanwhile, the yihY gene product of E. coli previously was incorrectly identified as RNase BN. [Transcription, RNA processing]


Pssm-ID: 131697  Cd Length: 303  Bit Score: 627.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759    3 LIFLGTSAGVPTRTRNVTAILLNLQHPTQSGLWLFDCGEGTQHQLLHTTFNPGKLDKIFISHLHGDHLFGLPGLLCSRSM 82
Cdd:TIGR02649   1 LIFLGTSAGVPTRTRNVTAILLNLQHPTQSGLWLFDCGEGTQHQLLHTAFNPGKLDKIFISHLHGDHLFGLPGLLCSRSM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759   83 SGIIQPLTIYGPQGIREFVETALRISGSWIDYPLEIVEIGAGEILDDGLRKVTAYPLEHPLECYGYRIEEHDKPGALNAQ 162
Cdd:TIGR02649  81 SGIIQPLTIYGPQGIREFVETALRISGSWTDYPLEIVEIGAGEILDDGLRKVTAYPLEHPLECYGYRIEEHDKPGALNAQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759  163 ALKAAGVPPGPLFQALKAGKTIMLEDGRQINGADYLAAPVPGKALAIFGDTGPCDAALDLAKGVDVMVHEATLDITMEAK 242
Cdd:TIGR02649 161 ALKAAGVPPGPLFQELKAGKTITLEDGRQINGADYLAAPVPGKALAIFGDTGPCDAALDLAKGVDVMVHEATLDITMEAK 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 508536759  243 ANSRGHSSTRQAATLAREAGVGKLIITHVSSRYDDKGCQHLLRECRSIFPATELANDFTVFNV 305
Cdd:TIGR02649 241 ANSRGHSSTRQAATLAREAGVGKLIITHVSSRYDDKGCQHLLRECRSIFPATELANDFTVFNV 303
PRK00055 PRK00055
ribonuclease Z; Reviewed
 1-305 9.47e-140

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 395.32  E-value: 9.47e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759   1 MELIFLGTSAGVPTRTRNVTAILLNLQHptqsGLWLFDCGEGTQHQLLHTTFNPGKLDKIFISHLHGDHLFGLPGLLCSR 80
Cdd:PRK00055   2 MELTFLGTGSGVPTPTRNVSSILLRLGG----ELFLFDCGEGTQRQLLKTGIKPRKIDKIFITHLHGDHIFGLPGLLSTR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759  81 SMSGIIQPLTIYGPQGIREFVETALRISGSwidypleiveigageilddglrkvtayplehplecYGYRIEEHDKPGALN 160
Cdd:PRK00055  78 SLSGRTEPLTIYGPKGIKEFVETLLRASGS-----------------------------------LGYRIAEKDKPGKLD 122

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759 161 AQALKAAGVPPGPLFQALKAGKTIMLEDGRQINGADYLAAPVPGKALAIFGDTGPCDAALDLAKGVDVMVHEATLDITME 240
Cdd:PRK00055 123 AEKLKALGVPPGPLFGKLKRGEDVTLEDGRIINPADVLGPPRKGRKVAYCGDTRPCEALVELAKGADLLVHEATFGDEDE 202

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 508536759 241 AKANSRGHSSTRQAATLAREAGVGKLIITHVSSRYDDkGCQHLLRECRSIFPATELANDFTVFNV 305
Cdd:PRK00055 203 ELAKEYGHSTARQAAEIAKEAGVKRLILTHFSPRYTG-DPEELLKEAREIFPNTELAEDLMRVEV 266
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 2-305 1.84e-138

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: 393.12  E-value: 1.84e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759    2 ELIFLGTSAGVPTRTRNVTAILLNLqhptqSG-LWLFDCGEGTQHQLLHTTFNPGKLDKIFISHLHGDHLFGLPGLLCSR 80
Cdd:TIGR02651   1 EITFLGTGGGVPTKERNLPSIALKL-----NGeLWLFDCGEGTQRQMLRSGISPMKIDRIFITHLHGDHILGLPGLLSTM 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759   81 SMSGIIQPLTIYGPQGIREFVETALRISGSWIDYPLEIVEIGAGE-ILDDGLRKVTAYPLEHPLECYGYRIEEHDKPGAL 159
Cdd:TIGR02651  76 SFQGRKEPLTIYGPPGIKEFIETSLRVSYTYLNYPIKIHEIEEGGlVFEDDGFKVEAFPLDHSIPSLGYRFEEKDRPGKF 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759  160 NAQALKAAGVPPGPLFQALKAGKTIMLEDGRQINGADYLAAPVPGKALAIFGDTGPCDAALDLAKGVDVMVHEATLDITM 239
Cdd:TIGR02651 156 DREKAKELGIPPGPLYGKLKRGETVTLIDGRIIDPEDVLGPPRKGRKIAYTGDTRPCEEVIEFAKNADLLIHEATFLDED 235

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 508536759  240 EAKANSRGHSSTRQAATLAREAGVGKLIITHVSSRYDDKgcQHLLRECRSIFPATELANDFTVFNV 305
Cdd:TIGR02651 236 KKLAKEYGHSTAAQAAEIAKEANVKRLILTHISPRYSDE--EELLEEAKKIFPNTYIAEDFMEIEI 299
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 3-303 3.47e-123

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: 352.52  E-value: 3.47e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759   3 LIFLGTSAGVPTRTRNVTAILLNLQHPtqsgLWLFDCGEGTQHQLLHTTFNPGKLDKIFISHLHGDHLFGLPGLLCSRSM 82
Cdd:cd07717    1 LTFLGTGSAVPTPERNLSSIALRLEGE----LWLFDCGEGTQRQLLRAGLSPSKIDRIFITHLHGDHILGLPGLLSTMSL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759  83 SGIIQPLTIYGPQGIREFVETALRISGSWIDYPLEIVEI--GAGEILDDGLRKVTAYPLEHPLECYGYRIEEhdkpgaln 160
Cdd:cd07717   77 LGRTEPLTIYGPKGLKEFLETLLRLSASRLPYPIEVHELepDPGLVFEDDGFTVTAFPLDHRVPCFGYRFEE-------- 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759 161 aqalkaagvppgplfqalkagktimledgrqingadylaapvpGKALAIFGDTGPCDAALDLAKGVDVMVHEATLDITME 240
Cdd:cd07717  149 -------------------------------------------GRKIAYLGDTRPCEGLVELAKGADLLIHEATFLDDDA 185

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 508536759 241 AKANSRGHSSTRQAATLAREAGVGKLIITHVSSRYDDkgCQHLLRECRSIFPATELANDFTVF 303
Cdd:cd07717  186 EKAKETGHSTAKQAAEIAKKAGVKKLVLTHFSARYKD--PEELLKEARAVFPNTILAEDFMTI 246
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
1-305 5.30e-107

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 311.36  E-value: 5.30e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759   1 MELIFLGTSAGVPTRTRNVTAILLNLQhptqSGLWLFDCGEGTQHQLLHTTFNPGKLDKIFISHLHGDHLFGLPGLLCSR 80
Cdd:COG1234    1 MKLTFLGTGGAVPTPGRATSSYLLEAG----GERLLIDCGEGTQRQLLRAGLDPRDIDAIFITHLHGDHIAGLPGLLSTR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759  81 SMSGIIQPLTIYGPQGIREFVETALRISGSWIDYPLEIVEIGAGEILDDGLRKVTAYPLEHPLECYGYRIEEhdkpgaln 160
Cdd:COG1234   77 SLAGREKPLTIYGPPGTKEFLEALLKASGTDLDFPLEFHEIEPGEVFEIGGFTVTAFPLDHPVPAYGYRFEE-------- 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759 161 aqalkaagvppgplfqalkagktimledgrqingadylaapvPGKALAIFGDTGPCDAALDLAKGVDVMVHEATLDITME 240
Cdd:COG1234  149 ------------------------------------------PGRSLVYSGDTRPCEALVELAKGADLLIHEATFLDEEA 186

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 508536759 241 AKANSRGHSSTRQAATLAREAGVGKLIITHVSSRYDDKgcQHLLRECRSIFPA-TELANDFTVFNV 305
Cdd:COG1234  187 ELAKETGHSTAKEAAELAAEAGVKRLVLTHFSPRYDDP--EELLAEARAVFPGpVELAEDGMVIEL 250
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 3-233 6.04e-60

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: 189.01  E-value: 6.04e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759   3 LIFLGTSAGVPTRTRNVTAILLNlqhpTQSGLWLFDCGEGTQHQLLHTTFNPGKLDKIFISHLHGDHLFGLPGLLCSRSM 82
Cdd:cd16272    1 LTFLGTGGAVPSLTRNTSSYLLE----TGGTRILLDCGEGTVYRLLKAGVDPDKLDAIFLSHFHLDHIGGLPTLLFARRY 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759  83 SGIIQPLTIYGPQGIREFVETALRIS--GSWIDYPLEIVEIG-AGEILDDGLRKVTAYPLEHPLECYGYRIEEHdkpgal 159
Cdd:cd16272   77 GGRKKPLTIYGPKGIKEFLEKLLNFPveILPLGFPLEIEELEeGGEVLELGDLKVEAFPVKHSVESLGYRIEAE------ 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 508536759 160 naqalkaagvppgplfqalkagktimledgrqingadylaapvpGKALAIFGDTGPCDAALDLAKGVDVMVHEA 233
Cdd:cd16272  151 --------------------------------------------GKSIVYSGDTGPCENLVELAKGADLLIHEC 180
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 2-231 1.16e-34

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: 124.55  E-value: 1.16e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759   2 ELIFLGTSAGVPTRTRNVTAILLnlqhptQSG--LWLFDCGEGTQHQLLHTTFNPGKLDKIFISHLHGDHLFGLPGLLCS 79
Cdd:cd07719    1 RVTLLGTGGPIPDPDRAGPSTLV------VVGgrVYLVDAGSGVVRRLAQAGLPLGDLDAVFLTHLHSDHVADLPALLLT 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759  80 RSMSGIIQPLTIYGPQGIREFVETALRISGSWIDYP--------------LEIVEIGAGEIL--DDGLRkVTAYPLEHP- 142
Cdd:cd07719   75 AWLAGRKTPLPVYGPPGTRALVDGLLAAYALDIDYRarigdegrpdpgalVEVHEIAAGGVVyeDDGVK-VTAFLVDHGp 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759 143 -LECYGYRIEehdkpgalnaqalkaagvppgplfqalkagktimledgrqingadylaapVPGKALAIFGDTGPCDAALD 221
Cdd:cd07719  154 vPPALAYRFD--------------------------------------------------TPGRSVVFSGDTGPSENLIE 183

                        250
                 ....*....|
gi 508536759 222 LAKGVDVMVH 231
Cdd:cd07719  184 LAKGADLLVH 193
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 1-305 2.58e-31

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 117.69  E-value: 2.58e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759   1 MELIFLGT--SAGVP--------------TRTRNVTAILLNlqhpTQSGLWLFDCGEGTQHQLLHTTFNPGKLDKIFISH 64
Cdd:COG1235    1 MKVTFLGSgsSGGVPqigcdcpvcastdpRYGRTRSSILVE----ADGTRLLIDAGPDLREQLLRLGLDPSKIDAILLTH 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759  65 LHGDHLFGLPGLlcsrSMSGIIQPLTIYGPQGIREFVETALRISGSWIDYPLEIVEIGAGEILD-DGLRkVTAYPLEHP- 142
Cdd:COG1235   77 EHADHIAGLDDL----RPRYGPNPIPVYATPGTLEALERRFPYLFAPYPGKLEFHEIEPGEPFEiGGLT-VTPFPVPHDa 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759 143 LECYGYRIEEhdkpgalnaqalkaagvppgplfqalkagktimledgrqingadylaapvPGKALAIFGDTGP-CDAALD 221
Cdd:COG1235  152 GDPVGYRIED--------------------------------------------------GGKKLAYATDTGYiPEEVLE 181

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759 222 LAKGVDVMVHEATLDitmeakANSRGHSSTRQAATLAREAGVGKLIITHVSSRYDDKGCQHLLRECRSIFPATELANDFT 301
Cdd:COG1235  182 LLRGADLLILDATYD------DPEPGHLSNEEALELLARLGPKRLVLTHLSPDNNDHELDYDELEAALLPAGVEVAYDGM 255


                 ....
gi 508536759 302 VFNV 305
Cdd:COG1235  256 EIEL 259
RNaseZ_ELAC1_ELAC2-C-term-like_MBL-fold cd07718
Ribonuclease Z ELAC1, C-terminus of ELAC2, and related proteins; MBL-fold metallo-hydrolase ...
 3-234 4.70e-30

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


Pssm-ID: 293804 [Multi-domain]  Cd Length: 204  Bit Score: 112.64  E-value: 4.70e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759   3 LIFLGTSAGVPTRTRNVTAILLNLqhPTQSGLwLFDCGEGTQHQLLHTtFNPGKLDK-------IFISHLHGDHLFGLPG 75
Cdd:cd07718    1 VVFLGTGSAIPSKYRNVSGILLRI--PGDGSI-LLDCGEGTLGQLRRH-YGPEEADEvlrnlkcIFISHLHADHHLGLIR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759  76 LLCSRS--MSGIIQPLTIYGPQGIREFvetaLRISGSWIDYPLEIVEIGAGEILDD--------------------GLRK 133
Cdd:cd07718   77 LLAERKklFKPPSPPLYVVAPRQLRRW----LREYSSLEDLGLHDISFISNRVSQSlpesddplsrdllsnlleelGLKS 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759 134 VTAYPLEHPLECYGYRIeEHDKpgalnaqalkaagvppgplfqalkagktimledgrqingadylaapvpGKALAIFGDT 213
Cdd:cd07718  153 IETVPVIHCPDAYGIVL-THED------------------------------------------------GWKIVYSGDT 183

                        250       260
                 ....*....|....*....|.
gi 508536759 214 GPCDAALDLAKGVDVMVHEAT 234
Cdd:cd07718  184 RPCEALVEAGKGADLLIHEAT 204
PRK02126 PRK02126
ribonuclease Z; Provisional
 36-293 1.24e-27

ribonuclease Z; Provisional


Pssm-ID: 235006 [Multi-domain]  Cd Length: 334  Bit Score: 109.62  E-value: 1.24e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759  36 LFDCGEgtqhqlLHTtFNPGKL---DKIFISHLHGDHLFGLPGLLcsRSMSGIIQPLTIYGPQGIREFVETALR------ 106
Cdd:PRK02126  31 LFDLGD------LHH-LPPRELlriSHIFVSHTHMDHFIGFDRLL--RHCLGRPRRLRLFGPPGFADQVEHKLAgytwnl 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759 107 ISGSWIDYPLEIVEIGA--------------------------GEILDDGLRKVTAYPLEHPLECYGYRIEEHDKPgALN 160
Cdd:PRK02126 102 VENYPTTFRVHEVELHDgrirralfscrrafareaeeelslpdGVLLDEPWFRVRAAFLDHGIPCLAFALEEKAHI-NID 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759 161 AQALKAAGVPPGPLFQALKAG----------KTIMLEDGRQINGADYLAAP--------VPGKALAIFGDTGP----CDA 218
Cdd:PRK02126 181 KNRLAELGLPPGPWLRELKHAvlrgepddtpIRVLWRDGGGEHERVRPLGElkervlriEPGQKIGYVTDIGYteenLAR 260

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 508536759 219 ALDLAKGVDVMVHEAT-LDITMEaKANSRGHSSTRQAATLAREAGVGKLIITHVSSRYDDKGcQHLLRECRSIFPA 293
Cdd:PRK02126 261 IVELAAGVDLLFIEAVfLDEDAE-KARRKNHLTARQAGRLAREAGVKRLLPFHFSPRYQGRG-AELYREARAAFAG 334
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 4-233 1.00e-24

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: 98.49  E-value: 1.00e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759   4 IFLGTSAGVPTRTRNVTAILLNlqhpTQSGLWLFDCGEGTQHQLLHTTFNPGKLDKIFISHLHGDHLFGLPGLLCS-RSM 82
Cdd:cd07740    1 TFLGSGDAFGSGGRLNTCFHVA----SEAGRFLIDCGASSLIALKRAGIDPNAIDAIFITHLHGDHFGGLPFFLLDaQFV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759  83 SGIIQPLTIYGPQGIREFVETALRIS---GSWIDY--PLEIVEIGAGEILDDGLRKVTAYPLEHPLECYGYRieehdkpg 157
Cdd:cd07740   77 AKRTRPLTIAGPPGLRERLRRAMEALfpgSSKVPRrfDLEVIELEPGEPTTLGGVTVTAFPVVHPSGALPLA-------- 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 508536759 158 alnaqalkaagvppgplfqalkagktimledGRQINGadylaapvpGKALAIFGDTGPCDAALDLAKGVDVMVHEA 233
Cdd:cd07740  149 -------------------------------LRLEAA---------GRVLAYSGDTEWTDALVPLARGADLFICEC 184
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 36-233 4.19e-21

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: 88.27  E-value: 4.19e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759  36 LFDCGEGTQHQLLHTTfNPGKLDKIFISHLHGDHLFGLPGLLCSRSMS---GIIQPLTIYGPQGIREFVETAlrisgSWI 112
Cdd:cd07716   31 LLDCGSGVLSRLQRYI-DPEDLDAVVLSHLHPDHCADLGVLQYARRYHprgARKPPLPLYGPAGPAERLAAL-----YGL 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759 113 DYPLEIVEIGAGEILDDGLRKVTAYPLEHPLECYGYRIEEhdkpgalnaqalkaagvppgplfqalkagktimledgrqi 192
Cdd:cd07716  105 EDVFDFHPIEPGEPLEIGPFTITFFRTVHPVPCYAMRIED---------------------------------------- 144

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 508536759 193 ngadylaapvPGKALAIFGDTGPCDAALDLAKGVDVMVHEA 233
Cdd:cd07716  145 ----------GGKVLVYTGDTGYCDELVEFARGADLLLCEA 175
GntH_guanitoxin NF041257
guanitoxin biosynthesis MBL fold metallo-hydrolase GntH;
1-305 8.05e-17

guanitoxin biosynthesis MBL fold metallo-hydrolase GntH;


Pssm-ID: 469157 [Multi-domain]  Cd Length: 372  Bit Score: 79.67  E-value: 8.05e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759   1 MELIFLGTSAGVPTRTRNVTAILLNLQHPTQSGLwLFDCGEGTQHQLLHTTFNPGKLDKIFISHLHGDHLFGLPGLLCSR 80
Cdd:NF041257  13 MRITFLGSGPPPPRRGQANTSILVELGNGERDKF-FFDIGSGSVANIIALQIPYNLLNKVFITHLHVDHYGDLPYLYPFG 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759  81 SMSGIIQPLTIYGPQ------GIREFVEtalrisgswidypleiveigageilddGLRKVTAYPLEHPLECY---GYRIE 151
Cdd:NF041257  92 AWSGRWTPLRVWGPSgrtpelGTKHMVE---------------------------GMKEMLAWDTDAFSGFPigdGYEIE 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759 152 EHDkpgalnaqalkaagvppgplFQALKAGKTIMLEDG------RQINGADylaAPVP------GKALAIFGDTGPCDAA 219
Cdd:NF041257 145 VNE--------------------FDFRDENGVVYEENGvtvrswPRSHAKD---GAVSyrldwnGLSFVFTGDGRPNELT 201

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759 220 LDLAKGVDVMVHEATldITMEAKANSRG-------------HSSTRQAATLAREAGVGKLIITHVSsrYDDKGCQHLLRE 286
Cdd:NF041257 202 VEYAKGADVFIHECF--DTPELLSGKYGvppelarytidthHTPPYAAGKVFSLVQPRLAMATHFF--NDPDTVAEILAE 277

                        330       340
                 ....*....|....*....|
gi 508536759 287 CRSIFPA-TELANDFTVFNV 305
Cdd:NF041257 278 IRAHYDGpLSFGPDLMVVNV 297
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 36-270 2.77e-14

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: 70.03  E-value: 2.77e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759   36 LFDCGEGTQHQLLHTTFNP----GKLDKIFISHLHGDHLFGLPGLLCSRsmsgiiqPLTIYGPQGIREFVETALRISGSW 111
Cdd:pfam12706   4 LIDPGPDLRQQALPALQPGrlrdDPIDAVLLTHDHYDHLAGLLDLREGR-------PRPLYAPLGVLAHLRRNFPYLFLL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759  112 IDYPLEIVEIGAGEI--LDDGLRKVTAYPLEH---------PLECYGYRIEEhdkpgalnaqalkaagvppgplfqalka 180
Cdd:pfam12706  77 EHYGVRVHEIDWGESftVGDGGLTVTATPARHgsprgldpnPGDTLGFRIEG---------------------------- 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759  181 gktimledgrqingadylaapvPGKALAIFGDTGPCDAAL-DLAKGVDVMVHEATLdiTMEAKANSRGHSSTRQAATLAR 259
Cdd:pfam12706 129 ----------------------PGKRVYYAGDTGYFPDEIgERLGGADLLLLDGGA--WRDDEMIHMGHMTPEEAVEAAA 184

                         250
                  ....*....|.
gi 508536759  260 EAGVGKLIITH 270
Cdd:pfam12706 185 DLGARRKVLIH 195
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 1-151 1.47e-12

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: 65.19  E-value: 1.47e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759   1 MELIFLGT--SAGVPT----------------RTRnvTAILLnlQHPTQSglWLFDCGEGTQHQLLhtTFNPGKLDKIFI 62
Cdd:cd16279    1 MKLTFLGTgtSSGVPVigcdcgvcdssdpknrRLR--SSILI--ETGGKN--ILIDTGPDFRQQAL--RAGIRKLDAVLL 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759  63 SHLHGDHLFGLPGLlcsRSMSGIIQ-PLTIYGPQ----GIREFVETALRISGSWIDYPLEIVEIGAGEILD-DGLrKVTA 136
Cdd:cd16279   73 THAHADHIHGLDDL---RPFNRLQQrPIPVYASEetldDLKRRFPYFFAATGGGGVPKLDLHIIEPDEPFTiGGL-EITP 148

                        170
                 ....*....|....*.
gi 508536759 137 YPLEH-PLECYGYRIE 151
Cdd:cd16279  149 LPVLHgKLPSLGFRFG 164
metallo-hydrolase-like_MBL-fold cd07741
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 3-270 3.45e-10

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


Pssm-ID: 293827 [Multi-domain]  Cd Length: 212  Bit Score: 58.74  E-value: 3.45e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759   3 LIFLGTSAGvptrtRNVTA--------ILLNLqhptqSGLWLF-DCGEGTQHQLLHTTFNPGKLDKIFISHLHGDHLFGL 73
Cdd:cd07741    1 IIFLGTGGG-----RFVVItqlrasggIWIEL-----NGKNIHiDPGPGALVRMCRPKLDPTKLDAIILSHRHLDHSNDA 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759  74 PGLLCSRSMSGIIQPLTIYGPqgirefvETAL----RISGSWIDYPLEIVEI-GAGEILDDGLRKVTAYPLEHPLE-CYG 147
Cdd:cd07741   71 NVLIEAMTEGGFKKRGTLLAP-------EDALngepVVLLYYHRRKLEEIEIlEEGDEYELGGIKIEATRHKHSDPtTYG 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759 148 YRIEehdkpgalnaqalkaagvppgplfqalkagktimledgrqingadylaapVPGKALAIFGDTGPCDAALDLAKGVD 227
Cdd:cd07741  144 FIFR--------------------------------------------------TSDKKIGYISDTRYFEELIEYYSNCD 173

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 508536759 228 VMVheatLDITMEAKANSRGHSSTRQAATLAREAGVGKLIITH 270
Cdd:cd07741  174 VLI----INVTRPRPRKGVDHLSVEDVEKILKEIKPKLAILTH 212
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 30-153 4.47e-10

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: 57.95  E-value: 4.47e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759    30 TQSGLWLFDCGEGTQHQLLHT--TFNPGKLDKIFISHLHGDHLFGLPGLLCsrsmsgiIQPLTIYGPQGIREFVETALRI 107
Cdd:smart00849   7 DDGGAILIDTGPGEAEDLLAElkKLGPKKIDAIILTHGHPDHIGGLPELLE-------APGAPVYAPEGTAELLKDLLAL 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 508536759   108 SGS---WIDYPLEIVEIGAGEILDDGLRKVTAYPLE-HPLECYGYRIEEH 153
Cdd:smart00849  80 LGElgaEAEPAPPDRTLKDGDELDLGGGELEVIHTPgHTPGSIVLYLPEG 129
TaR3-like_MBL-fold cd07715
MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold ...
 36-234 6.10e-09

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: 55.19  E-value: 6.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759  36 LFDCGEGTQ---HQLLHTTFnPGKLDkIFISHLHGDHLFGLP---GLLCSRSMsgiiqpLTIYGPQGIREFVETALRisg 109
Cdd:cd07715   36 ILDAGTGIRelgNELMKEGP-PGEAH-LLLSHTHWDHIQGFPffaPAYDPGNR------IHIYGPHKDGGSLEEVLR--- 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759 110 SWIDYP------------LEIVEIGAGEILD-DGLRkVTAYPLEHPLECYGYRIEEHdkpgalnaqalkaagvppgplfq 176
Cdd:cd07715  105 RQMSPPyfpvpleellaaIEFHDLEPGEPFSiGGVT-VTTIPLNHPGGALGYRIEED----------------------- 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 508536759 177 alkagktimledgrqingadylaapvpGKALAIFGDT-------GPCDAALDLAKGVDVMVHEAT 234
Cdd:cd07715  161 ---------------------------GKSVVYATDTehypddgESDEALLEFARGADLLIHDAQ 198
class_II_PDE_MBL-fold cd07735
class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium ...
 1-155 1.67e-08

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: 54.52  E-value: 1.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759   1 MELIFLGTSAGVP-TRTrnvTAILLNlqhPTQSGLW-LFDCGEG----TQHQLLHTTFNPG---------KLDKIFISHL 65
Cdd:cd07735    1 FELVVLGCSGGPDeGNT---SSFLLD---PAGSDGDiLLDAGTGvgalSLEEMFNDILFPSqkaayelyqRIRHYLITHA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759  66 HGDHLFGLPglLCSRSMSGII-QPLTIYGPQgireFVETALRIS----------GSWID--YP-LEIVEIGAGEILDDGL 131
Cdd:cd07735   75 HLDHIAGLP--LLSPNDGGQRgSPKTIYGLP----ETIDALKKHifnwviwpdfTSIPSgkYPyLRLEPIEPEYPIALTG 148

                        170       180
                 ....*....|....*....|....*
gi 508536759 132 RKVTAYPLEHP-LECYGYRIEEHDK 155
Cdd:cd07735  149 LSVTAFPVSHGvPVSTAFLIRDGGD 173
PhnP-like_MBL-fold cd07736
phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase ...
 1-155 5.25e-08

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: 51.85  E-value: 5.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759   1 MELIFLGT--SAGVPT---------RTRNVTAIL-----LNLQHptQSGLWLFDCGegtqHQLLHTTFNPGKLDKIFISH 64
Cdd:cd07736    1 MKLTFLGTgdAGGVPVygcdcsacqRARQDPSYRrrpcsALIEV--DGERILLDAG----LTDLAERFPPGSIDAILLTH 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759  65 LHGDHLFGLPGLlcsRsmSGIIQPLTIYGP---QGIREFVETALRISGSWIDYPLEIVEIGageilddGLRkVTAYPLEH 141
Cdd:cd07736   75 FHMDHVQGLFHL---R--WGVGDPIPVYGPpdpQGCADLFKHPGILDFQPLVAPFQSFELG-------GLK-ITPLPLNH 141

                        170
                 ....*....|....
gi 508536759 142 PLECYGYRIEEHDK 155
Cdd:cd07736  142 SKPTFGYLLESGGK 155
RNaseZ_ELAC2-N-term-like_MBL-fold cd16296
Ribonuclease Z, N-terminus of human ELAC2 and related proteins; MBL-fold metallo-hydrolase ...
 35-209 4.85e-07

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: 49.18  E-value: 4.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759  35 WLFDCGEGTQHQLLHTTFNPGKLDKIFISHLHGDHLFGLPGLLCSRSMSGIiqpltiygPQGIrefvetalrISGSWIDY 114
Cdd:cd16296   24 YLFNCGEGVQRLMQEHKLKVARLDNIFLTRMHWSNVGGLSGMILTLKETGL--------PKCV---------LSGPNKQS 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759 115 PLEIVEIGAGEILDDGLrkVTAYPlehpleCygyriEEHDKPGALNAQALKAAGVPPG-----PLFQALKAGKTIMLEdG 189
Cdd:cd16296   87 PDKIGVRRQILERDPSL--VVAFI------C-----KLHLKKGNFLVLKAKELGLPVGtaaiaPIIAAVKDGKSITFE-G 152

                        170       180
                 ....*....|....*....|
gi 508536759 190 RQINGADYLAAPVPGKALAI 209
Cdd:cd16296  153 REILAEELCTPPDPGIVFIV 172
PDE1 COG5212
cAMP phosphodiesterase [Signal transduction mechanisms];
1-154 9.03e-06

cAMP phosphodiesterase [Signal transduction mechanisms];


Pssm-ID: 444071 [Multi-domain]  Cd Length: 300  Bit Score: 46.49  E-value: 9.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759   1 MELIFLGTSAGVptRTRNVTAILLnLQHPTQSGLwLFDCGEGT-------QHQLLHTTFNPG--KLDKIFISHLHGDHLF 71
Cdd:COG5212   12 MEVRVLGCSGGI--SDGNLTTYLL-RPLGSDDYV-LLDAGTVVsglelaeQKGAFKGRQGYVleHIKGYLISHAHLDHIA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759  72 GLPgllcsrSMSGIIQPLTIYGPQGIREFVETALRISGSWID------------YPLEIVEIGAGEILDDGLRKVTAYPL 139
Cdd:COG5212   88 GLP------ILSPDDSPKTIYALPETIDALRNHYFNWVIWPDftdigsaphlpkYRYVPLKPGQTFPLGGTGLRVTAFPL 161

                        170
                 ....*....|....*
gi 508536759 140 EHPLECYGYRIEEHD 154
Cdd:COG5212  162 SHSVPSSAFLIESGG 176
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 36-138 1.37e-05

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: 44.97  E-value: 1.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759  36 LFDCGEGTQHQLL-HTTFNPGKLDKIFISHLHGDHLFGLPGLlcsRSMSGIiqplTIYGPQGIREF----VETALRISGS 110
Cdd:cd06262   24 LIDPGAGALEKILeAIEELGLKIKAILLTHGHFDHIGGLAEL---KEAPGA----PVYIHEADAELledpELNLAFFGGG 96

                         90       100
                 ....*....|....*....|....*...
gi 508536759 111 WIDYPLEIVEIGAGEILDDGLRKVTAYP 138
Cdd:cd06262   97 PLPPPEPDILLEDGDTIELGGLELEVIH 124
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 1-86 4.88e-04

RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 41.33  E-value: 4.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759   1 MELIFLGtsagvptRTRNVT--AILLnlqhPTQSGLWLFDCG---EGTQHQLLHTTFNPGKLDKIFISHLHGDHLFGLPg 75
Cdd:COG1236    1 MKLTFLG-------AAGEVTgsCYLL----ETGGTRILIDCGlfqGGKERNWPPFPFRPSDVDAVVLTHAHLDHSGALP- 68

                         90
                 ....*....|.
gi 508536759  76 LLCSRSMSGII 86
Cdd:COG1236   69 LLVKEGFRGPI 79
PRK02113 PRK02113
MBL fold metallo-hydrolase;
1-76 1.27e-03

MBL fold metallo-hydrolase;


Pssm-ID: 179371 [Multi-domain]  Cd Length: 252  Bit Score: 39.77  E-value: 1.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759   1 MELIFLG--TSAGVPT----------------RTRnvTAILLNlqhpTQSGLWLFDCGEGTQHQLLHTTFnpGKLDKIFI 62
Cdd:PRK02113   1 MKIRILGsgTSTGVPEigctcpvctskdprdnRLR--TSALVE----TEGARILIDCGPDFREQMLRLPF--GKIDAVLI 72

                         90
                 ....*....|....
gi 508536759  63 SHLHGDHLFGLPGL 76
Cdd:PRK02113  73 THEHYDHVGGLDDL 86
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
36-142 2.50e-03

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 38.50  E-value: 2.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759   36 LFDCGEGTQHQLL----HTTFNPGKLDKIFISHLHGDHLFGLPGLLCSRSMSGIIQPLTIY---GPQGIREFVETALRIS 108
Cdd:pfam00753  19 LIDTGGSAEAALLlllaALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARellDEELGLAASRLGLPGP 98

                          90       100       110
                  ....*....|....*....|....*....|....
gi 508536759  109 GSWIDYPLEIVEIGAGEILDDGLRKVTAYPLEHP 142
Cdd:pfam00753  99 PVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGP 132
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 35-97 9.30e-03

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: 37.22  E-value: 9.30e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508536759  35 WLFDCGEGTQhqLLHttfN-------PGKLDKIFISHLHGDHLFGLPGLLcsrsmsGIIQPLTIYGPQGI 97
Cdd:cd07713   32 ILFDTGQSGV--LLH---NakklgidLSDIDAVVLSHGHYDHTGGLKALL------ELNPKAPVYAHPDA 90
 
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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