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Conserved domains on  [gi|1418783820|gb|RAZ45522|]
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ribonuclease Z [Enterobacter hormaechei subsp. xiangfangensis]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 581040)

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
metallo-hydrolase-like_MBL-fold super family cl23716
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 3-305 0e+00

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.


The actual alignment was detected with superfamily member TIGR02649:

Pssm-ID: 451500  Cd Length: 303  Bit Score: 520.34  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820   3 LIFLGTSAGVPTRSRNVTAILLDLKHPTRGGLWLFDCGEGTQHQLLHTSYHPGKVDKIFITHLHGDHLFGLPGLLCSRSM 82
Cdd:TIGR02649   1 LIFLGTSAGVPTRTRNVTAILLNLQHPTQSGLWLFDCGEGTQHQLLHTAFNPGKLDKIFISHLHGDHLFGLPGLLCSRSM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820  83 AGNANPLTIYGPAGIQEFVETTLRLSGSWTDYPLEVLQIGEGLVFDDGDYLVRAYPLNHPVECYGYRVEEHDKPGALNAA 162
Cdd:TIGR02649  81 SGIIQPLTIYGPQGIREFVETALRISGSWTDYPLEIVEIGAGEILDDGLRKVTAYPLEHPLECYGYRIEEHDKPGALNAQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820 163 ALQADGVKPGPLFQRLKHGETVTLEDGRVINGQDYLAPPQPGKKLAIFGDTAPCSSALRLARGVDVMVHEATLEAAMEEK 242
Cdd:TIGR02649 161 ALKAAGVPPGPLFQELKAGKTITLEDGRQINGADYLAAPVPGKALAIFGDTGPCDAALDLAKGVDVMVHEATLDITMEAK 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1418783820 243 ANSRGHSSTRQAAQLAREAGVRKLIVTHVSSRYDVRGAESLLAECREVFPACELAEDFAQVSV 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: 520.34  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820   3 LIFLGTSAGVPTRSRNVTAILLDLKHPTRGGLWLFDCGEGTQHQLLHTSYHPGKVDKIFITHLHGDHLFGLPGLLCSRSM 82
Cdd:TIGR02649   1 LIFLGTSAGVPTRTRNVTAILLNLQHPTQSGLWLFDCGEGTQHQLLHTAFNPGKLDKIFISHLHGDHLFGLPGLLCSRSM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820  83 AGNANPLTIYGPAGIQEFVETTLRLSGSWTDYPLEVLQIGEGLVFDDGDYLVRAYPLNHPVECYGYRVEEHDKPGALNAA 162
Cdd:TIGR02649  81 SGIIQPLTIYGPQGIREFVETALRISGSWTDYPLEIVEIGAGEILDDGLRKVTAYPLEHPLECYGYRIEEHDKPGALNAQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820 163 ALQADGVKPGPLFQRLKHGETVTLEDGRVINGQDYLAPPQPGKKLAIFGDTAPCSSALRLARGVDVMVHEATLEAAMEEK 242
Cdd:TIGR02649 161 ALKAAGVPPGPLFQELKAGKTITLEDGRQINGADYLAAPVPGKALAIFGDTGPCDAALDLAKGVDVMVHEATLDITMEAK 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1418783820 243 ANSRGHSSTRQAAQLAREAGVRKLIVTHVSSRYDVRGAESLLAECREVFPACELAEDFAQVSV 305
Cdd:TIGR02649 241 ANSRGHSSTRQAATLAREAGVGKLIITHVSSRYDDKGCQHLLRECRSIFPATELANDFTVFNV 303
PRK00055 PRK00055
ribonuclease Z; Reviewed
 1-305 2.17e-144

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 406.87  E-value: 2.17e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820   1 MELIFLGTSAGVPTRSRNVTAILLDLkhptRGGLWLFDCGEGTQHQLLHTSYHPGKVDKIFITHLHGDHLFGLPGLLCSR 80
Cdd:PRK00055    2 MELTFLGTGSGVPTPTRNVSSILLRL----GGELFLFDCGEGTQRQLLKTGIKPRKIDKIFITHLHGDHIFGLPGLLSTR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820  81 SMAGNANPLTIYGPAGIQEFVETTLRLSGSwtdyplevlqigeglvfddgdylvrayplnhpvecYGYRVEEHDKPGALN 160
Cdd:PRK00055   78 SLSGRTEPLTIYGPKGIKEFVETLLRASGS-----------------------------------LGYRIAEKDKPGKLD 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820 161 AAALQADGVKPGPLFQRLKHGETVTLEDGRVINGQDYLAPPQPGKKLAIFGDTAPCSSALRLARGVDVMVHEATLEAAME 240
Cdd:PRK00055  123 AEKLKALGVPPGPLFGKLKRGEDVTLEDGRIINPADVLGPPRKGRKVAYCGDTRPCEALVELAKGADLLVHEATFGDEDE 202

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1418783820 241 EKANSRGHSSTRQAAQLAREAGVRKLIVTHVSSRYDVRgAESLLAECREVFPACELAEDFAQVSV 305
Cdd:PRK00055  203 ELAKEYGHSTARQAAEIAKEAGVKRLILTHFSPRYTGD-PEELLKEAREIFPNTELAEDLMRVEV 266
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 3-304 6.53e-127

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: 361.77  E-value: 6.53e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820   3 LIFLGTSAGVPTRSRNVTAILLDLkhptRGGLWLFDCGEGTQHQLLHTSYHPGKVDKIFITHLHGDHLFGLPGLLCSRSM 82
Cdd:cd07717     1 LTFLGTGSAVPTPERNLSSIALRL----EGELWLFDCGEGTQRQLLRAGLSPSKIDRIFITHLHGDHILGLPGLLSTMSL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820  83 AGNANPLTIYGPAGIQEFVETTLRLSGSWTDYPLEV--LQIGEGLVFDDGDYLVRAYPLNHPVECYGYRVEEhdkpgaln 160
Cdd:cd07717    77 LGRTEPLTIYGPKGLKEFLETLLRLSASRLPYPIEVheLEPDPGLVFEDDGFTVTAFPLDHRVPCFGYRFEE-------- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820 161 aaalqadgvkpgplfqrlkhgetvtledgrvingqdylappqpGKKLAIFGDTAPCSSALRLARGVDVMVHEATLEAAME 240
Cdd:cd07717   149 -------------------------------------------GRKIAYLGDTRPCEGLVELAKGADLLIHEATFLDDDA 185

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1418783820 241 EKANSRGHSSTRQAAQLAREAGVRKLIVTHVSSRYdvRGAESLLAECREVFPACELAEDFAQVS 304
Cdd:cd07717   186 EKAKETGHSTAKQAAEIAKKAGVKKLVLTHFSARY--KDPEELLKEARAVFPNTILAEDFMTIE 247
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
1-305 1.89e-108

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 315.21  E-value: 1.89e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820   1 MELIFLGTSAGVPTRSRNVTAILLDLkhptRGGLWLFDCGEGTQHQLLHTSYHPGKVDKIFITHLHGDHLFGLPGLLCSR 80
Cdd:COG1234     1 MKLTFLGTGGAVPTPGRATSSYLLEA----GGERLLIDCGEGTQRQLLRAGLDPRDIDAIFITHLHGDHIAGLPGLLSTR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820  81 SMAGNANPLTIYGPAGIQEFVETTLRLSGSWTDYPLEVLQIGEGLVFDDGDYLVRAYPLNHPVECYGYRVEEhdkpgaln 160
Cdd:COG1234    77 SLAGREKPLTIYGPPGTKEFLEALLKASGTDLDFPLEFHEIEPGEVFEIGGFTVTAFPLDHPVPAYGYRFEE-------- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820 161 aaalqadgvkpgplfqrlkhgetvtledgrvingqdylappqPGKKLAIFGDTAPCSSALRLARGVDVMVHEATLEAAME 240
Cdd:COG1234   149 ------------------------------------------PGRSLVYSGDTRPCEALVELAKGADLLIHEATFLDEEA 186

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1418783820 241 EKANSRGHSSTRQAAQLAREAGVRKLIVTHVSSRYDvrGAESLLAECREVFPA-CELAEDFAQVSV 305
Cdd:COG1234   187 ELAKETGHSTAKEAAELAAEAGVKRLVLTHFSPRYD--DPEELLAEARAVFPGpVELAEDGMVIEL 250
GntH_guanitoxin NF041257
guanitoxin biosynthesis MBL fold metallo-hydrolase GntH;
1-291 7.78e-24

guanitoxin biosynthesis MBL fold metallo-hydrolase GntH;


Pssm-ID: 469157 [Multi-domain]  Cd Length: 372  Bit Score: 99.70  E-value: 7.78e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820   1 MELIFLGTSAGVPTRSRNVTAILLDLKHPTRGGLwLFDCGEGTQHQLLHTSYHPGKVDKIFITHLHGDHLFGLPGLLCSR 80
Cdd:NF041257   13 MRITFLGSGPPPPRRGQANTSILVELGNGERDKF-FFDIGSGSVANIIALQIPYNLLNKVFITHLHVDHYGDLPYLYPFG 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820  81 SMAGNANPLTIYGPA------GIQEFVEtTLRLSGSW-TDyplevlqigEGLVFDDGDylvrayplnhpvecyGYRVE-- 151
Cdd:NF041257   92 AWSGRWTPLRVWGPSgrtpelGTKHMVE-GMKEMLAWdTD---------AFSGFPIGD---------------GYEIEvn 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820 152 --EHDKPgalNAAALQADGVKpgplfqrLKHGETVTLEDGRVINGQDYlappqPGKKLAIFGDTAPCSSALRLARGVDVM 229
Cdd:NF041257  147 efDFRDE---NGVVYEENGVT-------VRSWPRSHAKDGAVSYRLDW-----NGLSFVFTGDGRPNELTVEYAKGADVF 211

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1418783820 230 VHEAT-LEAAMEEKAN----------SRGHSSTRQAAQLAREAGVRKLIVTHVSsrYDVRGAESLLAECREVF 291
Cdd:NF041257  212 IHECFdTPELLSGKYGvppelarytiDTHHTPPYAAGKVFSLVQPRLAMATHFF--NDPDTVAEILAEIRAHY 282
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 36-270 5.25e-15

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: 71.96  E-value: 5.25e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820  36 LFDCGEGTQHQLLHTSyHPG-----KVDKIFITHLHGDHLFGLPGLLCSRsmagnanPLTIYGPAGIQEFVETTLRLSGS 110
Cdd:pfam12706   4 LIDPGPDLRQQALPAL-QPGrlrddPIDAVLLTHDHYDHLAGLLDLREGR-------PRPLYAPLGVLAHLRRNFPYLFL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820 111 WTDYPLEV--LQIGEGLVFDDGDYLVRAYPLNH---------PVECYGYRVEEhdkpgalnaaalqadgvkpgplfqrlk 179
Cdd:pfam12706  76 LEHYGVRVheIDWGESFTVGDGGLTVTATPARHgsprgldpnPGDTLGFRIEG--------------------------- 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820 180 hgetvtledgrvingqdylappqPGKKLAIFGDTAPCSSALR-LARGVDVMVHEATLEAAMEEKANsrGHSSTRQAAQLA 258
Cdd:pfam12706 129 -----------------------PGKRVYYAGDTGYFPDEIGeRLGGADLLLLDGGAWRDDEMIHM--GHMTPEEAVEAA 183

                         250
                  ....*....|..
gi 1418783820 259 REAGVRKLIVTH 270
Cdd:pfam12706 184 ADLGARRKVLIH 195
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 30-153 2.46e-12

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: 64.11  E-value: 2.46e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820   30 TRGGLWLFDCGEGTQHQLLHT--SYHPGKVDKIFITHLHGDHLFGLPGLLcsrsmagNANPLTIYGPAGIQEFVETTLRL 107
Cdd:smart00849   7 DDGGAILIDTGPGEAEDLLAElkKLGPKKIDAIILTHGHPDHIGGLPELL-------EAPGAPVYAPEGTAELLKDLLAL 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1418783820  108 SGSWTDY-----PLEVLQIGEGLVFDDGDYLVRAYPlNHPVECYGYRVEEH 153
Cdd:smart00849  80 LGELGAEaepapPDRTLKDGDELDLGGGELEVIHTP-GHTPGSIVLYLPEG 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: 520.34  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820   3 LIFLGTSAGVPTRSRNVTAILLDLKHPTRGGLWLFDCGEGTQHQLLHTSYHPGKVDKIFITHLHGDHLFGLPGLLCSRSM 82
Cdd:TIGR02649   1 LIFLGTSAGVPTRTRNVTAILLNLQHPTQSGLWLFDCGEGTQHQLLHTAFNPGKLDKIFISHLHGDHLFGLPGLLCSRSM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820  83 AGNANPLTIYGPAGIQEFVETTLRLSGSWTDYPLEVLQIGEGLVFDDGDYLVRAYPLNHPVECYGYRVEEHDKPGALNAA 162
Cdd:TIGR02649  81 SGIIQPLTIYGPQGIREFVETALRISGSWTDYPLEIVEIGAGEILDDGLRKVTAYPLEHPLECYGYRIEEHDKPGALNAQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820 163 ALQADGVKPGPLFQRLKHGETVTLEDGRVINGQDYLAPPQPGKKLAIFGDTAPCSSALRLARGVDVMVHEATLEAAMEEK 242
Cdd:TIGR02649 161 ALKAAGVPPGPLFQELKAGKTITLEDGRQINGADYLAAPVPGKALAIFGDTGPCDAALDLAKGVDVMVHEATLDITMEAK 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1418783820 243 ANSRGHSSTRQAAQLAREAGVRKLIVTHVSSRYDVRGAESLLAECREVFPACELAEDFAQVSV 305
Cdd:TIGR02649 241 ANSRGHSSTRQAATLAREAGVGKLIITHVSSRYDDKGCQHLLRECRSIFPATELANDFTVFNV 303
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 2-305 1.39e-148

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: 418.93  E-value: 1.39e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820   2 ELIFLGTSAGVPTRSRNVTAILLDLkhptRGGLWLFDCGEGTQHQLLHTSYHPGKVDKIFITHLHGDHLFGLPGLLCSRS 81
Cdd:TIGR02651   1 EITFLGTGGGVPTKERNLPSIALKL----NGELWLFDCGEGTQRQMLRSGISPMKIDRIFITHLHGDHILGLPGLLSTMS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820  82 MAGNANPLTIYGPAGIQEFVETTLRLSGSWTDYPLEVLQIGEG-LVFDDGDYLVRAYPLNHPVECYGYRVEEHDKPGALN 160
Cdd:TIGR02651  77 FQGRKEPLTIYGPPGIKEFIETSLRVSYTYLNYPIKIHEIEEGgLVFEDDGFKVEAFPLDHSIPSLGYRFEEKDRPGKFD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820 161 AAALQADGVKPGPLFQRLKHGETVTLEDGRVINGQDYLAPPQPGKKLAIFGDTAPCSSALRLARGVDVMVHEATLEAAME 240
Cdd:TIGR02651 157 REKAKELGIPPGPLYGKLKRGETVTLIDGRIIDPEDVLGPPRKGRKIAYTGDTRPCEEVIEFAKNADLLIHEATFLDEDK 236

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1418783820 241 EKANSRGHSSTRQAAQLAREAGVRKLIVTHVSSRYDvrGAESLLAECREVFPACELAEDFAQVSV 305
Cdd:TIGR02651 237 KLAKEYGHSTAAQAAEIAKEANVKRLILTHISPRYS--DEEELLEEAKKIFPNTYIAEDFMEIEI 299
PRK00055 PRK00055
ribonuclease Z; Reviewed
 1-305 2.17e-144

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 406.87  E-value: 2.17e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820   1 MELIFLGTSAGVPTRSRNVTAILLDLkhptRGGLWLFDCGEGTQHQLLHTSYHPGKVDKIFITHLHGDHLFGLPGLLCSR 80
Cdd:PRK00055    2 MELTFLGTGSGVPTPTRNVSSILLRL----GGELFLFDCGEGTQRQLLKTGIKPRKIDKIFITHLHGDHIFGLPGLLSTR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820  81 SMAGNANPLTIYGPAGIQEFVETTLRLSGSwtdyplevlqigeglvfddgdylvrayplnhpvecYGYRVEEHDKPGALN 160
Cdd:PRK00055   78 SLSGRTEPLTIYGPKGIKEFVETLLRASGS-----------------------------------LGYRIAEKDKPGKLD 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820 161 AAALQADGVKPGPLFQRLKHGETVTLEDGRVINGQDYLAPPQPGKKLAIFGDTAPCSSALRLARGVDVMVHEATLEAAME 240
Cdd:PRK00055  123 AEKLKALGVPPGPLFGKLKRGEDVTLEDGRIINPADVLGPPRKGRKVAYCGDTRPCEALVELAKGADLLVHEATFGDEDE 202

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1418783820 241 EKANSRGHSSTRQAAQLAREAGVRKLIVTHVSSRYDVRgAESLLAECREVFPACELAEDFAQVSV 305
Cdd:PRK00055  203 ELAKEYGHSTARQAAEIAKEAGVKRLILTHFSPRYTGD-PEELLKEAREIFPNTELAEDLMRVEV 266
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 3-304 6.53e-127

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: 361.77  E-value: 6.53e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820   3 LIFLGTSAGVPTRSRNVTAILLDLkhptRGGLWLFDCGEGTQHQLLHTSYHPGKVDKIFITHLHGDHLFGLPGLLCSRSM 82
Cdd:cd07717     1 LTFLGTGSAVPTPERNLSSIALRL----EGELWLFDCGEGTQRQLLRAGLSPSKIDRIFITHLHGDHILGLPGLLSTMSL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820  83 AGNANPLTIYGPAGIQEFVETTLRLSGSWTDYPLEV--LQIGEGLVFDDGDYLVRAYPLNHPVECYGYRVEEhdkpgaln 160
Cdd:cd07717    77 LGRTEPLTIYGPKGLKEFLETLLRLSASRLPYPIEVheLEPDPGLVFEDDGFTVTAFPLDHRVPCFGYRFEE-------- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820 161 aaalqadgvkpgplfqrlkhgetvtledgrvingqdylappqpGKKLAIFGDTAPCSSALRLARGVDVMVHEATLEAAME 240
Cdd:cd07717   149 -------------------------------------------GRKIAYLGDTRPCEGLVELAKGADLLIHEATFLDDDA 185

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1418783820 241 EKANSRGHSSTRQAAQLAREAGVRKLIVTHVSSRYdvRGAESLLAECREVFPACELAEDFAQVS 304
Cdd:cd07717   186 EKAKETGHSTAKQAAEIAKKAGVKKLVLTHFSARY--KDPEELLKEARAVFPNTILAEDFMTIE 247
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
1-305 1.89e-108

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 315.21  E-value: 1.89e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820   1 MELIFLGTSAGVPTRSRNVTAILLDLkhptRGGLWLFDCGEGTQHQLLHTSYHPGKVDKIFITHLHGDHLFGLPGLLCSR 80
Cdd:COG1234     1 MKLTFLGTGGAVPTPGRATSSYLLEA----GGERLLIDCGEGTQRQLLRAGLDPRDIDAIFITHLHGDHIAGLPGLLSTR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820  81 SMAGNANPLTIYGPAGIQEFVETTLRLSGSWTDYPLEVLQIGEGLVFDDGDYLVRAYPLNHPVECYGYRVEEhdkpgaln 160
Cdd:COG1234    77 SLAGREKPLTIYGPPGTKEFLEALLKASGTDLDFPLEFHEIEPGEVFEIGGFTVTAFPLDHPVPAYGYRFEE-------- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820 161 aaalqadgvkpgplfqrlkhgetvtledgrvingqdylappqPGKKLAIFGDTAPCSSALRLARGVDVMVHEATLEAAME 240
Cdd:COG1234   149 ------------------------------------------PGRSLVYSGDTRPCEALVELAKGADLLIHEATFLDEEA 186

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1418783820 241 EKANSRGHSSTRQAAQLAREAGVRKLIVTHVSSRYDvrGAESLLAECREVFPA-CELAEDFAQVSV 305
Cdd:COG1234   187 ELAKETGHSTAKEAAELAAEAGVKRLVLTHFSPRYD--DPEELLAEARAVFPGpVELAEDGMVIEL 250
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 3-233 4.50e-56

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: 179.38  E-value: 4.50e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820   3 LIFLGTSAGVPTRSRNVTAILLDlkhpTRGGLWLFDCGEGTQHQLLHTSYHPGKVDKIFITHLHGDHLFGLPGLLCSRSM 82
Cdd:cd16272     1 LTFLGTGGAVPSLTRNTSSYLLE----TGGTRILLDCGEGTVYRLLKAGVDPDKLDAIFLSHFHLDHIGGLPTLLFARRY 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820  83 AGNANPLTIYGPAGIQEFVETTLR--LSGSWTDYPLEVLQIGE-GLVFDDGDYLVRAYPLNHPVECYGYRVEEHdkpgal 159
Cdd:cd16272    77 GGRKKPLTIYGPKGIKEFLEKLLNfpVEILPLGFPLEIEELEEgGEVLELGDLKVEAFPVKHSVESLGYRIEAE------ 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1418783820 160 naaalqadgvkpgplfqrlkhgetvtledgrvingqdylappqpGKKLAIFGDTAPCSSALRLARGVDVMVHEA 233
Cdd:cd16272   151 --------------------------------------------GKSIVYSGDTGPCENLVELAKGADLLIHEC 180
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 2-231 2.96e-33

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: 120.70  E-value: 2.96e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820   2 ELIFLGTSAGVPTRSRNVTAILLDLKhptrGGLWLFDCGEGTQHQLLHTSYHPGKVDKIFITHLHGDHLFGLPGLLCSRS 81
Cdd:cd07719     1 RVTLLGTGGPIPDPDRAGPSTLVVVG----GRVYLVDAGSGVVRRLAQAGLPLGDLDAVFLTHLHSDHVADLPALLLTAW 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820  82 MAGNANPLTIYGPAGIQEFVETTLRLSGSWTDYP--------------LEVLQIGEG-LVFDDGDYLVRAYPLNHPV--E 144
Cdd:cd07719    77 LAGRKTPLPVYGPPGTRALVDGLLAAYALDIDYRarigdegrpdpgalVEVHEIAAGgVVYEDDGVKVTAFLVDHGPvpP 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820 145 CYGYRVeehdkpgalnaaalqadgvkpgplfqrlkhgetvtledgrvingqDYlappqPGKKLAIFGDTAPCSSALRLAR 224
Cdd:cd07719   157 ALAYRF---------------------------------------------DT-----PGRSVVFSGDTGPSENLIELAK 186


                  ....*..
gi 1418783820 225 GVDVMVH 231
Cdd:cd07719   187 GADLLVH 193
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 1-305 3.91e-33

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 122.31  E-value: 3.91e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820   1 MELIFLGT--SAGVP--------------TRSRNVTAILLDlkhpTRGGLWLFDCGEGTQHQLLHTSYHPGKVDKIFITH 64
Cdd:COG1235     1 MKVTFLGSgsSGGVPqigcdcpvcastdpRYGRTRSSILVE----ADGTRLLIDAGPDLREQLLRLGLDPSKIDAILLTH 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820  65 LHGDHLFGLPGLlcsrSMAGNANPLTIYGPAGIQEFVETTLRLSGSWTDYPLEVLQIGEGLVFDDGDYLVRAYPLNHP-V 143
Cdd:COG1235    77 EHADHIAGLDDL----RPRYGPNPIPVYATPGTLEALERRFPYLFAPYPGKLEFHEIEPGEPFEIGGLTVTPFPVPHDaG 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820 144 ECYGYRVEEhdkpgalnaaalqadgvkpgplfqrlkhgetvtledgrvingqdylappqPGKKLAIFGDTAPCSSALR-L 222
Cdd:COG1235   153 DPVGYRIED--------------------------------------------------GGKKLAYATDTGYIPEEVLeL 182

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820 223 ARGVDVMVHEATLEAAMEekansrGHSSTRQAAQLAREAGVRKLIVTHVSSRYDVRGAESLLAECREVFPACELAEDFAQ 302
Cdd:COG1235   183 LRGADLLILDATYDDPEP------GHLSNEEALELLARLGPKRLVLTHLSPDNNDHELDYDELEAALLPAGVEVAYDGME 256


                  ...
gi 1418783820 303 VSV 305
Cdd:COG1235   257 IEL 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 3.20e-31

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: 115.72  E-value: 3.20e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820   3 LIFLGTSAGVPTRSRNVTAILLDLkhPTRGGLwLFDCGEGTQHQLLHTsYHPGKVDK-------IFITHLHGDHLFGLPG 75
Cdd:cd07718     1 VVFLGTGSAIPSKYRNVSGILLRI--PGDGSI-LLDCGEGTLGQLRRH-YGPEEADEvlrnlkcIFISHLHADHHLGLIR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820  76 LLCSRSMA--GNANPLTIYGPAGIQEFvettLRLSGSwtdyplevlqigeglVFDDGDYLVRAYPLnhpVECYGYRVEEH 153
Cdd:cd07718    77 LLAERKKLfkPPSPPLYVVAPRQLRRW----LREYSS---------------LEDLGLHDISFISN---RVSQSLPESDD 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820 154 DKPGALNAAALQADGVKpgplfqRLK----------HGETVTLEDgrvingqdylappqpGKKLAIFGDTAPCSSALRLA 223
Cdd:cd07718   135 PLSRDLLSNLLEELGLK------SIEtvpvihcpdaYGIVLTHED---------------GWKIVYSGDTRPCEALVEAG 193

                         250
                  ....*....|.
gi 1418783820 224 RGVDVMVHEAT 234
Cdd:cd07718   194 KGADLLIHEAT 204
PRK02126 PRK02126
ribonuclease Z; Provisional
 36-293 3.94e-31

ribonuclease Z; Provisional


Pssm-ID: 235006 [Multi-domain]  Cd Length: 334  Bit Score: 118.86  E-value: 3.94e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820  36 LFDCGEGTQ---HQLLhtsyhpgKVDKIFITHLHGDHLFGLPGLLcsRSMAGNANPLTIYGPAGIQEFVETtlRLSG--- 109
Cdd:PRK02126   31 LFDLGDLHHlppRELL-------RISHIFVSHTHMDHFIGFDRLL--RHCLGRPRRLRLFGPPGFADQVEH--KLAGytw 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820 110 -----SWTDYPLEVLQIGE--------------------------GLVFDDGDYLVRAYPLNHPVECYGYRVEEHDKPgA 158
Cdd:PRK02126  100 nlvenYPTTFRVHEVELHDgrirralfscrrafareaeeelslpdGVLLDEPWFRVRAAFLDHGIPCLAFALEEKAHI-N 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820 159 LNAAALQADGVKPGPLFQRLKHG-ETVTLEDGRVI-----NGQDYLAPP------------QPGKKLAIFGDTAP----C 216
Cdd:PRK02126  179 IDKNRLAELGLPPGPWLRELKHAvLRGEPDDTPIRvlwrdGGGEHERVRplgelkervlriEPGQKIGYVTDIGYteenL 258

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1418783820 217 SSALRLARGVDVMVHEATLEAAMEEKANSRGHSSTRQAAQLAREAGVRKLIVTHVSSRYDVRGAEsLLAECREVFPA 293
Cdd:PRK02126  259 ARIVELAAGVDLLFIEAVFLDEDAEKARRKNHLTARQAGRLAREAGVKRLLPFHFSPRYQGRGAE-LYREARAAFAG 334
GntH_guanitoxin NF041257
guanitoxin biosynthesis MBL fold metallo-hydrolase GntH;
1-291 7.78e-24

guanitoxin biosynthesis MBL fold metallo-hydrolase GntH;


Pssm-ID: 469157 [Multi-domain]  Cd Length: 372  Bit Score: 99.70  E-value: 7.78e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820   1 MELIFLGTSAGVPTRSRNVTAILLDLKHPTRGGLwLFDCGEGTQHQLLHTSYHPGKVDKIFITHLHGDHLFGLPGLLCSR 80
Cdd:NF041257   13 MRITFLGSGPPPPRRGQANTSILVELGNGERDKF-FFDIGSGSVANIIALQIPYNLLNKVFITHLHVDHYGDLPYLYPFG 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820  81 SMAGNANPLTIYGPA------GIQEFVEtTLRLSGSW-TDyplevlqigEGLVFDDGDylvrayplnhpvecyGYRVE-- 151
Cdd:NF041257   92 AWSGRWTPLRVWGPSgrtpelGTKHMVE-GMKEMLAWdTD---------AFSGFPIGD---------------GYEIEvn 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820 152 --EHDKPgalNAAALQADGVKpgplfqrLKHGETVTLEDGRVINGQDYlappqPGKKLAIFGDTAPCSSALRLARGVDVM 229
Cdd:NF041257  147 efDFRDE---NGVVYEENGVT-------VRSWPRSHAKDGAVSYRLDW-----NGLSFVFTGDGRPNELTVEYAKGADVF 211

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1418783820 230 VHEAT-LEAAMEEKAN----------SRGHSSTRQAAQLAREAGVRKLIVTHVSsrYDVRGAESLLAECREVF 291
Cdd:NF041257  212 IHECFdTPELLSGKYGvppelarytiDTHHTPPYAAGKVFSLVQPRLAMATHFF--NDPDTVAEILAEIRAHY 282
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 4-233 6.19e-22

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: 90.78  E-value: 6.19e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820   4 IFLGTSAGVPTRSRNVTAILLDlkhpTRGGLWLFDCGEGTQHQLLHTSYHPGKVDKIFITHLHGDHLFGLPGLLCS-RSM 82
Cdd:cd07740     1 TFLGSGDAFGSGGRLNTCFHVA----SEAGRFLIDCGASSLIALKRAGIDPNAIDAIFITHLHGDHFGGLPFFLLDaQFV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820  83 AGNANPLTIYGPAGIQEFVETTLRLS---GSWTDY--PLEVLQIGEGLVFDDGDYLVRAYPLNHPVECygyrveehdkpg 157
Cdd:cd07740    77 AKRTRPLTIAGPPGLRERLRRAMEALfpgSSKVPRrfDLEVIELEPGEPTTLGGVTVTAFPVVHPSGA------------ 144

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1418783820 158 alnaaalqadgvkpGPLFQRLkhgetvtLEDGRVingqdylappqpgkkLAIFGDTAPCSSALRLARGVDVMVHEA 233
Cdd:cd07740   145 --------------LPLALRL-------EAAGRV---------------LAYSGDTEWTDALVPLARGADLFICEC 184
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 36-233 2.85e-20

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: 85.96  E-value: 2.85e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820  36 LFDCGEGTQHQLL-HTsyHPGKVDKIFITHLHGDHLFGLPGLLCSRSMA---GNANPLTIYGPAGIQEFVETTLRLSGSw 111
Cdd:cd07716    31 LLDCGSGVLSRLQrYI--DPEDLDAVVLSHLHPDHCADLGVLQYARRYHprgARKPPLPLYGPAGPAERLAALYGLEDV- 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820 112 tdypLEVLQIGEGLVFDDGDYLVRAYPLNHPVECYGYRVEEhdkpgalnaaalqadgvkpgplfqrlkhgetvtledgrv 191
Cdd:cd07716   108 ----FDFHPIEPGEPLEIGPFTITFFRTVHPVPCYAMRIED--------------------------------------- 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1418783820 192 ingqdylappqPGKKLAIFGDTAPCSSALRLARGVDVMVHEA 233
Cdd:cd07716   145 -----------GGKVLVYTGDTGYCDELVEFARGADLLLCEA 175
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 36-270 5.25e-15

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: 71.96  E-value: 5.25e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820  36 LFDCGEGTQHQLLHTSyHPG-----KVDKIFITHLHGDHLFGLPGLLCSRsmagnanPLTIYGPAGIQEFVETTLRLSGS 110
Cdd:pfam12706   4 LIDPGPDLRQQALPAL-QPGrlrddPIDAVLLTHDHYDHLAGLLDLREGR-------PRPLYAPLGVLAHLRRNFPYLFL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820 111 WTDYPLEV--LQIGEGLVFDDGDYLVRAYPLNH---------PVECYGYRVEEhdkpgalnaaalqadgvkpgplfqrlk 179
Cdd:pfam12706  76 LEHYGVRVheIDWGESFTVGDGGLTVTATPARHgsprgldpnPGDTLGFRIEG--------------------------- 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820 180 hgetvtledgrvingqdylappqPGKKLAIFGDTAPCSSALR-LARGVDVMVHEATLEAAMEEKANsrGHSSTRQAAQLA 258
Cdd:pfam12706 129 -----------------------PGKRVYYAGDTGYFPDEIGeRLGGADLLLLDGGAWRDDEMIHM--GHMTPEEAVEAA 183

                         250
                  ....*....|..
gi 1418783820 259 REAGVRKLIVTH 270
Cdd:pfam12706 184 ADLGARRKVLIH 195
TaR3-like_MBL-fold cd07715
MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold ...
 36-155 3.70e-13

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: 67.14  E-value: 3.70e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820  36 LFDCGEGTQ---HQLLHtSYHPGKVDkIFITHLHGDHLFGLP---GLLCSRsmagnaNPLTIYGPAGIQEFVETTLR--L 107
Cdd:cd07715    36 ILDAGTGIRelgNELMK-EGPPGEAH-LLLSHTHWDHIQGFPffaPAYDPG------NRIHIYGPHKDGGSLEEVLRrqM 107

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1418783820 108 SGSWtdYPLEVLQIGEGLVFDD---------GDYLVRAYPLNHPVECYGYRVEEHDK 155
Cdd:cd07715   108 SPPY--FPVPLEELLAAIEFHDlepgepfsiGGVTVTTIPLNHPGGALGYRIEEDGK 162
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 30-153 2.46e-12

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: 64.11  E-value: 2.46e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820   30 TRGGLWLFDCGEGTQHQLLHT--SYHPGKVDKIFITHLHGDHLFGLPGLLcsrsmagNANPLTIYGPAGIQEFVETTLRL 107
Cdd:smart00849   7 DDGGAILIDTGPGEAEDLLAElkKLGPKKIDAIILTHGHPDHIGGLPELL-------EAPGAPVYAPEGTAELLKDLLAL 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1418783820  108 SGSWTDY-----PLEVLQIGEGLVFDDGDYLVRAYPlNHPVECYGYRVEEH 153
Cdd:smart00849  80 LGELGAEaepapPDRTLKDGDELDLGGGELEVIHTP-GHTPGSIVLYLPEG 129
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 1-151 2.77e-11

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


Pssm-ID: 293837 [Multi-domain]  Cd Length: 193  Bit Score: 61.34  E-value: 2.77e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820   1 MELIFLGT--SAGVPT----------------RSRnvTAILLDlkhpTRGGLWLFDCGEGTQHQLLhtSYHPGKVDKIFI 62
Cdd:cd16279     1 MKLTFLGTgtSSGVPVigcdcgvcdssdpknrRLR--SSILIE----TGGKNILIDTGPDFRQQAL--RAGIRKLDAVLL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820  63 THLHGDHLFGLPGL--LCSRsmagNANPLTIYGPAGIQEFVETTLRLSGSWTDYP----LEVLQIGEGLVFDDGDYLVRA 136
Cdd:cd16279    73 THAHADHIHGLDDLrpFNRL----QQRPIPVYASEETLDDLKRRFPYFFAATGGGgvpkLDLHIIEPDEPFTIGGLEITP 148

                         170
                  ....*....|....*.
gi 1418783820 137 YPLNH-PVECYGYRVE 151
Cdd:cd16279   149 LPVLHgKLPSLGFRFG 164
class_II_PDE_MBL-fold cd07735
class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium ...
 1-155 1.08e-10

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: 60.69  E-value: 1.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820   1 MELIFLGTSAGVPtrSRNVTAILLdlKHPTRGGLWLFDCGEGTQHQLLHTSYHPG-------------KVDKIFITHLHG 67
Cdd:cd07735     1 FELVVLGCSGGPD--EGNTSSFLL--DPAGSDGDILLDAGTGVGALSLEEMFNDIlfpsqkaayelyqRIRHYLITHAHL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820  68 DHLFGLPglLCSRSMAGNAN-PLTIYGPAgiqefvETTLRLS------------GSWTD--YPLEVLQ-IGEGLVFDDGD 131
Cdd:cd07735    77 DHIAGLP--LLSPNDGGQRGsPKTIYGLP------ETIDALKkhifnwviwpdfTSIPSgkYPYLRLEpIEPEYPIALTG 148

                         170       180
                  ....*....|....*....|....*
gi 1418783820 132 YLVRAYPLNHPV-ECYGYRVEEHDK 155
Cdd:cd07735   149 LSVTAFPVSHGVpVSTAFLIRDGGD 173
metallo-hydrolase-like_MBL-fold cd07741
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 3-270 4.47e-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: 58.36  E-value: 4.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820   3 LIFLGTSAGvptrsRNVTAilldlkHPTR--GGLWL--------FDCGEGTQHQLLHTSYHPGKVDKIFITHLHGDHLFG 72
Cdd:cd07741     1 IIFLGTGGG-----RFVVI------TQLRasGGIWIelngknihIDPGPGALVRMCRPKLDPTKLDAIILSHRHLDHSND 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820  73 LPGLLCSRSMAGNANPLTIYGPagiQEFVETTLRLSGSWT-DYPLEVLQIGEGLVFDDGDYLVRAYPLNHPVE-CYGYRV 150
Cdd:cd07741    70 ANVLIEAMTEGGFKKRGTLLAP---EDALNGEPVVLLYYHrRKLEEIEILEEGDEYELGGIKIEATRHKHSDPtTYGFIF 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820 151 EEhdkpgalnaaalqadgvkpgplfqrlkhgetvtledgrvingqdylappqPGKKLAIFGDTAPCSSALRLARGVDVMV 230
Cdd:cd07741   147 RT--------------------------------------------------SDKKIGYISDTRYFEELIEYYSNCDVLI 176

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1418783820 231 HEATLeaamEEKANSRGHSSTRQAAQLAREAGVRKLIVTH 270
Cdd:cd07741   177 INVTR----PRPRKGVDHLSVEDVEKILKEIKPKLAILTH 212
PDE1 COG5212
cAMP phosphodiesterase [Signal transduction mechanisms];
1-154 2.67e-09

cAMP phosphodiesterase [Signal transduction mechanisms];


Pssm-ID: 444071 [Multi-domain]  Cd Length: 300  Bit Score: 57.28  E-value: 2.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820   1 MELIFLGTSAGVptRSRNVTAILLdLKHPTRGGLwLFDCGEGT-------QHQLLHTS--YHPGKVDKIFITHLHGDHLF 71
Cdd:COG5212    12 MEVRVLGCSGGI--SDGNLTTYLL-RPLGSDDYV-LLDAGTVVsglelaeQKGAFKGRqgYVLEHIKGYLISHAHLDHIA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820  72 GLPgllcsrSMAGNANPLTIYGPAgiqeFVETTLRLS----GSWTD------------YPLEVLQIGEGLVFDDGDYLVR 135
Cdd:COG5212    88 GLP------ILSPDDSPKTIYALP----ETIDALRNHyfnwVIWPDftdigsaphlpkYRYVPLKPGQTFPLGGTGLRVT 157

                         170
                  ....*....|....*....
gi 1418783820 136 AYPLNHPVECYGYRVEEHD 154
Cdd:COG5212   158 AFPLSHSVPSSAFLIESGG 176
PhnP-like_MBL-fold cd07736
phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase ...
 1-155 6.29e-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: 6.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820   1 MELIFLGT--SAGVPT---------RSRNVTAI-------LLDLKhptrGGLWLFDCGegtqHQLLHTSYHPGKVDKIFI 62
Cdd:cd07736     1 MKLTFLGTgdAGGVPVygcdcsacqRARQDPSYrrrpcsaLIEVD----GERILLDAG----LTDLAERFPPGSIDAILL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820  63 THLHGDHLFGLPGLlcsRsmAGNANPLTIYGPA------------GIQEFVETTlrlsgswtdYPLEVLQIgeglvfddG 130
Cdd:cd07736    73 THFHMDHVQGLFHL---R--WGVGDPIPVYGPPdpqgcadlfkhpGILDFQPLV---------APFQSFEL--------G 130

                         170       180
                  ....*....|....*....|....*
gi 1418783820 131 DYLVRAYPLNHPVECYGYRVEEHDK 155
Cdd:cd07736   131 GLKITPLPLNHSKPTFGYLLESGGK 155
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 32-131 3.15e-06

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


Pssm-ID: 293792 [Multi-domain]  Cd Length: 188  Bit Score: 46.90  E-value: 3.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820  32 GGLWLFDCGEGTQHQLL-HTSYHPGKVDKIFITHLHGDHLFGLPGLLcsrsmagNANPLTIYGPAGIQEFVETTLRLSGS 110
Cdd:cd06262    20 GEAILIDPGAGALEKILeAIEELGLKIKAILLTHGHFDHIGGLAELK-------EAPGAPVYIHEADAELLEDPELNLAF 92

                          90       100
                  ....*....|....*....|.
gi 1418783820 111 WTDYPLEVLQIGEglVFDDGD 131
Cdd:cd06262    93 FGGGPLPPPEPDI--LLEDGD 111
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 18-73 8.81e-06

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: 46.00  E-value: 8.81e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1418783820  18 NVTAILLDlkhpTRGGLWLFDCGEGTQHQ----LLHTS-----YHPGKVDKIFITHLHGDHLFGL 73
Cdd:cd07720    48 SVNAFLVR----TGGRLILVDTGAGGLFGptagKLLANlaaagIDPEDIDDVLLTHLHPDHIGGL 108
RNaseZ_ELAC2-N-term-like_MBL-fold cd16296
Ribonuclease Z, N-terminus of human ELAC2 and related proteins; MBL-fold metallo-hydrolase ...
 35-204 3.67e-05

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: 43.41  E-value: 3.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820  35 WLFDCGEGTQHQLLHTSYHPGKVDKIFITHLHGDHLFGLPGLLCSRSMAGnaNPLTIYGPAGIQEFVETTLRLSGSWTDY 114
Cdd:cd16296    24 YLFNCGEGVQRLMQEHKLKVARLDNIFLTRMHWSNVGGLSGMILTLKETG--LPKCVLSGPNKQSPDKIGVRRQILERDP 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820 115 PLEVLQIGEgLVFDDGDYLV-RAYPLNHPVecygyrveehdkpgalNAAALqadgvkpGPLFQRLKHGETVTLEdGRVIN 193
Cdd:cd16296   102 SLVVAFICK-LHLKKGNFLVlKAKELGLPV----------------GTAAI-------APIIAAVKDGKSITFE-GREIL 156

                         170
                  ....*....|.
gi 1418783820 194 GQDYLAPPQPG 204
Cdd:cd16296   157 AEELCTPPDPG 167
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 1-76 1.48e-04

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 42.87  E-value: 1.48e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1418783820   1 MELIFLGtSAGVPTRSrnvtAILLdlkhPTRGGLWLFDCG---EGTQHQLLHTSYHPGKVDKIFITHLHGDHLFGLPGL 76
Cdd:COG1236     1 MKLTFLG-AAGEVTGS----CYLL----ETGGTRILIDCGlfqGGKERNWPPFPFRPSDVDAVVLTHAHLDHSGALPLL 70
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
36-77 1.69e-04

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 41.97  E-value: 1.69e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1418783820  36 LFDCGEGTQHQLL----HTSYHPGKVDKIFITHLHGDHLFGLPGLL 77
Cdd:pfam00753  19 LIDTGGSAEAALLlllaALGLGPKDIDAVILTHGHFDHIGGLGELA 64
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 55-142 1.38e-03

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 39.13  E-value: 1.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820  55 GKVDKIFITHLHGDHlFGLPGLlcsRSMAgnANPLTIYGPAGIQEFVEttlrlsgSWTDYPLEVLQIGEGLVFDDGDylV 134
Cdd:COG2220    47 PKIDAVLVTHDHYDH-LDDATL---RALK--RTGATVVAPLGVAAWLR-------AWGFPRVTELDWGESVELGGLT--V 111


                  ....*...
gi 1418783820 135 RAYPLNHP 142
Cdd:COG2220   112 TAVPARHS 119
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 36-155 1.39e-03

uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold metallo hydrolase domain; Includes the uncharacterized Bacillus subtilis YycJ protein. 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: 293819 [Multi-domain]  Cd Length: 151  Bit Score: 38.40  E-value: 1.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820  36 LFDCGEG---TQHQLLHTSYHPGKVDKIFITHLHGDHLFGLpGLLcSRSMAgnanpLTIYGPAGIQEFVETTLRLSGSWT 112
Cdd:cd07733    22 LIDAGLSgrkITGRLAEIGRDPEDIDAILVTHEHADHIKGL-GVL-ARKYN-----VPIYATAGTLRAMERKVGLIDVDQ 94

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1418783820 113 DYPLEVlqigeGLVFDDGDYLVRAYPLNH-PVECYGYRVEEHDK 155
Cdd:cd07733    95 KQIFEP-----GETFSIGDFDVESFGVSHdAADPVGYRFEEGGR 133
PRK02113 PRK02113
MBL fold metallo-hydrolase;
1-76 1.49e-03

MBL fold metallo-hydrolase;


Pssm-ID: 179371 [Multi-domain]  Cd Length: 252  Bit Score: 39.38  E-value: 1.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820   1 MELIFLG--TSAGVPT--------RS------RNVTAILLDlkhpTRGGLWLFDCGEGTQHQLLHTSYhpGKVDKIFITH 64
Cdd:PRK02113    1 MKIRILGsgTSTGVPEigctcpvcTSkdprdnRLRTSALVE----TEGARILIDCGPDFREQMLRLPF--GKIDAVLITH 74

                          90
                  ....*....|..
gi 1418783820  65 LHGDHLFGLPGL 76
Cdd:PRK02113   75 EHYDHVGGLDDL 86
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 30-139 1.81e-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: 38.90  E-value: 1.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820  30 TRGGLWLFDCGEGTQH-----QLLHTsyHPGKVDKIFITHLHGDHLFGLPGLLcsrsmagNANPLTIYGPAGIQEFVETT 104
Cdd:COG0491    22 GGDGAVLIDTGLGPADaeallAALAA--LGLDIKAVLLTHLHPDHVGGLAALA-------EAFGAPVYAHAAEAEALEAP 92

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1418783820 105 LRLSGSWTDYPLEVLQIGEGLVFDDGDYLVRAYPL 139
Cdd:COG0491    93 AAGALFGREPVPPDRTLEDGDTLELGGPGLEVIHT 127
DdPDE5-like_MBL-fold cd07738
Dictyostelium discoideum phosphodiesterase 5 and related proteins; MBL-fold metallo hydrolase ...
 5-155 3.78e-03

Dictyostelium discoideum phosphodiesterase 5 and related proteins; MBL-fold metallo hydrolase domain; Includes Dictyostelium discoideum cAMP/cGMP-dependent 3',5'-cAMP/cGMP phosphodiesterase A (also known as cyclic GMP-binding protein A, phosphodiesterase 5, phosphodiesterase D, and PDE5) and cAMP/cGMP-dependent 3',5'-cAMP/cGMP phosphodiesterase B (also known as cyclic GMP-binding protein B, phosphodiesterase 6, phosphodiesterase E, and PDE6. 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: 293824  Cd Length: 189  Bit Score: 37.66  E-value: 3.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820   5 FLGTSAGVpTRSRNVTAILLDLKHptRGglWLFDCGEGTQHQLLHTSYHPGKVDKIFITHLHGDHLFGLPGLLCSRsmag 84
Cdd:cd07738     2 FLGVSHGF-DPKGHTSGFIIWING--RG--IMVDPPVNSTSYLRQNGISPRLVDHVILTHCHADHDAGTFQKILEE---- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820  85 naNPLTIYGPAGIQefvETTLRLSGSWTDYPLEVLQ---------IGEGLVFDDG----DYLVrayplnHPVECYGYRVE 151
Cdd:cd07738    73 --EKITLYTTRTIN---ESFLRKYAALTGLPPDFLEelfdfrpviIGEKTKINGAefefDYSF------HSIPTIRFKVS 141


                  ....
gi 1418783820 152 EHDK 155
Cdd:cd07738   142 YGGK 145
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 3-84 5.04e-03

Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; MBL-fold metallo-hydrolase domain; Includes the archaeal cleavage and polyadenylation specificity factors (CPSFs) such as Methanothermobacter thermautotrophicus MTH1203, and Pyrococcus horikoshii PH1404. In addition to the MBL-fold metallo-hydrolase nuclease and the beta-CASP domains, members of this subgroup contain two contiguous KH domains. 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: 293853 [Multi-domain]  Cd Length: 197  Bit Score: 37.44  E-value: 5.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418783820   3 LIFLGtSAGVPTRSrnvtAILLDlkhpTRGGLWLFDCG------EGTQHQLLHTSYHPGKVDKIFITHLHGDHLFGLPgL 76
Cdd:cd16295     1 LTFLG-AAREVTGS----CYLLE----TGGKRILLDCGlfqggkELEELNNEPFPFDPKEIDAVILTHAHLDHSGRLP-L 70


                  ....*...
gi 1418783820  77 LCSRSMAG 84
Cdd:cd16295    71 LVKEGFRG 78
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 26-73 5.95e-03

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) 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: 37.63  E-value: 5.95e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1418783820  26 LKHPTrGGLWLFDCG--------------------------EGTQHQLLHTSYHPGKVDKIFITHLHGDHLFGL 73
Cdd:cd07730    28 IEHPT-GGKILFDLGyrkdfeeytprvperlyrtpvpleveEDVAEQLAAGGIDPEDIDAVILSHLHWDHIGGL 100
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 53-83 7.41e-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: 7.41e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1418783820  53 HPGKVDKIFITHLHGDHlFGLPGLLCSRSMA 83
Cdd:cd07725    52 KPSDIDRVLLTHHHPDH-IGLAGKLQEKSGA 81
metallo-hydrolase-like_MBL-fold cd07739
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 60-77 8.36e-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: 36.71  E-value: 8.36e-03
                          10
                  ....*....|....*...
gi 1418783820  60 IFITHLHGDHLFGLPGLL 77
Cdd:cd07739    56 IYITHGHPDHYFGLEVLL 73
 
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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