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Conserved domains on  [gi|119610369|gb|EAW89963|]
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elaC homolog 2 (E. coli), isoform CRA_c [Homo sapiens]

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; ...
 1-217 4.49e-80

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 cd16296:

Pssm-ID: 451500 [Multi-domain]  Cd Length: 175  Bit Score: 247.18  E-value: 4.49e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119610369   1 MQEHKLKVARLDNIFLTRMHWSNVGGLSGMILTLKETGLPKCVLSGPpqlekyleaikifsgplkgielavrphsapeye 80
Cdd:cd16296   36 MQEHKLKVARLDNIFLTRMHWSNVGGLSGMILTLKETGLPKCVLSGP--------------------------------- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119610369  81 detmtvyqipihseqrrgkhqpwqsperplsrlsperssdsesnENEPHLPHGVSQRRGVRDSSLVVAFICKLHLKRGNF 160
Cdd:cd16296   83 --------------------------------------------NKQSPDKIGVRRQILERDPSLVVAFICKLHLKKGNF 118

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 119610369 161 LVLKAKEMGLPVGTAAIAPIIAAVKDGKSITHEGREILAEELCTPPDPGAAFVVVEC 217
Cdd:cd16296  119 LVLKAKELGLPVGTAAIAPIIAAVKDGKSITFEGREILAEELCTPPDPGIVFIVVEC 175
metallo-hydrolase-like_MBL-fold super family cl23716
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 389-458 5.04e-39

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 cd07718:

Pssm-ID: 451500 [Multi-domain]  Cd Length: 204  Bit Score: 140.76  E-value: 5.04e-39
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119610369 389 IIFLGTGSAIPMKIRNVSATLVNISPDTSLLLDCGEGTFGQLCRHYGDQ-VDRVLGTLAAVFVSHLHADHH 458
Cdd:cd07718    1 VVFLGTGSAIPSKYRNVSGILLRIPGDGSILLDCGEGTLGQLRRHYGPEeADEVLRNLKCIFISHLHADHH 71
 
Name Accession Description Interval E-value
RNaseZ_ELAC2-N-term-like_MBL-fold cd16296
Ribonuclease Z, N-terminus of human ELAC2 and related proteins; MBL-fold metallo-hydrolase ...
 1-217 4.49e-80

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: 247.18  E-value: 4.49e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119610369   1 MQEHKLKVARLDNIFLTRMHWSNVGGLSGMILTLKETGLPKCVLSGPpqlekyleaikifsgplkgielavrphsapeye 80
Cdd:cd16296   36 MQEHKLKVARLDNIFLTRMHWSNVGGLSGMILTLKETGLPKCVLSGP--------------------------------- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119610369  81 detmtvyqipihseqrrgkhqpwqsperplsrlsperssdsesnENEPHLPHGVSQRRGVRDSSLVVAFICKLHLKRGNF 160
Cdd:cd16296   83 --------------------------------------------NKQSPDKIGVRRQILERDPSLVVAFICKLHLKKGNF 118

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 119610369 161 LVLKAKEMGLPVGTAAIAPIIAAVKDGKSITHEGREILAEELCTPPDPGAAFVVVEC 217
Cdd:cd16296  119 LVLKAKELGLPVGTAAIAPIIAAVKDGKSITFEGREILAEELCTPPDPGIVFIVVEC 175
RNaseZ_ELAC1_ELAC2-C-term-like_MBL-fold cd07718
Ribonuclease Z ELAC1, C-terminus of ELAC2, and related proteins; MBL-fold metallo-hydrolase ...
 389-458 5.04e-39

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: 140.76  E-value: 5.04e-39
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119610369 389 IIFLGTGSAIPMKIRNVSATLVNISPDTSLLLDCGEGTFGQLCRHYGDQ-VDRVLGTLAAVFVSHLHADHH 458
Cdd:cd07718    1 VVFLGTGSAIPSKYRNVSGILLRIPGDGSILLDCGEGTLGQLRRHYGPEeADEVLRNLKCIFISHLHADHH 71
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
388-457 6.87e-19

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 86.02  E-value: 6.87e-19
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119610369 388 EIIFLGTGSAIPMKIRNVSATLVNIsPDTSLLLDCGEGTFGQLCRHYGDqvdrvLGTLAAVFVSHLHADH 457
Cdd:COG1234    2 KLTFLGTGGAVPTPGRATSSYLLEA-GGERLLIDCGEGTQRQLLRAGLD-----PRDIDAIFITHLHGDH 65
PRK00055 PRK00055
ribonuclease Z; Reviewed
 388-457 3.80e-15

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 75.60  E-value: 3.80e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119610369 388 EIIFLGTGSAIPMKIRNVSATLVNIsPDTSLLLDCGEGTFGQLcRHYG---DQVDRvlgtlaaVFVSHLHADH 457
Cdd:PRK00055   3 ELTFLGTGSGVPTPTRNVSSILLRL-GGELFLFDCGEGTQRQL-LKTGikpRKIDK-------IFITHLHGDH 66
Lactamase_B_4 pfam13691
tRNase Z endonuclease; This is family of tRNase Z enzymes, that are closely related ...
 1-26 6.21e-05

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


Pssm-ID: 404562 [Multi-domain]  Cd Length: 63  Bit Score: 41.04  E-value: 6.21e-05
                          10        20
                  ....*....|....*....|....*..
gi 119610369    1 MQEHKLKVARLDNIFLTRMH-WSNVGG 26
Cdd:pfam13691  37 LNEQKVRLSKLEDIFLTGKVsWSNIGG 63
 
Name Accession Description Interval E-value
RNaseZ_ELAC2-N-term-like_MBL-fold cd16296
Ribonuclease Z, N-terminus of human ELAC2 and related proteins; MBL-fold metallo-hydrolase ...
 1-217 4.49e-80

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: 247.18  E-value: 4.49e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119610369   1 MQEHKLKVARLDNIFLTRMHWSNVGGLSGMILTLKETGLPKCVLSGPpqlekyleaikifsgplkgielavrphsapeye 80
Cdd:cd16296   36 MQEHKLKVARLDNIFLTRMHWSNVGGLSGMILTLKETGLPKCVLSGP--------------------------------- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119610369  81 detmtvyqipihseqrrgkhqpwqsperplsrlsperssdsesnENEPHLPHGVSQRRGVRDSSLVVAFICKLHLKRGNF 160
Cdd:cd16296   83 --------------------------------------------NKQSPDKIGVRRQILERDPSLVVAFICKLHLKKGNF 118

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 119610369 161 LVLKAKEMGLPVGTAAIAPIIAAVKDGKSITHEGREILAEELCTPPDPGAAFVVVEC 217
Cdd:cd16296  119 LVLKAKELGLPVGTAAIAPIIAAVKDGKSITFEGREILAEELCTPPDPGIVFIVVEC 175
RNaseZ_ELAC1_ELAC2-C-term-like_MBL-fold cd07718
Ribonuclease Z ELAC1, C-terminus of ELAC2, and related proteins; MBL-fold metallo-hydrolase ...
 389-458 5.04e-39

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: 140.76  E-value: 5.04e-39
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119610369 389 IIFLGTGSAIPMKIRNVSATLVNISPDTSLLLDCGEGTFGQLCRHYGDQ-VDRVLGTLAAVFVSHLHADHH 458
Cdd:cd07718    1 VVFLGTGSAIPSKYRNVSGILLRIPGDGSILLDCGEGTLGQLRRHYGPEeADEVLRNLKCIFISHLHADHH 71
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
388-457 6.87e-19

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 86.02  E-value: 6.87e-19
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119610369 388 EIIFLGTGSAIPMKIRNVSATLVNIsPDTSLLLDCGEGTFGQLCRHYGDqvdrvLGTLAAVFVSHLHADH 457
Cdd:COG1234    2 KLTFLGTGGAVPTPGRATSSYLLEA-GGERLLIDCGEGTQRQLLRAGLD-----PRDIDAIFITHLHGDH 65
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 389-457 1.47e-18

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: 83.47  E-value: 1.47e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119610369 389 IIFLGTGSAIPMKIRNVSATLVNIsPDTSLLLDCGEGTFGQLCRHYGDqvdrvLGTLAAVFVSHLHADH 457
Cdd:cd16272    1 LTFLGTGGAVPSLTRNTSSYLLET-GGTRILLDCGEGTVYRLLKAGVD-----PDKLDAIFLSHFHLDH 63
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 389-457 1.52e-16

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: 79.03  E-value: 1.52e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119610369 389 IIFLGTGSAIPMKIRNVSATLVNIsPDTSLLLDCGEGTFGQLcRHYGdqvdRVLGTLAAVFVSHLHADH 457
Cdd:cd07717    1 LTFLGTGSAVPTPERNLSSIALRL-EGELWLFDCGEGTQRQL-LRAG----LSPSKIDRIFITHLHGDH 63
PRK00055 PRK00055
ribonuclease Z; Reviewed
 388-457 3.80e-15

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 75.60  E-value: 3.80e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119610369 388 EIIFLGTGSAIPMKIRNVSATLVNIsPDTSLLLDCGEGTFGQLcRHYG---DQVDRvlgtlaaVFVSHLHADH 457
Cdd:PRK00055   3 ELTFLGTGSGVPTPTRNVSSILLRL-GGELFLFDCGEGTQRQL-LKTGikpRKIDK-------IFITHLHGDH 66
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 388-457 1.97e-11

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: 62.92  E-value: 1.97e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119610369 388 EIIFLGTGSAIPMKIRNVSATLVnISPDTSLLLDCGEGTFGQLCrhygdQVDRVLGTLAAVFVSHLHADH 457
Cdd:cd07719    1 RVTLLGTGGPIPDPDRAGPSTLV-VVGGRVYLVDAGSGVVRRLA-----QAGLPLGDLDAVFLTHLHSDH 64
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 1-74 1.11e-10

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: 60.35  E-value: 1.11e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119610369   1 MQEHKLKVARLDNIFLTRMHWSNVGGLSGMILTLKETGLPK-CVLSGPPQLEKYLEAIKIFSGPLKGIELAVRPH 74
Cdd:cd16272   41 LLKAGVDPDKLDAIFLSHFHLDHIGGLPTLLFARRYGGRKKpLTIYGPKGIKEFLEKLLNFPVEILPLGFPLEIE 115
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 413-457 1.41e-09

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


Pssm-ID: 293802 [Multi-domain]  Cd Length: 175  Bit Score: 57.07  E-value: 1.41e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 119610369 413 SPDTSLLLDCGEGTFGQLCRHygdqVDrvLGTLAAVFVSHLHADH 457
Cdd:cd07716   25 ADGFRILLDCGSGVLSRLQRY----ID--PEDLDAVVLSHLHPDH 63
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 388-457 4.50e-07

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 51.05  E-value: 4.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119610369 388 EIIFLGTGSAIPM----------------KIRNVSATLVNiSPDTSLLLDCGEGtfgqlCRHYGDQVDRVLGTLAAVFVS 451
Cdd:COG1235    2 KVTFLGSGSSGGVpqigcdcpvcastdprYGRTRSSILVE-ADGTRLLIDAGPD-----LREQLLRLGLDPSKIDAILLT 75


                 ....*.
gi 119610369 452 HLHADH 457
Cdd:COG1235   76 HEHADH 81
Lactamase_B_4 pfam13691
tRNase Z endonuclease; This is family of tRNase Z enzymes, that are closely related ...
 1-26 6.21e-05

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


Pssm-ID: 404562 [Multi-domain]  Cd Length: 63  Bit Score: 41.04  E-value: 6.21e-05
                          10        20
                  ....*....|....*....|....*..
gi 119610369    1 MQEHKLKVARLDNIFLTRMH-WSNVGG 26
Cdd:pfam13691  37 LNEQKVRLSKLEDIFLTGKVsWSNIGG 63
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 390-457 1.92e-04

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) 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: 42.63  E-value: 1.92e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119610369 390 IFLGTGSAIPMKIRNVSATLVNiSPDTSLLLDCGEGTFGQLCRhYGdqVDRVlgTLAAVFVSHLHADH 457
Cdd:cd07740    1 TFLGSGDAFGSGGRLNTCFHVA-SEAGRFLIDCGASSLIALKR-AG--IDPN--AIDAIFITHLHGDH 62
metallo-hydrolase-like_MBL-fold cd07741
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 389-457 4.61e-04

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) 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: 41.41  E-value: 4.61e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119610369 389 IIFLGTGSAipmkiRNVSATLVNIS-------PDTSLLLDCGEGTFGQLCRHYGDQVDrvlgtLAAVFVSHLHADH 457
Cdd:cd07741    1 IIFLGTGGG-----RFVVITQLRASggiwielNGKNIHIDPGPGALVRMCRPKLDPTK-----LDAIILSHRHLDH 66
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 388-465 3.29e-03

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: 38.61  E-value: 3.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119610369 388 EIIFLGTGSA--IPM---------------KIRNVSAtLVNIsPDTSLLLDCGEgTF-GQLCRHYGDQVDrvlgtlaAVF 449
Cdd:cd16279    2 KLTFLGTGTSsgVPVigcdcgvcdssdpknRRLRSSI-LIET-GGKNILIDTGP-DFrQQALRAGIRKLD-------AVL 71

                         90
                 ....*....|....*..
gi 119610369 450 VSHLHADH-HtvsvGLD 465
Cdd:cd16279   72 LTHAHADHiH----GLD 84
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 389-457 9.94e-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: 9.94e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119610369 389 IIFLG-----TGSAIpmkirnvsatLVNIsPDTSLLLDCGegTF---GQLCRHYGDQVDRVLGTLAAVFVSHLHADH 457
Cdd:cd16295    1 LTFLGaarevTGSCY----------LLET-GGKRILLDCG--LFqggKELEELNNEPFPFDPKEIDAVILTHAHLDH 64
 
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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