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Conserved domains on  [gi|1936509518|ref|NP_758829|]
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zinc phosphodiesterase ELAC protein 2 [Rattus norvegicus]

Protein Classification

ribonuclease Z family protein( domain architecture ID 11039737)

ribonuclease Z family protein such as the tRNA maturase RNase Z (also known as tRNase Z or 3' tRNase), which 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;

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RNaseZ_ELAC1_ELAC2-C-term-like_MBL-fold cd07718
Ribonuclease Z ELAC1, C-terminus of ELAC2, and related proteins; MBL-fold metallo-hydrolase ...
 482-687 2.83e-103

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: 317.18  E-value: 2.83e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509518 482 IVFLGTGSAIPMKIRNVSSTLVNLSPDKSVLLDCGEGTFGQLCRHYGQQ-IDRVLCNLTAVFVSHLHADHHTGLLNILLQ 560
Cdd:cd07718     1 VVFLGTGSAIPSKYRNVSGILLRIPGDGSILLDCGEGTLGQLRRHYGPEeADEVLRNLKCIFISHLHADHHLGLIRLLAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509518 561 REHALAslgKPFQPLLVVAPTQLRAWLQQYHNQCQEILHHISMIPAKCLQKGAEVPSPPVERLISLLLETCDLQEFQTCL 640
Cdd:cd07718    81 RKKLFK---PPSPPLYVVAPRQLRRWLREYSSLEDLGLHDISFISNRVSQSLPESDDPLSRDLLSNLLEELGLKSIETVP 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1936509518 641 VRHCKHAFGCALVHSSGWKVVYSGDTMPCEALVQMGKDATLLIHEAT 687
Cdd:cd07718   158 VIHCPDAYGIVLTHEDGWKIVYSGDTRPCEALVEAGKGADLLIHEAT 204
metallo-hydrolase-like_MBL-fold super family cl23716
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 54-310 5.94e-98

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: 302.26  E-value: 5.94e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509518  54 LQVVAAGGRDAGAALYVFSEYNRYLFNCGEGVQRLMQEHKLKVARLDNIFLTRMHWSNVGGLCGMILTLKETGLPKCVLS 133
Cdd:cd16296     1 LQVVAAGSRDMGAALYVFSEYNRYLFNCGEGVQRLMQEHKLKVARLDNIFLTRMHWSNVGGLSGMILTLKETGLPKCVLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509518 134 GPpqlekyleaikifsgplkgidlavrphsapeykdetmtvyqvpihserrcgeqepsrspkrspnrlspkqsssdpgsa 213
Cdd:cd16296    81 GP------------------------------------------------------------------------------ 82

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509518 214 engqCLPEGSSAGVNGKAWGRDPSLVVAFVCKLHLRKGNFLVLKAKELGLPVGTAAIAPIIAAVKDGKSITYEGREIAAE 293
Cdd:cd16296    83 ----NKQSPDKIGVRRQILERDPSLVVAFICKLHLKKGNFLVLKAKELGLPVGTAAIAPIIAAVKDGKSITFEGREILAE 158

                         250
                  ....*....|....*..
gi 1936509518 294 ELCTPPDPGLVFIVVEC 310
Cdd:cd16296   159 ELCTPPDPGIVFIVVEC 175
metallo-hydrolase-like_MBL-fold super family cl23716
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 657-729 1.59e-03

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 PRK02126:

Pssm-ID: 451500 [Multi-domain]  Cd Length: 334  Bit Score: 41.44  E-value: 1.59e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1936509518 657 GWKVVYSGDTMP----CEALVQMGKDATLLIHEATLEDGLEEEAVEKTHSTTSQAIGVGMRMNAEFIMLNHFSQRYA 729
Cdd:PRK02126  242 GQKIGYVTDIGYteenLARIVELAAGVDLLFIEAVFLDEDAEKARRKNHLTARQAGRLAREAGVKRLLPFHFSPRYQ 318
 
Name Accession Description Interval E-value
RNaseZ_ELAC1_ELAC2-C-term-like_MBL-fold cd07718
Ribonuclease Z ELAC1, C-terminus of ELAC2, and related proteins; MBL-fold metallo-hydrolase ...
 482-687 2.83e-103

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: 317.18  E-value: 2.83e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509518 482 IVFLGTGSAIPMKIRNVSSTLVNLSPDKSVLLDCGEGTFGQLCRHYGQQ-IDRVLCNLTAVFVSHLHADHHTGLLNILLQ 560
Cdd:cd07718     1 VVFLGTGSAIPSKYRNVSGILLRIPGDGSILLDCGEGTLGQLRRHYGPEeADEVLRNLKCIFISHLHADHHLGLIRLLAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509518 561 REHALAslgKPFQPLLVVAPTQLRAWLQQYHNQCQEILHHISMIPAKCLQKGAEVPSPPVERLISLLLETCDLQEFQTCL 640
Cdd:cd07718    81 RKKLFK---PPSPPLYVVAPRQLRRWLREYSSLEDLGLHDISFISNRVSQSLPESDDPLSRDLLSNLLEELGLKSIETVP 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1936509518 641 VRHCKHAFGCALVHSSGWKVVYSGDTMPCEALVQMGKDATLLIHEAT 687
Cdd:cd07718   158 VIHCPDAYGIVLTHEDGWKIVYSGDTRPCEALVEAGKGADLLIHEAT 204
RNaseZ_ELAC2-N-term-like_MBL-fold cd16296
Ribonuclease Z, N-terminus of human ELAC2 and related proteins; MBL-fold metallo-hydrolase ...
 54-310 5.94e-98

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: 302.26  E-value: 5.94e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509518  54 LQVVAAGGRDAGAALYVFSEYNRYLFNCGEGVQRLMQEHKLKVARLDNIFLTRMHWSNVGGLCGMILTLKETGLPKCVLS 133
Cdd:cd16296     1 LQVVAAGSRDMGAALYVFSEYNRYLFNCGEGVQRLMQEHKLKVARLDNIFLTRMHWSNVGGLSGMILTLKETGLPKCVLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509518 134 GPpqlekyleaikifsgplkgidlavrphsapeykdetmtvyqvpihserrcgeqepsrspkrspnrlspkqsssdpgsa 213
Cdd:cd16296    81 GP------------------------------------------------------------------------------ 82

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509518 214 engqCLPEGSSAGVNGKAWGRDPSLVVAFVCKLHLRKGNFLVLKAKELGLPVGTAAIAPIIAAVKDGKSITYEGREIAAE 293
Cdd:cd16296    83 ----NKQSPDKIGVRRQILERDPSLVVAFICKLHLKKGNFLVLKAKELGLPVGTAAIAPIIAAVKDGKSITFEGREILAE 158

                         250
                  ....*....|....*..
gi 1936509518 294 ELCTPPDPGLVFIVVEC 310
Cdd:cd16296   159 ELCTPPDPGIVFIVVEC 175
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
481-751 3.28e-48

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 171.15  E-value: 3.28e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509518 481 EIVFLGTGSAIPMKIRNVSSTLVNlSPDKSVLLDCGEGTFGQLCRHygqQIDrvLCNLTAVFVSHLHADHHTGLLNILLQ 560
Cdd:COG1234     2 KLTFLGTGGAVPTPGRATSSYLLE-AGGERLLIDCGEGTQRQLLRA---GLD--PRDIDAIFITHLHGDHIAGLPGLLST 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509518 561 RehalaSLGKPFQPLLVVAPTQLRAWLQQYHNQCQEILH-HISMIPakcLQKGAEVPSPPVErlisllletcdlqeFQTC 639
Cdd:COG1234    76 R-----SLAGREKPLTIYGPPGTKEFLEALLKASGTDLDfPLEFHE---IEPGEVFEIGGFT--------------VTAF 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509518 640 LVRHCKHAFGcALVHSSGWKVVYSGDTMPCEALVQMGKDATLLIHEATLEDGLEEEAVEKTHSTTSQAIGVGMRMNAEFI 719
Cdd:COG1234   134 PLDHPVPAYG-YRFEEPGRSLVYSGDTRPCEALVELAKGADLLIHEATFLDEEAELAKETGHSTAKEAAELAAEAGVKRL 212

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1936509518 720 MLNHFSQRYAKIPLF----SPDFNEKVGIAFDHMKV 751
Cdd:COG1234   213 VLTHFSPRYDDPEELlaeaRAVFPGPVELAEDGMVI 248
PRK00055 PRK00055
ribonuclease Z; Reviewed
 481-728 9.22e-41

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 150.72  E-value: 9.22e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509518 481 EIVFLGTGSAIPMKIRNVSSTLVNLsPDKSVLLDCGEGTFGQLcRHYG---QQIDRVlcnltavFVSHLHADHHTGLLNI 557
Cdd:PRK00055    3 ELTFLGTGSGVPTPTRNVSSILLRL-GGELFLFDCGEGTQRQL-LKTGikpRKIDKI-------FITHLHGDHIFGLPGL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509518 558 LLQRehalaSLGKPFQPLLVVAPtqlrAWLQQYHNQCQEILHHIS----------MIPAKCLQKGAEVPSPPVERLisll 627
Cdd:PRK00055   74 LSTR-----SLSGRTEPLTIYGP----KGIKEFVETLLRASGSLGyriaekdkpgKLDAEKLKALGVPPGPLFGKL---- 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509518 628 letcdlQEFQTCLV---RHCKHAFGCALVHSsGWKVVYSGDTMPCEALVQMGKDATLLIHEATLEDGLEEEAVEKTHSTT 704
Cdd:PRK00055  141 ------KRGEDVTLedgRIINPADVLGPPRK-GRKVAYCGDTRPCEALVELAKGADLLVHEATFGDEDEELAKEYGHSTA 213

                         250       260
                  ....*....|....*....|....
gi 1936509518 705 SQAIGVGMRMNAEFIMLNHFSQRY 728
Cdd:PRK00055  214 RQAAEIAKEAGVKRLILTHFSPRY 237
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 481-728 2.04e-33

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: 130.80  E-value: 2.04e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509518 481 EIVFLGTGSAIPMKIRNVSSTLVNLsPDKSVLLDCGEGTFGQLcRHYG---QQIDRVlcnltavFVSHLHADHHTGLLNI 557
Cdd:TIGR02651   1 EITFLGTGGGVPTKERNLPSIALKL-NGELWLFDCGEGTQRQM-LRSGispMKIDRI-------FITHLHGDHILGLPGL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509518 558 LLQRehalaSLGKPFQPLLVVAPtqlrawlqqyhnqcQEILHHISMIpakcLQKGAEVPSPPVErlISLLLETCDLQEF- 636
Cdd:TIGR02651  72 LSTM-----SFQGRKEPLTIYGP--------------PGIKEFIETS----LRVSYTYLNYPIK--IHEIEEGGLVFEDd 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509518 637 ----QTCLVRHCKHAFGCALV-------------------------------------------------HSSGWKVVYS 663
Cdd:TIGR02651 127 gfkvEAFPLDHSIPSLGYRFEekdrpgkfdrekakelgippgplygklkrgetvtlidgriidpedvlgpPRKGRKIAYT 206

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1936509518 664 GDTMPCEALVQMGKDATLLIHEATLEDGLEEEAVEKTHSTTSQAIGVGMRMNAEFIMLNHFSQRY 728
Cdd:TIGR02651 207 GDTRPCEEVIEFAKNADLLIHEATFLDEDKKLAKEYGHSTAAQAAEIAKEANVKRLILTHISPRY 271
Lactamase_B_4 pfam13691
tRNase Z endonuclease; This is family of tRNase Z enzymes, that are closely related ...
 68-114 9.82e-15

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: 69.15  E-value: 9.82e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1936509518  68 LYVFSEYNRYLF-NCGEGVQRLMQEHKLKVARLDNIFLTRMH-WSNVGG 114
Cdd:pfam13691  15 LLLHFDSKRYLFgNVGEGTQRALNEQKVRLSKLEDIFLTGKVsWSNIGG 63
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
76-174 6.91e-13

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 69.45  E-value: 6.91e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509518  76 RYLFNCGEGVQRLMQEHKLKVARLDNIFLTRMHWSNVGGLCGMILTLKETGLPK-CVLSGPPQLEKYLEAIKIFSGPLKG 154
Cdd:COG1234    30 RLLIDCGEGTQRQLLRAGLDPRDIDAIFITHLHGDHIAGLPGLLSTRSLAGREKpLTIYGPPGTKEFLEALLKASGTDLD 109

                          90       100
                  ....*....|....*....|.
gi 1936509518 155 IDLAVRPHSAPE-YKDETMTV 174
Cdd:COG1234   110 FPLEFHEIEPGEvFEIGGFTV 130
PRK00055 PRK00055
ribonuclease Z; Reviewed
 77-152 2.73e-07

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 52.88  E-value: 2.73e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1936509518  77 YLFNCGEGVQRLMQEHKLKVARLDNIFLTRMHWSNVGGLCGMILTLKETGLPKCV-LSGPPQLEKYLEAIKIFSGPL 152
Cdd:PRK00055   32 FLFDCGEGTQRQLLKTGIKPRKIDKIFITHLHGDHIFGLPGLLSTRSLSGRTEPLtIYGPKGIKEFVETLLRASGSL 108
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 511-724 3.14e-06

Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and is related to pfam00753.


Pssm-ID: 432732 [Multi-domain]  Cd Length: 196  Bit Score: 48.46  E-value: 3.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509518 511 VLLDCGEGTFGQL------CRHYGQQIDrvlcnltAVFVSHLHADHHTGLLNIllqrehalaslgKPFQPLLVVAP---- 580
Cdd:pfam12706   3 ILIDPGPDLRQQAlpalqpGRLRDDPID-------AVLLTHDHYDHLAGLLDL------------REGRPRPLYAPlgvl 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509518 581 TQLRAW------LQQYHNQCQEI-----------LHHISMIPAKclQKGAEVPSPPVERLISLLLETcdlqefqtclvrh 643
Cdd:pfam12706  64 AHLRRNfpylflLEHYGVRVHEIdwgesftvgdgGLTVTATPAR--HGSPRGLDPNPGDTLGFRIEG------------- 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509518 644 ckhafgcalvhsSGWKVVYSGDTMPCEALV-QMGKDATLLIHEATLEDglEEEAVEKTHSTTSQAIGVGMRMNAEFIMLN 722
Cdd:pfam12706 129 ------------PGKRVYYAGDTGYFPDEIgERLGGADLLLLDGGAWR--DDEMIHMGHMTPEEAVEAAADLGARRKVLI 194


                  ..
gi 1936509518 723 HF 724
Cdd:pfam12706 195 HI 196
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 499-690 1.40e-05

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: 46.39  E-value: 1.40e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509518  499 SSTLVNlSPDKSVLLDCGEGTFGQLCRHYGQQIDRvlcNLTAVFVSHLHADhHTGLLNILLQREHAlaslgkpfqplLVV 578
Cdd:smart00849   1 NSYLVR-DDGGAILIDTGPGEAEDLLAELKKLGPK---KIDAIILTHGHPD-HIGGLPELLEAPGA-----------PVY 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509518  579 APTQLRAWLQQYHNQCQEILHHI-SMIPAKCLQKGAEVpsppverlisllletcDLQEFQTCLVRHCKHAFGCALVHSSG 657
Cdd:smart00849  65 APEGTAELLKDLLALLGELGAEAePAPPDRTLKDGDEL----------------DLGGGELEVIHTPGHTPGSIVLYLPE 128

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1936509518  658 WKVVYSGDTMPCEALVQMGKDATLLIHEATLED 690
Cdd:smart00849 129 GKILFTGDLLFAGGDGRTLVDGGDAAASDALES 161
PRK02126 PRK02126
ribonuclease Z; Provisional
 657-729 1.59e-03

ribonuclease Z; Provisional


Pssm-ID: 235006 [Multi-domain]  Cd Length: 334  Bit Score: 41.44  E-value: 1.59e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1936509518 657 GWKVVYSGDTMP----CEALVQMGKDATLLIHEATLEDGLEEEAVEKTHSTTSQAIGVGMRMNAEFIMLNHFSQRYA 729
Cdd:PRK02126  242 GQKIGYVTDIGYteenLARIVELAAGVDLLFIEAVFLDEDAEKARRKNHLTARQAGRLAREAGVKRLLPFHFSPRYQ 318
 
Name Accession Description Interval E-value
RNaseZ_ELAC1_ELAC2-C-term-like_MBL-fold cd07718
Ribonuclease Z ELAC1, C-terminus of ELAC2, and related proteins; MBL-fold metallo-hydrolase ...
 482-687 2.83e-103

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: 317.18  E-value: 2.83e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509518 482 IVFLGTGSAIPMKIRNVSSTLVNLSPDKSVLLDCGEGTFGQLCRHYGQQ-IDRVLCNLTAVFVSHLHADHHTGLLNILLQ 560
Cdd:cd07718     1 VVFLGTGSAIPSKYRNVSGILLRIPGDGSILLDCGEGTLGQLRRHYGPEeADEVLRNLKCIFISHLHADHHLGLIRLLAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509518 561 REHALAslgKPFQPLLVVAPTQLRAWLQQYHNQCQEILHHISMIPAKCLQKGAEVPSPPVERLISLLLETCDLQEFQTCL 640
Cdd:cd07718    81 RKKLFK---PPSPPLYVVAPRQLRRWLREYSSLEDLGLHDISFISNRVSQSLPESDDPLSRDLLSNLLEELGLKSIETVP 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1936509518 641 VRHCKHAFGCALVHSSGWKVVYSGDTMPCEALVQMGKDATLLIHEAT 687
Cdd:cd07718   158 VIHCPDAYGIVLTHEDGWKIVYSGDTRPCEALVEAGKGADLLIHEAT 204
RNaseZ_ELAC2-N-term-like_MBL-fold cd16296
Ribonuclease Z, N-terminus of human ELAC2 and related proteins; MBL-fold metallo-hydrolase ...
 54-310 5.94e-98

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: 302.26  E-value: 5.94e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509518  54 LQVVAAGGRDAGAALYVFSEYNRYLFNCGEGVQRLMQEHKLKVARLDNIFLTRMHWSNVGGLCGMILTLKETGLPKCVLS 133
Cdd:cd16296     1 LQVVAAGSRDMGAALYVFSEYNRYLFNCGEGVQRLMQEHKLKVARLDNIFLTRMHWSNVGGLSGMILTLKETGLPKCVLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509518 134 GPpqlekyleaikifsgplkgidlavrphsapeykdetmtvyqvpihserrcgeqepsrspkrspnrlspkqsssdpgsa 213
Cdd:cd16296    81 GP------------------------------------------------------------------------------ 82

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509518 214 engqCLPEGSSAGVNGKAWGRDPSLVVAFVCKLHLRKGNFLVLKAKELGLPVGTAAIAPIIAAVKDGKSITYEGREIAAE 293
Cdd:cd16296    83 ----NKQSPDKIGVRRQILERDPSLVVAFICKLHLKKGNFLVLKAKELGLPVGTAAIAPIIAAVKDGKSITFEGREILAE 158

                         250
                  ....*....|....*..
gi 1936509518 294 ELCTPPDPGLVFIVVEC 310
Cdd:cd16296   159 ELCTPPDPGIVFIVVEC 175
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
481-751 3.28e-48

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 171.15  E-value: 3.28e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509518 481 EIVFLGTGSAIPMKIRNVSSTLVNlSPDKSVLLDCGEGTFGQLCRHygqQIDrvLCNLTAVFVSHLHADHHTGLLNILLQ 560
Cdd:COG1234     2 KLTFLGTGGAVPTPGRATSSYLLE-AGGERLLIDCGEGTQRQLLRA---GLD--PRDIDAIFITHLHGDHIAGLPGLLST 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509518 561 RehalaSLGKPFQPLLVVAPTQLRAWLQQYHNQCQEILH-HISMIPakcLQKGAEVPSPPVErlisllletcdlqeFQTC 639
Cdd:COG1234    76 R-----SLAGREKPLTIYGPPGTKEFLEALLKASGTDLDfPLEFHE---IEPGEVFEIGGFT--------------VTAF 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509518 640 LVRHCKHAFGcALVHSSGWKVVYSGDTMPCEALVQMGKDATLLIHEATLEDGLEEEAVEKTHSTTSQAIGVGMRMNAEFI 719
Cdd:COG1234   134 PLDHPVPAYG-YRFEEPGRSLVYSGDTRPCEALVELAKGADLLIHEATFLDEEAELAKETGHSTAKEAAELAAEAGVKRL 212

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1936509518 720 MLNHFSQRYAKIPLF----SPDFNEKVGIAFDHMKV 751
Cdd:COG1234   213 VLTHFSPRYDDPEELlaeaRAVFPGPVELAEDGMVI 248
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 482-728 7.07e-46

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: 164.54  E-value: 7.07e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509518 482 IVFLGTGSAIPMKIRNVSSTLVNLsPDKSVLLDCGEGTFGQLcRHYGqqidRVLCNLTAVFVSHLHADHHTGLLNiLLQR 561
Cdd:cd07717     1 LTFLGTGSAVPTPERNLSSIALRL-EGELWLFDCGEGTQRQL-LRAG----LSPSKIDRIFITHLHGDHILGLPG-LLST 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509518 562 ehalASLGKPFQPLLVVAPTQLRAWLQQYHNQCQ-----EILHHismipakclqkgaEVPSPPVErlislLLETCDLQeF 636
Cdd:cd07717    74 ----MSLLGRTEPLTIYGPKGLKEFLETLLRLSAsrlpyPIEVH-------------ELEPDPGL-----VFEDDGFT-V 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509518 637 QTCLVRHCKHAFGCALVhsSGWKVVYSGDTMPCEALVQMGKDATLLIHEATLEDGLEEEAVEKTHSTTSQAIGVGMRMNA 716
Cdd:cd07717   131 TAFPLDHRVPCFGYRFE--EGRKIAYLGDTRPCEGLVELAKGADLLIHEATFLDDDAEKAKETGHSTAKQAAEIAKKAGV 208

                         250
                  ....*....|..
gi 1936509518 717 EFIMLNHFSQRY 728
Cdd:cd07717   209 KKLVLTHFSARY 220
PRK00055 PRK00055
ribonuclease Z; Reviewed
 481-728 9.22e-41

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 150.72  E-value: 9.22e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509518 481 EIVFLGTGSAIPMKIRNVSSTLVNLsPDKSVLLDCGEGTFGQLcRHYG---QQIDRVlcnltavFVSHLHADHHTGLLNI 557
Cdd:PRK00055    3 ELTFLGTGSGVPTPTRNVSSILLRL-GGELFLFDCGEGTQRQL-LKTGikpRKIDKI-------FITHLHGDHIFGLPGL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509518 558 LLQRehalaSLGKPFQPLLVVAPtqlrAWLQQYHNQCQEILHHIS----------MIPAKCLQKGAEVPSPPVERLisll 627
Cdd:PRK00055   74 LSTR-----SLSGRTEPLTIYGP----KGIKEFVETLLRASGSLGyriaekdkpgKLDAEKLKALGVPPGPLFGKL---- 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509518 628 letcdlQEFQTCLV---RHCKHAFGCALVHSsGWKVVYSGDTMPCEALVQMGKDATLLIHEATLEDGLEEEAVEKTHSTT 704
Cdd:PRK00055  141 ------KRGEDVTLedgRIINPADVLGPPRK-GRKVAYCGDTRPCEALVELAKGADLLVHEATFGDEDEELAKEYGHSTA 213

                         250       260
                  ....*....|....*....|....
gi 1936509518 705 SQAIGVGMRMNAEFIMLNHFSQRY 728
Cdd:PRK00055  214 RQAAEIAKEAGVKRLILTHFSPRY 237
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 482-686 9.48e-41

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: 147.79  E-value: 9.48e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509518 482 IVFLGTGSAIPMKIRNVSSTLVNlSPDKSVLLDCGEGTFGQLCRHyGQQIDRvlcnLTAVFVSHLHADHHTGLLNILLQR 561
Cdd:cd16272     1 LTFLGTGGAVPSLTRNTSSYLLE-TGGTRILLDCGEGTVYRLLKA-GVDPDK----LDAIFLSHFHLDHIGGLPTLLFAR 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509518 562 EhalasLGKPFQPLLVVAPTQLRAWLQQYHNQCQEILHHismipakclqkgaevPSPPVERLISLLLETCDLQEF--QTC 639
Cdd:cd16272    75 R-----YGGRKKPLTIYGPKGIKEFLEKLLNFPVEILPL---------------GFPLEIEELEEGGEVLELGDLkvEAF 134

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1936509518 640 LVRHCKHAFGCALvHSSGWKVVYSGDTMPCEALVQMGKDATLLIHEA 686
Cdd:cd16272   135 PVKHSVESLGYRI-EAEGKSIVYSGDTGPCENLVELAKGADLLIHEC 180
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 481-728 2.04e-33

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: 130.80  E-value: 2.04e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509518 481 EIVFLGTGSAIPMKIRNVSSTLVNLsPDKSVLLDCGEGTFGQLcRHYG---QQIDRVlcnltavFVSHLHADHHTGLLNI 557
Cdd:TIGR02651   1 EITFLGTGGGVPTKERNLPSIALKL-NGELWLFDCGEGTQRQM-LRSGispMKIDRI-------FITHLHGDHILGLPGL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509518 558 LLQRehalaSLGKPFQPLLVVAPtqlrawlqqyhnqcQEILHHISMIpakcLQKGAEVPSPPVErlISLLLETCDLQEF- 636
Cdd:TIGR02651  72 LSTM-----SFQGRKEPLTIYGP--------------PGIKEFIETS----LRVSYTYLNYPIK--IHEIEEGGLVFEDd 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509518 637 ----QTCLVRHCKHAFGCALV-------------------------------------------------HSSGWKVVYS 663
Cdd:TIGR02651 127 gfkvEAFPLDHSIPSLGYRFEekdrpgkfdrekakelgippgplygklkrgetvtlidgriidpedvlgpPRKGRKIAYT 206

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1936509518 664 GDTMPCEALVQMGKDATLLIHEATLEDGLEEEAVEKTHSTTSQAIGVGMRMNAEFIMLNHFSQRY 728
Cdd:TIGR02651 207 GDTRPCEEVIEFAKNADLLIHEATFLDEDKKLAKEYGHSTAAQAAEIAKEANVKRLILTHISPRY 271
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 481-684 1.53e-22

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: 96.05  E-value: 1.53e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509518 481 EIVFLGTGSAIPMKIRNVSSTLVnLSPDKSVLLDCGEGTFGQLCRHyGQQIDRvlcnLTAVFVSHLHADHHTGLLNILLQ 560
Cdd:cd07719     1 RVTLLGTGGPIPDPDRAGPSTLV-VVGGRVYLVDAGSGVVRRLAQA-GLPLGD----LDAVFLTHLHSDHVADLPALLLT 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509518 561 REHALASlgkpfQPLLVVAPTQLRAW----LQQYHnqcQEILHHISMIPAKCLQKGA-----EVPSPPVerlislLLETC 631
Cdd:cd07719    75 AWLAGRK-----TPLPVYGPPGTRALvdglLAAYA---LDIDYRARIGDEGRPDPGAlvevhEIAAGGV------VYEDD 140

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1936509518 632 DLQeFQTCLVRH--CKHAFgcAL-VHSSGWKVVYSGDTMPCEALVQMGKDATLLIH 684
Cdd:cd07719   141 GVK-VTAFLVDHgpVPPAL--AYrFDTPGRSVVFSGDTGPSENLIELAKGADLLVH 193
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 484-686 6.11e-18

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: 82.69  E-value: 6.11e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509518 484 FLGTGSAIPMKIRNVSSTLVNlSPDKSVLLDCGEGTFGQLCRhygQQIDRVlcNLTAVFVSHLHADHHTGLLNILLQREH 563
Cdd:cd07740     2 FLGSGDAFGSGGRLNTCFHVA-SEAGRFLIDCGASSLIALKR---AGIDPN--AIDAIFITHLHGDHFGGLPFFLLDAQF 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509518 564 ALaslgKPFQPLLVVAPTQLRAWLQQyhnqCQEILH-HISMIPAKclqkgAEVPSPPVERLISLLLETCDLQEFQtclVR 642
Cdd:cd07740    76 VA----KRTRPLTIAGPPGLRERLRR----AMEALFpGSSKVPRR-----FDLEVIELEPGEPTTLGGVTVTAFP---VV 139

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1936509518 643 HCKHAFGCALVHSSGWKVV-YSGDTMPCEALVQMGKDATLLIHEA 686
Cdd:cd07740   140 HPSGALPLALRLEAAGRVLaYSGDTEWTDALVPLARGADLFICEC 184
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 499-686 1.02e-17

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: 81.33  E-value: 1.02e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509518 499 SSTLVNlSPDKSVLLDCGEGTFGQLCRHygqqIDrvLCNLTAVFVSHLHADHHTGLlnILLQREHALASLGKPFQPLLVV 578
Cdd:cd07716    19 SGYLLE-ADGFRILLDCGSGVLSRLQRY----ID--PEDLDAVVLSHLHPDHCADL--GVLQYARRYHPRGARKPPLPLY 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509518 579 APTQLRAWLQQ-YHNQCQEILHHIsmipakclqkgaEVPSPpverlisllLETCDLqEFQTCLVRHCKHAFGCALVHSSG 657
Cdd:cd07716    90 GPAGPAERLAAlYGLEDVFDFHPI------------EPGEP---------LEIGPF-TITFFRTVHPVPCYAMRIEDGGK 147

                         170       180
                  ....*....|....*....|....*....
gi 1936509518 658 wKVVYSGDTMPCEALVQMGKDATLLIHEA 686
Cdd:cd07716   148 -VLVYTGDTGYCDELVEFARGADLLLCEA 175
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 75-166 3.67e-16

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: 77.30  E-value: 3.67e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509518  75 NRYLFNCGEGVQRLMQEHKLKVARLDNIFLTRMHWSNVGGLCGMILTLKETGLPK-CVLSGPPQLEKYLEAIKIFSGPL- 152
Cdd:cd16272    27 TRILLDCGEGTVYRLLKAGVDPDKLDAIFLSHFHLDHIGGLPTLLFARRYGGRKKpLTIYGPKGIKEFLEKLLNFPVEIl 106

                          90
                  ....*....|....*
gi 1936509518 153 -KGIDLAVRPHSAPE 166
Cdd:cd16272   107 pLGFPLEIEELEEGG 121
Lactamase_B_4 pfam13691
tRNase Z endonuclease; This is family of tRNase Z enzymes, that are closely related ...
 68-114 9.82e-15

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: 69.15  E-value: 9.82e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1936509518  68 LYVFSEYNRYLF-NCGEGVQRLMQEHKLKVARLDNIFLTRMH-WSNVGG 114
Cdd:pfam13691  15 LLLHFDSKRYLFgNVGEGTQRALNEQKVRLSKLEDIFLTGKVsWSNIGG 63
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 481-751 1.03e-14

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 74.93  E-value: 1.03e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509518 481 EIVFLGTGSAIPM----------------KIRNVSSTLVNlSPDKSVLLDCGEGtFGQLCRHYGQQIDRvlcnLTAVFVS 544
Cdd:COG1235     2 KVTFLGSGSSGGVpqigcdcpvcastdprYGRTRSSILVE-ADGTRLLIDAGPD-LREQLLRLGLDPSK----IDAILLT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509518 545 HLHADHHTGLLNIllqREHALAslgkpfQPLLVVAPTQLRAWLQQYHNQCQEilHHISMIPAKCLQKGAEVpsppverli 624
Cdd:COG1235    76 HEHADHIAGLDDL---RPRYGP------NPIPVYATPGTLEALERRFPYLFA--PYPGKLEFHEIEPGEPF--------- 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509518 625 slllETCDLqEFQTCLVRH-CKHAFGCaLVHSSGWKVVYSGDT-MPCEALVQMGKDATLLIHEATLEDGleeeavEKTHS 702
Cdd:COG1235   136 ----EIGGL-TVTPFPVPHdAGDPVGY-RIEDGGKKLAYATDTgYIPEEVLELLRGADLLILDATYDDP------EPGHL 203

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1936509518 703 TTSQAIGVGMRMNAEFIMLNHFSQRYAKIPLF-----SPDFNEKVGIAFDHMKV 751
Cdd:COG1235   204 SNEEALELLARLGPKRLVLTHLSPDNNDHELDydeleAALLPAGVEVAYDGMEI 257
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
76-174 6.91e-13

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 69.45  E-value: 6.91e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509518  76 RYLFNCGEGVQRLMQEHKLKVARLDNIFLTRMHWSNVGGLCGMILTLKETGLPK-CVLSGPPQLEKYLEAIKIFSGPLKG 154
Cdd:COG1234    30 RLLIDCGEGTQRQLLRAGLDPRDIDAIFITHLHGDHIAGLPGLLSTRSLAGREKpLTIYGPPGTKEFLEALLKASGTDLD 109

                          90       100
                  ....*....|....*....|.
gi 1936509518 155 IDLAVRPHSAPE-YKDETMTV 174
Cdd:COG1234   110 FPLEFHEIEPGEvFEIGGFTV 130
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 75-181 8.34e-13

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: 69.02  E-value: 8.34e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509518  75 NRYLFNCGEGVQRLMQEHKLKVARLDNIFLTRMHwsnvG----GLCGMILTLKETGLPKCV-LSGPPQLEKYLEAIKIFS 149
Cdd:cd07717    27 ELWLFDCGEGTQRQLLRAGLSPSKIDRIFITHLH----GdhilGLPGLLSTMSLLGRTEPLtIYGPKGLKEFLETLLRLS 102

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1936509518 150 GPLKGIDLAVRPHSAPE---YKDETMTVYQVPI-HS 181
Cdd:cd07717   103 ASRLPYPIEVHELEPDPglvFEDDGFTVTAFPLdHR 138
PRK00055 PRK00055
ribonuclease Z; Reviewed
 77-152 2.73e-07

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 52.88  E-value: 2.73e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1936509518  77 YLFNCGEGVQRLMQEHKLKVARLDNIFLTRMHWSNVGGLCGMILTLKETGLPKCV-LSGPPQLEKYLEAIKIFSGPL 152
Cdd:PRK00055   32 FLFDCGEGTQRQLLKTGIKPRKIDKIFITHLHGDHIFGLPGLLSTRSLSGRTEPLtIYGPKGIKEFVETLLRASGSL 108
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 511-724 3.14e-06

Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and is related to pfam00753.


Pssm-ID: 432732 [Multi-domain]  Cd Length: 196  Bit Score: 48.46  E-value: 3.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509518 511 VLLDCGEGTFGQL------CRHYGQQIDrvlcnltAVFVSHLHADHHTGLLNIllqrehalaslgKPFQPLLVVAP---- 580
Cdd:pfam12706   3 ILIDPGPDLRQQAlpalqpGRLRDDPID-------AVLLTHDHYDHLAGLLDL------------REGRPRPLYAPlgvl 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509518 581 TQLRAW------LQQYHNQCQEI-----------LHHISMIPAKclQKGAEVPSPPVERLISLLLETcdlqefqtclvrh 643
Cdd:pfam12706  64 AHLRRNfpylflLEHYGVRVHEIdwgesftvgdgGLTVTATPAR--HGSPRGLDPNPGDTLGFRIEG------------- 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509518 644 ckhafgcalvhsSGWKVVYSGDTMPCEALV-QMGKDATLLIHEATLEDglEEEAVEKTHSTTSQAIGVGMRMNAEFIMLN 722
Cdd:pfam12706 129 ------------PGKRVYYAGDTGYFPDEIgERLGGADLLLLDGGAWR--DDEMIHMGHMTPEEAVEAAADLGARRKVLI 194


                  ..
gi 1936509518 723 HF 724
Cdd:pfam12706 195 HI 196
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 499-690 1.40e-05

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: 46.39  E-value: 1.40e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509518  499 SSTLVNlSPDKSVLLDCGEGTFGQLCRHYGQQIDRvlcNLTAVFVSHLHADhHTGLLNILLQREHAlaslgkpfqplLVV 578
Cdd:smart00849   1 NSYLVR-DDGGAILIDTGPGEAEDLLAELKKLGPK---KIDAIILTHGHPD-HIGGLPELLEAPGA-----------PVY 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509518  579 APTQLRAWLQQYHNQCQEILHHI-SMIPAKCLQKGAEVpsppverlisllletcDLQEFQTCLVRHCKHAFGCALVHSSG 657
Cdd:smart00849  65 APEGTAELLKDLLALLGELGAEAePAPPDRTLKDGDEL----------------DLGGGELEVIHTPGHTPGSIVLYLPE 128

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1936509518  658 WKVVYSGDTMPCEALVQMGKDATLLIHEATLED 690
Cdd:smart00849 129 GKILFTGDLLFAGGDGRTLVDGGDAAASDALES 161
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
496-666 6.26e-05

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 44.67  E-value: 6.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509518 496 RNVSSTLVNlSPDKSVLLDCGEGTFGQLCRHYGQQIDRVLcNLTAVFVSHLHADhHTGLLNILLQRehalaslgkpFQPL 575
Cdd:pfam00753   4 GQVNSYLIE-GGGGAVLIDTGGSAEAALLLLLAALGLGPK-DIDAVILTHGHFD-HIGGLGELAEA----------TDVP 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509518 576 LVVAPTQLRAWLQQYHNQCQEILHHISMIPakclqkgaeVPSPPVERLISLLLETCDLQEFqtcLVRHCK-HAFGCALVH 654
Cdd:pfam00753  71 VIVVAEEARELLDEELGLAASRLGLPGPPV---------VPLPPDVVLEEGDGILGGGLGL---LVTHGPgHGPGHVVVY 138

                         170
                  ....*....|..
gi 1936509518 655 SSGWKVVYSGDT 666
Cdd:pfam00753 139 YGGGKVLFTGDL 150
metallo-hydrolase-like_MBL-fold cd07739
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 492-561 8.73e-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: 293825 [Multi-domain]  Cd Length: 201  Bit Score: 41.33  E-value: 8.73e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1936509518 492 PMKIRNVSSTLVnLSPDKSVLLDCgegtfgQLCRHYGQQ----IDRVLCNLTAVFVSHLHADHHTGlLNILLQR 561
Cdd:cd07739    10 EISSFPVTSTLI-YGETEAVLVDA------QFTRADAERladwIKASGKTLTTIYITHGHPDHYFG-LEVLLEA 75
PRK02126 PRK02126
ribonuclease Z; Provisional
 657-729 1.59e-03

ribonuclease Z; Provisional


Pssm-ID: 235006 [Multi-domain]  Cd Length: 334  Bit Score: 41.44  E-value: 1.59e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1936509518 657 GWKVVYSGDTMP----CEALVQMGKDATLLIHEATLEDGLEEEAVEKTHSTTSQAIGVGMRMNAEFIMLNHFSQRYA 729
Cdd:PRK02126  242 GQKIGYVTDIGYteenLARIVELAAGVDLLFIEAVFLDEDAEKARRKNHLTARQAGRLAREAGVKRLLPFHFSPRYQ 318
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 75-145 2.18e-03

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: 40.19  E-value: 2.18e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1936509518  75 NRYLFNCGEGVQRLMQEHKLKVARLDNIFLTRMHWSNVGGLCGMILTLKETGLPKCV-LSGPPQLEKYLEAI 145
Cdd:cd07719    28 RVYLVDAGSGVVRRLAQAGLPLGDLDAVFLTHLHSDHVADLPALLLTAWLAGRKTPLpVYGPPGTRALVDGL 99
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 481-550 2.35e-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: 40.15  E-value: 2.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509518 481 EIVFLGTGSA--IPM-----------KIRNV---SSTLVNlSPDKSVLLDCGEgTF-GQLCRHYGQQIDrvlcnltAVFV 543
Cdd:cd16279     2 KLTFLGTGTSsgVPVigcdcgvcdssDPKNRrlrSSILIE-TGGKNILIDTGP-DFrQQALRAGIRKLD-------AVLL 72


                  ....*..
gi 1936509518 544 SHLHADH 550
Cdd:cd16279    73 THAHADH 79
metallo-hydrolase-like_MBL-fold cd07741
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 482-550 3.34e-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: 293827 [Multi-domain]  Cd Length: 212  Bit Score: 39.87  E-value: 3.34e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1936509518 482 IVFLGTGSA--IPMK-IRNVSSTLVNLsPDKSVLLDCGEGTFGQLCRHygqQIDRVlcNLTAVFVSHLHADH 550
Cdd:cd07741     1 IIFLGTGGGrfVVITqLRASGGIWIEL-NGKNIHIDPGPGALVRMCRP---KLDPT--KLDAIILSHRHLDH 66
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 502-671 3.76e-03

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: 39.19  E-value: 3.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509518 502 LVNLSPDKSVLLDCGEGTFGQLCRHygqqIDRVLCNLTAVFVSHLHADhHTGLLNILLQREHALASLGKPFQPLLVVAPT 581
Cdd:cd06262    14 LVSDEEGEAILIDPGAGALEKILEA----IEELGLKIKAILLTHGHFD-HIGGLAELKEAPGAPVYIHEADAELLEDPEL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509518 582 QLRAWLqqyhnqcqeilhhismipakclqkGAEVPSPPVERLIS----LLLETCDLQefqtclVRHCK-HAFGCALVHSS 656
Cdd:cd06262    89 NLAFFG------------------------GGPLPPPEPDILLEdgdtIELGGLELE------VIHTPgHTPGSVCFYIE 138

                         170
                  ....*....|....*
gi 1936509518 657 GWKVVYSGDTMPCEA 671
Cdd:cd06262   139 EEGVLFTGDTLFAGS 153
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 482-555 7.60e-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: 38.59  E-value: 7.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509518 482 IVFLG-----TGSAIpmkirnvsstLVNLsPDKSVLLDCG-----EGTFGQLCRHYGQQIDRvlcnLTAVFVSHLHADhH 551
Cdd:cd16295     1 LTFLGaarevTGSCY----------LLET-GGKRILLDCGlfqggKELEELNNEPFPFDPKE----IDAVILTHAHLD-H 64


                  ....
gi 1936509518 552 TGLL 555
Cdd:cd16295    65 SGRL 68
 
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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