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Conserved domains on  [gi|1331883511|gb|PNJ31633|]
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ELAC2 isoform 1 [Pongo abelii]

Protein Classification

zinc phosphodiesterase ELAC protein 2( domain architecture ID 10888841)

zinc phosphodiesterase ELAC protein 2 is involved in tRNA maturation by catalyzing endonucleolytic cleavage and removing extra 3' nucleotides from tRNA precursors, generating 3' termini of tRNAs

Graphical summary

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List of domain hits

 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 ...
 60-311 4.11e-115

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: 346.94  E-value: 4.11e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883511  60 LQVVAAGSRDSGAALYVFSEFNRYLFNCGEGVQRLMQEHKLKVARLDNIFLTRMHWSNVGGLSGMILTLKETGLPKCVLS 139
Cdd:cd16296     1 LQVVAAGSRDMGAALYVFSEYNRYLFNCGEGVQRLMQEHKLKVARLDNIFLTRMHWSNVGGLSGMILTLKETGLPKCVLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883511 140 GPpqlekyleaikifsgplkgiemavrphsapeykdetmtvyqipihseqkrgkhqpwqsperplgrlsperssdsesnE 219
Cdd:cd16296    81 GP-----------------------------------------------------------------------------N 83

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883511 220 NEPHLPHGVSQRRGARDSSLVVAFICKLHLKRGNFLVLKAKEMGLPVGTAAIAPIIAAVKDGKSITHEGREILAEELCTP 299
Cdd:cd16296    84 KQSPDKIGVRRQILERDPSLVVAFICKLHLKKGNFLVLKAKELGLPVGTAAIAPIIAAVKDGKSITFEGREILAEELCTP 163

                         250
                  ....*....|..
gi 1331883511 300 PDPGAAFVVVEC 311
Cdd:cd16296   164 PDPGIVFIVVEC 175
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 3.56e-101

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: 311.40  E-value: 3.56e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883511 482 IIFLGTGSAIPMKIRNVSATLVNISPNTSLLLDCGEGTFGQLCRHYGDQ-VDRVLGTLAAVFVSHLHADHHTGLLNILLQ 560
Cdd:cd07718     1 VVFLGTGSAIPSKYRNVSGILLRIPGDGSILLDCGEGTLGQLRRHYGPEeADEVLRNLKCIFISHLHADHHLGLIRLLAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883511 561 RERALAslgKPLHPLLVIAPSQLKAWLQQYHNQCQEVLHHISMIPAKCLQEGAEISSLAVERLISSLLGTCDLEGFQTCL 640
Cdd:cd07718    81 RKKLFK---PPSPPLYVVAPRQLRRWLREYSSLEDLGLHDISFISNRVSQSLPESDDPLSRDLLSNLLEELGLKSIETVP 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1331883511 641 VRHCKHAFGCALVHTSGWKVVYSGDTMPCEALVRMGKDATLLIHEAT 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; ...
 655-729 4.47e-04

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: 43.37  E-value: 4.47e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1331883511 655 TSGWKVVYSGDTMP----CEALVRMGKDATLLIHEATLEDGLEEEAVEKTHSTTSQAISVGMRMNAEFIMLNHFSQRYA 729
Cdd:PRK02126  240 EPGQKIGYVTDIGYteenLARIVELAAGVDLLFIEAVFLDEDAEKARRKNHLTARQAGRLAREAGVKRLLPFHFSPRYQ 318
 
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 ...
 60-311 4.11e-115

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: 346.94  E-value: 4.11e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883511  60 LQVVAAGSRDSGAALYVFSEFNRYLFNCGEGVQRLMQEHKLKVARLDNIFLTRMHWSNVGGLSGMILTLKETGLPKCVLS 139
Cdd:cd16296     1 LQVVAAGSRDMGAALYVFSEYNRYLFNCGEGVQRLMQEHKLKVARLDNIFLTRMHWSNVGGLSGMILTLKETGLPKCVLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883511 140 GPpqlekyleaikifsgplkgiemavrphsapeykdetmtvyqipihseqkrgkhqpwqsperplgrlsperssdsesnE 219
Cdd:cd16296    81 GP-----------------------------------------------------------------------------N 83

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883511 220 NEPHLPHGVSQRRGARDSSLVVAFICKLHLKRGNFLVLKAKEMGLPVGTAAIAPIIAAVKDGKSITHEGREILAEELCTP 299
Cdd:cd16296    84 KQSPDKIGVRRQILERDPSLVVAFICKLHLKKGNFLVLKAKELGLPVGTAAIAPIIAAVKDGKSITFEGREILAEELCTP 163

                         250
                  ....*....|..
gi 1331883511 300 PDPGAAFVVVEC 311
Cdd:cd16296   164 PDPGIVFIVVEC 175
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 3.56e-101

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: 311.40  E-value: 3.56e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883511 482 IIFLGTGSAIPMKIRNVSATLVNISPNTSLLLDCGEGTFGQLCRHYGDQ-VDRVLGTLAAVFVSHLHADHHTGLLNILLQ 560
Cdd:cd07718     1 VVFLGTGSAIPSKYRNVSGILLRIPGDGSILLDCGEGTLGQLRRHYGPEeADEVLRNLKCIFISHLHADHHLGLIRLLAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883511 561 RERALAslgKPLHPLLVIAPSQLKAWLQQYHNQCQEVLHHISMIPAKCLQEGAEISSLAVERLISSLLGTCDLEGFQTCL 640
Cdd:cd07718    81 RKKLFK---PPSPPLYVVAPRQLRRWLREYSSLEDLGLHDISFISNRVSQSLPESDDPLSRDLLSNLLEELGLKSIETVP 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1331883511 641 VRHCKHAFGCALVHTSGWKVVYSGDTMPCEALVRMGKDATLLIHEAT 687
Cdd:cd07718   158 VIHCPDAYGIVLTHEDGWKIVYSGDTRPCEALVEAGKGADLLIHEAT 204
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
481-751 7.74e-50

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 175.77  E-value: 7.74e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883511 481 EIIFLGTGSAIPMKIRNVSATLVNIsPNTSLLLDCGEGTFGQLCRHYGDqvdrvLGTLAAVFVSHLHADHHTGLLNILLQ 560
Cdd:COG1234     2 KLTFLGTGGAVPTPGRATSSYLLEA-GGERLLIDCGEGTQRQLLRAGLD-----PRDIDAIFITHLHGDHIAGLPGLLST 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883511 561 ReralaSLGKPLHPLLVIAPSQLKAWLQQYHNQCQEVLH-HISMIPakcLQEGAEIsslaverlissllgtcDLEGFQ-- 637
Cdd:COG1234    76 R-----SLAGREKPLTIYGPPGTKEFLEALLKASGTDLDfPLEFHE---IEPGEVF----------------EIGGFTvt 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883511 638 TCLVRHCKHAFGcALVHTSGWKVVYSGDTMPCEALVRMGKDATLLIHEATLEDGLEEEAVEKTHSTTSQAISVGMRMNAE 717
Cdd:COG1234   132 AFPLDHPVPAYG-YRFEEPGRSLVYSGDTRPCEALVELAKGADLLIHEATFLDEEAELAKETGHSTAKEAAELAAEAGVK 210

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1331883511 718 FIMLNHFSQRYAKVPLF----SPNFNEKVGVAFDHMKV 751
Cdd:COG1234   211 RLVLTHFSPRYDDPEELlaeaRAVFPGPVELAEDGMVI 248
PRK00055 PRK00055
ribonuclease Z; Reviewed
 481-728 1.58e-38

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 144.55  E-value: 1.58e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883511 481 EIIFLGTGSAIPMKIRNVSATLVNIsPNTSLLLDCGEGTFGQLcRHYG---DQVDRVlgtlaavFVSHLHADHHTGLLNI 557
Cdd:PRK00055    3 ELTFLGTGSGVPTPTRNVSSILLRL-GGELFLFDCGEGTQRQL-LKTGikpRKIDKI-------FITHLHGDHIFGLPGL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883511 558 LLQReralaSLGKPLHPLLVIAPsqlkAWLQQYHNQCQEVLHHIS----------MIPA--------------KCLQEGA 613
Cdd:PRK00055   74 LSTR-----SLSGRTEPLTIYGP----KGIKEFVETLLRASGSLGyriaekdkpgKLDAeklkalgvppgplfGKLKRGE 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883511 614 EISsLAVERLISSLLGTCDlegfqtclVRHckhafgcalvhtsGWKVVYSGDTMPCEALVRMGKDATLLIHEATLEDGLE 693
Cdd:PRK00055  145 DVT-LEDGRIINPADVLGP--------PRK-------------GRKVAYCGDTRPCEALVELAKGADLLVHEATFGDEDE 202

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1331883511 694 EEAVEKTHSTTSQAISVGMRMNAEFIMLNHFSQRY 728
Cdd:PRK00055  203 ELAKEYGHSTARQAAEIAKEAGVKRLILTHFSPRY 237
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 481-728 1.72e-32

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: 128.11  E-value: 1.72e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883511 481 EIIFLGTGSAIPMKIRNVSATLVNIsPNTSLLLDCGEGTFGQLcRHYG---DQVDRVlgtlaavFVSHLHADHHTGLLNI 557
Cdd:TIGR02651   1 EITFLGTGGGVPTKERNLPSIALKL-NGELWLFDCGEGTQRQM-LRSGispMKIDRI-------FITHLHGDHILGLPGL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883511 558 LLQReralaSLGKPLHPLLVIAPSQLKAWLQqyhNQCQEVLHHISMIPakclqEGAEISSLAVERlissllgtcDLEGFQ 637
Cdd:TIGR02651  72 LSTM-----SFQGRKEPLTIYGPPGIKEFIE---TSLRVSYTYLNYPI-----KIHEIEEGGLVF---------EDDGFK 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883511 638 --TCLVRHCKHAFGCALV-------------------------------------------------HTSGWKVVYSGDT 666
Cdd:TIGR02651 130 veAFPLDHSIPSLGYRFEekdrpgkfdrekakelgippgplygklkrgetvtlidgriidpedvlgpPRKGRKIAYTGDT 209

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331883511 667 MPCEALVRMGKDATLLIHEATLEDGLEEEAVEKTHSTTSQAISVGMRMNAEFIMLNHFSQRY 728
Cdd:TIGR02651 210 RPCEEVIEFAKNADLLIHEATFLDEDKKLAKEYGHSTAAQAAEIAKEANVKRLILTHISPRY 271
Lactamase_B_4 pfam13691
tRNase Z endonuclease; This is family of tRNase Z enzymes, that are closely related ...
 61-120 2.96e-18

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: 79.17  E-value: 2.96e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1331883511  61 QVVAAGSRDS-GAALYVFSEFNRYLF-NCGEGVQRLMQEHKLKVARLDNIFLTRMH-WSNVGG 120
Cdd:pfam13691   1 QVVTTPTADTpGPLLLLHFDSKRYLFgNVGEGTQRALNEQKVRLSKLEDIFLTGKVsWSNIGG 63
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
82-180 6.74e-12

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 66.37  E-value: 6.74e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883511  82 RYLFNCGEGVQRLMQEHKLKVARLDNIFLTRMHWSNVGGLSGMILTLKETGLPK-CVLSGPPQLEKYLEAIKIFSGPLKG 160
Cdd:COG1234    30 RLLIDCGEGTQRQLLRAGLDPRDIDAIFITHLHGDHIAGLPGLLSTRSLAGREKpLTIYGPPGTKEFLEALLKASGTDLD 109

                          90       100
                  ....*....|....*....|.
gi 1331883511 161 IEMAVRPHSAPE-YKDETMTV 180
Cdd:COG1234   110 FPLEFHEIEPGEvFEIGGFTV 130
PRK00055 PRK00055
ribonuclease Z; Reviewed
 83-158 1.68e-07

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 53.65  E-value: 1.68e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331883511  83 YLFNCGEGVQRLMQEHKLKVARLDNIFLTRMHWSNVGGLSGMILTLKETGLPKCV-LSGPPQLEKYLEAIKIFSGPL 158
Cdd:PRK00055   32 FLFDCGEGTQRQLLKTGIKPRKIDKIFITHLHGDHIFGLPGLLSTRSLSGRTEPLtIYGPKGIKEFVETLLRASGSL 108
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 499-690 2.26e-06

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: 48.70  E-value: 2.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883511  499 SATLVnISPNTSLLLDCGEGT----FGQLCRHYGDQVDrvlgtlaAVFVSHLHADhHTGLLNILLQRERAlaslgkplhp 574
Cdd:smart00849   1 NSYLV-RDDGGAILIDTGPGEaedlLAELKKLGPKKID-------AIILTHGHPD-HIGGLPELLEAPGA---------- 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883511  575 lLVIAPSQLKAWLQQYHNQCQEVLHHI-SMIPAKCLQEGAEIsslaverlissllgtcDLEGFQTCLVRHCKHAFGCALV 653
Cdd:smart00849  62 -PVYAPEGTAELLKDLLALLGELGAEAePAPPDRTLKDGDEL----------------DLGGGELEVIHTPGHTPGSIVL 124

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1331883511  654 HTSGWKVVYSGDTMPCEALVRMGKDATLLIHEATLED 690
Cdd:smart00849 125 YLPEGKILFTGDLLFAGGDGRTLVDGGDAAASDALES 161
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 511-724 2.37e-05

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: 46.15  E-value: 2.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883511 511 LLLDCGEGTFGQLcRHYGDQVDRVLGTLAAVFVSHLHADHHTGLLNIllqreralaslgKPLHPLLVIAP----SQLKAW 586
Cdd:pfam12706   3 ILIDPGPDLRQQA-LPALQPGRLRDDPIDAVLLTHDHYDHLAGLLDL------------REGRPRPLYAPlgvlAHLRRN 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883511 587 LQQYHNQCQEVLHHISMIPAKCLQ---EGAEISSLAVErlissllgtcdlegfQTCLVRHCKHAFGCA--LVHTSGWKVV 661
Cdd:pfam12706  70 FPYLFLLEHYGVRVHEIDWGESFTvgdGGLTVTATPAR---------------HGSPRGLDPNPGDTLgfRIEGPGKRVY 134

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331883511 662 YSGDTMPCEALV--RMGkDATLLIHEATLEDglEEEAVEKTHSTTSQAISVGMRMNAEFIMLNHF 724
Cdd:pfam12706 135 YAGDTGYFPDEIgeRLG-GADLLLLDGGAWR--DDEMIHMGHMTPEEAVEAAADLGARRKVLIHI 196
PRK02126 PRK02126
ribonuclease Z; Provisional
 655-729 4.47e-04

ribonuclease Z; Provisional


Pssm-ID: 235006 [Multi-domain]  Cd Length: 334  Bit Score: 43.37  E-value: 4.47e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1331883511 655 TSGWKVVYSGDTMP----CEALVRMGKDATLLIHEATLEDGLEEEAVEKTHSTTSQAISVGMRMNAEFIMLNHFSQRYA 729
Cdd:PRK02126  240 EPGQKIGYVTDIGYteenLARIVELAAGVDLLFIEAVFLDEDAEKARRKNHLTARQAGRLAREAGVKRLLPFHFSPRYQ 318
 
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 ...
 60-311 4.11e-115

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: 346.94  E-value: 4.11e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883511  60 LQVVAAGSRDSGAALYVFSEFNRYLFNCGEGVQRLMQEHKLKVARLDNIFLTRMHWSNVGGLSGMILTLKETGLPKCVLS 139
Cdd:cd16296     1 LQVVAAGSRDMGAALYVFSEYNRYLFNCGEGVQRLMQEHKLKVARLDNIFLTRMHWSNVGGLSGMILTLKETGLPKCVLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883511 140 GPpqlekyleaikifsgplkgiemavrphsapeykdetmtvyqipihseqkrgkhqpwqsperplgrlsperssdsesnE 219
Cdd:cd16296    81 GP-----------------------------------------------------------------------------N 83

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883511 220 NEPHLPHGVSQRRGARDSSLVVAFICKLHLKRGNFLVLKAKEMGLPVGTAAIAPIIAAVKDGKSITHEGREILAEELCTP 299
Cdd:cd16296    84 KQSPDKIGVRRQILERDPSLVVAFICKLHLKKGNFLVLKAKELGLPVGTAAIAPIIAAVKDGKSITFEGREILAEELCTP 163

                         250
                  ....*....|..
gi 1331883511 300 PDPGAAFVVVEC 311
Cdd:cd16296   164 PDPGIVFIVVEC 175
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 3.56e-101

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: 311.40  E-value: 3.56e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883511 482 IIFLGTGSAIPMKIRNVSATLVNISPNTSLLLDCGEGTFGQLCRHYGDQ-VDRVLGTLAAVFVSHLHADHHTGLLNILLQ 560
Cdd:cd07718     1 VVFLGTGSAIPSKYRNVSGILLRIPGDGSILLDCGEGTLGQLRRHYGPEeADEVLRNLKCIFISHLHADHHLGLIRLLAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883511 561 RERALAslgKPLHPLLVIAPSQLKAWLQQYHNQCQEVLHHISMIPAKCLQEGAEISSLAVERLISSLLGTCDLEGFQTCL 640
Cdd:cd07718    81 RKKLFK---PPSPPLYVVAPRQLRRWLREYSSLEDLGLHDISFISNRVSQSLPESDDPLSRDLLSNLLEELGLKSIETVP 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1331883511 641 VRHCKHAFGCALVHTSGWKVVYSGDTMPCEALVRMGKDATLLIHEAT 687
Cdd:cd07718   158 VIHCPDAYGIVLTHEDGWKIVYSGDTRPCEALVEAGKGADLLIHEAT 204
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
481-751 7.74e-50

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 175.77  E-value: 7.74e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883511 481 EIIFLGTGSAIPMKIRNVSATLVNIsPNTSLLLDCGEGTFGQLCRHYGDqvdrvLGTLAAVFVSHLHADHHTGLLNILLQ 560
Cdd:COG1234     2 KLTFLGTGGAVPTPGRATSSYLLEA-GGERLLIDCGEGTQRQLLRAGLD-----PRDIDAIFITHLHGDHIAGLPGLLST 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883511 561 ReralaSLGKPLHPLLVIAPSQLKAWLQQYHNQCQEVLH-HISMIPakcLQEGAEIsslaverlissllgtcDLEGFQ-- 637
Cdd:COG1234    76 R-----SLAGREKPLTIYGPPGTKEFLEALLKASGTDLDfPLEFHE---IEPGEVF----------------EIGGFTvt 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883511 638 TCLVRHCKHAFGcALVHTSGWKVVYSGDTMPCEALVRMGKDATLLIHEATLEDGLEEEAVEKTHSTTSQAISVGMRMNAE 717
Cdd:COG1234   132 AFPLDHPVPAYG-YRFEEPGRSLVYSGDTRPCEALVELAKGADLLIHEATFLDEEAELAKETGHSTAKEAAELAAEAGVK 210

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1331883511 718 FIMLNHFSQRYAKVPLF----SPNFNEKVGVAFDHMKV 751
Cdd:COG1234   211 RLVLTHFSPRYDDPEELlaeaRAVFPGPVELAEDGMVI 248
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 482-728 8.43e-47

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: 167.24  E-value: 8.43e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883511 482 IIFLGTGSAIPMKIRNVSATLVNIsPNTSLLLDCGEGTFGQLcRHYGdqvdRVLGTLAAVFVSHLHADHHTGLLNiLLQR 561
Cdd:cd07717     1 LTFLGTGSAVPTPERNLSSIALRL-EGELWLFDCGEGTQRQL-LRAG----LSPSKIDRIFITHLHGDHILGLPG-LLST 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883511 562 eralASLGKPLHPLLVIAPSQLKAWLQQYHNQCQEVLhhismipakclqeGAEIsslAVERLISSLLGTCDLEGFQ--TC 639
Cdd:cd07717    74 ----MSLLGRTEPLTIYGPKGLKEFLETLLRLSASRL-------------PYPI---EVHELEPDPGLVFEDDGFTvtAF 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883511 640 LVRHCKHAFGCALvhTSGWKVVYSGDTMPCEALVRMGKDATLLIHEATLEDGLEEEAVEKTHSTTSQAISVGMRMNAEFI 719
Cdd:cd07717   134 PLDHRVPCFGYRF--EEGRKIAYLGDTRPCEGLVELAKGADLLIHEATFLDDDAEKAKETGHSTAKQAAEIAKKAGVKKL 211


                  ....*....
gi 1331883511 720 MLNHFSQRY 728
Cdd:cd07717   212 VLTHFSARY 220
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 482-686 7.43e-42

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: 150.88  E-value: 7.43e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883511 482 IIFLGTGSAIPMKIRNVSATLVNIsPNTSLLLDCGEGTFGQLCRHYGDqvdrvLGTLAAVFVSHLHADHHTGLLNILLQR 561
Cdd:cd16272     1 LTFLGTGGAVPSLTRNTSSYLLET-GGTRILLDCGEGTVYRLLKAGVD-----PDKLDAIFLSHFHLDHIGGLPTLLFAR 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883511 562 EralasLGKPLHPLLVIAPSQLKAWLQQYHNQCQEVLHHISMIpakclqEGAEISSLAVERLISSLLgtcdlegFQTCLV 641
Cdd:cd16272    75 R-----YGGRKKPLTIYGPKGIKEFLEKLLNFPVEILPLGFPL------EIEELEEGGEVLELGDLK-------VEAFPV 136

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1331883511 642 RHCKHAFGCALVHTsGWKVVYSGDTMPCEALVRMGKDATLLIHEA 686
Cdd:cd16272   137 KHSVESLGYRIEAE-GKSIVYSGDTGPCENLVELAKGADLLIHEC 180
PRK00055 PRK00055
ribonuclease Z; Reviewed
 481-728 1.58e-38

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 144.55  E-value: 1.58e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883511 481 EIIFLGTGSAIPMKIRNVSATLVNIsPNTSLLLDCGEGTFGQLcRHYG---DQVDRVlgtlaavFVSHLHADHHTGLLNI 557
Cdd:PRK00055    3 ELTFLGTGSGVPTPTRNVSSILLRL-GGELFLFDCGEGTQRQL-LKTGikpRKIDKI-------FITHLHGDHIFGLPGL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883511 558 LLQReralaSLGKPLHPLLVIAPsqlkAWLQQYHNQCQEVLHHIS----------MIPA--------------KCLQEGA 613
Cdd:PRK00055   74 LSTR-----SLSGRTEPLTIYGP----KGIKEFVETLLRASGSLGyriaekdkpgKLDAeklkalgvppgplfGKLKRGE 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883511 614 EISsLAVERLISSLLGTCDlegfqtclVRHckhafgcalvhtsGWKVVYSGDTMPCEALVRMGKDATLLIHEATLEDGLE 693
Cdd:PRK00055  145 DVT-LEDGRIINPADVLGP--------PRK-------------GRKVAYCGDTRPCEALVELAKGADLLVHEATFGDEDE 202

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1331883511 694 EEAVEKTHSTTSQAISVGMRMNAEFIMLNHFSQRY 728
Cdd:PRK00055  203 ELAKEYGHSTARQAAEIAKEAGVKRLILTHFSPRY 237
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 481-728 1.72e-32

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: 128.11  E-value: 1.72e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883511 481 EIIFLGTGSAIPMKIRNVSATLVNIsPNTSLLLDCGEGTFGQLcRHYG---DQVDRVlgtlaavFVSHLHADHHTGLLNI 557
Cdd:TIGR02651   1 EITFLGTGGGVPTKERNLPSIALKL-NGELWLFDCGEGTQRQM-LRSGispMKIDRI-------FITHLHGDHILGLPGL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883511 558 LLQReralaSLGKPLHPLLVIAPSQLKAWLQqyhNQCQEVLHHISMIPakclqEGAEISSLAVERlissllgtcDLEGFQ 637
Cdd:TIGR02651  72 LSTM-----SFQGRKEPLTIYGPPGIKEFIE---TSLRVSYTYLNYPI-----KIHEIEEGGLVF---------EDDGFK 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883511 638 --TCLVRHCKHAFGCALV-------------------------------------------------HTSGWKVVYSGDT 666
Cdd:TIGR02651 130 veAFPLDHSIPSLGYRFEekdrpgkfdrekakelgippgplygklkrgetvtlidgriidpedvlgpPRKGRKIAYTGDT 209

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331883511 667 MPCEALVRMGKDATLLIHEATLEDGLEEEAVEKTHSTTSQAISVGMRMNAEFIMLNHFSQRY 728
Cdd:TIGR02651 210 RPCEEVIEFAKNADLLIHEATFLDEDKKLAKEYGHSTAAQAAEIAKEANVKRLILTHISPRY 271
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 481-684 9.55e-24

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: 99.51  E-value: 9.55e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883511 481 EIIFLGTGSAIPMKIRNVSATLVnISPNTSLLLDCGEGTFGQLCrhygdQVDRVLGTLAAVFVSHLHADHHTGLLNILLQ 560
Cdd:cd07719     1 RVTLLGTGGPIPDPDRAGPSTLV-VVGGRVYLVDAGSGVVRRLA-----QAGLPLGDLDAVFLTHLHSDHVADLPALLLT 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883511 561 ReralaSLGKPLHPLLVIAPSQLKAW---LQQYHNQCQEVLHHISMIPAkcLQEGAEISslAVErlISSLLGTCDLEGFQ 637
Cdd:cd07719    75 A-----WLAGRKTPLPVYGPPGTRALvdgLLAAYALDIDYRARIGDEGR--PDPGALVE--VHE--IAAGGVVYEDDGVK 143

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1331883511 638 --TCLVRH--CKHAFgcAL-VHTSGWKVVYSGDTMPCEALVRMGKDATLLIH 684
Cdd:cd07719   144 vtAFLVDHgpVPPAL--AYrFDTPGRSVVFSGDTGPSENLIELAKGADLLVH 193
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 506-686 1.61e-20

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


Pssm-ID: 293802 [Multi-domain]  Cd Length: 175  Bit Score: 89.42  E-value: 1.61e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883511 506 SPNTSLLLDCGEGTFGQLCRHygdqVDrvLGTLAAVFVSHLHADHHTGLlnILLQRERALASLGKPLHPLLVIAPSQLKA 585
Cdd:cd07716    25 ADGFRILLDCGSGVLSRLQRY----ID--PEDLDAVVLSHLHPDHCADL--GVLQYARRYHPRGARKPPLPLYGPAGPAE 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883511 586 WLQQ-YHNQCQEVLHHIsmipakclQEGAEISslaverlisslLGTCDLEGFQTclvrhcKHAFGCALVH-TSGWKV-VY 662
Cdd:cd07716    97 RLAAlYGLEDVFDFHPI--------EPGEPLE-----------IGPFTITFFRT------VHPVPCYAMRiEDGGKVlVY 151

                         170       180
                  ....*....|....*....|....
gi 1331883511 663 SGDTMPCEALVRMGKDATLLIHEA 686
Cdd:cd07716   152 TGDTGYCDELVEFARGADLLLCEA 175
Lactamase_B_4 pfam13691
tRNase Z endonuclease; This is family of tRNase Z enzymes, that are closely related ...
 61-120 2.96e-18

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: 79.17  E-value: 2.96e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1331883511  61 QVVAAGSRDS-GAALYVFSEFNRYLF-NCGEGVQRLMQEHKLKVARLDNIFLTRMH-WSNVGG 120
Cdd:pfam13691   1 QVVTTPTADTpGPLLLLHFDSKRYLFgNVGEGTQRALNEQKVRLSKLEDIFLTGKVsWSNIGG 63
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 483-686 2.85e-17

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: 80.77  E-value: 2.85e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883511 483 IFLGTGSAIPMKIRNVSATLVNISPnTSLLLDCGEGTFGQLCRhYGdqVDRVlgTLAAVFVSHLHADHHTGL----LNIL 558
Cdd:cd07740     1 TFLGSGDAFGSGGRLNTCFHVASEA-GRFLIDCGASSLIALKR-AG--IDPN--AIDAIFITHLHGDHFGGLpfflLDAQ 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883511 559 LQRERAlaslgkplHPLLVIAPSQLKAWLQQyhnqCQEVLH-HISMIPAKclqegAEISSLAVERLISSLLGTCDLEGFQ 637
Cdd:cd07740    75 FVAKRT--------RPLTIAGPPGLRERLRR----AMEALFpGSSKVPRR-----FDLEVIELEPGEPTTLGGVTVTAFP 137

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1331883511 638 tclVRHCKHAFGCALVHTSGWKVV-YSGDTMPCEALVRMGKDATLLIHEA 686
Cdd:cd07740   138 ---VVHPSGALPLALRLEAAGRVLaYSGDTEWTDALVPLARGADLFICEC 184
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 70-159 1.37e-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: 78.46  E-value: 1.37e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883511  70 SGAALYVFSEFNRYLFNCGEGVQRLMQEHKLKVARLDNIFLTRMHWSNVGGLSGMILTLKETGLPK-CVLSGPPQLEKYL 148
Cdd:cd16272    16 NTSSYLLETGGTRILLDCGEGTVYRLLKAGVDPDKLDAIFLSHFHLDHIGGLPTLLFARRYGGRKKpLTIYGPKGIKEFL 95

                          90
                  ....*....|.
gi 1331883511 149 EAIKIFSGPLK 159
Cdd:cd16272    96 EKLLNFPVEIL 106
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 481-751 6.02e-16

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 78.40  E-value: 6.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883511 481 EIIFLGTGSAIPM----------------KIRNVSATLVNiSPNTSLLLDCGEGtfgqlCRHYGDQVDRVLGTLAAVFVS 544
Cdd:COG1235     2 KVTFLGSGSSGGVpqigcdcpvcastdprYGRTRSSILVE-ADGTRLLIDAGPD-----LREQLLRLGLDPSKIDAILLT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883511 545 HLHADHHTGLLNIllqRERALAslgKPLHpllVIAPSQLKAWLQQYHNQCQEvlHHISMIPAKCLQEGAEISslaverli 624
Cdd:COG1235    76 HEHADHIAGLDDL---RPRYGP---NPIP---VYATPGTLEALERRFPYLFA--PYPGKLEFHEIEPGEPFE-------- 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883511 625 sslLGtcDLEgFQTCLVRH-CKHAFGCaLVHTSGWKVVYSGDT-MPCEALVRMGKDATLLIHEATLEDGleeeavEKTHS 702
Cdd:COG1235   137 ---IG--GLT-VTPFPVPHdAGDPVGY-RIEDGGKKLAYATDTgYIPEEVLELLRGADLLILDATYDDP------EPGHL 203

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1331883511 703 TTSQAISVGMRMNAEFIMLNHFSQRYAKVPLF-----SPNFNEKVGVAFDHMKV 751
Cdd:COG1235   204 SNEEALELLARLGPKRLVLTHLSPDNNDHELDydeleAALLPAGVEVAYDGMEI 257
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 81-187 9.56e-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: 9.56e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883511  81 NRYLFNCGEGVQRLMQEHKLKVARLDNIFLTRMHWSNVGGLSGMILTLKETGLPKCV-LSGPPQLEKYLEAIKIFSGPLK 159
Cdd:cd07717    27 ELWLFDCGEGTQRQLLRAGLSPSKIDRIFITHLHGDHILGLPGLLSTMSLLGRTEPLtIYGPKGLKEFLETLLRLSASRL 106

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1331883511 160 GIEMAVRPHSAPE---YKDETMTVYQIPI-HS 187
Cdd:cd07717   107 PYPIEVHELEPDPglvFEDDGFTVTAFPLdHR 138
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
82-180 6.74e-12

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 66.37  E-value: 6.74e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883511  82 RYLFNCGEGVQRLMQEHKLKVARLDNIFLTRMHWSNVGGLSGMILTLKETGLPK-CVLSGPPQLEKYLEAIKIFSGPLKG 160
Cdd:COG1234    30 RLLIDCGEGTQRQLLRAGLDPRDIDAIFITHLHGDHIAGLPGLLSTRSLAGREKpLTIYGPPGTKEFLEALLKASGTDLD 109

                          90       100
                  ....*....|....*....|.
gi 1331883511 161 IEMAVRPHSAPE-YKDETMTV 180
Cdd:COG1234   110 FPLEFHEIEPGEvFEIGGFTV 130
PRK00055 PRK00055
ribonuclease Z; Reviewed
 83-158 1.68e-07

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 53.65  E-value: 1.68e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331883511  83 YLFNCGEGVQRLMQEHKLKVARLDNIFLTRMHWSNVGGLSGMILTLKETGLPKCV-LSGPPQLEKYLEAIKIFSGPL 158
Cdd:PRK00055   32 FLFDCGEGTQRQLLKTGIKPRKIDKIFITHLHGDHIFGLPGLLSTRSLSGRTEPLtIYGPKGIKEFVETLLRASGSL 108
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 499-690 2.26e-06

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: 48.70  E-value: 2.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883511  499 SATLVnISPNTSLLLDCGEGT----FGQLCRHYGDQVDrvlgtlaAVFVSHLHADhHTGLLNILLQRERAlaslgkplhp 574
Cdd:smart00849   1 NSYLV-RDDGGAILIDTGPGEaedlLAELKKLGPKKID-------AIILTHGHPD-HIGGLPELLEAPGA---------- 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883511  575 lLVIAPSQLKAWLQQYHNQCQEVLHHI-SMIPAKCLQEGAEIsslaverlissllgtcDLEGFQTCLVRHCKHAFGCALV 653
Cdd:smart00849  62 -PVYAPEGTAELLKDLLALLGELGAEAePAPPDRTLKDGDEL----------------DLGGGELEVIHTPGHTPGSIVL 124

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1331883511  654 HTSGWKVVYSGDTMPCEALVRMGKDATLLIHEATLED 690
Cdd:smart00849 125 YLPEGKILFTGDLLFAGGDGRTLVDGGDAAASDALES 161
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 511-724 2.37e-05

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: 46.15  E-value: 2.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883511 511 LLLDCGEGTFGQLcRHYGDQVDRVLGTLAAVFVSHLHADHHTGLLNIllqreralaslgKPLHPLLVIAP----SQLKAW 586
Cdd:pfam12706   3 ILIDPGPDLRQQA-LPALQPGRLRDDPIDAVLLTHDHYDHLAGLLDL------------REGRPRPLYAPlgvlAHLRRN 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883511 587 LQQYHNQCQEVLHHISMIPAKCLQ---EGAEISSLAVErlissllgtcdlegfQTCLVRHCKHAFGCA--LVHTSGWKVV 661
Cdd:pfam12706  70 FPYLFLLEHYGVRVHEIDWGESFTvgdGGLTVTATPAR---------------HGSPRGLDPNPGDTLgfRIEGPGKRVY 134

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331883511 662 YSGDTMPCEALV--RMGkDATLLIHEATLEDglEEEAVEKTHSTTSQAISVGMRMNAEFIMLNHF 724
Cdd:pfam12706 135 YAGDTGYFPDEIgeRLG-GADLLLLDGGAWR--DDEMIHMGHMTPEEAVEAAADLGARRKVLIHI 196
metallo-hydrolase-like_MBL-fold cd07741
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 482-683 4.58e-05

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: 45.26  E-value: 4.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883511 482 IIFLGTGSAipmkiRNVSATLVNIS-------PNTSLLLDCGEGTFGQLCRHYGDQVDrvlgtLAAVFVSHLHADHHTGl 554
Cdd:cd07741     1 IIFLGTGGG-----RFVVITQLRASggiwielNGKNIHIDPGPGALVRMCRPKLDPTK-----LDAIILSHRHLDHSND- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883511 555 LNILLQrerALASLGKPlHPLLVIAPSQ--------LKAWLQQYhnqCQEVLHhismipakcLQEGAEISslaverliss 626
Cdd:cd07741    70 ANVLIE---AMTEGGFK-KRGTLLAPEDalngepvvLLYYHRRK---LEEIEI---------LEEGDEYE---------- 123

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1331883511 627 lLGtcDLEGFQTCLVRHCKHAFGcALVHTSGWKVVYSGDTMPCEALVRMGKDATLLI 683
Cdd:cd07741   124 -LG--GIKIEATRHKHSDPTTYG-FIFRTSDKKIGYISDTRYFEELIEYYSNCDVLI 176
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 52-151 2.51e-04

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: 42.89  E-value: 2.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883511  52 SGGPntvylqvVAAGSRdSGAALYVFSEFNRYLFNCGEGVQRLMQEHKLKVARLDNIFLTRMHWSNVGGLSGMILTLKET 131
Cdd:cd07719     7 TGGP-------IPDPDR-AGPSTLVVVGGRVYLVDAGSGVVRRLAQAGLPLGDLDAVFLTHLHSDHVADLPALLLTAWLA 78

                          90       100
                  ....*....|....*....|.
gi 1331883511 132 GLPKCV-LSGPPQLEKYLEAI 151
Cdd:cd07719    79 GRKTPLpVYGPPGTRALVDGL 99
PRK02126 PRK02126
ribonuclease Z; Provisional
 655-729 4.47e-04

ribonuclease Z; Provisional


Pssm-ID: 235006 [Multi-domain]  Cd Length: 334  Bit Score: 43.37  E-value: 4.47e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1331883511 655 TSGWKVVYSGDTMP----CEALVRMGKDATLLIHEATLEDGLEEEAVEKTHSTTSQAISVGMRMNAEFIMLNHFSQRYA 729
Cdd:PRK02126  240 EPGQKIGYVTDIGYteenLARIVELAAGVDLLFIEAVFLDEDAEKARRKNHLTARQAGRLAREAGVKRLLPFHFSPRYQ 318
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 502-674 1.61e-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: 40.35  E-value: 1.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883511 502 LVNISPNTSLLLDCGEGTFGQLCRHygdqVDRVLGTLAAVFVSHLHADhHTGLLNILLQRERAlaslgkPlhpllVIAPS 581
Cdd:cd06262    14 LVSDEEGEAILIDPGAGALEKILEA----IEELGLKIKAILLTHGHFD-HIGGLAELKEAPGA------P-----VYIHE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883511 582 QLKAWLQQYHNQCQEVL--HHISMIPAKCLQEGAEISslaverlisslLGTCDLEgfqtclVRHCK-HAFGCALVHTSGW 658
Cdd:cd06262    78 ADAELLEDPELNLAFFGggPLPPPEPDILLEDGDTIE-----------LGGLELE------VIHTPgHTPGSVCFYIEEE 140

                         170
                  ....*....|....*.
gi 1331883511 659 KVVYSGDTMPCEALVR 674
Cdd:cd06262   141 GVLFTGDTLFAGSIGR 156
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 481-550 3.36e-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: 39.38  E-value: 3.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883511 481 EIIFLGTGSA--IPM---------------KIRNVSAtLVNIsPNTSLLLDCGEgTF-GQLCRHYGDQVDrvlgtlaAVF 542
Cdd:cd16279     2 KLTFLGTGTSsgVPVigcdcgvcdssdpknRRLRSSI-LIET-GGKNILIDTGP-DFrQQALRAGIRKLD-------AVL 71


                  ....*...
gi 1331883511 543 VSHLHADH 550
Cdd:cd16279    72 LTHAHADH 79
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 482-555 3.66e-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: 39.36  E-value: 3.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883511 482 IIFLG-----TGSAIpmkirnvsatLVNIsPNTSLLLDCGegTF---GQLCRHYGDQVDRVLGTLAAVFVSHLHADhHTG 553
Cdd:cd16295     1 LTFLGaarevTGSCY----------LLET-GGKRILLDCG--LFqggKELEELNNEPFPFDPKEIDAVILTHAHLD-HSG 66


                  ..
gi 1331883511 554 LL 555
Cdd:cd16295    67 RL 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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