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Conserved domains on  [gi|2019657023|gb|QTI13831|]
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ribonuclease Z [Klebsiella variicola]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 11440933)

MBL fold metallo-hydrolase similar to Methanopyrus kandleri ribonuclease Z

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
1-240 1.23e-38

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


:

Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 134.94  E-value: 1.23e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019657023   1 MLGCGSAF-SCTQNTSALrVIDADNKQWLIDCGPTVPRALWQRGGGVNDIDAIYFTHVHPDHCTGLTALLNYWKSGSRQK 79
Cdd:COG1234     5 FLGTGGAVpTPGRATSSY-LLEAGGERLLIDCGEGTQRQLLRAGLDPRDIDAIFITHLHGDHIAGLPGLLSTRSLAGREK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019657023  80 PLIIYCQPAQQPVlmqLAALANWPQADPGFTIDWQECREAWTWQ--DWQIRTAATQHELSNRAIRITIAGQTLFYSGDGR 157
Cdd:COG1234    84 PLTIYGPPGTKEF---LEALLKASGTDLDFPLEFHEIEPGEVFEigGFTVTAFPLDHPVPAYGYRFEEPGRSLVYSGDTR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019657023 158 PTADSIALMAGAGLAFQECASVAALDDDAsHGDFPSC----LMLFRTLQLPALGLYH---CEDAALSALKQTCQPWQG-L 229
Cdd:COG1234   161 PCEALVELAKGADLLIHEATFLDEEAELA-KETGHSTakeaAELAAEAGVKRLVLTHfspRYDDPEELLAEARAVFPGpV 239

                         250
                  ....*....|.
gi 2019657023 230 FVSQDGDHFTL 240
Cdd:COG1234   240 ELAEDGMVIEL 250
 
Name Accession Description Interval E-value
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
1-240 1.23e-38

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 134.94  E-value: 1.23e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019657023   1 MLGCGSAF-SCTQNTSALrVIDADNKQWLIDCGPTVPRALWQRGGGVNDIDAIYFTHVHPDHCTGLTALLNYWKSGSRQK 79
Cdd:COG1234     5 FLGTGGAVpTPGRATSSY-LLEAGGERLLIDCGEGTQRQLLRAGLDPRDIDAIFITHLHGDHIAGLPGLLSTRSLAGREK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019657023  80 PLIIYCQPAQQPVlmqLAALANWPQADPGFTIDWQECREAWTWQ--DWQIRTAATQHELSNRAIRITIAGQTLFYSGDGR 157
Cdd:COG1234    84 PLTIYGPPGTKEF---LEALLKASGTDLDFPLEFHEIEPGEVFEigGFTVTAFPLDHPVPAYGYRFEEPGRSLVYSGDTR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019657023 158 PTADSIALMAGAGLAFQECASVAALDDDAsHGDFPSC----LMLFRTLQLPALGLYH---CEDAALSALKQTCQPWQG-L 229
Cdd:COG1234   161 PCEALVELAKGADLLIHEATFLDEEAELA-KETGHSTakeaAELAAEAGVKRLVLTHfspRYDDPEELLAEARAVFPGpV 239

                         250
                  ....*....|.
gi 2019657023 230 FVSQDGDHFTL 240
Cdd:COG1234   240 ELAEDGMVIEL 250
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 2-176 6.80e-33

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: 117.75  E-value: 6.80e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019657023   2 LGCGSAF-SCTQNTSALrVIDADNKQWLIDCGPTVPRALWQRGGGVNDIDAIYFTHVHPDHCTGLTALLNYWKSGSRQKP 80
Cdd:cd16272     4 LGTGGAVpSLTRNTSSY-LLETGGTRILLDCGEGTVYRLLKAGVDPDKLDAIFLSHFHLDHIGGLPTLLFARRYGGRKKP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019657023  81 LIIYCQPAQQPVLMQLAALANWPqADPGFTIDWQECREAWTWQ---DWQIRTAATQHELSNRAIRITIAGQTLFYSGDGR 157
Cdd:cd16272    83 LTIYGPKGIKEFLEKLLNFPVEI-LPLGFPLEIEELEEGGEVLelgDLKVEAFPVKHSVESLGYRIEAEGKSIVYSGDTG 161

                         170
                  ....*....|....*....
gi 2019657023 158 PTADSIALMAGAGLAFQEC 176
Cdd:cd16272   162 PCENLVELAKGADLLIHEC 180
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 2-84 8.62e-13

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: 66.47  E-value: 8.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019657023   2 LGCGSAF-SCTQNTSALrVIDADNKQWLIDCGPTVPRALWQRGGGVNDIDAIYFTHVHPDHCTGLTALLNYWKSGSRQKP 80
Cdd:TIGR02651   5 LGTGGGVpTKERNLPSI-ALKLNGELWLFDCGEGTQRQMLRSGISPMKIDRIFITHLHGDHILGLPGLLSTMSFQGRKEP 83


                  ....
gi 2019657023  81 LIIY 84
Cdd:TIGR02651  84 LTIY 87
PRK00055 PRK00055
ribonuclease Z; Reviewed
 2-84 4.05e-11

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 61.35  E-value: 4.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019657023   2 LGCGSAF-SCTQNTSALrVIDADNKQWLIDCGPTVPRALWQRGGGVNDIDAIYFTHVHPDHCTGLTALL-NYWKSGsRQK 79
Cdd:PRK00055    7 LGTGSGVpTPTRNVSSI-LLRLGGELFLFDCGEGTQRQLLKTGIKPRKIDKIFITHLHGDHIFGLPGLLsTRSLSG-RTE 84


                  ....*
gi 2019657023  80 PLIIY 84
Cdd:PRK00055   85 PLTIY 89
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 28-173 7.50e-09

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: 53.85  E-value: 7.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019657023  28 LIDCGPTV----PRALWQRGGGVNDIDAIYFTHVHPDHCTGLTALLnywksgsRQKPLIIYCQPAQQPVLMQLAALANWP 103
Cdd:pfam12706   4 LIDPGPDLrqqaLPALQPGRLRDDPIDAVLLTHDHYDHLAGLLDLR-------EGRPRPLYAPLGVLAHLRRNFPYLFLL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019657023 104 QADP--GFTIDWQECREAwTWQDWQIRTAATQHELSNRAI---------RITIAGQTLFYSGD-GRPTADSIALMAGAGL 171
Cdd:pfam12706  77 EHYGvrVHEIDWGESFTV-GDGGLTVTATPARHGSPRGLDpnpgdtlgfRIEGPGKRVYYAGDtGYFPDEIGERLGGADL 155


                  ..
gi 2019657023 172 AF 173
Cdd:pfam12706 156 LL 157
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 19-73 1.33e-07

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: 50.24  E-value: 1.33e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2019657023   19 VIDADNKQWLIDCGPTVPRAL--WQRGGGVNDIDAIYFTHVHPDHCTGLTALLNYWK 73
Cdd:smart00849   4 LVRDDGGAILIDTGPGEAEDLlaELKKLGPKKIDAIILTHGHPDHIGGLPELLEAPG 60
 
Name Accession Description Interval E-value
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
1-240 1.23e-38

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 134.94  E-value: 1.23e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019657023   1 MLGCGSAF-SCTQNTSALrVIDADNKQWLIDCGPTVPRALWQRGGGVNDIDAIYFTHVHPDHCTGLTALLNYWKSGSRQK 79
Cdd:COG1234     5 FLGTGGAVpTPGRATSSY-LLEAGGERLLIDCGEGTQRQLLRAGLDPRDIDAIFITHLHGDHIAGLPGLLSTRSLAGREK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019657023  80 PLIIYCQPAQQPVlmqLAALANWPQADPGFTIDWQECREAWTWQ--DWQIRTAATQHELSNRAIRITIAGQTLFYSGDGR 157
Cdd:COG1234    84 PLTIYGPPGTKEF---LEALLKASGTDLDFPLEFHEIEPGEVFEigGFTVTAFPLDHPVPAYGYRFEEPGRSLVYSGDTR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019657023 158 PTADSIALMAGAGLAFQECASVAALDDDAsHGDFPSC----LMLFRTLQLPALGLYH---CEDAALSALKQTCQPWQG-L 229
Cdd:COG1234   161 PCEALVELAKGADLLIHEATFLDEEAELA-KETGHSTakeaAELAAEAGVKRLVLTHfspRYDDPEELLAEARAVFPGpV 239

                         250
                  ....*....|.
gi 2019657023 230 FVSQDGDHFTL 240
Cdd:COG1234   240 ELAEDGMVIEL 250
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 2-176 6.80e-33

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: 117.75  E-value: 6.80e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019657023   2 LGCGSAF-SCTQNTSALrVIDADNKQWLIDCGPTVPRALWQRGGGVNDIDAIYFTHVHPDHCTGLTALLNYWKSGSRQKP 80
Cdd:cd16272     4 LGTGGAVpSLTRNTSSY-LLETGGTRILLDCGEGTVYRLLKAGVDPDKLDAIFLSHFHLDHIGGLPTLLFARRYGGRKKP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019657023  81 LIIYCQPAQQPVLMQLAALANWPqADPGFTIDWQECREAWTWQ---DWQIRTAATQHELSNRAIRITIAGQTLFYSGDGR 157
Cdd:cd16272    83 LTIYGPKGIKEFLEKLLNFPVEI-LPLGFPLEIEELEEGGEVLelgDLKVEAFPVKHSVESLGYRIEAEGKSIVYSGDTG 161

                         170
                  ....*....|....*....
gi 2019657023 158 PTADSIALMAGAGLAFQEC 176
Cdd:cd16272   162 PCENLVELAKGADLLIHEC 180
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 28-171 1.18e-21

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


Pssm-ID: 293802 [Multi-domain]  Cd Length: 175  Bit Score: 88.27  E-value: 1.18e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019657023  28 LIDCGPTVPRALWQRGGgVNDIDAIYFTHVHPDHCTGLTALLNYWK---SGSRQKPLIIYCqPAQQPVLmqLAALANWPQ 104
Cdd:cd07716    31 LLDCGSGVLSRLQRYID-PEDLDAVVLSHLHPDHCADLGVLQYARRyhpRGARKPPLPLYG-PAGPAER--LAALYGLED 106

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2019657023 105 AdpgFT-IDWQEcREAWTWQDWQIRTAATQHELSNRAIRITIAGQTLFYSGDGRPTADSIALMAGAGL 171
Cdd:cd07716   107 V---FDfHPIEP-GEPLEIGPFTITFFRTVHPVPCYAMRIEDGGKVLVYTGDTGYCDELVEFARGADL 170
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 2-176 4.02e-19

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: 82.31  E-value: 4.02e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019657023   2 LGCGSAFSCTQNTSALRVIDADNKQWLIDCGPTVPRALWQRGGGVNDIDAIYFTHVHPDHCTGLTA-LLNYWKSGSRQKP 80
Cdd:cd07740     3 LGSGDAFGSGGRLNTCFHVASEAGRFLIDCGASSLIALKRAGIDPNAIDAIFITHLHGDHFGGLPFfLLDAQFVAKRTRP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019657023  81 LIIYCQPAQQPVLMQL--AALANWPQADPGFTIDWQECREAWTWQ--DWQIRTAATQHelSNRA----IRITIAGQTLFY 152
Cdd:cd07740    83 LTIAGPPGLRERLRRAmeALFPGSSKVPRRFDLEVIELEPGEPTTlgGVTVTAFPVVH--PSGAlplaLRLEAAGRVLAY 160

                         170       180
                  ....*....|....*....|....
gi 2019657023 153 SGDGRPTADSIALMAGAGLAFQEC 176
Cdd:cd07740   161 SGDTEWTDALVPLARGADLFICEC 184
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 2-240 2.14e-17

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 78.78  E-value: 2.14e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019657023   2 LGCGSAFSCTQ-----------------NTSALrVIDADNKQWLIDCGPTVpRALWQRGG-GVNDIDAIYFTHVHPDHCT 63
Cdd:COG1235     6 LGSGSSGGVPQigcdcpvcastdprygrTRSSI-LVEADGTRLLIDAGPDL-REQLLRLGlDPSKIDAILLTHEHADHIA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019657023  64 GLTALLNYWksgsRQKPLIIYCQPAqqpVLMQLAalANWPQADPGF--TIDWQECR--EAWTWQDWQIRTAATQHElSNR 139
Cdd:COG1235    84 GLDDLRPRY----GPNPIPVYATPG---TLEALE--RRFPYLFAPYpgKLEFHEIEpgEPFEIGGLTVTPFPVPHD-AGD 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019657023 140 AI--RITIAGQTLFYSGD-GRPTADSIALMAGAGLAFQECASVaalDDDASHGDFPSCLMLFRTLQLPALGLYH------ 210
Cdd:COG1235   154 PVgyRIEDGGKKLAYATDtGYIPEEVLELLRGADLLILDATYD---DPEPGHLSNEEALELLARLGPKRLVLTHlspdnn 230

                         250       260       270
                  ....*....|....*....|....*....|
gi 2019657023 211 CEDAALSALKQTCQPwQGLFVSQDGDHFTL 240
Cdd:COG1235   231 DHELDYDELEAALLP-AGVEVAYDGMEIEL 259
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 19-169 2.29e-16

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: 74.86  E-value: 2.29e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019657023  19 VIDADNKQWLIDCGPTVPRALWQRGGGVNDIDAIYFTHVHPDHCTGLTALL-NYWKSGsRQKPLIIYCQPAQQPV----- 92
Cdd:cd07719    22 LVVVGGRVYLVDAGSGVVRRLAQAGLPLGDLDAVFLTHLHSDHVADLPALLlTAWLAG-RKTPLPVYGPPGTRALvdgll 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019657023  93 -LMQLAALANWPQAD-----PGFTIDWQECREAWTW---QDWQIRTAATQHELSNRAI--RITIAGQTLFYSGDGRPTAD 161
Cdd:cd07719   101 aAYALDIDYRARIGDegrpdPGALVEVHEIAAGGVVyedDGVKVTAFLVDHGPVPPALayRFDTPGRSVVFSGDTGPSEN 180


                  ....*...
gi 2019657023 162 SIALMAGA 169
Cdd:cd07719   181 LIELAKGA 188
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 2-169 3.83e-15

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: 72.48  E-value: 3.83e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019657023   2 LGCGSAF-SCTQNTSALrVIDADNKQWLIDCGPTVPRALWQRGGGVNDIDAIYFTHVHPDHCTGLTALLNYWKSGSRQKP 80
Cdd:cd07717     4 LGTGSAVpTPERNLSSI-ALRLEGELWLFDCGEGTQRQLLRAGLSPSKIDRIFITHLHGDHILGLPGLLSTMSLLGRTEP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019657023  81 LIIYcqpAQQPVLMQLAALANWPQADPGFTIDWQECREAWT----WQDWQIRTAATQHELSNRAIRITIaGQTLFYSGDG 156
Cdd:cd07717    83 LTIY---GPKGLKEFLETLLRLSASRLPYPIEVHELEPDPGlvfeDDGFTVTAFPLDHRVPCFGYRFEE-GRKIAYLGDT 158

                         170
                  ....*....|...
gi 2019657023 157 RPTADSIALMAGA 169
Cdd:cd07717   159 RPCEGLVELAKGA 171
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 2-84 8.62e-13

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: 66.47  E-value: 8.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019657023   2 LGCGSAF-SCTQNTSALrVIDADNKQWLIDCGPTVPRALWQRGGGVNDIDAIYFTHVHPDHCTGLTALLNYWKSGSRQKP 80
Cdd:TIGR02651   5 LGTGGGVpTKERNLPSI-ALKLNGELWLFDCGEGTQRQMLRSGISPMKIDRIFITHLHGDHILGLPGLLSTMSFQGRKEP 83


                  ....
gi 2019657023  81 LIIY 84
Cdd:TIGR02651  84 LTIY 87
PRK00055 PRK00055
ribonuclease Z; Reviewed
 2-84 4.05e-11

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 61.35  E-value: 4.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019657023   2 LGCGSAF-SCTQNTSALrVIDADNKQWLIDCGPTVPRALWQRGGGVNDIDAIYFTHVHPDHCTGLTALL-NYWKSGsRQK 79
Cdd:PRK00055    7 LGTGSGVpTPTRNVSSI-LLRLGGELFLFDCGEGTQRQLLKTGIKPRKIDKIFITHLHGDHIFGLPGLLsTRSLSG-RTE 84


                  ....*
gi 2019657023  80 PLIIY 84
Cdd:PRK00055   85 PLTIY 89
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 13-128 2.16e-09

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: 55.56  E-value: 2.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019657023  13 NTSALrvIDADNKQWLIDCGPTVPRALWQRGggVNDIDAIYFTHVHPDHCTGLTAL--LNYWksgsRQKPLIIYCQPAQQ 90
Cdd:cd16279    35 RSSIL--IETGGKNILIDTGPDFRQQALRAG--IRKLDAVLLTHAHADHIHGLDDLrpFNRL----QQRPIPVYASEETL 106

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2019657023  91 PVLMQLAALANWPQADPGF-TIDWQECR--EAWTWQDWQIR 128
Cdd:cd16279   107 DDLKRRFPYFFAATGGGGVpKLDLHIIEpdEPFTIGGLEIT 147
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 28-173 7.50e-09

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: 53.85  E-value: 7.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019657023  28 LIDCGPTV----PRALWQRGGGVNDIDAIYFTHVHPDHCTGLTALLnywksgsRQKPLIIYCQPAQQPVLMQLAALANWP 103
Cdd:pfam12706   4 LIDPGPDLrqqaLPALQPGRLRDDPIDAVLLTHDHYDHLAGLLDLR-------EGRPRPLYAPLGVLAHLRRNFPYLFLL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019657023 104 QADP--GFTIDWQECREAwTWQDWQIRTAATQHELSNRAI---------RITIAGQTLFYSGD-GRPTADSIALMAGAGL 171
Cdd:pfam12706  77 EHYGvrVHEIDWGESFTV-GDGGLTVTATPARHGSPRGLDpnpgdtlgfRIEGPGKRVYYAGDtGYFPDEIGERLGGADL 155


                  ..
gi 2019657023 172 AF 173
Cdd:pfam12706 156 LL 157
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 19-155 2.61e-08

DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 441904 [Multi-domain]  Cd Length: 253  Bit Score: 52.94  E-value: 2.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019657023  19 VIDADNKQWLIDCGP---------TVPRALWQRGggVNDIDAIYFTHVHPDHCTGLTALLNYWKSGSrqkplIIYCQPAQ 89
Cdd:COG2333    16 IRTPDGKTILIDTGPrpsfdagerVVLPYLRALG--IRRLDLLVLTHPDADHIGGLAAVLEAFPVGR-----VLVSGPPD 88

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2019657023  90 QPVLMQ--LAALANWPqadpgftIDWQECR--EAWTWQDWQIR-----TAATQHELSNRA---IRITIAGQTLFYSGD 155
Cdd:COG2333    89 TSETYErlLEALKEKG-------IPVRPCRagDTWQLGGVRFEvlwppEDLLEGSDENNNslvLRLTYGGFSFLLTGD 159
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 19-73 1.33e-07

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: 50.24  E-value: 1.33e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2019657023   19 VIDADNKQWLIDCGPTVPRAL--WQRGGGVNDIDAIYFTHVHPDHCTGLTALLNYWK 73
Cdd:smart00849   4 LVRDDGGAILIDTGPGEAEDLlaELKKLGPKKIDAIILTHGHPDHIGGLPELLEAPG 60
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
28-155 7.31e-07

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 48.52  E-value: 7.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019657023  28 LIDCGPTVPRA----LWQRGGGVNDIDAIYFTHVHPDHCTGLTALLNYW--KSGSRQKPLIIYCQPAQQPVLMQLAALAN 101
Cdd:pfam00753  19 LIDTGGSAEAAllllLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATdvPVIVVAEEARELLDEELGLAASRLGLPGP 98

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2019657023 102 WPQADPGFTIDWQECREAWTWQDWQIRTAATQHELSnraIRITIAGQTLFYSGD 155
Cdd:pfam00753  99 PVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGH---VVVYYGGGKVLFTGD 149
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 19-73 1.11e-06

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


Pssm-ID: 293792 [Multi-domain]  Cd Length: 188  Bit Score: 47.67  E-value: 1.11e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2019657023  19 VIDADNKQWLIDCGPTVPRALWQRGGGVN-DIDAIYFTHVHPDHCTGLTALLNYWK 73
Cdd:cd06262    15 VSDEEGEAILIDPGAGALEKILEAIEELGlKIKAILLTHGHFDHIGGLAELKEAPG 70
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 19-66 1.11e-05

Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold metallo hydrolase domain; Pseudomonas pseudoalcaligenes OPHC2 is a thermostable organophosphorus hydrolase which a broad substrate activity spectrum: it hydrolyzes various phosphotriesters, esters, and a lactone. This subgroup also includes Pseudomonas oleovorans PoOPH which exhibits high lactonase and esterase activities, and latent PTE activity. However, double mutations His250Ile/Ile263Trp switch PoOPH into an efficient and thermostable PTE. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293806 [Multi-domain]  Cd Length: 251  Bit Score: 45.23  E-value: 1.11e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2019657023  19 VIDADNKQWLIDCG------PT---VPRALwqRGGGVN--DIDAIYFTHVHPDHCTGLT 66
Cdd:cd07720    53 LVRTGGRLILVDTGagglfgPTagkLLANL--AAAGIDpeDIDDVLLTHLHPDHIGGLV 109
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 15-87 1.13e-05

Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, and related proteins; MBL-fold metallo hydrolase domain; This subgroup includes Methanocaldococcus jannaschii 7,8-dihydropterin-6-methyl-4-(beta-D-ribofuranosyl)-aminobenzene-5'-phosphate synthase (EC 2.5.1.15), a folate biosynthetic enzyme also known as dihydropteroate synthase and 7,8 dihydropteroate synthase. Thermoanaerobacter tengcongensis Tflp is a ferredoxin-like member. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293799  Cd Length: 269  Bit Score: 45.31  E-value: 1.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019657023  15 SALrvIDADNKQWLIDCGPTVP-----RALwqrggGVN--DIDAIYFTHVHPDHCTGLTALLNYWksgsrqKPLIIYCQP 87
Cdd:cd07713    22 SLL--IETEGKKILFDTGQSGVllhnaKKL-----GIDlsDIDAVVLSHGHYDHTGGLKALLELN------PKAPVYAHP 88
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 1-111 2.41e-05

Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];


Pssm-ID: 440257 [Multi-domain]  Cd Length: 215  Bit Score: 43.91  E-value: 2.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019657023   1 MLGCGSAFSCTQNTSALrvIDADNKQWLIDCGPTVP------RALWQRGGgvnDIDAIYFTHVHPDHCTGLTALLNYWks 74
Cdd:COG0491     3 VLPGGTPGAGLGVNSYL--IVGGDGAVLIDTGLGPAdaeallAALAALGL---DIKAVLLTHLHPDHVGGLAALAEAF-- 75

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2019657023  75 GSRqkpliIYCQPAQQPVLMQLAALANWPQADPGFTI 111
Cdd:COG0491    76 GAP-----VYAHAAEAEALEAPAAGALFGREPVPPDR 107
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 19-82 3.17e-05

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


Pssm-ID: 293807 [Multi-domain]  Cd Length: 202  Bit Score: 43.75  E-value: 3.17e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2019657023  19 VIDADNKQWLIDCG-----PTVPRALWQRGGGVNDIDAIYFTHVHPDHCTGLTALLNYWK----SGSRQKPLI 82
Cdd:cd07721    15 LIEDDDGLTLIDTGlpgsaKRILKALRELGLSPKDIRRILLTHGHIDHIGSLAALKEAPGapvyAHEREAPYL 87
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 19-73 3.64e-05

Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This subgroup includes proteins required for natural transformation competence including Neisseria gonorrhoeae ComA, Pseudomonas stutzeri ComA, Bacillus subtilis ComEC (also known as ComE operon protein 3) and Haemophilus influenza ORF2 encoded by the rec-2 gene, as well as Escherichia coli YcaI which does not mediate spontaneous plasmid transformation on nutrient-containing agar plates. It also includes the phosphorylcholine esterase (Pce) domain of choline-binding protein e from streptococcus pneumonia. 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: 293817 [Multi-domain]  Cd Length: 179  Bit Score: 43.28  E-value: 3.64e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2019657023  19 VIDADNKQWLIDCGPTVPRA-------LWQRGggVNDIDAIYFTHVHPDHCTGLTALLNYWK 73
Cdd:cd07731    14 LIQTPGKTILIDTGPRDSFGedvvvpyLKARG--IKKLDYLILTHPDADHIGGLDAVLKNFP 73
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 2-134 5.94e-05

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


Pssm-ID: 293819 [Multi-domain]  Cd Length: 151  Bit Score: 42.25  E-value: 5.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019657023   2 LGCGSAFSCTqntsalrVIDADNKQWLIDCG---PTVPRALWQRGGGVNDIDAIYFTHVHPDHCTGLTALlnywksgSRQ 78
Cdd:cd07733     3 LASGSKGNCT-------YLETEDGKLLIDAGlsgRKITGRLAEIGRDPEDIDAILVTHEHADHIKGLGVL-------ARK 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2019657023  79 KPLIIYCQPAqqpvlmQLAALANWPQADPGFTIDWQECREAWTWQDWQIRTAATQH 134
Cdd:cd07733    69 YNVPIYATAG------TLRAMERKVGLIDVDQKQIFEPGETFSIGDFDVESFGVSH 118
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 19-155 6.32e-05

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 42.98  E-value: 6.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019657023  19 VIDADNKQWLID------CGPTVPRALwqRGGGVNDIDAIYFTHVHPDHC--TGLTALlnywksgsRQKPLIIYCQPaqq 90
Cdd:COG2220    15 LIETGGKRILIDpvfsgrASPVNPLPL--DPEDLPKIDAVLVTHDHYDHLddATLRAL--------KRTGATVVAPL--- 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2019657023  91 pvlmqlaALANWPQADpGFT----IDWqecREAWTWQDWQIRTAATQHElSNRAIR---------ITIAGQTLFYSGD 155
Cdd:COG2220    82 -------GVAAWLRAW-GFPrvteLDW---GESVELGGLTVTAVPARHS-SGRPDRngglwvgfvIETDGKTIYHAGD 147
PhnP-like_MBL-fold cd07736
phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase ...
 14-90 9.11e-05

phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase domain; Escherichia coli PhnP catalyzes the hydrolysis of 5-phospho-D-ribose-1,2-cyclic phosphate to D-ribose-1,5-bisphosphate, a step in the C-P lyase pathway. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293822 [Multi-domain]  Cd Length: 186  Bit Score: 42.22  E-value: 9.11e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2019657023  14 TSALrvIDADNKQWLIDCGPTvprALWQRGGGVnDIDAIYFTHVHPDHCTGLTALlnYWKSGsrqKPLIIYCQPAQQ 90
Cdd:cd07736    38 CSAL--IEVDGERILLDAGLT---DLAERFPPG-SIDAILLTHFHMDHVQGLFHL--RWGVG---DPIPVYGPPDPQ 103
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 28-65 1.07e-04

uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized Thermus thermophilus TTHA1429 and related proteins. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293811 [Multi-domain]  Cd Length: 184  Bit Score: 41.90  E-value: 1.07e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2019657023  28 LIDCGPTVP---RALWQR----GGGVNDIDAIYFTHVHPDHCTGL 65
Cdd:cd07725    28 LIDTGLATEedaEALWEGlkelGLKPSDIDRVLLTHHHPDHIGLA 72
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 19-65 2.33e-04

uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized human MBLAC1 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: 293797 [Multi-domain]  Cd Length: 190  Bit Score: 41.03  E-value: 2.33e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2019657023  19 VID---ADNKQWLIDcgptvprALWQRGGGVNDIDAIYFTHVHPDHCTGL 65
Cdd:cd07711    35 LVDtgtPWDRDLLLK-------ALAEHGLSPEDIDYVVLTHGHPDHIGNL 77
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 20-158 4.70e-04

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 40.94  E-value: 4.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019657023  20 IDADNKQWLIDCG--PTVPRALWQRGG-GVNDIDAIYFTHVHPDHCTGLTALLnywKSGSRQKpliIYCQPAQQP---VL 93
Cdd:COG1236    19 LETGGTRILIDCGlfQGGKERNWPPFPfRPSDVDAVVLTHAHLDHSGALPLLV---KEGFRGP---IYATPATADlarIL 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019657023  94 MQLAA--LANWPQADPGFTID--------WQECR--EAWTWQDWQIRT--------AATqhelsnraIRITIAGQTLFYS 153
Cdd:COG1236    93 LGDSAkiQEEEAEAEPLYTEEdaeralelFQTVDygEPFEIGGVRVTFhpaghilgSAQ--------VELEVGGKRIVFS 164


                  ....*.
gi 2019657023 154 GD-GRP 158
Cdd:COG1236   165 GDyGRE 170
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 20-88 5.79e-04

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: 39.75  E-value: 5.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019657023  20 IDADNKQWLIDCGptvpraLWQRGGG------------VNDIDAIYFTHVHPDHCtGltALLNYWKSGSRQKpliIYCQP 87
Cdd:cd16295    17 LETGGKRILLDCG------LFQGGKEleelnnepfpfdPKEIDAVILTHAHLDHS-G--RLPLLVKEGFRGP---IYATP 84


                  .
gi 2019657023  88 A 88
Cdd:cd16295    85 A 85
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 19-61 6.09e-04

uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo hydrolase domain; This subgroup includes the uncharacterized Sulfolobus tokodaii ST1585 protein. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293812 [Multi-domain]  Cd Length: 215  Bit Score: 39.78  E-value: 6.09e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2019657023  19 VIDADNKQWLIDCGP--TVPR---ALWQRGGGVNDIDAIYFTHVHPDH 61
Cdd:cd07726    20 LLDGEGRPALIDTGPssSVPRllaALEALGIAPEDVDYIILTHIHLDH 67
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 27-66 1.09e-03

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


Pssm-ID: 293816 [Multi-domain]  Cd Length: 250  Bit Score: 39.17  E-value: 1.09e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2019657023  27 WLIDCGPTVPRALWQRGGGVNDIDAIYFTHVHPDHCTGLT 66
Cdd:cd07730    62 VPLEVEEDVAEQLAAGGIDPEDIDAVILSHLHWDHIGGLS 101
RNaseZ_ELAC1_ELAC2-C-term-like_MBL-fold cd07718
Ribonuclease Z ELAC1, C-terminus of ELAC2, and related proteins; MBL-fold metallo-hydrolase ...
 48-83 2.33e-03

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: 37.91  E-value: 2.33e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2019657023  48 DIDAIYFTHVHPDHCTGLTALLNYWK--SGSRQKPLII 83
Cdd:cd07718    57 NLKCIFISHLHADHHLGLIRLLAERKklFKPPSPPLYV 94
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 27-70 2.56e-03

uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold metallo hydrolase domain; Includes functionally uncharacterized human lactamase beta 2. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293808 [Multi-domain]  Cd Length: 188  Bit Score: 37.90  E-value: 2.56e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2019657023  27 WLIDCG-------PTVPRALwqRGGGVNDIDAIYFTHVHPDHCTGLTALLN 70
Cdd:cd07722    30 ILIDTGegrpsyiPLLKSVL--DSEGNATISDILLTHWHHDHVGGLPDVLD 78
DdPDE5-like_MBL-fold cd07738
Dictyostelium discoideum phosphodiesterase 5 and related proteins; MBL-fold metallo hydrolase ...
 2-166 2.87e-03

Dictyostelium discoideum phosphodiesterase 5 and related proteins; MBL-fold metallo hydrolase domain; Includes Dictyostelium discoideum cAMP/cGMP-dependent 3',5'-cAMP/cGMP phosphodiesterase A (also known as cyclic GMP-binding protein A, phosphodiesterase 5, phosphodiesterase D, and PDE5) and cAMP/cGMP-dependent 3',5'-cAMP/cGMP phosphodiesterase B (also known as cyclic GMP-binding protein B, phosphodiesterase 6, phosphodiesterase E, and PDE6. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293824  Cd Length: 189  Bit Score: 37.66  E-value: 2.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019657023   2 LGCGSAFSCTQNTSALrVIDADNKQWLIDcgPTVPRALWQRGGGVN--DIDAIYFTHVHPDHCTGLtallnYWKSGSRQK 79
Cdd:cd07738     3 LGVSHGFDPKGHTSGF-IIWINGRGIMVD--PPVNSTSYLRQNGISprLVDHVILTHCHADHDAGT-----FQKILEEEK 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019657023  80 PLIIYCQPAQQPVLMQLAALANWPQADPGFTIDWQECR--EAWTWQDWQIRTAATQHELSNRAIRITIAGQTLFYSGDGR 157
Cdd:cd07738    75 ITLYTTRTINESFLRKYAALTGLPPDFLEELFDFRPVIigEKTKINGAEFEFDYSFHSIPTIRFKVSYGGKSIAYSGDTR 154


                  ....*....
gi 2019657023 158 PTADSIALM 166
Cdd:cd07738   155 YDPDGLKSL 163
PRK02113 PRK02113
MBL fold metallo-hydrolase;
14-68 4.10e-03

MBL fold metallo-hydrolase;


Pssm-ID: 179371 [Multi-domain]  Cd Length: 252  Bit Score: 37.45  E-value: 4.10e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2019657023  14 TSALrvIDADNKQWLIDCGPTVPralWQR-GGGVNDIDAIYFTHVHPDHCTGLTAL 68
Cdd:PRK02113   36 TSAL--VETEGARILIDCGPDFR---EQMlRLPFGKIDAVLITHEHYDHVGGLDDL 86
TaR3-like_MBL-fold cd07715
MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold ...
 13-171 5.16e-03

MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold metallo-hydrolase domain; Myxococcus xanthus Tar3 may function as an ammonium regulator/effector protein involved in biosynthesis of the antibiotic TA. Some are members of this subgroup are annotated as ribonucleases. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293801 [Multi-domain]  Cd Length: 212  Bit Score: 37.09  E-value: 5.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019657023  13 NTSALrVIDADNKQWLIDCGpTVPRALWQR---GGGVNDIDaIYFTHVHPDHCTGL---TALlnyWKSGSRqkpLIIY-C 85
Cdd:cd07715    22 NTSCV-EVRAGGELLILDAG-TGIRELGNElmkEGPPGEAH-LLLSHTHWDHIQGFpffAPA---YDPGNR---IHIYgP 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019657023  86 QPAQQPVLMQLAALanwpQADPGFTIDWQECR-----------EAWTWQDWQIRTAATQHELSNRAIRITIAGQTLFYSG 154
Cdd:cd07715    93 HKDGGSLEEVLRRQ----MSPPYFPVPLEELLaaiefhdlepgEPFSIGGVTVTTIPLNHPGGALGYRIEEDGKSVVYAT 168

                         170       180
                  ....*....|....*....|....
gi 2019657023 155 D-------GRPTADSIALMAGAGL 171
Cdd:cd07715   169 DtehypddGESDEALLEFARGADL 192
metallo-hydrolase-like_MBL-fold cd16281
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 16-67 5.28e-03

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


Pssm-ID: 293839  Cd Length: 252  Bit Score: 37.09  E-value: 5.28e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2019657023  16 ALRV--IDADNKQWLIDCG------------------PTVPRALWQRGGGVNDIDAIYFTHVHPDHCTGLTA 67
Cdd:cd16281    42 AMRCllIETGGRNILIDTGigdkqdpkfrsiyvqhseHSLLKSLARLGLSPEDITDVILTHLHFDHCGGATR 113
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 28-102 5.52e-03

uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized Thermus thermophilus TTHA1623 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. This family includes homologs present in a wide range of bacteria and archaea and some eukaryota. Members of the MBL-fold metallo-hydrolase superfamily exhibit a variety of active site metallo-chemistry, TTHA1623 exhibiting a uniquely shaped putative substrate-binding pocket with a glyoxalase II-type metal-coordination mode.


Pssm-ID: 293877 [Multi-domain]  Cd Length: 204  Bit Score: 36.94  E-value: 5.52e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2019657023  28 LIDCGPTVPRALWQRGGGVNDIDAIYFTHVHPDHCTGLTALLnywksgsRQKPLIIYCQPAQQPVLMQLAALANW 102
Cdd:cd16322    26 LVDPGDESEKLLARFGTTGLTLLYILLTHAHFDHVGGVADLR-------RHPGAPVYLHPDDLPLYEAADLGAKA 93
metallo-hydrolase-like_MBL-fold cd07741
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 19-69 9.23e-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: 36.40  E-value: 9.23e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2019657023  19 VIDADNKQWLIDCGP-TVPRAlWQRGGGVNDIDAIYFTHVHPDHCTGLTALL 69
Cdd:cd07741    24 WIELNGKNIHIDPGPgALVRM-CRPKLDPTKLDAIILSHRHLDHSNDANVLI 74
 
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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