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Conserved domains on  [gi|1488968958|gb|RKT47730|]
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phosphoribosyl 1,2-cyclic phosphodiesterase [Thiocapsa rosea]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 11440937)

uncharacterized MBL fold metallo-hydrolase similar to uncharacterized Bacillus subtilis YycJ (WalJ) which affects the coordination of cell division with DNA replication, and may play a role in cell wall metabolism

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 1-229 3.57e-54

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


:

Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 175.08  E-value: 3.57e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488968958   1 MRFCSLGSGSRG-----------------------NATLVESAGCRVLVDNGLSLRELHQRLrsvDVEPGSIDVLLLTHE 57
Cdd:COG1235     1 MKVTFLGSGSSGgvpqigcdcpvcastdprygrtrSSILVEADGTRLLIDAGPDLREQLLRL---GLDPSKIDAILLTHE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488968958  58 HGDHVKGVWSFARRH---RVEVWTTPGTWRAVGA---------PEIPRLRLLSGqGQSMRIDGLRIRSYPVPHDAREPCQ 125
Cdd:COG1235    78 HADHIAGLDDLRPRYgpnPIPVYATPGTLEALERrfpylfapyPGKLEFHEIEP-GEPFEIGGLTVTPFPVPHDAGDPVG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488968958 126 FLFEADGRRLGMLTDAGCVTPHMTEVLQDCDALILELNHDPemlrrgPYPpslqrrvagdfGHLSNLQAACFLDALPHRa 205
Cdd:COG1235   157 YRIEDGGKKLAYATDTGYIPEEVLELLRGADLLILDATYDD------PEP-----------GHLSNEEALELLARLGPK- 218

                         250       260
                  ....*....|....*....|....
gi 1488968958 206 iaQLCVAHVSETNNHPDLVRASIR 229
Cdd:COG1235   219 --RLVLTHLSPDNNDHELDYDELE 240
 
Name Accession Description Interval E-value
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 1-229 3.57e-54

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 175.08  E-value: 3.57e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488968958   1 MRFCSLGSGSRG-----------------------NATLVESAGCRVLVDNGLSLRELHQRLrsvDVEPGSIDVLLLTHE 57
Cdd:COG1235     1 MKVTFLGSGSSGgvpqigcdcpvcastdprygrtrSSILVEADGTRLLIDAGPDLREQLLRL---GLDPSKIDAILLTHE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488968958  58 HGDHVKGVWSFARRH---RVEVWTTPGTWRAVGA---------PEIPRLRLLSGqGQSMRIDGLRIRSYPVPHDAREPCQ 125
Cdd:COG1235    78 HADHIAGLDDLRPRYgpnPIPVYATPGTLEALERrfpylfapyPGKLEFHEIEP-GEPFEIGGLTVTPFPVPHDAGDPVG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488968958 126 FLFEADGRRLGMLTDAGCVTPHMTEVLQDCDALILELNHDPemlrrgPYPpslqrrvagdfGHLSNLQAACFLDALPHRa 205
Cdd:COG1235   157 YRIEDGGKKLAYATDTGYIPEEVLELLRGADLLILDATYDD------PEP-----------GHLSNEEALELLARLGPK- 218

                         250       260
                  ....*....|....*....|....
gi 1488968958 206 iaQLCVAHVSETNNHPDLVRASIR 229
Cdd:COG1235   219 --RLVLTHLSPDNNDHELDYDELE 240
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 5-140 7.30e-47

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: 152.80  E-value: 7.30e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488968958   5 SLGSGSRGNATLVESAGCRVLVDNGLSLRELHQRLRSVDVEPGSIDVLLLTHEHGDHVKGVWSFARRHRVEVWTTPGTWR 84
Cdd:cd07733     2 VLASGSKGNCTYLETEDGKLLIDAGLSGRKITGRLAEIGRDPEDIDAILVTHEHADHIKGLGVLARKYNVPIYATAGTLR 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488968958  85 AVGAP----EIPRLRLLSgQGQSMRIDGLRIRSYPVPHDAREPCQFLFEADGRRLGMLTD 140
Cdd:cd07733    82 AMERKvgliDVDQKQIFE-PGETFSIGDFDVESFGVSHDAADPVGYRFEEGGRRFGMLTD 140
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 23-172 6.46e-16

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: 73.50  E-value: 6.46e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488968958  23 RVLVDNGLSLRELHQRLRS-VDVEPGSIDVLLLTHEHGDHVKGVWSFARRHRVEVWTTPGTWRAVGAPEIPRLRLLSGQ- 100
Cdd:pfam12706   2 RILIDPGPDLRQQALPALQpGRLRDDPIDAVLLTHDHYDHLAGLLDLREGRPRPLYAPLGVLAHLRRNFPYLFLLEHYGv 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488968958 101 -------GQSMRID--GLRIRSYPVPHDAR--------EPCQFLFEADGRRLGMLTDAGCVTPHMTEVLQDCDALILELN 163
Cdd:pfam12706  82 rvheidwGESFTVGdgGLTVTATPARHGSPrgldpnpgDTLGFRIEGPGKRVYYAGDTGYFPDEIGERLGGADLLLLDGG 161

                         170
                  ....*....|.
gi 1488968958 164 --HDPEMLRRG 172
Cdd:pfam12706 162 awRDDEMIHMG 172
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 13-132 1.65e-13

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: 66.81  E-value: 1.65e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488968958   13 NATLVESAGCRVLVDNGLS-LRELHQRLRSVDVEPgsIDVLLLTHEHGDHVKGVWSFARRHRVEVWTTPGTWRAVGAPEI 91
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGeAEDLLAELKKLGPKK--IDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELLKDLLA 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1488968958   92 PRLRLLSGQ-----------GQSMRIDGLRIRSYPVPHDAREPCQFLFEADG 132
Cdd:smart00849  79 LLGELGAEAepappdrtlkdGDELDLGGGELEVIHTPGHTPGSIVLYLPEGK 130
PRK02113 PRK02113
MBL fold metallo-hydrolase;
16-175 2.21e-06

MBL fold metallo-hydrolase;


Pssm-ID: 179371 [Multi-domain]  Cd Length: 252  Bit Score: 47.47  E-value: 2.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488968958  16 LVESAGCRVLVDNGLSLRElhQRLRsvdVEPGSIDVLLLTHEHGDHVKG---VWSFARRHRVEVWTTPGTWRAVGA---- 88
Cdd:PRK02113   39 LVETEGARILIDCGPDFRE--QMLR---LPFGKIDAVLITHEHYDHVGGlddLRPFCRFGEVPIYAEQYVAERLRSrmpy 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488968958  89 -------PEIPRLRLLS-GQGQSMRIDGLRIRSYPVPHdAREPcqFLFEADGrRLGMLTDAGCVTPHMTEVLQDCDALIL 160
Cdd:PRK02113  114 cfvehsyPGVPNIPLREiEPDRPFLVNHTEVTPLRVMH-GKLP--ILGYRIG-KMAYITDMLTMPEEEYEQLQGIDVLVM 189

                         170
                  ....*....|....*
gi 1488968958 161 elnhdpEMLRRGPYP 175
Cdd:PRK02113  190 ------NALRIAPHP 198
 
Name Accession Description Interval E-value
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 1-229 3.57e-54

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 175.08  E-value: 3.57e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488968958   1 MRFCSLGSGSRG-----------------------NATLVESAGCRVLVDNGLSLRELHQRLrsvDVEPGSIDVLLLTHE 57
Cdd:COG1235     1 MKVTFLGSGSSGgvpqigcdcpvcastdprygrtrSSILVEADGTRLLIDAGPDLREQLLRL---GLDPSKIDAILLTHE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488968958  58 HGDHVKGVWSFARRH---RVEVWTTPGTWRAVGA---------PEIPRLRLLSGqGQSMRIDGLRIRSYPVPHDAREPCQ 125
Cdd:COG1235    78 HADHIAGLDDLRPRYgpnPIPVYATPGTLEALERrfpylfapyPGKLEFHEIEP-GEPFEIGGLTVTPFPVPHDAGDPVG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488968958 126 FLFEADGRRLGMLTDAGCVTPHMTEVLQDCDALILELNHDPemlrrgPYPpslqrrvagdfGHLSNLQAACFLDALPHRa 205
Cdd:COG1235   157 YRIEDGGKKLAYATDTGYIPEEVLELLRGADLLILDATYDD------PEP-----------GHLSNEEALELLARLGPK- 218

                         250       260
                  ....*....|....*....|....
gi 1488968958 206 iaQLCVAHVSETNNHPDLVRASIR 229
Cdd:COG1235   219 --RLVLTHLSPDNNDHELDYDELE 240
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 5-140 7.30e-47

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: 152.80  E-value: 7.30e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488968958   5 SLGSGSRGNATLVESAGCRVLVDNGLSLRELHQRLRSVDVEPGSIDVLLLTHEHGDHVKGVWSFARRHRVEVWTTPGTWR 84
Cdd:cd07733     2 VLASGSKGNCTYLETEDGKLLIDAGLSGRKITGRLAEIGRDPEDIDAILVTHEHADHIKGLGVLARKYNVPIYATAGTLR 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488968958  85 AVGAP----EIPRLRLLSgQGQSMRIDGLRIRSYPVPHDAREPCQFLFEADGRRLGMLTD 140
Cdd:cd07733    82 AMERKvgliDVDQKQIFE-PGETFSIGDFDVESFGVSHDAADPVGYRFEEGGRRFGMLTD 140
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
1-231 2.88e-20

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 86.40  E-value: 2.88e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488968958   1 MRFCSLGSGS-------RGNATLVESAGCRVLVD--NGlSLRelhqRLRSVDVEPGSIDVLLLTHEHGDHVKGV------ 65
Cdd:COG1234     1 MKLTFLGTGGavptpgrATSSYLLEAGGERLLIDcgEG-TQR----QLLRAGLDPRDIDAIFITHLHGDHIAGLpgllst 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488968958  66 -WSFARRHRVEVWTTPGTWRAVGA-----PEIPRLRL----LSgQGQSMRIDGLRIRSYPVPHdaREPCQ-FLFEADGRR 134
Cdd:COG1234    76 rSLAGREKPLTIYGPPGTKEFLEAllkasGTDLDFPLefheIE-PGEVFEIGGFTVTAFPLDH--PVPAYgYRFEEPGRS 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488968958 135 LGMLTDAGcVTPHMTEVLQDCDALILELNHDPEMLRRgpyppslqrrvAGDFGHLSNLQAACFLDALphrAIAQLCVAHV 214
Cdd:COG1234   153 LVYSGDTR-PCEALVELAKGADLLIHEATFLDEEAEL-----------AKETGHSTAKEAAELAAEA---GVKRLVLTHF 217

                         250
                  ....*....|....*..
gi 1488968958 215 SETNNHPDLVRASIRGV 231
Cdd:COG1234   218 SPRYDDPEELLAEARAV 234
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 23-172 6.46e-16

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: 73.50  E-value: 6.46e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488968958  23 RVLVDNGLSLRELHQRLRS-VDVEPGSIDVLLLTHEHGDHVKGVWSFARRHRVEVWTTPGTWRAVGAPEIPRLRLLSGQ- 100
Cdd:pfam12706   2 RILIDPGPDLRQQALPALQpGRLRDDPIDAVLLTHDHYDHLAGLLDLREGRPRPLYAPLGVLAHLRRNFPYLFLLEHYGv 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488968958 101 -------GQSMRID--GLRIRSYPVPHDAR--------EPCQFLFEADGRRLGMLTDAGCVTPHMTEVLQDCDALILELN 163
Cdd:pfam12706  82 rvheidwGESFTVGdgGLTVTATPARHGSPrgldpnpgDTLGFRIEGPGKRVYYAGDTGYFPDEIGERLGGADLLLLDGG 161

                         170
                  ....*....|.
gi 1488968958 164 --HDPEMLRRG 172
Cdd:pfam12706 162 awRDDEMIHMG 172
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 12-163 2.48e-14

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 69.95  E-value: 2.48e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488968958  12 GNAT-LVESAGCRVLVDNGLSLRELHQRLRSVDVE-PGSIDVLLLTHEHGDHV-KGVWSFARRHRVEVWTTPGTWRAVGA 88
Cdd:COG2220    10 GHATfLIETGGKRILIDPVFSGRASPVNPLPLDPEdLPKIDAVLVTHDHYDHLdDATLRALKRTGATVVAPLGVAAWLRA 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488968958  89 PEIPRLRLLSGqGQSMRIDGLRIRSYPVPH-------DAREPCQFLFEADGRRL---GmltDAGcVTPHMTEVLQDC--D 156
Cdd:COG2220    90 WGFPRVTELDW-GESVELGGLTVTAVPARHssgrpdrNGGLWVGFVIETDGKTIyhaG---DTG-YFPEMKEIGERFpiD 164


                  ....*..
gi 1488968958 157 ALILELN 163
Cdd:COG2220   165 VALLPIG 171
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 13-132 1.65e-13

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: 66.81  E-value: 1.65e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488968958   13 NATLVESAGCRVLVDNGLS-LRELHQRLRSVDVEPgsIDVLLLTHEHGDHVKGVWSFARRHRVEVWTTPGTWRAVGAPEI 91
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGeAEDLLAELKKLGPKK--IDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELLKDLLA 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1488968958   92 PRLRLLSGQ-----------GQSMRIDGLRIRSYPVPHDAREPCQFLFEADG 132
Cdd:smart00849  79 LLGELGAEAepappdrtlkdGDELDLGGGELEVIHTPGHTPGSIVLYLPEGK 130
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 6-161 3.54e-13

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: 65.75  E-value: 3.54e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488968958   6 LGSGS-------RGNATLVESAGCRVLVDNGlslRELHQRLRSVDVEPGSIDVLLLTHEHGDHVKGVWSFARRHRVEVWT 78
Cdd:cd16272     4 LGTGGavpsltrNTSSYLLETGGTRILLDCG---EGTVYRLLKAGVDPDKLDAIFLSHFHLDHIGGLPTLLFARRYGGRK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488968958  79 TP----------GTWRAVGAPEIPRLRL--------LSGQGQSMRIDGLRIRSYPVPHdaREPCQFL-FEADGRRLGMLT 139
Cdd:cd16272    81 KPltiygpkgikEFLEKLLNFPVEILPLgfpleieeLEEGGEVLELGDLKVEAFPVKH--SVESLGYrIEAEGKSIVYSG 158

                         170       180
                  ....*....|....*....|..
gi 1488968958 140 DAGCvTPHMTEVLQDCDALILE 161
Cdd:cd16272   159 DTGP-CENLVELAKGADLLIHE 179
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 16-160 1.52e-12

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: 64.42  E-value: 1.52e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488968958  16 LVESAGCRVLVDNGLSLRElhQRLRS-VDvepgSIDVLLLTHEHGDHVKG-----VWSFARRHRVEVWTTPGTWRAV--- 86
Cdd:cd16279    39 LIETGGKNILIDTGPDFRQ--QALRAgIR----KLDAVLLTHAHADHIHGlddlrPFNRLQQRPIPVYASEETLDDLkrr 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488968958  87 --------GAPEIPRLRLLS-GQGQSMRIDGLRIRSYPVPHDAREPCQFLFEadgrRLGMLTDAGCVTPHMTEVLQDCDA 157
Cdd:cd16279   113 fpyffaatGGGGVPKLDLHIiEPDEPFTIGGLEITPLPVLHGKLPSLGFRFG----DFAYLTDVSEIPEESLEKLRGLDV 188


                  ...
gi 1488968958 158 LIL 160
Cdd:cd16279   189 LIL 191
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
12-159 9.84e-11

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 59.30  E-value: 9.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488968958  12 GNATLVESAGCRVLVDNGLSL-RELHQRLRSVDVEPGSIDVLLLTHEHGDHVKGVWSFARRHRVEVWttpgtwraVGAPE 90
Cdd:pfam00753   6 VNSYLIEGGGGAVLIDTGGSAeAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVI--------VVAEE 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1488968958  91 IPRLRLLSGQGQSMRIDGLRIRSYPVPHDAREPCQFLFEADGRRLGMLTDAGCVTPHMTEVLQDCDALI 159
Cdd:pfam00753  78 ARELLDEELGLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLF 146
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 7-135 2.29e-10

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


Pssm-ID: 293826 [Multi-domain]  Cd Length: 194  Bit Score: 58.42  E-value: 2.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488968958   7 GSGSRGNA-TLVESAGCRVLVDNGLSLrelHQRLRSVDVEPGSIDVLLLTHEHGDHVKGV-------WSFARRHR-VEVW 77
Cdd:cd07740    10 GSGGRLNTcFHVASEAGRFLIDCGASS---LIALKRAGIDPNAIDAIFITHLHGDHFGGLpfflldaQFVAKRTRpLTIA 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1488968958  78 TTPGT---WRAV------GAPEIPR---LRLLSGQ-GQSMRIDGLRIRSYPVPHDARE-PCQFLFEADGRRL 135
Cdd:cd07740    87 GPPGLrerLRRAmealfpGSSKVPRrfdLEVIELEpGEPTTLGGVTVTAFPVVHPSGAlPLALRLEAAGRVL 158
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 6-159 8.97e-10

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: 56.76  E-value: 8.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488968958   6 LGSGS------R-GNATLVESAGCRVLVDNGL-SLRelhqRLRSVDVEPGSIDVLLLTHEHGDHV-------KGVWSFAR 70
Cdd:cd07719     5 LGTGGpipdpdRaGPSTLVVVGGRVYLVDAGSgVVR----RLAQAGLPLGDLDAVFLTHLHSDHVadlpallLTAWLAGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488968958  71 RHRVEVW-------TTPGTWRAVGAPEIPRLRL----------------LSGQGQSMRIDGLRIRSYPVPHDAREPCQ-F 126
Cdd:cd07719    81 KTPLPVYgppgtraLVDGLLAAYALDIDYRARIgdegrpdpgalvevheIAAGGVVYEDDGVKVTAFLVDHGPVPPALaY 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1488968958 127 LFEADGRRL---GmltDAGcVTPHMTEVLQDCDALI 159
Cdd:cd07719   161 RFDTPGRSVvfsG---DTG-PSENLIELAKGADLLV 192
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 1-161 9.94e-10

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 57.89  E-value: 9.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488968958   1 MRFCSLGSGSR--GNATLVESAGCRVLVDNGLSLRELHQRLRSVDVEPGSIDVLLLTHEHGDHVKGVWSFARRH-RVEVW 77
Cdd:COG1236     1 MKLTFLGAAGEvtGSCYLLETGGTRILIDCGLFQGGKERNWPPFPFRPSDVDAVVLTHAHLDHSGALPLLVKEGfRGPIY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488968958  78 TTPGT-----------------WRAVGAP----EIPR-LRLLSGQ--GQSMRIDGLRIRSYPVPH---DArepcQFLFEA 130
Cdd:COG1236    81 ATPATadlarillgdsakiqeeEAEAEPLyteeDAERaLELFQTVdyGEPFEIGGVRVTFHPAGHilgSA----QVELEV 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1488968958 131 DGRRL-----------GMLTDAgcvtphmtEVLQDCDALILE 161
Cdd:COG1236   157 GGKRIvfsgdygreddPLLAPP--------EPVPPADVLITE 190
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 6-197 1.24e-09

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: 57.07  E-value: 1.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488968958   6 LGSGS------RG-NATLVESAGCRVLVDNGlslrELHQR-LRSVDVEPGSIDVLLLTHEHGDHVKG----VWSFA---R 70
Cdd:cd07717     4 LGTGSavptpeRNlSSIALRLEGELWLFDCG----EGTQRqLLRAGLSPSKIDRIFITHLHGDHILGlpglLSTMSllgR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488968958  71 RHRVEVWTTPGTWRAV-GAPEIPRLRL---------LSGQGQSMRIDGLRIRSYPVPHdaREPCQ-FLFEAdGRRLGMLT 139
Cdd:cd07717    80 TEPLTIYGPKGLKEFLeTLLRLSASRLpypievhelEPDPGLVFEDDGFTVTAFPLDH--RVPCFgYRFEE-GRKIAYLG 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1488968958 140 DaGCVTPHMTEVLQDCDALILELNHDPEMLRRgpyppslqrrvAGDFGHLSNLQAACF 197
Cdd:cd07717   157 D-TRPCEGLVELAKGADLLIHEATFLDDDAEK-----------AKETGHSTAKQAAEI 202
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 12-135 1.70e-09

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Includes functionally uncharacterized Enterococcus faecalis EF2904. 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: 293818 [Multi-domain]  Cd Length: 202  Bit Score: 56.08  E-value: 1.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488968958  12 GNATLVESAGCRVLVDNGLSLR-------ELHQRLRSV-------------------DVEPGSIDVLLLTHEHGDHVKGV 65
Cdd:cd07732    13 GNCIEVETGGTRILLDFGLPLDpeskyfdEVLDFLELGllpdivglyrdplllgglrSEEDPSVDAVLLSHAHLDHYGLL 92

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1488968958  66 wSFArRHRVEVWTTPGTWRAVGA------PEIPRLRLLSG--QGQSMRIDGLRIRSYPVPHDAREPCQFLFEADGRRL 135
Cdd:cd07732    93 -NYL-RPDIPVYMGEATKRILKAllpffgEGDPVPRNIRVfeSGKSFTIGDFTVTPYLVDHSAPGAYAFLIEAPGKRI 168
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 13-136 2.07e-08

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: 52.99  E-value: 2.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488968958  13 NATLVESAGCRVLVDNGL--SLRELHQRLRSVDVEPGSIDVLLLTHEHGDHVKGVWSFARRHRVEVWTTPGTWRAVGAPE 90
Cdd:cd07721    12 NAYLIEDDDGLTLIDTGLpgSAKRILKALRELGLSPKDIRRILLTHGHIDHIGSLAALKEAPGAPVYAHEREAPYLEGEK 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1488968958  91 IPRLRLLSGQGQSMRidglrirsYPVPHDAREPCQFLfeADGRRLG 136
Cdd:cd07721    92 PYPPPVRLGLLGLLS--------PLLPVKPVPVDRTL--EDGDTLD 127
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 12-161 2.36e-08

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: 52.06  E-value: 2.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488968958  12 GNAT---LVESAGCRVLVD--NGlSLRELHQRlrsvdVEPGSIDVLLLTHEHGDHVK--GVWSFARR--------HRVEV 76
Cdd:cd07716    15 GGACsgyLLEADGFRILLDcgSG-VLSRLQRY-----IDPEDLDAVVLSHLHPDHCAdlGVLQYARRyhprgarkPPLPL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488968958  77 WTTPGTW----RAVGAPEIPRLRLLSgQGQSMRIDGLRIRSYPVPHDArePC-QFLFEADGRRLGMLTDAGcVTPHMTEV 151
Cdd:cd07716    89 YGPAGPAerlaALYGLEDVFDFHPIE-PGEPLEIGPFTITFFRTVHPV--PCyAMRIEDGGKVLVYTGDTG-YCDELVEF 164

                         170
                  ....*....|
gi 1488968958 152 LQDCDALILE 161
Cdd:cd07716   165 ARGADLLLCE 174
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 13-117 2.59e-08

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: 52.77  E-value: 2.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488968958  13 NATLVESAGCRVLVDNGLSLRELHQRLRSVDVEPGSIDVLLLTHEHGDHVKGVWSFARRHRVEVWTTPGTWRA------- 85
Cdd:COG0491    16 NSYLIVGGDGAVLIDTGLGPADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFGAPVYAHAAEAEAleapaag 95

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1488968958  86 --VGAPEIPRLRLLSGqGQSMRIDGLRIRSYPVP 117
Cdd:COG0491    96 alFGREPVPPDRTLED-GDTLELGGPGLEVIHTP 128
PhnP-like_MBL-fold cd07736
phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase ...
 16-140 3.41e-08

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


Pssm-ID: 293822 [Multi-domain]  Cd Length: 186  Bit Score: 51.85  E-value: 3.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488968958  16 LVESAGCRVLVDNGLSlrELHQRLRsvdvePGSIDVLLLTHEHGDHVKGV----WSFARrhRVEVWTTPGtwrAVGA--- 88
Cdd:cd07736    41 LIEVDGERILLDAGLT--DLAERFP-----PGSIDAILLTHFHMDHVQGLfhlrWGVGD--PIPVYGPPD---PQGCadl 108

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1488968958  89 ---PEIPRLRLLSGQGQSMRIDGLRIRSYPVPHdAREPCQFLFEADGRRLGMLTD 140
Cdd:cd07736   109 fkhPGILDFQPLVAPFQSFELGGLKITPLPLNH-SKPTFGYLLESGGKRLAYLTD 162
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 13-64 4.39e-08

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: 52.55  E-value: 4.39e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1488968958  13 NATLVESAGCRVLVDNGL------SLRELHQRLRSVDVEPGSIDVLLLTHEHGDHVKG 64
Cdd:cd07720    50 NAFLVRTGGRLILVDTGAgglfgpTAGKLLANLAAAGIDPEDIDDVLLTHLHPDHIGG 107
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 12-112 5.37e-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: 52.17  E-value: 5.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488968958  12 GNATLVES-AGCRVLVDNG------LSLRELHQRLRSVDVEpgSIDVLLLTHEHGDHVKGVWSFARRHRV-EVWTTPGT- 82
Cdd:COG2333    11 GDAILIRTpDGKTILIDTGprpsfdAGERVVLPYLRALGIR--RLDLLVLTHPDADHIGGLAAVLEAFPVgRVLVSGPPd 88

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1488968958  83 --------WRAVGAPEIPRLRLLsgQGQSMRIDGLRIR 112
Cdd:COG2333    89 tsetyerlLEALKEKGIPVRPCR--AGDTWQLGGVRFE 124
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 13-117 1.91e-06

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


Pssm-ID: 293792 [Multi-domain]  Cd Length: 188  Bit Score: 46.90  E-value: 1.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488968958  13 NATLVES-AGCRVLVDNGLSLRELHQRLrsVDVEPGSIDVLLLTHEHGDHVKGVWSFARRHRVEVWTTPGTWRAVGAPE- 90
Cdd:cd06262    11 NCYLVSDeEGEAILIDPGAGALEKILEA--IEELGLKIKAILLTHGHFDHIGGLAELKEAPGAPVYIHEADAELLEDPEl 88

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1488968958  91 ------------IPRLRLLSGqGQSMRIDGLRIRSYPVP 117
Cdd:cd06262    89 nlaffgggplppPEPDILLED-GDTIELGGLELEVIHTP 126
PRK02113 PRK02113
MBL fold metallo-hydrolase;
16-175 2.21e-06

MBL fold metallo-hydrolase;


Pssm-ID: 179371 [Multi-domain]  Cd Length: 252  Bit Score: 47.47  E-value: 2.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488968958  16 LVESAGCRVLVDNGLSLRElhQRLRsvdVEPGSIDVLLLTHEHGDHVKG---VWSFARRHRVEVWTTPGTWRAVGA---- 88
Cdd:PRK02113   39 LVETEGARILIDCGPDFRE--QMLR---LPFGKIDAVLITHEHYDHVGGlddLRPFCRFGEVPIYAEQYVAERLRSrmpy 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488968958  89 -------PEIPRLRLLS-GQGQSMRIDGLRIRSYPVPHdAREPcqFLFEADGrRLGMLTDAGCVTPHMTEVLQDCDALIL 160
Cdd:PRK02113  114 cfvehsyPGVPNIPLREiEPDRPFLVNHTEVTPLRVMH-GKLP--ILGYRIG-KMAYITDMLTMPEEEYEQLQGIDVLVM 189

                         170
                  ....*....|....*
gi 1488968958 161 elnhdpEMLRRGPYP 175
Cdd:PRK02113  190 ------NALRIAPHP 198
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 7-97 2.22e-06

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: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 47.18  E-value: 2.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488968958   7 GSGSRGNATLVESAGCRVLVDNGLSL---RELHQRLRSVDvePGSIDVLLLTHEHGDHVKGVWSFARRHrVEVWTTPGTW 83
Cdd:cd16282    10 GGGFISNIGFIVGDDGVVVIDTGASPrlaRALLAAIRKVT--DKPVRYVVNTHYHGDHTLGNAAFADAG-APIIAHENTR 86

                          90
                  ....*....|....
gi 1488968958  84 RAVGAPEIPRLRLL 97
Cdd:cd16282    87 EELAARGEAYLELM 100
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 12-82 2.95e-06

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: 46.68  E-value: 2.95e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1488968958  12 GNATLVESAGCRVLVDNGL--SLRELHQRLRSV-DVEPGSIDVLLLTHEHGDHVKGVWSFARRH-RVEVWTTPGT 82
Cdd:cd16295    12 GSCYLLETGGKRILLDCGLfqGGKELEELNNEPfPFDPKEIDAVILTHAHLDHSGRLPLLVKEGfRGPIYATPAT 86
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 12-112 3.61e-06

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: 45.97  E-value: 3.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488968958  12 GNATLVESAGCRVLVDNGLSLRELHQR----LRSVDVEpgSIDVLLLTHEHGDHVKGVWSFARRHRV-EVWTTPGT---- 82
Cdd:cd07731    10 GDAILIQTPGKTILIDTGPRDSFGEDVvvpyLKARGIK--KLDYLILTHPDADHIGGLDAVLKNFPVkEVYMPGVThttk 87

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1488968958  83 -----WRAVGAPEIPRLRLLsgQGQSMRIDGLRIR 112
Cdd:cd07731    88 tyedlLDAIKEKGIPVTPCK--AGDRWQLGGVSFE 120
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 13-117 8.11e-06

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: 45.42  E-value: 8.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488968958  13 NATLV--ESAGCRVLVDNGLSLRELhqrLRSVDVEPGSIDVLLLTHEHGDHVKGVWSFARRHRVEVWTTPGTwravgape 90
Cdd:cd16322    12 NTYLVadEGGGEAVLVDPGDESEKL---LARFGTTGLTLLYILLTHAHFDHVGGVADLRRHPGAPVYLHPDD-------- 80

                          90       100
                  ....*....|....*....|....*..
gi 1488968958  91 iprLRLLSGQGQSMRIDGLRIRSYPVP 117
Cdd:cd16322    81 ---LPLYEAADLGAKAFGLGIEPLPPP 104
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 15-62 2.09e-05

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: 44.11  E-value: 2.09e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1488968958  15 TLVESAGCRVLVDNGLSL--RELHQRLRSVDVEPGSIDVLLLTHEHGDHV 62
Cdd:cd07711    25 TLIKDGGKNILVDTGTPWdrDLLLKALAEHGLSPEDIDYVVLTHGHPDHI 74
Lactamase_B_3 pfam13483
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 13-142 2.64e-05

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


Pssm-ID: 433247 [Multi-domain]  Cd Length: 160  Bit Score: 43.35  E-value: 2.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488968958  13 NATLVESAGCRVLVDNGLslRELHQRLrsvdvEPGSIDVLLLTHEHGDHvkgvwsfarrhrvevwttpgtWRAVGAPEIP 92
Cdd:pfam13483   8 SSFLIEGGGARILTDPFR--ATVGYRP-----PPVTADLVLISHGHDDH---------------------GHPETLPGNP 59

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1488968958  93 rlRLLSGqGQSMRIDGLRIRSYPVPHDAREP------CQFLFEADGRRLGMLTDAG 142
Cdd:pfam13483  60 --HVLDG-GGSYTVGGLEIRGVPTDHDRVGGrrrggnSIFLFEQDGLTIYHLGHLG 112
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 16-62 1.14e-04

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) 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: 293835 [Multi-domain]  Cd Length: 222  Bit Score: 42.12  E-value: 1.14e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1488968958  16 LVESAGCRVLVDNGL-------SLRELHQ-------RLRSVDVEPGSIDVLLLTHEHGDHV 62
Cdd:cd16277    17 LVRTPGRTILVDTGIgndkprpGPPAFHNlntpyleRLAAAGVRPEDVDYVLCTHLHVDHV 77
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 16-84 1.24e-04

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: 42.22  E-value: 1.24e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1488968958  16 LVESAGCRVLVDNGLSLRELH--QRLrsvDVEPGSIDVLLLTHEHGDHVKGVWSF-ARRHRVEVWTTPGTWR 84
Cdd:cd07713    24 LIETEGKKILFDTGQSGVLLHnaKKL---GIDLSDIDAVVLSHGHYDHTGGLKALlELNPKAPVYAHPDAFE 92
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 13-62 1.41e-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: 41.52  E-value: 1.41e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1488968958  13 NATLVESAGCRVLVDNGLSLRE----LHQRLRSVDVEPGSIDVLLLTHEHGDHV 62
Cdd:cd07725    16 NVYLLRDGDETTLIDTGLATEEdaeaLWEGLKELGLKPSDIDRVLLTHHHPDHI 69
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 35-93 2.18e-04

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) 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: 41.48  E-value: 2.18e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1488968958  35 LHQRLRSVDVEPGSIDVLLLTHEHGDHVKGVWSFArrhRVEVWTTPGTWRAVGAPEIPR 93
Cdd:cd07730    70 VAEQLAAGGIDPEDIDAVILSHLHWDHIGGLSDFP---NARLIVGPGAKEALRPPGYPS 125
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 39-117 2.31e-04

Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; Bacillus amyloliquefaciens BaeB may play a role in the synthesis of the antibiotic polyketide bacillaene. 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: 293833 [Multi-domain]  Cd Length: 174  Bit Score: 40.60  E-value: 2.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488968958  39 LRSVDVEPGSIDVLLLTHEHGDHVKGVWSFARRHRVEVWttpgtwraVGAPEI-------PRLRLLSGqGQSMRIDGLRI 111
Cdd:cd16275    38 LAKLNELGLTLTGILLTHSHFDHVNLVEPLLAKYDAPVY--------MSKEEIdyygfrcPNLIPLED-GDTIKIGDTEI 108


                  ....*.
gi 1488968958 112 RSYPVP 117
Cdd:cd16275   109 TCLLTP 114
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 16-108 3.02e-04

quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl Homoserine Lactones (also known as AHLs) are signal molecules which coordinate gene expression in quorum sensing, in many Gram-negative bacteria. Quorum-quenching N-acyl-homoserine lactonase (also known as AHL lactonase, N-acyl-L-homoserine lactone hydrolase, EC 3.1.1.81) catalyzes the hydrolysis and opening of the homoserine lactone rings of AHLs, a reaction that can block quorum sensing. These enzymes 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: 293815 [Multi-domain]  Cd Length: 238  Bit Score: 41.05  E-value: 3.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488968958  16 LVESAGCRVLVDNGLS--------------------LRELHQRLRSVDVEPGSIDVLLLTHEHGDHVKGVWSFARR---- 71
Cdd:cd07729    36 LIEHPEGTILVDTGFHpdaaddpgglelafppgvteEQTLEEQLARLGLDPEDIDYVILSHLHFDHAGGLDLFPNAtiiv 115

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1488968958  72 HRVEV--WTTPGTWRAVGAPEIPRLRLLSGQGQSMRIDG 108
Cdd:cd07729   116 QRAELeyATGPDPLAAGYYEDVLALDDDLPGGRVRLVDG 154
PRK00685 PRK00685
metal-dependent hydrolase; Provisional
 14-76 4.08e-04

metal-dependent hydrolase; Provisional


Pssm-ID: 234811 [Multi-domain]  Cd Length: 228  Bit Score: 40.57  E-value: 4.08e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1488968958  14 ATLVESAGCRVLVD-----NGLSlrelhqrlrSVDVEPGSIDVLLLTHEHGDHVKGVWSFARRHRVEV 76
Cdd:PRK00685   10 AFLIETGGKKILIDpfitgNPLA---------DLKPEDVKVDYILLTHGHGDHLGDTVEIAKRTGATV 68
class_II_PDE_MBL-fold cd07735
class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium ...
 24-163 1.07e-03

class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium discoideum PDE1 and PDE7, and related proteins; MBL-fold metallo-hydrolase domain; Cyclic nucleotide phosphodiesterases (PDEs) decompose the second messengers cyclic adenosine and guanosine 3',5'-monophosphate (cAMP and cGMP, respectively). Saccharomyces cerevisiae PDE1 and Dictyostelium discoideum PDE1 and PDE7, have dual cAMP/cGMP specificity. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293821  Cd Length: 259  Bit Score: 39.50  E-value: 1.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488968958  24 VLVDNG-----LSLRELHQRLRSVDVEPG-----SIDVLLLTHEHGDHVKG-------VWSFaRRHRVEVWTTPGT---- 82
Cdd:cd07735    31 ILLDAGtgvgaLSLEEMFNDILFPSQKAAyelyqRIRHYLITHAHLDHIAGlpllspnDGGQ-RGSPKTIYGLPETidal 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488968958  83 ------WRA------VGAPEIPRLRLLSG-QGQSMRIDGLRIRSYPVPHDAREPCQFLFEADGRRLGMLTDagcVTPHMT 149
Cdd:cd07735   110 kkhifnWVIwpdftsIPSGKYPYLRLEPIePEYPIALTGLSVTAFPVSHGVPVSTAFLIRDGGDSFLFFGD---TGPDSV 186

                         170
                  ....*....|....
gi 1488968958 150 EVLQDCDALILELN 163
Cdd:cd07735   187 SKSPRLDALWRALA 200
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 6-117 1.39e-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: 38.67  E-value: 1.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488968958   6 LGSGSRgnatlvesagcRVLVDNGLSLRELHQRLRSV--DVEPGSIDVLLLTHEHGDHVKGVWSF---ARRHRVEVWTTP 80
Cdd:cd07722    23 VGTGKR-----------RILIDTGEGRPSYIPLLKSVldSEGNATISDILLTHWHHDHVGGLPDVldlLRGPSPRVYKFP 91

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1488968958  81 GTwRAVGAPEIPRLRLLSGQ-GQSMRIDGLRIRSYPVP 117
Cdd:cd07722    92 RP-EEDEDPDEDGGDIHDLQdGQVFKVEGATLRVIHTP 128
L1_POM-1-like_MBL-B3 cd16289
Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-1 and related ...
 14-71 1.49e-03

Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of L1- and Pom-1-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293847  Cd Length: 239  Bit Score: 39.03  E-value: 1.49e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488968958  14 ATLVESAGCRVLVDNGL--SLRELHQRLRSVDVEPGSIDVLLLTHEHGDHVKGVWSFARR 71
Cdd:cd16289    24 ALLVKTPDGAVLLDGGMpqAADMLLDNMRALGVAPGDLKLILHSHAHADHAGPLAALKRA 83
PRK00055 PRK00055
ribonuclease Z; Reviewed
 1-64 1.54e-03

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 39.01  E-value: 1.54e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1488968958   1 MRFCSLGSGS------R-GNATLVESAGCRVLVDNGlslrELHQR-LRSVDVEPGSIDVLLLTHEHGDHVKG 64
Cdd:PRK00055    2 MELTFLGTGSgvptptRnVSSILLRLGGELFLFDCG----EGTQRqLLKTGIKPRKIDKIFITHLHGDHIFG 69
PRK04286 PRK04286
hypothetical protein; Provisional
 1-62 2.60e-03

hypothetical protein; Provisional


Pssm-ID: 235270  Cd Length: 298  Bit Score: 38.41  E-value: 2.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488968958   1 MRFCSLGS---GSRGNATLVESAGCRVLVDNGLSL-----------RELhQRLRSVDVE----PGSIDVLLLTHEHGDHV 62
Cdd:PRK04286    1 MKIIPLASeslGVRSMATFVETKDVRILIDPGVSLaprryglpphpIEL-ERLEEVREKileyAKKADVITISHYHYDHH 79
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 16-71 4.32e-03

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: 37.47  E-value: 4.32e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1488968958  16 LVESAGCRVLVDNG--LSLRELHQRLRSVDVEPGSIDVLLLTHEHGDHVKGVWSFARR 71
Cdd:cd07726    20 LLDGEGRPALIDTGpsSSVPRLLAALEALGIAPEDVDYIILTHIHLDHAGGAGLLAEA 77
metallo-hydrolase-like_MBL-fold cd16281
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 16-64 6.05e-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: 6.05e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1488968958  16 LVESAGCRVLVDNGL---------------SLRELHQRLRSVDVEPGSIDVLLLTHEHGDHVKG 64
Cdd:cd16281    47 LIETGGRNILIDTGIgdkqdpkfrsiyvqhSEHSLLKSLARLGLSPEDITDVILTHLHFDHCGG 110
YtnP-like_MBL-fold cd07728
Bacillus subtilis YtnP and related proteins; MBL-fold metallo hydrolase domain; Bacillus ...
 16-91 6.78e-03

Bacillus subtilis YtnP and related proteins; MBL-fold metallo hydrolase domain; Bacillus subtilis YtnP inhibits the signaling pathway required for the streptomycin production and development of aerial mycelium in Streptomyces griseus. 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: 293814  Cd Length: 249  Bit Score: 36.85  E-value: 6.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488968958  16 LVESAGCRVLVDNGLS---LRELHQR-------------LRSVDVEPGSIDVLLLTHEHGDHVKGVWSFARRHRVEV--- 76
Cdd:cd07728    47 LIQYQGKNYLIDAGIGngkLTEKQKRnfgvteessieesLAELGLTPEDIDYVLMTHLHFDHASGLTKVKGEQLVSVfpn 126

                          90
                  ....*....|....*...
gi 1488968958  77 ---WTTPGTWRAVGAPEI 91
Cdd:cd07728   127 atiYVSEIEWEEMRNPNI 144
 
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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