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Conserved domains on  [gi|499769092|ref|WP_011449826|]
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MBL fold metallo-hydrolase [Methanospirillum hungatei]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 10870184)

MBL fold metallo-hydrolase is most likely a hydrolytic enzyme that may have substrate towards phosphotriesters, esters, and/or lactones

CATH:  3.60.15.10
EC:  3.-.-.-
Gene Ontology:  GO:0016787|GO:0046872
PubMed:  17597585|12177301|11471246|11513844
SCOP:  3001057

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 4-197 5.20e-69

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: 210.58  E-value: 5.20e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092   4 SVLASGSKGNCVYIEGTSGALIIDAGRSAREIlgtkdrKGRLFEAGGNRDLIEGILITHEHGDHVKGLGPLGNALKVSAY 83
Cdd:cd07733    1 SVLASGSKGNCTYLETEDGKLLIDAGLSGRKI------TGRLAEIGRDPEDIDAILVTHEHADHIKGLGVLARKYNVPIY 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092  84 GTSGTLDVTNRMIQTKKNFTFQSVHPGDPFSIGDFTVTAFSVSHDATDPVGYLIEEGGLRICYCTDtgvvtsgmmemikk 163
Cdd:cd07733   75 ATAGTLRAMERKVGLIDVDQKQIFEPGETFSIGDFDVESFGVSHDAADPVGYRFEEGGRRFGMLTD-------------- 140

                        170       180       190
                 ....*....|....*....|....*....|....
gi 499769092 164 sdgvilesnhcpqmlkdgpypafLKRRIASSRGH 197
Cdd:cd07733  141 -----------------------LKQRILSDRGH 151
 
Name Accession Description Interval E-value
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 4-197 5.20e-69

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: 210.58  E-value: 5.20e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092   4 SVLASGSKGNCVYIEGTSGALIIDAGRSAREIlgtkdrKGRLFEAGGNRDLIEGILITHEHGDHVKGLGPLGNALKVSAY 83
Cdd:cd07733    1 SVLASGSKGNCTYLETEDGKLLIDAGLSGRKI------TGRLAEIGRDPEDIDAILVTHEHADHIKGLGVLARKYNVPIY 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092  84 GTSGTLDVTNRMIQTKKNFTFQSVHPGDPFSIGDFTVTAFSVSHDATDPVGYLIEEGGLRICYCTDtgvvtsgmmemikk 163
Cdd:cd07733   75 ATAGTLRAMERKVGLIDVDQKQIFEPGETFSIGDFDVESFGVSHDAADPVGYRFEEGGRRFGMLTD-------------- 140

                        170       180       190
                 ....*....|....*....|....*....|....
gi 499769092 164 sdgvilesnhcpqmlkdgpypafLKRRIASSRGH 197
Cdd:cd07733  141 -----------------------LKQRILSDRGH 151
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 1-232 5.89e-56

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 180.86  E-value: 5.89e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092   1 MNISVLASGSKG-----------------------NCVYIEGTSGALIIDAGRSAREILgtkdrkgRLFEAGGNRdlIEG 57
Cdd:COG1235    1 MKVTFLGSGSSGgvpqigcdcpvcastdprygrtrSSILVEADGTRLLIDAGPDLREQL-------LRLGLDPSK--IDA 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092  58 ILITHEHGDHVKGLGPLG---NALKVSAYGTSGTLDVTNRMI-----QTKKNFTFQSVHPGDPFSIGDFTVTAFSVSHDA 129
Cdd:COG1235   72 ILLTHEHADHIAGLDDLRpryGPNPIPVYATPGTLEALERRFpylfaPYPGKLEFHEIEPGEPFEIGGLTVTPFPVPHDA 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092 130 TDPVGYLIEEGGLRICYCTDTGVVTSGMMEMIKKSDGVILESNHcpqmlkDGPYPaflkrriassrGHLSNEDAGMVLAE 209
Cdd:COG1235  152 GDPVGYRIEDGGKKLAYATDTGYIPEEVLELLRGADLLILDATY------DDPEP-----------GHLSNEEALELLAR 214

                        250       260
                 ....*....|....*....|...
gi 499769092 210 IsrSIHCAILAHLSEENNEPGLA 232
Cdd:COG1235  215 L--GPKRLVLTHLSPDNNDHELD 235
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 55-172 1.73e-17

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: 78.51  E-value: 1.73e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092   55 IEGILITHEHGDHVKGLGPLGNALKVSAYGTSGTLDVTNR-----MIQTKKNFTFQSVHPGDPFSIGDF--TVTAFSVSH 127
Cdd:pfam12706  29 IDAVLLTHDHYDHLAGLLDLREGRPRPLYAPLGVLAHLRRnfpylFLLEHYGVRVHEIDWGESFTVGDGglTVTATPARH 108

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 499769092  128 DA--------TDPVGYLIEEGGLRICYCTDTGVVTSGMMEMIKKSDGVILESN 172
Cdd:pfam12706 109 GSprgldpnpGDTLGFRIEGPGKRVYYAGDTGYFPDEIGERLGGADLLLLDGG 161
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 13-151 4.16e-16

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: 74.51  E-value: 4.16e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092    13 NCVYIEGTSGALIIDAGrsareiLGTKDRKGRLFEAGGNRDlIEGILITHEHGDHVKGLGPLGNALKVSAYGTSGTLDV- 91
Cdd:smart00849   1 NSYLVRDDGGAILIDTG------PGEAEDLLAELKKLGPKK-IDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELl 73

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499769092    92 -------TNRMIQTKKNFTFQSVHPGDPFSIGDFTVTAFSVSHDATDPVGYLIEEGglRICYCTDTG 151
Cdd:smart00849  74 kdllallGELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEG--KILFTGDLL 138
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 55-223 6.47e-09

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: 55.69  E-value: 6.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092   55 IEGILITHEHGDHVKGLGPL-------GNALKVSAYGTSGTLDVTN---RMIQTKKNF--TFQSVHPGDP-FSIGDFTVT 121
Cdd:TIGR02651  52 IDRIFITHLHGDHILGLPGLlstmsfqGRKEPLTIYGPPGIKEFIEtslRVSYTYLNYpiKIHEIEEGGLvFEDDGFKVE 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092  122 AFSVSHDaTDPVGYLIEE--------------------------------------------------GGLRICYCTDTG 151
Cdd:TIGR02651 132 AFPLDHS-IPSLGYRFEEkdrpgkfdrekakelgippgplygklkrgetvtlidgriidpedvlgpprKGRKIAYTGDTR 210

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499769092  152 VVTSgMMEMIKKSDGVILESnhcpqMLKDGpypaflKRRIASSRGHLSNEDAgmvlAEISRSihcA-----ILAHLS 223
Cdd:TIGR02651 211 PCEE-VIEFAKNADLLIHEA-----TFLDE------DKKLAKEYGHSTAAQA----AEIAKE---AnvkrlILTHIS 268
PRK02113 PRK02113
MBL fold metallo-hydrolase;
55-149 3.23e-06

MBL fold metallo-hydrolase;


Pssm-ID: 179371 [Multi-domain]  Cd Length: 252  Bit Score: 47.47  E-value: 3.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092  55 IEGILITHEHGDHVKGLG---PLGNALKVSAYGTSGTLD-VTNRM--------IQTKKNFTFQSVHPGDPFSIGDFTVTA 122
Cdd:PRK02113  67 IDAVLITHEHYDHVGGLDdlrPFCRFGEVPIYAEQYVAErLRSRMpycfvehsYPGVPNIPLREIEPDRPFLVNHTEVTP 146

                         90       100
                 ....*....|....*....|....*..
gi 499769092 123 FSVSHDATDPVGYLIEegglRICYCTD 149
Cdd:PRK02113 147 LRVMHGKLPILGYRIG----KMAYITD 169
GntH_guanitoxin NF041257
guanitoxin biosynthesis MBL fold metallo-hydrolase GntH;
1-247 3.57e-04

guanitoxin biosynthesis MBL fold metallo-hydrolase GntH;


Pssm-ID: 469157 [Multi-domain]  Cd Length: 372  Bit Score: 41.53  E-value: 3.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092   1 MNISVLASG-------SKGNCVYIE---GTSGALIIDAGR-SAREILGtkdrkgrlfeAGGNRDLIEGILITHEHGDHVK 69
Cdd:NF041257  13 MRITFLGSGpppprrgQANTSILVElgnGERDKFFFDIGSgSVANIIA----------LQIPYNLLNKVFITHLHVDHYG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092  70 GL------GPLG---NALKVsaYGTSGTLDV--TNRMIQTKKNF------TFQSVHPGDPFSIG----DF---------- 118
Cdd:NF041257  83 DLpylypfGAWSgrwTPLRV--WGPSGRTPElgTKHMVEGMKEMlawdtdAFSGFPIGDGYEIEvnefDFrdengvvyee 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092 119 ---TVTAFSVSHDATDPVGYLIEEGGLRICYCTDTgVVTSGMMEMIKKSDGVILESNHCPQ--MLKDGpYPAFLKrRIAS 193
Cdd:NF041257 161 ngvTVRSWPRSHAKDGAVSYRLDWNGLSFVFTGDG-RPNELTVEYAKGADVFIHECFDTPEllSGKYG-VPPELA-RYTI 237

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 499769092 194 SRGHLSNEDAGMVLAEISRSIHCAILAHLSEENNEPGLA-IRKAHEALGLAADDV 247
Cdd:NF041257 238 DTHHTPPYAAGKVFSLVQPRLAMATHFFNDPDTVAEILAeIRAHYDGPLSFGPDL 292
 
Name Accession Description Interval E-value
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 4-197 5.20e-69

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: 210.58  E-value: 5.20e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092   4 SVLASGSKGNCVYIEGTSGALIIDAGRSAREIlgtkdrKGRLFEAGGNRDLIEGILITHEHGDHVKGLGPLGNALKVSAY 83
Cdd:cd07733    1 SVLASGSKGNCTYLETEDGKLLIDAGLSGRKI------TGRLAEIGRDPEDIDAILVTHEHADHIKGLGVLARKYNVPIY 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092  84 GTSGTLDVTNRMIQTKKNFTFQSVHPGDPFSIGDFTVTAFSVSHDATDPVGYLIEEGGLRICYCTDtgvvtsgmmemikk 163
Cdd:cd07733   75 ATAGTLRAMERKVGLIDVDQKQIFEPGETFSIGDFDVESFGVSHDAADPVGYRFEEGGRRFGMLTD-------------- 140

                        170       180       190
                 ....*....|....*....|....*....|....
gi 499769092 164 sdgvilesnhcpqmlkdgpypafLKRRIASSRGH 197
Cdd:cd07733  141 -----------------------LKQRILSDRGH 151
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 1-232 5.89e-56

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 180.86  E-value: 5.89e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092   1 MNISVLASGSKG-----------------------NCVYIEGTSGALIIDAGRSAREILgtkdrkgRLFEAGGNRdlIEG 57
Cdd:COG1235    1 MKVTFLGSGSSGgvpqigcdcpvcastdprygrtrSSILVEADGTRLLIDAGPDLREQL-------LRLGLDPSK--IDA 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092  58 ILITHEHGDHVKGLGPLG---NALKVSAYGTSGTLDVTNRMI-----QTKKNFTFQSVHPGDPFSIGDFTVTAFSVSHDA 129
Cdd:COG1235   72 ILLTHEHADHIAGLDDLRpryGPNPIPVYATPGTLEALERRFpylfaPYPGKLEFHEIEPGEPFEIGGLTVTPFPVPHDA 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092 130 TDPVGYLIEEGGLRICYCTDTGVVTSGMMEMIKKSDGVILESNHcpqmlkDGPYPaflkrriassrGHLSNEDAGMVLAE 209
Cdd:COG1235  152 GDPVGYRIEDGGKKLAYATDTGYIPEEVLELLRGADLLILDATY------DDPEP-----------GHLSNEEALELLAR 214

                        250       260
                 ....*....|....*....|...
gi 499769092 210 IsrSIHCAILAHLSEENNEPGLA 232
Cdd:COG1235  215 L--GPKRLVLTHLSPDNNDHELD 235
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
14-239 3.23e-26

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 103.35  E-value: 3.23e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092  14 CVYIEGTSGALIIDAGRsareilGTKdrkGRLFEAGGNRDLIEGILITHEHGDHVKGLGPLGNALKVSA-------YGTS 86
Cdd:COG1234   21 SYLLEAGGERLLIDCGE------GTQ---RQLLRAGLDPRDIDAIFITHLHGDHIAGLPGLLSTRSLAGrekpltiYGPP 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092  87 GTLDVTNRMIQTKK-----NFTFQSVHPGDPFSIGDFTVTAFSVSHdATDPVGYLIEEGGLRICYCTDTGvVTSGMMEMI 161
Cdd:COG1234   92 GTKEFLEALLKASGtdldfPLEFHEIEPGEVFEIGGFTVTAFPLDH-PVPAYGYRFEEPGRSLVYSGDTR-PCEALVELA 169

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499769092 162 KKSDGVILESNHCPQMlkdgpypaflkRRIASSRGHLSNEDAGMVLAEIsrSIHCAILAHLSEENNEPGLAIRKAHEA 239
Cdd:COG1234  170 KGADLLIHEATFLDEE-----------AELAKETGHSTAKEAAELAAEA--GVKRLVLTHFSPRYDDPEELLAEARAV 234
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 12-151 7.16e-20

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: 84.97  E-value: 7.16e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092  12 GNCVYIEgTSGA-LIIDAGRSAREILGTKDRKGRLFEAGGNRDL--------------------IEGILITHEHGDHVKG 70
Cdd:cd07732   13 GNCIEVE-TGGTrILLDFGLPLDPESKYFDEVLDFLELGLLPDIvglyrdplllgglrseedpsVDAVLLSHAHLDHYGL 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092  71 LGPLGNALKVsaYGTSGTLDVTNRMIQTKKNF-----TFQSVHPGDPFSIGDFTVTAFSVSHDATDPVGYLIEEGGLRIC 145
Cdd:cd07732   92 LNYLRPDIPV--YMGEATKRILKALLPFFGEGdpvprNIRVFESGKSFTIGDFTVTPYLVDHSAPGAYAFLIEAPGKRIF 169


                 ....*.
gi 499769092 146 YctdTG 151
Cdd:cd07732  170 Y---TG 172
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 55-206 3.46e-18

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: 81.34  E-value: 3.46e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092  55 IEGILITHEHGDHVKGLGPL-------GNALKVSAYGTSGTLDVTNRMIQ-TKKNFTFQ-SVH-----PGDPFSIGDFTV 120
Cdd:cd07717   51 IDRIFITHLHGDHILGLPGLlstmsllGRTEPLTIYGPKGLKEFLETLLRlSASRLPYPiEVHelepdPGLVFEDDGFTV 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092 121 TAFSVSHDaTDPVGYLIEEgGLRICYCTDTGvVTSGMMEMIKKSDGVILESNHCPQMLKDgpypaflkrriASSRGHLSN 200
Cdd:cd07717  131 TAFPLDHR-VPCFGYRFEE-GRKIAYLGDTR-PCEGLVELAKGADLLIHEATFLDDDAEK-----------AKETGHSTA 196


                 ....*.
gi 499769092 201 EDAGMV 206
Cdd:cd07717  197 KQAAEI 202
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 55-172 1.73e-17

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: 78.51  E-value: 1.73e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092   55 IEGILITHEHGDHVKGLGPLGNALKVSAYGTSGTLDVTNR-----MIQTKKNFTFQSVHPGDPFSIGDF--TVTAFSVSH 127
Cdd:pfam12706  29 IDAVLLTHDHYDHLAGLLDLREGRPRPLYAPLGVLAHLRRnfpylFLLEHYGVRVHEIDWGESFTVGDGglTVTATPARH 108

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 499769092  128 DA--------TDPVGYLIEEGGLRICYCTDTGVVTSGMMEMIKKSDGVILESN 172
Cdd:pfam12706 109 GSprgldpnpGDTLGFRIEGPGKRVYYAGDTGYFPDEIGERLGGADLLLLDGG 161
PDE1 COG5212
cAMP phosphodiesterase [Signal transduction mechanisms];
18-151 3.36e-17

cAMP phosphodiesterase [Signal transduction mechanisms];


Pssm-ID: 444071 [Multi-domain]  Cd Length: 300  Bit Score: 79.62  E-value: 3.36e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092  18 EGTSGALIIDAGRSAREIlgTKDRKGRLFE--AGGNRDLIEGILITHEHGDHVKGLGPL-GNALKVSAYGTSGTLDV--- 91
Cdd:COG5212   36 LGSDDYVLLDAGTVVSGL--ELAEQKGAFKgrQGYVLEHIKGYLISHAHLDHIAGLPILsPDDSPKTIYALPETIDAlrn 113

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499769092  92 -----------TNRMIQTKKNF-TFQSVHPGDPFSIGD--FTVTAFSVSHdATDPVGYLIEEGGLRICYCTDTG 151
Cdd:COG5212  114 hyfnwviwpdfTDIGSAPHLPKyRYVPLKPGQTFPLGGtgLRVTAFPLSH-SVPSSAFLIESGGGAFLYSGDTG 186
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 13-151 4.16e-16

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: 74.51  E-value: 4.16e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092    13 NCVYIEGTSGALIIDAGrsareiLGTKDRKGRLFEAGGNRDlIEGILITHEHGDHVKGLGPLGNALKVSAYGTSGTLDV- 91
Cdd:smart00849   1 NSYLVRDDGGAILIDTG------PGEAEDLLAELKKLGPKK-IDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELl 73

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499769092    92 -------TNRMIQTKKNFTFQSVHPGDPFSIGDFTVTAFSVSHDATDPVGYLIEEGglRICYCTDTG 151
Cdd:smart00849  74 kdllallGELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEG--KILFTGDLL 138
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 3-171 1.32e-15

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: 73.07  E-value: 1.32e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092   3 ISVLASGS-------KGNCVYIEGTSGALIIDAGRSAReilgtkdrkGRLFEAGGNRDLIEGILITHEHGDHVKGLGPLG 75
Cdd:cd16272    1 LTFLGTGGavpsltrNTSSYLLETGGTRILLDCGEGTV---------YRLLKAGVDPDKLDAIFLSHFHLDHIGGLPTLL 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092  76 NALKVSA-------YGTSGTLDVTNRMIQ-----TKKNFTFQSV---HPGDPFSIGDFTVTAFSVSHdaTDP-VGYLIEE 139
Cdd:cd16272   72 FARRYGGrkkpltiYGPKGIKEFLEKLLNfpveiLPLGFPLEIEeleEGGEVLELGDLKVEAFPVKH--SVEsLGYRIEA 149

                        170       180       190
                 ....*....|....*....|....*....|..
gi 499769092 140 GGLRICYCTDTGvVTSGMMEMIKKSDGVILES 171
Cdd:cd16272  150 EGKSIVYSGDTG-PCENLVELAKGADLLIHEC 180
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 55-171 5.50e-15

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: 71.32  E-value: 5.50e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092  55 IEGILITHEHGDHVKGLGPLGNALKVSA----------YGTSGTLDVTNRMIQTKKNFTFQSVHPGDPFSIGDFTVTAFS 124
Cdd:cd07716   51 LDAVVLSHLHPDHCADLGVLQYARRYHPrgarkpplplYGPAGPAERLAALYGLEDVFDFHPIEPGEPLEIGPFTITFFR 130

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 499769092 125 VSHdatdPV---GYLIEEGGLRICYCTDTGvVTSGMMEMIKKSDGVILES 171
Cdd:cd07716  131 TVH----PVpcyAMRIEDGGKVLVYTGDTG-YCDELVEFARGADLLLCEA 175
TaR3-like_MBL-fold cd07715
MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold ...
 12-150 5.16e-14

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: 69.45  E-value: 5.16e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092  12 GN--CVYIEGTSGALIIDAGRSAREiLGTkdrkgRLFEAGGNRDLIegILITHEHGDHVKGL---GPL---GNALKVsaY 83
Cdd:cd07715   21 GNtsCVEVRAGGELLILDAGTGIRE-LGN-----ELMKEGPPGEAH--LLLSHTHWDHIQGFpffAPAydpGNRIHI--Y 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092  84 GTSGTLDVTNRMIQT--------------KKNFTFQSVHPGDPFSIGDFTVTAFSVSHdatdP---VGYLIEEGGLRICY 146
Cdd:cd07715   91 GPHKDGGSLEEVLRRqmsppyfpvpleelLAAIEFHDLEPGEPFSIGGVTVTTIPLNH----PggaLGYRIEEDGKSVVY 166


                 ....
gi 499769092 147 CTDT 150
Cdd:cd07715  167 ATDT 170
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 8-150 2.66e-13

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: 66.90  E-value: 2.66e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092   8 SGSKGN-CVYIEGTSGALIIDAGRSAREilgtkdrkgRLFEAGGNRDLIEGILITHEHGDHVKGL--------------- 71
Cdd:cd07740   11 SGGRLNtCFHVASEAGRFLIDCGASSLI---------ALKRAGIDPNAIDAIFITHLHGDHFGGLpfflldaqfvakrtr 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092  72 -----GPLG------NALKVSAYGTSGTldvtnrmiQTKKNFTFQSVHPGDPFSIGDFTVTAFSVSHDATDPVGYL-IEE 139
Cdd:cd07740   82 pltiaGPPGlrerlrRAMEALFPGSSKV--------PRRFDLEVIELEPGEPTTLGGVTVTAFPVVHPSGALPLALrLEA 153

                        170
                 ....*....|.
gi 499769092 140 GGLRICYCTDT 150
Cdd:cd07740  154 AGRVLAYSGDT 164
class_II_PDE_MBL-fold cd07735
class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium ...
 19-151 2.90e-13

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: 68.01  E-value: 2.90e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092  19 GTSGALIIDAG----RSAREILGTKDRKGRLFEAGGNRDLIEGILITHEHGDHVKGL--------GPLGNALKVsaYGTS 86
Cdd:cd07735   26 GSDGDILLDAGtgvgALSLEEMFNDILFPSQKAAYELYQRIRHYLITHAHLDHIAGLpllspndgGQRGSPKTI--YGLP 103

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499769092  87 GTLDVTNR------------MIQTKKN--FTFQSVHPGDPFSIGDFTVTAFSVSHDATDPVGYLIEEGGLRICYCTDTG 151
Cdd:cd07735  104 ETIDALKKhifnwviwpdftSIPSGKYpyLRLEPIEPEYPIALTGLSVTAFPVSHGVPVSTAFLIRDGGDSFLFFGDTG 182
PhnP-like_MBL-fold cd07736
phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase ...
 14-150 1.65e-12

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: 64.57  E-value: 1.65e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092  14 CVYIEGTSGALIIDAGrsareILGTKDRkgrlFEAGGnrdlIEGILITHEHGDHVKGLGPL--GNALKVSAYGTSGTLDV 91
Cdd:cd07736   39 SALIEVDGERILLDAG-----LTDLAER----FPPGS----IDAILLTHFHMDHVQGLFHLrwGVGDPIPVYGPPDPQGC 105

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499769092  92 TNrMIQTKKNFTFQ-SVHPGDPFSIGDFTVTAFSVSHdaTDP-VGYLIEEGGLRICYCTDT 150
Cdd:cd07736  106 AD-LFKHPGILDFQpLVAPFQSFELGGLKITPLPLNH--SKPtFGYLLESGGKRLAYLTDT 163
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 55-169 1.98e-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: 1.98e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092  55 IEGILITHEHGDHVKGLGPL-------GNALKVsaYGTSGTLDVTNRMIQTKKN---------FTFQSVHPGDPFSIGDF 118
Cdd:cd16279   67 LDAVLLTHAHADHIHGLDDLrpfnrlqQRPIPV--YASEETLDDLKRRFPYFFAatggggvpkLDLHIIEPDEPFTIGGL 144

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 499769092 119 TVTAFSVSHDATDPVGYLIEegglRICYCTDTGVVTSGMMEMIKKSDGVIL 169
Cdd:cd16279  145 EITPLPVLHGKLPSLGFRFG----DFAYLTDVSEIPEESLEKLRGLDVLIL 191
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 23-151 1.62e-11

Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold metallo-hydrolase domain; Arylsulfatase (also known as aryl-sulfate sulfohydrolase, EC 3.1.6.1). Pseudoalteromonas carrageenovora arylsulfatase AtsA may function as a glycosulfohydrolase involved with desulfation of sulfated polysaccharides, which catalyzes hydrolysis of the arylsulfate ester bond, producing the aryl compounds and inorganic sulfate. CD also includes some sequences annotated as ribonucleases. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily.


Pssm-ID: 293805 [Multi-domain]  Cd Length: 193  Bit Score: 61.76  E-value: 1.62e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092  23 ALIIDAGRSAREilgtkdrkgRLFEAGGNRDLIEGILITHEHGDHVKGLGPL-------GNALKVSAYGTSGTLDVTNRM 95
Cdd:cd07719   29 VYLVDAGSGVVR---------RLAQAGLPLGDLDAVFLTHLHSDHVADLPALlltawlaGRKTPLPVYGPPGTRALVDGL 99

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499769092  96 IQTKKNFTFQSVHPGDP--------------------FSIGDFTVTAFSVSHDATDP-VGYLIEEGGLRICYCTDTG 151
Cdd:cd07719  100 LAAYALDIDYRARIGDEgrpdpgalvevheiaaggvvYEDDGVKVTAFLVDHGPVPPaLAYRFDTPGRSVVFSGDTG 176
RnjA COG0595
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];
51-138 1.97e-10

mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 60.85  E-value: 1.97e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092  51 NRDLIEGILITHEHGDHVKGLGPLGNALKVSAYGTSGTLDvtnrMIQTK-------KNFTFQSVHPGDPFSIGDFTVTAF 123
Cdd:COG0595   60 NKDKIKGIVLTHGHEDHIGALPYLLKELNVPVYGTPLTLA----LLEAKlkehgllKKVKLHVVKPGDRIKFGPFKVEFF 135

                         90
                 ....*....|....*
gi 499769092 124 SVSHDATDPVGYLIE 138
Cdd:COG0595  136 RVTHSIPDSLGLAIR 150
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 13-153 2.90e-10

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 58.78  E-value: 2.90e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092  13 NCVYIEGTSGALIIDAGRSAReiLGTKDRKGRLFEAGGNRDLIegiLITHEHGDHV--KGLGPL-GNALKVSAygtsgTL 89
Cdd:COG2220   12 ATFLIETGGKRILIDPVFSGR--ASPVNPLPLDPEDLPKIDAV---LVTHDHYDHLddATLRALkRTGATVVA-----PL 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499769092  90 DVTNRMiqTKKNFT-FQSVHPGDPFSIGDFTVTAFSVSH-------DATDPVGYLIEEGGLRICYCTDTGVV 153
Cdd:COG2220   82 GVAAWL--RAWGFPrVTELDWGESVELGGLTVTAVPARHssgrpdrNGGLWVGFVIETDGKTIYHAGDTGYF 151
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 51-138 3.15e-10

RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a prokaryotic ribonuclease which plays a key part in RNA processing and in RNA degradation. It can act as an endonuclease which is specific for single-stranded regions of RNA irrespective of their sequence or location, and as a processive 5' exonuclease which only acts on substrates having a single phosphate or a hydroxyl at the 5' end. Many bacterial species have only one RNase J, but some, such as Bacillus subtilis, have two. 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: 293800 [Multi-domain]  Cd Length: 248  Bit Score: 58.96  E-value: 3.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092  51 NRDLIEGILITHEHGDHVKGLGPLGNALKVSAYGTSGTLDvtnrMIQTK-------KNFTFQSVHPGDPFSIGDFTVTAF 123
Cdd:cd07714   52 NKDKIKGIFITHGHEDHIGALPYLLPELNVPIYATPLTLA----LIKKKleefkliKKVKLNEIKPGERIKLGDFEVEFF 127

                         90
                 ....*....|....*
gi 499769092 124 SVSHDATDPVGYLIE 138
Cdd:cd07714  128 RVTHSIPDSVGLAIK 142
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
12-151 4.95e-10

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 57.76  E-value: 4.95e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092   12 GNCVYIEGTSGALIIDAGRSAREilgtkDRKGRLFEAGGNRDLIEGILITHEHGDHVKGLGPLGNALKVSAY-------- 83
Cdd:pfam00753   6 VNSYLIEGGGGAVLIDTGGSAEA-----ALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIvvaeeare 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499769092   84 -------GTSGTLDVTNRMIQTKKNFTFQSVHPGDPFSIGDFTVTAfsvsHDATDPVGYLIEEGGLRICYCTDTG 151
Cdd:pfam00753  81 lldeelgLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTH----GPGHGPGHVVVYYGGGKVLFTGDLL 151
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 1-176 1.72e-09

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: 1.72e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092   1 MNISVL--ASGSKGNCVYIEGTSGALIIDAGRsareILGTKDRKGRLFEAGGNRdlIEGILITHEHGDHVkGLGPL---- 74
Cdd:COG1236    1 MKLTFLgaAGEVTGSCYLLETGGTRILIDCGL----FQGGKERNWPPFPFRPSD--VDAVVLTHAHLDHS-GALPLlvke 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092  75 GNALKVsaYGTSGTLDVTNRM------IQTKKN-----FT----------FQSVHPGDPFSIGDFTVTaFsvsHDAtdpv 133
Cdd:COG1236   74 GFRGPI--YATPATADLARILlgdsakIQEEEAeaeplYTeedaeralelFQTVDYGEPFEIGGVRVT-F---HPA---- 143

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 499769092 134 G-------YLIEEGGLRICYCTDTGVVTSGMM---EMIKKSDGVILES-----NHCPQ 176
Cdd:COG1236  144 GhilgsaqVELEVGGKRIVFSGDYGREDDPLLappEPVPPADVLITEStygdrLHPPR 201
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 13-145 2.68e-09

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: 55.85  E-value: 2.68e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092  13 NCVYIEGTSGALIIDAG---RSAREILgtkdrkgRLFEAGGNRdlIEGILITHEHGDHVKGLGPLGNALKVSAYGTSGTL 89
Cdd:COG0491   16 NSYLIVGGDGAVLIDTGlgpADAEALL-------AALAALGLD--IKAVLLTHLHPDHVGGLAALAEAFGAPVYAHAAEA 86

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499769092  90 DVTnRMIQTKKNFTFQSVHP------GDPFSIGDFTVTAFSVS-HDATDpVGYLIEEGGLRIC 145
Cdd:COG0491   87 EAL-EAPAAGALFGREPVPPdrtledGDTLELGGPGLEVIHTPgHTPGH-VSFYVPDEKVLFT 147
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 13-150 4.71e-09

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: 54.98  E-value: 4.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092  13 NCVYIEGTSG-ALIIDAGRSAREilgtkdrkgRLFEAGGNRDL-IEGILITHEHGDHVKGLGPLGNALKVSAYGTSGTLD 90
Cdd:cd06262   11 NCYLVSDEEGeAILIDPGAGALE---------KILEAIEELGLkIKAILLTHGHFDHIGGLAELKEAPGAPVYIHEADAE 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499769092  91 VTNRMIQTKKNFTFQS---------VHPGDPFSIGDFTVTAFSVshdatdP------VGYLIEEGGlrICYCTDT 150
Cdd:cd06262   82 LLEDPELNLAFFGGGPlpppepdilLEDGDTIELGGLELEVIHT------PghtpgsVCFYIEEEG--VLFTGDT 148
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 55-223 6.47e-09

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: 55.69  E-value: 6.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092   55 IEGILITHEHGDHVKGLGPL-------GNALKVSAYGTSGTLDVTN---RMIQTKKNF--TFQSVHPGDP-FSIGDFTVT 121
Cdd:TIGR02651  52 IDRIFITHLHGDHILGLPGLlstmsfqGRKEPLTIYGPPGIKEFIEtslRVSYTYLNYpiKIHEIEEGGLvFEDDGFKVE 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092  122 AFSVSHDaTDPVGYLIEE--------------------------------------------------GGLRICYCTDTG 151
Cdd:TIGR02651 132 AFPLDHS-IPSLGYRFEEkdrpgkfdrekakelgippgplygklkrgetvtlidgriidpedvlgpprKGRKIAYTGDTR 210

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499769092  152 VVTSgMMEMIKKSDGVILESnhcpqMLKDGpypaflKRRIASSRGHLSNEDAgmvlAEISRSihcA-----ILAHLS 223
Cdd:TIGR02651 211 PCEE-VIEFAKNADLLIHEA-----TFLDE------DKKLAKEYGHSTAAQA----AEIAKE---AnvkrlILTHIS 268
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 12-124 1.35e-07

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: 51.40  E-value: 1.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092  12 GNCVYIEGTSG-ALIIDAGRSAREILGTKDRKGRLFEAGGNRdlIEGILITHEHGDHVKGLGPLGNALKVSAYGTSGTLD 90
Cdd:COG2333   11 GDAILIRTPDGkTILIDTGPRPSFDAGERVVLPYLRALGIRR--LDLLVLTHPDADHIGGLAAVLEAFPVGRVLVSGPPD 88

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 499769092  91 VTNRMIQ-----TKKNFTFQSVHPGDPFSIGDFTVTAFS 124
Cdd:COG2333   89 TSETYERllealKEKGIPVRPCRAGDTWQLGGVRFEVLW 127
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 2-80 1.68e-06

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: 47.60  E-value: 1.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092   2 NISVLASGSKGNCVYIEGTSGALIIDAG--RSAREILGtkdrkgRLFEAGGNRDLIEGILITHEHGDHVKGLGPLGNALK 79
Cdd:cd07721    1 GVYQLPLLPPVNAYLIEDDDGLTLIDTGlpGSAKRILK------ALRELGLSPKDIRRILLTHGHIDHIGSLAALKEAPG 74


                 .
gi 499769092  80 V 80
Cdd:cd07721   75 A 75
PRK02113 PRK02113
MBL fold metallo-hydrolase;
55-149 3.23e-06

MBL fold metallo-hydrolase;


Pssm-ID: 179371 [Multi-domain]  Cd Length: 252  Bit Score: 47.47  E-value: 3.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092  55 IEGILITHEHGDHVKGLG---PLGNALKVSAYGTSGTLD-VTNRM--------IQTKKNFTFQSVHPGDPFSIGDFTVTA 122
Cdd:PRK02113  67 IDAVLITHEHYDHVGGLDdlrPFCRFGEVPIYAEQYVAErLRSRMpycfvehsYPGVPNIPLREIEPDRPFLVNHTEVTP 146

                         90       100
                 ....*....|....*....|....*..
gi 499769092 123 FSVSHDATDPVGYLIEegglRICYCTD 149
Cdd:PRK02113 147 LRVMHGKLPILGYRIG----KMAYITD 169
Lactamase_B_3 pfam13483
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 13-146 9.09e-06

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: 44.89  E-value: 9.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092   13 NCVYIEGTSGALIIDAGRSAreiLGTKDRKGrlfeaggNRDLIegiLITHEHGDHvkglgplgnalkvsayGTSGTLdvt 92
Cdd:pfam13483   8 SSFLIEGGGARILTDPFRAT---VGYRPPPV-------TADLV---LISHGHDDH----------------GHPETL--- 55

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092   93 nrmiqtKKNFTFqsVHPGDPFSIGDFTVTAFSVSHDATDP------VGYLIEEGGLRICY 146
Cdd:pfam13483  56 ------PGNPHV--LDGGGSYTVGGLEIRGVPTDHDRVGGrrrggnSIFLFEQDGLTIYH 107
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 12-131 1.37e-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: 44.82  E-value: 1.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092  12 GNCVYIEGTSGALIIDAGrsAREILGTKDRKGRLFEAGGNRdlIEGILITHEHGDHVKGLGPLGNALKVSAYGTSGTLDV 91
Cdd:cd07731   10 GDAILIQTPGKTILIDTG--PRDSFGEDVVVPYLKARGIKK--LDYLILTHPDADHIGGLDAVLKNFPVKEVYMPGVTHT 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 499769092  92 T---NRMIQT--KKNFTFQSVHPGDPFSIGDFTVTAFSVSHDATD 131
Cdd:cd07731   86 TktyEDLLDAikEKGIPVTPCKAGDRWQLGGVSFEVLSPPKDDYD 130
PRK00055 PRK00055
ribonuclease Z; Reviewed
 55-206 6.34e-05

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 43.63  E-value: 6.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092  55 IEGILITHEHGDHVKGLGPL-------GNALKVSAYGTSGTLDVTNRMIQTKKNFTFQSVHPGDP--------FSIGDFT 119
Cdd:PRK00055  54 IDKIFITHLHGDHIFGLPGLlstrslsGRTEPLTIYGPKGIKEFVETLLRASGSLGYRIAEKDKPgkldaeklKALGVPP 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092 120 VTAFS---VSHDATDPVGYLI--------EEGGLRICYCTDTgVVTSGMMEMIKKSDGVILESnhcpqMLKDGpypaflK 188
Cdd:PRK00055 134 GPLFGklkRGEDVTLEDGRIInpadvlgpPRKGRKVAYCGDT-RPCEALVELAKGADLLVHEA-----TFGDE------D 201

                        170
                 ....*....|....*...
gi 499769092 189 RRIASSRGHLSNEDAGMV 206
Cdd:PRK00055 202 EELAKEYGHSTARQAAEI 219
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 13-122 9.83e-05

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: 42.14  E-value: 9.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092  13 NCVYI---EGTSGALIIDAGRSAREILGTKDRKGRLfeaggnrdlIEGILITHEHGDHVKGLGPLGNALKVSAYgtsgtl 89
Cdd:cd16275   12 NYSYIiidKATREAAVVDPAWDIEKILAKLNELGLT---------LTGILLTHSHFDHVNLVEPLLAKYDAPVY------ 76

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 499769092  90 dvtnrMIQTKKNFT------FQSVHPGDPFSIGDFTVTA 122
Cdd:cd16275   77 -----MSKEEIDYYgfrcpnLIPLEDGDTIKIGDTEITC 110
metallo-hydrolase-like_MBL-fold cd07741
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 55-221 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) 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: 42.18  E-value: 1.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092  55 IEGILITHEHGDH-------VKGLGPLGNALKVSAYGTSGTLDVTNRMI-QTKKNFTFQSVH--PGDPFSIGDFTVTAFS 124
Cdd:cd07741   54 LDAIILSHRHLDHsndanvlIEAMTEGGFKKRGTLLAPEDALNGEPVVLlYYHRRKLEEIEIleEGDEYELGGIKIEATR 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092 125 VSHDATDPVGYLIEEGGLRICYCTDTGvVTSGMMEMIKKSDGVILesnhcpqmlkdgpYPAFLKRRiaSSRGHLSNEDAG 204
Cdd:cd07741  134 HKHSDPTTYGFIFRTSDKKIGYISDTR-YFEELIEYYSNCDVLII-------------NVTRPRPR--KGVDHLSVEDVE 197

                        170
                 ....*....|....*..
gi 499769092 205 MVLAEISRSihCAILAH 221
Cdd:cd07741  198 KILKEIKPK--LAILTH 212
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 15-141 1.36e-04

hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione hydrolase (EC 3.1.2.6, also known as, glyoxalase II; S-2-hydroxylacylglutathione hydrolase; hydroxyacylglutathione hydrolase; acetoacetylglutathione hydrolase). In the second step of the glycoxlase system this enzyme hydrolyzes S-d-lactoylglutathione to d-lactate and regenerates glutathione in the process. It has broad substrate specificity for glutathione thiol esters, hydrolyzing a number of these species to their corresponding carboxylic acids and reduced glutathione. It appears to hydrolyze 2-hydroxy thiol esters with greatest efficiency. It belongs to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293809 [Multi-domain]  Cd Length: 165  Bit Score: 41.68  E-value: 1.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092  15 VYIEGTSGALIIDAGrSAREILGT-KDRKGRLfeaggnrdliEGILITHEHGDHVKGLGPLGNA---LKV--SAYGTSGT 88
Cdd:cd07723   14 IVDEATGEAAVVDPG-EAEPVLAAlEKNGLTL----------TAILTTHHHWDHTGGNAELKALfpdAPVygPAEDRIPG 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 499769092  89 LDvtnrmiqtkknftfQSVHPGDPFSIGDFTVTAFSVS-HdaT-DPVGYLIEEGG 141
Cdd:cd07723   83 LD--------------HPVKDGDEIKLGGLEVKVLHTPgH--TlGHICYYVPDEP 121
PRK00685 PRK00685
metal-dependent hydrolase; Provisional
 58-161 3.28e-04

metal-dependent hydrolase; Provisional


Pssm-ID: 234811 [Multi-domain]  Cd Length: 228  Bit Score: 40.95  E-value: 3.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092  58 ILITHEHGDHvkglgpLGNALKVS-AYGTS--GTLDVTNrMIQTKKNFTFQSVHPGDPFSIGDFTVT---AF-SVSHDAT 130
Cdd:PRK00685  44 ILLTHGHGDH------LGDTVEIAkRTGATviANAELAN-YLSEKGVEKTHPMNIGGTVEFDGGKVKltpALhSSSFIDE 116

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 499769092 131 D-------PVGYLIEEGGLRICYCTDTGVVtsGMMEMI 161
Cdd:PRK00685 117 DgitylgnPTGFVITFEGKTIYHAGDTGLF--SDMKLI 152
GntH_guanitoxin NF041257
guanitoxin biosynthesis MBL fold metallo-hydrolase GntH;
1-247 3.57e-04

guanitoxin biosynthesis MBL fold metallo-hydrolase GntH;


Pssm-ID: 469157 [Multi-domain]  Cd Length: 372  Bit Score: 41.53  E-value: 3.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092   1 MNISVLASG-------SKGNCVYIE---GTSGALIIDAGR-SAREILGtkdrkgrlfeAGGNRDLIEGILITHEHGDHVK 69
Cdd:NF041257  13 MRITFLGSGpppprrgQANTSILVElgnGERDKFFFDIGSgSVANIIA----------LQIPYNLLNKVFITHLHVDHYG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092  70 GL------GPLG---NALKVsaYGTSGTLDV--TNRMIQTKKNF------TFQSVHPGDPFSIG----DF---------- 118
Cdd:NF041257  83 DLpylypfGAWSgrwTPLRV--WGPSGRTPElgTKHMVEGMKEMlawdtdAFSGFPIGDGYEIEvnefDFrdengvvyee 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092 119 ---TVTAFSVSHDATDPVGYLIEEGGLRICYCTDTgVVTSGMMEMIKKSDGVILESNHCPQ--MLKDGpYPAFLKrRIAS 193
Cdd:NF041257 161 ngvTVRSWPRSHAKDGAVSYRLDWNGLSFVFTGDG-RPNELTVEYAKGADVFIHECFDTPEllSGKYG-VPPELA-RYTI 237

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 499769092 194 SRGHLSNEDAGMVLAEISRSIHCAILAHLSEENNEPGLA-IRKAHEALGLAADDV 247
Cdd:NF041257 238 DTHHTPPYAAGKVFSLVQPRLAMATHFFNDPDTVAEILAeIRAHYDGPLSFGPDL 292
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 18-74 4.52e-04

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: 40.41  E-value: 4.52e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 499769092  18 EGTSGALIIDAGRSAREILGTKDRKGRLfeaggnrdlIEGILITHEHGDHVKGLGPL 74
Cdd:cd16322   19 EGGGEAVLVDPGDESEKLLARFGTTGLT---------LLYILLTHAHFDHVGGVADL 66
metallo-hydrolase-like_MBL-fold cd07739
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 13-136 5.81e-04

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


Pssm-ID: 293825 [Multi-domain]  Cd Length: 201  Bit Score: 40.18  E-value: 5.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092  13 NCVYIEGTSGALIIDAG-------RSAREILGTkdrkgrlfeaggNRDLiEGILITHEHGDHVKGLGPLGNAL-KVSAYG 84
Cdd:cd07739   17 TSTLIYGETEAVLVDAQftradaeRLADWIKAS------------GKTL-TTIYITHGHPDHYFGLEVLLEAFpDAKVVA 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499769092  85 TSGTLDVTNRMIQTKKNFTFQS-------------VHPGDPFSIGDFTVTAFSVSHDATDPVGYL 136
Cdd:cd07739   84 TPAVVAHIKAQLEPKLAFWGPLlggnaparlvvpePLDGDTLTLEGHPLEIVGVGGGDTDDTTYL 148
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 15-70 9.37e-04

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


Pssm-ID: 293829 [Multi-domain]  Cd Length: 197  Bit Score: 39.44  E-value: 9.37e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 499769092  15 VYIEGTSGALIIDAGRSarEILGTKDRKgrLFEAGGNRdlIEGILITHEHGDHVKG 70
Cdd:cd07743   12 VYVFGDKEALLIDSGLD--EDAGRKIRK--ILEELGWK--LKAIINTHSHADHIGG 61
arylsulfatase_Sdsa1-like_MBL-fold cd07710
Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and ...
 12-70 9.92e-04

Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and related proteins; MBL-fold metallo-hydrolase domain; Arylsulfatase (also known as aryl-sulfate sulfohydrolase, EC 3.1.6.1). Pseudomonas aeruginosa SdsA1 is a secreted SDS hydrolase that allows the bacterium to use primary sulfates such as the detergent SDS common in commercial personal hygiene products as a sole carbon or sulfur source. Pseudomonas inverting secondary alkylsulfatase 1 (Pisa1) is specific for secondary alkyl sulfates. 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: 293796 [Multi-domain]  Cd Length: 239  Bit Score: 39.79  E-value: 9.92e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499769092  12 GNCVYIEGTSGALIIDAGRSA----------REILGTKDrkgrlfeaggnrdlIEGILITHEHGDHVKG 70
Cdd:cd07710   18 SNMTFIEGDTGLIIIDTLESAeaakaalelfRKHTGDKP--------------VKAIIYTHSHPDHFGG 72
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 1-77 2.09e-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.


Pssm-ID: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 38.32  E-value: 2.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092   1 MNISVLASGSKGNCVYIEGTSGALIIDAG---RSAREIlgtkdrkgrlfeaggnRDLIEGI--------LITHEHGDHVk 69
Cdd:cd16282    4 ALIGPDGGGFISNIGFIVGDDGVVVIDTGaspRLARAL----------------LAAIRKVtdkpvryvVNTHYHGDHT- 66


                 ....*...
gi 499769092  70 glgpLGNA 77
Cdd:cd16282   67 ----LGNA 70
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 55-122 2.89e-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: 2.89e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499769092  55 IEGILITHEHGDHVKGLGPL-----GNALKVSAYGTSgtldvTNRMIQTKKNFTFQSVHPGDPFSIGDFTVTA 122
Cdd:cd07722   57 ISDILLTHWHHDHVGGLPDVldllrGPSPRVYKFPRP-----EEDEDPDEDGGDIHDLQDGQVFKVEGATLRV 124
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 13-127 5.16e-03

Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase domain; This subgroup includes Salmonella enterica serovar typhimurium YcbL which has type II hydroxyacylglutathione hydrolase (EC 3.1.2.6, also known as glyoxalase II) activity, and has a single metal ion binding site, and Thermus thermophilus TTHA1623 which does not have GLX2 activity and has two metal ion binding sites with a glyoxalase II-type metal coordination. 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: 293823 [Multi-domain]  Cd Length: 190  Bit Score: 37.15  E-value: 5.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092  13 NC--VYIEGTSGALIIDAGRSAREILGTKDRKGRLFEAggnrdliegILITHEHGDHVKGLGPLGNALKVSAYGTS---- 86
Cdd:cd07737   12 NCslIWCEETKEAAVIDPGGDADKILQAIEDLGLTLKK---------ILLTHGHLDHVGGAAELAEHYGVPIIGPHkedk 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 499769092  87 ---GTLDVTNRMiqtkknFTF---QSVHP------GDPFSIGDFTvtaFSVSH 127
Cdd:cd07737   83 fllENLPEQSQM------FGFppaEAFTPdrwleeGDTVTVGNLT---LEVLH 126
PQQB-like_MBL-fold cd16274
Coenzyme pyrroloquinoline quinone (PQQ) synthesis protein B and related proteins; MBL-fold ...
 45-169 6.95e-03

Coenzyme pyrroloquinoline quinone (PQQ) synthesis protein B and related proteins; MBL-fold metallo hydrolase domainhydrolase domain; PQQB is essential for the synthesis of the cofactor pyrroloquinoline quinone (PQQ) in Klebsiella pneumonia. PqqB is not directly involved in the PQQ biosynthesis but may serve as a carrier for PQQ when PQQ is released from PqqC. 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: 293832 [Multi-domain]  Cd Length: 220  Bit Score: 36.83  E-value: 6.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499769092  45 LFEAGGNRDL-IEGILITHEHGDHVKGLGPLGNALKVSAYGTSGTLDVTNrmiqtkKNFTF------------QSVHPGD 111
Cdd:cd16274   70 LQPRPGLRDTpIAAVLLTDAEIDHTTGLLSLREGQPLTVYATAPVLEDLT------TNFPFfvllhayggvrrHRILPGE 143

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499769092 112 PFSIGDF---TVTAFSV-------SHDATDP-----VGYLIEEG--GLRICYCTDTGVVTSGMMEMIKKSDGVIL 169
Cdd:cd16274  144 PFTLAGCpglTVTPFPVpgkaplySEHRDAPepgdtIGLRIEDGrtGGRLFYAPGCAAVTDELRARLAGADCLLF 218
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 13-71 8.49e-03

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: 36.76  E-value: 8.49e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499769092  13 NCVYIEgTSGALI-IDAGrsAREILGtkDRKGRLFE----AGGNRDLIEGILITHEHGDHVKGL 71
Cdd:cd07720   50 NAFLVR-TGGRLIlVDTG--AGGLFG--PTAGKLLAnlaaAGIDPEDIDDVLLTHLHPDHIGGL 108
 
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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