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Conserved domains on  [gi|663531341|gb|AIF21304|]
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beta-lactamase domain-containing protein [uncultured marine group II/III euryarchaeote KM3_99_A09]

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]; ...
 5-230 8.73e-43

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


:

Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 146.19  E-value: 8.73e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663531341   5 ITHLGSGSGG-----------------------NATLLSTPESKILIDCGFSGRQLERRLGLlemKPTDLDAILVSHFHG 61
Cdd:COG1235    3 VTFLGSGSSGgvpqigcdcpvcastdprygrtrSSILVEADGTRLLIDAGPDLREQLLRLGL---DPSKIDAILLTHEHA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663531341  62 DHSKGA-VIANK--KWDIPLMMNFQSCERL------------GLDPVNECKLFESLDLiamgPDLSILPVPVNHGEADNV 126
Cdd:COG1235   80 DHIAGLdDLRPRygPNPIPVYATPGTLEALerrfpylfapypGKLEFHEIEPGEPFEI----GGLTVTPFPVPHDAGDPV 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663531341 127 GFIASHLGERAAVVTDLGSWSDELARHLEGCVHISIEANYDskrlweGPYPerlkqriagrgGHLSNRQTADLLSHVVTK 206
Cdd:COG1235  156 GYRIEDGGKKLAYATDTGYIPEEVLELLRGADLLILDATYD------DPEP-----------GHLSNEEALELLARLGPK 218

                        250       260
                 ....*....|....*....|....
gi 663531341 207 KtrsIVLCHLSAQNNAPHLAESEV 230
Cdd:COG1235  219 R---LVLTHLSPDNNDHELDYDEL 239
 
Name Accession Description Interval E-value
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 5-230 8.73e-43

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 146.19  E-value: 8.73e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663531341   5 ITHLGSGSGG-----------------------NATLLSTPESKILIDCGFSGRQLERRLGLlemKPTDLDAILVSHFHG 61
Cdd:COG1235    3 VTFLGSGSSGgvpqigcdcpvcastdprygrtrSSILVEADGTRLLIDAGPDLREQLLRLGL---DPSKIDAILLTHEHA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663531341  62 DHSKGA-VIANK--KWDIPLMMNFQSCERL------------GLDPVNECKLFESLDLiamgPDLSILPVPVNHGEADNV 126
Cdd:COG1235   80 DHIAGLdDLRPRygPNPIPVYATPGTLEALerrfpylfapypGKLEFHEIEPGEPFEI----GGLTVTPFPVPHDAGDPV 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663531341 127 GFIASHLGERAAVVTDLGSWSDELARHLEGCVHISIEANYDskrlweGPYPerlkqriagrgGHLSNRQTADLLSHVVTK 206
Cdd:COG1235  156 GYRIEDGGKKLAYATDTGYIPEEVLELLRGADLLILDATYD------DPEP-----------GHLSNEEALELLARLGPK 218

                        250       260
                 ....*....|....*....|....
gi 663531341 207 KtrsIVLCHLSAQNNAPHLAESEV 230
Cdd:COG1235  219 R---LVLTHLSPDNNDHELDYDEL 239
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 8-190 1.74e-30

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: 111.20  E-value: 1.74e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663531341   8 LGSGSGGNATLLSTPESKILIDCGFSGRQLERRLGLLEMKPTDLDAILVSHFHGDHSKGAVIANKKWDIPLMMNFQSCE- 86
Cdd:cd07733    3 LASGSKGNCTYLETEDGKLLIDAGLSGRKITGRLAEIGRDPEDIDAILVTHEHADHIKGLGVLARKYNVPIYATAGTLRa 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663531341  87 ---RLGLDPVNECKLFESLDLIAMGpDLSILPVPVNHGEADNVGFIASHLGERAAVVTDlgswsdelarhlegcvhisie 163
Cdd:cd07733   83 merKVGLIDVDQKQIFEPGETFSIG-DFDVESFGVSHDAADPVGYRFEEGGRRFGMLTD--------------------- 140

                        170       180
                 ....*....|....*....|....*..
gi 663531341 164 anydskrlwegpyperLKQRIAGRGGH 190
Cdd:cd07733  141 ----------------LKQRILSDRGH 151
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 26-203 1.41e-11

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: 61.94  E-value: 1.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663531341   26 ILIDCGFSGR-QLERRLGLLEMKPTDLDAILVSHFHGDH----------SKGAVIANKKWDIPLMMNFQSCERLGLDPVN 94
Cdd:pfam12706   3 ILIDPGPDLRqQALPALQPGRLRDDPIDAVLLTHDHYDHlaglldlregRPRPLYAPLGVLAHLRRNFPYLFLLEHYGVR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663531341   95 --ECKLFESLDLiaMGPDLSILPVPVNHG--------EADNVGFIASHLGERAAVVTDLGSWSDELARHLEGCVHISIEA 164
Cdd:pfam12706  83 vhEIDWGESFTV--GDGGLTVTATPARHGsprgldpnPGDTLGFRIEGPGKRVYYAGDTGYFPDEIGERLGGADLLLLDG 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 663531341  165 NYDSKRLWEGPyperlkqriagrgGHLSNRQTADLLSHV 203
Cdd:pfam12706 161 GAWRDDEMIHM-------------GHMTPEEAVEAAADL 186
PRK00055 PRK00055
ribonuclease Z; Reviewed
 3-63 4.68e-10

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 58.65  E-value: 4.68e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 663531341   3 LSITHLGSGSG-------GNATLLSTPESKILIDCGfSGRQleRRLGLLEMKPTDLDAILVSHFHGDH 63
Cdd:PRK00055   2 MELTFLGTGSGvptptrnVSSILLRLGGELFLFDCG-EGTQ--RQLLKTGIKPRKIDKIFITHLHGDH 66
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 15-81 1.85e-09

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: 55.64  E-value: 1.85e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 663531341    15 NATLLSTPESKILIDCGFsGRQLERRLGLLEMKPTDLDAILVSHFHGDHSKGAVIANKKWDIPLMMN 81
Cdd:smart00849   1 NSYLVRDDGGAILIDTGP-GEAEDLLAELKKLGPKKIDAIILTHGHPDHIGGLPELLEAPGAPVYAP 66
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 5-66 6.49e-07

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: 49.52  E-value: 6.49e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 663531341    5 ITHLGSGSG-------GNATLLSTPESKILIDCGfSG--RQLeRRLGLlemKPTDLDAILVSHFHGDHSKG 66
Cdd:TIGR02651   2 ITFLGTGGGvptkernLPSIALKLNGELWLFDCG-EGtqRQM-LRSGI---SPMKIDRIFITHLHGDHILG 67
 
Name Accession Description Interval E-value
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 5-230 8.73e-43

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 146.19  E-value: 8.73e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663531341   5 ITHLGSGSGG-----------------------NATLLSTPESKILIDCGFSGRQLERRLGLlemKPTDLDAILVSHFHG 61
Cdd:COG1235    3 VTFLGSGSSGgvpqigcdcpvcastdprygrtrSSILVEADGTRLLIDAGPDLREQLLRLGL---DPSKIDAILLTHEHA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663531341  62 DHSKGA-VIANK--KWDIPLMMNFQSCERL------------GLDPVNECKLFESLDLiamgPDLSILPVPVNHGEADNV 126
Cdd:COG1235   80 DHIAGLdDLRPRygPNPIPVYATPGTLEALerrfpylfapypGKLEFHEIEPGEPFEI----GGLTVTPFPVPHDAGDPV 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663531341 127 GFIASHLGERAAVVTDLGSWSDELARHLEGCVHISIEANYDskrlweGPYPerlkqriagrgGHLSNRQTADLLSHVVTK 206
Cdd:COG1235  156 GYRIEDGGKKLAYATDTGYIPEEVLELLRGADLLILDATYD------DPEP-----------GHLSNEEALELLARLGPK 218

                        250       260
                 ....*....|....*....|....
gi 663531341 207 KtrsIVLCHLSAQNNAPHLAESEV 230
Cdd:COG1235  219 R---LVLTHLSPDNNDHELDYDEL 239
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 8-190 1.74e-30

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: 111.20  E-value: 1.74e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663531341   8 LGSGSGGNATLLSTPESKILIDCGFSGRQLERRLGLLEMKPTDLDAILVSHFHGDHSKGAVIANKKWDIPLMMNFQSCE- 86
Cdd:cd07733    3 LASGSKGNCTYLETEDGKLLIDAGLSGRKITGRLAEIGRDPEDIDAILVTHEHADHIKGLGVLARKYNVPIYATAGTLRa 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663531341  87 ---RLGLDPVNECKLFESLDLIAMGpDLSILPVPVNHGEADNVGFIASHLGERAAVVTDlgswsdelarhlegcvhisie 163
Cdd:cd07733   83 merKVGLIDVDQKQIFEPGETFSIG-DFDVESFGVSHDAADPVGYRFEEGGRRFGMLTD--------------------- 140

                        170       180
                 ....*....|....*....|....*..
gi 663531341 164 anydskrlwegpyperLKQRIAGRGGH 190
Cdd:cd07733  141 ----------------LKQRILSDRGH 151
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
5-244 1.09e-16

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 77.16  E-value: 1.09e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663531341   5 ITHLGSGSG-------GNATLLSTPESKILIDCGfSGRQleRRLGLLEMKPTDLDAILVSHFHGDHskgavIAnkkwDIP 77
Cdd:COG1234    3 LTFLGTGGAvptpgraTSSYLLEAGGERLLIDCG-EGTQ--RQLLRAGLDPRDIDAIFITHLHGDH-----IA----GLP 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663531341  78 LM---MNFQSCER----LGLDPVNE-----CKLFES-----LDLIAMGP-------DLSILPVPVNHGeADNVGFIASHL 133
Cdd:COG1234   71 GLlstRSLAGREKpltiYGPPGTKEflealLKASGTdldfpLEFHEIEPgevfeigGFTVTAFPLDHP-VPAYGYRFEEP 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663531341 134 GERAAVVTDlGSWSDELARHLEGCVHISIEANydskrlwegpYPERLKQRiAGRGGHLSNRQTADLLSHVvtkKTRSIVL 213
Cdd:COG1234  150 GRSLVYSGD-TRPCEALVELAKGADLLIHEAT----------FLDEEAEL-AKETGHSTAKEAAELAAEA---GVKRLVL 214

                        250       260       270
                 ....*....|....*....|....*....|.
gi 663531341 214 CHLSAQNNAPhlaeSEVLMEIDDIFEGDISI 244
Cdd:COG1234  215 THFSPRYDDP----EELLAEARAVFPGPVEL 241
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 26-203 1.41e-11

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: 61.94  E-value: 1.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663531341   26 ILIDCGFSGR-QLERRLGLLEMKPTDLDAILVSHFHGDH----------SKGAVIANKKWDIPLMMNFQSCERLGLDPVN 94
Cdd:pfam12706   3 ILIDPGPDLRqQALPALQPGRLRDDPIDAVLLTHDHYDHlaglldlregRPRPLYAPLGVLAHLRRNFPYLFLLEHYGVR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663531341   95 --ECKLFESLDLiaMGPDLSILPVPVNHG--------EADNVGFIASHLGERAAVVTDLGSWSDELARHLEGCVHISIEA 164
Cdd:pfam12706  83 vhEIDWGESFTV--GDGGLTVTATPARHGsprgldpnPGDTLGFRIEGPGKRVYYAGDTGYFPDEIGERLGGADLLLLDG 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 663531341  165 NYDSKRLWEGPyperlkqriagrgGHLSNRQTADLLSHV 203
Cdd:pfam12706 161 GAWRDDEMIHM-------------GHMTPEEAVEAAADL 186
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 5-227 2.24e-11

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: 62.08  E-value: 2.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663531341   5 ITHLGSGSGG-------NATLLSTPESKILIDCGfSG--RQLeRRLGLlemKPTDLDAILVSHFHGDHSKG-----AVIA 70
Cdd:cd07717    1 LTFLGTGSAVptpernlSSIALRLEGELWLFDCG-EGtqRQL-LRAGL---SPSKIDRIFITHLHGDHILGlpgllSTMS 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663531341  71 NKKWDIPL--------------MMNFqSCERLGLdPVNECKLFESLDLIAMGPDLSILPVPVNHGeADNVGFIAShLGER 136
Cdd:cd07717   76 LLGRTEPLtiygpkglkefletLLRL-SASRLPY-PIEVHELEPDPGLVFEDDGFTVTAFPLDHR-VPCFGYRFE-EGRK 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663531341 137 AAVVTDlGSWSDELARHLEGC---VHisiEANYDskrlwegpypERLKQRiAGRGGHLSNRQTADL--LSHVvtkktRSI 211
Cdd:cd07717  152 IAYLGD-TRPCEGLVELAKGAdllIH---EATFL----------DDDAEK-AKETGHSTAKQAAEIakKAGV-----KKL 211

                        250
                 ....*....|....*...
gi 663531341 212 VLCHLSA--QNNAPHLAE 227
Cdd:cd07717  212 VLTHFSAryKDPEELLKE 229
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 5-68 1.75e-10

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: 58.62  E-value: 1.75e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 663531341   5 ITHLGSGS--GGNATLLSTPESKILIDCG--FSGRQLERR-LGLLEMKPTDLDAILVSHFHGDHSkGAV 68
Cdd:cd16295    1 LTFLGAARevTGSCYLLETGGKRILLDCGlfQGGKELEELnNEPFPFDPKEIDAVILTHAHLDHS-GRL 68
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 5-80 2.83e-10

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: 58.39  E-value: 2.83e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 663531341   5 ITHLGSGSGGNATLLSTPESKILIDCGF--SGRQLERRLGLLEMKPTDLDAILVSHFHGDHSKGAVIANKKWDIPLMM 80
Cdd:cd07721    2 VYQLPLLPPVNAYLIEDDDGLTLIDTGLpgSAKRILKALRELGLSPKDIRRILLTHGHIDHIGSLAALKEAPGAPVYA 79
PRK00055 PRK00055
ribonuclease Z; Reviewed
 3-63 4.68e-10

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 58.65  E-value: 4.68e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 663531341   3 LSITHLGSGSG-------GNATLLSTPESKILIDCGfSGRQleRRLGLLEMKPTDLDAILVSHFHGDH 63
Cdd:PRK00055   2 MELTFLGTGSGvptptrnVSSILLRLGGELFLFDCG-EGTQ--RQLLKTGIKPRKIDKIFITHLHGDH 66
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 5-63 4.89e-10

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: 57.27  E-value: 4.89e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 663531341   5 ITHLGSGSG-------GNATLLSTPESKILIDCGFSG-RQLeRRLGLlemKPTDLDAILVSHFHGDH 63
Cdd:cd16272    1 LTFLGTGGAvpsltrnTSSYLLETGGTRILLDCGEGTvYRL-LKAGV---DPDKLDAIFLSHFHLDH 63
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 15-81 1.85e-09

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: 55.64  E-value: 1.85e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 663531341    15 NATLLSTPESKILIDCGFsGRQLERRLGLLEMKPTDLDAILVSHFHGDHSKGAVIANKKWDIPLMMN 81
Cdd:smart00849   1 NSYLVRDDGGAILIDTGP-GEAEDLLAELKKLGPKKIDAIILTHGHPDHIGGLPELLEAPGAPVYAP 66
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
13-81 2.00e-09

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 55.84  E-value: 2.00e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663531341   13 GGNATLLSTPESKILIDCGFSG-RQLERRLGLLEMKPTDLDAILVSHFHGDHSKGAVIANKKWDIPLMMN 81
Cdd:pfam00753   5 QVNSYLIEGGGGAVLIDTGGSAeAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVV 74
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 6-66 4.77e-09

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: 54.57  E-value: 4.77e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 663531341   6 THLGSG----SGGNA---TLLSTPESKILIDCGFSGRQLERRLGLlemKPTDLDAILVSHFHGDHSKG 66
Cdd:cd07740    1 TFLGSGdafgSGGRLntcFHVASEAGRFLIDCGASSLIALKRAGI---DPNAIDAIFITHLHGDHFGG 65
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 1-64 1.00e-08

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 55.19  E-value: 1.00e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 663531341   1 MTLSITHLGSGSGGNATLLSTPESKILIDCGFSGRQLERRLGLLEMKPTDLDAILVSHFHGDHS 64
Cdd:COG1236    1 MKLTFLGAAGEVTGSCYLLETGGTRILIDCGLFQGGKERNWPPFPFRPSDVDAVVLTHAHLDHS 64
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 3-117 1.05e-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: 53.93  E-value: 1.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663531341   3 LSITHLGSGSGGNATLLSTPESKILIDCGFSGRQLERRLGLLEMKPTDLDAILVSHFHGDHSKGA----------VIANK 72
Cdd:COG0491    4 LPGGTPGAGLGVNSYLIVGGDGAVLIDTGLGPADAEALLAALAALGLDIKAVLLTHLHPDHVGGLaalaeafgapVYAHA 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 663531341  73 KwDIPLMMNFQSCERLGLDPVNECKLFESLDLIAMG-PDLSILPVP 117
Cdd:COG0491   84 A-EAEALEAPAAGALFGREPVPPDRTLEDGDTLELGgPGLEVIHTP 128
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 2-155 1.13e-08

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 54.15  E-value: 1.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663531341   2 TLSITHLGsgsggNAT-LLSTPESKILIDCGFSGRQLERRLGLLEMK-PTDLDAILVSHFHGDH-SKGAVIANKKWDIPL 78
Cdd:COG2220    3 GMKITWLG-----HATfLIETGGKRILIDPVFSGRASPVNPLPLDPEdLPKIDAVLVTHDHYDHlDDATLRALKRTGATV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663531341  79 MMNFQSCERL---GLDPVNECKLFESLDLiamgPDLSILPVPVNHGEA-------DNVGFIASHLGERAAVVTDLGsWSD 148
Cdd:COG2220   78 VAPLGVAAWLrawGFPRVTELDWGESVEL----GGLTVTAVPARHSSGrpdrnggLWVGFVIETDGKTIYHAGDTG-YFP 152


                 ....*..
gi 663531341 149 ELARHLE 155
Cdd:COG2220  153 EMKEIGE 159
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 5-63 1.89e-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: 52.83  E-value: 1.89e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 663531341   5 ITHLG-SGS---GGNAT---LLSTPESKILIDCGfSG--RQLERRLGllemkPTDLDAILVSHFHGDH 63
Cdd:cd07716    2 LTVLGcSGSypgPGGACsgyLLEADGFRILLDCG-SGvlSRLQRYID-----PEDLDAVVLSHLHPDH 63
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 15-73 2.25e-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: 53.32  E-value: 2.25e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 663531341  15 NATLLSTPESKILIDCGFSGR------QLERRLGLLEMKPTDLDAILVSHFHGDHSKGAVIANKK 73
Cdd:cd07720   50 NAFLVRTGGRLILVDTGAGGLfgptagKLLANLAAAGIDPEDIDDVLLTHLHPDHIGGLVDAGGK 114
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 8-63 3.43e-08

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: 52.13  E-value: 3.43e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 663531341   8 LGSGS-------GGNATLLSTPESKILIDCGfSGRQleRRLGLLEMKPTDLDAILVSHFHGDH 63
Cdd:cd07719    5 LGTGGpipdpdrAGPSTLVVVGGRVYLVDAG-SGVV--RRLAQAGLPLGDLDAVFLTHLHSDH 64
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 15-82 4.14e-07

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: 48.83  E-value: 4.14e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663531341  15 NATLLSTPESKILIDCGF----SGRQLERRLGLLEMKPTDLDAILVSHFHGDHSKGAVIANKKWDIPLMMNF 82
Cdd:cd07725   16 NVYLLRDGDETTLIDTGLateeDAEALWEGLKELGLKPSDIDRVLLTHHHPDHIGLAGKLQEKSGATVYILD 87
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 15-110 5.79e-07

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: 48.44  E-value: 5.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663531341  15 NATLLSTPESK-ILIDCGFSGrqLERRLGLLEMKPTDLDAILVSHFHGDHSKGAVIANKKWDIPLMMNfQSCERLGLDPV 93
Cdd:cd06262   11 NCYLVSDEEGEaILIDPGAGA--LEKILEAIEELGLKIKAILLTHGHFDHIGGLAELKEAPGAPVYIH-EADAELLEDPE 87

                         90
                 ....*....|....*..
gi 663531341  94 NECKLFESLDLIAMGPD 110
Cdd:cd06262   88 LNLAFFGGGPLPPPEPD 104
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 5-66 6.49e-07

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: 49.52  E-value: 6.49e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 663531341    5 ITHLGSGSG-------GNATLLSTPESKILIDCGfSG--RQLeRRLGLlemKPTDLDAILVSHFHGDHSKG 66
Cdd:TIGR02651   2 ITFLGTGGGvptkernLPSIALKLNGELWLFDCG-EGtqRQM-LRSGI---SPMKIDRIFITHLHGDHILG 67
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 18-157 7.44e-07

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: 48.24  E-value: 7.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663531341  18 LLSTPESKILIDCG--FsgrqlerRLGLLEMKPTDLDAILVSHFHGDHSKG-----AVIANKKWDIPLMMNFQSCERL-- 88
Cdd:cd16279   39 LIETGGKNILIDTGpdF-------RQQALRAGIRKLDAVLLTHAHADHIHGlddlrPFNRLQQRPIPVYASEETLDDLkr 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663531341  89 ---------------GLDPvNECKLFESLDLiamgPDLSILPVPVNHGEADNVGFIashLGeRAAVVTDLGSWSDELARH 153
Cdd:cd16279  112 rfpyffaatggggvpKLDL-HIIEPDEPFTI----GGLEITPLPVLHGKLPSLGFR---FG-DFAYLTDVSEIPEESLEK 182


                 ....
gi 663531341 154 LEGC 157
Cdd:cd16279  183 LRGL 186
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 14-67 1.69e-06

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: 47.93  E-value: 1.69e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 663531341  14 GNATLLSTPESK-ILIDCG--FSGRQLERRLG--LLEMKPTDLDAILVSHFHGDHSKGA 67
Cdd:COG2333   11 GDAILIRTPDGKtILIDTGprPSFDAGERVVLpyLRALGIRRLDLLVLTHPDADHIGGL 69
SMB-1-like_MBL-B3 cd16313
SMB-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase ...
 11-66 5.44e-06

SMB-1, THIN-B 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 SMB-1- and THIN-B-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: 293871 [Multi-domain]  Cd Length: 254  Bit Score: 46.39  E-value: 5.44e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 663531341  11 GSGG-NATLLSTPESKILIDCGFSG--RQLERRLGLLEMKPTDLDAILVSHFHGDHSKG 66
Cdd:cd16313   18 GTGGiSAVLITSPQGHILIDGGFPKspEQIAASIRQLGFKLEDVKYILSSHDHWDHAGG 76
Int9-11_CPSF2-3-like_MBL-fold cd07734
Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; ...
 8-63 1.81e-05

Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; MBL-fold metallo-hydrolase domain; CPSF3 (cleavage and polyadenylation specificity factor subunit 3; also known as cleavage and polyadenylation specificity factor 73 kDa subunit, CPSF-73) and CPSF2 (also known as cleavage and polyadenylation specificity factor 100 kDa subunit /CPSF-100) are components of the CPSF complex, which plays a role in 3' end processing of pre-mRNAs during cleavage/polyadenylation, and during processing of metazoan histone pre-mRNAs. CPSF3 functions as a 3' endonuclease. Int11 (also known as cleavage and polyadenylation-specific factor (CPSF) 3-like protein, and protein related to CPSF subunits of 68 kDa (RC-68)), and Int9, also known as protein related to CPSF subunits of 74 kDa (RC-74) are subunits of Integrator, a metazoan-specific multifunctional protein complex composed of 14 subunits. Integrator has been implicated in a variety of Pol II transcription events including 3' end processing of snRNA, transcription initiation, promoter-proximal pausing, termination of protein-coding transcripts, and in HVS pre-miRNA 3' end processing. 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: 293820 [Multi-domain]  Cd Length: 193  Bit Score: 44.24  E-value: 1.81e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 663531341   8 LGSGSGGNATLLSTPESKILIDCG-FSGRQL-ERRLGLLEMKPTDLDAILVSHFHGDH 63
Cdd:cd07734    5 GGQEVGRSCFLVEFKGRTVLLDCGmNPGKEDpEACLPQFELLPPEIDAILISHFHLDH 62
RNaseZ_ELAC1_ELAC2-C-term-like_MBL-fold cd07718
Ribonuclease Z ELAC1, C-terminus of ELAC2, and related proteins; MBL-fold metallo-hydrolase ...
 5-63 2.20e-05

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


Pssm-ID: 293804 [Multi-domain]  Cd Length: 204  Bit Score: 44.08  E-value: 2.20e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663531341   5 ITHLGSGS-------GGNATLLSTPESK-ILIDCG---FSgrQLERRLGLLEMKPT--DLDAILVSHFHGDH 63
Cdd:cd07718    1 VVFLGTGSaipskyrNVSGILLRIPGDGsILLDCGegtLG--QLRRHYGPEEADEVlrNLKCIFISHLHADH 70
metallo-hydrolase-like_MBL-fold cd07741
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 5-157 4.16e-05

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


Pssm-ID: 293827 [Multi-domain]  Cd Length: 212  Bit Score: 43.33  E-value: 4.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663531341   5 ITHLGSG------------SGGnaTLLSTPESKILIDCGfSGRQLerRLGLLEMKPTDLDAILVSHFHGDHS-------- 64
Cdd:cd07741    1 IIFLGTGggrfvvitqlraSGG--IWIELNGKNIHIDPG-PGALV--RMCRPKLDPTKLDAIILSHRHLDHSndanvlie 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663531341  65 ---------KGAVIAnkkwdiplmmnfqSCERLGLDPV----------NECKLFESLDLIAMGpDLSILPVPVNHGEADN 125
Cdd:cd07741   76 amteggfkkRGTLLA-------------PEDALNGEPVvllyyhrrklEEIEILEEGDEYELG-GIKIEATRHKHSDPTT 141

                        170       180       190
                 ....*....|....*....|....*....|..
gi 663531341 126 VGFIASHLGERAAVVTDlGSWSDELARHLEGC 157
Cdd:cd07741  142 YGFIFRTSDKKIGYISD-TRYFEELIEYYSNC 172
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 18-64 5.21e-05

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: 43.36  E-value: 5.21e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 663531341  18 LLSTPESKILIDCGFS--------------------GRQLERRLGLLEMKPTDLDAILVSHFHGDHS 64
Cdd:cd07729   36 LIEHPEGTILVDTGFHpdaaddpgglelafppgvteEQTLEEQLARLGLDPEDIDYVILSHLHFDHA 102
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 18-74 6.47e-05

BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; This subgroup of B3 subclass MBLs includes Bradyrhizobium diazoefficiens BJP-1, Fluoribacter gormanii FEZ-1, Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) GOB-1, Caulobacter crescentus Mbl1b. 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. 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: 293846 [Multi-domain]  Cd Length: 254  Bit Score: 43.08  E-value: 6.47e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663531341  18 LLSTPESKILIDCGF--SGRQLE---RRLGLlemKPTDLDAILVSHFHGDHSkGAVIANKKW 74
Cdd:cd16288   26 LITTPQGLILIDTGLesSAPMIKaniRKLGF---KPSDIKILLNSHAHLDHA-GGLAALKKL 83
CPSF3-like_MBL-fold cd16292
cleavage and polyadenylation specificity factor (CPSF) subunit 3 and related proteins; ...
 3-68 1.08e-04

cleavage and polyadenylation specificity factor (CPSF) subunit 3 and related proteins; MBL-fold metallo-hydrolase domain; CPSF3 (also known as cleavage and polyadenylation specificity factor 73 kDa subunit/CPSF-73) functions as a 3' endonuclease in 3' end processing of pre-mRNAs during cleavage/polyadenylation, and in 3' end processing of metazoan histone pre-mRNAs. This subgroup also contains the yeast homolog of CPSF-73, Ysh1/Brr5 which has roles in mRNA and snoRNA synthesis. In addition to this MBL-fold metallo-hydrolase domain, members of this subgroup contain a beta-CASP (named for metallo-beta-lactamase, CPSF, Artemis, Snm1, Pso2) domain, and a RMMBL domain (RNA-metabolizing metallo-beta-lactamase). 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: 293850  Cd Length: 194  Bit Score: 42.19  E-value: 1.08e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 663531341   3 LSITHLGSGS--GGNATLLSTPESKILIDCG----FSGrqlerrLGLL----EMKPTDLDAILVSHFHGDHSkGAV 68
Cdd:cd16292    1 LEITPLGAGQevGRSCVILEFKGKTIMLDCGihpgYSG------LASLpffdEIDLSEIDLLLITHFHLDHC-GAL 69
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 13-129 1.18e-04

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: 41.83  E-value: 1.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663531341  13 GGNATLLSTPESKILIDCG---------FSGRQLERRLGLL-----------------EMKPTDLDAILVSHFHGDHSkG 66
Cdd:cd07732   12 GGNCIEVETGGTRILLDFGlpldpeskyFDEVLDFLELGLLpdivglyrdplllgglrSEEDPSVDAVLLSHAHLDHY-G 90

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 663531341  67 AV--IANkkwDIPLMMNfQSCERL----------GLDPVNECKLFESLDLIAMGpDLSILPVPVNHGEADNVGFI 129
Cdd:cd07732   91 LLnyLRP---DIPVYMG-EATKRIlkallpffgeGDPVPRNIRVFESGKSFTIG-DFTVTPYLVDHSAPGAYAFL 160
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
18-66 1.31e-04

Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];


Pssm-ID: 440850  Cd Length: 273  Bit Score: 42.56  E-value: 1.31e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 663531341  18 LLSTPESKILIDCGfSGRQLERRLGLLEMKPTDLDAILVSHFHGDHSKG 66
Cdd:COG1237   26 LIETEGKRILFDTG-QSDVLLKNAEKLGIDLSDIDAVVLSHGHYDHTGG 73
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 18-66 1.41e-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: 1.41e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 663531341  18 LLSTPESKILIDCGFSGRQLE--RRLGLlemKPTDLDAILVSHFHGDHSKG 66
Cdd:cd07713   24 LIETEGKKILFDTGQSGVLLHnaKKLGI---DLSDIDAVVLSHGHYDHTGG 71
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 9-67 1.66e-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: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 41.78  E-value: 1.66e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 663531341   9 GSGSGGNATLLSTPESKILIDCGFS---GRQLERRLGllemKPTDL--DAILVSHFHGDHSKGA 67
Cdd:cd16282   10 GGGFISNIGFIVGDDGVVVIDTGASprlARALLAAIR----KVTDKpvRYVVNTHYHGDHTLGN 69
L1_POM-1-like_MBL-B3 cd16289
Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-1 and related ...
 7-73 2.03e-04

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: 41.73  E-value: 2.03e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 663531341   7 HLGSgSGGNATLLSTPESKILIDCGF--SGRQLERRLGLLEMKPTDLDAILVSHFHGDHSkGAVIANKK 73
Cdd:cd16289   16 YIGT-ESLTALLVKTPDGAVLLDGGMpqAADMLLDNMRALGVAPGDLKLILHSHAHADHA-GPLAALKR 82
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 14-71 2.83e-04

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: 40.58  E-value: 2.83e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663531341  14 GNATLLSTPESKILIDCGFSGRQLERRLG--LLEMKPTDLDAILVSHFHGDHSKGA--VIAN 71
Cdd:cd07731   10 GDAILIQTPGKTILIDTGPRDSFGEDVVVpyLKARGIKKLDYLILTHPDADHIGGLdaVLKN 71
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 13-63 3.48e-04

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: 40.59  E-value: 3.48e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 663531341  13 GGNATLLSTPESKILIDCGFSGRQLERRLG--LLEMKPTDLDAILVSHFHGDH 63
Cdd:cd07722   17 GTNTYLVGTGKRRILIDTGEGRPSYIPLLKsvLDSEGNATISDILLTHWHHDH 69
INTS11-like_MBL-fold cd16291
Integrator complex subunit 11, and related proteins; MBL-fold metallo-hydrolase domain; ...
 5-63 4.49e-04

Integrator complex subunit 11, and related proteins; MBL-fold metallo-hydrolase domain; Integrator is a metazoan-specific multisubunit, multifunctional protein complex composed of 14 subunits named Int1-Int14 (Integrator subunits). This subgroup includes Int11 (also known as cleavage and polyadenylation-specific factor (CPSF) 3-like protein, and protein related to CPSF subunits of 68 kDa (RC-68)). Integrator complex has been implicated in a variety of Pol II transcription events including 3' end processing of snRNA, transcription initiation, promoter-proximal pausing, termination of protein-coding transcripts, and in HVS pre-miRNA 3' end processing. 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: 293849  Cd Length: 199  Bit Score: 40.32  E-value: 4.49e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 663531341   5 ITHLGSGS--GGNATLLSTPESKILIDCGF-SGRQLERRLGLLEM-----KPTD-LDAILVSHFHGDH 63
Cdd:cd16291    1 VTPLGAGQdvGRSCILVTIGGKNIMFDCGMhMGYNDERRFPDFSYisqngPFTEhIDCVIISHFHLDH 68
metallo-hydrolase-like_MBL-fold cd07739
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 10-63 8.80e-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: 39.41  E-value: 8.80e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 663531341  10 SGSGGNATLLSTPESKILIDCGFSGRQLERrlgLLEM-----KPtdLDAILVSHFHGDH 63
Cdd:cd07739   12 SSFPVTSTLIYGETEAVLVDAQFTRADAER---LADWikasgKT--LTTIYITHGHPDH 65
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 11-66 2.28e-03

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. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. B3 MBLs include Fluoribacter gormanii FEZ-1, Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) GOB-1, Stenotrophomonas Maltophilia L1, and Bradyrhizobium diazoefficiens BJP-1, Serratia marcescens SMB-1, and Pseudomonas Aeruginosa AIM-1. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293794 [Multi-domain]  Cd Length: 248  Bit Score: 38.68  E-value: 2.28e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 663531341  11 GSGG-NATLLSTPESKILIDCGF--SGRQLERRLGLLEMKPTDLDAILVSHFHGDHSKG 66
Cdd:cd07708   18 GTDDlAAYLIVTPQGNILIDGDMeqNAPMIKANIKKLGFKFSDTKLILISHAHFDHAGG 76
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 17-63 2.38e-03

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: 37.95  E-value: 2.38e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 663531341  17 TLLSTPESKILIDCG--FSGRQLERRLGLLEMKPTDLDAILVSHFHGDH 63
Cdd:cd07711   25 TLIKDGGKNILVDTGtpWDRDLLLKALAEHGLSPEDIDYVVLTHGHPDH 73
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 16-67 2.61e-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: 293838 [Multi-domain]  Cd Length: 251  Bit Score: 38.33  E-value: 2.61e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 663531341  16 ATLLSTPESKILIDCGFS---GRQLE---RRLGLlemKPTDLDAILVSHFHGDHSKGA 67
Cdd:cd16280   24 AWAIDTGDGLILIDALNNneaADLIVdglEKLGL---DPADIKYILITHGHGDHYGGA 78
PhnP-like_MBL-fold cd07736
phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase ...
 24-142 6.28e-03

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: 36.83  E-value: 6.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663531341  24 SKILIDCGFSgrQLERRLGllemkPTDLDAILVSHFHGDHSKGavIANKKWDIPLMMNF------QSCERLGLDPVN--- 94
Cdd:cd07736   47 ERILLDAGLT--DLAERFP-----PGSIDAILLTHFHMDHVQG--LFHLRWGVGDPIPVygppdpQGCADLFKHPGIldf 117

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 663531341  95 --ECKLFESLDLiamgPDLSILPVPVNHGEAdNVGFIASHLGERAAVVTD 142
Cdd:cd07736  118 qpLVAPFQSFEL----GGLKITPLPLNHSKP-TFGYLLESGGKRLAYLTD 162
PRK11709 PRK11709
putative L-ascorbate 6-phosphate lactonase; Provisional
 34-78 6.78e-03

putative L-ascorbate 6-phosphate lactonase; Provisional


Pssm-ID: 236958  Cd Length: 355  Bit Score: 37.28  E-value: 6.78e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 663531341  34 GRQLERRLGLLEMKP--------------TDLDAILVSHFHGDH----SKGAVIANKKWDIPL 78
Cdd:PRK11709  79 GHQMARMAGVRKLQPnlrtqpfvldpfaiREIDAVLATHDHSDHidvnVAAAVLQNCADHVKF 141
CPSF2-like_MBL-fold cd16293
cleavage and polyadenylation specificity factor (CPSF) subunit 2 and related proteins; ...
 10-58 8.17e-03

cleavage and polyadenylation specificity factor (CPSF) subunit 2 and related proteins; MBL-fold metallo-hydrolase domain; CPSF2, also known as cleavage and polyadenylation specificity factor 100 kDa subunit (CPSF-100), is a component of the CPSF complex, which plays a role in 3' end processing of pre-mRNAs during cleavage/polyadenylation, and during processing of metazoan histone pre-mRNAs. This subgroup includes Ydh1p, the yeast homolog of CPSF2. In addition to this MBL-fold metallo-hydrolase domain, members of this subgroup contain a beta-CASP (named for metallo-beta-lactamase, CPSF, Artemis, Snm1, Pso2) domain. 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: 293851  Cd Length: 199  Bit Score: 36.34  E-value: 8.17e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 663531341  10 SGSGGNATLLSTPESKILIDCGFSGRQLERRLGLLEMKPTDLDAILVSH 58
Cdd:cd16293    8 GDESPLCYLLEIDDVTILLDCGWDESFDMEYLESLKRIAPTIDAVLLSH 56
 
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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