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Conserved domains on  [gi|1589195042|gb|TCU58216|]
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phosphoribosyl 1,2-cyclic phosphodiesterase [Longicatena caecimuris]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 11440937)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 1-234 5.61e-50

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


:

Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 164.30  E-value: 5.61e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195042   1 MKFALLASGSKG-----------------------NCCLIKHNDTKLVIDCGSTrkyLKACFERLQYDHLSSDAILITHT 57
Cdd:COG1235     1 MKVTFLGSGSSGgvpqigcdcpvcastdprygrtrSSILVEADGTRLLIDAGPD---LREQLLRLGLDPSKIDAILLTHE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195042  58 HTDHVSQMKMF------QSIDTYATQDIATD----------------HLHAIRPFESFDIKDFHITVLPMSHDCEGTVGY 115
Cdd:COG1235    78 HADHIAGLDDLrprygpNPIPVYATPGTLEAlerrfpylfapypgklEFHEIEPGEPFEIGGLTVTPFPVPHDAGDPVGY 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195042 116 VIECENEKMVYVTDTGYIKKEVKDYIRDADYYVFESNHDIEmlmqtsrpvyvkqriinDYGHLCNEDSANILSEVIseet 195
Cdd:COG1235   158 RIEDGGKKLAYATDTGYIPEEVLELLRGADLLILDATYDDP-----------------EPGHLSNEEALELLARLG---- 216

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1589195042 196 TKEIVLAHISQEGNTRDMALRTLQQTFDKKQIH--REHMRL 234
Cdd:COG1235   217 PKRLVLTHLSPDNNDHELDYDELEAALLPAGVEvaYDGMEI 257
 
Name Accession Description Interval E-value
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 1-234 5.61e-50

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 164.30  E-value: 5.61e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195042   1 MKFALLASGSKG-----------------------NCCLIKHNDTKLVIDCGSTrkyLKACFERLQYDHLSSDAILITHT 57
Cdd:COG1235     1 MKVTFLGSGSSGgvpqigcdcpvcastdprygrtrSSILVEADGTRLLIDAGPD---LREQLLRLGLDPSKIDAILLTHE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195042  58 HTDHVSQMKMF------QSIDTYATQDIATD----------------HLHAIRPFESFDIKDFHITVLPMSHDCEGTVGY 115
Cdd:COG1235    78 HADHIAGLDDLrprygpNPIPVYATPGTLEAlerrfpylfapypgklEFHEIEPGEPFEIGGLTVTPFPVPHDAGDPVGY 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195042 116 VIECENEKMVYVTDTGYIKKEVKDYIRDADYYVFESNHDIEmlmqtsrpvyvkqriinDYGHLCNEDSANILSEVIseet 195
Cdd:COG1235   158 RIEDGGKKLAYATDTGYIPEEVLELLRGADLLILDATYDDP-----------------EPGHLSNEEALELLARLG---- 216

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1589195042 196 TKEIVLAHISQEGNTRDMALRTLQQTFDKKQIH--REHMRL 234
Cdd:COG1235   217 PKRLVLTHLSPDNNDHELDYDELEAALLPAGVEvaYDGMEI 257
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 4-130 7.54e-21

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: 85.78  E-value: 7.54e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195042   4 ALLASGSKGNCCLIKHNDTKLVIDCGSTRKYLKACFERLQYDHLSSDAILITHTHTDHVSQMKMFQ---SIDTYATQD-- 78
Cdd:cd07733     1 SVLASGSKGNCTYLETEDGKLLIDAGLSGRKITGRLAEIGRDPEDIDAILVTHEHADHIKGLGVLArkyNVPIYATAGtl 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1589195042  79 ---------IATDHLHAIRPFESFDIKDFHITVLPMSHDCEGTVGYVIECENEKMVYVTDT 130
Cdd:cd07733    81 ramerkvglIDVDQKQIFEPGETFSIGDFDVESFGVSHDAADPVGYRFEEGGRRFGMLTDL 141
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 50-152 1.70e-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: 61.56  E-value: 1.70e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195042  50 DAILITHTHTDHVSQMKM---FQSIDTYATQDIATD----------------HLHAIRPFESFDIKDF--HITVLPMSHD 108
Cdd:pfam12706  30 DAVLLTHDHYDHLAGLLDlreGRPRPLYAPLGVLAHlrrnfpylfllehygvRVHEIDWGESFTVGDGglTVTATPARHG 109

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1589195042 109 C--------EGTVGYVIECENEKMVYVTDTGYIKKEVKDYIRDADYYVFESN 152
Cdd:pfam12706 110 SprgldpnpGDTLGFRIEGPGKRVYYAGDTGYFPDEIGERLGGADLLLLDGG 161
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 13-167 2.02e-11

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: 61.03  E-value: 2.02e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195042   13 NCCLIKHNDTKLVIDCGSTRKY-LKACFERLQYDHLssDAILITHTHTDHVSQMKMFQS---IDTYATQ----------- 77
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAEdLLAELKKLGPKKI--DAIILTHGHPDHIGGLPELLEapgAPVYAPEgtaellkdlla 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195042   78 --------DIATDHLHAIRPFESFDIKDFHITVLPMSHDCEGTVGYVIecENEKMVYVTDTGYIKKEVKDYIRDADYYVF 149
Cdd:smart00849  79 llgelgaeAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYL--PEGKILFTGDLLFAGGDGRTLVDGGDAAAS 156

                          170
                   ....*....|....*...
gi 1589195042  150 ESNHDIEMLMQTSRPVYV 167
Cdd:smart00849 157 DALESLLKLLKLLPKLVV 174
PRK02113 PRK02113
MBL fold metallo-hydrolase;
16-136 2.42e-06

MBL fold metallo-hydrolase;


Pssm-ID: 179371 [Multi-domain]  Cd Length: 252  Bit Score: 47.47  E-value: 2.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195042  16 LIKHNDTKLVIDCGSTrkyLKACFERLQYDHLssDAILITHTHTDHVSQMK------MFQSIDTYATQDIA--------- 80
Cdd:PRK02113   39 LVETEGARILIDCGPD---FREQMLRLPFGKI--DAVLITHEHYDHVGGLDdlrpfcRFGEVPIYAEQYVAerlrsrmpy 113

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1589195042  81 --TDH---------LHAIRPFESFDIKDFHITVLPMSHDCEGTVGYVIecenEKMVYVTDTGYIKKE 136
Cdd:PRK02113  114 cfVEHsypgvpnipLREIEPDRPFLVNHTEVTPLRVMHGKLPILGYRI----GKMAYITDMLTMPEE 176
 
Name Accession Description Interval E-value
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 1-234 5.61e-50

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 164.30  E-value: 5.61e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195042   1 MKFALLASGSKG-----------------------NCCLIKHNDTKLVIDCGSTrkyLKACFERLQYDHLSSDAILITHT 57
Cdd:COG1235     1 MKVTFLGSGSSGgvpqigcdcpvcastdprygrtrSSILVEADGTRLLIDAGPD---LREQLLRLGLDPSKIDAILLTHE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195042  58 HTDHVSQMKMF------QSIDTYATQDIATD----------------HLHAIRPFESFDIKDFHITVLPMSHDCEGTVGY 115
Cdd:COG1235    78 HADHIAGLDDLrprygpNPIPVYATPGTLEAlerrfpylfapypgklEFHEIEPGEPFEIGGLTVTPFPVPHDAGDPVGY 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195042 116 VIECENEKMVYVTDTGYIKKEVKDYIRDADYYVFESNHDIEmlmqtsrpvyvkqriinDYGHLCNEDSANILSEVIseet 195
Cdd:COG1235   158 RIEDGGKKLAYATDTGYIPEEVLELLRGADLLILDATYDDP-----------------EPGHLSNEEALELLARLG---- 216

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1589195042 196 TKEIVLAHISQEGNTRDMALRTLQQTFDKKQIH--REHMRL 234
Cdd:COG1235   217 PKRLVLTHLSPDNNDHELDYDELEAALLPAGVEvaYDGMEI 257
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
14-223 6.02e-24

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 96.42  E-value: 6.02e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195042  14 CCLIKHNDTKLVIDCGStrkylkACFERLQYDHLSS---DAILITHTHTDHVS------QMKMFQSIDT----YA---TQ 77
Cdd:COG1234    21 SYLLEAGGERLLIDCGE------GTQRQLLRAGLDPrdiDAIFITHLHGDHIAglpgllSTRSLAGREKpltiYGppgTK 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195042  78 DIATDHL-------------HAIRPFESFDIKDFHITVLPMSHDCEgTVGYVIECENEKMVYVTDTGYIkKEVKDYIRDA 144
Cdd:COG1234    95 EFLEALLkasgtdldfplefHEIEPGEVFEIGGFTVTAFPLDHPVP-AYGYRFEEPGRSLVYSGDTRPC-EALVELAKGA 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195042 145 DYYVFESNHDIEMlmqtsrpvyvkQRIINDYGHLCNEDSANILSE--ViseettKEIVLAHISQEGNTRDMALRTLQQTF 222
Cdd:COG1234   173 DLLIHEATFLDEE-----------AELAKETGHSTAKEAAELAAEagV------KRLVLTHFSPRYDDPEELLAEARAVF 235


                  .
gi 1589195042 223 D 223
Cdd:COG1234   236 P 236
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 4-130 7.54e-21

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: 85.78  E-value: 7.54e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195042   4 ALLASGSKGNCCLIKHNDTKLVIDCGSTRKYLKACFERLQYDHLSSDAILITHTHTDHVSQMKMFQ---SIDTYATQD-- 78
Cdd:cd07733     1 SVLASGSKGNCTYLETEDGKLLIDAGLSGRKITGRLAEIGRDPEDIDAILVTHEHADHIKGLGVLArkyNVPIYATAGtl 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1589195042  79 ---------IATDHLHAIRPFESFDIKDFHITVLPMSHDCEGTVGYVIECENEKMVYVTDT 130
Cdd:cd07733    81 ramerkvglIDVDQKQIFEPGETFSIGDFDVESFGVSHDAADPVGYRFEEGGRRFGMLTDL 141
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 16-148 1.44e-17

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: 77.90  E-value: 1.44e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195042  16 LIKHNDTKLVIDCGSTrkyLKACFERLQYDHLssDAILITHTHTDHVS--------QMKMFQSIDTYATQDIATD----- 82
Cdd:cd16279    39 LIETGGKNILIDTGPD---FRQQALRAGIRKL--DAVLLTHAHADHIHglddlrpfNRLQQRPIPVYASEETLDDlkrrf 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195042  83 ---------------HLHAIRPFESFDIKDFHITVLPMSHDCEGTVGYVIecenEKMVYVTDTGYIKKEVKDYIRDADYY 147
Cdd:cd16279   114 pyffaatggggvpklDLHIIEPDEPFTIGGLEITPLPVLHGKLPSLGFRF----GDFAYLTDVSEIPEESLEKLRGLDVL 189


                  .
gi 1589195042 148 V 148
Cdd:cd16279   190 I 190
PhnP-like_MBL-fold cd07736
phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase ...
 14-143 2.42e-16

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: 74.58  E-value: 2.42e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195042  14 CCLIKHNDTKLVIDCGSTRkylkaCFERlqYDHLSSDAILITHTHTDHVSQM-----KMFQSIDTYATQDIAT------- 81
Cdd:cd07736    39 SALIEVDGERILLDAGLTD-----LAER--FPPGSIDAILLTHFHMDHVQGLfhlrwGVGDPIPVYGPPDPQGcadlfkh 111

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1589195042  82 ----DHLHAIRPFESFDIKDFHITVLPMSHDCEgTVGYVIECENEKMVYVTDTGYIKKEVKDYIRD 143
Cdd:cd07736   112 pgilDFQPLVAPFQSFELGGLKITPLPLNHSKP-TFGYLLESGGKRLAYLTDTLGLPEETLEFLKQ 176
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 13-206 1.16e-15

Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as tRNase Z or 3' tRNase) catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors. Escherichia coli zinc phosphodiesterase (ZiPD, also known as ecoZ, tRNase Z, or RNase BN) is a 3' tRNA-processing endonuclease, encoded by the elaC gene. Two forms of RNase Z exist in eukaryotes, one long (ELAC2) and one short form (ELAC1), the former may have resulted from a duplication of the shorter enzyme; this subgroup includes the short form (ELAC1). Only the short form exists in bacteria. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293803 [Multi-domain]  Cd Length: 247  Bit Score: 74.02  E-value: 1.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195042  13 NCCLIKHNDTKLVIDCGstrkylkacfE----RLQYDHLSS---DAILITHTHTDHV----------------------- 62
Cdd:cd07717    18 SSIALRLEGELWLFDCG----------EgtqrQLLRAGLSPskiDRIFITHLHGDHIlglpgllstmsllgrtepltiyg 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195042  63 ---------SQMKMFQSIDTYatqDIatdHLHAIRPF--ESFDIKDFHITVLPMSHDCEgTVGYVIEcENEKMVYVTDTG 131
Cdd:cd07717    88 pkglkefleTLLRLSASRLPY---PI---EVHELEPDpgLVFEDDGFTVTAFPLDHRVP-CFGYRFE-EGRKIAYLGDTR 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1589195042 132 YIkKEVKDYIRDADYYVFESNHDIEMLMQtsrpvyvkqriINDYGHLCNEDSANI--LSEViseettKEIVLAHISQ 206
Cdd:cd07717   160 PC-EGLVELAKGADLLIHEATFLDDDAEK-----------AKETGHSTAKQAAEIakKAGV------KKLVLTHFSA 218
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 8-145 1.39e-14

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: 69.39  E-value: 1.39e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195042   8 SGS---KGNCC---LIKHNDTKLVIDCGStrkylkACFERLQ--YDHLSSDAILITHTHTDHVS-------------QMK 66
Cdd:cd07716     8 SGSypgPGGACsgyLLEADGFRILLDCGS------GVLSRLQryIDPEDLDAVVLSHLHPDHCAdlgvlqyarryhpRGA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195042  67 MFQSIDTYATQDIATDH-----------LHAIRPFESFDIKDFHITVLPMSHDCEgTVGYVIECENEKMVYVTDTGYiKK 135
Cdd:cd07716    82 RKPPLPLYGPAGPAERLaalygledvfdFHPIEPGEPLEIGPFTITFFRTVHPVP-CYAMRIEDGGKVLVYTGDTGY-CD 159

                         170
                  ....*....|
gi 1589195042 136 EVKDYIRDAD 145
Cdd:cd07716   160 ELVEFARGAD 169
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 14-151 8.75e-13

Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as tRNase Z or 3' tRNase) catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors. Two forms of RNase Z exist in eukaryotes, one long (ELAC2) and one short form (ELAC1), the former may have resulted from a duplication of the shorter enzyme. Only the short form exists in bacteria. It includes the C-terminus of human ELAC2 and Escherichia coli zinc phosphodiesterase (ZiPD, also known as ecoZ, tRNase Z, or RNase BN) is a 3' tRNA-processing endonuclease, encoded by the elaC gene. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293830 [Multi-domain]  Cd Length: 180  Bit Score: 64.59  E-value: 8.75e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195042  14 CCLIKHNDTKLVIDCGStrkylkACFERLQ---YDHLSSDAILITHTHTDHVSQMKMFQSIDTYATQD------------ 78
Cdd:cd16272    19 SYLLETGGTRILLDCGE------GTVYRLLkagVDPDKLDAIFLSHFHLDHIGGLPTLLFARRYGGRKkpltiygpkgik 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195042  79 -----------------IATDHLHAIRPFESFDIKDFHITVLPMSHdCEGTVGYVIECENEKMVYVTDTGYIkKEVKDYI 141
Cdd:cd16272    93 eflekllnfpveilplgFPLEIEELEEGGEVLELGDLKVEAFPVKH-SVESLGYRIEAEGKSIVYSGDTGPC-ENLVELA 170

                         170
                  ....*....|
gi 1589195042 142 RDADYYVFES 151
Cdd:cd16272   171 KGADLLIHEC 180
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 13-133 1.65e-12

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 64.94  E-value: 1.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195042  13 NCCLIKHNDTKLVIDCGSTRKYLKACFERLQYDHLSS-DAILITHTHTDHVSqMKMFQSIDT-----YATQDIAT----- 81
Cdd:COG2220    12 ATFLIETGGKRILIDPVFSGRASPVNPLPLDPEDLPKiDAVLVTHDHYDHLD-DATLRALKRtgatvVAPLGVAAwlraw 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1589195042  82 --DHLHAIRPFESFDIKDFHITVLPMSH-------DCEGTVGYVIECENEKmVYVT-DTGYI 133
Cdd:COG2220    91 gfPRVTELDWGESVELGGLTVTAVPARHssgrpdrNGGLWVGFVIETDGKT-IYHAgDTGYF 151
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 12-131 2.59e-12

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: 63.79  E-value: 2.59e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195042  12 GNCCLIKHNDTKLVIDCGST-RKYLKACFERLQY-------------------------DHLSSDAILITHTHTDHVSQM 65
Cdd:cd07732    13 GNCIEVETGGTRILLDFGLPlDPESKYFDEVLDFlelgllpdivglyrdplllgglrseEDPSVDAVLLSHAHLDHYGLL 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195042  66 K-MFQSIDTYATQ-------------DIATDHLHAIRPFE---SFDIKDFHITVLPMSHDCEGTVGYVIECENEKMVYvt 128
Cdd:cd07732    93 NyLRPDIPVYMGEatkrilkallpffGEGDPVPRNIRVFEsgkSFTIGDFTVTPYLVDHSAPGAYAFLIEAPGKRIFY-- 170


                  ...
gi 1589195042 129 dTG 131
Cdd:cd07732   171 -TG 172
TaR3-like_MBL-fold cd07715
MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold ...
 12-146 6.35e-12

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: 62.90  E-value: 6.35e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195042  12 GN--CCLIKHNDTKLVIDCGSTrkyLKACFERLQYDHLSSDA-ILITHTHTDHVSQMKMFQ-------SIDTYAT----- 76
Cdd:cd07715    21 GNtsCVEVRAGGELLILDAGTG---IRELGNELMKEGPPGEAhLLLSHTHWDHIQGFPFFApaydpgnRIHIYGPhkdgg 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195042  77 --------------------QDIATDHLHAIRPFESFDIKDFHITVLPMSHDCeGTVGYVIECENEKMVYVTDTGYIK-- 134
Cdd:cd07715    98 sleevlrrqmsppyfpvpleELLAAIEFHDLEPGEPFSIGGVTVTTIPLNHPG-GALGYRIEEDGKSVVYATDTEHYPdd 176

                         170
                  ....*....|....*.
gi 1589195042 135 ----KEVKDYIRDADY 146
Cdd:cd07715   177 gesdEALLEFARGADL 192
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 50-152 1.70e-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: 61.56  E-value: 1.70e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195042  50 DAILITHTHTDHVSQMKM---FQSIDTYATQDIATD----------------HLHAIRPFESFDIKDF--HITVLPMSHD 108
Cdd:pfam12706  30 DAVLLTHDHYDHLAGLLDlreGRPRPLYAPLGVLAHlrrnfpylfllehygvRVHEIDWGESFTVGDGglTVTATPARHG 109

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1589195042 109 C--------EGTVGYVIECENEKMVYVTDTGYIKKEVKDYIRDADYYVFESN 152
Cdd:pfam12706 110 SprgldpnpGDTLGFRIEGPGKRVYYAGDTGYFPDEIGERLGGADLLLLDGG 161
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 13-167 2.02e-11

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: 61.03  E-value: 2.02e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195042   13 NCCLIKHNDTKLVIDCGSTRKY-LKACFERLQYDHLssDAILITHTHTDHVSQMKMFQS---IDTYATQ----------- 77
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAEdLLAELKKLGPKKI--DAIILTHGHPDHIGGLPELLEapgAPVYAPEgtaellkdlla 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195042   78 --------DIATDHLHAIRPFESFDIKDFHITVLPMSHDCEGTVGYVIecENEKMVYVTDTGYIKKEVKDYIRDADYYVF 149
Cdd:smart00849  79 llgelgaeAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYL--PEGKILFTGDLLFAGGDGRTLVDGGDAAAS 156

                          170
                   ....*....|....*...
gi 1589195042  150 ESNHDIEMLMQTSRPVYV 167
Cdd:smart00849 157 DALESLLKLLKLLPKLVV 174
PDE1 COG5212
cAMP phosphodiesterase [Signal transduction mechanisms];
8-131 1.30e-10

cAMP phosphodiesterase [Signal transduction mechanisms];


Pssm-ID: 444071 [Multi-domain]  Cd Length: 300  Bit Score: 60.36  E-value: 1.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195042   8 SGSKGNCCLIKHNDTK--LVIDCGS-----TRKYLKACFERLQYDHLSS-DAILITHTHTDHVSQMKMFQSIDT----YA 75
Cdd:COG5212    24 SDGNLTTYLLRPLGSDdyVLLDAGTvvsglELAEQKGAFKGRQGYVLEHiKGYLISHAHLDHIAGLPILSPDDSpktiYA 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195042  76 TQDIA----------------TD----------HLHAIRPFESFDIKD--FHITVLPMSHDCEgTVGYVIECENEKMVYV 127
Cdd:COG5212   104 LPETIdalrnhyfnwviwpdfTDigsaphlpkyRYVPLKPGQTFPLGGtgLRVTAFPLSHSVP-SSAFLIESGGGAFLYS 182


                  ....
gi 1589195042 128 TDTG 131
Cdd:COG5212   183 GDTG 186
metallo-hydrolase-like_MBL-fold cd07741
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 16-190 5.40e-10

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


Pssm-ID: 293827 [Multi-domain]  Cd Length: 212  Bit Score: 57.58  E-value: 5.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195042  16 LIKHNDTKLVIDCGStrkylkACFERLQ---YDHLSSDAILITHTHTDHVSQM-----KMFQS----------------- 70
Cdd:cd07741    24 WIELNGKNIHIDPGP------GALVRMCrpkLDPTKLDAIILSHRHLDHSNDAnvlieAMTEGgfkkrgtllapedalng 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195042  71 ---IDTYATQDIATDhLHAIRPFESFDIKDFHITVLPMSHDCEGTVGYVIECENEKMVYVTDTGYIkKEVKDYIRDADYy 147
Cdd:cd07741    98 epvVLLYYHRRKLEE-IEILEEGDEYELGGIKIEATRHKHSDPTTYGFIFRTSDKKIGYISDTRYF-EELIEYYSNCDV- 174

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1589195042 148 vfesnhdieMLMQTSRPvyvkqRIINDYGHLCNEDSANILSEV 190
Cdd:cd07741   175 ---------LIINVTRP-----RPRKGVDHLSVEDVEKILKEI 203
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 16-148 1.41e-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: 53.29  E-value: 1.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195042  16 LIKHNDTKLVIDCGS--TRKYLKAcfeRLQYDHLssDAILITHTHTDHVSQM-------------------------KMF 68
Cdd:cd07719    22 LVVVGGRVYLVDAGSgvVRRLAQA---GLPLGDL--DAVFLTHLHSDHVADLpallltawlagrktplpvygppgtrALV 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195042  69 QSIDTYATQDIA--TDHLHAIRPFESFDIK--------------DFHITVLPMSH-DCEGTVGYVIECENEKMVYVTDTG 131
Cdd:cd07719    97 DGLLAAYALDIDyrARIGDEGRPDPGALVEvheiaaggvvyeddGVKVTAFLVDHgPVPPALAYRFDTPGRSVVFSGDTG 176

                         170
                  ....*....|....*..
gi 1589195042 132 YiKKEVKDYIRDADYYV 148
Cdd:cd07719   177 P-SENLIELAKGADLLV 192
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 12-151 2.92e-08

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 53.65  E-value: 2.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195042  12 GNCCLIKHNDTKLVIDCGSTRKYLKACFERLQYDHLSSDAILITHTHTDHV----------------------------- 62
Cdd:COG1236    14 GSCYLLETGGTRILIDCGLFQGGKERNWPPFPFRPSDVDAVVLTHAHLDHSgalpllvkegfrgpiyatpatadlarill 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195042  63 -----SQMKMFQSIDTYATQDI--ATDHLHAIRPFESFDIKDFHIT------VLpmshdceGTVGYVIECENEKMVYvtd 129
Cdd:COG1236    94 gdsakIQEEEAEAEPLYTEEDAerALELFQTVDYGEPFEIGGVRVTfhpaghIL-------GSAQVELEVGGKRIVF--- 163

                         170       180
                  ....*....|....*....|....*...
gi 1589195042 130 TGYIKKEVK------DYIRDADYYVFES 151
Cdd:COG1236   164 SGDYGREDDpllappEPVPPADVLITES 191
class_II_PDE_MBL-fold cd07735
class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium ...
 7-143 2.21e-07

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: 50.29  E-value: 2.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195042   7 ASG--SKGNCC--LIKHNDTK--LVIDCGS-------TRKYLKACFERLQYDHLSSDAI---LITHTHTDHVSQM----- 65
Cdd:cd07735     8 CSGgpDEGNTSsfLLDPAGSDgdILLDAGTgvgalslEEMFNDILFPSQKAAYELYQRIrhyLITHAHLDHIAGLpllsp 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195042  66 ----KMFQSIDTYATQ---DIATDH----------------------LHAIRPFESFDIKDFHITVLPMSHDCEGTVGYV 116
Cdd:cd07735    88 ndggQRGSPKTIYGLPetiDALKKHifnwviwpdftsipsgkypylrLEPIEPEYPIALTGLSVTAFPVSHGVPVSTAFL 167

                         170       180
                  ....*....|....*....|....*..
gi 1589195042 117 IECENEKMVYVTDTGYIKKEVKDYIRD 143
Cdd:cd07735   168 IRDGGDSFLFFGDTGPDSVSKSPRLDA 194
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
12-149 6.52e-07

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 48.52  E-value: 6.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195042  12 GNCCLIKHNDTKLVIDCGSTRKYLKACFERLQYDHLSS-DAILITHTHTDHVS--------------------------- 63
Cdd:pfam00753   6 VNSYLIEGGGGAVLIDTGGSAEAALLLLLAALGLGPKDiDAVILTHGHFDHIGglgelaeatdvpvivvaeearelldee 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195042  64 --QMKMFQSIDTYATQDIATDHLHAIRPFESFDIKDFHITVLPMShdceGTVGYVIECENEKMVYVTDTGYIKKEVKDYI 141
Cdd:pfam00753  86 lgLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGH----GPGHVVVYYGGGKVLFTGDLLFAGEIGRLDL 161


                  ....*...
gi 1589195042 142 RDADYYVF 149
Cdd:pfam00753 162 PLGGLLVL 169
PRK02113 PRK02113
MBL fold metallo-hydrolase;
16-136 2.42e-06

MBL fold metallo-hydrolase;


Pssm-ID: 179371 [Multi-domain]  Cd Length: 252  Bit Score: 47.47  E-value: 2.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195042  16 LIKHNDTKLVIDCGSTrkyLKACFERLQYDHLssDAILITHTHTDHVSQMK------MFQSIDTYATQDIA--------- 80
Cdd:PRK02113   39 LVETEGARILIDCGPD---FREQMLRLPFGKI--DAVLITHEHYDHVGGLDdlrpfcRFGEVPIYAEQYVAerlrsrmpy 113

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1589195042  81 --TDH---------LHAIRPFESFDIKDFHITVLPMSHDCEGTVGYVIecenEKMVYVTDTGYIKKE 136
Cdd:PRK02113  114 cfVEHsypgvpnipLREIEPDRPFLVNHTEVTPLRVMHGKLPILGYRI----GKMAYITDMLTMPEE 176
Int9-11_CPSF2-3-like_MBL-fold cd07734
Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; ...
 14-162 5.33e-06

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: 45.78  E-value: 5.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195042  14 CCLIKHNDTKLVIDCGS--TRKYLKACFERLQYDHLSSDAILITHTHTDHV------SQMKMFqSIDTYAT--------- 76
Cdd:cd07734    13 CFLVEFKGRTVLLDCGMnpGKEDPEACLPQFELLPPEIDAILISHFHLDHCgalpylFRGFIF-RGPIYAThptvalgrl 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195042  77 ---------------------QDI--ATDHLHAIRPFESFDI-KDFHITVLPMSHdCEGTVGYVIECENEKMVYvtdTGY 132
Cdd:cd07734    92 lledyvksaerigqdqslytpEDIeeALKHIVPLGYGQSIDLfPALSLTAYNAGH-VLGAAMWEIQIYGEKLVY---TGD 167

                         170       180       190
                  ....*....|....*....|....*....|
gi 1589195042 133 IKKEVKDYIRDADYyvfeSNHDIEMLMQTS 162
Cdd:cd07734   168 FSNTEDRLLPAASI----LPPRPDLLITES 193
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 12-62 1.18e-05

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: 44.76  E-value: 1.18e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1589195042  12 GNCCLIKHNDTKLVIDCG---STRKYLKACFERLQYDHLSSDAILITHTHTDHV 62
Cdd:cd16295    12 GSCYLLETGGKRILLDCGlfqGGKELEELNNEPFPFDPKEIDAVILTHAHLDHS 65
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 13-129 1.53e-05

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: 44.70  E-value: 1.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195042  13 NCCLIKHNDTKLVIDCG----------------STRkYLKACFERLQydhlssdAILITHTHTDHVSQM-KMFQSIDT-- 73
Cdd:cd07714    12 NMYVVEYDDDIIIIDCGlkfpdedmpgvdyiipDFS-YLEENKDKIK-------GIFITHGHEDHIGALpYLLPELNVpi 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195042  74 YATQ--------------DIATDHLHAIRPFESFDIKDFHITVLPMSHDCEGTVGYVIECENEKMVYVTD 129
Cdd:cd07714    84 YATPltlalikkkleefkLIKKVKLNEIKPGERIKLGDFEVEFFRVTHSIPDSVGLAIKTPEGTIVHTGD 153
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 13-62 1.67e-05

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


Pssm-ID: 293807 [Multi-domain]  Cd Length: 202  Bit Score: 44.52  E-value: 1.67e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1589195042  13 NCCLIKHNDTKLVIDCG--STRKYLKACFERLQYDHLSSDAILITHTHTDHV 62
Cdd:cd07721    12 NAYLIEDDDGLTLIDTGlpGSAKRILKALRELGLSPKDIRRILLTHGHIDHI 63
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 13-130 3.65e-05

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: 43.06  E-value: 3.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195042  13 NCCLIKHNDTKLVIDCGS----TRKYLKACFERLQYDHLSSDAILITHTHTDHVSQMKMFQSIDtyaTQDIATDHLHAIR 88
Cdd:cd07725    16 NVYLLRDGDETTLIDTGLateeDAEALWEGLKELGLKPSDIDRVLLTHHHPDHIGLAGKLQEKS---GATVYILDVTPVK 92

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1589195042  89 PFESFDIKDFHITVLPMSHDCEGTVGYVieCENEKMVYVTDT 130
Cdd:cd07725    93 DGDKIDLGGLRLKVIETPGHTPGHIVLY--DEDRRELFVGDA 132
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 8-152 4.89e-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: 293826 [Multi-domain]  Cd Length: 194  Bit Score: 43.02  E-value: 4.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195042   8 SGSKGNCCL-IKHNDTKLVIDCGSTRkyLKAcFERLQYDHLSSDAILITHTHTDHVSQMKMF------------------ 68
Cdd:cd07740    11 SGGRLNTCFhVASEAGRFLIDCGASS--LIA-LKRAGIDPNAIDAIFITHLHGDHFGGLPFFlldaqfvakrtrpltiag 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195042  69 -QSIDTYATQDIATDHLHA-------------IRPFESFDIKDFHITVLPMSHDCeGTVGY--VIECENEKMVYVTDTGY 132
Cdd:cd07740    88 pPGLRERLRRAMEALFPGSskvprrfdlevieLEPGEPTTLGGVTVTAFPVVHPS-GALPLalRLEAAGRVLAYSGDTEW 166

                         170       180
                  ....*....|....*....|
gi 1589195042 133 IkKEVKDYIRDADYYVFESN 152
Cdd:cd07740   167 T-DALVPLARGADLFICECY 185
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 12-121 5.10e-05

uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized human MBLAC1 and related proteins. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293797 [Multi-domain]  Cd Length: 190  Bit Score: 42.96  E-value: 5.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195042  12 GNCCLIKHNDTKLVIDCG---STRKYLKAcferLQYDHLSS---DAILITHTHTDHVSQMKMFQSIDTYATQDIATDH-- 83
Cdd:cd07711    22 STVTLIKDGGKNILVDTGtpwDRDLLLKA----LAEHGLSPediDYVVLTHGHPDHIGNLNLFPNATVIVGWDICGDSyd 97

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1589195042  84 LHAIRPFESFDIKDfHITVLP-----MSH-------DCEGTV---GYVIECEN 121
Cdd:cd07711    98 DHSLEEGDGYEIDE-NVEVIPtpghtPEDvsvlvetEKKGTVavaGDLFEREE 149
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 16-103 7.01e-05

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: 42.06  E-value: 7.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195042  16 LIKHNDTK--LVIDCGSTRKYLKAcferLQYDHLSSDAILITHTHTDHVSQ----MKMFQSIDTYATQDIATDHL-HAIR 88
Cdd:cd07723    13 LIVDEATGeaAVVDPGEAEPVLAA----LEKNGLTLTAILTTHHHWDHTGGnaelKALFPDAPVYGPAEDRIPGLdHPVK 88

                          90
                  ....*....|....*
gi 1589195042  89 PFESFDIKDFHITVL 103
Cdd:cd07723    89 DGDEIKLGGLEVKVL 103
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 13-103 8.60e-05

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


Pssm-ID: 440257 [Multi-domain]  Cd Length: 215  Bit Score: 42.37  E-value: 8.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195042  13 NCCLIKHNDTKLVIDCGSTRKYLKACFERLQYDHLSSDAILITHTHTDHVSQMKMFQS---IDTYATQDIAtDHLHAIRP 89
Cdd:COG0491    16 NSYLIVGGDGAVLIDTGLGPADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEafgAPVYAHAAEA-EALEAPAA 94

                          90
                  ....*....|....
gi 1589195042  90 FESFDIKDFHITVL 103
Cdd:COG0491    95 GALFGREPVPPDRT 108
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 12-62 1.16e-04

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: 42.15  E-value: 1.16e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1589195042  12 GNCCLIKHNDTK-LVIDCGST------RKYLKACFERLQYDHLssDAILITHTHTDHV 62
Cdd:COG2333    11 GDAILIRTPDGKtILIDTGPRpsfdagERVVLPYLRALGIRRL--DLLVLTHPDADHI 66
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 13-130 1.91e-04

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


Pssm-ID: 293792 [Multi-domain]  Cd Length: 188  Bit Score: 41.12  E-value: 1.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195042  13 NCCLIKHNDTK-LVIDCG-STRKYLKACFERLQYDHlssDAILITHTHTDHVSQMKMFQS---IDTYATQDIA------- 80
Cdd:cd06262    11 NCYLVSDEEGEaILIDPGaGALEKILEAIEELGLKI---KAILLTHGHFDHIGGLAELKEapgAPVYIHEADAelledpe 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1589195042  81 ----------TDHLHAIRPFE---SFDIKDFHITVLPMSHDCEGTVGYVIecENEKMVYVTDT 130
Cdd:cd06262    88 lnlaffgggpLPPPEPDILLEdgdTIELGGLELEVIHTPGHTPGSVCFYI--EEEGVLFTGDT 148
CPSF2-like_MBL-fold cd16293
cleavage and polyadenylation specificity factor (CPSF) subunit 2 and related proteins; ...
 7-97 8.10e-04

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: 39.43  E-value: 8.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195042   7 ASGSKGNCCLIKHNDTKLVIDCGSTRKYLKACFERLQYdHLSS-DAILITHTHTDHVS-----QMKMFQSIDTYATQDIA 80
Cdd:cd16293     7 AGDESPLCYLLEIDDVTILLDCGWDESFDMEYLESLKR-IAPTiDAVLLSHPDLEHLGalpylVGKLGLTCPVYATLPVH 85

                          90       100
                  ....*....|....*....|....*..
gi 1589195042  81 -------TDHL---HAIRPFESFDIKD 97
Cdd:cd16293    86 kmgrmfmYDLYqsrGLEEDFNLFTLDD 112
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 13-62 1.92e-03

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


Pssm-ID: 293829 [Multi-domain]  Cd Length: 197  Bit Score: 38.28  E-value: 1.92e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1589195042  13 NCCLIKHNDTK-LVIDCGSTRKYLKACFERLQYDHLSSDAILITHTHTDHV 62
Cdd:cd07743     9 NIGVYVFGDKEaLLIDSGLDEDAGRKIRKILEELGWKLKAIINTHSHADHI 59
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 13-62 4.70e-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: 37.13  E-value: 4.70e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1589195042  13 NCCLIKHNDTKLVIDCGSTRKYLKACFERLQYDHLSS--DAILITHTHTDHV 62
Cdd:cd07722    19 NTYLVGTGKRRILIDTGEGRPSYIPLLKSVLDSEGNAtiSDILLTHWHHDHV 70
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 13-62 7.99e-03

uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized Thermus thermophilus TTHA1623 and related proteins. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. This family includes homologs present in a wide range of bacteria and archaea and some eukaryota. Members of the MBL-fold metallo-hydrolase superfamily exhibit a variety of active site metallo-chemistry, TTHA1623 exhibiting a uniquely shaped putative substrate-binding pocket with a glyoxalase II-type metal-coordination mode.


Pssm-ID: 293877 [Multi-domain]  Cd Length: 204  Bit Score: 36.56  E-value: 7.99e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1589195042  13 NCCLIKHNDTK--LVIDCGS-TRKYLKACFERlqydHLSSDAILITHTHTDHV 62
Cdd:cd16322    12 NTYLVADEGGGeaVLVDPGDeSEKLLARFGTT----GLTLLYILLTHAHFDHV 60
 
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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