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Conserved domains on  [gi|499906034|ref|WP_011586768|]
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MBL fold metallo-hydrolase RNA specificity domain-containing protein [Cytophaga hutchinsonii]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG1782 COG1782
Predicted metal-dependent RNase, contains metallo-beta-lactamase and KH domains [General ...
 1-451 1.20e-177

Predicted metal-dependent RNase, contains metallo-beta-lactamase and KH domains [General function prediction only];


:

Pssm-ID: 441388 [Multi-domain]  Cd Length: 460  Bit Score: 504.66  E-value: 1.20e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034   1 MKLTFWGAARKVTGSMYLLESLGYKILIDCGSDFSDRHKVLTG-GLFPFEASEIDLVILTHAHVDHSGNIPALIRAGYRG 79
Cdd:COG1782    1 MRITFLGAAREVTGSCHLLETGESRILLDCGLFQGGREERERNnDAFPFDPEELDAVVLTHAHLDHSGLLPLLVKYGYRG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034  80 QILSTAPTAELSELLFADSAYIQRAEKKIANSAPSD--------YSYKPV----DRFIPIAFNKDFELNERITVRLTPVG 147
Cdd:COG1782   81 PIYCTPPTRDLMALLLLDSAKIQEEEAEYANKKRYSghppveplYTEKDVekalKHFITLDYGEVTDIAPDIKLTFYNAG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034 148 HILGAASVFVKVEEegKTKTILFSGDVGRDNYPLLPDPEQSPQADYVLCETTYGNRVHKETEPAEEIVKRIVTEAcVDKP 227
Cdd:COG1782  161 HILGSAIVHLHIGD--GLHNIVFSGDLGRGKTPLLRPPTPFPRADTLIMESTYGGRLHPSREEAEEELAKVINET-IERG 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034 228 GRLIIPAFSLGRTQSLLYTLNKLALKNELPPIKVFTDSALAAEGTNIYSKYSSLMNGEALAIKAQDESLFDFENLDHVKT 307
Cdd:COG1782  238 GKVLIPAFAVGRTQEILYVLNELMREGKIPEVPVYLDSPMAIEATAIHTAYPEYLDEELRDLIFKGENPFLFENLHYVES 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034 308 FKESKNISNYLKPCIILSSSGMITGGRIQHHIRQNIQNPYCTILLVGYAVEGTIGHDLLAGKQTIRFKKRSIPVAAKIIY 387
Cdd:COG1782  318 VEESKEINDSDEPAIIIATSGMLTGGRILHHLKHLAPDPKNTILFVGYQAEGTLGRRLLDGAKEVKIFGETIPVRAEVET 397

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499906034 388 TDIFSGHTDVNGLIKYLGHQDKaKLKKIFLVHGEHQSMLDFEKRLHEEGYNNIEIPDYGQSYDL 451
Cdd:COG1782  398 IDGFSGHADRNELLNWLRRLKP-KPKKVFLVHGEPEAAEALASSIRKKLGIEVVIPENLETIRL 460
 
Name Accession Description Interval E-value
COG1782 COG1782
Predicted metal-dependent RNase, contains metallo-beta-lactamase and KH domains [General ...
 1-451 1.20e-177

Predicted metal-dependent RNase, contains metallo-beta-lactamase and KH domains [General function prediction only];


Pssm-ID: 441388 [Multi-domain]  Cd Length: 460  Bit Score: 504.66  E-value: 1.20e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034   1 MKLTFWGAARKVTGSMYLLESLGYKILIDCGSDFSDRHKVLTG-GLFPFEASEIDLVILTHAHVDHSGNIPALIRAGYRG 79
Cdd:COG1782    1 MRITFLGAAREVTGSCHLLETGESRILLDCGLFQGGREERERNnDAFPFDPEELDAVVLTHAHLDHSGLLPLLVKYGYRG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034  80 QILSTAPTAELSELLFADSAYIQRAEKKIANSAPSD--------YSYKPV----DRFIPIAFNKDFELNERITVRLTPVG 147
Cdd:COG1782   81 PIYCTPPTRDLMALLLLDSAKIQEEEAEYANKKRYSghppveplYTEKDVekalKHFITLDYGEVTDIAPDIKLTFYNAG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034 148 HILGAASVFVKVEEegKTKTILFSGDVGRDNYPLLPDPEQSPQADYVLCETTYGNRVHKETEPAEEIVKRIVTEAcVDKP 227
Cdd:COG1782  161 HILGSAIVHLHIGD--GLHNIVFSGDLGRGKTPLLRPPTPFPRADTLIMESTYGGRLHPSREEAEEELAKVINET-IERG 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034 228 GRLIIPAFSLGRTQSLLYTLNKLALKNELPPIKVFTDSALAAEGTNIYSKYSSLMNGEALAIKAQDESLFDFENLDHVKT 307
Cdd:COG1782  238 GKVLIPAFAVGRTQEILYVLNELMREGKIPEVPVYLDSPMAIEATAIHTAYPEYLDEELRDLIFKGENPFLFENLHYVES 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034 308 FKESKNISNYLKPCIILSSSGMITGGRIQHHIRQNIQNPYCTILLVGYAVEGTIGHDLLAGKQTIRFKKRSIPVAAKIIY 387
Cdd:COG1782  318 VEESKEINDSDEPAIIIATSGMLTGGRILHHLKHLAPDPKNTILFVGYQAEGTLGRRLLDGAKEVKIFGETIPVRAEVET 397

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499906034 388 TDIFSGHTDVNGLIKYLGHQDKaKLKKIFLVHGEHQSMLDFEKRLHEEGYNNIEIPDYGQSYDL 451
Cdd:COG1782  398 IDGFSGHADRNELLNWLRRLKP-KPKKVFLVHGEPEAAEALASSIRKKLGIEVVIPENLETIRL 460
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 3-197 1.05e-78

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: 242.75  E-value: 1.05e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034   3 LTFWGAARKVTGSMYLLESLGYKILIDCGSDFSDRHKVLTG-GLFPFEASEIDLVILTHAHVDHSGNIPALIRAGYRGQI 81
Cdd:cd16295    1 LTFLGAAREVTGSCYLLETGGKRILLDCGLFQGGKELEELNnEPFPFDPKEIDAVILTHAHLDHSGRLPLLVKEGFRGPI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034  82 LSTAPTAELSELLFADSAYIQRAEKKIANSAPSdYSYKPVD----RFIPIAFNKDFELNERITVRLTPVGHILGAASVFV 157
Cdd:cd16295   81 YATPATKDLAELLLLDSAKIQEEEAEHPPAEPL-YTEEDVEkalkHFRPVEYGEPFEIGPGVKVTFYDAGHILGSASVEL 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 499906034 158 KVEeegKTKTILFSGDVGRDNYPLLPDPEQSPQADYVLCE 197
Cdd:cd16295  160 EIG---GGKRILFSGDLGRKNTPLLRDPAPPPEADYLIME 196
Beta-Casp smart01027
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 240-365 1.87e-43

Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in pre-mRNA 3'-end-processing endonuclease. The active site of this enzyme is located at the interface of these two domains.


Pssm-ID: 214983 [Multi-domain]  Cd Length: 126  Bit Score: 148.84  E-value: 1.87e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034   240 TQSLLYTLNKLALKNELPPIKVFTDSALAAEGTNIYSKYSSLMNGEALAIKAQDESLFDFENLDHVKTFKESKNISNYLK 319
Cdd:smart01027   1 TQELLLILEELWREGELPNVPIYLDSPMAARATEIYKSYPEWMSDEIRKRFEQGRNPFDFKNLKFVKSLEESKRLNDYKG 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 499906034   320 PCIILSSSGMITGGRIQHHIRQNIQNPYCTILLVGYAVEGTIGHDL 365
Cdd:smart01027  81 PKVIIASSGMLTGGRSRHYLKRLAPDPRNTVILTGYQAEGTLGRKL 126
Beta-Casp pfam10996
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 240-363 1.17e-34

Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in pre-mRNA 3'-end-processing endonuclease. The active site of this enzyme is located at the interface of these two domains.


Pssm-ID: 463203  Cd Length: 109  Bit Score: 124.93  E-value: 1.17e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034  240 TQSLLYTLNKLALKNELPPIKVFTDSALAAEGTNIYSKYSSLMNGEALAIkaqdeslfdfenldhVKTFKESKNISNYLK 319
Cdd:pfam10996   1 AQELLYLLDELWREGRLPKIPIYLDSPLAIKATEVYRRYPEYLDDEARHF---------------VISKSESKAINEGKG 65

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 499906034  320 PCIILSSSGMITGGRIQHHIRQNIQNPYCTILLVGYAVEGTIGH 363
Cdd:pfam10996  66 PKVIIASSGMLEGGRSRHHLKHWAPDPKNTVIFTGYQAEGTLGR 109
PRK02113 PRK02113
MBL fold metallo-hydrolase;
18-72 1.43e-05

MBL fold metallo-hydrolase;


Pssm-ID: 179371 [Multi-domain]  Cd Length: 252  Bit Score: 46.31  E-value: 1.43e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 499906034  18 LLESLGYKILIDCGSDFsdRHKVLTGGLFPFEAseidlVILTHAHVDHSGNIPAL 72
Cdd:PRK02113  39 LVETEGARILIDCGPDF--REQMLRLPFGKIDA-----VLITHEHYDHVGGLDDL 86
 
Name Accession Description Interval E-value
COG1782 COG1782
Predicted metal-dependent RNase, contains metallo-beta-lactamase and KH domains [General ...
 1-451 1.20e-177

Predicted metal-dependent RNase, contains metallo-beta-lactamase and KH domains [General function prediction only];


Pssm-ID: 441388 [Multi-domain]  Cd Length: 460  Bit Score: 504.66  E-value: 1.20e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034   1 MKLTFWGAARKVTGSMYLLESLGYKILIDCGSDFSDRHKVLTG-GLFPFEASEIDLVILTHAHVDHSGNIPALIRAGYRG 79
Cdd:COG1782    1 MRITFLGAAREVTGSCHLLETGESRILLDCGLFQGGREERERNnDAFPFDPEELDAVVLTHAHLDHSGLLPLLVKYGYRG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034  80 QILSTAPTAELSELLFADSAYIQRAEKKIANSAPSD--------YSYKPV----DRFIPIAFNKDFELNERITVRLTPVG 147
Cdd:COG1782   81 PIYCTPPTRDLMALLLLDSAKIQEEEAEYANKKRYSghppveplYTEKDVekalKHFITLDYGEVTDIAPDIKLTFYNAG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034 148 HILGAASVFVKVEEegKTKTILFSGDVGRDNYPLLPDPEQSPQADYVLCETTYGNRVHKETEPAEEIVKRIVTEAcVDKP 227
Cdd:COG1782  161 HILGSAIVHLHIGD--GLHNIVFSGDLGRGKTPLLRPPTPFPRADTLIMESTYGGRLHPSREEAEEELAKVINET-IERG 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034 228 GRLIIPAFSLGRTQSLLYTLNKLALKNELPPIKVFTDSALAAEGTNIYSKYSSLMNGEALAIKAQDESLFDFENLDHVKT 307
Cdd:COG1782  238 GKVLIPAFAVGRTQEILYVLNELMREGKIPEVPVYLDSPMAIEATAIHTAYPEYLDEELRDLIFKGENPFLFENLHYVES 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034 308 FKESKNISNYLKPCIILSSSGMITGGRIQHHIRQNIQNPYCTILLVGYAVEGTIGHDLLAGKQTIRFKKRSIPVAAKIIY 387
Cdd:COG1782  318 VEESKEINDSDEPAIIIATSGMLTGGRILHHLKHLAPDPKNTILFVGYQAEGTLGRRLLDGAKEVKIFGETIPVRAEVET 397

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499906034 388 TDIFSGHTDVNGLIKYLGHQDKaKLKKIFLVHGEHQSMLDFEKRLHEEGYNNIEIPDYGQSYDL 451
Cdd:COG1782  398 IDGFSGHADRNELLNWLRRLKP-KPKKVFLVHGEPEAAEALASSIRKKLGIEVVIPENLETIRL 460
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 1-421 3.90e-162

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 463.12  E-value: 3.90e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034   1 MKLTFWGAARKVTGSMYLLESLGYKILIDCGSDFSdrHKVLTGGLFPFEASEIDLVILTHAHVDHSGNIPALIRAGYRGQ 80
Cdd:COG1236    1 MKLTFLGAAGEVTGSCYLLETGGTRILIDCGLFQG--GKERNWPPFPFRPSDVDAVVLTHAHLDHSGALPLLVKEGFRGP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034  81 ILSTAPTAELSELLFADSAYIQRAEKKiansAPSDYSYKPVDR----FIPIAFNKDFELNErITVRLTPVGHILGAASVF 156
Cdd:COG1236   79 IYATPATADLARILLGDSAKIQEEEAE----AEPLYTEEDAERalelFQTVDYGEPFEIGG-VRVTFHPAGHILGSAQVE 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034 157 VKVEEegktKTILFSGDVGRDNYPLLPDPEQSPQADYVLCETTYGNRVHKETEPAEEIVKRIVTEAcVDKPGRLIIPAFS 236
Cdd:COG1236  154 LEVGG----KRIVFSGDYGREDDPLLAPPEPVPPADVLITESTYGDRLHPPREEVEAELAEWVRET-LARGGTVLIPAFA 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034 237 LGRTQSLLYTLNKLALKNELPPIKVFTDSaLAAEGTNIYSKYSSLMNGEAlaikaqdESLFDFENLDHVKTFKESKNIsN 316
Cdd:COG1236  229 LGRAQELLYLLRELKKEGRLPDIPIYVSG-MAIRATEIYRRHGEYLRDEA-------QDPFALPNLRFVTSVEESKAL-N 299

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034 317 YLKPCIILSSSGMITGGRIQHHIRQNIQNPYCTILLVGYAVEGTIGHDLLAGKQTIRFKKRSIPVAAKIIYTDIFSGHTD 396
Cdd:COG1236  300 RKGPAIIIAPSGMLTGGRILHHLKRFLWDPRNTILFVGYQAEGTLGRRLLRGAKEVKIFGEEVPVRARVERLFGLSAHAD 379

                        410       420
                 ....*....|....*....|....*
gi 499906034 397 VNGLIKYLGHQDKAklKKIFLVHGE 421
Cdd:COG1236  380 WDELLEWIKATGKP--ERVFLVHGE 402
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 3-197 1.05e-78

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: 242.75  E-value: 1.05e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034   3 LTFWGAARKVTGSMYLLESLGYKILIDCGSDFSDRHKVLTG-GLFPFEASEIDLVILTHAHVDHSGNIPALIRAGYRGQI 81
Cdd:cd16295    1 LTFLGAAREVTGSCYLLETGGKRILLDCGLFQGGKELEELNnEPFPFDPKEIDAVILTHAHLDHSGRLPLLVKEGFRGPI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034  82 LSTAPTAELSELLFADSAYIQRAEKKIANSAPSdYSYKPVD----RFIPIAFNKDFELNERITVRLTPVGHILGAASVFV 157
Cdd:cd16295   81 YATPATKDLAELLLLDSAKIQEEEAEHPPAEPL-YTEEDVEkalkHFRPVEYGEPFEIGPGVKVTFYDAGHILGSASVEL 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 499906034 158 KVEeegKTKTILFSGDVGRDNYPLLPDPEQSPQADYVLCE 197
Cdd:cd16295  160 EIG---GGKRILFSGDLGRKNTPLLRDPAPPPEADYLIME 196
Beta-Casp smart01027
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 240-365 1.87e-43

Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in pre-mRNA 3'-end-processing endonuclease. The active site of this enzyme is located at the interface of these two domains.


Pssm-ID: 214983 [Multi-domain]  Cd Length: 126  Bit Score: 148.84  E-value: 1.87e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034   240 TQSLLYTLNKLALKNELPPIKVFTDSALAAEGTNIYSKYSSLMNGEALAIKAQDESLFDFENLDHVKTFKESKNISNYLK 319
Cdd:smart01027   1 TQELLLILEELWREGELPNVPIYLDSPMAARATEIYKSYPEWMSDEIRKRFEQGRNPFDFKNLKFVKSLEESKRLNDYKG 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 499906034   320 PCIILSSSGMITGGRIQHHIRQNIQNPYCTILLVGYAVEGTIGHDL 365
Cdd:smart01027  81 PKVIIASSGMLTGGRSRHYLKRLAPDPRNTVILTGYQAEGTLGRKL 126
Beta-Casp pfam10996
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 240-363 1.17e-34

Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in pre-mRNA 3'-end-processing endonuclease. The active site of this enzyme is located at the interface of these two domains.


Pssm-ID: 463203  Cd Length: 109  Bit Score: 124.93  E-value: 1.17e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034  240 TQSLLYTLNKLALKNELPPIKVFTDSALAAEGTNIYSKYSSLMNGEALAIkaqdeslfdfenldhVKTFKESKNISNYLK 319
Cdd:pfam10996   1 AQELLYLLDELWREGRLPKIPIYLDSPLAIKATEVYRRYPEYLDDEARHF---------------VISKSESKAINEGKG 65

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 499906034  320 PCIILSSSGMITGGRIQHHIRQNIQNPYCTILLVGYAVEGTIGH 363
Cdd:pfam10996  66 PKVIIASSGMLEGGRSRHHLKHWAPDPKNTVIFTGYQAEGTLGR 109
Int9-11_CPSF2-3-like_MBL-fold cd07734
Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; ...
 4-197 5.78e-22

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: 93.16  E-value: 5.78e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034   4 TFWGAARKVTGSMYLLESLGYKILIDCGSDFSdrhKVLTGGLFP---FEASEIDLVILTHAHVDHSGNIPALIR-AGYRG 79
Cdd:cd07734    1 TPLGGGQEVGRSCFLVEFKGRTVLLDCGMNPG---KEDPEACLPqfeLLPPEIDAILISHFHLDHCGALPYLFRgFIFRG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034  80 QILSTAPTAELSELLFADSAyiqraeKKIANSAPSDYSYKP------VDRFIPIAFNKDFELNERITVRLTPVGHILGAA 153
Cdd:cd07734   78 PIYATHPTVALGRLLLEDYV------KSAERIGQDQSLYTPedieeaLKHIVPLGYGQSIDLFPALSLTAYNAGHVLGAA 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 499906034 154 SVFVKVEEEgktkTILFSGDVGRDNYPLLPDPEQSP-QADYVLCE 197
Cdd:cd07734  152 MWEIQIYGE----KLVYTGDFSNTEDRLLPAASILPpRPDLLITE 192
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 15-193 2.50e-17

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: 79.52  E-value: 2.50e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034    15 SMYLLESLGYKILIDCGSDFSDRhkvLTGGLFPFEASEIDLVILTHAHVDHSGNIPALIRAgYRGQILSTAPTAELsell 94
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAED---LLAELKKLGPKKIDAIILTHGHPDHIGGLPELLEA-PGAPVYAPEGTAEL---- 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034    95 fadsayiqrAEKKIANSAPSDYSYKPVDRFIPIAFNKDFEL-NERITVRLTPvGHILGAASVFVkveEEGKtktILFSGD 173
Cdd:smart00849  73 ---------LKDLLALLGELGAEAEPAPPDRTLKDGDELDLgGGELEVIHTP-GHTPGSIVLYL---PEGK---ILFTGD 136

                          170       180
                   ....*....|....*....|
gi 499906034   174 VGRDNYPLLPDPEQSPQADY 193
Cdd:smart00849 137 LLFAGGDGRTLVDGGDAAAS 156
CPSF3-like_MBL-fold cd16292
cleavage and polyadenylation specificity factor (CPSF) subunit 3 and related proteins; ...
 1-197 1.87e-16

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: 77.24  E-value: 1.87e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034   1 MKLTFWGAARKVTGSMYLLESLGYKILIDCGSdfsdrHKVLTG-GLFPF----EASEIDLVILTHAHVDHSGNIPALI-R 74
Cdd:cd16292    1 LEITPLGAGQEVGRSCVILEFKGKTIMLDCGI-----HPGYSGlASLPFfdeiDLSEIDLLLITHFHLDHCGALPYFLqK 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034  75 AGYRGQILSTAPTAELSELLFADSAyiqraekKIANSAPSDYSY------KPVDRFIPIAFNKDFELNeriTVRLTP--V 146
Cdd:cd16292   76 TNFKGRVFMTHPTKAIYKWLLSDYV-------RVSNISSDEMLYtetdleASMDKIETIDFHQEVEVN---GIKFTAynA 145

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 499906034 147 GHILGAASVFVkveEEGKTKtILFSGDVGRDNYPLLPDPEQSP-QADYVLCE 197
Cdd:cd16292  146 GHVLGAAMFMV---EIAGVR-VLYTGDYSREEDRHLPAAEIPPiKPDVLIVE 193
INTS11-like_MBL-fold cd16291
Integrator complex subunit 11, and related proteins; MBL-fold metallo-hydrolase domain; ...
 7-184 2.55e-16

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: 77.30  E-value: 2.55e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034   7 GAARKVTGSMYLLESLGYKILIDCGSD--------FSDRHKVLTGGLFpfeASEIDLVILTHAHVDHSGNIPALI-RAGY 77
Cdd:cd16291    5 GAGQDVGRSCILVTIGGKNIMFDCGMHmgynderrFPDFSYISQNGPF---TEHIDCVIISHFHLDHCGALPYFTeVVGY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034  78 RGQILSTAPTAELSELLFADSAYIQRAEKKIANSAPSDYSYKPVDRFIPIAFNKDFELNERITVRLTPVGHILGAASVFV 157
Cdd:cd16291   82 DGPIYMTHPTKAICPILLEDYRKIAVERKGETNFFTSQMIKDCMKKVIAVNLHETVQVDDELEIKAYYAGHVLGAAMFYV 161

                        170       180
                 ....*....|....*....|....*..
gi 499906034 158 KVEEEgktkTILFSGDvgrdnYPLLPD 184
Cdd:cd16291  162 RVGDE----SVVYTGD-----YNMTPD 179
RMMBL pfam07521
Zn-dependent metallo-hydrolase RNA specificity domain; The metallo-beta-lactamase fold ...
 378-443 7.24e-15

Zn-dependent metallo-hydrolase RNA specificity domain; The metallo-beta-lactamase fold contains five sequence motifs. The first four motifs are found in pfam00753 and are common to all metallo-beta-lactamases. This, the fifth motif, appears to be specific to Zn-dependent metallohydrolases such as ribonuclease J 2 which are involved in the processing of mRNA. This domain adds essential structural elements to the CASP-domain and is unique to RNA/DNA-processing nucleases, showing that they are pre-mRNA 3'-end-processing endonucleases.


Pssm-ID: 462191 [Multi-domain]  Cd Length: 63  Bit Score: 68.80  E-value: 7.24e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499906034  378 SIPVAAKIIYTDIFSGHTDVNGLIKYLGHqdkAKLKKIFLVHGEHQSMLDFEKRLHEEGYNNIEIP 443
Cdd:pfam07521   1 GIPVRARIETIDGFSGHADRRELLELIKG---LKPKPIVLVHGEPRALLALAELLKEELGIEVFVP 63
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
1-232 9.38e-15

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 73.69  E-value: 9.38e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034   1 MKLTFWG-------AARKVTGsmYLLESLGYKILIDCGSDFSDR---HKVltgglfpfEASEIDLVILTHAHVDHSGNIP 70
Cdd:COG1234    1 MKLTFLGtggavptPGRATSS--YLLEAGGERLLIDCGEGTQRQllrAGL--------DPRDIDAIFITHLHGDHIAGLP 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034  71 ALIRAGY------RGQILSTAPTAELSELLFADSAYiqraekkiansaPSDYSYkpvdRFIPIAFNKDFELNErITVRLT 144
Cdd:COG1234   71 GLLSTRSlagrekPLTIYGPPGTKEFLEALLKASGT------------DLDFPL----EFHEIEPGEVFEIGG-FTVTAF 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034 145 PVGHILGAASvfVKVEEEGktKTILFSGDVGrdnypllPDP---EQSPQADYVLCETTYGNRVHKETEP-----AEEiVK 216
Cdd:COG1234  134 PLDHPVPAYG--YRFEEPG--RSLVYSGDTR-------PCEalvELAKGADLLIHEATFLDEEAELAKEtghstAKE-AA 201

                        250
                 ....*....|....*.
gi 499906034 217 RIVTEAcvdKPGRLII 232
Cdd:COG1234  202 ELAAEA---GVKRLVL 214
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 15-179 1.15e-13

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: 70.32  E-value: 1.15e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034  15 SMYLLESLGYKILIDCGsdFSDRHKVLTGGLFPFEA--------------------SEIDLVILTHAHVDHSGNIPALir 74
Cdd:cd07729   33 YAYLIEHPEGTILVDTG--FHPDAADDPGGLELAFPpgvteeqtleeqlarlgldpEDIDYVILSHLHFDHAGGLDLF-- 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034  75 agyrgqilstaPTAELsellfadsaYIQRAE-KKIANSAPSDYSYKPVDRFIP--------IAFNKDFELNERITVRLTP 145
Cdd:cd07729  109 -----------PNATI---------IVQRAElEYATGPDPLAAGYYEDVLALDddlpggrvRLVDGDYDLFPGVTLIPTP 168

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 499906034 146 vGHILGAASVFVKVEEegktKTILFSGDVG--RDNY 179
Cdd:cd07729  169 -GHTPGHQSVLVRLPE----GTVLLAGDAAytYENL 199
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 11-174 2.59e-12

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: 65.30  E-value: 2.59e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034  11 KVTGSMYLLESLGYKILIDCGSdFSDRHKVLTG----GLFPfeaSEIDLVILTHAHVDHSGNIPaliragyrgqilstap 86
Cdd:cd07711   19 RASSTVTLIKDGGKNILVDTGT-PWDRDLLLKAlaehGLSP---EDIDYVVLTHGHPDHIGNLN---------------- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034  87 taelselLFADSayiqraeKKIANSAPSDYSYKPVDRFipiaFNKDFELNERITVRLTPvGHILGAASVFVKVEEEGktk 166
Cdd:cd07711   79 -------LFPNA-------TVIVGWDICGDSYDDHSLE----EGDGYEIDENVEVIPTP-GHTPEDVSVLVETEKKG--- 136


                 ....*...
gi 499906034 167 TILFSGDV 174
Cdd:cd07711  137 TVAVAGDL 144
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 17-197 4.77e-12

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: 64.21  E-value: 4.77e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034  17 YLLESLGYKILIDCGSdfSDRHKVLTGGLFPfeaSEIDLVILTHAHVDHSGNIPALI---RAGYRGQILStaptaelsel 93
Cdd:cd16272   20 YLLETGGTRILLDCGE--GTVYRLLKAGVDP---DKLDAIFLSHFHLDHIGGLPTLLfarRYGGRKKPLT---------- 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034  94 LFA---DSAYIQRAEKKIANSAPSDYSYKpvdrFIPIAFNKDFELNERITVRLTPVGHILGaaSVFVKVEEEGktKTILF 170
Cdd:cd16272   85 IYGpkgIKEFLEKLLNFPVEILPLGFPLE----IEELEEGGEVLELGDLKVEAFPVKHSVE--SLGYRIEAEG--KSIVY 156

                        170       180
                 ....*....|....*....|....*..
gi 499906034 171 SGDVGrdnyPLLPDPEQSPQADYVLCE 197
Cdd:cd16272  157 SGDTG----PCENLVELAKGADLLIHE 179
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 17-180 4.01e-11

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: 61.92  E-value: 4.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034  17 YLLES-LGYKILIDCGSDFSDR--HKVLTGGLfpfeasEIDLVILTHAHVDHSGNIPALiRAGYRGQIlstaptaelsel 93
Cdd:cd06262   13 YLVSDeEGEAILIDPGAGALEKilEAIEELGL------KIKAILLTHGHFDHIGGLAEL-KEAPGAPV------------ 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034  94 lfadsaYIQRAEKKIANSAPSDYSY------KPVDRFIPIAFNKDFEL-NERITVRLTPvGHilGAASVFVKVEEEGktk 166
Cdd:cd06262   74 ------YIHEADAELLEDPELNLAFfgggplPPPEPDILLEDGDTIELgGLELEVIHTP-GH--TPGSVCFYIEEEG--- 141

                        170       180
                 ....*....|....*....|
gi 499906034 167 tILFSGD------VGRDNYP 180
Cdd:cd06262  142 -VLFTGDtlfagsIGRTDLP 160
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 2-173 4.92e-11

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: 61.86  E-value: 4.92e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034   2 KLTFWGAARKVTGSMYLLESLGYKILIDCGSDFSDRHK------------------------VLTGGLFPFEASEIDLVI 57
Cdd:cd07732    1 RITIHRGTNEIGGNCIEVETGGTRILLDFGLPLDPESKyfdevldflelgllpdivglyrdpLLLGGLRSEEDPSVDAVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034  58 LTHAHVDHSGNIPAL---IragyrgQILSTAPTAELSELLFADSAYIQRAEKKIansapsdysykpvdrfIPIAFNKDFE 134
Cdd:cd07732   81 LSHAHLDHYGLLNYLrpdI------PVYMGEATKRILKALLPFFGEGDPVPRNI----------------RVFESGKSFT 138

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 499906034 135 LNErITVRLTPVGH-ILGAASVFVKVEEegktKTILFSGD 173
Cdd:cd07732  139 IGD-FTVTPYLVDHsAPGAYAFLIEAPG----KRIFYTGD 173
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 1-200 5.39e-11

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 62.61  E-value: 5.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034   1 MKLTFWGAA---------------------RKVTGSMYLLESLGYKILIDCGSDFsdRHKVLTGGLFPfeaSEIDLVILT 59
Cdd:COG1235    1 MKVTFLGSGssggvpqigcdcpvcastdprYGRTRSSILVEADGTRLLIDAGPDL--REQLLRLGLDP---SKIDAILLT 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034  60 HAHVDHSGNIPALIRAGYRGQIlstaPtaelselLFADSAYIQRAEKKIansAPSDYSYKPVDRFIPIAFNKDFELNErI 139
Cdd:COG1235   76 HEHADHIAGLDDLRPRYGPNPI----P-------VYATPGTLEALERRF---PYLFAPYPGKLEFHEIEPGEPFEIGG-L 140

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499906034 140 TVRLTPVGHilGAA-SVFVKVEEEGktKTILFSGDVGRdnyplLPDP--EQSPQADYVLCETTY 200
Cdd:COG1235  141 TVTPFPVPH--DAGdPVGYRIEDGG--KKLAYATDTGY-----IPEEvlELLRGADLLILDATY 195
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
14-175 9.83e-11

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 60.85  E-value: 9.83e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034   14 GSMYLLESLGYKILIDCGSDFSDRHKVLTGGLFpFEASEIDLVILTHAHVDHSGNIPALIRAGyrgqilsTAPTAELSEL 93
Cdd:pfam00753   6 VNSYLIEGGGGAVLIDTGGSAEAALLLLLAALG-LGPKDIDAVILTHGHFDHIGGLGELAEAT-------DVPVIVVAEE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034   94 LFadsAYIQRAEKKIANSAPSDYSYKPVDRFIPIAFNKDFELNERITVRLTpvgHILGAASVFVKVEEEGktKTILFSGD 173
Cdd:pfam00753  78 AR---ELLDEELGLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVT---HGPGHGPGHVVVYYGG--GKVLFTGD 149


                  ..
gi 499906034  174 VG 175
Cdd:pfam00753 150 LL 151
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 15-173 3.66e-10

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


Pssm-ID: 293826 [Multi-domain]  Cd Length: 194  Bit Score: 59.19  E-value: 3.66e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034  15 SMYLLESLGYKILIDCGSDfsdrhkVLTG----GLFPfeaSEIDLVILTHAHVDHSGNIPALI-----RAGYRG--QILS 83
Cdd:cd07740   17 TCFHVASEAGRFLIDCGAS------SLIAlkraGIDP---NAIDAIFITHLHGDHFGGLPFFLldaqfVAKRTRplTIAG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034  84 TAPTAE----LSELLFADSAYIQRAekkiansapSDYSYKPVDRFIPIAFNkdfelneRITVRLTPVGHILGAASVFVKV 159
Cdd:cd07740   88 PPGLRErlrrAMEALFPGSSKVPRR---------FDLEVIELEPGEPTTLG-------GVTVTAFPVVHPSGALPLALRL 151

                        170
                 ....*....|....
gi 499906034 160 EEEGktKTILFSGD 173
Cdd:cd07740  152 EAAG--RVLAYSGD 163
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 2-198 4.61e-10

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: 58.61  E-value: 4.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034   2 KLT---FWGAARKVTG--SMYLLESLGYKILIDCGSDfsdrhkVLtGGLFPF-EASEIDLVILTHAHVDHSGNIPALIRA 75
Cdd:cd07716    1 KLTvlgCSGSYPGPGGacSGYLLEADGFRILLDCGSG------VL-SRLQRYiDPEDLDAVVLSHLHPDHCADLGVLQYA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034  76 gyrgqiLSTAPTAELSE--LLFA---DSAYIQRAekkiansapsdYSYKPVDRFIPIAFNKDFELnERITVRLTPVGHIL 150
Cdd:cd07716   74 ------RRYHPRGARKPplPLYGpagPAERLAAL-----------YGLEDVFDFHPIEPGEPLEI-GPFTITFFRTVHPV 135

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 499906034 151 GAASvfVKVEEEGktKTILFSGDVGrdnypllPDPEQSP---QADYVLCET 198
Cdd:cd07716  136 PCYA--MRIEDGG--KVLVYTGDTG-------YCDELVEfarGADLLLCEA 175
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 17-174 5.35e-10

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: 58.93  E-value: 5.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034  17 YLLESLGYKILIDCGSDFSDRHKVLTG----GLfpfeasEIDLVILTHAHVDHSGNIPALiRAGYRGQIlstaptaelse 92
Cdd:COG0491   18 YLIVGGDGAVLIDTGLGPADAEALLAAlaalGL------DIKAVLLTHLHPDHVGGLAAL-AEAFGAPV----------- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034  93 llfadsaYIQRAEKKIANSAPSD--YSYKPVDRFIPIAFNKDFEL-NERITVRLTPvGHILGaaSVFVKVEEEGktktIL 169
Cdd:COG0491   80 -------YAHAAEAEALEAPAAGalFGREPVPPDRTLEDGDTLELgGPGLEVIHTP-GHTPG--HVSFYVPDEK----VL 145


                 ....*
gi 499906034 170 FSGDV 174
Cdd:COG0491  146 FTGDA 150
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 18-151 8.17e-09

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


Pssm-ID: 293837 [Multi-domain]  Cd Length: 193  Bit Score: 55.17  E-value: 8.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034  18 LLESLGYKILIDCGSDFsdRHKVLTGGLfpfeaSEIDLVILTHAHVDHSGNIPALiRAGYRGQ-----ILSTAPTAELSE 92
Cdd:cd16279   39 LIETGGKNILIDTGPDF--RQQALRAGI-----RKLDAVLLTHAHADHIHGLDDL-RPFNRLQqrpipVYASEETLDDLK 110

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499906034  93 LLFADSAYiqraekkiansaPSDYSYKPVDRFIPIAFNKDFELNErITVRLTPVGH----ILG 151
Cdd:cd16279  111 RRFPYFFA------------ATGGGGVPKLDLHIIEPDEPFTIGG-LEITPLPVLHgklpSLG 160
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 26-175 1.75e-08

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: 54.24  E-value: 1.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034   26 ILIDCGSDFSDRHKVLtggLFPFEA--SEIDLVILTHAHVDHSGNIPALiRAGYRGQILSTAPTAE-LSELLFADSAYIQ 102
Cdd:pfam12706   3 ILIDPGPDLRQQALPA---LQPGRLrdDPIDAVLLTHDHYDHLAGLLDL-REGRPRPLYAPLGVLAhLRRNFPYLFLLEH 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034  103 RAEkkiansapsdysykpvdRFIPIAFNKDFELN-ERITVRLTPVGHilGAASVFVKVEE-------EGKTKTILFSGDV 174
Cdd:pfam12706  79 YGV-----------------RVHEIDWGESFTVGdGGLTVTATPARH--GSPRGLDPNPGdtlgfriEGPGKRVYYAGDT 139


                  .
gi 499906034  175 G 175
Cdd:pfam12706 140 G 140
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 14-173 4.43e-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: 52.90  E-value: 4.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034  14 GSMYLLESLGYKILIDCGSDFSDRHkVLTGglFPFEAseIDLVILTHAHVDHSGNIPALIRAGYRGQILST------APT 87
Cdd:cd07719   18 GPSTLVVVGGRVYLVDAGSGVVRRL-AQAG--LPLGD--LDAVFLTHLHSDHVADLPALLLTAWLAGRKTPlpvygpPGT 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034  88 AELSELLFADSAYIQRAEKKIANSAPSDYSYKPvdRFIPIAFNKDFELNERITVRLTPVGHILGAASV---FvkveeEGK 164
Cdd:cd07719   93 RALVDGLLAAYALDIDYRARIGDEGRPDPGALV--EVHEIAAGGVVYEDDGVKVTAFLVDHGPVPPALayrF-----DTP 165


                 ....*....
gi 499906034 165 TKTILFSGD 173
Cdd:cd07719  166 GRSVVFSGD 174
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 26-187 5.12e-08

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: 53.74  E-value: 5.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034  26 ILIDCGSDFSDRHkVLTGGL--FPFEASEIDLVILTHAHVDHSGNiPALIRAGYRGQILSTAPTAELSEllfadsayiQR 103
Cdd:cd16280   34 ILIDALNNNEAAD-LIVDGLekLGLDPADIKYILITHGHGDHYGG-AAYLKDLYGAKVVMSEADWDMME---------EP 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034 104 AEKKIANSAPSDYsykPVDRFI----PIAFNkdfelNERITVRLTPvGHILGAASVFVKVEEEGKTKTILFSGDVGrdnY 179
Cdd:cd16280  103 PEEGDNPRWGPPP---ERDIVIkdgdTLTLG-----DTTITVYLTP-GHTPGTLSLIFPVKDGGKTHRAGLWGGTG---L 170


                 ....*...
gi 499906034 180 PLLPDPEQ 187
Cdd:cd16280  171 NTGPNLER 178
class_II_PDE_MBL-fold cd07735
class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium ...
 17-207 1.65e-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: 52.21  E-value: 1.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034  17 YLL---ESLGYkILIDCGSDFSD--RHKVLTGGLFP------FEASEIDLVILTHAHVDH-SG---NIPALIRAGYRG-Q 80
Cdd:cd07735   20 FLLdpaGSDGD-ILLDAGTGVGAlsLEEMFNDILFPsqkaayELYQRIRHYLITHAHLDHiAGlplLSPNDGGQRGSPkT 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034  81 ILSTAPTAE-LSELLFADSAYIqraekKIANSAPSDYSYKpvdRFIPIAFNKDFELNERiTVRLTPVGHILGAASVFVkV 159
Cdd:cd07735   99 IYGLPETIDaLKKHIFNWVIWP-----DFTSIPSGKYPYL---RLEPIEPEYPIALTGL-SVTAFPVSHGVPVSTAFL-I 168

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 499906034 160 EEEGktKTILFSGDVGRD---NYPLLPD------PEQSPQADYVLCETTYGNRVHKE 207
Cdd:cd07735  169 RDGG--DSFLFFGDTGPDsvsKSPRLDAlwralaPLIPKKLKAIIIECSFPNSRPDA 223
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 23-177 2.87e-07

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


Pssm-ID: 441904 [Multi-domain]  Cd Length: 253  Bit Score: 51.40  E-value: 2.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034  23 GYKILIDCGSDFSDR--HKVLTGGLFPFEASEIDLVILTHAHVDHSGNIPALIRAgYR-GQILSTAPTaelsellfADSA 99
Cdd:COG2333   21 GKTILIDTGPRPSFDagERVVLPYLRALGIRRLDLLVLTHPDADHIGGLAAVLEA-FPvGRVLVSGPP--------DTSE 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034 100 YIQRAEKKIANSAPSDYSYKPVDRfipiafnkdFELNE-RITVrLTPVGHILG-----AASVFVKVeeEGKTKTILFSGD 173
Cdd:COG2333   92 TYERLLEALKEKGIPVRPCRAGDT---------WQLGGvRFEV-LWPPEDLLEgsdenNNSLVLRL--TYGGFSFLLTGD 159


                 ....
gi 499906034 174 VGRD 177
Cdd:COG2333  160 AEAE 163
CPSF2-like_MBL-fold cd16293
cleavage and polyadenylation specificity factor (CPSF) subunit 2 and related proteins; ...
 17-90 1.35e-06

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: 48.67  E-value: 1.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034  17 YLLESLGYKILIDCGSDfsdrhkvltgGLFPFE--------ASEIDLVILTHAHVDHSGNIPALIRA-GYRGQILSTAPT 87
Cdd:cd16293   15 YLLEIDDVTILLDCGWD----------ESFDMEyleslkriAPTIDAVLLSHPDLEHLGALPYLVGKlGLTCPVYATLPV 84


                 ...
gi 499906034  88 AEL 90
Cdd:cd16293   85 HKM 87
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 1-173 1.81e-06

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 48.76  E-value: 1.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034   1 MKLTFWGaarkvtGSMYLLESLGYKILIDCGsdFSDRHKVLTGGLFPFEA-SEIDLVILTHAHVDHSGniPALIRAgyrg 79
Cdd:COG2220    4 MKITWLG------HATFLIETGGKRILIDPV--FSGRASPVNPLPLDPEDlPKIDAVLVTHDHYDHLD--DATLRA---- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034  80 qILSTAPTaelselLFA---DSAYIQRaekkiansapsdysyKPVDRFIPIAFNKDFELNErITVRLTPVGH-------I 149
Cdd:COG2220   70 -LKRTGAT------VVAplgVAAWLRA---------------WGFPRVTELDWGESVELGG-LTVTAVPARHssgrpdrN 126

                        170       180
                 ....*....|....*....|....
gi 499906034 150 LGAASVFVkVEEEGktKTILFSGD 173
Cdd:COG2220  127 GGLWVGFV-IETDG--KTIYHAGD 147
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 18-75 1.98e-06

Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This subgroup includes proteins required for natural transformation competence including Neisseria gonorrhoeae ComA, Pseudomonas stutzeri ComA, Bacillus subtilis ComEC (also known as ComE operon protein 3) and Haemophilus influenza ORF2 encoded by the rec-2 gene, as well as Escherichia coli YcaI which does not mediate spontaneous plasmid transformation on nutrient-containing agar plates. It also includes the phosphorylcholine esterase (Pce) domain of choline-binding protein e from streptococcus pneumonia. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293817 [Multi-domain]  Cd Length: 179  Bit Score: 47.90  E-value: 1.98e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 499906034  18 LLESLGYKILIDCGSDFSDRHKVLTGGLFPFEASEIDLVILTHAHVDHSGNIPALIRA 75
Cdd:cd07731   14 LIQTPGKTILIDTGPRDSFGEDVVVPYLKARGIKKLDYLILTHPDADHIGGLDAVLKN 71
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 17-185 2.71e-06

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


Pssm-ID: 293807 [Multi-domain]  Cd Length: 202  Bit Score: 47.99  E-value: 2.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034  17 YLLESLGYKILIDCGsdFSDRHKVLTGGLFP--FEASEIDLVILTHAHVDHSGNIPALIRAgyrgqilSTAPT----AEL 90
Cdd:cd07721   14 YLIEDDDGLTLIDTG--LPGSAKRILKALRElgLSPKDIRRILLTHGHIDHIGSLAALKEA-------PGAPVyaheREA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034  91 sELLFADSAYIQRAEKKIANSAPSDYSYKPVDRFIPIAFNKDFELNERITVRLTPvGHILGAASVFvkVEEEGktktILF 170
Cdd:cd07721   85 -PYLEGEKPYPPPVRLGLLGLLSPLLPVKPVPVDRTLEDGDTLDLAGGLRVIHTP-GHTPGHISLY--LEEDG----VLI 156

                        170
                 ....*....|....*..
gi 499906034 171 SGD--VGRDNYPLLPDP 185
Cdd:cd07721  157 AGDalVTVGGELVPPPP 173
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 17-174 3.87e-06

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: 47.93  E-value: 3.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034  17 YLLESLGYKILIDCGSdfsdrhkvltGGLFP--------------FEASEIDLVILTHAHVDHSGNipaLIRAGYRgqil 82
Cdd:cd07720   52 FLVRTGGRLILVDTGA----------GGLFGptagkllanlaaagIDPEDIDDVLLTHLHPDHIGG---LVDAGGK---- 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034  83 STAPTAELsellfadsaYIQRAE----KKIANSAPSDYSYKPV-----DRFIPIA----FNKDFELNERITVRLTPvGHI 149
Cdd:cd07720  115 PVFPNAEV---------HVSEAEwdfwLDDANAAKAPEGAKRFfdaarDRLRPYAaagrFEDGDEVLPGITAVPAP-GHT 184

                        170       180
                 ....*....|....*....|....*
gi 499906034 150 LGAASVFVkveeEGKTKTILFSGDV 174
Cdd:cd07720  185 PGHTGYRI----ESGGERLLIWGDI 205
SMB-1-like_MBL-B3 cd16313
SMB-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase ...
 15-193 5.76e-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: 47.55  E-value: 5.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034  15 SMYLLESLGYKILIDCGsdFSDRHKVLTGGL--FPFEASEIDLVILTHAHVDHSGNIPALIRAGyRGQILSTAPTAELse 92
Cdd:cd16313   23 SAVLITSPQGHILIDGG--FPKSPEQIAASIrqLGFKLEDVKYILSSHDHWDHAGGIAALQKLT-GAQVLASPATVAV-- 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034  93 llfadsayIQRAEkkianSAPSDYSYKPVDRFIPIAFNK---DFELneritVRLTPV--------GHILGAASVFVKVEE 161
Cdd:cd16313   98 --------LRSGS-----MGKDDPQFGGLTPMPPVASVRavrDGEV-----VKLGPLavtahatpGHTTGGTSWTWQSCE 159

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 499906034 162 EGKTKTILFsGD----VGRDNYPLLPDPEQspQADY 193
Cdd:cd16313  160 QGRCANMVF-ADsltaVSADGYRFSAHPAV--LADV 192
PRK02113 PRK02113
MBL fold metallo-hydrolase;
18-72 1.43e-05

MBL fold metallo-hydrolase;


Pssm-ID: 179371 [Multi-domain]  Cd Length: 252  Bit Score: 46.31  E-value: 1.43e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 499906034  18 LLESLGYKILIDCGSDFsdRHKVLTGGLFPFEAseidlVILTHAHVDHSGNIPAL 72
Cdd:PRK02113  39 LVETEGARILIDCGPDF--REQMLRLPFGKIDA-----VLITHEHYDHVGGLDDL 86
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 16-185 1.97e-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: 45.86  E-value: 1.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034  16 MYLLESLGYKILIDCGSDFSDrhkVLTGGlfpfeaseIDLVI-----------------LTHAHVDHSGNIPALIRAgYR 78
Cdd:cd07714   13 MYVVEYDDDIIIIDCGLKFPD---EDMPG--------VDYIIpdfsyleenkdkikgifITHGHEDHIGALPYLLPE-LN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034  79 GQILSTAPTAELsellfadsayiqrAEKKIansapSDYSYKPVDRFIPIAFNKDFELNErITVRLTPVGH-ILGAASVFV 157
Cdd:cd07714   81 VPIYATPLTLAL-------------IKKKL-----EEFKLIKKVKLNEIKPGERIKLGD-FEVEFFRVTHsIPDSVGLAI 141

                        170       180
                 ....*....|....*....|....*...
gi 499906034 158 KVeEEGktkTILFSGDVGRDNYPLLPDP 185
Cdd:cd07714  142 KT-PEG---TIVHTGDFKFDQTPVDGKP 165
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 17-174 2.36e-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) for which this fold was named perform only a small fraction of the activities included in this superfamily.Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293835 [Multi-domain]  Cd Length: 222  Bit Score: 45.21  E-value: 2.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034  17 YLLESLGYKILIDCGSDfsdRHKVLTGGLF------PFEAS---------EIDLVILTHAHVDHSG-N--------IPAL 72
Cdd:cd16277   16 WLVRTPGRTILVDTGIG---NDKPRPGPPAfhnlntPYLERlaaagvrpeDVDYVLCTHLHVDHVGwNtrlvdgrwVPTF 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034  73 IRAGYrgqilstaptaelselLF--ADSAYIQRAEKKIANSAPSDysykpVDRFIPI-------AFNKDFELNERITVRL 143
Cdd:cd16277   93 PNARY----------------LFsrAEYDHWSSPDAGGPPNRGVF-----EDSVLPVieagladLVDDDHEILDGIRLEP 151

                        170       180       190
                 ....*....|....*....|....*....|.
gi 499906034 144 TPvGHILGAASVFVkveeEGKTKTILFSGDV 174
Cdd:cd16277  152 TP-GHTPGHVSVEL----ESGGERALFTGDV 177
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 15-194 4.07e-05

uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized human MBLAC2 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: 293798 [Multi-domain]  Cd Length: 182  Bit Score: 44.16  E-value: 4.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034  15 SMYLLESLGYKILIDCGS-DFSDRHKVLTGGLFPFeaseidLVILTHAHVDHSGNIpaliraGYrgqilstaptaelsel 93
Cdd:cd07712   10 NIYLLRGRDRALLIDTGLgIGDLKEYVRTLTDLPL------LVVATHGHFDHIGGL------HE---------------- 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034  94 lFADsAYIQRAEKKIANS---------APSDYSYKPVDRFIPIAFNKDFELNER-ITVRLTPvGHILGAASVFvkveeeG 163
Cdd:cd07712   62 -FEE-VYVHPADAEILAApdnfetltwDAATYSVPPAGPTLPLRDGDVIDLGDRqLEVIHTP-GHTPGSIALL------D 132

                        170       180       190
                 ....*....|....*....|....*....|.
gi 499906034 164 KTKTILFSGDVGRDNyPLLPDPEQSPQADYV 194
Cdd:cd07712  133 RANRLLFSGDVVYDG-PLIMDLPHSDLDDYL 162
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
17-141 2.22e-04

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


Pssm-ID: 440850  Cd Length: 273  Bit Score: 42.95  E-value: 2.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034  17 YLLESLGYKILIDCGSdfsdrhkvltGGLFP-------FEASEIDLVILTHAHVDHSGNIPALIRAGYRGQILstaptae 89
Cdd:COG1237   25 ALIETEGKRILFDTGQ----------SDVLLknaeklgIDLSDIDAVVLSHGHYDHTGGLPALLELNPKAPVY------- 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 499906034  90 LSELLFADSAYIQRAEKKIANSAPSDYSYKPVDRFIPIafNKDFELNERITV 141
Cdd:COG1237   88 AHPDAFEKRYSKRPGGKYIGIPFSREELEKLGARLILV--KEPTEIAPGVYL 137
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 17-141 2.29e-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: 42.61  E-value: 2.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034  17 YLLESLGYKILIDCGSdfsdrhkvlTGGLFP------FEASEIDLVILTHAHVDHSGNIPALIRAGYRGQILstaptaeL 90
Cdd:cd07713   23 LLIETEGKKILFDTGQ---------SGVLLHnakklgIDLSDIDAVVLSHGHYDHTGGLKALLELNPKAPVY-------A 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 499906034  91 SELLFaDSAYIQRAEKKIANSAPSDYSYKPVDRFIPIafNKDFELNERITV 141
Cdd:cd07713   87 HPDAF-EPRYSKRGGGKKGIGIGREELEKAGARLVLV--EEPTEIAPGVYL 134
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 48-180 2.44e-04

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: 42.69  E-value: 2.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034  48 FEASEIDLVILTHAHVDHSGNIpALIRAGYRGQILSTAPTAELsellfadsayiqraekkIANSAPSDYSY-KPVDRFIP 126
Cdd:cd16288   56 FKPSDIKILLNSHAHLDHAGGL-AALKKLTGAKLMASAEDAAL-----------------LASGGKSDFHYgDDSLAFPP 117

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034 127 IAFNKDFELNERI-------TVRLTPvGHILGAASVFVKVEEEGKTKTILFSGD---------VGRDNYP 180
Cdd:cd16288  118 VKVDRVLKDGDRVtlggttlTAHLTP-GHTRGCTTWTMTVKDDGKVYQVVFADSltvnpgyklVGNPTYP 186
metallo-hydrolase-like_MBL-fold cd07741
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 7-75 2.44e-04

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


Pssm-ID: 293827 [Multi-domain]  Cd Length: 212  Bit Score: 42.18  E-value: 2.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034   7 GAARKV-------TGSMYLlESLGYKILIDCGSdfsdrhkvltGGL-----FPFEASEIDLVILTHAHVDHSGNIPALIR 74
Cdd:cd07741    7 GGGRFVvitqlraSGGIWI-ELNGKNIHIDPGP----------GALvrmcrPKLDPTKLDAIILSHRHLDHSNDANVLIE 75


                 .
gi 499906034  75 A 75
Cdd:cd07741   76 A 76
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 15-175 2.90e-04

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: 42.53  E-value: 2.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034  15 SMYLLESLGYKILIDCGSDFSDRHKVLTGGLFPFEASEIDLVILTHAHVDHSGNIpALIRAGYRGQILSTAPTAELseLL 94
Cdd:cd07708   23 AAYLIVTPQGNILIDGDMEQNAPMIKANIKKLGFKFSDTKLILISHAHFDHAGGS-AEIKKQTGAKVMAGAEDVSL--LL 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034  95 FADSAYIQRaekkiANSAPSDYSYKPVDRFIpiafnKDFELNE----RITVRLTPvGHILGAASVFVKVEEEGKTKTILF 170
Cdd:cd07708  100 SGGSSDFHY-----ANDSSTYFPQSTVDRAV-----HDGERVTlggtVLTAHATP-GHTPGCTTWTMTLKDHGKQYQVVF 168


                 ....*
gi 499906034 171 SGDVG 175
Cdd:cd07708  169 ADSLT 173
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 11-75 3.73e-04

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


Pssm-ID: 293812 [Multi-domain]  Cd Length: 215  Bit Score: 41.71  E-value: 3.73e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499906034  11 KVTGSmYLLESLGYKILIDCGSdfSDRHKVLTGGL----FPFEasEIDLVILTHAHVDHSGNIPALIRA 75
Cdd:cd07726   14 GRIAS-YLLDGEGRPALIDTGP--SSSVPRLLAALealgIAPE--DVDYIILTHIHLDHAGGAGLLAEA 77
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 13-89 9.95e-04

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: 39.55  E-value: 9.95e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499906034  13 TGSMYLLESLGYKILIDCGsdFSDRHkvLTGGLFPF--EASEIDLVILTHAHVDHSGNIPALIRAgYRGQILSTAPTAE 89
Cdd:cd07733    8 KGNCTYLETEDGKLLIDAG--LSGRK--ITGRLAEIgrDPEDIDAILVTHEHADHIKGLGVLARK-YNVPIYATAGTLR 81
AIM-1_SMB-1-like_MBL-B3 cd16290
AIM-1, SMB-1, EVM-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 48-179 1.40e-03

AIM-1, SMB-1, EVM-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; This subgroup of B3 subclass MBLs includes Pseudomonas Aeruginosa AIM-1, Serratia marcescens SMB-1, Erythrobacter vulgaris EVM-1, and Janthinobacterium lividum THIN-B. 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 AIM-1-,SMB-1-, EVM-1-, 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: 293848 [Multi-domain]  Cd Length: 256  Bit Score: 40.41  E-value: 1.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034  48 FEASEIDLVILTHAHVDHSGNIPALIRAgyrgqilSTAPTAELSellfADSAYIQRAEkkianSAPSDYSYKPVDRFIPI 127
Cdd:cd16290   56 FRLEDVKLILNSHAHFDHAGGIAALQRD-------SGATVAASP----AGAAALRSGG-----VDPDDPQAGAADPFPPV 119

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499906034 128 AfnKDFELNERITVRLTPV--------GHILGAASVFVKVEEEGKTKTILF---SGDVGRDNY 179
Cdd:cd16290  120 A--KVRVVADGEVVKLGPLavtahatpGHTPGGTSWTWRSCEGGRCLDIVYadsLTAVSADGF 180
metallo-hydrolase-like_MBL-fold cd16281
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 18-67 1.44e-03

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


Pssm-ID: 293839  Cd Length: 252  Bit Score: 40.17  E-value: 1.44e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499906034  18 LLESLGYKILIDCGSD------FSDRHKVLTGGLFP-------FEASEIDLVILTHAHVDHSG 67
Cdd:cd16281   47 LIETGGRNILIDTGIGdkqdpkFRSIYVQHSEHSLLkslarlgLSPEDITDVILTHLHFDHCG 109
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 17-75 1.50e-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: 39.44  E-value: 1.50e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 499906034  17 YLLESLGYKILIDCGSDFSDRHKVLTGGLFPFEASEIDLVILTHAHVDHSGNIPALIRA 75
Cdd:cd07722   21 YLVGTGKRRILIDTGEGRPSYIPLLKSVLDSEGNATISDILLTHWHHDHVGGLPDVLDL 79
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 53-174 1.61e-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: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 39.86  E-value: 1.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034  53 IDLVILTHAHVDHS-GNiPALIRAGyrGQILSTAPTAElsELLFADSAYIQRAEKKIANSAPSDYSYKPVdrfIPIAFNK 131
Cdd:cd16282   53 VRYVVNTHYHGDHTlGN-AAFADAG--APIIAHENTRE--ELAARGEAYLELMRRLGGDAMAGTELVLPD---RTFDDGL 124

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 499906034 132 DFELNERiTVRLTPVGHILGAASVFVKVEEEGktktILFSGDV 174
Cdd:cd16282  125 TLDLGGR-TVELIHLGPAHTPGDLVVWLPEEG----VLFAGDL 162
YtnP-like_MBL-fold cd07728
Bacillus subtilis YtnP and related proteins; MBL-fold metallo hydrolase domain; Bacillus ...
 18-181 1.65e-03

Bacillus subtilis YtnP and related proteins; MBL-fold metallo hydrolase domain; Bacillus subtilis YtnP inhibits the signaling pathway required for the streptomycin production and development of aerial mycelium in Streptomyces griseus. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293814  Cd Length: 249  Bit Score: 39.93  E-value: 1.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034  18 LLESLGYKILIDCG---SDFSDRHKVLTG--------------GLFPfeaSEIDLVILTHAHVDHSGNIPALirAGyrGQ 80
Cdd:cd07728   47 LIQYQGKNYLIDAGignGKLTEKQKRNFGvteessieeslaelGLTP---EDIDYVLMTHLHFDHASGLTKV--KG--EQ 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034  81 ILSTAPTAELsellfadsaYIQRAEKK--IANSAPSDYSYKPvDRFIPIA-----FNKDFELNERITVRLTPvGHILGAA 153
Cdd:cd07728  120 LVSVFPNATI---------YVSEIEWEemRNPNIRSKNTYWK-ENWEPIEdqvktFSDEIEIVPGITMIHTG-GHSDGHS 188

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 499906034 154 svFVKVEEEGktKTILFSGDV-------------GRDNYPL 181
Cdd:cd07728  189 --IIEIEQGG--ETAIHMADLmpthahqnplwvlAYDDYPM 225
EVM-1-like_MBL-B3 cd16315
Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 48-170 1.97e-03

Erythrobacter vulgaris EVM-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 EVM-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: 293873 [Multi-domain]  Cd Length: 248  Bit Score: 39.64  E-value: 1.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034  48 FEASEIDLVILTHAHVDHSGNIPALIRA-GYRgqILSTAPTAELSELLFADSAYIQRAEkkIANSAPSdysykPVDRFI- 125
Cdd:cd16315   56 FDPKDVRWLLSSHEHFDHVGGLAALQRAtGAR--VAASAAAAPVLESGKPAPDDPQAGL--HEPFPPV-----RVDRIVe 126

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 499906034 126 ---PIAFNkdfelNERITVRLTPvGHILGAASVFVKVEEEGKTKTILF 170
Cdd:cd16315  127 dgdTVALG-----SLRLTAHATP-GHTPGALSWTWRSCEGADCRTIVY 168
GOB1-like_MBL-B3 cd16308
Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; ...
 15-193 1.98e-03

Elizabethkingia meningoseptica GOB-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 GOB-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: 293866 [Multi-domain]  Cd Length: 254  Bit Score: 39.76  E-value: 1.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034  15 SMYLLESLGYKILIDCGSDFSD---RHKVLTGGlfpFEASEIDLVILTHAHVDHSGNIPALIRagyrgqilstaptaELS 91
Cdd:cd16308   23 ACYLIVTPKGNILINTGLAESVpliKKNIQALG---FKFKDIKILLTTQAHYDHVGAMAAIKQ--------------QTG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034  92 ELLFADSAyiqrAEKKIANSAPSDY-------SYKPV--DRFIpiafnKDFEL----NERITVRLTPvGHILGAASVFVK 158
Cdd:cd16308   86 AKMMVDEK----DAKVLADGGKSDYemggygsTFAPVkaDKLL-----HDGDTiklgGTKLTLLHHP-GHTKGSCSFLFD 155

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 499906034 159 VEEEGKTKTILFSgdvgrdNYP-LLPDPEQSPQADY 193
Cdd:cd16308  156 VKDEKRTYRVLIA------NMPtILPDTKLSGMPGY 185
Lactamase_B_6 pfam16661
Metallo-beta-lactamase superfamily domain; This family is part of the metallo-beta-lactamase ...
 18-90 2.37e-03

Metallo-beta-lactamase superfamily domain; This family is part of the metallo-beta-lactamase superfamily.


Pssm-ID: 406948  Cd Length: 192  Bit Score: 39.12  E-value: 2.37e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499906034   18 LLESLGYKILIDCGSDFSDRHKVLTGGLfPFEASEIDLVILTHAHVDHSGNIPALIRAGY-----RGQILSTAPTAEL 90
Cdd:pfam16661   1 LLEFDNVRILLDPGWDGSFSYESDLKYL-EKILPEVDLILLSHPTLEHLGAYPLLYYKFGshlgsNIPVYATLPVANL 77
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 17-187 3.00e-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: 38.87  E-value: 3.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034  17 YLLESLGYK--ILIDCGSDFSDRHKVL-TGGLfpfeasEIDLVILTHAHVDHSGNIPALIRagyrgqilstAPTAELsel 93
Cdd:cd16322   14 YLVADEGGGeaVLVDPGDESEKLLARFgTTGL------TLLYILLTHAHFDHVGGVADLRR----------HPGAPV--- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034  94 lfadsaYIQRAEKKIANSAP--SDYSYKPVDRFIPIafnkDFELNERITVRL---------TPvGHILGaaSVFVKVEEE 162
Cdd:cd16322   75 ------YLHPDDLPLYEAADlgAKAFGLGIEPLPPP----DRLLEDGQTLTLgglefkvlhTP-GHSPG--HVCFYVEEE 141

                        170       180       190
                 ....*....|....*....|....*....|.
gi 499906034 163 GktktILFSGD------VGRDNYPlLPDPEQ 187
Cdd:cd16322  142 G----LLFSGDllfqgsIGRTDLP-GGDPKA 167
DdPDE5-like_MBL-fold cd07738
Dictyostelium discoideum phosphodiesterase 5 and related proteins; MBL-fold metallo hydrolase ...
 53-173 3.55e-03

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


Pssm-ID: 293824  Cd Length: 189  Bit Score: 38.43  E-value: 3.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499906034  53 IDLVILTHAHVDHSGNIPALIRAGYRGQILSTAPTAE-----LSELLFADSAYIQRAekkiansapsdYSYKPVDRFIPI 127
Cdd:cd07738   49 VDHVILTHCHADHDAGTFQKILEEEKITLYTTRTINEsflrkYAALTGLPPDFLEEL-----------FDFRPVIIGEKT 117

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 499906034 128 AFNK-DFELNERItvrltpvgHILgaASVFVKVEEEGktKTILFSGD 173
Cdd:cd07738  118 KINGaEFEFDYSF--------HSI--PTIRFKVSYGG--KSIAYSGD 152
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 4-72 6.09e-03

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


Pssm-ID: 293836 [Multi-domain]  Cd Length: 185  Bit Score: 37.86  E-value: 6.09e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499906034   4 TFWGaarkvTGSmYLLESLGYKILIDCGSDfSDRH-----KVLTGGlfpfeasEIDLVILTHAHVDHSGNIPAL 72
Cdd:cd16278   14 TLDG-----TNT-YLLGAPDGVVVIDPGPD-DPAHldallAALGGG-------RVSAILVTHTHRDHSPGAARL 73
 
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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