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Conserved domains on  [gi|727185786|ref|WP_033647688|]
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MULTISPECIES: MBL fold metallo-hydrolase [Serratia]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 581040)

MBL fold metallo-hydrolase is most likely a hydrolytic enzyme

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold super family cl23716
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 75-257 3.86e-99

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.


The actual alignment was detected with superfamily member cd16283:

Pssm-ID: 451500  Cd Length: 181  Bit Score: 290.33  E-value: 3.86e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185786  75 WLGHASMLLRLGGRYILIDPVLSERASPLSFYGPKRRTPTPLTVGQLPAVDAVLISHNHYDHLDRRTVRQLARRFPqaeF 154
Cdd:cd16283    1 WIGHATFLIQIEGLNILTDPVFSERASPVSFGGPKRLTPPGLPLEELPPIDAVLISHNHYDHLDLPTVKRLGGRPP---Y 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185786 155 IVPLGLKRWFRRYRLK-VHELDWWQSLSLGELTVYATPARHWSMRTLWDRNRSLWCGWVIHHPALRFYFSGDSGYSERLA 233
Cdd:cd16283   78 LVPLGLKKWFLKKGITnVVELDWWQSTEIGGVRITFVPAQHWSRRTLFDTNESLWGGWVIEGEGFRIYFAGDTGYFPGFR 157

                        170       180
                 ....*....|....*....|....
gi 727185786 234 EIGQRLGPFDVAALPIGAYAPRWF 257
Cdd:cd16283  158 EIGRRFGPIDLALLPIGAYEPRWF 181
 
Name Accession Description Interval E-value
RomA-like_MBL-fold cd16283
Enterobacter cloacae RomA and related proteins; MBL-fold metallo hydrolase domain; ...
 75-257 3.86e-99

Enterobacter cloacae RomA and related proteins; MBL-fold metallo hydrolase domain; Derepression of the romA-ramA locus results in a multidrug-resistance phenotype. 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: 293841  Cd Length: 181  Bit Score: 290.33  E-value: 3.86e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185786  75 WLGHASMLLRLGGRYILIDPVLSERASPLSFYGPKRRTPTPLTVGQLPAVDAVLISHNHYDHLDRRTVRQLARRFPqaeF 154
Cdd:cd16283    1 WIGHATFLIQIEGLNILTDPVFSERASPVSFGGPKRLTPPGLPLEELPPIDAVLISHNHYDHLDLPTVKRLGGRPP---Y 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185786 155 IVPLGLKRWFRRYRLK-VHELDWWQSLSLGELTVYATPARHWSMRTLWDRNRSLWCGWVIHHPALRFYFSGDSGYSERLA 233
Cdd:cd16283   78 LVPLGLKKWFLKKGITnVVELDWWQSTEIGGVRITFVPAQHWSRRTLFDTNESLWGGWVIEGEGFRIYFAGDTGYFPGFR 157

                        170       180
                 ....*....|....*....|....
gi 727185786 234 EIGQRLGPFDVAALPIGAYAPRWF 257
Cdd:cd16283  158 EIGRRFGPIDLALLPIGAYEPRWF 181
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 68-310 3.74e-88

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 264.09  E-value: 3.74e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185786  68 GGDDSIWWLGHASMLLRLGGRYILIDPVLSERASPLSfygpkrrtPTPLTVGQLPAVDAVLISHNHYDHLDRRTVRQLAR 147
Cdd:COG2220    1 PGGMKITWLGHATFLIETGGKRILIDPVFSGRASPVN--------PLPLDPEDLPKIDAVLVTHDHYDHLDDATLRALKR 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185786 148 RFPQaeFIVPLGLKRWFRRYRL-KVHELDWWQSLSLGELTVYATPARHWSMRtlWDRNRSLWCGWVIHHPALRFYFSGDS 226
Cdd:COG2220   73 TGAT--VVAPLGVAAWLRAWGFpRVTELDWGESVELGGLTVTAVPARHSSGR--PDRNGGLWVGFVIETDGKTIYHAGDT 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185786 227 GYSERLAEIGQRLgPFDVAALPIGAYAprwfmqeQHMDPQQSVTLYRELNQPRAIPIHWGVFELADEsldEPPQQLNLAL 306
Cdd:COG2220  149 GYFPEMKEIGERF-PIDVALLPIGAYP-------FTMGPEEAAEAARDLKPKVVIPIHYGTFPLLDE---DPLERFAAAL 217


                 ....
gi 727185786 307 SEAG 310
Cdd:COG2220  218 AAAG 221
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 88-285 9.38e-47

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: 157.09  E-value: 9.38e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185786   88 RYILIDPVLSerasplsFYGPKRRTPTPLTVGQLPaVDAVLISHNHYDHL-DRRTVRqlarRFPQAEFIVPLG----LKR 162
Cdd:pfam12706   1 RRILIDPGPD-------LRQQALPALQPGRLRDDP-IDAVLLTHDHYDHLaGLLDLR----EGRPRPLYAPLGvlahLRR 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185786  163 WF------RRYRLKVHELDWWQSLSLGE--LTVYATPARHWSMRTLwDRNRSLWCGWVIHHPALRFYFSGDSGYSErlAE 234
Cdd:pfam12706  69 NFpylfllEHYGVRVHEIDWGESFTVGDggLTVTATPARHGSPRGL-DPNPGDTLGFRIEGPGKRVYYAGDTGYFP--DE 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 727185786  235 IGQRLGPFDVAALPIGAYAPRWFMQEQHMDPQQSVTLYRELNQPRAIPIHW 285
Cdd:pfam12706 146 IGERLGGADLLLLDGGAWRDDEMIHMGHMTPEEAVEAAADLGARRKVLIHI 196
PRK00685 PRK00685
metal-dependent hydrolase; Provisional
 73-327 4.57e-22

metal-dependent hydrolase; Provisional


Pssm-ID: 234811 [Multi-domain]  Cd Length: 228  Bit Score: 92.95  E-value: 4.57e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185786  73 IWWLGHASMLLRLGGRYILIDPVLSEraSPLSfygpkrrtptPLTVGQLpAVDAVLISHNHYDHL-DrrTVrQLARRfPQ 151
Cdd:PRK00685   3 ITWLGHSAFLIETGGKKILIDPFITG--NPLA----------DLKPEDV-KVDYILLTHGHGDHLgD--TV-EIAKR-TG 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185786 152 AEFIVPLGLKRWFRRYRL-KVHELDWWQSLSLGELTVYATPARHWSMRTLWDRNRSLW--CGWVIHHPALRFYFSGDSGY 228
Cdd:PRK00685  66 ATVIANAELANYLSEKGVeKTHPMNIGGTVEFDGGKVKLTPALHSSSFIDEDGITYLGnpTGFVITFEGKTIYHAGDTGL 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185786 229 SERLAEIGQRLGPfDVAALPIGAYaprwFMqeqhMDPQQSVtLYRELNQPR-AIPIHWGVFELadesLDEPPQQLNLALS 307
Cdd:PRK00685 146 FSDMKLIGELHKP-DVALLPIGDN----FT----MGPEDAA-LAVELIKPKiVIPMHYNTFPL----IEQDPEKFKALVE 211

                        250       260
                 ....*....|....*....|
gi 727185786 308 EAGLDqhqFHPLKIGERIAL 327
Cdd:PRK00685 212 GLGTK---VVILKPGESIEL 228
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 80-245 6.87e-07

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: 48.70  E-value: 6.87e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185786    80 SMLLRLGGRYILIDPVLSERASPLSF---YGPKRrtptpltvgqlpaVDAVLISHNHYDHLdrRTVRQLARRfPQAEFIV 156
Cdd:smart00849   2 SYLVRDDGGAILIDTGPGEAEDLLAElkkLGPKK-------------IDAIILTHGHPDHI--GGLPELLEA-PGAPVYA 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185786   157 PLGLKRWFRRYRLKVHELDWW-------------QSLSLG--ELTVYATPArHW--SMrtlwdrnrslwcgwVIHHPALR 219
Cdd:smart00849  66 PEGTAELLKDLLALLGELGAEaepappdrtlkdgDELDLGggELEVIHTPG-HTpgSI--------------VLYLPEGK 130

                          170       180
                   ....*....|....*....|....*.
gi 727185786   220 FYFSGDSGYSERLAEIGQRLGPFDVA 245
Cdd:smart00849 131 ILFTGDLLFAGGDGRTLVDGGDAAAS 156
 
Name Accession Description Interval E-value
RomA-like_MBL-fold cd16283
Enterobacter cloacae RomA and related proteins; MBL-fold metallo hydrolase domain; ...
 75-257 3.86e-99

Enterobacter cloacae RomA and related proteins; MBL-fold metallo hydrolase domain; Derepression of the romA-ramA locus results in a multidrug-resistance phenotype. 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: 293841  Cd Length: 181  Bit Score: 290.33  E-value: 3.86e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185786  75 WLGHASMLLRLGGRYILIDPVLSERASPLSFYGPKRRTPTPLTVGQLPAVDAVLISHNHYDHLDRRTVRQLARRFPqaeF 154
Cdd:cd16283    1 WIGHATFLIQIEGLNILTDPVFSERASPVSFGGPKRLTPPGLPLEELPPIDAVLISHNHYDHLDLPTVKRLGGRPP---Y 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185786 155 IVPLGLKRWFRRYRLK-VHELDWWQSLSLGELTVYATPARHWSMRTLWDRNRSLWCGWVIHHPALRFYFSGDSGYSERLA 233
Cdd:cd16283   78 LVPLGLKKWFLKKGITnVVELDWWQSTEIGGVRITFVPAQHWSRRTLFDTNESLWGGWVIEGEGFRIYFAGDTGYFPGFR 157

                        170       180
                 ....*....|....*....|....
gi 727185786 234 EIGQRLGPFDVAALPIGAYAPRWF 257
Cdd:cd16283  158 EIGRRFGPIDLALLPIGAYEPRWF 181
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 68-310 3.74e-88

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 264.09  E-value: 3.74e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185786  68 GGDDSIWWLGHASMLLRLGGRYILIDPVLSERASPLSfygpkrrtPTPLTVGQLPAVDAVLISHNHYDHLDRRTVRQLAR 147
Cdd:COG2220    1 PGGMKITWLGHATFLIETGGKRILIDPVFSGRASPVN--------PLPLDPEDLPKIDAVLVTHDHYDHLDDATLRALKR 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185786 148 RFPQaeFIVPLGLKRWFRRYRL-KVHELDWWQSLSLGELTVYATPARHWSMRtlWDRNRSLWCGWVIHHPALRFYFSGDS 226
Cdd:COG2220   73 TGAT--VVAPLGVAAWLRAWGFpRVTELDWGESVELGGLTVTAVPARHSSGR--PDRNGGLWVGFVIETDGKTIYHAGDT 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185786 227 GYSERLAEIGQRLgPFDVAALPIGAYAprwfmqeQHMDPQQSVTLYRELNQPRAIPIHWGVFELADEsldEPPQQLNLAL 306
Cdd:COG2220  149 GYFPEMKEIGERF-PIDVALLPIGAYP-------FTMGPEEAAEAARDLKPKVVIPIHYGTFPLLDE---DPLERFAAAL 217


                 ....
gi 727185786 307 SEAG 310
Cdd:COG2220  218 AAAG 221
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 88-285 9.38e-47

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: 157.09  E-value: 9.38e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185786   88 RYILIDPVLSerasplsFYGPKRRTPTPLTVGQLPaVDAVLISHNHYDHL-DRRTVRqlarRFPQAEFIVPLG----LKR 162
Cdd:pfam12706   1 RRILIDPGPD-------LRQQALPALQPGRLRDDP-IDAVLLTHDHYDHLaGLLDLR----EGRPRPLYAPLGvlahLRR 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185786  163 WF------RRYRLKVHELDWWQSLSLGE--LTVYATPARHWSMRTLwDRNRSLWCGWVIHHPALRFYFSGDSGYSErlAE 234
Cdd:pfam12706  69 NFpylfllEHYGVRVHEIDWGESFTVGDggLTVTATPARHGSPRGL-DPNPGDTLGFRIEGPGKRVYYAGDTGYFP--DE 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 727185786  235 IGQRLGPFDVAALPIGAYAPRWFMQEQHMDPQQSVTLYRELNQPRAIPIHW 285
Cdd:pfam12706 146 IGERLGGADLLLLDGGAWRDDEMIHMGHMTPEEAVEAAADLGARRKVLIHI 196
PRK00685 PRK00685
metal-dependent hydrolase; Provisional
 73-327 4.57e-22

metal-dependent hydrolase; Provisional


Pssm-ID: 234811 [Multi-domain]  Cd Length: 228  Bit Score: 92.95  E-value: 4.57e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185786  73 IWWLGHASMLLRLGGRYILIDPVLSEraSPLSfygpkrrtptPLTVGQLpAVDAVLISHNHYDHL-DrrTVrQLARRfPQ 151
Cdd:PRK00685   3 ITWLGHSAFLIETGGKKILIDPFITG--NPLA----------DLKPEDV-KVDYILLTHGHGDHLgD--TV-EIAKR-TG 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185786 152 AEFIVPLGLKRWFRRYRL-KVHELDWWQSLSLGELTVYATPARHWSMRTLWDRNRSLW--CGWVIHHPALRFYFSGDSGY 228
Cdd:PRK00685  66 ATVIANAELANYLSEKGVeKTHPMNIGGTVEFDGGKVKLTPALHSSSFIDEDGITYLGnpTGFVITFEGKTIYHAGDTGL 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185786 229 SERLAEIGQRLGPfDVAALPIGAYaprwFMqeqhMDPQQSVtLYRELNQPR-AIPIHWGVFELadesLDEPPQQLNLALS 307
Cdd:PRK00685 146 FSDMKLIGELHKP-DVALLPIGDN----FT----MGPEDAA-LAVELIKPKiVIPMHYNTFPL----IEQDPEKFKALVE 211

                        250       260
                 ....*....|....*....|
gi 727185786 308 EAGLDqhqFHPLKIGERIAL 327
Cdd:PRK00685 212 GLGTK---VVILKPGESIEL 228
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
77-284 1.16e-13

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 69.84  E-value: 1.16e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185786  77 GHASMLLRLGGRYILIDPvlserasplsfyGP-----KRRTPTPLTvgqlpAVDAVLISHNHYDH-------LDRRTVRQ 144
Cdd:COG1234   18 ATSSYLLEAGGERLLIDC------------GEgtqrqLLRAGLDPR-----DIDAIFITHLHGDHiaglpglLSTRSLAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185786 145 LARRFPqaeFIVPLGLKRWFRR----------YRLKVHELDWWQSLSLGELTVYATPARHwSMRTlwdrnrslwCGWVIH 214
Cdd:COG1234   81 REKPLT---IYGPPGTKEFLEAllkasgtdldFPLEFHEIEPGEVFEIGGFTVTAFPLDH-PVPA---------YGYRFE 147

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 727185786 215 HPALRFYFSGDSGYSERLAEIGQRLgpfDV----AALP--IGAYAPRWFmqeqHMDPQQSVTLYRELNQPRAIPIH 284
Cdd:COG1234  148 EPGRSLVYSGDTRPCEALVELAKGA---DLliheATFLdeEAELAKETG----HSTAKEAAELAAEAGVKRLVLTH 216
Lactamase_B_3 pfam13483
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 72-284 1.20e-13

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


Pssm-ID: 433247 [Multi-domain]  Cd Length: 160  Bit Score: 67.62  E-value: 1.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185786   72 SIWWLGHASMLLRLGGRYILIDPVLSEraspLSFYGPKrrtptpltvgqlPAVDAVLISHNHYDHLDRRTVRQlarrfpq 151
Cdd:pfam13483   1 EITWLGHSSFLIEGGGARILTDPFRAT----VGYRPPP------------VTADLVLISHGHDDHGHPETLPG------- 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185786  152 aefivplglkrwfrryrlKVHELDWWQSLSLGELTVYATPARHWSmrtLWDRNRSLWCGWVIHHPALRFYFSGDsGYSER 231
Cdd:pfam13483  58 ------------------NPHVLDGGGSYTVGGLEIRGVPTDHDR---VGGRRRGGNSIFLFEQDGLTIYHLGH-LGHPL 115

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 727185786  232 LAEIGQRLGPFDVAALPIGayAPRWfmqeqhMDPQQSVTLYRELNQPRAIPIH 284
Cdd:pfam13483 116 SDEQLAELGRVDVLLIPVG--GPLT------YGAEEALELAKRLRPRVVIPMH 160
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
75-244 5.89e-09

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 55.07  E-value: 5.89e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185786   75 WLGHASMLLRLGGRYILIDPVLSERASPLSFYGPKRRTPTPltvgqlpaVDAVLISHNHYDHLdrRTVRQLARRFPQAEF 154
Cdd:pfam00753   3 PGQVNSYLIEGGGGAVLIDTGGSAEAALLLLLAALGLGPKD--------IDAVILTHGHFDHI--GGLGELAEATDVPVI 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185786  155 IVPLGLKRWFRRyrlkvHELDWWQSLSLGELTVYATPARHWS---MRTLWDRNRSLW--------CGWVIHHPALRFYFS 223
Cdd:pfam00753  73 VVAEEARELLDE-----ELGLAASRLGLPGPPVVPLPPDVVLeegDGILGGGLGLLVthgpghgpGHVVVYYGGGKVLFT 147

                         170       180
                  ....*....|....*....|.
gi 727185786  224 GDSGYSERLAEIGQRLGPFDV 244
Cdd:pfam00753 148 GDLLFAGEIGRLDLPLGGLLV 168
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 77-235 1.75e-08

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


Pssm-ID: 293803 [Multi-domain]  Cd Length: 247  Bit Score: 54.38  E-value: 1.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185786  77 GHASMLLRLGGRYILIDPvlSE------RASPLSFygpkrrtptpltvgqlPAVDAVLISHNHYDH------------LD 138
Cdd:cd07717   16 NLSSIALRLEGELWLFDC--GEgtqrqlLRAGLSP----------------SKIDRIFITHLHGDHilglpgllstmsLL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185786 139 RRTvRQLarrfpqaEFIVPLGLKRWFRR----------YRLKVHELD--WWQSLSLGELTVYATPARHwsmrtlwdRNRS 206
Cdd:cd07717   78 GRT-EPL-------TIYGPKGLKEFLETllrlsasrlpYPIEVHELEpdPGLVFEDDGFTVTAFPLDH--------RVPC 141

                        170       180
                 ....*....|....*....|....*....
gi 727185786 207 LwcGWVIHHPaLRFYFSGDSGYSERLAEI 235
Cdd:cd07717  142 F--GYRFEEG-RKIAYLGDTRPCEGLVEL 167
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 79-284 3.86e-08

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 53.75  E-value: 3.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185786  79 ASMLLRLGGRYILIDpvlserASPlsfyGPKRRTP-TPLTVGQLpavDAVLISHNHYDHL-------------------D 138
Cdd:COG1235   36 SSILVEADGTRLLID------AGP----DLREQLLrLGLDPSKI---DAILLTHEHADHIaglddlrprygpnpipvyaT 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185786 139 RRTVRQLARRFPQAEFIVPlglkrwfrrYRLKVHELDWWQSLSLGELTVYATPARHwsmrtlwDRNRSLwcGWVIHHPAL 218
Cdd:COG1235  103 PGTLEALERRFPYLFAPYP---------GKLEFHEIEPGEPFEIGGLTVTPFPVPH-------DAGDPV--GYRIEDGGK 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 727185786 219 RFYFSGDSGYSErlAEIGQRLGPFDVAALPiGAY-APRWFmqeqHMDPQQSVTLYRELNQPRAIPIH 284
Cdd:COG1235  165 KLAYATDTGYIP--EEVLELLRGADLLILD-ATYdDPEPG----HLSNEEALELLARLGPKRLVLTH 224
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 79-200 8.97e-08

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: 51.71  E-value: 8.97e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185786  79 ASMLLRLGGRYILIDpvlserASPlSFYGpkrrtptpltvgQL-----PAVDAVLISHNHYDH----------------- 136
Cdd:cd16279   36 SSILIETGGKNILID------TGP-DFRQ------------QAlragiRKLDAVLLTHAHADHihglddlrpfnrlqqrp 96

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 727185786 137 ----LDRRTVRQLARRFPQAEFIvplglKRWFRRYRLKVHELDWWQSLSLGELTVYATPARHWSMRTL 200
Cdd:cd16279   97 ipvyASEETLDDLKRRFPYFFAA-----TGGGGVPKLDLHIIEPDEPFTIGGLEITPLPVLHGKLPSL 159
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 121-234 4.89e-07

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: 48.98  E-value: 4.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185786 121 LPAVDAVLISHNHYDH-LD------RRTVRQLARRFPQAEFIVPLGLKRWFRR-YRLK----VHELDWWQSLSLGELTVY 188
Cdd:cd07716   48 PEDLDAVVLSHLHPDHcADlgvlqyARRYHPRGARKPPLPLYGPAGPAERLAAlYGLEdvfdFHPIEPGEPLEIGPFTIT 127

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 727185786 189 ATPARH----WSMRtlwdrnrslwcgwvIHHPALRFYFSGDSGYSERLAE 234
Cdd:cd07716  128 FFRTVHpvpcYAMR--------------IEDGGKVLVYTGDTGYCDELVE 163
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 80-245 6.87e-07

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: 48.70  E-value: 6.87e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185786    80 SMLLRLGGRYILIDPVLSERASPLSF---YGPKRrtptpltvgqlpaVDAVLISHNHYDHLdrRTVRQLARRfPQAEFIV 156
Cdd:smart00849   2 SYLVRDDGGAILIDTGPGEAEDLLAElkkLGPKK-------------IDAIILTHGHPDHI--GGLPELLEA-PGAPVYA 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185786   157 PLGLKRWFRRYRLKVHELDWW-------------QSLSLG--ELTVYATPArHW--SMrtlwdrnrslwcgwVIHHPALR 219
Cdd:smart00849  66 PEGTAELLKDLLALLGELGAEaepappdrtlkdgDELDLGggELEVIHTPG-HTpgSI--------------VLYLPEGK 130

                          170       180
                   ....*....|....*....|....*.
gi 727185786   220 FYFSGDSGYSERLAEIGQRLGPFDVA 245
Cdd:smart00849 131 ILFTGDLLFAGGDGRTLVDGGDAAAS 156
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 77-237 7.52e-07

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: 48.80  E-value: 7.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185786  77 GHASMLLRLGGRYILIDpvlserASPLSFYGPKRRTPTPLTVgqlpavDAVLISHNHYDHldrrtV---------RQLAR 147
Cdd:cd16272   16 NTSSYLLETGGTRILLD------CGEGTVYRLLKAGVDPDKL------DAIFLSHFHLDH-----IgglptllfaRRYGG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185786 148 RFPQAEFIVPLGLKRWFRR------------YRLKVHELDWWQ-SLSLGELTVYATPARHWSMRtlwdrnrslwCGWVIH 214
Cdd:cd16272   79 RKKPLTIYGPKGIKEFLEKllnfpveilplgFPLEIEELEEGGeVLELGDLKVEAFPVKHSVES----------LGYRIE 148

                        170       180
                 ....*....|....*....|...
gi 727185786 215 HPALRFYFSGDSGYSERLAEIGQ 237
Cdd:cd16272  149 AEGKSIVYSGDTGPCENLVELAK 171
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 82-179 2.84e-04

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: 41.77  E-value: 2.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185786  82 LLRLGGRYILIDpvlserASPLSFYGPkrrtptplTVGQLPA-----------VDAVLISHNHYDHL------DRRTVrq 144
Cdd:cd07720   53 LVRTGGRLILVD------TGAGGLFGP--------TAGKLLAnlaaagidpedIDDVLLTHLHPDHIgglvdaGGKPV-- 116

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 727185786 145 larrFPQAEFIVPlglKRwfrryrlkvhELDWWQS 179
Cdd:cd07720  117 ----FPNAEVHVS---EA----------EWDFWLD 134
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 82-156 3.75e-04

quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl Homoserine Lactones (also known as AHLs) are signal molecules which coordinate gene expression in quorum sensing, in many Gram-negative bacteria. Quorum-quenching N-acyl-homoserine lactonase (also known as AHL lactonase, N-acyl-L-homoserine lactone hydrolase, EC 3.1.1.81) catalyzes the hydrolysis and opening of the homoserine lactone rings of AHLs, a reaction that can block quorum sensing. These enzymes belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293815 [Multi-domain]  Cd Length: 238  Bit Score: 41.43  E-value: 3.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185786  82 LLRLGGRYILID----PVLSERASPLSFYGPKRRTPTPLTVGQL------PA-VDAVLISHNHYDHLDRrtvrqlARRFP 150
Cdd:cd07729   36 LIEHPEGTILVDtgfhPDAADDPGGLELAFPPGVTEEQTLEEQLarlgldPEdIDYVILSHLHFDHAGG------LDLFP 109


                 ....*.
gi 727185786 151 QAEFIV 156
Cdd:cd07729  110 NATIIV 115
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 82-136 1.22e-03

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 40.56  E-value: 1.22e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 727185786  82 LLRLGGRYILIDPVLserasplsFYGPKRRTPTPLTVGqLPAVDAVLISHNHYDH 136
Cdd:COG1236   18 LLETGGTRILIDCGL--------FQGGKERNWPPFPFR-PSDVDAVVLTHAHLDH 63
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 80-239 3.49e-03

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: 38.69  E-value: 3.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185786  80 SMLLRLG-GRYILIDpvlserASPLSFYGPKRRTPTP----LTVGQLpavDAVLISHNHYDH-------LDRRTVRQLAR 147
Cdd:COG2333   13 AILIRTPdGKTILID------TGPRPSFDAGERVVLPylraLGIRRL---DLLVLTHPDADHigglaavLEAFPVGRVLV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185786 148 RFPQAEFIVPLGLKRWFRRYRLKVHELDWWQSLSLG--ELTVYATPARHWSMRTlwDRNRSLwcgwV--IHHPALRFYFS 223
Cdd:COG2333   84 SGPPDTSETYERLLEALKEKGIPVRPCRAGDTWQLGgvRFEVLWPPEDLLEGSD--ENNNSL----VlrLTYGGFSFLLT 157

                        170
                 ....*....|....*...
gi 727185786 224 GDSGYS--ERLAEIGQRL 239
Cdd:COG2333  158 GDAEAEaeAALLARGPDL 175
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 87-170 3.95e-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. Some members of this subgroup are annotated as GumP protein.


Pssm-ID: 293816 [Multi-domain]  Cd Length: 250  Bit Score: 38.40  E-value: 3.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185786  87 GRYILIDPVLSER--ASPLSFYGPKRRTPTPLTVG-----QLPA-------VDAVLISHNHYDHL-DrrtvrqlARRFPQ 151
Cdd:cd07730   33 GGKILFDLGYRKDfeEYTPRVPERLYRTPVPLEVEedvaeQLAAggidpedIDAVILSHLHWDHIgG-------LSDFPN 105

                         90
                 ....*....|....*....
gi 727185786 152 AEFIVPLGLKRWFRRYRLK 170
Cdd:cd07730  106 ARLIVGPGAKEALRPPGYP 124
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 79-136 4.85e-03

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: 37.82  E-value: 4.85e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 727185786  79 ASMLLRLGGRYILIDpvlserasplsfYG--PKRRTPTPLTVGQLP----AVDAVLISHNHYDH 136
Cdd:cd16295   13 SCYLLETGGKRILLD------------CGlfQGGKELEELNNEPFPfdpkEIDAVILTHAHLDH 64
 
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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