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Conserved domains on  [gi|26348849|dbj|BAC38064|]
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unnamed protein product [Mus musculus]

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; ...
 129-316 1.47e-92

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: 275.70  E-value: 1.47e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26348849 129 WLGHATLMVEMDELIFLTDPMFSSRASPSQYMGPKRFRRPPCTISELPTIDAVLISHNHYDHLDYGSVLALNERFGselr 208
Cdd:cd16283   1 WIGHATFLIQIEGLNILTDPVFSERASPVSFGGPKRLTPPGLPLEELPPIDAVLISHNHYDHLDLPTVKRLGGRPP---- 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26348849 209 WFVPLGLLDWMQKCGCENVIELDWWEENcvpGHDKVTFVFTPSQHWCKRTLLDDNKVLWGSWSVLGPWSRFFFAGDTGYC 288
Cdd:cd16283  77 YLVPLGLKKWFLKKGITNVVELDWWQST---EIGGVRITFVPAQHWSRRTLFDTNESLWGGWVIEGEGFRIYFAGDTGYF 153

                       170       180
                ....*....|....*....|....*...
gi 26348849 289 PAFEEIGKRFGPFDLAAIPIGAYEPRWF 316
Cdd:cd16283 154 PGFREIGRRFGPIDLALLPIGAYEPRWF 181
 
Name Accession Description Interval E-value
RomA-like_MBL-fold cd16283
Enterobacter cloacae RomA and related proteins; MBL-fold metallo hydrolase domain; ...
 129-316 1.47e-92

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: 275.70  E-value: 1.47e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26348849 129 WLGHATLMVEMDELIFLTDPMFSSRASPSQYMGPKRFRRPPCTISELPTIDAVLISHNHYDHLDYGSVLALNERFGselr 208
Cdd:cd16283   1 WIGHATFLIQIEGLNILTDPVFSERASPVSFGGPKRLTPPGLPLEELPPIDAVLISHNHYDHLDLPTVKRLGGRPP---- 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26348849 209 WFVPLGLLDWMQKCGCENVIELDWWEENcvpGHDKVTFVFTPSQHWCKRTLLDDNKVLWGSWSVLGPWSRFFFAGDTGYC 288
Cdd:cd16283  77 YLVPLGLKKWFLKKGITNVVELDWWQST---EIGGVRITFVPAQHWSRRTLFDTNESLWGGWVIEGEGFRIYFAGDTGYF 153

                       170       180
                ....*....|....*....|....*...
gi 26348849 289 PAFEEIGKRFGPFDLAAIPIGAYEPRWF 316
Cdd:cd16283 154 PGFREIGRRFGPIDLALLPIGAYEPRWF 181
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 122-369 9.11e-75

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 231.73  E-value: 9.11e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26348849 122 EAGLRVTWLGHATLMVEMDELIFLTDPMFSSRASPsqymgpkrFRRPPCTISELPTIDAVLISHNHYDHLDYGSVLALNE 201
Cdd:COG2220   1 PGGMKITWLGHATFLIETGGKRILIDPVFSGRASP--------VNPLPLDPEDLPKIDAVLVTHDHYDHLDDATLRALKR 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26348849 202 RFgseLRWFVPLGLLDWMQKCGCENVIELDWWEENCVPGhdkVTFVFTPSQHWCKRtlLDDNKVLWGSWSVLGPWSRFFF 281
Cdd:COG2220  73 TG---ATVVAPLGVAAWLRAWGFPRVTELDWGESVELGG---LTVTAVPARHSSGR--PDRNGGLWVGFVIETDGKTIYH 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26348849 282 AGDTGYCPAFEEIGKRFgPFDLAAIPIGAYeprwfmkYQHADPEDAVRIHIDLQTKRSVAIHWGTFALANEhylEPPVKL 361
Cdd:COG2220 145 AGDTGYFPEMKEIGERF-PIDVALLPIGAY-------PFTMGPEEAAEAARDLKPKVVIPIHYGTFPLLDE---DPLERF 213


                ....*...
gi 26348849 362 NEALERYG 369
Cdd:COG2220 214 AAALAAAG 221
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 144-344 8.08e-42

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: 145.53  E-value: 8.08e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26348849   144 FLTDPMFSSRaspsqymGPKRFRRPPCTISELPtIDAVLISHNHYDHLdyGSVLALneRFGSELRWFVPLGLLDWMQKCG 223
Cdd:pfam12706   3 ILIDPGPDLR-------QQALPALQPGRLRDDP-IDAVLLTHDHYDHL--AGLLDL--REGRPRPLYAPLGVLAHLRRNF 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26348849   224 C---------ENVIELDWWEENCVPGHDkVTFVFTPSQHWCKRtLLDDNKVLWGSWSVLGPWSRFFFAGDTGYCPafEEI 294
Cdd:pfam12706  71 PylfllehygVRVHEIDWGESFTVGDGG-LTVTATPARHGSPR-GLDPNPGDTLGFRIEGPGKRVYYAGDTGYFP--DEI 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 26348849   295 GKRFGPFDLAAIPIGAYEPRWFMKYQHADPEDAVRIHIDLQTKRSVAIHW 344
Cdd:pfam12706 147 GERLGGADLLLLDGGAWRDDEMIHMGHMTPEEAVEAAADLGARRKVLIHI 196
PRK00685 PRK00685
metal-dependent hydrolase; Provisional
 125-383 4.47e-14

metal-dependent hydrolase; Provisional


Pssm-ID: 234811 [Multi-domain]  Cd Length: 228  Bit Score: 71.00  E-value: 4.47e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26348849  125 LRVTWLGHATLMVEMDELIFLTDPMFSSRASpsqymgpkrfrrPPCTISELpTIDAVLISHNHYDHLdyGSVLALNERFG 204
Cdd:PRK00685   1 MKITWLGHSAFLIETGGKKILIDPFITGNPL------------ADLKPEDV-KVDYILLTHGHGDHL--GDTVEIAKRTG 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26348849  205 SELrwFVPLGLLDWMQKCGCENVIeldwweencvPGH-------DKVTFVFTPSQHWCKRTlLDDNKVLWGSWS---VLG 274
Cdd:PRK00685  66 ATV--IANAELANYLSEKGVEKTH----------PMNiggtvefDGGKVKLTPALHSSSFI-DEDGITYLGNPTgfvITF 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26348849  275 PWSRFFFAGDTGYCPAFEEIGKRFGPfDLAAIPIGAyepRWFMkyqhaDPEDAVRIHIDLQTKRSVAIHWGTFalanehy 354
Cdd:PRK00685 133 EGKTIYHAGDTGLFSDMKLIGELHKP-DVALLPIGD---NFTM-----GPEDAALAVELIKPKIVIPMHYNTF------- 196

                        250       260       270
                 ....*....|....*....|....*....|....
gi 26348849  355 lePPVKLN-----EALERYGLSCedfFILKHGES 383
Cdd:PRK00685 197 --PLIEQDpekfkALVEGLGTKV---VILKPGES 225
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 175-304 1.33e-03

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: 39.46  E-value: 1.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26348849    175 LPTIDAVLISHNHYDHldYGSVLALNERFGseLRWFVPLGLLDWMQKCGCENVIELDWWEENCVP-----------GHDK 243
Cdd:smart00849  33 PKKIDAIILTHGHPDH--IGGLPELLEAPG--APVYAPEGTAELLKDLLALLGELGAEAEPAPPDrtlkdgdeldlGGGE 108

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26348849    244 VTFVFTPSqHW----CkrTLLDDNKVLwgswsvlgpwsrffFAGDTGYCPAFEEIGKRFGPFDLA 304
Cdd:smart00849 109 LEVIHTPG-HTpgsiV--LYLPEGKIL--------------FTGDLLFAGGDGRTLVDGGDAAAS 156
 
Name Accession Description Interval E-value
RomA-like_MBL-fold cd16283
Enterobacter cloacae RomA and related proteins; MBL-fold metallo hydrolase domain; ...
 129-316 1.47e-92

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: 275.70  E-value: 1.47e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26348849 129 WLGHATLMVEMDELIFLTDPMFSSRASPSQYMGPKRFRRPPCTISELPTIDAVLISHNHYDHLDYGSVLALNERFGselr 208
Cdd:cd16283   1 WIGHATFLIQIEGLNILTDPVFSERASPVSFGGPKRLTPPGLPLEELPPIDAVLISHNHYDHLDLPTVKRLGGRPP---- 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26348849 209 WFVPLGLLDWMQKCGCENVIELDWWEENcvpGHDKVTFVFTPSQHWCKRTLLDDNKVLWGSWSVLGPWSRFFFAGDTGYC 288
Cdd:cd16283  77 YLVPLGLKKWFLKKGITNVVELDWWQST---EIGGVRITFVPAQHWSRRTLFDTNESLWGGWVIEGEGFRIYFAGDTGYF 153

                       170       180
                ....*....|....*....|....*...
gi 26348849 289 PAFEEIGKRFGPFDLAAIPIGAYEPRWF 316
Cdd:cd16283 154 PGFREIGRRFGPIDLALLPIGAYEPRWF 181
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 122-369 9.11e-75

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 231.73  E-value: 9.11e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26348849 122 EAGLRVTWLGHATLMVEMDELIFLTDPMFSSRASPsqymgpkrFRRPPCTISELPTIDAVLISHNHYDHLDYGSVLALNE 201
Cdd:COG2220   1 PGGMKITWLGHATFLIETGGKRILIDPVFSGRASP--------VNPLPLDPEDLPKIDAVLVTHDHYDHLDDATLRALKR 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26348849 202 RFgseLRWFVPLGLLDWMQKCGCENVIELDWWEENCVPGhdkVTFVFTPSQHWCKRtlLDDNKVLWGSWSVLGPWSRFFF 281
Cdd:COG2220  73 TG---ATVVAPLGVAAWLRAWGFPRVTELDWGESVELGG---LTVTAVPARHSSGR--PDRNGGLWVGFVIETDGKTIYH 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26348849 282 AGDTGYCPAFEEIGKRFgPFDLAAIPIGAYeprwfmkYQHADPEDAVRIHIDLQTKRSVAIHWGTFALANEhylEPPVKL 361
Cdd:COG2220 145 AGDTGYFPEMKEIGERF-PIDVALLPIGAY-------PFTMGPEEAAEAARDLKPKVVIPIHYGTFPLLDE---DPLERF 213


                ....*...
gi 26348849 362 NEALERYG 369
Cdd:COG2220 214 AAALAAAG 221
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 144-344 8.08e-42

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: 145.53  E-value: 8.08e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26348849   144 FLTDPMFSSRaspsqymGPKRFRRPPCTISELPtIDAVLISHNHYDHLdyGSVLALneRFGSELRWFVPLGLLDWMQKCG 223
Cdd:pfam12706   3 ILIDPGPDLR-------QQALPALQPGRLRDDP-IDAVLLTHDHYDHL--AGLLDL--REGRPRPLYAPLGVLAHLRRNF 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26348849   224 C---------ENVIELDWWEENCVPGHDkVTFVFTPSQHWCKRtLLDDNKVLWGSWSVLGPWSRFFFAGDTGYCPafEEI 294
Cdd:pfam12706  71 PylfllehygVRVHEIDWGESFTVGDGG-LTVTATPARHGSPR-GLDPNPGDTLGFRIEGPGKRVYYAGDTGYFP--DEI 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 26348849   295 GKRFGPFDLAAIPIGAYEPRWFMKYQHADPEDAVRIHIDLQTKRSVAIHW 344
Cdd:pfam12706 147 GERLGGADLLLLDGGAWRDDEMIHMGHMTPEEAVEAAADLGARRKVLIHI 196
PRK00685 PRK00685
metal-dependent hydrolase; Provisional
 125-383 4.47e-14

metal-dependent hydrolase; Provisional


Pssm-ID: 234811 [Multi-domain]  Cd Length: 228  Bit Score: 71.00  E-value: 4.47e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26348849  125 LRVTWLGHATLMVEMDELIFLTDPMFSSRASpsqymgpkrfrrPPCTISELpTIDAVLISHNHYDHLdyGSVLALNERFG 204
Cdd:PRK00685   1 MKITWLGHSAFLIETGGKKILIDPFITGNPL------------ADLKPEDV-KVDYILLTHGHGDHL--GDTVEIAKRTG 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26348849  205 SELrwFVPLGLLDWMQKCGCENVIeldwweencvPGH-------DKVTFVFTPSQHWCKRTlLDDNKVLWGSWS---VLG 274
Cdd:PRK00685  66 ATV--IANAELANYLSEKGVEKTH----------PMNiggtvefDGGKVKLTPALHSSSFI-DEDGITYLGNPTgfvITF 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26348849  275 PWSRFFFAGDTGYCPAFEEIGKRFGPfDLAAIPIGAyepRWFMkyqhaDPEDAVRIHIDLQTKRSVAIHWGTFalanehy 354
Cdd:PRK00685 133 EGKTIYHAGDTGLFSDMKLIGELHKP-DVALLPIGD---NFTM-----GPEDAALAVELIKPKIVIPMHYNTF------- 196

                        250       260       270
                 ....*....|....*....|....*....|....
gi 26348849  355 lePPVKLN-----EALERYGLSCedfFILKHGES 383
Cdd:PRK00685 197 --PLIEQDpekfkALVEGLGTKV---VILKPGES 225
Lactamase_B_3 pfam13483
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 126-190 2.65e-08

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: 52.98  E-value: 2.65e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26348849   126 RVTWLGHATLMVEMDELIFLTDPMFSSraspsqymgpKRFRRPPctiselPTIDAVLISHNHYDH 190
Cdd:pfam13483   1 EITWLGHSSFLIEGGGARILTDPFRAT----------VGYRPPP------VTADLVLISHGHDDH 49
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 175-296 4.05e-04

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: 40.89  E-value: 4.05e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26348849 175 LPTIDAVLISHNHYDH-LD-----YGSVLALNERFGSELRWFVPLGLLDWMQK-CGCENVIELDWWEENCVPGHDKVTFV 247
Cdd:cd07716  48 PEDLDAVVLSHLHPDHcADlgvlqYARRYHPRGARKPPLPLYGPAGPAERLAAlYGLEDVFDFHPIEPGEPLEIGPFTIT 127

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 26348849 248 FTPSQHWCK----RtLLDDNKVlwgswsvlgpwsrFFFAGDTGYCPAFEEIGK 296
Cdd:cd07716 128 FFRTVHPVPcyamR-IEDGGKV-------------LVYTGDTGYCDELVEFAR 166
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 175-304 1.33e-03

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: 39.46  E-value: 1.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26348849    175 LPTIDAVLISHNHYDHldYGSVLALNERFGseLRWFVPLGLLDWMQKCGCENVIELDWWEENCVP-----------GHDK 243
Cdd:smart00849  33 PKKIDAIILTHGHPDH--IGGLPELLEAPG--APVYAPEGTAELLKDLLALLGELGAEAEPAPPDrtlkdgdeldlGGGE 108

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26348849    244 VTFVFTPSqHW----CkrTLLDDNKVLwgswsvlgpwsrffFAGDTGYCPAFEEIGKRFGPFDLA 304
Cdd:smart00849 109 LEVIHTPG-HTpgsiV--LYLPEGKIL--------------FTGDLLFAGGDGRTLVDGGDAAAS 156
 
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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