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Conserved domains on  [gi|564345310|ref|XP_006235972|]
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N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D isoform X2 [Rattus norvegicus]

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; ...
 137-324 5.24e-93

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: 277.24  E-value: 5.24e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345310 137 WLGHATLMVEMDELILLTDPMFSSRASPSQYMGPKRFRRPPCTISELPPIDAVLISHNHYDHLDYGSVLALNERFGselr 216
Cdd:cd16283    1 WIGHATFLIQIEGLNILTDPVFSERASPVSFGGPKRLTPPGLPLEELPPIDAVLISHNHYDHLDLPTVKRLGGRPP---- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345310 217 WFVPLGLLDWMQKCGCENVIELDWWEENcvpGHDKVTFVFTPSQHWCKRTLLDDNKVLWGSWSVLGPWNRFFFAGDTGYC 296
Cdd:cd16283   77 YLVPLGLKKWFLKKGITNVVELDWWQST---EIGGVRITFVPAQHWSRRTLFDTNESLWGGWVIEGEGFRIYFAGDTGYF 153

                        170       180
                 ....*....|....*....|....*...
gi 564345310 297 PAFEEIGKRFGPFDLAAIPIGAYEPRWF 324
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; ...
 137-324 5.24e-93

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: 277.24  E-value: 5.24e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345310 137 WLGHATLMVEMDELILLTDPMFSSRASPSQYMGPKRFRRPPCTISELPPIDAVLISHNHYDHLDYGSVLALNERFGselr 216
Cdd:cd16283    1 WIGHATFLIQIEGLNILTDPVFSERASPVSFGGPKRLTPPGLPLEELPPIDAVLISHNHYDHLDLPTVKRLGGRPP---- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345310 217 WFVPLGLLDWMQKCGCENVIELDWWEENcvpGHDKVTFVFTPSQHWCKRTLLDDNKVLWGSWSVLGPWNRFFFAGDTGYC 296
Cdd:cd16283   77 YLVPLGLKKWFLKKGITNVVELDWWQST---EIGGVRITFVPAQHWSRRTLFDTNESLWGGWVIEGEGFRIYFAGDTGYF 153

                        170       180
                 ....*....|....*....|....*...
gi 564345310 297 PAFEEIGKRFGPFDLAAIPIGAYEPRWF 324
Cdd:cd16283  154 PGFREIGRRFGPIDLALLPIGAYEPRWF 181
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 130-379 5.31e-76

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 235.20  E-value: 5.31e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345310 130 EAGLRVTWLGHATLMVEMDELILLTDPMFSSRASPsqymgpkrFRRPPCTISELPPIDAVLISHNHYDHLDYGSVLALNE 209
Cdd:COG2220    1 PGGMKITWLGHATFLIETGGKRILIDPVFSGRASP--------VNPLPLDPEDLPKIDAVLVTHDHYDHLDDATLRALKR 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345310 210 RFgseLRWFVPLGLLDWMQKCGCENVIELDWWEENCVPGhdkVTFVFTPSQHWCKRtlLDDNKVLWGSWSVLGPWNRFFF 289
Cdd:COG2220   73 TG---ATVVAPLGVAAWLRAWGFPRVTELDWGESVELGG---LTVTAVPARHSSGR--PDRNGGLWVGFVIETDGKTIYH 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345310 290 AGDTGYCPAFEEIGKRFgPFDLAAIPIGAYeprwfmkYQHADPEDAVRIHIDVQAKRSVAIHWGTFALANEhylEPPVKL 369
Cdd:COG2220  145 AGDTGYFPEMKEIGERF-PIDVALLPIGAY-------PFTMGPEEAAEAARDLKPKVVIPIHYGTFPLLDE---DPLERF 213

                        250
                 ....*....|
gi 564345310 370 NEALERYGLK 379
Cdd:COG2220  214 AAALAAAGVR 223
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 152-352 5.43e-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: 146.30  E-value: 5.43e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345310  152 LLTDPMFSSRaspsqymGPKRFRRPPCTISElPPIDAVLISHNHYDHLdyGSVLALneRFGSELRWFVPLGLLDWMQKCG 231
Cdd:pfam12706   3 ILIDPGPDLR-------QQALPALQPGRLRD-DPIDAVLLTHDHYDHL--AGLLDL--REGRPRPLYAPLGVLAHLRRNF 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345310  232 C---------ENVIELDWWEENCVPGHDkVTFVFTPSQHWCKRtLLDDNKVLWGSWSVLGPWNRFFFAGDTGYCPafEEI 302
Cdd:pfam12706  71 PylfllehygVRVHEIDWGESFTVGDGG-LTVTATPARHGSPR-GLDPNPGDTLGFRIEGPGKRVYYAGDTGYFP--DEI 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 564345310  303 GKRFGPFDLAAIPIGAYEPRWFMKYQHADPEDAVRIHIDVQAKRSVAIHW 352
Cdd:pfam12706 147 GERLGGADLLLLDGGAWRDDEMIHMGHMTPEEAVEAAADLGARRKVLIHI 196
PRK00685 PRK00685
metal-dependent hydrolase; Provisional
 133-391 3.34e-14

metal-dependent hydrolase; Provisional


Pssm-ID: 234811 [Multi-domain]  Cd Length: 228  Bit Score: 71.38  E-value: 3.34e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345310 133 LRVTWLGHATLMVEMDELILLTDPMFSSRASpsqymgpkrfrrPPCTISELPPiDAVLISHNHYDHLdyGSVLALNERFG 212
Cdd:PRK00685   1 MKITWLGHSAFLIETGGKKILIDPFITGNPL------------ADLKPEDVKV-DYILLTHGHGDHL--GDTVEIAKRTG 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345310 213 SELrwFVPLGLLDWMQKCGCENVIeldwweencvPGH-------DKVTFVFTPSQHWCKRTlLDDNKVLWGSWS---VLG 282
Cdd:PRK00685  66 ATV--IANAELANYLSEKGVEKTH----------PMNiggtvefDGGKVKLTPALHSSSFI-DEDGITYLGNPTgfvITF 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345310 283 PWNRFFFAGDTGYCPAFEEIGKRFGPfDLAAIPIGAyepRWFMkyqhaDPEDAVRIHIDVQAKRSVAIHWGTFalanehy 362
Cdd:PRK00685 133 EGKTIYHAGDTGLFSDMKLIGELHKP-DVALLPIGD---NFTM-----GPEDAALAVELIKPKIVIPMHYNTF------- 196

                        250       260       270
                 ....*....|....*....|....*....|....
gi 564345310 363 lePPVKLN-----EALERYGLKSedfFILKHGES 391
Cdd:PRK00685 197 --PLIEQDpekfkALVEGLGTKV---VILKPGES 225
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 183-312 8.45e-04

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: 39.84  E-value: 8.45e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345310   183 LPPIDAVLISHNHYDHldYGSVLALNERFGseLRWFVPLGLLDWMQKCGCENVIELDWWEENCVP-----------GHDK 251
Cdd:smart00849  33 PKKIDAIILTHGHPDH--IGGLPELLEAPG--APVYAPEGTAELLKDLLALLGELGAEAEPAPPDrtlkdgdeldlGGGE 108

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564345310   252 VTFVFTPSqHW----CkrTLLDDNKVLwgswsvlgpwnrffFAGDTGYCPAFEEIGKRFGPFDLA 312
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; ...
 137-324 5.24e-93

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: 277.24  E-value: 5.24e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345310 137 WLGHATLMVEMDELILLTDPMFSSRASPSQYMGPKRFRRPPCTISELPPIDAVLISHNHYDHLDYGSVLALNERFGselr 216
Cdd:cd16283    1 WIGHATFLIQIEGLNILTDPVFSERASPVSFGGPKRLTPPGLPLEELPPIDAVLISHNHYDHLDLPTVKRLGGRPP---- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345310 217 WFVPLGLLDWMQKCGCENVIELDWWEENcvpGHDKVTFVFTPSQHWCKRTLLDDNKVLWGSWSVLGPWNRFFFAGDTGYC 296
Cdd:cd16283   77 YLVPLGLKKWFLKKGITNVVELDWWQST---EIGGVRITFVPAQHWSRRTLFDTNESLWGGWVIEGEGFRIYFAGDTGYF 153

                        170       180
                 ....*....|....*....|....*...
gi 564345310 297 PAFEEIGKRFGPFDLAAIPIGAYEPRWF 324
Cdd:cd16283  154 PGFREIGRRFGPIDLALLPIGAYEPRWF 181
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 130-379 5.31e-76

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 235.20  E-value: 5.31e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345310 130 EAGLRVTWLGHATLMVEMDELILLTDPMFSSRASPsqymgpkrFRRPPCTISELPPIDAVLISHNHYDHLDYGSVLALNE 209
Cdd:COG2220    1 PGGMKITWLGHATFLIETGGKRILIDPVFSGRASP--------VNPLPLDPEDLPKIDAVLVTHDHYDHLDDATLRALKR 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345310 210 RFgseLRWFVPLGLLDWMQKCGCENVIELDWWEENCVPGhdkVTFVFTPSQHWCKRtlLDDNKVLWGSWSVLGPWNRFFF 289
Cdd:COG2220   73 TG---ATVVAPLGVAAWLRAWGFPRVTELDWGESVELGG---LTVTAVPARHSSGR--PDRNGGLWVGFVIETDGKTIYH 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345310 290 AGDTGYCPAFEEIGKRFgPFDLAAIPIGAYeprwfmkYQHADPEDAVRIHIDVQAKRSVAIHWGTFALANEhylEPPVKL 369
Cdd:COG2220  145 AGDTGYFPEMKEIGERF-PIDVALLPIGAY-------PFTMGPEEAAEAARDLKPKVVIPIHYGTFPLLDE---DPLERF 213

                        250
                 ....*....|
gi 564345310 370 NEALERYGLK 379
Cdd:COG2220  214 AAALAAAGVR 223
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 152-352 5.43e-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: 146.30  E-value: 5.43e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345310  152 LLTDPMFSSRaspsqymGPKRFRRPPCTISElPPIDAVLISHNHYDHLdyGSVLALneRFGSELRWFVPLGLLDWMQKCG 231
Cdd:pfam12706   3 ILIDPGPDLR-------QQALPALQPGRLRD-DPIDAVLLTHDHYDHL--AGLLDL--REGRPRPLYAPLGVLAHLRRNF 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345310  232 C---------ENVIELDWWEENCVPGHDkVTFVFTPSQHWCKRtLLDDNKVLWGSWSVLGPWNRFFFAGDTGYCPafEEI 302
Cdd:pfam12706  71 PylfllehygVRVHEIDWGESFTVGDGG-LTVTATPARHGSPR-GLDPNPGDTLGFRIEGPGKRVYYAGDTGYFP--DEI 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 564345310  303 GKRFGPFDLAAIPIGAYEPRWFMKYQHADPEDAVRIHIDVQAKRSVAIHW 352
Cdd:pfam12706 147 GERLGGADLLLLDGGAWRDDEMIHMGHMTPEEAVEAAADLGARRKVLIHI 196
PRK00685 PRK00685
metal-dependent hydrolase; Provisional
 133-391 3.34e-14

metal-dependent hydrolase; Provisional


Pssm-ID: 234811 [Multi-domain]  Cd Length: 228  Bit Score: 71.38  E-value: 3.34e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345310 133 LRVTWLGHATLMVEMDELILLTDPMFSSRASpsqymgpkrfrrPPCTISELPPiDAVLISHNHYDHLdyGSVLALNERFG 212
Cdd:PRK00685   1 MKITWLGHSAFLIETGGKKILIDPFITGNPL------------ADLKPEDVKV-DYILLTHGHGDHL--GDTVEIAKRTG 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345310 213 SELrwFVPLGLLDWMQKCGCENVIeldwweencvPGH-------DKVTFVFTPSQHWCKRTlLDDNKVLWGSWS---VLG 282
Cdd:PRK00685  66 ATV--IANAELANYLSEKGVEKTH----------PMNiggtvefDGGKVKLTPALHSSSFI-DEDGITYLGNPTgfvITF 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345310 283 PWNRFFFAGDTGYCPAFEEIGKRFGPfDLAAIPIGAyepRWFMkyqhaDPEDAVRIHIDVQAKRSVAIHWGTFalanehy 362
Cdd:PRK00685 133 EGKTIYHAGDTGLFSDMKLIGELHKP-DVALLPIGD---NFTM-----GPEDAALAVELIKPKIVIPMHYNTF------- 196

                        250       260       270
                 ....*....|....*....|....*....|....
gi 564345310 363 lePPVKLN-----EALERYGLKSedfFILKHGES 391
Cdd:PRK00685 197 --PLIEQDpekfkALVEGLGTKV---VILKPGES 225
Lactamase_B_3 pfam13483
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 134-198 9.96e-09

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: 54.13  E-value: 9.96e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564345310  134 RVTWLGHATLMVEMDELILLTDPMFSSraspsqymgpKRFRRPPctiselPPIDAVLISHNHYDH 198
Cdd:pfam13483   1 EITWLGHSSFLIEGGGARILTDPFRAT----------VGYRPPP------VTADLVLISHGHDDH 49
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 183-312 8.45e-04

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: 39.84  E-value: 8.45e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345310   183 LPPIDAVLISHNHYDHldYGSVLALNERFGseLRWFVPLGLLDWMQKCGCENVIELDWWEENCVP-----------GHDK 251
Cdd:smart00849  33 PKKIDAIILTHGHPDH--IGGLPELLEAPG--APVYAPEGTAELLKDLLALLGELGAEAEPAPPDrtlkdgdeldlGGGE 108

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564345310   252 VTFVFTPSqHW----CkrTLLDDNKVLwgswsvlgpwnrffFAGDTGYCPAFEEIGKRFGPFDLA 312
Cdd:smart00849 109 LEVIHTPG-HTpgsiV--LYLPEGKIL--------------FTGDLLFAGGDGRTLVDGGDAAAS 156
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 186-304 1.02e-03

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: 39.73  E-value: 1.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345310 186 IDAVLISHNHYDH-LD-----YGSVLALNERFGSELRWFVPLGLLDWMQK-CGCENVIELDWWEENCVPGHDKVTFVFTP 258
Cdd:cd07716   51 LDAVVLSHLHPDHcADlgvlqYARRYHPRGARKPPLPLYGPAGPAERLAAlYGLEDVFDFHPIEPGEPLEIGPFTITFFR 130

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 564345310 259 SQHWCK----RtLLDDNKVlwgswsvlgpwnrFFFAGDTGYCPAFEEIGK 304
Cdd:cd07716  131 TVHPVPcyamR-IEDGGKV-------------LVYTGDTGYCDELVEFAR 166
 
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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