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Conserved domains on  [gi|1952697099|ref|XP_038310107|]
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N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D isoform X1 [Canis lupus familiaris]

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 1.56e-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: 275.31  E-value: 1.56e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952697099 129 WLGHATVLVEMDGLVLLTDPVFSPRASPWQRVGPRRFRRAPCSVAELPAVHAVVLSHNHYDHLDCGSVRALNERFGpelr 208
Cdd:cd16283     1 WIGHATFLIQIEGLNILTDPVFSERASPVSFGGPKRLTPPGLPLEELPPIDAVLISHNHYDHLDLPTVKRLGGRPP---- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952697099 209 WFVPLGLLDWMQKCGCENVIELDWWEENcvpGHDSVTFVFTPAQHWCKRTLLDDNRVLWGSWAVLGPWSRFFFAGDTGYC 288
Cdd:cd16283    77 YLVPLGLKKWFLKKGITNVVELDWWQST---EIGGVRITFVPAQHWSRRTLFDTNESLWGGWVIEGEGFRIYFAGDTGYF 153

                         170       180
                  ....*....|....*....|....*...
gi 1952697099 289 SAFEEIGRRFGPFDLAAIPIGAYEPRWF 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 1.56e-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: 275.31  E-value: 1.56e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952697099 129 WLGHATVLVEMDGLVLLTDPVFSPRASPWQRVGPRRFRRAPCSVAELPAVHAVVLSHNHYDHLDCGSVRALNERFGpelr 208
Cdd:cd16283     1 WIGHATFLIQIEGLNILTDPVFSERASPVSFGGPKRLTPPGLPLEELPPIDAVLISHNHYDHLDLPTVKRLGGRPP---- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952697099 209 WFVPLGLLDWMQKCGCENVIELDWWEENcvpGHDSVTFVFTPAQHWCKRTLLDDNRVLWGSWAVLGPWSRFFFAGDTGYC 288
Cdd:cd16283    77 YLVPLGLKKWFLKKGITNVVELDWWQST---EIGGVRITFVPAQHWSRRTLFDTNESLWGGWVIEGEGFRIYFAGDTGYF 153

                         170       180
                  ....*....|....*....|....*...
gi 1952697099 289 SAFEEIGRRFGPFDLAAIPIGAYEPRWF 316
Cdd:cd16283   154 PGFREIGRRFGPIDLALLPIGAYEPRWF 181
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 122-369 2.45e-75

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 233.27  E-value: 2.45e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952697099 122 GAGLRVTWLGHATVLVEMDGLVLLTDPVFSPRASPwqrvgprrFRRAPCSVAELPAVHAVVLSHNHYDHLDCGSVRALNE 201
Cdd:COG2220     1 PGGMKITWLGHATFLIETGGKRILIDPVFSGRASP--------VNPLPLDPEDLPKIDAVLVTHDHYDHLDDATLRALKR 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952697099 202 RFGPelrWFVPLGLLDWMQKCGCENVIELDWWEENCVPGhdsVTFVFTPAQHWCKRtlLDDNRVLWGSWAVLGPWSRFFF 281
Cdd:COG2220    73 TGAT---VVAPLGVAAWLRAWGFPRVTELDWGESVELGG---LTVTAVPARHSSGR--PDRNGGLWVGFVIETDGKTIYH 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952697099 282 AGDTGYCSAFEEIGRRFgPFDLAAIPIGAYeprwfmkYQHVDPEEAVRIHIDVQTKKSVAIHWGTFALANEhylEPPVKL 361
Cdd:COG2220   145 AGDTGYFPEMKEIGERF-PIDVALLPIGAY-------PFTMGPEEAAEAARDLKPKVVIPIHYGTFPLLDE---DPLERF 213


                  ....*...
gi 1952697099 362 SEALGRYG 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 2.40e-40

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: 141.68  E-value: 2.40e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952697099 144 LLTDPVFSPRaspwqrvGPRRFRRAPCSVAELPaVHAVVLSHNHYDHL-DCGSVRALNERfgpelRWFVPLGLLDWMQKC 222
Cdd:pfam12706   3 ILIDPGPDLR-------QQALPALQPGRLRDDP-IDAVLLTHDHYDHLaGLLDLREGRPR-----PLYAPLGVLAHLRRN 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952697099 223 GC---------ENVIELDWWEEnCVPGHDSVTFVFTPAQHWCKRtLLDDNRVLWGSWAVLGPWSRFFFAGDTGYCSafEE 293
Cdd:pfam12706  70 FPylfllehygVRVHEIDWGES-FTVGDGGLTVTATPARHGSPR-GLDPNPGDTLGFRIEGPGKRVYYAGDTGYFP--DE 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1952697099 294 IGRRFGPFDLAAIPIGAYEPRWFMKYQHVDPEEAVRIHIDVQTKKSVAIHW 344
Cdd:pfam12706 146 IGERLGGADLLLLDGGAWRDDEMIHMGHMTPEEAVEAAADLGARRKVLIHI 196
PRK00685 PRK00685
metal-dependent hydrolase; Provisional
 125-347 2.96e-16

metal-dependent hydrolase; Provisional


Pssm-ID: 234811 [Multi-domain]  Cd Length: 228  Bit Score: 77.16  E-value: 2.96e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952697099 125 LRVTWLGHATVLVEMDGLVLLTDPVFSPRASpwqrvgprrfrrAPCSVAELPAVHaVVLSHNHYDHLdcGSVRALNERFG 204
Cdd:PRK00685    1 MKITWLGHSAFLIETGGKKILIDPFITGNPL------------ADLKPEDVKVDY-ILLTHGHGDHL--GDTVEIAKRTG 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952697099 205 PELrwFVPLGLLDWMQKCGCENVIeldwweencvPGH-------DSVTFVFTPAQHwcKRTLLDDNRVLWGSWA----VL 273
Cdd:PRK00685   66 ATV--IANAELANYLSEKGVEKTH----------PMNiggtvefDGGKVKLTPALH--SSSFIDEDGITYLGNPtgfvIT 131

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952697099 274 GPWSRFFFAGDTGYCSAFEEIGRRFGPfDLAAIPIGAyepRWFMkyqhvDPEEAVRIHIDVQTKKSVAIHWGTF 347
Cdd:PRK00685  132 FEGKTIYHAGDTGLFSDMKLIGELHKP-DVALLPIGD---NFTM-----GPEDAALAVELIKPKIVIPMHYNTF 196
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 134-304 3.84e-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: 41.00  E-value: 3.84e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952697099  134 TVLVEMDGLVLLTDPVFSPRASP---WQRVGPRRfrrapcsvaelpaVHAVVLSHNHYDHldCGSVRALNERFGPELrwF 210
Cdd:smart00849   2 SYLVRDDGGAILIDTGPGEAEDLlaeLKKLGPKK-------------IDAIILTHGHPDH--IGGLPELLEAPGAPV--Y 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952697099  211 VPLGLLDWMQKCGCENVIELDWWEENCVP-----------GHDSVTFVFTPAqHW----CkrTLLDDNRVLwgswavlgp 275
Cdd:smart00849  65 APEGTAELLKDLLALLGELGAEAEPAPPDrtlkdgdeldlGGGELEVIHTPG-HTpgsiV--LYLPEGKIL--------- 132

                          170       180
                   ....*....|....*....|....*....
gi 1952697099  276 wsrffFAGDTGYCSAFEEIGRRFGPFDLA 304
Cdd:smart00849 133 -----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 1.56e-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: 275.31  E-value: 1.56e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952697099 129 WLGHATVLVEMDGLVLLTDPVFSPRASPWQRVGPRRFRRAPCSVAELPAVHAVVLSHNHYDHLDCGSVRALNERFGpelr 208
Cdd:cd16283     1 WIGHATFLIQIEGLNILTDPVFSERASPVSFGGPKRLTPPGLPLEELPPIDAVLISHNHYDHLDLPTVKRLGGRPP---- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952697099 209 WFVPLGLLDWMQKCGCENVIELDWWEENcvpGHDSVTFVFTPAQHWCKRTLLDDNRVLWGSWAVLGPWSRFFFAGDTGYC 288
Cdd:cd16283    77 YLVPLGLKKWFLKKGITNVVELDWWQST---EIGGVRITFVPAQHWSRRTLFDTNESLWGGWVIEGEGFRIYFAGDTGYF 153

                         170       180
                  ....*....|....*....|....*...
gi 1952697099 289 SAFEEIGRRFGPFDLAAIPIGAYEPRWF 316
Cdd:cd16283   154 PGFREIGRRFGPIDLALLPIGAYEPRWF 181
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 122-369 2.45e-75

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 233.27  E-value: 2.45e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952697099 122 GAGLRVTWLGHATVLVEMDGLVLLTDPVFSPRASPwqrvgprrFRRAPCSVAELPAVHAVVLSHNHYDHLDCGSVRALNE 201
Cdd:COG2220     1 PGGMKITWLGHATFLIETGGKRILIDPVFSGRASP--------VNPLPLDPEDLPKIDAVLVTHDHYDHLDDATLRALKR 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952697099 202 RFGPelrWFVPLGLLDWMQKCGCENVIELDWWEENCVPGhdsVTFVFTPAQHWCKRtlLDDNRVLWGSWAVLGPWSRFFF 281
Cdd:COG2220    73 TGAT---VVAPLGVAAWLRAWGFPRVTELDWGESVELGG---LTVTAVPARHSSGR--PDRNGGLWVGFVIETDGKTIYH 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952697099 282 AGDTGYCSAFEEIGRRFgPFDLAAIPIGAYeprwfmkYQHVDPEEAVRIHIDVQTKKSVAIHWGTFALANEhylEPPVKL 361
Cdd:COG2220   145 AGDTGYFPEMKEIGERF-PIDVALLPIGAY-------PFTMGPEEAAEAARDLKPKVVIPIHYGTFPLLDE---DPLERF 213


                  ....*...
gi 1952697099 362 SEALGRYG 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 2.40e-40

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: 141.68  E-value: 2.40e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952697099 144 LLTDPVFSPRaspwqrvGPRRFRRAPCSVAELPaVHAVVLSHNHYDHL-DCGSVRALNERfgpelRWFVPLGLLDWMQKC 222
Cdd:pfam12706   3 ILIDPGPDLR-------QQALPALQPGRLRDDP-IDAVLLTHDHYDHLaGLLDLREGRPR-----PLYAPLGVLAHLRRN 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952697099 223 GC---------ENVIELDWWEEnCVPGHDSVTFVFTPAQHWCKRtLLDDNRVLWGSWAVLGPWSRFFFAGDTGYCSafEE 293
Cdd:pfam12706  70 FPylfllehygVRVHEIDWGES-FTVGDGGLTVTATPARHGSPR-GLDPNPGDTLGFRIEGPGKRVYYAGDTGYFP--DE 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1952697099 294 IGRRFGPFDLAAIPIGAYEPRWFMKYQHVDPEEAVRIHIDVQTKKSVAIHW 344
Cdd:pfam12706 146 IGERLGGADLLLLDGGAWRDDEMIHMGHMTPEEAVEAAADLGARRKVLIHI 196
PRK00685 PRK00685
metal-dependent hydrolase; Provisional
 125-347 2.96e-16

metal-dependent hydrolase; Provisional


Pssm-ID: 234811 [Multi-domain]  Cd Length: 228  Bit Score: 77.16  E-value: 2.96e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952697099 125 LRVTWLGHATVLVEMDGLVLLTDPVFSPRASpwqrvgprrfrrAPCSVAELPAVHaVVLSHNHYDHLdcGSVRALNERFG 204
Cdd:PRK00685    1 MKITWLGHSAFLIETGGKKILIDPFITGNPL------------ADLKPEDVKVDY-ILLTHGHGDHL--GDTVEIAKRTG 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952697099 205 PELrwFVPLGLLDWMQKCGCENVIeldwweencvPGH-------DSVTFVFTPAQHwcKRTLLDDNRVLWGSWA----VL 273
Cdd:PRK00685   66 ATV--IANAELANYLSEKGVEKTH----------PMNiggtvefDGGKVKLTPALH--SSSFIDEDGITYLGNPtgfvIT 131

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952697099 274 GPWSRFFFAGDTGYCSAFEEIGRRFGPfDLAAIPIGAyepRWFMkyqhvDPEEAVRIHIDVQTKKSVAIHWGTF 347
Cdd:PRK00685  132 FEGKTIYHAGDTGLFSDMKLIGELHKP-DVALLPIGD---NFTM-----GPEDAALAVELIKPKIVIPMHYNTF 196
Lactamase_B_3 pfam13483
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 126-190 1.06e-07

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: 51.05  E-value: 1.06e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952697099 126 RVTWLGHATVLVEMDGLVLLTDPVFSPRASPWQRVGPRrfrrapcsvaelpavhAVVLSHNHYDH 190
Cdd:pfam13483   1 EITWLGHSSFLIEGGGARILTDPFRATVGYRPPPVTAD----------------LVLISHGHDDH 49
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 175-296 1.46e-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: 42.04  E-value: 1.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952697099 175 LPAVHAVVLSHNHYDH-LDCGS---VRALNERFGPE--LRWFVPLGLLDWMQK-CGCENVIELDWWEENCVPGHDSVTFV 247
Cdd:cd07716    48 PEDLDAVVLSHLHPDHcADLGVlqyARRYHPRGARKppLPLYGPAGPAERLAAlYGLEDVFDFHPIEPGEPLEIGPFTIT 127

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1952697099 248 FTPAQHWCKrtllddnrvlwgSWA--VLGPWSRFFFAGDTGYCSAFEEIGR 296
Cdd:cd07716   128 FFRTVHPVP------------CYAmrIEDGGKVLVYTGDTGYCDELVEFAR 166
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 134-304 3.84e-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: 41.00  E-value: 3.84e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952697099  134 TVLVEMDGLVLLTDPVFSPRASP---WQRVGPRRfrrapcsvaelpaVHAVVLSHNHYDHldCGSVRALNERFGPELrwF 210
Cdd:smart00849   2 SYLVRDDGGAILIDTGPGEAEDLlaeLKKLGPKK-------------IDAIILTHGHPDH--IGGLPELLEAPGAPV--Y 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952697099  211 VPLGLLDWMQKCGCENVIELDWWEENCVP-----------GHDSVTFVFTPAqHW----CkrTLLDDNRVLwgswavlgp 275
Cdd:smart00849  65 APEGTAELLKDLLALLGELGAEAEPAPPDrtlkdgdeldlGGGELEVIHTPG-HTpgsiV--LYLPEGKIL--------- 132

                          170       180
                   ....*....|....*....|....*....
gi 1952697099  276 wsrffFAGDTGYCSAFEEIGRRFGPFDLA 304
Cdd:smart00849 133 -----FTGDLLFAGGDGRTLVDGGDAAAS 156
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 178-297 2.26e-03

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: 38.81  E-value: 2.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952697099 178 VHAVVLSHNHYDHldCGSVRALNERFGpelrwfVPLglldWMQKcgcenvIELDWWEEncvPGHDSVTFVFTPAQHWCKR 257
Cdd:cd06262    46 IKAILLTHGHFDH--IGGLAELKEAPG------APV----YIHE------ADAELLED---PELNLAFFGGGPLPPPEPD 104

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1952697099 258 TLLDDNRVLW----------------GSWAVLGPWSRFFFAGDTGYCsafEEIGRR 297
Cdd:cd06262   105 ILLEDGDTIElgglelevihtpghtpGSVCFYIEEEGVLFTGDTLFA---GSIGRT 157
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
127-205 2.29e-03

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 38.89  E-value: 2.29e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1952697099 127 VTWLGHATVLVEMDGLVLLTDPVFSPRASpwqrvgprRFRRAPCSVAELPAVHAVVLSHNHYDHldCGSVRALNERFGP 205
Cdd:pfam00753   1 LGPGQVNSYLIEGGGGAVLIDTGGSAEAA--------LLLLLAALGLGPKDIDAVILTHGHFDH--IGGLGELAEATDV 69
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 123-285 3.02e-03

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: 38.52  E-value: 3.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952697099 123 AGLRVTWLGHATVLVEMDGLVLLTDPVFSPRAspwqrvgPRRFRRApcsVAELPA-VHAVVLSHNHYDHldCGSVRALNE 201
Cdd:COG0491     6 GGTPGAGLGVNSYLIVGGDGAVLIDTGLGPAD-------AEALLAA---LAALGLdIKAVLLTHLHPDH--VGGLAALAE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952697099 202 RFGPELrwFVPLGLLDWMQKCGCENVIELDWWEENCVP--------GHDSVTFVFTPAqHwckrTllddnrvlWGSWAVL 273
Cdd:COG0491    74 AFGAPV--YAHAAEAEALEAPAAGALFGREPVPPDRTLedgdtlelGGPGLEVIHTPG-H----T--------PGHVSFY 138

                         170
                  ....*....|..
gi 1952697099 274 GPWSRFFFAGDT 285
Cdd:COG0491   139 VPDEKVLFTGDA 150
 
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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