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Conserved domains on  [gi|1890346407|ref|NP_001373142|]
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N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D isoform 1 [Homo sapiens]

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 1.53e-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: 278.01  E-value: 1.53e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346407 129 WLGHATVMVEMDELIFLTDPIFSSRASPSQYMGPKRFRRSPCTISELPPIDAVLISHNHYDHLDYNSVIALNERFGnelr 208
Cdd:cd16283     1 WIGHATFLIQIEGLNILTDPVFSERASPVSFGGPKRLTPPGLPLEELPPIDAVLISHNHYDHLDLPTVKRLGGRPP---- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346407 209 WFVPLGLLDWMQKCGCENVIELDWWEENcvpGHDKVTFVFTPSQHWCKRTLMDDNKVLWGSWSVLGPWNRFFFAGDTGYC 288
Cdd:cd16283    77 YLVPLGLKKWFLKKGITNVVELDWWQST---EIGGVRITFVPAQHWSRRTLFDTNESLWGGWVIEGEGFRIYFAGDTGYF 153
                         170       180
                  ....*....|....*....|....*...
gi 1890346407 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 1.53e-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: 278.01  E-value: 1.53e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346407 129 WLGHATVMVEMDELIFLTDPIFSSRASPSQYMGPKRFRRSPCTISELPPIDAVLISHNHYDHLDYNSVIALNERFGnelr 208
Cdd:cd16283     1 WIGHATFLIQIEGLNILTDPVFSERASPVSFGGPKRLTPPGLPLEELPPIDAVLISHNHYDHLDLPTVKRLGGRPP---- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346407 209 WFVPLGLLDWMQKCGCENVIELDWWEENcvpGHDKVTFVFTPSQHWCKRTLMDDNKVLWGSWSVLGPWNRFFFAGDTGYC 288
Cdd:cd16283    77 YLVPLGLKKWFLKKGITNVVELDWWQST---EIGGVRITFVPAQHWSRRTLFDTNESLWGGWVIEGEGFRIYFAGDTGYF 153
                         170       180
                  ....*....|....*....|....*...
gi 1890346407 289 PAFEEIGKRFGPFDLAAIPIGAYEPRWF 316
Cdd:cd16283   154 PGFREIGRRFGPIDLALLPIGAYEPRWF 181
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
122-369 1.49e-75

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 233.66  E-value: 1.49e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346407 122 EAGLRVTWLGHATVMVEMDELIFLTDPIFSSRASPsqymgpkrFRRSPCTISELPPIDAVLISHNHYDHLDYNSVIALNE 201
Cdd:COG2220     1 PGGMKITWLGHATFLIETGGKRILIDPVFSGRASP--------VNPLPLDPEDLPKIDAVLVTHDHYDHLDDATLRALKR 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346407 202 RFgneLRWFVPLGLLDWMQKCGCENVIELDWWEENCVPGhdkVTFVFTPSQHWCKRTlmDDNKVLWGSWSVLGPWNRFFF 281
Cdd:COG2220    73 TG---ATVVAPLGVAAWLRAWGFPRVTELDWGESVELGG---LTVTAVPARHSSGRP--DRNGGLWVGFVIETDGKTIYH 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346407 282 AGDTGYCPAFEEIGKRFgPFDLAAIPIGAYeprwfmkYQHVDPEEAVRIHTDVQTKKSMAIHWGTFALANEhylEPPVKL 361
Cdd:COG2220   145 AGDTGYFPEMKEIGERF-PIDVALLPIGAY-------PFTMGPEEAAEAARDLKPKVVIPIHYGTFPLLDE---DPLERF 213

                  ....*...
gi 1890346407 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 1.52e-41

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: 144.76  E-value: 1.52e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346407 144 FLTDPIFSSRASPSQYMGPKRFRRSPctiselppIDAVLISHNHYDHL-DYNSVIALNERfgnelRWFVPLGLLDWMQKC 222
Cdd:pfam12706   3 ILIDPGPDLRQQALPALQPGRLRDDP--------IDAVLLTHDHYDHLaGLLDLREGRPR-----PLYAPLGVLAHLRRN 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346407 223 GC---------ENVIELDWWEENCVPGHDkVTFVFTPSQHWCKRTLmDDNKVLWGSWSVLGPWNRFFFAGDTGYCPafEE 293
Cdd:pfam12706  70 FPylfllehygVRVHEIDWGESFTVGDGG-LTVTATPARHGSPRGL-DPNPGDTLGFRIEGPGKRVYYAGDTGYFP--DE 145
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1890346407 294 IGKRFGPFDLAAIPIGAYEPRWFMKYQHVDPEEAVRIHTDVQTKKSMAIHW 344
Cdd:pfam12706 146 IGERLGGADLLLLDGGAWRDDEMIHMGHMTPEEAVEAAADLGARRKVLIHI 196
PRK00685 PRK00685
metal-dependent hydrolase; Provisional
125-347 2.15e-12

metal-dependent hydrolase; Provisional


Pssm-ID: 234811 [Multi-domain]  Cd Length: 228  Bit Score: 65.99  E-value: 2.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346407 125 LRVTWLGHATVMVEMDELIFLTDPIFSSRASpsqymgpkrfrrSPCTISELPPiDAVLISHNHYDHL--------DYNS- 195
Cdd:PRK00685    1 MKITWLGHSAFLIETGGKKILIDPFITGNPL------------ADLKPEDVKV-DYILLTHGHGDHLgdtveiakRTGAt 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346407 196 VIALNErfgnelrwfvplgLLDWMQKCGCENVIeldwweencvPGH-------DKVTFVFTPSQHWCKRTlMDDNKVLWG 268
Cdd:PRK00685   68 VIANAE-------------LANYLSEKGVEKTH----------PMNiggtvefDGGKVKLTPALHSSSFI-DEDGITYLG 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346407 269 SWS---VLGPWNRFFFAGDTGYCPAFEEIGKRFGPfDLAAIPIGAyepRWFMkyqhvDPEEAVRIHTDVQTKKSMAIHWG 345
Cdd:PRK00685  124 NPTgfvITFEGKTIYHAGDTGLFSDMKLIGELHKP-DVALLPIGD---NFTM-----GPEDAALAVELIKPKIVIPMHYN 194

                  ..
gi 1890346407 346 TF 347
Cdd:PRK00685  195 TF 196
 
Name Accession Description Interval E-value
RomA-like_MBL-fold cd16283
Enterobacter cloacae RomA and related proteins; MBL-fold metallo hydrolase domain; ...
129-316 1.53e-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: 278.01  E-value: 1.53e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346407 129 WLGHATVMVEMDELIFLTDPIFSSRASPSQYMGPKRFRRSPCTISELPPIDAVLISHNHYDHLDYNSVIALNERFGnelr 208
Cdd:cd16283     1 WIGHATFLIQIEGLNILTDPVFSERASPVSFGGPKRLTPPGLPLEELPPIDAVLISHNHYDHLDLPTVKRLGGRPP---- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346407 209 WFVPLGLLDWMQKCGCENVIELDWWEENcvpGHDKVTFVFTPSQHWCKRTLMDDNKVLWGSWSVLGPWNRFFFAGDTGYC 288
Cdd:cd16283    77 YLVPLGLKKWFLKKGITNVVELDWWQST---EIGGVRITFVPAQHWSRRTLFDTNESLWGGWVIEGEGFRIYFAGDTGYF 153
                         170       180
                  ....*....|....*....|....*...
gi 1890346407 289 PAFEEIGKRFGPFDLAAIPIGAYEPRWF 316
Cdd:cd16283   154 PGFREIGRRFGPIDLALLPIGAYEPRWF 181
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
122-369 1.49e-75

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 233.66  E-value: 1.49e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346407 122 EAGLRVTWLGHATVMVEMDELIFLTDPIFSSRASPsqymgpkrFRRSPCTISELPPIDAVLISHNHYDHLDYNSVIALNE 201
Cdd:COG2220     1 PGGMKITWLGHATFLIETGGKRILIDPVFSGRASP--------VNPLPLDPEDLPKIDAVLVTHDHYDHLDDATLRALKR 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346407 202 RFgneLRWFVPLGLLDWMQKCGCENVIELDWWEENCVPGhdkVTFVFTPSQHWCKRTlmDDNKVLWGSWSVLGPWNRFFF 281
Cdd:COG2220    73 TG---ATVVAPLGVAAWLRAWGFPRVTELDWGESVELGG---LTVTAVPARHSSGRP--DRNGGLWVGFVIETDGKTIYH 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346407 282 AGDTGYCPAFEEIGKRFgPFDLAAIPIGAYeprwfmkYQHVDPEEAVRIHTDVQTKKSMAIHWGTFALANEhylEPPVKL 361
Cdd:COG2220   145 AGDTGYFPEMKEIGERF-PIDVALLPIGAY-------PFTMGPEEAAEAARDLKPKVVIPIHYGTFPLLDE---DPLERF 213

                  ....*...
gi 1890346407 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 1.52e-41

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: 144.76  E-value: 1.52e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346407 144 FLTDPIFSSRASPSQYMGPKRFRRSPctiselppIDAVLISHNHYDHL-DYNSVIALNERfgnelRWFVPLGLLDWMQKC 222
Cdd:pfam12706   3 ILIDPGPDLRQQALPALQPGRLRDDP--------IDAVLLTHDHYDHLaGLLDLREGRPR-----PLYAPLGVLAHLRRN 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346407 223 GC---------ENVIELDWWEENCVPGHDkVTFVFTPSQHWCKRTLmDDNKVLWGSWSVLGPWNRFFFAGDTGYCPafEE 293
Cdd:pfam12706  70 FPylfllehygVRVHEIDWGESFTVGDGG-LTVTATPARHGSPRGL-DPNPGDTLGFRIEGPGKRVYYAGDTGYFP--DE 145
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1890346407 294 IGKRFGPFDLAAIPIGAYEPRWFMKYQHVDPEEAVRIHTDVQTKKSMAIHW 344
Cdd:pfam12706 146 IGERLGGADLLLLDGGAWRDDEMIHMGHMTPEEAVEAAADLGARRKVLIHI 196
PRK00685 PRK00685
metal-dependent hydrolase; Provisional
125-347 2.15e-12

metal-dependent hydrolase; Provisional


Pssm-ID: 234811 [Multi-domain]  Cd Length: 228  Bit Score: 65.99  E-value: 2.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346407 125 LRVTWLGHATVMVEMDELIFLTDPIFSSRASpsqymgpkrfrrSPCTISELPPiDAVLISHNHYDHL--------DYNS- 195
Cdd:PRK00685    1 MKITWLGHSAFLIETGGKKILIDPFITGNPL------------ADLKPEDVKV-DYILLTHGHGDHLgdtveiakRTGAt 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346407 196 VIALNErfgnelrwfvplgLLDWMQKCGCENVIeldwweencvPGH-------DKVTFVFTPSQHWCKRTlMDDNKVLWG 268
Cdd:PRK00685   68 VIANAE-------------LANYLSEKGVEKTH----------PMNiggtvefDGGKVKLTPALHSSSFI-DEDGITYLG 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346407 269 SWS---VLGPWNRFFFAGDTGYCPAFEEIGKRFGPfDLAAIPIGAyepRWFMkyqhvDPEEAVRIHTDVQTKKSMAIHWG 345
Cdd:PRK00685  124 NPTgfvITFEGKTIYHAGDTGLFSDMKLIGELHKP-DVALLPIGD---NFTM-----GPEDAALAVELIKPKIVIPMHYN 194

                  ..
gi 1890346407 346 TF 347
Cdd:PRK00685  195 TF 196
Lactamase_B_3 pfam13483
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
126-190 4.70e-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: 52.21  E-value: 4.70e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1890346407 126 RVTWLGHATVMVEMDELIFLTDPifssraspsqymgpkrFRRSPCTISELPPIDAVLISHNHYDH 190
Cdd:pfam13483   1 EITWLGHSSFLIEGGGARILTDP----------------FRATVGYRPPPVTADLVLISHGHDDH 49
 
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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