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Conserved domains on  [gi|148237490|ref|NP_001074082|]
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N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D [Danio rerio]

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; ...
 98-283 1.42e-91

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: 271.84  E-value: 1.42e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237490  98 WLGHATVLVEMEGLLVLTDPIFSQRASPVAFMGPKRYRDPPCTIEQLPRLDAVVISHTHYDHLDAASVTALNSRFgsalH 177
Cdd:cd16283    1 WIGHATFLIQIEGLNILTDPVFSERASPVSFGGPKRLTPPGLPLEELPPIDAVLISHNHYDHLDLPTVKRLGGRP----P 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237490 178 WFVPLGLAEWMQKTGCENVTELDWWVGSRipgHDNVSFFCTPAQHWCKRTPVDDNKTLWGSWSIVGSHSRFFFAGDTGYC 257
Cdd:cd16283   77 YLVPLGLKKWFLKKGITNVVELDWWQSTE---IGGVRITFVPAQHWSRRTLFDTNESLWGGWVIEGEGFRIYFAGDTGYF 153

                        170       180
                 ....*....|....*....|....*.
gi 148237490 258 ASFKEIGRHFGPFDLAAIPIGAYVPR 283
Cdd:cd16283  154 PGFREIGRRFGPIDLALLPIGAYEPR 179
 
Name Accession Description Interval E-value
RomA-like_MBL-fold cd16283
Enterobacter cloacae RomA and related proteins; MBL-fold metallo hydrolase domain; ...
 98-283 1.42e-91

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: 271.84  E-value: 1.42e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237490  98 WLGHATVLVEMEGLLVLTDPIFSQRASPVAFMGPKRYRDPPCTIEQLPRLDAVVISHTHYDHLDAASVTALNSRFgsalH 177
Cdd:cd16283    1 WIGHATFLIQIEGLNILTDPVFSERASPVSFGGPKRLTPPGLPLEELPPIDAVLISHNHYDHLDLPTVKRLGGRP----P 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237490 178 WFVPLGLAEWMQKTGCENVTELDWWVGSRipgHDNVSFFCTPAQHWCKRTPVDDNKTLWGSWSIVGSHSRFFFAGDTGYC 257
Cdd:cd16283   77 YLVPLGLKKWFLKKGITNVVELDWWQSTE---IGGVRITFVPAQHWSRRTLFDTNESLWGGWVIEGEGFRIYFAGDTGYF 153

                        170       180
                 ....*....|....*....|....*.
gi 148237490 258 ASFKEIGRHFGPFDLAAIPIGAYVPR 283
Cdd:cd16283  154 PGFREIGRRFGPIDLALLPIGAYEPR 179
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 91-334 1.61e-72

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 224.80  E-value: 1.61e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237490  91 GTSVRATWLGHATVLVEMEGLLVLTDPIFSQRASPVAFMgpkryrdpPCTIEQLPRLDAVVISHTHYDHLDAASVTALNS 170
Cdd:COG2220    1 PGGMKITWLGHATFLIETGGKRILIDPVFSGRASPVNPL--------PLDPEDLPKIDAVLVTHDHYDHLDDATLRALKR 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237490 171 RFgsaLHWFVPLGLAEWMQKTGCENVTELDWWVGSRIPGhdnVSFFCTPAQHWCKRTpvDDNKTLWGSWSIVGSHSRFFF 250
Cdd:COG2220   73 TG---ATVVAPLGVAAWLRAWGFPRVTELDWGESVELGG---LTVTAVPARHSSGRP--DRNGGLWVGFVIETDGKTIYH 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237490 251 AGDTGYCASFKEIGRHFgPFDLAAIPIGAYvprgimkSQHVDPEEAVQIHIDVQAKASLAIHWGTFPLSYEhylEPPARL 330
Cdd:COG2220  145 AGDTGYFPEMKEIGERF-PIDVALLPIGAY-------PFTMGPEEAAEAARDLKPKVVIPIHYGTFPLLDE---DPLERF 213


                 ....
gi 148237490 331 REAM 334
Cdd:COG2220  214 AAAL 217
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 113-313 1.14e-35

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: 128.58  E-value: 1.14e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237490  113 VLTDPIFSqraspvaFMGPKRYRDPPCTIEQLPrLDAVVISHTHYDHL-DAASVtalnsRFGSALHWFVPLGLAEWMQKT 191
Cdd:pfam12706   3 ILIDPGPD-------LRQQALPALQPGRLRDDP-IDAVLLTHDHYDHLaGLLDL-----REGRPRPLYAPLGVLAHLRRN 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237490  192 GC---------ENVTELDWWVGSRIPGHDnVSFFCTPAQHWCKRtPVDDNKTLWGSWSIVGSHSRFFFAGDTGYCAsfKE 262
Cdd:pfam12706  70 FPylfllehygVRVHEIDWGESFTVGDGG-LTVTATPARHGSPR-GLDPNPGDTLGFRIEGPGKRVYYAGDTGYFP--DE 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 148237490  263 IGRHFGPFDLAAIPIGAYVPRGIMKSQHVDPEEAVQIHIDVQAKASLAIHW 313
Cdd:pfam12706 146 IGERLGGADLLLLDGGAWRDDEMIHMGHMTPEEAVEAAADLGARRKVLIHI 196
PRK00685 PRK00685
metal-dependent hydrolase; Provisional
 94-318 5.37e-14

metal-dependent hydrolase; Provisional


Pssm-ID: 234811 [Multi-domain]  Cd Length: 228  Bit Score: 70.61  E-value: 5.37e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237490  94 VRATWLGHATVLVEMEGLLVLTDPIFSqrASPVAfmgpkryrdpPCTIEQLpRLDAVVISHTHYDHL-DAasvTALNSRF 172
Cdd:PRK00685   1 MKITWLGHSAFLIETGGKKILIDPFIT--GNPLA----------DLKPEDV-KVDYILLTHGHGDHLgDT---VEIAKRT 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237490 173 GSALhwFVPLGLAEWMQKTGCENVteldwwvgsrIPGH-------DNVSFFCTPAQHwCKRTPVDDNKTLWGSWS---IV 242
Cdd:PRK00685  65 GATV--IANAELANYLSEKGVEKT----------HPMNiggtvefDGGKVKLTPALH-SSSFIDEDGITYLGNPTgfvIT 131

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148237490 243 GSHSRFFFAGDTGYCASFKEIGRHFGPfDLAAIPIGAyvpRGIMksqhvDPEEAVQIHIDVQAKASLAIHWGTFPL 318
Cdd:PRK00685 132 FEGKTIYHAGDTGLFSDMKLIGELHKP-DVALLPIGD---NFTM-----GPEDAALAVELIKPKIVIPMHYNTFPL 198
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 103-159 9.15e-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: 36.76  E-value: 9.15e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 148237490   103 TVLVEMEGLLVLTDPifsqraspvafmGPKRYRDPPCTIEQL--PRLDAVVISHTHYDH 159
Cdd:smart00849   2 SYLVRDDGGAILIDT------------GPGEAEDLLAELKKLgpKKIDAIILTHGHPDH 48
 
Name Accession Description Interval E-value
RomA-like_MBL-fold cd16283
Enterobacter cloacae RomA and related proteins; MBL-fold metallo hydrolase domain; ...
 98-283 1.42e-91

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: 271.84  E-value: 1.42e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237490  98 WLGHATVLVEMEGLLVLTDPIFSQRASPVAFMGPKRYRDPPCTIEQLPRLDAVVISHTHYDHLDAASVTALNSRFgsalH 177
Cdd:cd16283    1 WIGHATFLIQIEGLNILTDPVFSERASPVSFGGPKRLTPPGLPLEELPPIDAVLISHNHYDHLDLPTVKRLGGRP----P 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237490 178 WFVPLGLAEWMQKTGCENVTELDWWVGSRipgHDNVSFFCTPAQHWCKRTPVDDNKTLWGSWSIVGSHSRFFFAGDTGYC 257
Cdd:cd16283   77 YLVPLGLKKWFLKKGITNVVELDWWQSTE---IGGVRITFVPAQHWSRRTLFDTNESLWGGWVIEGEGFRIYFAGDTGYF 153

                        170       180
                 ....*....|....*....|....*.
gi 148237490 258 ASFKEIGRHFGPFDLAAIPIGAYVPR 283
Cdd:cd16283  154 PGFREIGRRFGPIDLALLPIGAYEPR 179
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 91-334 1.61e-72

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 224.80  E-value: 1.61e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237490  91 GTSVRATWLGHATVLVEMEGLLVLTDPIFSQRASPVAFMgpkryrdpPCTIEQLPRLDAVVISHTHYDHLDAASVTALNS 170
Cdd:COG2220    1 PGGMKITWLGHATFLIETGGKRILIDPVFSGRASPVNPL--------PLDPEDLPKIDAVLVTHDHYDHLDDATLRALKR 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237490 171 RFgsaLHWFVPLGLAEWMQKTGCENVTELDWWVGSRIPGhdnVSFFCTPAQHWCKRTpvDDNKTLWGSWSIVGSHSRFFF 250
Cdd:COG2220   73 TG---ATVVAPLGVAAWLRAWGFPRVTELDWGESVELGG---LTVTAVPARHSSGRP--DRNGGLWVGFVIETDGKTIYH 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237490 251 AGDTGYCASFKEIGRHFgPFDLAAIPIGAYvprgimkSQHVDPEEAVQIHIDVQAKASLAIHWGTFPLSYEhylEPPARL 330
Cdd:COG2220  145 AGDTGYFPEMKEIGERF-PIDVALLPIGAY-------PFTMGPEEAAEAARDLKPKVVIPIHYGTFPLLDE---DPLERF 213


                 ....
gi 148237490 331 REAM 334
Cdd:COG2220  214 AAAL 217
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 113-313 1.14e-35

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: 128.58  E-value: 1.14e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237490  113 VLTDPIFSqraspvaFMGPKRYRDPPCTIEQLPrLDAVVISHTHYDHL-DAASVtalnsRFGSALHWFVPLGLAEWMQKT 191
Cdd:pfam12706   3 ILIDPGPD-------LRQQALPALQPGRLRDDP-IDAVLLTHDHYDHLaGLLDL-----REGRPRPLYAPLGVLAHLRRN 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237490  192 GC---------ENVTELDWWVGSRIPGHDnVSFFCTPAQHWCKRtPVDDNKTLWGSWSIVGSHSRFFFAGDTGYCAsfKE 262
Cdd:pfam12706  70 FPylfllehygVRVHEIDWGESFTVGDGG-LTVTATPARHGSPR-GLDPNPGDTLGFRIEGPGKRVYYAGDTGYFP--DE 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 148237490  263 IGRHFGPFDLAAIPIGAYVPRGIMKSQHVDPEEAVQIHIDVQAKASLAIHW 313
Cdd:pfam12706 146 IGERLGGADLLLLDGGAWRDDEMIHMGHMTPEEAVEAAADLGARRKVLIHI 196
PRK00685 PRK00685
metal-dependent hydrolase; Provisional
 94-318 5.37e-14

metal-dependent hydrolase; Provisional


Pssm-ID: 234811 [Multi-domain]  Cd Length: 228  Bit Score: 70.61  E-value: 5.37e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237490  94 VRATWLGHATVLVEMEGLLVLTDPIFSqrASPVAfmgpkryrdpPCTIEQLpRLDAVVISHTHYDHL-DAasvTALNSRF 172
Cdd:PRK00685   1 MKITWLGHSAFLIETGGKKILIDPFIT--GNPLA----------DLKPEDV-KVDYILLTHGHGDHLgDT---VEIAKRT 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237490 173 GSALhwFVPLGLAEWMQKTGCENVteldwwvgsrIPGH-------DNVSFFCTPAQHwCKRTPVDDNKTLWGSWS---IV 242
Cdd:PRK00685  65 GATV--IANAELANYLSEKGVEKT----------HPMNiggtvefDGGKVKLTPALH-SSSFIDEDGITYLGNPTgfvIT 131

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148237490 243 GSHSRFFFAGDTGYCASFKEIGRHFGPfDLAAIPIGAyvpRGIMksqhvDPEEAVQIHIDVQAKASLAIHWGTFPL 318
Cdd:PRK00685 132 FEGKTIYHAGDTGLFSDMKLIGELHKP-DVALLPIGD---NFTM-----GPEDAALAVELIKPKIVIPMHYNTFPL 198
Lactamase_B_3 pfam13483
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 97-312 2.27e-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: 55.67  E-value: 2.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237490   97 TWLGHATVLVEMEGLLVLTDPIFsqraspvafmGPKRYRDPPctieqlPRLDAVVISHTHYDHLDAASVTAlnsrfgsal 176
Cdd:pfam13483   3 TWLGHSSFLIEGGGARILTDPFR----------ATVGYRPPP------VTADLVLISHGHDDHGHPETLPG--------- 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237490  177 hwfvplglaewmqktgceNVTELDWWVGSRIpghDNVSFFCTPAQHWCKRTPVDDNKTLWGsWSIVGshSRFFFAGDTGY 256
Cdd:pfam13483  58 ------------------NPHVLDGGGSYTV---GGLEIRGVPTDHDRVGGRRRGGNSIFL-FEQDG--LTIYHLGHLGH 113

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 148237490  257 CASFKEIgRHFGPFDLAAIPIGA-YVprgimksqhVDPEEAVQIHIDVQAKASLAIH 312
Cdd:pfam13483 114 PLSDEQL-AELGRVDVLLIPVGGpLT---------YGAEEALELAKRLRPRVVIPMH 160
COG2248 COG2248
Predicted hydrolase, metallo-beta-lactamase superfamily [General function prediction only];
102-161 5.23e-05

Predicted hydrolase, metallo-beta-lactamase superfamily [General function prediction only];


Pssm-ID: 441849  Cd Length: 300  Bit Score: 44.55  E-value: 5.23e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148237490 102 ATvLVEMEGLLVLTDPIFSqraspvafMGPKRYRDPPCTIEqLPRL--------------DAVVISHTHYDHLD 161
Cdd:COG2248   17 AT-FVETKDVRILIDPGVS--------LAPRRYGLPPHPRE-LERLeelreeiqeyakkaDIIIITHYHYDHHD 80
PRK04286 PRK04286
hypothetical protein; Provisional
 105-159 3.48e-04

hypothetical protein; Provisional


Pssm-ID: 235270  Cd Length: 298  Bit Score: 41.88  E-value: 3.48e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148237490 105 LVEMEGLLVLTDPIFSqraspvafMGPKRYRDPPCTIEqLPRL--------------DAVVISHTHYDH 159
Cdd:PRK04286  19 FVETKDVRILIDPGVS--------LAPRRYGLPPHPIE-LERLeevrekileyakkaDVITISHYHYDH 78
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 144-265 3.65e-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: 3.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237490 144 LPRLDAVVISHTHYDH-LDAAS--VTALNSRFGSA---LHWFVPLGLAEWMQK-TGCENVTEL-DWWVGSRIP-GHDNVS 214
Cdd:cd07716   48 PEDLDAVVLSHLHPDHcADLGVlqYARRYHPRGARkppLPLYGPAGPAERLAAlYGLEDVFDFhPIEPGEPLEiGPFTIT 127

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 148237490 215 FFctPAQHwckrtPVDDnktlWGsWSIVGSHSRFFFAGDTGYCASFKEIGR 265
Cdd:cd07716  128 FF--RTVH-----PVPC----YA-MRIEDGGKVLVYTGDTGYCDELVEFAR 166
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 103-159 9.15e-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: 36.76  E-value: 9.15e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 148237490   103 TVLVEMEGLLVLTDPifsqraspvafmGPKRYRDPPCTIEQL--PRLDAVVISHTHYDH 159
Cdd:smart00849   2 SYLVRDDGGAILIDT------------GPGEAEDLLAELKKLgpKKIDAIILTHGHPDH 48
 
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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