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Conserved domains on  [gi|1156048370|emb|SKQ26501|]
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Conserved exported protein of uncharacterised function [Mycobacteroides abscessus subsp. massiliense]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 11454817)

MBL fold metallo-hydrolase similar to as Sus scrofa cytidine monophosphate-N-acetylneuraminic acid hydroxylase and Bacillus subtilis UPF0173 protein YddR; may be inactive as a hydrolase such as human inactive cytidine monophosphate-N-acetylneuraminic CMAHP

CATH:  3.60.15.30
Gene Ontology:  GO:0016787|GO:0046872
PubMed:  11471246|17597585
SCOP:  3001057

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 98-344 8.21e-83

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


:

Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 251.37  E-value: 8.21e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1156048370  98 PADLAATWFGHSSVLVEIDGYRVLTDPVWSDRCSPSRvvgphrqhPVPVELSALPALDAVVISHDHYDHLDMDSIIALtR 177
Cdd:COG2220     1 PGGMKITWLGHATFLIETGGKRILIDPVFSGRASPVN--------PLPLDPEDLPKIDAVLVTHDHYDHLDDATLRAL-K 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1156048370 178 SQNAVFVVPLGVGAHLRGWGVSpaRVIELDWDQSHQLGKLTLTCTQARHFSGRSiARNTTLWASWAFAGPKHKVFFGGDT 257
Cdd:COG2220    72 RTGATVVAPLGVAAWLRAWGFP--RVTELDWGESVELGGLTVTAVPARHSSGRP-DRNGGLWVGFVIETDGKTIYHAGDT 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1156048370 258 GYTKAFKVIGDTYgPFDLTLLPVGAYNtswadIHMNPEEAVQTHLDLATAQAplLPIHWATFNLALHpwaEPIERVLAAA 337
Cdd:COG2220   149 GYFPEMKEIGERF-PIDVALLPIGAYP-----FTMGPEEAAEAARDLKPKVV--IPIHYGTFPLLDE---DPLERFAAAL 217


                  ....*..
gi 1156048370 338 EEQGVTV 344
Cdd:COG2220   218 AAAGVRV 224
 
Name Accession Description Interval E-value
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 98-344 8.21e-83

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 251.37  E-value: 8.21e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1156048370  98 PADLAATWFGHSSVLVEIDGYRVLTDPVWSDRCSPSRvvgphrqhPVPVELSALPALDAVVISHDHYDHLDMDSIIALtR 177
Cdd:COG2220     1 PGGMKITWLGHATFLIETGGKRILIDPVFSGRASPVN--------PLPLDPEDLPKIDAVLVTHDHYDHLDDATLRAL-K 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1156048370 178 SQNAVFVVPLGVGAHLRGWGVSpaRVIELDWDQSHQLGKLTLTCTQARHFSGRSiARNTTLWASWAFAGPKHKVFFGGDT 257
Cdd:COG2220    72 RTGATVVAPLGVAAWLRAWGFP--RVTELDWGESVELGGLTVTAVPARHSSGRP-DRNGGLWVGFVIETDGKTIYHAGDT 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1156048370 258 GYTKAFKVIGDTYgPFDLTLLPVGAYNtswadIHMNPEEAVQTHLDLATAQAplLPIHWATFNLALHpwaEPIERVLAAA 337
Cdd:COG2220   149 GYFPEMKEIGERF-PIDVALLPIGAYP-----FTMGPEEAAEAARDLKPKVV--IPIHYGTFPLLDE---DPLERFAAAL 217


                  ....*..
gi 1156048370 338 EEQGVTV 344
Cdd:COG2220   218 AAAGVRV 224
RomA-like_MBL-fold cd16283
Enterobacter cloacae RomA and related proteins; MBL-fold metallo hydrolase domain; ...
 105-287 1.84e-70

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: 218.30  E-value: 1.84e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1156048370 105 WFGHSSVLVEIDGYRVLTDPVWSDRCSPSRVVGPHRQHPVPVELSALPALDAVVISHDHYDHLDMDSIIALtrSQNAVFV 184
Cdd:cd16283     1 WIGHATFLIQIEGLNILTDPVFSERASPVSFGGPKRLTPPGLPLEELPPIDAVLISHNHYDHLDLPTVKRL--GGRPPYL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1156048370 185 VPLGVGAHLRGWGVSpaRVIELDWDQSHQLGKLTLTCTQARHFSGRSIA-RNTTLWASWAFAGPKHKVFFGGDTGYTKAF 263
Cdd:cd16283    79 VPLGLKKWFLKKGIT--NVVELDWWQSTEIGGVRITFVPAQHWSRRTLFdTNESLWGGWVIEGEGFRIYFAGDTGYFPGF 156

                         170       180
                  ....*....|....*....|....
gi 1156048370 264 KVIGDTYGPFDLTLLPVGAYNTSW 287
Cdd:cd16283   157 REIGRRFGPIDLALLPIGAYEPRW 180
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 118-316 5.86e-45

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: 153.23  E-value: 5.86e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1156048370 118 YRVLTDPVWSdrcspsrVVGPHRQHPVPVELSALPaLDAVVISHDHYDHL-DMDSIIALtrsQNAVFVVPLGVGAHLRGW 196
Cdd:pfam12706   1 RRILIDPGPD-------LRQQALPALQPGRLRDDP-IDAVLLTHDHYDHLaGLLDLREG---RPRPLYAPLGVLAHLRRN 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1156048370 197 GVSPA-------RVIELDWDQSHQLG--KLTLTCTQARHFSGRSIARNTTLWASWAFAGPKHKVFFGGDTGYTKAfkVIG 267
Cdd:pfam12706  70 FPYLFllehygvRVHEIDWGESFTVGdgGLTVTATPARHGSPRGLDPNPGDTLGFRIEGPGKRVYYAGDTGYFPD--EIG 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1156048370 268 DTYGPFDLTLLPVGAYNTSW--ADIHMNPEEAVQTHLDLATAQAplLPIHW 316
Cdd:pfam12706 148 ERLGGADLLLLDGGAWRDDEmiHMGHMTPEEAVEAAADLGARRK--VLIHI 196
PRK00685 PRK00685
metal-dependent hydrolase; Provisional
 104-351 1.96e-20

metal-dependent hydrolase; Provisional


Pssm-ID: 234811 [Multi-domain]  Cd Length: 228  Bit Score: 88.71  E-value: 1.96e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1156048370 104 TWFGHSSVLVEIDGYRVLTDPVWSDrcSPSRVVGphrqhpvPVELSAlpalDAVVISHDHYDHLDmDSiIALTRSQNAVF 183
Cdd:PRK00685    4 TWLGHSAFLIETGGKKILIDPFITG--NPLADLK-------PEDVKV----DYILLTHGHGDHLG-DT-VEIAKRTGATV 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1156048370 184 VVPLGVGAHLRGWGVSpaRVIELDWDQSHQLGKLTLTCTQARHFSGRSIARNTTLW---ASWAFAGPKHKVFFGGDTGYT 260
Cdd:PRK00685   69 IANAELANYLSEKGVE--KTHPMNIGGTVEFDGGKVKLTPALHSSSFIDEDGITYLgnpTGFVITFEGKTIYHAGDTGLF 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1156048370 261 KAFKVIGDTYGPfDLTLLPVGAYNTswadihMNPEEAVQThLDLATAQApLLPIHWATFnlalhpwaEPI----ERVLAA 336
Cdd:PRK00685  147 SDMKLIGELHKP-DVALLPIGDNFT------MGPEDAALA-VELIKPKI-VIPMHYNTF--------PLIeqdpEKFKAL 209

                         250
                  ....*....|....*
gi 1156048370 337 AEEQGVTVVTPRPGQ 351
Cdd:PRK00685  210 VEGLGTKVVILKPGE 224
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 109-276 3.46e-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: 3.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1156048370  109 SSVLVEIDGYRVLTDPVWSDRcspsrvvgphRQHPVPVELSALPALDAVVISHDHYDHldMDSIIALTRSQNAVFVVPLG 188
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEA----------EDLLAELKKLGPKKIDAIILTHGHPDH--IGGLPELLEAPGAPVYAPEG 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1156048370  189 VGAHLRG----------WGVSPARVIELDWDQSHQLGKLTLTctqARHFSGRSIARNTTLWaswafagPKHKVFFGGDTG 258
Cdd:smart00849  69 TAELLKDllallgelgaEAEPAPPDRTLKDGDELDLGGGELE---VIHTPGHTPGSIVLYL-------PEGKILFTGDLL 138

                          170
                   ....*....|....*...
gi 1156048370  259 YTKAFKVIGDTYGPFDLT 276
Cdd:smart00849 139 FAGGDGRTLVDGGDAAAS 156
 
Name Accession Description Interval E-value
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 98-344 8.21e-83

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 251.37  E-value: 8.21e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1156048370  98 PADLAATWFGHSSVLVEIDGYRVLTDPVWSDRCSPSRvvgphrqhPVPVELSALPALDAVVISHDHYDHLDMDSIIALtR 177
Cdd:COG2220     1 PGGMKITWLGHATFLIETGGKRILIDPVFSGRASPVN--------PLPLDPEDLPKIDAVLVTHDHYDHLDDATLRAL-K 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1156048370 178 SQNAVFVVPLGVGAHLRGWGVSpaRVIELDWDQSHQLGKLTLTCTQARHFSGRSiARNTTLWASWAFAGPKHKVFFGGDT 257
Cdd:COG2220    72 RTGATVVAPLGVAAWLRAWGFP--RVTELDWGESVELGGLTVTAVPARHSSGRP-DRNGGLWVGFVIETDGKTIYHAGDT 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1156048370 258 GYTKAFKVIGDTYgPFDLTLLPVGAYNtswadIHMNPEEAVQTHLDLATAQAplLPIHWATFNLALHpwaEPIERVLAAA 337
Cdd:COG2220   149 GYFPEMKEIGERF-PIDVALLPIGAYP-----FTMGPEEAAEAARDLKPKVV--IPIHYGTFPLLDE---DPLERFAAAL 217


                  ....*..
gi 1156048370 338 EEQGVTV 344
Cdd:COG2220   218 AAAGVRV 224
RomA-like_MBL-fold cd16283
Enterobacter cloacae RomA and related proteins; MBL-fold metallo hydrolase domain; ...
 105-287 1.84e-70

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: 218.30  E-value: 1.84e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1156048370 105 WFGHSSVLVEIDGYRVLTDPVWSDRCSPSRVVGPHRQHPVPVELSALPALDAVVISHDHYDHLDMDSIIALtrSQNAVFV 184
Cdd:cd16283     1 WIGHATFLIQIEGLNILTDPVFSERASPVSFGGPKRLTPPGLPLEELPPIDAVLISHNHYDHLDLPTVKRL--GGRPPYL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1156048370 185 VPLGVGAHLRGWGVSpaRVIELDWDQSHQLGKLTLTCTQARHFSGRSIA-RNTTLWASWAFAGPKHKVFFGGDTGYTKAF 263
Cdd:cd16283    79 VPLGLKKWFLKKGIT--NVVELDWWQSTEIGGVRITFVPAQHWSRRTLFdTNESLWGGWVIEGEGFRIYFAGDTGYFPGF 156

                         170       180
                  ....*....|....*....|....
gi 1156048370 264 KVIGDTYGPFDLTLLPVGAYNTSW 287
Cdd:cd16283   157 REIGRRFGPIDLALLPIGAYEPRW 180
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 118-316 5.86e-45

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: 153.23  E-value: 5.86e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1156048370 118 YRVLTDPVWSdrcspsrVVGPHRQHPVPVELSALPaLDAVVISHDHYDHL-DMDSIIALtrsQNAVFVVPLGVGAHLRGW 196
Cdd:pfam12706   1 RRILIDPGPD-------LRQQALPALQPGRLRDDP-IDAVLLTHDHYDHLaGLLDLREG---RPRPLYAPLGVLAHLRRN 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1156048370 197 GVSPA-------RVIELDWDQSHQLG--KLTLTCTQARHFSGRSIARNTTLWASWAFAGPKHKVFFGGDTGYTKAfkVIG 267
Cdd:pfam12706  70 FPYLFllehygvRVHEIDWGESFTVGdgGLTVTATPARHGSPRGLDPNPGDTLGFRIEGPGKRVYYAGDTGYFPD--EIG 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1156048370 268 DTYGPFDLTLLPVGAYNTSW--ADIHMNPEEAVQTHLDLATAQAplLPIHW 316
Cdd:pfam12706 148 ERLGGADLLLLDGGAWRDDEmiHMGHMTPEEAVEAAADLGARRK--VLIHI 196
PRK00685 PRK00685
metal-dependent hydrolase; Provisional
 104-351 1.96e-20

metal-dependent hydrolase; Provisional


Pssm-ID: 234811 [Multi-domain]  Cd Length: 228  Bit Score: 88.71  E-value: 1.96e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1156048370 104 TWFGHSSVLVEIDGYRVLTDPVWSDrcSPSRVVGphrqhpvPVELSAlpalDAVVISHDHYDHLDmDSiIALTRSQNAVF 183
Cdd:PRK00685    4 TWLGHSAFLIETGGKKILIDPFITG--NPLADLK-------PEDVKV----DYILLTHGHGDHLG-DT-VEIAKRTGATV 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1156048370 184 VVPLGVGAHLRGWGVSpaRVIELDWDQSHQLGKLTLTCTQARHFSGRSIARNTTLW---ASWAFAGPKHKVFFGGDTGYT 260
Cdd:PRK00685   69 IANAELANYLSEKGVE--KTHPMNIGGTVEFDGGKVKLTPALHSSSFIDEDGITYLgnpTGFVITFEGKTIYHAGDTGLF 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1156048370 261 KAFKVIGDTYGPfDLTLLPVGAYNTswadihMNPEEAVQThLDLATAQApLLPIHWATFnlalhpwaEPI----ERVLAA 336
Cdd:PRK00685  147 SDMKLIGELHKP-DVALLPIGDNFT------MGPEDAALA-VELIKPKI-VIPMHYNTF--------PLIeqdpEKFKAL 209

                         250
                  ....*....|....*
gi 1156048370 337 AEEQGVTVVTPRPGQ 351
Cdd:PRK00685  210 VEGLGTKVVILKPGE 224
Lactamase_B_3 pfam13483
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 104-299 4.27e-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: 49.13  E-value: 4.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1156048370 104 TWFGHSSVLVEIDGYRVLTDPVwsdrcspsRVVGPHRQHPVPVelsalpalDAVVISHDHYDHLDMDSIIALTRsqnavf 183
Cdd:pfam13483   3 TWLGHSSFLIEGGGARILTDPF--------RATVGYRPPPVTA--------DLVLISHGHDDHGHPETLPGNPH------ 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1156048370 184 vvplgvgaHLRGWGvsparvieldwdqSHQLG--KLTLTCTQARHFSGRSIARNTTlwasWAFAGPKHKVFFGGDTGYTK 261
Cdd:pfam13483  61 --------VLDGGG-------------SYTVGglEIRGVPTDHDRVGGRRRGGNSI----FLFEQDGLTIYHLGHLGHPL 115

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1156048370 262 AFKVIgDTYGPFDLTLLPVGAYNTswadihMNPEEAVQ 299
Cdd:pfam13483 116 SDEQL-AELGRVDVLLIPVGGPLT------YGAEEALE 146
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
107-352 8.83e-07

Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 49.42  E-value: 8.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1156048370 107 GHSSVLVEIDGYRVLTDPvwsdrcspsrvvGPH-----RQHPVPvelsaLPALDAVVISHDHYDH-LD----MDSIIALT 176
Cdd:COG1234    18 ATSSYLLEAGGERLLIDC------------GEGtqrqlLRAGLD-----PRDIDAIFITHLHGDHiAGlpglLSTRSLAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1156048370 177 RSQNAVFVVPLG----VGAHLRGWGVSPA---RVIELDWDQSHQLGKLTLTCTQARHfSGRSIArnttlwasWAFAGPKH 249
Cdd:COG1234    81 REKPLTIYGPPGtkefLEALLKASGTDLDfplEFHEIEPGEVFEIGGFTVTAFPLDH-PVPAYG--------YRFEEPGR 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1156048370 250 KVFFGGDTGYTKAF-KVIGDTygpfDL----TLLPVGAYNTSWADIHMNPEEAVQThldLATAQAPLLpihWATfnlalH 324
Cdd:COG1234   152 SLVYSGDTRPCEALvELAKGA----DLliheATFLDEEAELAKETGHSTAKEAAEL---AAEAGVKRL---VLT-----H 216

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1156048370 325 --PWAEPIERVLAAAEE--QGVTVVtPRPGQR 352
Cdd:COG1234   217 fsPRYDDPEELLAEARAvfPGPVEL-AEDGMV 247
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 109-260 1.21e-06

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: 48.21  E-value: 1.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1156048370 109 SSVLVEIDGYRVLTDpvwsdrCSPSrVVGPHRQHpvpvelSALPALDAVVISHDHYDH-LDMDSI-----IALTRSQNAV 182
Cdd:cd07716    19 SGYLLEADGFRILLD------CGSG-VLSRLQRY------IDPEDLDAVVLSHLHPDHcADLGVLqyarrYHPRGARKPP 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1156048370 183 FVV--PLGVGAHLRGW-GVSPA-RVIELDWDQSHQLGKLTLTCTQARHFSGrsiarnttlwaswAFA----GPKHKVFFG 254
Cdd:cd07716    86 LPLygPAGPAERLAALyGLEDVfDFHPIEPGEPLEIGPFTITFFRTVHPVP-------------CYAmrieDGGKVLVYT 152


                  ....*.
gi 1156048370 255 GDTGYT 260
Cdd:cd07716   153 GDTGYC 158
COG2248 COG2248
Predicted hydrolase, metallo-beta-lactamase superfamily [General function prediction only];
110-175 1.15e-04

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


Pssm-ID: 441849  Cd Length: 300  Bit Score: 43.39  E-value: 1.15e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1156048370 110 SVLVEIDGYRVLTDPVWSdrCSPSRVVGPhrqhPVPVELSALPAL-----------DAVVISHDHYDHLDMDSIIAL 175
Cdd:COG2248    17 ATFVETKDVRILIDPGVS--LAPRRYGLP----PHPRELERLEELreeiqeyakkaDIIIITHYHYDHHDPGEEIPK 87
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 109-181 1.17e-04

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; 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, 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. Some members of this subgroup are named as octanoyltransferase (also known as lipoate-protein ligase B).


Pssm-ID: 293837 [Multi-domain]  Cd Length: 193  Bit Score: 42.46  E-value: 1.17e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1156048370 109 SSVLVEIDGYRVLTDpvwsdrCSPSrvvgpHRQhpvpvelSALPA----LDAVVISHDHYDHLD-MDSIIALTRSQNA 181
Cdd:cd16279    36 SSILIETGGKNILID------TGPD-----FRQ-------QALRAgirkLDAVLLTHAHADHIHgLDDLRPFNRLQQR 95
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 109-276 3.46e-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: 3.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1156048370  109 SSVLVEIDGYRVLTDPVWSDRcspsrvvgphRQHPVPVELSALPALDAVVISHDHYDHldMDSIIALTRSQNAVFVVPLG 188
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEA----------EDLLAELKKLGPKKIDAIILTHGHPDH--IGGLPELLEAPGAPVYAPEG 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1156048370  189 VGAHLRG----------WGVSPARVIELDWDQSHQLGKLTLTctqARHFSGRSIARNTTLWaswafagPKHKVFFGGDTG 258
Cdd:smart00849  69 TAELLKDllallgelgaEAEPAPPDRTLKDGDELDLGGGELE---VIHTPGHTPGSIVLYL-------PEGKILFTGDLL 138

                          170
                   ....*....|....*...
gi 1156048370  259 YTKAFKVIGDTYGPFDLT 276
Cdd:smart00849 139 FAGGDGRTLVDGGDAAAS 156
PRK04286 PRK04286
hypothetical protein; Provisional
 110-170 4.05e-04

hypothetical protein; Provisional


Pssm-ID: 235270  Cd Length: 298  Bit Score: 41.88  E-value: 4.05e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1156048370 110 SVLVEIDGYRVLTDPVWSdrcspsrvVGPHRQH--PVPVELSALPAL-----------DAVVISHDHYDHLDMD 170
Cdd:PRK04286   17 ATFVETKDVRILIDPGVS--------LAPRRYGlpPHPIELERLEEVrekileyakkaDVITISHYHYDHHTPF 82
PRK11709 PRK11709
putative L-ascorbate 6-phosphate lactonase; Provisional
 140-204 4.48e-04

putative L-ascorbate 6-phosphate lactonase; Provisional


Pssm-ID: 236958  Cd Length: 355  Bit Score: 41.91  E-value: 4.48e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1156048370 140 RQHPVPVELSALPALDAVVISHDHYDHLDMDSIIALTR--SQNAVFVVPLGVGAHLRGWGVSPARVI 204
Cdd:PRK11709   96 RTQPFVLDPFAIREIDAVLATHDHSDHIDVNVAAAVLQncADHVKFIGPQACVDLWIGWGVPKERCI 162
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 110-166 1.96e-03

Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, and related proteins; MBL-fold metallo hydrolase domain; This subgroup includes Methanocaldococcus jannaschii 7,8-dihydropterin-6-methyl-4-(beta-D-ribofuranosyl)-aminobenzene-5'-phosphate synthase (EC 2.5.1.15), a folate biosynthetic enzyme also known as dihydropteroate synthase and 7,8 dihydropteroate synthase. Thermoanaerobacter tengcongensis Tflp is a ferredoxin-like member. 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.


Pssm-ID: 293799  Cd Length: 269  Bit Score: 39.53  E-value: 1.96e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1156048370 110 SVLVEIDGYRVLTDpvwsdrCSPSRVV-------GphrqhpvpVELSALpalDAVVISHDHYDH 166
Cdd:cd07713    22 SLLIETEGKKILFD------TGQSGVLlhnakklG--------IDLSDI---DAVVLSHGHYDH 68
PRK02113 PRK02113
MBL fold metallo-hydrolase;
109-167 1.99e-03

MBL fold metallo-hydrolase;


Pssm-ID: 179371 [Multi-domain]  Cd Length: 252  Bit Score: 39.38  E-value: 1.99e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1156048370 109 SSVLVEIDGYRVLTDpvwsdrCSPSrvvgpHRQHPVPVELSALpalDAVVISHDHYDHL 167
Cdd:PRK02113   36 TSALVETEGARILID------CGPD-----FREQMLRLPFGKI---DAVLITHEHYDHV 80
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 107-262 2.46e-03

Ribonuclease Z; 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. It includes the C-terminus of human ELAC2 and Escherichia coli zinc phosphodiesterase (ZiPD, also known as ecoZ, tRNase Z, or RNase BN) is a 3' tRNA-processing endonuclease, encoded by the elaC gene. 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.


Pssm-ID: 293830 [Multi-domain]  Cd Length: 180  Bit Score: 38.40  E-value: 2.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1156048370 107 GHSSVLVEIDGYRVLTDpvwsdrCspsrvvGPHRQHPVPVELSALPALDAVVISHDHYDH-LDMDSIIALT----RSQNA 181
Cdd:cd16272    16 NTSSYLLETGGTRILLD------C------GEGTVYRLLKAGVDPDKLDAIFLSHFHLDHiGGLPTLLFARryggRKKPL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1156048370 182 VFVVPLGVGAHLRG---------WGVSPARVIELD-WDQSHQLGKLTLTCTQARH----------FSGRSIArnttlwas 241
Cdd:cd16272    84 TIYGPKGIKEFLEKllnfpveilPLGFPLEIEELEeGGEVLELGDLKVEAFPVKHsveslgyrieAEGKSIV-------- 155

                         170       180
                  ....*....|....*....|.
gi 1156048370 242 wafagpkhkvfFGGDTGYTKA 262
Cdd:cd16272   156 -----------YSGDTGPCEN 165
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 109-166 2.92e-03

Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; MBL-fold metallo-hydrolase domain; Includes the archaeal cleavage and polyadenylation specificity factors (CPSFs) such as Methanothermobacter thermautotrophicus MTH1203, and Pyrococcus horikoshii PH1404. In addition to the MBL-fold metallo-hydrolase nuclease and the beta-CASP domains, members of this subgroup contain two contiguous KH domains. 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.


Pssm-ID: 293853 [Multi-domain]  Cd Length: 197  Bit Score: 38.59  E-value: 2.92e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1156048370 109 SSVLVEIDGYRVLTDpvwsdrC-----SPSRVVGPHRQHPVPVElsalpALDAVVISHDHYDH 166
Cdd:cd16295    13 SCYLLETGGKRILLD------CglfqgGKELEELNNEPFPFDPK-----EIDAVILTHAHLDH 64
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
103-166 7.78e-03

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 37.35  E-value: 7.78e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1156048370 103 ATWFGHSSVLVEIDGYRVLTDPvwsdrcspsrvvGPHRQHPVPVELSAL----PALDAVVISHDHYDH 166
Cdd:pfam00753   1 LGPGQVNSYLIEGGGGAVLIDT------------GGSAEAALLLLLAALglgpKDIDAVILTHGHFDH 56
Lactamase_B_6 pfam16661
Metallo-beta-lactamase superfamily domain; This family is part of the metallo-beta-lactamase ...
 112-167 8.11e-03

Metallo-beta-lactamase superfamily domain; This family is part of the metallo-beta-lactamase superfamily.


Pssm-ID: 406948  Cd Length: 192  Bit Score: 37.19  E-value: 8.11e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1156048370 112 LVEIDGYRVLTDPVWSDRCSPSRVVGPHRQHpvpvelsaLPALDAVVISHDHYDHL 167
Cdd:pfam16661   1 LLEFDNVRILLDPGWDGSFSYESDLKYLEKI--------LPEVDLILLSHPTLEHL 48
UlaG-like_MBL-fold cd16284
UlaG a putative l-ascorbate-6-P lactonase and related proteins; MBL-fold metallo hydrolase ...
 150-204 8.41e-03

UlaG a putative l-ascorbate-6-P lactonase and related proteins; MBL-fold metallo hydrolase domain; UlaG is essential for L-ascorbate utilization under anaerobic conditions; it is a putative l-ascorbate-6-P lactonase thought to catalyze the hydrolysis of L-ascorbate-6-phosphate to 3-keto-L-gulonate-6-phosphate. 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.


Pssm-ID: 293842  Cd Length: 178  Bit Score: 37.06  E-value: 8.41e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1156048370 150 ALPALDAVVISHDHYDHLDMDSIIALTR--SQNAVFVVPLGVGAHLRGWGVSPARVI 204
Cdd:cd16284    35 AIKQIDAVLATHDHNDHIDVNVAAAVLQncAPDVPFIGPQACVDLWIGWGVPKERCI 91
 
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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