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Conserved domains on  [gi|1278166496|gb|PIX36051|]
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MBL fold metallo-hydrolase, partial [Bacteroidetes bacterium CG_4_8_14_3_um_filter_31_14]

Protein Classification

FprA family A-type flavoprotein( domain architecture ID 11417996)

FprA family A-type flavoprotein contains an MBL fold metallo-hydrolase domain having a binuclear iron center, and a flavodoxin-like domain containing one FMN moiety; similar to Desulfovibrio gigas rubredoxin-oxygen oxidoreductase, which catalyzes the four-electron reduction of one oxygen molecule to two water molecules

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NorV COG0426
Flavorubredoxin [Energy production and conversion];
5-239 2.53e-113

Flavorubredoxin [Energy production and conversion];


:

Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 329.87  E-value: 2.53e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278166496   5 QIINVTNDVKWIGILDESLVTFDVVMETKYGSTYNSYFINAEKKVIIETAKENFTEIYLNKVKQVVTPESIDYIIMNHTE 84
Cdd:COG0426     1 QAVEIAHGVYWVGVLDWDRRLFEGEYPTPRGTTYNSYLIVDEKTALIDTVGESFFEEFLENLSKVIDPKKIDYIIVNHQE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278166496  85 PDHSGCLRHLLKIAPNAVVIGSGNAIRYLQDIVDIP-FKSKQVKNGDTLNLGNKTLKFIAAPNLHWPDTMYSYLVEEKIL 163
Cdd:COG0426    81 PDHSGSLPELLELAPNAKIVCSKKAARFLPHFYGIPdFRFIVVKEGDTLDLGGHTLQFIPAPMLHWPDTMFTYDPEDKIL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1278166496 164 FTCDSFGSHFCKKEMFDDLVPN-FDDAYQYYFDVILKPYSKFMLKAIEKIKQLEIKTICTGHGPILRTYWKKYVDLY 239
Cdd:COG0426   161 FSGDAFGSHGASDELFDDEVDEhLEEEARRYYANIMMPFSKQVLKALKKVRGLDIDMIAPSHGPIWRGNPKEILDWY 237
 
Name Accession Description Interval E-value
NorV COG0426
Flavorubredoxin [Energy production and conversion];
5-239 2.53e-113

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 329.87  E-value: 2.53e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278166496   5 QIINVTNDVKWIGILDESLVTFDVVMETKYGSTYNSYFINAEKKVIIETAKENFTEIYLNKVKQVVTPESIDYIIMNHTE 84
Cdd:COG0426     1 QAVEIAHGVYWVGVLDWDRRLFEGEYPTPRGTTYNSYLIVDEKTALIDTVGESFFEEFLENLSKVIDPKKIDYIIVNHQE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278166496  85 PDHSGCLRHLLKIAPNAVVIGSGNAIRYLQDIVDIP-FKSKQVKNGDTLNLGNKTLKFIAAPNLHWPDTMYSYLVEEKIL 163
Cdd:COG0426    81 PDHSGSLPELLELAPNAKIVCSKKAARFLPHFYGIPdFRFIVVKEGDTLDLGGHTLQFIPAPMLHWPDTMFTYDPEDKIL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1278166496 164 FTCDSFGSHFCKKEMFDDLVPN-FDDAYQYYFDVILKPYSKFMLKAIEKIKQLEIKTICTGHGPILRTYWKKYVDLY 239
Cdd:COG0426   161 FSGDAFGSHGASDELFDDEVDEhLEEEARRYYANIMMPFSKQVLKALKKVRGLDIDMIAPSHGPIWRGNPKEILDWY 237
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 7-239 2.09e-112

catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold metallo-hydrolase domain; FDPs catalyze the reduction of oxygen and/or nitric oxide to water or nitrous oxide respectively. In addition to this N-terminal catalytic domain they contain a C-terminal flavin mononucleotide-binding flavodoxin-like domain. Although some FDPs are able to reduce NO or O2 with similar catalytic efficiencies others are selective for either NO or O2, such as Escherichia coli flavorubredoxin which is selective toward NO and G. intestinalis FDP which is selective toward O2. These enzymes belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. Some members of this subgroup are single domain.


Pssm-ID: 293795 [Multi-domain]  Cd Length: 238  Bit Score: 322.13  E-value: 2.09e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278166496   7 INVTNDVKWIGILDESLVTFDVVMETKYGSTYNSYFINAEKKVIIETAKENFTEIYLNKVKQVVTPESIDYIIMNHTEPD 86
Cdd:cd07709     1 VEIADDIYWVGVNDWDLRLFEGEYPTPRGTSYNSYLIKDEKTALIDTVKEPFFDEFLENLEEVIDPRKIDYIVVNHQEPD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278166496  87 HSGCLRHLLKIAPNAVVIGSGNAIRYLQDI-VDIPFKSKQVKNGDTLNLGNKTLKFIAAPNLHWPDTMYSYLVEEKILFT 165
Cdd:cd07709    81 HSGSLPELLELAPNAKIVCSKKAARFLKHFyPGIDERFVVVKDGDTLDLGKHTLKFIPAPMLHWPDTMVTYDPEDKILFS 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1278166496 166 CDSFGSHFCKKEMFDDLVPNFDDAYQYYFDVILKPYSKFMLKAIEKIKQLEIKTICTGHGPILRTYWKKYVDLY 239
Cdd:cd07709   161 GDAFGAHGASGELFDDEVEDYLEEARRYYANIMGPFSKQVRKALEKLEALDIKMIAPSHGPIWRKDPGEIIDLY 234
PRK11921 PRK11921
anaerobic nitric oxide reductase flavorubredoxin;
8-229 1.42e-60

anaerobic nitric oxide reductase flavorubredoxin;


Pssm-ID: 237023 [Multi-domain]  Cd Length: 394  Bit Score: 195.30  E-value: 1.42e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278166496   8 NVTNDVKWIGILDESLVTFD-VVMETKYGSTYNSYFINAEKKVIIETAKENFTEIYLNKVKQVVTPESIDYIIMNHTEPD 86
Cdd:PRK11921    2 KINDNVTWVGKIDWELRKFHgEEYSTHRGSSYNSYLIKDEKTVLIDTVWQPFAKEFVENLKKEIDLDKIDYIVANHGEID 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278166496  87 HSGCLRHLLKIAPNAVVIGSGNAIRYLQDIVDIPFKSKQVKNGDTLNLGNKTLKFIAAPNLHWPDTMYSYLVEEKILFTC 166
Cdd:PRK11921   82 HSGALPELMKEIPDTPIYCTKNGAKSLKGHYHQDWNFVVVKTGDRLEIGSNELIFIEAPMLHWPDSMFTYLTGDNILFSN 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1278166496 167 DSFGSHFCKKEMFDDLVPN---FDDAYQYYFDvILKPYSKFMLKAIEKIKQLE--IKTICTGHGPILR 229
Cdd:PRK11921  162 DAFGQHYASELMYNDLVDQgelYQEAIKYYAN-ILTPFSPLVIKKIEEILSLNlpVDMICPSHGVIWR 228
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 39-224 1.13e-23

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: 93.39  E-value: 1.13e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278166496   39 NSYFINAEKKVIIETAKENFTEIYLNKVKQVvTPESIDYIIMNHTEPDHSGCLRHLLKiAPNAVVIGSGNAIRYLQDIVD 118
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAEDLLAELKKL-GPKKIDAIILTHGHPDHIGGLPELLE-APGAPVYAPEGTAELLKDLLA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278166496  119 IPFKSKQ----------VKNGDTLNLGNKTLKFIAAPNlHWPDTMYSYLVEEKILFTCDSFGSHFCKKEMFDdlvPNFDD 188
Cdd:smart00849  79 LLGELGAeaepappdrtLKDGDELDLGGGELEVIHTPG-HTPGSIVLYLPEGKILFTGDLLFAGGDGRTLVD---GGDAA 154

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1278166496  189 AYQYyfdvilkpyskfmLKAIEKIKQLEIKTICTGH 224
Cdd:smart00849 155 ASDA-------------LESLLKLLKLLPKLVVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
39-224 1.04e-12

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 64.70  E-value: 1.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278166496  39 NSYFINAEKK-VIIETAKENFTEIYLNKVKQVVTPESIDYIIMNHTEPDHSGCLRHLLKIAPNAVVIGSGNAIRYLQDIV 117
Cdd:pfam00753   7 NSYLIEGGGGaVLIDTGGSAEAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARELLDEEL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278166496 118 DIPFKSKQVK--------------NGDTLNLGNKTLKFIAAPNlHWPDTMYSYLVEEKILFTCDSFGSHFCkkemfdDLV 183
Cdd:pfam00753  87 GLAASRLGLPgppvvplppdvvleEGDGILGGGLGLLVTHGPG-HGPGHVVVYYGGGKVLFTGDLLFAGEI------GRL 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1278166496 184 PNFDDAYQYYFDVILKPYskfmLKAIEKIKQLEIKTICTGH 224
Cdd:pfam00753 160 DLPLGGLLVLHPSSAESS----LESLLKLAKLKAAVIVPGH 196
 
Name Accession Description Interval E-value
NorV COG0426
Flavorubredoxin [Energy production and conversion];
5-239 2.53e-113

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 329.87  E-value: 2.53e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278166496   5 QIINVTNDVKWIGILDESLVTFDVVMETKYGSTYNSYFINAEKKVIIETAKENFTEIYLNKVKQVVTPESIDYIIMNHTE 84
Cdd:COG0426     1 QAVEIAHGVYWVGVLDWDRRLFEGEYPTPRGTTYNSYLIVDEKTALIDTVGESFFEEFLENLSKVIDPKKIDYIIVNHQE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278166496  85 PDHSGCLRHLLKIAPNAVVIGSGNAIRYLQDIVDIP-FKSKQVKNGDTLNLGNKTLKFIAAPNLHWPDTMYSYLVEEKIL 163
Cdd:COG0426    81 PDHSGSLPELLELAPNAKIVCSKKAARFLPHFYGIPdFRFIVVKEGDTLDLGGHTLQFIPAPMLHWPDTMFTYDPEDKIL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1278166496 164 FTCDSFGSHFCKKEMFDDLVPN-FDDAYQYYFDVILKPYSKFMLKAIEKIKQLEIKTICTGHGPILRTYWKKYVDLY 239
Cdd:COG0426   161 FSGDAFGSHGASDELFDDEVDEhLEEEARRYYANIMMPFSKQVLKALKKVRGLDIDMIAPSHGPIWRGNPKEILDWY 237
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 7-239 2.09e-112

catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold metallo-hydrolase domain; FDPs catalyze the reduction of oxygen and/or nitric oxide to water or nitrous oxide respectively. In addition to this N-terminal catalytic domain they contain a C-terminal flavin mononucleotide-binding flavodoxin-like domain. Although some FDPs are able to reduce NO or O2 with similar catalytic efficiencies others are selective for either NO or O2, such as Escherichia coli flavorubredoxin which is selective toward NO and G. intestinalis FDP which is selective toward O2. These enzymes belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. Some members of this subgroup are single domain.


Pssm-ID: 293795 [Multi-domain]  Cd Length: 238  Bit Score: 322.13  E-value: 2.09e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278166496   7 INVTNDVKWIGILDESLVTFDVVMETKYGSTYNSYFINAEKKVIIETAKENFTEIYLNKVKQVVTPESIDYIIMNHTEPD 86
Cdd:cd07709     1 VEIADDIYWVGVNDWDLRLFEGEYPTPRGTSYNSYLIKDEKTALIDTVKEPFFDEFLENLEEVIDPRKIDYIVVNHQEPD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278166496  87 HSGCLRHLLKIAPNAVVIGSGNAIRYLQDI-VDIPFKSKQVKNGDTLNLGNKTLKFIAAPNLHWPDTMYSYLVEEKILFT 165
Cdd:cd07709    81 HSGSLPELLELAPNAKIVCSKKAARFLKHFyPGIDERFVVVKDGDTLDLGKHTLKFIPAPMLHWPDTMVTYDPEDKILFS 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1278166496 166 CDSFGSHFCKKEMFDDLVPNFDDAYQYYFDVILKPYSKFMLKAIEKIKQLEIKTICTGHGPILRTYWKKYVDLY 239
Cdd:cd07709   161 GDAFGAHGASGELFDDEVEDYLEEARRYYANIMGPFSKQVRKALEKLEALDIKMIAPSHGPIWRKDPGEIIDLY 234
PRK11921 PRK11921
anaerobic nitric oxide reductase flavorubredoxin;
8-229 1.42e-60

anaerobic nitric oxide reductase flavorubredoxin;


Pssm-ID: 237023 [Multi-domain]  Cd Length: 394  Bit Score: 195.30  E-value: 1.42e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278166496   8 NVTNDVKWIGILDESLVTFD-VVMETKYGSTYNSYFINAEKKVIIETAKENFTEIYLNKVKQVVTPESIDYIIMNHTEPD 86
Cdd:PRK11921    2 KINDNVTWVGKIDWELRKFHgEEYSTHRGSSYNSYLIKDEKTVLIDTVWQPFAKEFVENLKKEIDLDKIDYIVANHGEID 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278166496  87 HSGCLRHLLKIAPNAVVIGSGNAIRYLQDIVDIPFKSKQVKNGDTLNLGNKTLKFIAAPNLHWPDTMYSYLVEEKILFTC 166
Cdd:PRK11921   82 HSGALPELMKEIPDTPIYCTKNGAKSLKGHYHQDWNFVVVKTGDRLEIGSNELIFIEAPMLHWPDSMFTYLTGDNILFSN 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1278166496 167 DSFGSHFCKKEMFDDLVPN---FDDAYQYYFDvILKPYSKFMLKAIEKIKQLE--IKTICTGHGPILR 229
Cdd:PRK11921  162 DAFGQHYASELMYNDLVDQgelYQEAIKYYAN-ILTPFSPLVIKKIEEILSLNlpVDMICPSHGVIWR 228
PRK05452 PRK05452
anaerobic nitric oxide reductase flavorubredoxin; Provisional
 7-229 3.48e-48

anaerobic nitric oxide reductase flavorubredoxin; Provisional


Pssm-ID: 235475 [Multi-domain]  Cd Length: 479  Bit Score: 164.93  E-value: 3.48e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278166496   7 INVTNDVKWIGILDESLVTFDvvmETKY----GSTYNSYFINAEKKVIIETAKENFTEIYLNKVKQVVTPESIDYIIMNH 82
Cdd:PRK05452    3 IHVKNNIHWVGQRDWEVRDFH---GTEYktlrGSSYNSYLIREEKNVLIDTVDHKFSREFVQNLRNEIDLADIDYIVINH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278166496  83 TEPDHSGCLRHLLKIAPNAVVIGSGNAIRYLQDIVDIP-FKSKQVKNGDTLNLGN-KTLKFIAAPNLHWPDTMYSYLVEE 160
Cdd:PRK05452   80 AEEDHAGALTELMAQIPDTPIYCTANAIDSINGHHHHPeWNFNVVKTGDTLDIGNgKQLIFVETPMLHWPDSMMTYLTGD 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1278166496 161 KILFTCDSFGSHFCKKEMFDDLVPN---FDDAYQYYFDvILKPYSKFMLKAIEKIK--QLEIKTICTGHGPILR 229
Cdd:PRK05452  160 AVLFSNDAFGQHYCDEHLFNDEVDQtelFEQCQRYYAN-ILTPFSRLVTPKITEILgfNLPVDMIATSHGVVWR 232
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 39-224 1.13e-23

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: 93.39  E-value: 1.13e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278166496   39 NSYFINAEKKVIIETAKENFTEIYLNKVKQVvTPESIDYIIMNHTEPDHSGCLRHLLKiAPNAVVIGSGNAIRYLQDIVD 118
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAEDLLAELKKL-GPKKIDAIILTHGHPDHIGGLPELLE-APGAPVYAPEGTAELLKDLLA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278166496  119 IPFKSKQ----------VKNGDTLNLGNKTLKFIAAPNlHWPDTMYSYLVEEKILFTCDSFGSHFCKKEMFDdlvPNFDD 188
Cdd:smart00849  79 LLGELGAeaepappdrtLKDGDELDLGGGELEVIHTPG-HTPGSIVLYLPEGKILFTGDLLFAGGDGRTLVD---GGDAA 154

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1278166496  189 AYQYyfdvilkpyskfmLKAIEKIKQLEIKTICTGH 224
Cdd:smart00849 155 ASDA-------------LESLLKLLKLLPKLVVPGH 177
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 39-237 2.03e-15

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: 72.42  E-value: 2.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278166496  39 NSYFINAEKK-VIIET-AKENFTEIYLNKVKQVvtPESIDYIIMNHTEPDHSGCLRHLLKiAPNAVVIGSGNAIRYLQDI 116
Cdd:COG0491    16 NSYLIVGGDGaVLIDTgLGPADAEALLAALAAL--GLDIKAVLLTHLHPDHVGGLAALAE-AFGAPVYAHAAEAEALEAP 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278166496 117 VDIPFKSKQ-------VKNGDTLNLGNKTLKFIAAPNlHWPDTMYSYLVEEKILFTCDSFGSHFCKKEMFDDlvPNFDDa 189
Cdd:COG0491    93 AAGALFGREpvppdrtLEDGDTLELGGPGLEVIHTPG-HTPGHVSFYVPDEKVLFTGDALFSGGVGRPDLPD--GDLAQ- 168

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1278166496 190 yqyyfdvilkpyskfMLKAIEKIKQLEIKTICTGHGPILRTYWKKYVD 237
Cdd:COG0491   169 ---------------WLASLERLLALPPDLVIPGHGPPTTAEAIDYLE 201
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 40-224 1.00e-13

uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo hydrolase domain; This subgroup includes the uncharacterized Sulfolobus tokodaii ST1585 protein. 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: 293812 [Multi-domain]  Cd Length: 215  Bit Score: 67.90  E-value: 1.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278166496  40 SYFINAEKK-VIIETAKENFTEIYLNKVKQV-VTPESIDYIIMNHTEPDHSGCLRHLLKIAPNAVVI------------- 104
Cdd:cd07726    18 SYLLDGEGRpALIDTGPSSSVPRLLAALEALgIAPEDVDYIILTHIHLDHAGGAGLLAEALPNAKVYvhprgarhlidps 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278166496 105 ----GS----GNAI-RYLQDIVDIPFKS-KQVKNGDTLNLGNKTLKFIAAP---NLHwpdtmYSYLVEE-KILFTCDSFG 170
Cdd:cd07726    98 klwaSAravyGDEAdRLGGEILPVPEERvIVLEDGETLDLGGRTLEVIDTPghaPHH-----LSFLDEEsDGLFTGDAAG 172

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1278166496 171 SHFckkemfddlvPNFDDAYQYY-----FDVILkpyskfMLKAIEKIKQLEIKTICTGH 224
Cdd:cd07726   173 VRY----------PELDVVGPPStpppdFDPEA------WLESLDRLLSLKPERIYLTH 215
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
39-224 1.04e-12

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 64.70  E-value: 1.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278166496  39 NSYFINAEKK-VIIETAKENFTEIYLNKVKQVVTPESIDYIIMNHTEPDHSGCLRHLLKIAPNAVVIGSGNAIRYLQDIV 117
Cdd:pfam00753   7 NSYLIEGGGGaVLIDTGGSAEAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARELLDEEL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278166496 118 DIPFKSKQVK--------------NGDTLNLGNKTLKFIAAPNlHWPDTMYSYLVEEKILFTCDSFGSHFCkkemfdDLV 183
Cdd:pfam00753  87 GLAASRLGLPgppvvplppdvvleEGDGILGGGLGLLVTHGPG-HGPGHVVVYYGGGKVLFTGDLLFAGEI------GRL 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1278166496 184 PNFDDAYQYYFDVILKPYskfmLKAIEKIKQLEIKTICTGH 224
Cdd:pfam00753 160 DLPLGGLLVLHPSSAESS----LESLLKLAKLKAAVIVPGH 196
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 39-165 3.33e-10

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: 57.68  E-value: 3.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278166496  39 NSYFINAEKK--VIIETAKENFTEIyLNKVKQvvTPESIDYIIMNHTEPDHSGCLRHLLKiAPNAVVIGS---------- 106
Cdd:cd06262    11 NCYLVSDEEGeaILIDPGAGALEKI-LEAIEE--LGLKIKAILLTHGHFDHIGGLAELKE-APGAPVYIHeadaelledp 86

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1278166496 107 -GNAIRYLQDIVDIPFKSKQVKNGDTLNLGNKTLKFIAAPNlHWPDTMySYLVE-EKILFT 165
Cdd:cd06262    87 eLNLAFFGGGPLPPPEPDILLEDGDTIELGGLELEVIHTPG-HTPGSV-CFYIEeEGVLFT 145
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 39-227 1.92e-09

uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized Thermus thermophilus TTHA1429 and related proteins. 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: 293811 [Multi-domain]  Cd Length: 184  Bit Score: 55.38  E-value: 1.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278166496  39 NSYFI-NAEKKVIIETA---KENFTEIYLNKVKQVVTPESIDYIIMNHTEPDHSGCLRhllKIAPnavvigsgnaiRYLQ 114
Cdd:cd07725    16 NVYLLrDGDETTLIDTGlatEEDAEALWEGLKELGLKPSDIDRVLLTHHHPDHIGLAG---KLQE-----------KSGA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278166496 115 DIVDIPFKSkqVKNGDTLNLGNKTLKFIAAPNlHWPDTMYSYLVEEKILFTCDSFGShfckkemfdDLVPNfddayqyyf 194
Cdd:cd07725    82 TVYILDVTP--VKDGDKIDLGGLRLKVIETPG-HTPGHIVLYDEDRRELFVGDAVLP---------KITPN--------- 140

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1278166496 195 dVILKPYSKFM-----LKAIEKIKQLEIKTICTGHG-PI 227
Cdd:cd07725   141 -VSLWAVRVEDplgayLESLDKLEKLDVDLAYPGHGgPI 178
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 74-167 1.56e-08

hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione hydrolase (EC 3.1.2.6, also known as, glyoxalase II; S-2-hydroxylacylglutathione hydrolase; hydroxyacylglutathione hydrolase; acetoacetylglutathione hydrolase). In the second step of the glycoxlase system this enzyme hydrolyzes S-d-lactoylglutathione to d-lactate and regenerates glutathione in the process. It has broad substrate specificity for glutathione thiol esters, hydrolyzing a number of these species to their corresponding carboxylic acids and reduced glutathione. It appears to hydrolyze 2-hydroxy thiol esters with greatest efficiency. It belongs to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293809 [Multi-domain]  Cd Length: 165  Bit Score: 52.46  E-value: 1.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278166496  74 SIDYIIMNHTEPDHSGCLRHLLKIAPNAVVIGSGNAirylqdivDIPFKSKQVKNGDTLNLGNKTLKFIAAPNlHWPDTM 153
Cdd:cd07723    43 TLTAILTTHHHWDHTGGNAELKALFPDAPVYGPAED--------RIPGLDHPVKDGDEIKLGGLEVKVLHTPG-HTLGHI 113

                          90
                  ....*....|....*
gi 1278166496 154 ySYLVE-EKILFTCD 167
Cdd:cd07723   114 -CYYVPdEPALFTGD 127
metallo-hydrolase-like_MBL-fold cd16276
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 37-228 2.91e-08

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase 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, 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: 293834 [Multi-domain]  Cd Length: 188  Bit Score: 52.20  E-value: 2.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278166496  37 TYNSYFINAEKKVIIETAKENFTEIYLNKVKQVvTPESIDYIIMNHTEPDHSGClRHLLKiAPNAVVIGSGNAIRYLQDI 116
Cdd:cd16276     9 GYQSMFLVTDKGVIVVDAPPSLGENLLAAIRKV-TDKPVTHVVYSHNHADHIGG-ASIFK-DEGATIIAHEATAELLKRN 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278166496 117 VD--IPFKSKQVKNGDTLNLGNKTLKFIAAPNLHWPDTMYSYLVEEKILFTCDSFgshfckkemFDDLVP--NFDDAyqy 192
Cdd:cd16276    86 PDpkRPVPTVTFDDEYTLEVGGQTLELSYFGPNHGPGNIVIYLPKQKVLMAVDLI---------NPGWVPffNFAGS--- 153

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1278166496 193 yFDVilkpysKFMLKAIEKIKQLEIKTICTGHGPIL 228
Cdd:cd16276   154 -EDI------PGYIEALDELLEYDFDTFVGGHGNRL 182
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 39-229 7.32e-08

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase 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, 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: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 51.03  E-value: 7.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278166496  39 NSYFINAEKKVI-IET-AKENFTEIYLNKVKQVvTPESIDYIIMNHTEPDHSGCLRHLLkiAPNAVVIGSGNAIRYLQ-- 114
Cdd:cd16282    16 NIGFIVGDDGVVvIDTgASPRLARALLAAIRKV-TDKPVRYVVNTHYHGDHTLGNAAFA--DAGAPIIAHENTREELAar 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278166496 115 ----------------DIVDIPFKSKQVKNGDTLNLGNKTLKFIAAPNLHWPDTMYSYLVEEKILFTCDSFgshfckkem 178
Cdd:cd16282    93 geaylelmrrlggdamAGTELVLPDRTFDDGLTLDLGGRTVELIHLGPAHTPGDLVVWLPEEGVLFAGDLV--------- 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1278166496 179 FDDLVPNFDDAYqyyfdvilkpySKFMLKAIEKIKQLEIKTICTGHGPILR 229
Cdd:cd16282   164 FNGRIPFLPDGS-----------LAGWIAALDRLLALDATVVVPGHGPVGD 203
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 74-167 5.22e-05

uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized Thermus thermophilus TTHA1623 and related proteins. 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. This family includes homologs present in a wide range of bacteria and archaea and some eukaryota. Members of the MBL-fold metallo-hydrolase superfamily exhibit a variety of active site metallo-chemistry, TTHA1623 exhibiting a uniquely shaped putative substrate-binding pocket with a glyoxalase II-type metal-coordination mode.


Pssm-ID: 293877 [Multi-domain]  Cd Length: 204  Bit Score: 42.72  E-value: 5.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278166496  74 SIDYIIMNHTEPDHSGCLRHLLKiAPNAVVI-----------GSGNAIRYLQDIVDIPFKSKQVKNGDTLNLGNKTLKFI 142
Cdd:cd16322    46 TLLYILLTHAHFDHVGGVADLRR-HPGAPVYlhpddlplyeaADLGAKAFGLGIEPLPPPDRLLEDGQTLTLGGLEFKVL 124

                          90       100
                  ....*....|....*....|....*
gi 1278166496 143 AAPNlHWPDTMYSYLVEEKILFTCD 167
Cdd:cd16322   125 HTPG-HSPGHVCFYVEEEGLLFSGD 148
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 36-168 6.02e-05

ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; MBL-fold metallo-hydrolase domain; Persulfide dioxygenase (PDO, also known as sulfur dioxygenase, SDO, EC 1.13.11.18) is a non-heme iron-dependent oxygenase which catalyzes the oxidation of glutathione persulfide to glutathione and persulfite in the mitochondria. Mutations in ethe1 (the human PDO gene) are responsible for a rare autosomal recessive metabolic disorder called ethylmalonic encephalopathy. Arabidopsis thaliana ETHE1 is essential for embryo and endosperm development. Bacterial ETHE1-type PDOs are also called Type 1 PDOs. Type II PDOs (also called PDOAs), are mainly proteobacterial. These enzymes 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: 293810 [Multi-domain]  Cd Length: 177  Bit Score: 42.39  E-value: 6.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278166496  36 STYnSYFI--NAEKK-VIIETAKEnFTEIYLNKVKQ--VvtpeSIDYIIMNHTEPDH-SGCLRhlLKIAPNA-VVIGSGn 108
Cdd:cd07724    11 GTL-SYLVgdPETGEaAVIDPVRD-SVDRYLDLAAElgL----KITYVLETHVHADHvSGARE--LAERTGApIVIGEG- 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1278166496 109 airylqdiVDIPFKSKQVKNGDTLNLGNKTLKFIAAPNlHWPDtMYSYLVEEKI-LFTCDS 168
Cdd:cd07724    82 --------APASFFDRLLKDGDVLELGNLTLEVLHTPG-HTPE-SVSYLVGDPDaVFTGDT 132
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 70-104 9.98e-05

quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl Homoserine Lactones (also known as AHLs) are signal molecules which coordinate gene expression in quorum sensing, in many Gram-negative bacteria. Quorum-quenching N-acyl-homoserine lactonase (also known as AHL lactonase, N-acyl-L-homoserine lactone hydrolase, EC 3.1.1.81) catalyzes the hydrolysis and opening of the homoserine lactone rings of AHLs, a reaction that can block quorum sensing. These enzymes 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: 293815 [Multi-domain]  Cd Length: 238  Bit Score: 42.20  E-value: 9.98e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1278166496  70 VTPESIDYIIMNHTEPDHSGCLRHLlkiaPNAVVI 104
Cdd:cd07729    84 LDPEDIDYVILSHLHFDHAGGLDLF----PNATII 114
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 46-119 8.70e-03

uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized human MBLAC1 and related proteins. 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: 293797 [Multi-domain]  Cd Length: 190  Bit Score: 36.02  E-value: 8.70e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1278166496  46 EKKVIIETAKENFTEIYLNKVKQV-VTPESIDYIIMNHTEPDHSGCLRhllkIAPNAVVIGSGNAIRYLQDIVDI 119
Cdd:cd07711    31 GKNILVDTGTPWDRDLLLKALAEHgLSPEDIDYVVLTHGHPDHIGNLN----LFPNATVIVGWDICGDSYDDHSL 101
 
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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