NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1542512438|gb|RTW08523|]
View 

alkyl/aryl-sulfatase [Pseudomonas aeruginosa]

Protein Classification

alkyl/aryl-sulfatase( domain architecture ID 11449593)

alkyl/aryl-sulfatase is a sulfohydrolase that allows the use of primary or secondary sulfates such as SDS as a sole sulfur source

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
BDS1 COG2015
Alkyl sulfatase BDS1 and related hydrolases, metallo-beta-lactamase superfamily [Secondary ...
 21-650 0e+00

Alkyl sulfatase BDS1 and related hydrolases, metallo-beta-lactamase superfamily [Secondary metabolites biosynthesis, transport and catabolism];


:

Pssm-ID: 441618 [Multi-domain]  Cd Length: 629  Bit Score: 1067.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542512438  21 TAPKPPSAFTVEAQRRVEAELPFADRADFERAERGLIRRPERLLIRNPDGSVAWQLGGYDFLLDGKPRDSINPSLQRQAL 100
Cdd:COG2015     1 TAPKPASEATAAANAAVAKSLPFEDTQDFEDARRGFIATLDDLVIRNADGRVVWDLDAYDFLEDGDAPDTVNPSLWRQAQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542512438 101 LNLKYGLFEVAEGIYQVRGFDLANITFIRGDSGWIVVDTLTTPATARAAYELVSRELGERPIRTVIYSHAHADHFGGVRG 180
Cdd:COG2015    81 LNNIHGLFEVTDGIYQVRGFDLANMTFIEGDTGWIVIDPLTSVETAAAALALYRKHLGDRPVKAVIYTHSHVDHFGGVRG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542512438 181 LVEPQQVASGAVQIIAPAGFMEAAIKENVLAGNAMMRRATYQYGTQLPKGPQGQVDMAIGKGLARGPLSLLAPTRLIEGE 260
Cdd:COG2015   161 VVDEEDVKSGKVPIIAPEGFMEHAVSENVYAGNAMGRRAQYMYGTLLPRGPKGQVDAGLGKTTSTGTVGLIPPTDTITKT 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542512438 261 GEDLVLDGVPFTFQNTPGTESPAEMNIWLPRQKALLMAENVVGTLHNLYTLRGAEVRDALGWSKYINQALHRFGRQAEVM 340
Cdd:COG2015   241 GEELTIDGVRMEFQLTPGTEAPAEMNFYFPDFKALCMAENATHTLHNLYTLRGAQVRDALAWSKYLDEALELFGDRAEVM 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542512438 341 FAVHNWPRWGNAEIVEVLEKQRDLYGYLHDQTLHLANQGVTIGQVHNRLRLPPSLDQEWYDRGYHGSVSHNARAVLNRYL 420
Cdd:COG2015   321 FASHHWPTWGNERIVEYLTNQRDAYKYLHDQTLRLANQGYTPDEIAEVIKLPPSLAKDWYTRGYYGSVSHNVKAVYQRYL 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542512438 421 GYYDGNPATLDPLSPEDSAGRYVEYMGGAERLLEQARASYARGEYRWVVEVVNRLVFAEPDNRAARELQADALEQLGYQA 500
Cdd:COG2015   401 GWYDGNPANLNPLPPEEAAKRYVEAMGGADAVLAKARAAFDAGDYRWAAELLNHLVFADPDNQEARELLADALEQLGYQA 480

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542512438 501 ENAGWRNSYLSAAYELRHGVPRDqPTMKAGSADALAAMDTGLLFDYLGVRLDAGAAEGKALSINLRLPDIGENYLLELKN 580
Cdd:COG2015   481 ESATWRNFYLTGALELRHGVPKS-PTPNTASPDMIAAMPTEMLFDYLAVRLDGPKAAGKDLTINLIFTDTGEKYLLELRN 559

                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542512438 581 SHLNNLRGVQSEDAGQTVSIDRADLNRLLLKEVSAVRLVFEGKLKSSGNPLLLGQLFGMLGDFDFWFDIV 650
Cdd:COG2015   560 GVLTYRKGPQADDADATLTLTRADLLALLLGKTTLDDLVASGGAKVEGDAAALARLLGLLDPFDPDFNIV 629
 
Name Accession Description Interval E-value
BDS1 COG2015
Alkyl sulfatase BDS1 and related hydrolases, metallo-beta-lactamase superfamily [Secondary ...
 21-650 0e+00

Alkyl sulfatase BDS1 and related hydrolases, metallo-beta-lactamase superfamily [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441618 [Multi-domain]  Cd Length: 629  Bit Score: 1067.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542512438  21 TAPKPPSAFTVEAQRRVEAELPFADRADFERAERGLIRRPERLLIRNPDGSVAWQLGGYDFLLDGKPRDSINPSLQRQAL 100
Cdd:COG2015     1 TAPKPASEATAAANAAVAKSLPFEDTQDFEDARRGFIATLDDLVIRNADGRVVWDLDAYDFLEDGDAPDTVNPSLWRQAQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542512438 101 LNLKYGLFEVAEGIYQVRGFDLANITFIRGDSGWIVVDTLTTPATARAAYELVSRELGERPIRTVIYSHAHADHFGGVRG 180
Cdd:COG2015    81 LNNIHGLFEVTDGIYQVRGFDLANMTFIEGDTGWIVIDPLTSVETAAAALALYRKHLGDRPVKAVIYTHSHVDHFGGVRG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542512438 181 LVEPQQVASGAVQIIAPAGFMEAAIKENVLAGNAMMRRATYQYGTQLPKGPQGQVDMAIGKGLARGPLSLLAPTRLIEGE 260
Cdd:COG2015   161 VVDEEDVKSGKVPIIAPEGFMEHAVSENVYAGNAMGRRAQYMYGTLLPRGPKGQVDAGLGKTTSTGTVGLIPPTDTITKT 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542512438 261 GEDLVLDGVPFTFQNTPGTESPAEMNIWLPRQKALLMAENVVGTLHNLYTLRGAEVRDALGWSKYINQALHRFGRQAEVM 340
Cdd:COG2015   241 GEELTIDGVRMEFQLTPGTEAPAEMNFYFPDFKALCMAENATHTLHNLYTLRGAQVRDALAWSKYLDEALELFGDRAEVM 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542512438 341 FAVHNWPRWGNAEIVEVLEKQRDLYGYLHDQTLHLANQGVTIGQVHNRLRLPPSLDQEWYDRGYHGSVSHNARAVLNRYL 420
Cdd:COG2015   321 FASHHWPTWGNERIVEYLTNQRDAYKYLHDQTLRLANQGYTPDEIAEVIKLPPSLAKDWYTRGYYGSVSHNVKAVYQRYL 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542512438 421 GYYDGNPATLDPLSPEDSAGRYVEYMGGAERLLEQARASYARGEYRWVVEVVNRLVFAEPDNRAARELQADALEQLGYQA 500
Cdd:COG2015   401 GWYDGNPANLNPLPPEEAAKRYVEAMGGADAVLAKARAAFDAGDYRWAAELLNHLVFADPDNQEARELLADALEQLGYQA 480

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542512438 501 ENAGWRNSYLSAAYELRHGVPRDqPTMKAGSADALAAMDTGLLFDYLGVRLDAGAAEGKALSINLRLPDIGENYLLELKN 580
Cdd:COG2015   481 ESATWRNFYLTGALELRHGVPKS-PTPNTASPDMIAAMPTEMLFDYLAVRLDGPKAAGKDLTINLIFTDTGEKYLLELRN 559

                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542512438 581 SHLNNLRGVQSEDAGQTVSIDRADLNRLLLKEVSAVRLVFEGKLKSSGNPLLLGQLFGMLGDFDFWFDIV 650
Cdd:COG2015   560 GVLTYRKGPQADDADATLTLTRADLLALLLGKTTLDDLVASGGAKVEGDAAALARLLGLLDPFDPDFNIV 629
arylsulfatase_Sdsa1-like_MBL-fold cd07710
Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and ...
 106-350 9.73e-134

Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and related proteins; MBL-fold metallo-hydrolase domain; Arylsulfatase (also known as aryl-sulfate sulfohydrolase, EC 3.1.6.1). Pseudomonas aeruginosa SdsA1 is a secreted SDS hydrolase that allows the bacterium to use primary sulfates such as the detergent SDS common in commercial personal hygiene products as a sole carbon or sulfur source. Pseudomonas inverting secondary alkylsulfatase 1 (Pisa1) is specific for secondary alkyl sulfates. 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: 293796 [Multi-domain]  Cd Length: 239  Bit Score: 392.25  E-value: 9.73e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542512438 106 GLFEVAEGIYQVRGFDLANITFIRGDSGWIVVDTLTTPATARAAYELVSRELGERPIRTVIYSHAHADHFGGVRGLVEPQ 185
Cdd:cd07710     1 GLFEVTDGVYQVRGYDLSNMTFIEGDTGLIIIDTLESAEAAKAALELFRKHTGDKPVKAIIYTHSHPDHFGGAGGFVEEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542512438 186 QvaSGAVQIIAPAGFMEAAIKENVLAGNAMMRRATYQYGTQLPKGPQGQVDMAIGKGLARGPLSLLAPTRLIEGEGEDLV 265
Cdd:cd07710    81 D--SGKVPIIAPEGFMEEAVSENVLAGNAMSRRAAYQFGALLPKGEKGQVGAGLGPGLSTGTVGFIPPTITITETGETLT 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542512438 266 LDGVPFTFQNTPGtESPAEMNIWLPRQKALLMAENVVGTLHNLYTLRGAEVRDALGWSKYINQALhrfGRQAEVMFAVHN 345
Cdd:cd07710   159 IDGVELEFQHAPG-EAPDEMMVWLPDYKVLFCADNVYHTFPNLYTLRGAKYRDALAWAKSLDEAI---SLKAEVLFPSHT 234


                  ....*
gi 1542512438 346 WPRWG 350
Cdd:cd07710   235 WPVWG 239
Alkyl_sulf_dimr pfam14863
Alkyl sulfatase dimerization; This domain is found in alkyl sulfatases such as the Pseudomonas ...
 381-516 8.40e-75

Alkyl sulfatase dimerization; This domain is found in alkyl sulfatases such as the Pseudomonas aeruginosa SDS hydrolase, where it acts as a dimerization domain


Pssm-ID: 464351  Cd Length: 136  Bit Score: 236.22  E-value: 8.40e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542512438 381 TIGQVHNRLRLPPSLDQEWYDRGYHGSVSHNARAVLNRYLGYYDGNPATLDPLSPEDSAGRYVEYMGGAERLLEQARASY 460
Cdd:pfam14863   1 TPDEIAEELKLPPSLAEAWYLRGYYGSVSHNVRAIYQRYLGWFDGNPAHLNPLPPVEAAKRYVELMGGADAVLAKAREAF 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1542512438 461 ARGEYRWVVEVVNRLVFAEPDNRAARELQADALEQLGYQAENAGWRNSYLSAAYEL 516
Cdd:pfam14863  81 DAGDYRWAAELLNHLVFADPDNQEARELLADALEQLGYQAESATWRNFYLTGALEL 136
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 124-330 2.74e-16

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: 77.21  E-value: 2.74e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542512438  124 NITFIRGDSGWIVVDTLTTPATARAAYElvsRELGERPIRTVIYSHAHADHFGGVRGLVEpqqvASGAvQIIAPAGFMEA 203
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAEDLLAEL---KKLGPKKIDAIILTHGHPDHIGGLPELLE----APGA-PVYAPEGTAEL 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542512438  204 AIKENVLAGNAMMRRATYqygtqlpkgpqgqvdmaigkglargplsllAPTRLIEgEGEDLVLDGVPFTFQNTPGtESPA 283
Cdd:smart00849  73 LKDLLALLGELGAEAEPA------------------------------PPDRTLK-DGDELDLGGGELEVIHTPG-HTPG 120

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1542512438  284 EMNIWLPRQKALLMAENVVGTLHNLYTLRGAEVRDALGWSKYINQAL 330
Cdd:smart00849 121 SIVLYLPEGKILFTGDLLFAGGDGRTLVDGGDAAASDALESLLKLLK 167
 
Name Accession Description Interval E-value
BDS1 COG2015
Alkyl sulfatase BDS1 and related hydrolases, metallo-beta-lactamase superfamily [Secondary ...
 21-650 0e+00

Alkyl sulfatase BDS1 and related hydrolases, metallo-beta-lactamase superfamily [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441618 [Multi-domain]  Cd Length: 629  Bit Score: 1067.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542512438  21 TAPKPPSAFTVEAQRRVEAELPFADRADFERAERGLIRRPERLLIRNPDGSVAWQLGGYDFLLDGKPRDSINPSLQRQAL 100
Cdd:COG2015     1 TAPKPASEATAAANAAVAKSLPFEDTQDFEDARRGFIATLDDLVIRNADGRVVWDLDAYDFLEDGDAPDTVNPSLWRQAQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542512438 101 LNLKYGLFEVAEGIYQVRGFDLANITFIRGDSGWIVVDTLTTPATARAAYELVSRELGERPIRTVIYSHAHADHFGGVRG 180
Cdd:COG2015    81 LNNIHGLFEVTDGIYQVRGFDLANMTFIEGDTGWIVIDPLTSVETAAAALALYRKHLGDRPVKAVIYTHSHVDHFGGVRG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542512438 181 LVEPQQVASGAVQIIAPAGFMEAAIKENVLAGNAMMRRATYQYGTQLPKGPQGQVDMAIGKGLARGPLSLLAPTRLIEGE 260
Cdd:COG2015   161 VVDEEDVKSGKVPIIAPEGFMEHAVSENVYAGNAMGRRAQYMYGTLLPRGPKGQVDAGLGKTTSTGTVGLIPPTDTITKT 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542512438 261 GEDLVLDGVPFTFQNTPGTESPAEMNIWLPRQKALLMAENVVGTLHNLYTLRGAEVRDALGWSKYINQALHRFGRQAEVM 340
Cdd:COG2015   241 GEELTIDGVRMEFQLTPGTEAPAEMNFYFPDFKALCMAENATHTLHNLYTLRGAQVRDALAWSKYLDEALELFGDRAEVM 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542512438 341 FAVHNWPRWGNAEIVEVLEKQRDLYGYLHDQTLHLANQGVTIGQVHNRLRLPPSLDQEWYDRGYHGSVSHNARAVLNRYL 420
Cdd:COG2015   321 FASHHWPTWGNERIVEYLTNQRDAYKYLHDQTLRLANQGYTPDEIAEVIKLPPSLAKDWYTRGYYGSVSHNVKAVYQRYL 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542512438 421 GYYDGNPATLDPLSPEDSAGRYVEYMGGAERLLEQARASYARGEYRWVVEVVNRLVFAEPDNRAARELQADALEQLGYQA 500
Cdd:COG2015   401 GWYDGNPANLNPLPPEEAAKRYVEAMGGADAVLAKARAAFDAGDYRWAAELLNHLVFADPDNQEARELLADALEQLGYQA 480

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542512438 501 ENAGWRNSYLSAAYELRHGVPRDqPTMKAGSADALAAMDTGLLFDYLGVRLDAGAAEGKALSINLRLPDIGENYLLELKN 580
Cdd:COG2015   481 ESATWRNFYLTGALELRHGVPKS-PTPNTASPDMIAAMPTEMLFDYLAVRLDGPKAAGKDLTINLIFTDTGEKYLLELRN 559

                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542512438 581 SHLNNLRGVQSEDAGQTVSIDRADLNRLLLKEVSAVRLVFEGKLKSSGNPLLLGQLFGMLGDFDFWFDIV 650
Cdd:COG2015   560 GVLTYRKGPQADDADATLTLTRADLLALLLGKTTLDDLVASGGAKVEGDAAALARLLGLLDPFDPDFNIV 629
arylsulfatase_Sdsa1-like_MBL-fold cd07710
Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and ...
 106-350 9.73e-134

Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and related proteins; MBL-fold metallo-hydrolase domain; Arylsulfatase (also known as aryl-sulfate sulfohydrolase, EC 3.1.6.1). Pseudomonas aeruginosa SdsA1 is a secreted SDS hydrolase that allows the bacterium to use primary sulfates such as the detergent SDS common in commercial personal hygiene products as a sole carbon or sulfur source. Pseudomonas inverting secondary alkylsulfatase 1 (Pisa1) is specific for secondary alkyl sulfates. 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: 293796 [Multi-domain]  Cd Length: 239  Bit Score: 392.25  E-value: 9.73e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542512438 106 GLFEVAEGIYQVRGFDLANITFIRGDSGWIVVDTLTTPATARAAYELVSRELGERPIRTVIYSHAHADHFGGVRGLVEPQ 185
Cdd:cd07710     1 GLFEVTDGVYQVRGYDLSNMTFIEGDTGLIIIDTLESAEAAKAALELFRKHTGDKPVKAIIYTHSHPDHFGGAGGFVEEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542512438 186 QvaSGAVQIIAPAGFMEAAIKENVLAGNAMMRRATYQYGTQLPKGPQGQVDMAIGKGLARGPLSLLAPTRLIEGEGEDLV 265
Cdd:cd07710    81 D--SGKVPIIAPEGFMEEAVSENVLAGNAMSRRAAYQFGALLPKGEKGQVGAGLGPGLSTGTVGFIPPTITITETGETLT 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542512438 266 LDGVPFTFQNTPGtESPAEMNIWLPRQKALLMAENVVGTLHNLYTLRGAEVRDALGWSKYINQALhrfGRQAEVMFAVHN 345
Cdd:cd07710   159 IDGVELEFQHAPG-EAPDEMMVWLPDYKVLFCADNVYHTFPNLYTLRGAKYRDALAWAKSLDEAI---SLKAEVLFPSHT 234


                  ....*
gi 1542512438 346 WPRWG 350
Cdd:cd07710   235 WPVWG 239
Alkyl_sulf_dimr pfam14863
Alkyl sulfatase dimerization; This domain is found in alkyl sulfatases such as the Pseudomonas ...
 381-516 8.40e-75

Alkyl sulfatase dimerization; This domain is found in alkyl sulfatases such as the Pseudomonas aeruginosa SDS hydrolase, where it acts as a dimerization domain


Pssm-ID: 464351  Cd Length: 136  Bit Score: 236.22  E-value: 8.40e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542512438 381 TIGQVHNRLRLPPSLDQEWYDRGYHGSVSHNARAVLNRYLGYYDGNPATLDPLSPEDSAGRYVEYMGGAERLLEQARASY 460
Cdd:pfam14863   1 TPDEIAEELKLPPSLAEAWYLRGYYGSVSHNVRAIYQRYLGWFDGNPAHLNPLPPVEAAKRYVELMGGADAVLAKAREAF 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1542512438 461 ARGEYRWVVEVVNRLVFAEPDNRAARELQADALEQLGYQAENAGWRNSYLSAAYEL 516
Cdd:pfam14863  81 DAGDYRWAAELLNHLVFADPDNQEARELLADALEQLGYQAESATWRNFYLTGALEL 136
Alkyl_sulf_C pfam14864
Alkyl sulfatase C-terminal; This domain is found at the C-terminus of alkyl sulfatases. ...
 529-652 1.10e-46

Alkyl sulfatase C-terminal; This domain is found at the C-terminus of alkyl sulfatases. Together with the N-terminal catalytic domain, this domain forms a hydrophobic chute and may recruit hydrophobic substrates.


Pssm-ID: 405542 [Multi-domain]  Cd Length: 124  Bit Score: 160.82  E-value: 1.10e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542512438 529 AGSADALAAMDTGLLFDYLGVRLDAGAAEGKALSINLRLPDIGENYLLELKNSHLNNLRGVQSEDAGQTVSIDRADLNRL 608
Cdd:pfam14864   1 TASPDMLRALTLEQLFDYLAVRVDGPKAEGKDLTINLVFPDVDEQYRLTLSNGVLTYRKGRQADDADATLTLTRADLLAL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1542512438 609 LLKEVSAVRLVFEGKLKSSGNPLLLGQLFGMLGDFDFWFDIVTP 652
Cdd:pfam14864  81 LLGKATLGKLIAAGKIKVEGDPSALAELLSLLDTFDPNFNIVTP 124
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 113-297 1.55e-19

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: 87.24  E-value: 1.55e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542512438 113 GIYQVRG----FDLANITFIRGDSGWIVVDTLTTPATARAAYELVsRELGERPIRTVIYSHAHADHFGGVrglvepQQVA 188
Cdd:cd16282     1 GVYALIGpdggGFISNIGFIVGDDGVVVIDTGASPRLARALLAAI-RKVTDKPVRYVVNTHYHGDHTLGN------AAFA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542512438 189 SGAVQIIAPagfmeAAIKENVLAGNAMMRRATYQYGTQLPKGPQgqvdmaigkglargplsLLAPTRLIEGEGEdLVLDG 268
Cdd:cd16282    74 DAGAPIIAH-----ENTREELAARGEAYLELMRRLGGDAMAGTE-----------------LVLPDRTFDDGLT-LDLGG 130

                         170       180
                  ....*....|....*....|....*....
gi 1542512438 269 VPFTFQNTPGTESPAEMNIWLPRQKALLM 297
Cdd:cd16282   131 RTVELIHLGPAHTPGDLVVWLPEEGVLFA 159
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
118-344 3.51e-19

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 86.27  E-value: 3.51e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542512438 118 RGFDLANITFIRGDSGWIVVDTLTTPATARAAyELVSRELGERPIRTVIYSHAHADHFGGVRGLVEPQQVASGAVQIIAP 197
Cdd:pfam00753   1 LGPGQVNSYLIEGGGGAVLIDTGGSAEAALLL-LLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEAR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542512438 198 AGFMEAAIKENVLagnammrratyqygtqlpkgpqgqvdmaiGKGLARGPLSLLAPTRLIEGEGEDLVLDGVPFTFqnTP 277
Cdd:pfam00753  80 ELLDEELGLAASR-----------------------------LGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTH--GP 128

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1542512438 278 GTeSPAEMNIWLPRQKALLM--AENVVGTLHNLYTLRGAEVRDALGWSKYINQALHRFGRQAEVMFAVH 344
Cdd:pfam00753 129 GH-GPGHVVVYYGGGKVLFTgdLLFAGEIGRLDLPLGGLLVLHPSSAESSLESLLKLAKLKAAVIVPGH 196
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 124-330 2.74e-16

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: 77.21  E-value: 2.74e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542512438  124 NITFIRGDSGWIVVDTLTTPATARAAYElvsRELGERPIRTVIYSHAHADHFGGVRGLVEpqqvASGAvQIIAPAGFMEA 203
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAEDLLAEL---KKLGPKKIDAIILTHGHPDHIGGLPELLE----APGA-PVYAPEGTAEL 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542512438  204 AIKENVLAGNAMMRRATYqygtqlpkgpqgqvdmaigkglargplsllAPTRLIEgEGEDLVLDGVPFTFQNTPGtESPA 283
Cdd:smart00849  73 LKDLLALLGELGAEAEPA------------------------------PPDRTLK-DGDELDLGGGELEVIHTPG-HTPG 120

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1542512438  284 EMNIWLPRQKALLMAENVVGTLHNLYTLRGAEVRDALGWSKYINQAL 330
Cdd:smart00849 121 SIVLYLPEGKILFTGDLLFAGGDGRTLVDGGDAAASDALESLLKLLK 167
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 114-298 3.54e-11

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: 63.17  E-value: 3.54e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542512438 114 IYQVRG-----FDLANITFIRGDSGWIVVDTLTTPATARAAYELVsRELGErPIRTVIYSHAHADHFGGVRGLVEpqqvA 188
Cdd:COG0491     1 VYVLPGgtpgaGLGVNSYLIVGGDGAVLIDTGLGPADAEALLAAL-AALGL-DIKAVLLTHLHPDHVGGLAALAE----A 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542512438 189 SGAvQIIAPAGfmEAAIKENVLAGNAMMRRAtyqygtqlpkgpqgqvdmaigkglargplslLAPTRLIEgEGEDLVLDG 268
Cdd:COG0491    75 FGA-PVYAHAA--EAEALEAPAAGALFGREP-------------------------------VPPDRTLE-DGDTLELGG 119

                         170       180       190
                  ....*....|....*....|....*....|
gi 1542512438 269 VPFTFQNTPGtESPAEMNIWLPRQKALLMA 298
Cdd:COG0491   120 PGLEVIHTPG-HTPGHVSFYVPDEKVLFTG 148
metallo-hydrolase-like_MBL-fold cd16276
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 106-196 1.18e-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: 55.28  E-value: 1.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542512438 106 GLFEVAEGIYQVrgfdlaniTFIRGDSGWIVVDTlttPATARAAYELVSRELGERPIRTVIYSHAHADHFGGVrglvepQ 185
Cdd:cd16276     1 GVYWVTDGGYQS--------MFLVTDKGVIVVDA---PPSLGENLLAAIRKVTDKPVTHVVYSHNHADHIGGA------S 63

                          90
                  ....*....|.
gi 1542512438 186 QVASGAVQIIA 196
Cdd:cd16276    64 IFKDEGATIIA 74
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 113-183 7.48e-08

uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase domain; This subgroup includes the uncharacterized Bacillus subtilis yflN 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: 293807 [Multi-domain]  Cd Length: 202  Bit Score: 52.99  E-value: 7.48e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1542512438 113 GIYQVRGFDLANITFIRGDSGWIVVDTlTTPATARAAYELVsRELGERP--IRTVIYSHAHADHFGGVRGLVE 183
Cdd:cd07721     1 GVYQLPLLPPVNAYLIEDDDGLTLIDT-GLPGSAKRILKAL-RELGLSPkdIRRILLTHGHIDHIGSLAALKE 71
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 123-296 8.04e-06

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: 46.90  E-value: 8.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542512438 123 ANITFIRGDSG-WIVVDtlttPATAraAYELVSRELGERP--IRTVIYSHAHADHFGGVRGLVEpqqvASGAvQIIAPAG 199
Cdd:cd06262    10 TNCYLVSDEEGeAILID----PGAG--ALEKILEAIEELGlkIKAILLTHGHFDHIGGLAELKE----APGA-PVYIHEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542512438 200 FMEaaikenvlagnaMMRRATYQYGTQLPkgpqgqvdmaigkglarGPLSLLAPTRLIEgEGEDLVLDGVPFTFQNTPGt 279
Cdd:cd06262    79 DAE------------LLEDPELNLAFFGG-----------------GPLPPPEPDILLE-DGDTIELGGLELEVIHTPG- 127

                         170
                  ....*....|....*..
gi 1542512438 280 ESPAEMNIWLPRQKALL 296
Cdd:cd06262   128 HTPGSVCFYIEEEGVLF 144
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 123-278 1.29e-05

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) 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: 293829 [Multi-domain]  Cd Length: 197  Bit Score: 46.37  E-value: 1.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542512438 123 ANITFIR-GDSGWIVVDTLTTPATARAAYELVsRELGERPiRTVIYSHAHADHFGGVRGLVEPQQvasgaVQIIAPAGfm 201
Cdd:cd07743     8 TNIGVYVfGDKEALLIDSGLDEDAGRKIRKIL-EELGWKL-KAIINTHSHADHIGGNAYLQKKTG-----CKVYAPKI-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542512438 202 EAAIKENVLAgnammrRATYQYGTQLPKGPQgqvdmaigkglargPLSLLAP----TRLIEgEGEdLVLDGVPFTFQNTP 277
Cdd:cd07743    79 EKAFIENPLL------EPSYLGGAYPPKELR--------------NKFLMAKpskvDDIIE-EGE-LELGGVGLEIIPLP 136


                  .
gi 1542512438 278 G 278
Cdd:cd07743   137 G 137
metallo-hydrolase-like_MBL-fold cd07739
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 126-331 2.07e-05

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) 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: 293825 [Multi-domain]  Cd Length: 201  Bit Score: 45.96  E-value: 2.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542512438 126 TFIRGDSGWIVVDTLTTPATARAAYELVsRELGeRPIRTVIYSHAHADHFGGVRGLVE--PQqvasgaVQIIAPAGFMEa 203
Cdd:cd07739    19 TLIYGETEAVLVDAQFTRADAERLADWI-KASG-KTLTTIYITHGHPDHYFGLEVLLEafPD------AKVVATPAVVA- 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542512438 204 AIKENVLAGNAMmrrATYQYGTQLPKgpqgqvdmaigkglargplSLLAPTRLiegEGEDLVLDGVPFTFQNTPGTESPA 283
Cdd:cd07739    90 HIKAQLEPKLAF---WGPLLGGNAPA-------------------RLVVPEPL---DGDTLTLEGHPLEIVGVGGGDTDD 144

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1542512438 284 EMNIWLPRQKALLMAENVVGTLHnLYT--LRGAEVRDAlgWSKYINQ--ALH 331
Cdd:cd07739   145 TTYLWIPSLKTVVAGDVVYNGVH-VWLadATTPELRAA--WLAALDKieALN 193
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 128-179 2.30e-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: 46.05  E-value: 2.30e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542512438 128 IRGDSGWIVVDT--------------LTTPATARAAYELVSR--ELGERP--IRTVIYSHAHADHFGGVR 179
Cdd:cd07729    37 IEHPEGTILVDTgfhpdaaddpggleLAFPPGVTEEQTLEEQlaRLGLDPedIDYVILSHLHFDHAGGLD 106
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 124-184 2.37e-05

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: 45.37  E-value: 2.37e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1542512438 124 NITFIRGDSGWIVVDT-LTTPATARAAYELVsRELGERP--IRTVIYSHAHADHFGGVRGLVEP 184
Cdd:cd07725    16 NVYLLRDGDETTLIDTgLATEEDAEALWEGL-KELGLKPsdIDRVLLTHHHPDHIGLAGKLQEK 78
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 126-183 6.10e-05

DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 441904 [Multi-domain]  Cd Length: 253  Bit Score: 45.23  E-value: 6.10e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1542512438 126 TFIRGDSG-WIVVDTLTTPATARAAYELVS--RELGERPIRTVIYSHAHADHFGGVRGLVE 183
Cdd:COG2333    14 ILIRTPDGkTILIDTGPRPSFDAGERVVLPylRALGIRRLDLLVLTHPDADHIGGLAAVLE 74
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 128-189 9.83e-05

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: 293838 [Multi-domain]  Cd Length: 251  Bit Score: 44.50  E-value: 9.83e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1542512438 128 IRGDSGWIVVDTLTTPataRAAYELVS--RELGERP--IRTVIYSHAHADHFGGVRGLVE---PQQVAS 189
Cdd:cd16280    27 IDTGDGLILIDALNNN---EAADLIVDglEKLGLDPadIKYILITHGHGDHYGGAAYLKDlygAKVVMS 92
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 160-204 2.86e-04

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) 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: 293826 [Multi-domain]  Cd Length: 194  Bit Score: 42.25  E-value: 2.86e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1542512438 160 RPIRTVIYSHAHADHFGGVRGLVEPQQVASG---AVQIIAPAGFMEAA 204
Cdd:cd07740    48 NAIDAIFITHLHGDHFGGLPFFLLDAQFVAKrtrPLTIAGPPGLRERL 95
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 134-199 3.34e-04

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: 42.30  E-value: 3.34e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1542512438 134 WIVVDTLTTPAtARAAYELVSRELGERPIRTVIYSHAHADHFGGVRGLVEPQQvasgaVQIIAPAG 199
Cdd:pfam12706   2 RILIDPGPDLR-QQALPALQPGRLRDDPIDAVLLTHDHYDHLAGLLDLREGRP-----RPLYAPLG 61
MBL-B1-B2-like cd07707
metallo-beta-lactamases; subclasses B1 and B2 and related proteins; MBL-fold metallo-hydrolase ...
 107-178 4.81e-04

metallo-beta-lactamases; subclasses B1 and B2 and related proteins; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. Subclass B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. B1 MBls include chromosomally-encoded MBLs such as Bacillus cereus BcII, Bacteroides fragilis CcrA, and Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) BlaB and acquired MBLs including IMP-1, VIM-1, VIM-2, GIM-1, NDM-1 and FIM-1. B2 MBLs have a narrow substrate profile that includes carbapenems, and they are active with one zinc ion bound in the Asp-Cys-His site, binding of a second zinc ion in the modified 3H site (Asn-His-His) inhibits catalysis. B2 MBLs include Aeromonas hydrophyla CphA, Aeromonas veronii ImiS, and Serratia fonticola Sfh-I.


Pssm-ID: 293793 [Multi-domain]  Cd Length: 219  Bit Score: 42.15  E-value: 4.81e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1542512438 107 LFEVAEGIYQV--RGFDLANITFIRGDSGWIVVDTLTTPATARAAYELVSRELGeRPIRTVIYSHAHADHFGGV 178
Cdd:cd07707     3 LTQINGPVWVVtdLGSVPSNGLVYNGSKGLVLVDSTWTPKTTKELIKEIEKVSQ-KPVTEVINTHFHTDRAGGN 75
SCP2 pfam02036
SCP-2 sterol transfer family; This domain is involved in binding sterols. It is found in the ...
 544-640 5.05e-04

SCP-2 sterol transfer family; This domain is involved in binding sterols. It is found in the SCP2 protein as well as the C terminus of the enzyme estradiol 17 beta-dehydrogenase EC:1.1.1.62. The UNC-24 protein contains an SPFH domain pfam01145.


Pssm-ID: 460423 [Multi-domain]  Cd Length: 100  Bit Score: 39.93  E-value: 5.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542512438 544 FDYLGVRLDAGAAEGKALS---INLRLPDIGENYLLELKNSHLnnlrGVQSEDAGQ---TVSIDRADLNRLLLKEVSAVR 617
Cdd:pfam02036   1 LNQLLARDPAARELLKKLNgkvIRFDLTDLGLSLTLDLKDGGG----RVLAGDEGKadvTLSASDSDLLALATGKLNPQK 76

                          90       100
                  ....*....|....*....|...
gi 1542512438 618 LVFEGKLKSSGNPLLLGQLFGML 640
Cdd:pfam02036  77 AFMQGKLKIEGDMELAQKLEGLL 99
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 113-278 5.64e-04

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: 41.71  E-value: 5.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542512438 113 GIYQV--RGFDLANIT---FIRGDSGWIVVDTltTPATARAAYELVSRELGERP--IRTVIYSHAHADHFGGVRGLVE-- 183
Cdd:cd07726     1 GIYLIdlGFLGFPGRIasyLLDGEGRPALIDT--GPSSSVPRLLAALEALGIAPedVDYIILTHIHLDHAGGAGLLAEal 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542512438 184 PQ-QVA---SGAVQIIAPAGFMEAAIKenVLaGNAMMRRatyqYGTQLPkgpqgqvdmaigkglargplslLAPTRLIE- 258
Cdd:cd07726    79 PNaKVYvhpRGARHLIDPSKLWASARA--VY-GDEADRL----GGEILP----------------------VPEERVIVl 129

                         170       180
                  ....*....|....*....|
gi 1542512438 259 GEGEDLVLDGVPFTFQNTPG 278
Cdd:cd07726   130 EDGETLDLGGRTLEVIDTPG 149
EVM-1-like_MBL-B3 cd16315
Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 128-252 9.33e-04

Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup EVM-1-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293873 [Multi-domain]  Cd Length: 248  Bit Score: 41.57  E-value: 9.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542512438 128 IRGDSGWIVVDTlttpATARAAyELVS---RELGERP--IRTVIYSHAHADHFGGVRGLvepqQVASGAvQIIAPAgfmE 202
Cdd:cd16315    27 ITGDDGHVLIDS----GTEEAA-PLVLaniRKLGFDPkdVRWLLSSHEHFDHVGGLAAL----QRATGA-RVAASA---A 93

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1542512438 203 AAikenvlagnAMMRRatyqyGTQLPKGPQG---------QVDMAI--GKGLARGPLSLLA 252
Cdd:cd16315    94 AA---------PVLES-----GKPAPDDPQAglhepfppvRVDRIVedGDTVALGSLRLTA 140
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
162-202 1.56e-03

Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];


Pssm-ID: 440850  Cd Length: 273  Bit Score: 41.02  E-value: 1.56e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1542512438 162 IRTVIYSHAHADHFGGVRGLVEpqqvASGAVQIIAPAGFME 202
Cdd:COG1237    58 IDAVVLSHGHYDHTGGLPALLE----LNPKAPVYAHPDAFE 94
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 108-278 1.60e-03

Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of BJP-1-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293867 [Multi-domain]  Cd Length: 252  Bit Score: 40.93  E-value: 1.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542512438 108 FEVAEGIYQVrGFDLANITFIRGDSGWIVVDTLTTPATARAAYELvsRELGERP--IRTVIYSHAHADHFGGVRGLvepq 185
Cdd:cd16309     8 FKLIGNIYYV-GTAGLGVFLITTPEGHILIDGAMPQSTPLIKDNI--KKLGFDVkdVKYLLNTHAHFDHAGGLAEL---- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542512438 186 QVASGAvQIIAPAgfmeaaikenvlAGNAMMRRATYQYG-TQLPKGPQGQVDMAIgkglargplsllaptrlieGEGEDL 264
Cdd:cd16309    81 KKATGA-QLVASA------------ADKPLLESGYVGSGdTKNLQFPPVRVDRVI-------------------GDGDKV 128

                         170
                  ....*....|....
gi 1542512438 265 VLDGVPFTFQNTPG 278
Cdd:cd16309   129 TLGGTTLTAHLTPG 142
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 123-179 2.16e-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: 39.88  E-value: 2.16e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1542512438 123 ANITFIRGDSGWIVVDTLTTPATAraayELVS--RELGERP--IRTVIYSHAHADHFGGVR 179
Cdd:cd07711    22 STVTLIKDGGKNILVDTGTPWDRD----LLLKalAEHGLSPedIDYVVLTHGHPDHIGNLN 78
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 128-183 5.13e-03

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: 293836 [Multi-domain]  Cd Length: 185  Bit Score: 38.63  E-value: 5.13e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1542512438 128 IRGDSGWIVVDtlttPATARAAY-ELVSRELGERPIRTVIYSHAHADHFGGVRGLVE 183
Cdd:cd16278    23 LGAPDGVVVID----PGPDDPAHlDALLAALGGGRVSAILVTHTHRDHSPGAARLAE 75
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 126-210 6.02e-03

Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This subgroup includes proteins required for natural transformation competence including Neisseria gonorrhoeae ComA, Pseudomonas stutzeri ComA, Bacillus subtilis ComEC (also known as ComE operon protein 3) and Haemophilus influenza ORF2 encoded by the rec-2 gene, as well as Escherichia coli YcaI which does not mediate spontaneous plasmid transformation on nutrient-containing agar plates. It also includes the phosphorylcholine esterase (Pce) domain of choline-binding protein e from streptococcus pneumonia. 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: 293817 [Multi-domain]  Cd Length: 179  Bit Score: 38.27  E-value: 6.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542512438 126 TFIRGDSGWIVVDTltTPATARAAYELVS--RELGERPIRTVIYSHAHADHFGGVRGLVEPQQVAsgavQIIAPAGFMEA 203
Cdd:cd07731    13 ILIQTPGKTILIDT--GPRDSFGEDVVVPylKARGIKKLDYLILTHPDADHIGGLDAVLKNFPVK----EVYMPGVTHTT 86


                  ....*..
gi 1542512438 204 AIKENVL 210
Cdd:cd07731    87 KTYEDLL 93
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 155-202 8.96e-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: 38.37  E-value: 8.96e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1542512438 155 RELGERP--IRTVIYSHAHADHFGGVRGLVEpqqvASGAVQIIAPAGFME 202
Cdd:cd07713    47 KKLGIDLsdIDAVVLSHGHYDHTGGLKALLE----LNPKAPVYAHPDAFE 92
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH