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Conserved domains on  [gi|970959093|ref|WP_058840392|]
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MBL fold metallo-hydrolase [Bacillus sp. G3(2015)]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 10845098)

MBL fold metallo-hydrolase containing Rhodanese Homology Domain(s) (RHOD), is most likely a hydrolytic enzyme that may have substrate towards phosphotriesters, esters, and/or lactones

CATH:  3.60.15.10
EC:  3.-.-.-
Gene Ontology:  GO:0016787|GO:0046872
PubMed:  17597585|12177301|11471246|11513844
SCOP:  3001057

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 122-296 5.79e-65

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: 204.17  E-value: 5.79e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093 122 YQFKRLGKGCLSYMVVSN--GEAAVIDAVR-TVEAYEEFAKEHGVTITNVMDTHLHADHISGGRKLAEKVGGTYWLPPKD 198
Cdd:cd07724    3 RQFFDPGLGTLSYLVGDPetGEAAVIDPVRdSVDRYLDLAAELGLKITYVLETHVHADHVSGARELAERTGAPIVIGEGA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093 199 aeEVVFSYEPLVEGSVITVGGTKIVidALYSPGHTIGSTSFIVDD-SYLLSGDILFVDSIGRPDLAGKAEDWVSDLRNTL 277
Cdd:cd07724   83 --PASFFDRLLKDGDVLELGNLTLE--VLHTPGHTPESVSYLVGDpDAVFTGDTLFVGDVGRPDLPGEAEGLARQLYDSL 158

                        170
                 ....*....|....*....
gi 970959093 278 YSRYKELSQNLVVLPAHYS 296
Cdd:cd07724  159 QRKLLLLPDETLVYPGHDY 177
RHOD_Lact_B cd01523
Member of the Rhodanese Homology Domain superfamily. This CD includes predicted proteins with ...
 6-105 7.13e-45

Member of the Rhodanese Homology Domain superfamily. This CD includes predicted proteins with rhodanese-like domains found N-terminal of the metallo-beta-lactamase domain.


:

Pssm-ID: 238781 [Multi-domain]  Cd Length: 100  Bit Score: 149.95  E-value: 7.13e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093   6 LQAKDVAEKVLFGE-LFILDVRNEADYEDWKIEGKQVSSINRPYFDLLDGVDHIVSELPKDKDVLVVCAKEGSSIFVAEQ 84
Cdd:cd01523    1 LDPEDLYARLLAGQpLFILDVRNESDYERWKIDGENNTPYFDPYFDFLEIEEDILDQLPDDQEVTVICAKEGSSQFVAEL 80

                         90       100
                 ....*....|....*....|.
gi 970959093  85 LTEAGLEnIYYLAGGMKAWSE 105
Cdd:cd01523   81 LAERGYD-VDYLAGGMKAWSE 100
 
Name Accession Description Interval E-value
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 122-296 5.79e-65

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: 204.17  E-value: 5.79e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093 122 YQFKRLGKGCLSYMVVSN--GEAAVIDAVR-TVEAYEEFAKEHGVTITNVMDTHLHADHISGGRKLAEKVGGTYWLPPKD 198
Cdd:cd07724    3 RQFFDPGLGTLSYLVGDPetGEAAVIDPVRdSVDRYLDLAAELGLKITYVLETHVHADHVSGARELAERTGAPIVIGEGA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093 199 aeEVVFSYEPLVEGSVITVGGTKIVidALYSPGHTIGSTSFIVDD-SYLLSGDILFVDSIGRPDLAGKAEDWVSDLRNTL 277
Cdd:cd07724   83 --PASFFDRLLKDGDVLELGNLTLE--VLHTPGHTPESVSYLVGDpDAVFTGDTLFVGDVGRPDLPGEAEGLARQLYDSL 158

                        170
                 ....*....|....*....
gi 970959093 278 YSRYKELSQNLVVLPAHYS 296
Cdd:cd07724  159 QRKLLLLPDETLVYPGHDY 177
RHOD_Lact_B cd01523
Member of the Rhodanese Homology Domain superfamily. This CD includes predicted proteins with ...
 6-105 7.13e-45

Member of the Rhodanese Homology Domain superfamily. This CD includes predicted proteins with rhodanese-like domains found N-terminal of the metallo-beta-lactamase domain.


Pssm-ID: 238781 [Multi-domain]  Cd Length: 100  Bit Score: 149.95  E-value: 7.13e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093   6 LQAKDVAEKVLFGE-LFILDVRNEADYEDWKIEGKQVSSINRPYFDLLDGVDHIVSELPKDKDVLVVCAKEGSSIFVAEQ 84
Cdd:cd01523    1 LDPEDLYARLLAGQpLFILDVRNESDYERWKIDGENNTPYFDPYFDFLEIEEDILDQLPDDQEVTVICAKEGSSQFVAEL 80

                         90       100
                 ....*....|....*....|.
gi 970959093  85 LTEAGLEnIYYLAGGMKAWSE 105
Cdd:cd01523   81 LAERGYD-VDYLAGGMKAWSE 100
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 126-294 4.62e-34

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: 125.57  E-value: 4.62e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093 126 RLGKGCLSYMVVSNGEAAVIDA---VRTVEAYEEFAKEHGVTITNVMDTHLHADHISGGRKLAEKVGGTYWLPPKDAE-- 200
Cdd:COG0491   10 GAGLGVNSYLIVGGDGAVLIDTglgPADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFGAPVYAHAAEAEal 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093 201 -----------EVVFSYEPLVEGSVITVGGTKivIDALYSPGHTIGSTSFIVDDS-YLLSGDILFVDSIGRPDLAGK-AE 267
Cdd:COG0491   90 eapaagalfgrEPVPPDRTLEDGDTLELGGPG--LEVIHTPGHTPGHVSFYVPDEkVLFTGDALFSGGVGRPDLPDGdLA 167

                        170       180
                 ....*....|....*....|....*..
gi 970959093 268 DWVSDLRntlysRYKELSqNLVVLPAH 294
Cdd:COG0491  168 QWLASLE-----RLLALP-PDLVIPGH 188
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 1-114 2.02e-26

Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; Rhodanese-related sulfurtransferase is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440372 [Multi-domain]  Cd Length: 106  Bit Score: 101.58  E-value: 2.02e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093   1 MSVKPLQAKDVAEKVLFGELFILDVRNEADYEDWKIEGkqvsSINRPYFDLLDGVDhivsELPKDKDVLVVCAKEGSSIF 80
Cdd:COG0607    1 ASVKEISPAELAELLESEDAVLLDVREPEEFAAGHIPG----AINIPLGELAERLD----ELPKDKPIVVYCASGGRSAQ 72

                         90       100       110
                 ....*....|....*....|....*....|....
gi 970959093  81 VAEQLTEAGLENIYYLAGGMKAWSEYVKPIKVGD 114
Cdd:COG0607   73 AAALLRRAGYTNVYNLAGGIEAWKAAGLPVEKGK 106
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 133-294 1.83e-20

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: 87.61  E-value: 1.83e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093   133 SYMVVSNGEAAVIDAV-RTVEAYEEFAKEHGV-TITNVMDTHLHADHISGGRKLAEKVGGTYWLPPKDAE---------- 200
Cdd:smart00849   2 SYLVRDDGGAILIDTGpGEAEDLLAELKKLGPkKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAEllkdllallg 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093   201 ------EVVFSYEPLVEGSVITVGGTKivIDALYSPGHTIGSTSFIVDD-SYLLSGDILFVDSIGRPDLAG---KAEDWV 270
Cdd:smart00849  82 elgaeaEPAPPDRTLKDGDELDLGGGE--LEVIHTPGHTPGSIVLYLPEgKILFTGDLLFAGGDGRTLVDGgdaAASDAL 159

                          170       180
                   ....*....|....*....|....
gi 970959093   271 SDLRNTLYSRYKelsqnlVVLPAH 294
Cdd:smart00849 160 ESLLKLLKLLPK------LVVPGH 177
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 18-104 7.99e-14

Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single copy of this duplicated domain. The domain is found as a single copy in other proteins, including phosphatases and ubiquitin C-terminal hydrolases.


Pssm-ID: 425764 [Multi-domain]  Cd Length: 92  Bit Score: 66.74  E-value: 7.99e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093   18 GELFILDVRNEADYEDWKIEGkqvsSINRPYFDLLDGVDHI------VSELPKDKDVLVVCAKEGSSIFVAEQLTEAGLE 91
Cdd:pfam00581   4 GKVVLIDVRPPEEYAKGHIPG----AVNVPLSSLSLPPLPLlellekLLELLKDKPIVVYCNSGNRAAAAAALLKALGYK 79

                          90
                  ....*....|...
gi 970959093   92 NIYYLAGGMKAWS 104
Cdd:pfam00581  80 NVYVLDGGFEAWK 92
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 131-279 1.45e-13

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 69.79  E-value: 1.45e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093 131 CL----SYMVV--SNGEAAVIDAVRtVEAYEEFAKEHGVTITNVMDTHLHADHISGGRKLAEKV------GGTywlppkd 198
Cdd:PLN02469   8 CLednyAYLIIdeSTKDAAVVDPVD-PEKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIKKLVpgikvyGGS------- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093 199 AEEVVFSYEPLVEGSVITVGGTkIVIDALYSPGHTIGSTSFIV-----DDSYLLSGDILFVDSIGRpDLAGKAEDWVSDL 273
Cdd:PLN02469  80 LDNVKGCTHPVENGDKLSLGKD-VNILALHTPCHTKGHISYYVtgkegEDPAVFTGDTLFIAGCGK-FFEGTAEQMYQSL 157


                 ....*.
gi 970959093 274 RNTLYS 279
Cdd:PLN02469 158 CVTLGS 163
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 18-109 2.72e-12

Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The the Cysteine containing enzymatically active version of the domain is also found in the CDC25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and stress proteins such as Senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions with a loss of the cysteine are also seen in Dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases. These are likely to play a role in protein interactions.


Pssm-ID: 197731 [Multi-domain]  Cd Length: 100  Bit Score: 62.48  E-value: 2.72e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093    18 GELFILDVRNEADYEDWKIEGkqvsSINRPYFDLLDGVDHIVS----------ELPKDKDVLVVCAKEGSSIFVAEQLTE 87
Cdd:smart00450   3 EKVVLLDVRSPEEYEGGHIPG----AVNIPLSELLDRRGELDIlefeellkrlGLDKDKPVVVYCRSGNRSAKAAWLLRE 78

                           90       100
                   ....*....|....*....|..
gi 970959093    88 AGLENIYYLAGGMKAWSEYVKP 109
Cdd:smart00450  79 LGFKNVYLLDGGYKEWSAAGPP 100
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
130-294 5.14e-11

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 61.23  E-value: 5.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093  130 GCLSYMVVSNGEAAVIDAVRTVE-AYEEFAKEHGVTITNVMD---THLHADHISGGRKLAEKVGGTYWLPPKDAEE---- 201
Cdd:pfam00753   5 QVNSYLIEGGGGAVLIDTGGSAEaALLLLLAALGLGPKDIDAvilTHGHFDHIGGLGELAEATDVPVIVVAEEAREllde 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093  202 ---------VVFSYEPLVEGSVITVGGTKIVID------ALYSPGHTIGSTSF-IVDDSYLLSGDILFVDSIGRPDL-AG 264
Cdd:pfam00753  85 elglaasrlGLPGPPVVPLPPDVVLEEGDGILGgglgllVTHGPGHGPGHVVVyYGGGKVLFTGDLLFAGEIGRLDLpLG 164

                         170       180       190
                  ....*....|....*....|....*....|..
gi 970959093  265 KAEDWVSDLRNTLYSRYKELSQ--NLVVLPAH 294
Cdd:pfam00753 165 GLLVLHPSSAESSLESLLKLAKlkAAVIVPGH 196
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
2-112 1.37e-07

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 52.71  E-value: 1.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093   2 SVKPLQAKDVAEKvlfGELFIlDVRNEADYEDWKIEGkqVSSINRPYFDLldgvdHIVSELP-KDKDVLVVCAKEGSSIF 80
Cdd:PRK08762   4 EISPAEARARAAQ---GAVLI-DVREAHERASGQAEG--ALRIPRGFLEL-----RIETHLPdRDREIVLICASGTRSAH 72

                         90       100       110
                 ....*....|....*....|....*....|..
gi 970959093  81 VAEQLTEAGLENIYYLAGGMKAWSEYVKPIKV 112
Cdd:PRK08762  73 AAATLRELGYTRVASVAGGFSAWKDAGLPLER 104
 
Name Accession Description Interval E-value
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 122-296 5.79e-65

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: 204.17  E-value: 5.79e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093 122 YQFKRLGKGCLSYMVVSN--GEAAVIDAVR-TVEAYEEFAKEHGVTITNVMDTHLHADHISGGRKLAEKVGGTYWLPPKD 198
Cdd:cd07724    3 RQFFDPGLGTLSYLVGDPetGEAAVIDPVRdSVDRYLDLAAELGLKITYVLETHVHADHVSGARELAERTGAPIVIGEGA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093 199 aeEVVFSYEPLVEGSVITVGGTKIVidALYSPGHTIGSTSFIVDD-SYLLSGDILFVDSIGRPDLAGKAEDWVSDLRNTL 277
Cdd:cd07724   83 --PASFFDRLLKDGDVLELGNLTLE--VLHTPGHTPESVSYLVGDpDAVFTGDTLFVGDVGRPDLPGEAEGLARQLYDSL 158

                        170
                 ....*....|....*....
gi 970959093 278 YSRYKELSQNLVVLPAHYS 296
Cdd:cd07724  159 QRKLLLLPDETLVYPGHDY 177
RHOD_Lact_B cd01523
Member of the Rhodanese Homology Domain superfamily. This CD includes predicted proteins with ...
 6-105 7.13e-45

Member of the Rhodanese Homology Domain superfamily. This CD includes predicted proteins with rhodanese-like domains found N-terminal of the metallo-beta-lactamase domain.


Pssm-ID: 238781 [Multi-domain]  Cd Length: 100  Bit Score: 149.95  E-value: 7.13e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093   6 LQAKDVAEKVLFGE-LFILDVRNEADYEDWKIEGKQVSSINRPYFDLLDGVDHIVSELPKDKDVLVVCAKEGSSIFVAEQ 84
Cdd:cd01523    1 LDPEDLYARLLAGQpLFILDVRNESDYERWKIDGENNTPYFDPYFDFLEIEEDILDQLPDDQEVTVICAKEGSSQFVAEL 80

                         90       100
                 ....*....|....*....|.
gi 970959093  85 LTEAGLEnIYYLAGGMKAWSE 105
Cdd:cd01523   81 LAERGYD-VDYLAGGMKAWSE 100
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 126-294 4.62e-34

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: 125.57  E-value: 4.62e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093 126 RLGKGCLSYMVVSNGEAAVIDA---VRTVEAYEEFAKEHGVTITNVMDTHLHADHISGGRKLAEKVGGTYWLPPKDAE-- 200
Cdd:COG0491   10 GAGLGVNSYLIVGGDGAVLIDTglgPADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFGAPVYAHAAEAEal 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093 201 -----------EVVFSYEPLVEGSVITVGGTKivIDALYSPGHTIGSTSFIVDDS-YLLSGDILFVDSIGRPDLAGK-AE 267
Cdd:COG0491   90 eapaagalfgrEPVPPDRTLEDGDTLELGGPG--LEVIHTPGHTPGHVSFYVPDEkVLFTGDALFSGGVGRPDLPDGdLA 167

                        170       180
                 ....*....|....*....|....*..
gi 970959093 268 DWVSDLRntlysRYKELSqNLVVLPAH 294
Cdd:COG0491  168 QWLASLE-----RLLALP-PDLVIPGH 188
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 139-294 5.56e-28

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: 108.14  E-value: 5.56e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093 139 NGEAAVIDA-VRTVEAYEEFAKEHGVTITNVMDTHLHADHISGGRKLAEKVGGTYWLPPKDAE----------------- 200
Cdd:cd06262   19 EGEAILIDPgAGALEKILEAIEELGLKIKAILLTHGHFDHIGGLAELKEAPGAPVYIHEADAElledpelnlaffgggpl 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093 201 EVVFSYEPLVEGSVITVGGTKivIDALYSPGHTIGSTSFIVDDS-YLLSGDILFVDSIGRPDLAGKAEDwvsDLRNTLYS 279
Cdd:cd06262   99 PPPEPDILLEDGDTIELGGLE--LEVIHTPGHTPGSVCFYIEEEgVLFTGDTLFAGSIGRTDLPGGDPE---QLIESIKK 173

                        170
                 ....*....|....*
gi 970959093 280 RYKELSQNLVVLPAH 294
Cdd:cd06262  174 LLLLLPDDTVVYPGH 188
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 1-114 2.02e-26

Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; Rhodanese-related sulfurtransferase is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440372 [Multi-domain]  Cd Length: 106  Bit Score: 101.58  E-value: 2.02e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093   1 MSVKPLQAKDVAEKVLFGELFILDVRNEADYEDWKIEGkqvsSINRPYFDLLDGVDhivsELPKDKDVLVVCAKEGSSIF 80
Cdd:COG0607    1 ASVKEISPAELAELLESEDAVLLDVREPEEFAAGHIPG----AINIPLGELAERLD----ELPKDKPIVVYCASGGRSAQ 72

                         90       100       110
                 ....*....|....*....|....*....|....
gi 970959093  81 VAEQLTEAGLENIYYLAGGMKAWSEYVKPIKVGD 114
Cdd:COG0607   73 AAALLRRAGYTNVYNLAGGIEAWKAAGLPVEKGK 106
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 133-294 3.11e-25

Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; Bacillus amyloliquefaciens BaeB may play a role in the synthesis of the antibiotic polyketide bacillaene. 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: 293833 [Multi-domain]  Cd Length: 174  Bit Score: 100.30  E-value: 3.11e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093 133 SYMVV--SNGEAAVIDAVRTVEAYEEFAKEHGVTITNVMDTHLHADHISGGRKLAEKVGGTYWLPPKDAEEVVFSYEPLV 210
Cdd:cd16275   14 SYIIIdkATREAAVVDPAWDIEKILAKLNELGLTLTGILLTHSHFDHVNLVEPLLAKYDAPVYMSKEEIDYYGFRCPNLI 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093 211 E---GSVITVGGTKIVidALYSPGHTIGSTSFIVDDSyLLSGDILFVDSIGRPDLAGKAedwVSDLRNTLYSRYKELSQN 287
Cdd:cd16275   94 PledGDTIKIGDTEIT--CLLTPGHTPGSMCYLLGDS-LFTGDTLFIEGCGRCDLPGGD---PEEMYESLQRLKKLPPPN 167


                 ....*..
gi 970959093 288 LVVLPAH 294
Cdd:cd16275  168 TRVYPGH 174
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 133-294 1.83e-20

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: 87.61  E-value: 1.83e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093   133 SYMVVSNGEAAVIDAV-RTVEAYEEFAKEHGV-TITNVMDTHLHADHISGGRKLAEKVGGTYWLPPKDAE---------- 200
Cdd:smart00849   2 SYLVRDDGGAILIDTGpGEAEDLLAELKKLGPkKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAEllkdllallg 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093   201 ------EVVFSYEPLVEGSVITVGGTKivIDALYSPGHTIGSTSFIVDD-SYLLSGDILFVDSIGRPDLAG---KAEDWV 270
Cdd:smart00849  82 elgaeaEPAPPDRTLKDGDELDLGGGE--LEVIHTPGHTPGSIVLYLPEgKILFTGDLLFAGGDGRTLVDGgdaAASDAL 159

                          170       180
                   ....*....|....*....|....
gi 970959093   271 SDLRNTLYSRYKelsqnlVVLPAH 294
Cdd:smart00849 160 ESLLKLLKLLPK------LVVPGH 177
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 133-294 2.60e-20

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: 86.75  E-value: 2.60e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093 133 SYMVVSN--GEAAVIDAVrtvEAYE--EFAKEHGVTITNVMDTHLHADHISGGRKLAEKVGGtywLP---PKDaEEVVFS 205
Cdd:cd07723   11 IYLIVDEatGEAAVVDPG---EAEPvlAALEKNGLTLTAILTTHHHWDHTGGNAELKALFPD---APvygPAE-DRIPGL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093 206 YEPLVEGSVITVGGTKivIDALYSPGHTIGSTSFIVDDS-YLLSGDILFVDSIGRPDLaGKAEdwvsDLRNTLySRYKEL 284
Cdd:cd07723   84 DHPVKDGDEIKLGGLE--VKVLHTPGHTLGHICYYVPDEpALFTGDTLFSGGCGRFFE-GTAE----QMYASL-QKLLAL 155

                        170
                 ....*....|
gi 970959093 285 SQNLVVLPAH 294
Cdd:cd07723  156 PDDTLVYCGH 165
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 10-103 4.71e-20

Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese protein. The cysteine containing enzymatically active version of the domain is also found in the Cdc25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and certain stress proteins such as senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions (no active site cysteine) are also seen in dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases, where they are believed to play a regulatory role in multidomain proteins.


Pssm-ID: 238089 [Multi-domain]  Cd Length: 89  Bit Score: 83.89  E-value: 4.71e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093  10 DVAEKVLFGELFILDVRNEADYEDWKIEGkqvsSINRPYFDLLDGVDhiVSELPKDKDVLVVCAKEGSSIFVAEQLTEAG 89
Cdd:cd00158    1 ELKELLDDEDAVLLDVREPEEYAAGHIPG----AINIPLSELEERAA--LLELDKDKPIVVYCRSGNRSARAAKLLRKAG 74

                         90
                 ....*....|....
gi 970959093  90 LENIYYLAGGMKAW 103
Cdd:cd00158   75 GTNVYNLEGGMLAW 88
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 140-294 1.08e-17

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: 80.47  E-value: 1.08e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093 140 GEAAVIDAVRTVEAYEEFAKEHGVTITNVMDTHLHADHISGGRKLAEKVGGTYWLPPKDAE--------------EVVFS 205
Cdd:cd16322   22 GEAVLVDPGDESEKLLARFGTTGLTLLYILLTHAHFDHVGGVADLRRHPGAPVYLHPDDLPlyeaadlgakafglGIEPL 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093 206 YEP---LVEGSVITVGGtkIVIDALYSPGHTIGSTSFIV-DDSYLLSGDILFVDSIGRPDLAGKAEdwvSDLRNTLySRY 281
Cdd:cd16322  102 PPPdrlLEDGQTLTLGG--LEFKVLHTPGHSPGHVCFYVeEEGLLFSGDLLFQGSIGRTDLPGGDP---KAMAASL-RRL 175

                        170
                 ....*....|...
gi 970959093 282 KELSQNLVVLPAH 294
Cdd:cd16322  176 LTLPDETRVFPGH 188
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 139-294 8.60e-17

Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase domain; This subgroup includes Salmonella enterica serovar typhimurium YcbL which has type II hydroxyacylglutathione hydrolase (EC 3.1.2.6, also known as glyoxalase II) activity, and has a single metal ion binding site, and Thermus thermophilus TTHA1623 which does not have GLX2 activity and has two metal ion binding sites with a glyoxalase II-type metal coordination. 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: 293823 [Multi-domain]  Cd Length: 190  Bit Score: 77.59  E-value: 8.60e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093 139 NGEAAVIDAVRTVEAYEEFAKEHGVTITNVMDTHLHADHISGGRKLAEKVGGTYWLPPKDAEEVVFS------------Y 206
Cdd:cd07737   21 TKEAAVIDPGGDADKILQAIEDLGLTLKKILLTHGHLDHVGGAAELAEHYGVPIIGPHKEDKFLLENlpeqsqmfgfppA 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093 207 EPLV------EGSVITVGGtkIVIDALYSPGHTIGSTSFIVDDS-YLLSGDILFVDSIGRPDLA-GKAEDWVSDLRNTLY 278
Cdd:cd07737  101 EAFTpdrwleEGDTVTVGN--LTLEVLHCPGHTPGHVVFFNRESkLAIVGDVLFKGSIGRTDFPgGNHAQLIASIKEKLL 178

                        170
                 ....*....|....*.
gi 970959093 279 SrykeLSQNLVVLPAH 294
Cdd:cd07737  179 P----LGDDVTFIPGH 190
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 18-104 7.99e-14

Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single copy of this duplicated domain. The domain is found as a single copy in other proteins, including phosphatases and ubiquitin C-terminal hydrolases.


Pssm-ID: 425764 [Multi-domain]  Cd Length: 92  Bit Score: 66.74  E-value: 7.99e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093   18 GELFILDVRNEADYEDWKIEGkqvsSINRPYFDLLDGVDHI------VSELPKDKDVLVVCAKEGSSIFVAEQLTEAGLE 91
Cdd:pfam00581   4 GKVVLIDVRPPEEYAKGHIPG----AVNVPLSSLSLPPLPLlellekLLELLKDKPIVVYCNSGNRAAAAAALLKALGYK 79

                          90
                  ....*....|...
gi 970959093   92 NIYYLAGGMKAWS 104
Cdd:pfam00581  80 NVYVLDGGFEAWK 92
GlpE_ST cd01444
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ...
 18-103 1.31e-13

GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain superfamily. Unlike other rhodanese sulfurtransferases, GlpE is a single domain protein but indications are that it functions as a dimer. The active site contains a catalytically active cysteine.


Pssm-ID: 238721 [Multi-domain]  Cd Length: 96  Bit Score: 66.13  E-value: 1.31e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093  18 GELFILDVRNEADYEDWK--IEGKQVSSINRpyfdlldgVDHIVSELPKDKDVLVVCAKEGSSIFVAEQLTEAGLENIYY 95
Cdd:cd01444   15 EAPVLLDVRDPASYAALPdhIPGAIHLDEDS--------LDDWLGDLDRDRPVVVYCYHGNSSAQLAQALREAGFTDVRS 86


                 ....*...
gi 970959093  96 LAGGMKAW 103
Cdd:cd01444   87 LAGGFEAW 94
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 131-279 1.45e-13

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 69.79  E-value: 1.45e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093 131 CL----SYMVV--SNGEAAVIDAVRtVEAYEEFAKEHGVTITNVMDTHLHADHISGGRKLAEKV------GGTywlppkd 198
Cdd:PLN02469   8 CLednyAYLIIdeSTKDAAVVDPVD-PEKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIKKLVpgikvyGGS------- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093 199 AEEVVFSYEPLVEGSVITVGGTkIVIDALYSPGHTIGSTSFIV-----DDSYLLSGDILFVDSIGRpDLAGKAEDWVSDL 273
Cdd:PLN02469  80 LDNVKGCTHPVENGDKLSLGKD-VNILALHTPCHTKGHISYYVtgkegEDPAVFTGDTLFIAGCGK-FFEGTAEQMYQSL 157


                 ....*.
gi 970959093 274 RNTLYS 279
Cdd:PLN02469 158 CVTLGS 163
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 18-109 2.72e-12

Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The the Cysteine containing enzymatically active version of the domain is also found in the CDC25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and stress proteins such as Senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions with a loss of the cysteine are also seen in Dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases. These are likely to play a role in protein interactions.


Pssm-ID: 197731 [Multi-domain]  Cd Length: 100  Bit Score: 62.48  E-value: 2.72e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093    18 GELFILDVRNEADYEDWKIEGkqvsSINRPYFDLLDGVDHIVS----------ELPKDKDVLVVCAKEGSSIFVAEQLTE 87
Cdd:smart00450   3 EKVVLLDVRSPEEYEGGHIPG----AVNIPLSELLDRRGELDIlefeellkrlGLDKDKPVVVYCRSGNRSAKAAWLLRE 78

                           90       100
                   ....*....|....*....|..
gi 970959093    88 AGLENIYYLAGGMKAWSEYVKP 109
Cdd:smart00450  79 LGFKNVYLLDGGYKEWSAAGPP 100
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 133-250 1.36e-11

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: 62.89  E-value: 1.36e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093 133 SYMVVSNGEAAVID-------AVRTVEAYEEfakehGVTITNVMDTHLHADHISGGRKLAEKVGG-TYWLPPKDAEEVVF 204
Cdd:cd16278   20 TYLLGAPDGVVVIDpgpddpaHLDALLAALG-----GGRVSAILVTHTHRDHSPGAARLAERTGApVRAFGPHRAGGQDT 94

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 970959093 205 SYEP---LVEGSVITVGGTKIVidALYSPGHTIGSTSFIVDDS-YLLSGD 250
Cdd:cd16278   95 DFAPdrpLADGEVIEGGGLRLT--VLHTPGHTSDHLCFALEDEgALFTGD 142
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 142-338 2.42e-11

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 63.28  E-value: 2.42e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093 142 AAVIDAV-RTVEAYEEFAKEHGVTITNVMDTHLHADHISGGRKLAEKVGGTywlppkdaeEVVFSYEPLVEGSVITVGGT 220
Cdd:PLN02962  38 ALLIDPVdKTVDRDLSLVKELGLKLIYAMNTHVHADHVTGTGLLKTKLPGV---------KSIISKASGSKADLFVEPGD 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093 221 KIVIDALY-----SPGHTIGSTSFIVDDS-------YLLSGDILFVDSIGRPDLAGKAEDwvsDLRNTLYSRYKELSQNL 288
Cdd:PLN02962 109 KIYFGDLYlevraTPGHTAGCVTYVTGEGpdqpqprMAFTGDALLIRGCGRTDFQGGSSD---QLYKSVHSQIFTLPKDT 185

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 970959093 289 VVLPAHYSKisemnesGIVSAKLKDLFEHNAGLNiEDEGEFRKVVTE-NLP 338
Cdd:PLN02962 186 LIYPAHDYK-------GFTVSTVGEEMLYNPRLT-KDEETFKTIMENlNLP 228
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 133-250 2.67e-11

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: 61.93  E-value: 2.67e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093 133 SYMVVSNGEAAVIDA-VRTVEAYEEF------AKEHGVTITNVMDTHLHADHISGGRKLAEKVGGTYWLPPkdaeevvfs 205
Cdd:cd07725   17 VYLLRDGDETTLIDTgLATEEDAEALweglkeLGLKPSDIDRVLLTHHHPDHIGLAGKLQEKSGATVYILD--------- 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 970959093 206 YEPLVEGSVITVGGTKIVidALYSPGHTIGSTSFIVDDS-YLLSGD 250
Cdd:cd07725   88 VTPVKDGDKIDLGGLRLK--VIETPGHTPGHIVLYDEDRrELFVGD 131
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
130-294 5.14e-11

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 61.23  E-value: 5.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093  130 GCLSYMVVSNGEAAVIDAVRTVE-AYEEFAKEHGVTITNVMD---THLHADHISGGRKLAEKVGGTYWLPPKDAEE---- 201
Cdd:pfam00753   5 QVNSYLIEGGGGAVLIDTGGSAEaALLLLLAALGLGPKDIDAvilTHGHFDHIGGLGELAEATDVPVIVVAEEAREllde 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093  202 ---------VVFSYEPLVEGSVITVGGTKIVID------ALYSPGHTIGSTSF-IVDDSYLLSGDILFVDSIGRPDL-AG 264
Cdd:pfam00753  85 elglaasrlGLPGPPVVPLPPDVVLEEGDGILGgglgllVTHGPGHGPGHVVVyYGGGKVLFTGDLLFAGEIGRLDLpLG 164

                         170       180       190
                  ....*....|....*....|....*....|..
gi 970959093  265 KAEDWVSDLRNTLYSRYKELSQ--NLVVLPAH 294
Cdd:pfam00753 165 GLLVLHPSSAESSLESLLKLAKlkAAVIVPGH 196
RHOD_2 cd01528
Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes ...
 22-107 3.18e-09

Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes uncharacterized putative rhodanese-related domains.


Pssm-ID: 238786 [Multi-domain]  Cd Length: 101  Bit Score: 53.94  E-value: 3.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093  22 ILDVRNEADYEDWKIEGkqvsSINRPyfdlLDGVDHIVSELP---KDKDVLVVCAKEGSSIFVAEQLTEAGLENIYYLAG 98
Cdd:cd01528   20 LIDVREPEELEIAFLPG----FLHLP----MSEIPERSKELDsdnPDKDIVVLCHHGGRSMQVAQWLLRQGFENVYNLQG 91


                 ....*....
gi 970959093  99 GMKAWSEYV 107
Cdd:cd01528   92 GIDAWSLEV 100
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 159-294 5.14e-09

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: 56.07  E-value: 5.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093 159 KEHGVTITNVMD---THLHADHISGGRKLA-----------EKVGGTYWLPPKDAEEVVFSYEPLVEGSVITVGGTKIV- 223
Cdd:cd07729   80 ARLGLDPEDIDYvilSHLHFDHAGGLDLFPnatiivqraelEYATGPDPLAAGYYEDVLALDDDLPGGRVRLVDGDYDLf 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093 224 --IDALYSPGHTIGSTSFIVD---DSYLLSGD-ILFVDSIGRPDLAGkaedWVSDLRNTLYS--RYKELSQNL--VVLPA 293
Cdd:cd07729  160 pgVTLIPTPGHTPGHQSVLVRlpeGTVLLAGDaAYTYENLEEGRPPG----INYDPEAALASleRLKALAEREgaRVIPG 235


                 .
gi 970959093 294 H 294
Cdd:cd07729  236 H 236
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 136-274 2.14e-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: 53.72  E-value: 2.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093 136 VVSNGEAAVIDA---VRTVEAYEEFAKEH-GVTITNVMDTHLHADHISG----------------GRKLAEKVGGTYWLP 195
Cdd:cd16282   20 IVGDDGVVVIDTgasPRLARALLAAIRKVtDKPVRYVVNTHYHGDHTLGnaafadagapiiahenTREELAARGEAYLEL 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093 196 PKDAEEVVFSYEPLV-------EGSVITVGGTKIVIDALySPGHTIGSTS-FIVDDSYLLSGDILFVDSIGrPDLAGKAE 267
Cdd:cd16282  100 MRRLGGDAMAGTELVlpdrtfdDGLTLDLGGRTVELIHL-GPAHTPGDLVvWLPEEGVLFAGDLVFNGRIP-FLPDGSLA 177


                 ....*..
gi 970959093 268 DWVSDLR 274
Cdd:cd16282  178 GWIAALD 184
RHOD_Pyr_redox cd01524
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ...
 19-104 2.37e-08

Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus lactis NADH oxidase, Bacillus cereus NADH dehydrogenase, and Bacteroides thetaiotaomicron pyridine nucleotide-disulphide oxidoreductase, and similar rhodanese-like domains found C-terminal of the pyridine nucleotide-disulphide oxidoreductase (Pyr-redox) domain and the Pyr-redox dimerization domain.


Pssm-ID: 238782 [Multi-domain]  Cd Length: 90  Bit Score: 51.11  E-value: 2.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093  19 ELFILDVRNEADYEDWKIEGkqvsSINRPYFDLLDGVDhivsELPKDKDVLVVCAKEGSSIFVAEQLTEAGLeNIYYLAG 98
Cdd:cd01524   13 GVTLIDVRTPQEFEKGHIKG----AINIPLDELRDRLN----ELPKDKEIIVYCAVGLRGYIAARILTQNGF-KVKNLDG 83


                 ....*.
gi 970959093  99 GMKAWS 104
Cdd:cd01524   84 GYKTYS 89
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
2-112 1.37e-07

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 52.71  E-value: 1.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093   2 SVKPLQAKDVAEKvlfGELFIlDVRNEADYEDWKIEGkqVSSINRPYFDLldgvdHIVSELP-KDKDVLVVCAKEGSSIF 80
Cdd:PRK08762   4 EISPAEARARAAQ---GAVLI-DVREAHERASGQAEG--ALRIPRGFLEL-----RIETHLPdRDREIVLICASGTRSAH 72

                         90       100       110
                 ....*....|....*....|....*....|..
gi 970959093  81 VAEQLTEAGLENIYYLAGGMKAWSEYVKPIKV 112
Cdd:PRK08762  73 AAATLRELGYTRVASVAGGFSAWKDAGLPLER 104
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 103-239 5.65e-07

Caulobacter crescentus Mbl1b 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 Mbl1b-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: 293868  Cd Length: 252  Bit Score: 50.14  E-value: 5.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093 103 WSEYVKPIKVGDlknggSMYQFKRLGKGclSYMVVSNGEAAVIDAV--RTVEAYEEFAKEHGVTITNV---MDTHLHADH 177
Cdd:cd16310    1 WTAPTEPFRIVD-----NIYYVGTKGIG--SYLITSNHGAILLDGGleENAALIEQNIKALGFKLSDIkiiINTHAHYDH 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093 178 ISGGRKLAEKVGGTYWLPPKDAEEVV------------FSYEP------LVEGSVITVGGTKIVidALYSPGHTIGSTSF 239
Cdd:cd16310   74 AGGLAQLKADTGAKLWASRGDRPALEagkhigdnitqpAPFPAvkvdriLGDGEKIKLGDITLT--ATLTPGHTKGCTTW 151
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 171-242 9.45e-07

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: 49.51  E-value: 9.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093 171 THLHADHISGGRKLAEKVGGTYWLPPKDAEEVVFSYEP---------------LVEGSVITVGGTKivIDALYSPGHTIG 235
Cdd:cd16280   68 THGHGDHYGGAAYLKDLYGAKVVMSEADWDMMEEPPEEgdnprwgppperdivIKDGDTLTLGDTT--ITVYLTPGHTPG 145


                 ....*..
gi 970959093 236 STSFIVD 242
Cdd:cd16280  146 TLSLIFP 152
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 133-258 1.36e-06

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: 48.64  E-value: 1.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093 133 SYMVVSNGEAAVIDA--VRTVEAYEEFAKEHGVT---ITNVMDTHLHADHISG-GR------------------------ 182
Cdd:cd07726   18 SYLLDGEGRPALIDTgpSSSVPRLLAALEALGIApedVDYIILTHIHLDHAGGaGLlaealpnakvyvhprgarhlidps 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093 183 KL---AEKVGG----TYWLPPK--DAEEVVfsyePLVEGSVITVGGTKIVidALYSPGHTIGSTSFIVDDSyllsgDILF 253
Cdd:cd07726   98 KLwasARAVYGdeadRLGGEILpvPEERVI----VLEDGETLDLGGRTLE--VIDTPGHAPHHLSFLDEES-----DGLF 166


                 ....*.
gi 970959093 254 V-DSIG 258
Cdd:cd07726  167 TgDAAG 172
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 134-259 1.53e-06

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: 48.37  E-value: 1.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093 134 YMVVSNGEAAVIDA--VRTVEAYEEFAKEHGVT---ITNVMDTHLHADHISGGRKLAEK--------------------- 187
Cdd:cd07721   14 YLIEDDDGLTLIDTglPGSAKRILKALRELGLSpkdIRRILLTHGHIDHIGSLAALKEApgapvyahereapylegekpy 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093 188 --------VGGTYWLPPKDAEEVVfsyEPLVEGSVITVGGTkivIDALYSPGHTIGSTSFIV-DDSYLLSGDiLFVDSIG 258
Cdd:cd07721   94 pppvrlglLGLLSPLLPVKPVPVD---RTLEDGDTLDLAGG---LRVIHTPGHTPGHISLYLeEDGVLIAGD-ALVTVGG 166


                 .
gi 970959093 259 R 259
Cdd:cd07721  167 E 167
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 165-263 4.39e-06

Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold metallo hydrolase domain; Pseudomonas pseudoalcaligenes OPHC2 is a thermostable organophosphorus hydrolase which a broad substrate activity spectrum: it hydrolyzes various phosphotriesters, esters, and a lactone. This subgroup also includes Pseudomonas oleovorans PoOPH which exhibits high lactonase and esterase activities, and latent PTE activity. However, double mutations His250Ile/Ile263Trp switch PoOPH into an efficient and thermostable PTE. 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: 293806 [Multi-domain]  Cd Length: 251  Bit Score: 47.54  E-value: 4.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093 165 ITNVMDTHLHADHISG----GRKLAEK-----VGGT---YWL-------PPKDAEEVVFSYEPLV---EGSVITVGGTKI 222
Cdd:cd07720   92 IDDVLLTHLHPDHIGGlvdaGGKPVFPnaevhVSEAewdFWLddanaakAPEGAKRFFDAARDRLrpyAAAGRFEDGDEV 171

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 970959093 223 V--IDALYSPGHTIGSTSFIV---DDSYLLSGDILFVD--SIGRPDLA 263
Cdd:cd07720  172 LpgITAVPAPGHTPGHTGYRIesgGERLLIWGDIVHHPalQFAHPDWT 219
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 140-257 6.97e-06

uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold metallo hydrolase domain; Includes functionally uncharacterized human lactamase beta 2. 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: 293808 [Multi-domain]  Cd Length: 188  Bit Score: 45.99  E-value: 6.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093 140 GEAAVIDAVRTVeayeeFAKEHGVTITNVMDTHLHADHIsGG----RKLAEKVGGTYW---LPPKDAEEVVFS--YEPLV 210
Cdd:cd07722   37 GRPSYIPLLKSV-----LDSEGNATISDILLTHWHHDHV-GGlpdvLDLLRGPSPRVYkfpRPEEDEDPDEDGgdIHDLQ 110

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 970959093 211 EGSVITVGGTKIVidALYSPGHTIGSTSFivddsYLLSGDILFV-DSI 257
Cdd:cd07722  111 DGQVFKVEGATLR--VIHTPGHTTDHVCF-----LLEEENALFTgDCV 151
GOB1-like_MBL-B3 cd16308
Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; ...
 171-242 4.87e-05

Elizabethkingia meningoseptica GOB-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 GOB-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: 293866 [Multi-domain]  Cd Length: 254  Bit Score: 44.38  E-value: 4.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093 171 THLHADHISGGRKLAEKVGGTYWLPPKDAEEVV-------------FSYEP------LVEGSVITVGGTKIVIdaLYSPG 231
Cdd:cd16308   67 TQAHYDHVGAMAAIKQQTGAKMMVDEKDAKVLAdggksdyemggygSTFAPvkadklLHDGDTIKLGGTKLTL--LHHPG 144

                         90
                 ....*....|.
gi 970959093 232 HTIGSTSFIVD 242
Cdd:cd16308  145 HTKGSCSFLFD 155
RHOD_ThiF cd01526
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ...
 22-109 5.91e-05

Member of the Rhodanese Homology Domain superfamily. This CD includes several putative molybdopterin synthase sulfurylases including the molybdenum cofactor biosynthetic protein (CnxF) of Aspergillus nidulans and the molybdenum cofactor synthesis protein 3 (MOCS3) of Homo sapiens. These rhodanese-like domains are found C-terminal of the ThiF and MoeZ_MoeB domains.


Pssm-ID: 238784 [Multi-domain]  Cd Length: 122  Bit Score: 42.30  E-value: 5.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093  22 ILDVRNEADYEDWKIEGkqvsSINRPYFDLLDGVDHIVSELP------KDKDVLVVCAKEGSSIFVAEQLTEAGLE-NIY 94
Cdd:cd01526   27 LLDVRPKVHFEICRLPE----AINIPLSELLSKAAELKSLQElpldndKDSPIYVVCRRGNDSQTAVRKLKELGLErFVR 102

                         90
                 ....*....|....*
gi 970959093  95 YLAGGMKAWSEYVKP 109
Cdd:cd01526  103 DIIGGLKAWADKVDP 117
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 171-277 6.47e-05

BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; This subgroup of B3 subclass MBLs includes Bradyrhizobium diazoefficiens BJP-1, Fluoribacter gormanii FEZ-1, Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) GOB-1, Caulobacter crescentus Mbl1b. 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 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: 293846 [Multi-domain]  Cd Length: 254  Bit Score: 43.85  E-value: 6.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093 171 THLHADHISGGRKLAEKVGGTYWLPPKDAEEV-------------VFSYEP------LVEGSVITVGGTKIVidALYSPG 231
Cdd:cd16288   67 SHAHLDHAGGLAALKKLTGAKLMASAEDAALLasggksdfhygddSLAFPPvkvdrvLKDGDRVTLGGTTLT--AHLTPG 144

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 970959093 232 HTIGSTSFIVDDSYllSG---DILFVDSIGRPD---LAGKAE--DWVSDLRNTL 277
Cdd:cd16288  145 HTRGCTTWTMTVKD--DGkvyQVVFADSLTVNPgykLVGNPTypGIAEDYRHSF 196
4RHOD_Repeats cd01529
Member of the Rhodanese Homology Domain superfamily. This CD includes putative ...
 19-103 8.48e-05

Member of the Rhodanese Homology Domain superfamily. This CD includes putative rhodanese-related sulfurtransferases which contain 4 copies of the Rhodanese Homology Domain. Only the second and most of the fourth repeats contain the putative catalytic Cys residue. This CD aligns the 1st , 2nd, 3rd, and 4th repeats.


Pssm-ID: 238787 [Multi-domain]  Cd Length: 96  Bit Score: 41.12  E-value: 8.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093  19 ELFILDVRNEADYEDWKIEGKqvssINRPYFDLLDGVDHIVSELPKDKD--VLVVCAKEGSSIFVAEQLTEAGLENIYYL 96
Cdd:cd01529   12 GTALLDVRAEDEYAAGHLPGK----RSIPGAALVLRSQELQALEAPGRAtrYVLTCDGSLLARFAAQELLALGGKPVALL 87


                 ....*..
gi 970959093  97 AGGMKAW 103
Cdd:cd01529   88 DGGTSAW 94
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 136-259 1.01e-04

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 43.68  E-value: 1.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093 136 VVSNGEAA-VIDAVrtveayeefaKEHGVTITNVMDTHLHADHISGGRKLAEKVGGTYWLPPKDAEEVVFSYEPLVEGSV 214
Cdd:PLN02398 102 VVDPSEAVpVIDAL----------SRKNRNLTYILNTHHHYDHTGGNLELKARYGAKVIGSAVDKDRIPGIDIVLKDGDK 171

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 970959093 215 ITVGGTKIVIdaLYSPGHTIGSTSFIVDDS-YLLSGDILFVDSIGR 259
Cdd:PLN02398 172 WMFAGHEVLV--METPGHTRGHISFYFPGSgAIFTGDTLFSLSCGK 215
YmaE-like_MBL-fold cd07727
uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold ...
 130-256 1.26e-04

uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold metallo hydrolase domain; Includes the uncharacterized Bacillus subtilis YmaE and Nostoc all1228 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. 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: 293813 [Multi-domain]  Cd Length: 181  Bit Score: 42.18  E-value: 1.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093 130 GCLSYMVVSNGEAAVIDAVRTVEAYEEFAKEHG----VTITnvmdthlHADHISGGRKLAEKVGGTYWLPPKDAEEVVFS 205
Cdd:cd07727   14 GAASYLILRPEGNILVDSPRYSPPLAKRIEALGgiryIFLT-------HRDDVADHAKWAERFGAKRIIHEDDVNAVTRP 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 970959093 206 YEPLVEGSVITVGGTKIViDALYSPGHTIGSTSFIVDDS-YLLSGDILFVDS 256
Cdd:cd07727   87 DEVIVLWGGDPWELDPDL-TLIPVPGHTRGSVVLLYKEKgVLFTGDHLAWSR 137
Polysulfide_ST cd01447
Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as ...
 62-105 1.32e-04

Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as a polysulfide binding and transferase domain in anaerobic gram-negative bacteria, functioning in oxidative phosphorylation with polysulfide-sulfur as a terminal electron acceptor. The active site contains the same conserved cysteine that is the catalytic residue in other Rhodanese Homology Domain proteins.


Pssm-ID: 238724 [Multi-domain]  Cd Length: 103  Bit Score: 40.87  E-value: 1.32e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 970959093  62 LPKDKDVLVVCAKEGSSIFVAEQLTEAGLENIYYLAGGMKAWSE 105
Cdd:cd01447   58 FAEDKPFVFYCASGWRSALAGKTLQDMGLKPVYNIEGGFKDWKE 101
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 159-294 1.50e-04

uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized human MBLAC2 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: 293798 [Multi-domain]  Cd Length: 182  Bit Score: 42.23  E-value: 1.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093 159 KEHGVTITN----VMDTHLHADHIsGGRKLAEKVggtyWLPPKDAE------------EVVFSYE--------PLVEGSV 214
Cdd:cd07712   33 KEYVRTLTDlpllVVATHGHFDHI-GGLHEFEEV----YVHPADAEilaapdnfetltWDAATYSvppagptlPLRDGDV 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093 215 ITVGGtkIVIDALYSPGHTIGSTSFI-VDDSYLLSGDILFVDSI-----GRPdlagkaedwVSDLRNTLYsRYKELSQNL 288
Cdd:cd07712  108 IDLGD--RQLEVIHTPGHTPGSIALLdRANRLLFSGDVVYDGPLimdlpHSD---------LDDYLASLE-KLSKLPDEF 175


                 ....*..
gi 970959093 289 -VVLPAH 294
Cdd:cd07712  176 dKVLPGH 182
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
1-109 1.70e-04

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 43.18  E-value: 1.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093   1 MSVKPLQAK-DVAEKvlfgELFILDVRNEADYEDWKIEGKQVssINRPYFDLLDGVDHiVSELPKDKDVLVVCAKEGSSI 79
Cdd:PRK07411 284 MTVTELKALlDSGAD----DFVLIDVRNPNEYEIARIPGSVL--VPLPDIENGPGVEK-VKELLNGHRLIAHCKMGGRSA 356

                         90       100       110
                 ....*....|....*....|....*....|
gi 970959093  80 FVAEQLTEAGLENIYyLAGGMKAWSEYVKP 109
Cdd:PRK07411 357 KALGILKEAGIEGTN-VKGGITAWSREVDP 385
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 171-294 2.78e-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) for which this fold was named perform only a small fraction of the activities included in this superfamily.Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry. Some members of this subgroup are annotated as GumP protein.


Pssm-ID: 293816 [Multi-domain]  Cd Length: 250  Bit Score: 41.87  E-value: 2.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093 171 THLHADHISG-----------GRKLAEKVGGTYW-------LPPKDAEEVVFSYEPLVEGSVITVGGTK----------I 222
Cdd:cd07730   90 SHLHWDHIGGlsdfpnarlivGPGAKEALRPPGYpsgflpeLLPSDFEGRLVRWEEDDFLWVPLGPFPRaldlfgdgslY 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093 223 VIDAlysPGHTIGSTSFIVDDS----YLLSGDI------LFVDSIGRPDLAGKAEDWVSDLRNTLySRYKELSQ--NLVV 290
Cdd:cd07730  170 LVDL---PGHAPGHLGLLARTTsgtwVFLAGDAchhrigLLRPSPLLPLPDLDDGADREAARETL-ARLRELDAapDVRV 245


                 ....
gi 970959093 291 LPAH 294
Cdd:cd07730  246 VLAH 249
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 19-109 3.25e-04

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 42.39  E-value: 3.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093  19 ELFILDVRNEADYEDWKIEGKQVSsinrPYFDLLDGvdHIVSELPKDKDVLVVCAKEGSSIFVAEQLTEAGLENIYYLAG 98
Cdd:PRK07878 303 KIALIDVREPVEWDIVHIPGAQLI----PKSEILSG--EALAKLPQDRTIVLYCKTGVRSAEALAALKKAGFSDAVHLQG 376

                         90
                 ....*....|.
gi 970959093  99 GMKAWSEYVKP 109
Cdd:PRK07878 377 GVVAWAKQVDP 387
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 22-106 3.91e-04

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 42.17  E-value: 3.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093  22 ILDVRNEADYEDWKIEGkqvsSINRPYFDLLDGvdHIVSELPKDKDVLVVCAKEGSSIFVAEQLTEAGLENIYYLAGGMK 101
Cdd:PRK05597 277 LIDVREPSEFAAYSIPG----AHNVPLSAIREG--ANPPSVSAGDEVVVYCAAGVRSAQAVAILERAGYTGMSSLDGGIE 350


                 ....*
gi 970959093 102 AWSEY 106
Cdd:PRK05597 351 GWLDS 355
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 136-253 5.17e-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: 293829 [Multi-domain]  Cd Length: 197  Bit Score: 40.59  E-value: 5.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093 136 VVSNGEAAVID------AVRTVEayeEFAKEHGVTITNVMDTHLHADHISGGRKLAEKVGGTYWLPPKDAE-------EV 202
Cdd:cd07743   14 VFGDKEALLIDsgldedAGRKIR---KILEELGWKLKAIINTHSHADHIGGNAYLQKKTGCKVYAPKIEKAfienpllEP 90

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 970959093 203 VFSY--------------------EPLVEGSVITVGGTKIVIDALysPGHTIGSTSFIVDDSYLLSGDILF 253
Cdd:cd07743   91 SYLGgayppkelrnkflmakpskvDDIIEEGELELGGVGLEIIPL--PGHSFGQIGILTPDGVLFAGDALF 159
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 139-251 8.14e-04

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: 40.61  E-value: 8.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093 139 NGEAAVIDA---------VRTVEAYeefAKEHGVT-ITNVMDTHLHADHISGGRKLAEKVG-GTYWLPPKDAEEVVF--- 204
Cdd:COG2333   20 DGKTILIDTgprpsfdagERVVLPY---LRALGIRrLDLLVLTHPDADHIGGLAAVLEAFPvGRVLVSGPPDTSETYerl 96

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 970959093 205 ---------SYEPLVEGSVITVGGtkIVIDALYSPGHTIGSTS-------FIVDD---SYLLSGDI 251
Cdd:COG2333   97 lealkekgiPVRPCRAGDTWQLGG--VRFEVLWPPEDLLEGSDennnslvLRLTYggfSFLLTGDA 160
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
133-257 1.51e-03

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 39.79  E-value: 1.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093 133 SYMVVSNGEAAVIDA-----VRTVEAYEEFAKehgvtITNVMDTHLHADHISGgrklaekVGG---TYWLP--------- 195
Cdd:COG1234   21 SYLLEAGGERLLIDCgegtqRQLLRAGLDPRD-----IDAIFITHLHGDHIAG-------LPGllsTRSLAgrekpltiy 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093 196 -PKDAEEVV--------------FSYEPLVEGSVITVGGTKIVIDALYspgHTIGSTSFIVDD---SYLLSGDILFVDSI 257
Cdd:COG1234   89 gPPGTKEFLeallkasgtdldfpLEFHEIEPGEVFEIGGFTVTAFPLD---HPVPAYGYRFEEpgrSLVYSGDTRPCEAL 165
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 128-251 2.50e-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: 38.65  E-value: 2.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093 128 GKGcLSYMVVSNGEAAVIDA-------VRTVEAYeefAKEHGVT-ITNVMDTHLHADHISGGRKLAEKV-GGTYWLPPKD 198
Cdd:cd07731    8 GQG-DAILIQTPGKTILIDTgprdsfgEDVVVPY---LKARGIKkLDYLILTHPDADHIGGLDAVLKNFpVKEVYMPGVT 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 970959093 199 AEEVVF------------SYEPLVEGSVITVGGTKIVIdalYSPGHTIGST----SfIV------DDSYLLSGDI 251
Cdd:cd07731   84 HTTKTYedlldaikekgiPVTPCKAGDRWQLGGVSFEV---LSPPKDDYDDlnnnS-CVlrltygGTSFLLTGDA 154
RHOD_1 cd01522
Member of the Rhodanese Homology Domain superfamily, subgroup 1. This CD includes the putative ...
 21-94 4.40e-03

Member of the Rhodanese Homology Domain superfamily, subgroup 1. This CD includes the putative rhodanese-related sulfurtransferases of several uncharacterized proteins.


Pssm-ID: 238780 [Multi-domain]  Cd Length: 117  Bit Score: 36.54  E-value: 4.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970959093  21 FILDVRNEADyedWKIEGKQVSSINRPYFDLLDG------VDHIVSELPKDKDVLVVCAKEGSSIFVAEQLTEAGLENIY 94
Cdd:cd01522   17 VLVDVRTEAE---WKFVGGVPDAVHVAWQVYPDMeinpnfLAELEEKVGKDRPVLLLCRSGNRSIAAAEAAAQAGFTNVY 93
 
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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