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Conserved domains on  [gi|446375420|ref|WP_000453275|]
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MULTISPECIES: rhodanese-like domain-containing protein [Bacillus]

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 3.44e-64

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: 202.24  E-value: 3.44e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420 122 YQFNRLGKGCLSYMVVSN--GEAAVIDAIR-TVEAYEQFAKENGVTITNVMDTHLHADHISGGRKLAEKVGGTYWLPPKD 198
Cdd:cd07724    3 RQFFDPGLGTLSYLVGDPetGEAAVIDPVRdSVDRYLDLAAELGLKITYVLETHVHADHVSGARELAERTGAPIVIGEGA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420 199 aeEVVFSYEPLVEGSVITVGGTKIEidALYSPGHTIGSTSFIV-DNSYLLSGDILFVDSIGRPDLAGKAEDWVSDLRNTL 277
Cdd:cd07724   83 --PASFFDRLLKDGDVLELGNLTLE--VLHTPGHTPESVSYLVgDPDAVFTGDTLFVGDVGRPDLPGEAEGLARQLYDSL 158

                        170
                 ....*....|....*....
gi 446375420 278 YSRYKELSQSLIVLPAHYS 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 1.51e-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: 151.49  E-value: 1.51e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420   6 LQAKDVAEKVLFGE-LFILDVRNETDYEDWKIEGKQISSINKPYFDLLDGVDQIVSELPKDKDVLVVCAKEGSSIFVAEQ 84
Cdd:cd01523    1 LDPEDLYARLLAGQpLFILDVRNESDYERWKIDGENNTPYFDPYFDFLEIEEDILDQLPDDQEVTVICAKEGSSQFVAEL 80

                         90       100
                 ....*....|....*....|.
gi 446375420  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 3.44e-64

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: 202.24  E-value: 3.44e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420 122 YQFNRLGKGCLSYMVVSN--GEAAVIDAIR-TVEAYEQFAKENGVTITNVMDTHLHADHISGGRKLAEKVGGTYWLPPKD 198
Cdd:cd07724    3 RQFFDPGLGTLSYLVGDPetGEAAVIDPVRdSVDRYLDLAAELGLKITYVLETHVHADHVSGARELAERTGAPIVIGEGA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420 199 aeEVVFSYEPLVEGSVITVGGTKIEidALYSPGHTIGSTSFIV-DNSYLLSGDILFVDSIGRPDLAGKAEDWVSDLRNTL 277
Cdd:cd07724   83 --PASFFDRLLKDGDVLELGNLTLE--VLHTPGHTPESVSYLVgDPDAVFTGDTLFVGDVGRPDLPGEAEGLARQLYDSL 158

                        170
                 ....*....|....*....
gi 446375420 278 YSRYKELSQSLIVLPAHYS 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 1.51e-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: 151.49  E-value: 1.51e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420   6 LQAKDVAEKVLFGE-LFILDVRNETDYEDWKIEGKQISSINKPYFDLLDGVDQIVSELPKDKDVLVVCAKEGSSIFVAEQ 84
Cdd:cd01523    1 LDPEDLYARLLAGQpLFILDVRNESDYERWKIDGENNTPYFDPYFDFLEIEEDILDQLPDDQEVTVICAKEGSSQFVAEL 80

                         90       100
                 ....*....|....*....|.
gi 446375420  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 9.59e-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: 124.42  E-value: 9.59e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420 126 RLGKGCLSYMVVSNGEAAVIDA---IRTVEAYEQFAKENGVTITNVMDTHLHADHISGGRKLAEKVGGTYWLPPKDAE-- 200
Cdd:COG0491   10 GAGLGVNSYLIVGGDGAVLIDTglgPADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFGAPVYAHAAEAEal 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420 201 -----------EVVFSYEPLVEGSVITVGGTKIEIdaLYSPGHTIGSTSFIV-DNSYLLSGDILFVDSIGRPDLAGK-AE 267
Cdd:COG0491   90 eapaagalfgrEPVPPDRTLEDGDTLELGGPGLEV--IHTPGHTPGHVSFYVpDEKVLFTGDALFSGGVGRPDLPDGdLA 167

                        170       180
                 ....*....|....*....|....*..
gi 446375420 268 DWVSDLRntlysRYKELSQSlIVLPAH 294
Cdd:COG0491  168 QWLASLE-----RLLALPPD-LVIPGH 188
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 1-114 1.08e-25

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: 99.66  E-value: 1.08e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420   1 MEVKSLQAKDVAEKVLFGELFILDVRNETDYEDWKIEGkqisSINKPYFDLldgvDQIVSELPKDKDVLVVCAKEGSSIF 80
Cdd:COG0607    1 ASVKEISPAELAELLESEDAVLLDVREPEEFAAGHIPG----AINIPLGEL----AERLDELPKDKPIVVYCASGGRSAQ 72

                         90       100       110
                 ....*....|....*....|....*....|....
gi 446375420  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 3.92e-21

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: 89.53  E-value: 3.92e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420   133 SYMVVSNGEAAVIDA-IRTVEAYEQFAKENGV-TITNVMDTHLHADHISGGRKLAEKVGGTYWLPPKDAE---------- 200
Cdd:smart00849   2 SYLVRDDGGAILIDTgPGEAEDLLAELKKLGPkKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAEllkdllallg 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420   201 ------EVVFSYEPLVEGSVITVGGTKIEIdaLYSPGHTIGSTSFIV-DNSYLLSGDILFVDSIGRPDLagkaeDWVSDL 273
Cdd:smart00849  82 elgaeaEPAPPDRTLKDGDELDLGGGELEV--IHTPGHTPGSIVLYLpEGKILFTGDLLFAGGDGRTLV-----DGGDAA 154

                          170       180
                   ....*....|....*....|...
gi 446375420   274 RNTLYSRYKELSQSL--IVLPAH 294
Cdd:smart00849 155 ASDALESLLKLLKLLpkLVVPGH 177
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 18-104 5.43e-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: 67.12  E-value: 5.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420   18 GELFILDVRNETDYEDWKIEGkqisSINKPYFDLLDGVDQI------VSELPKDKDVLVVCAKEGSSIFVAEQLTEAGLE 91
Cdd:pfam00581   4 GKVVLIDVRPPEEYAKGHIPG----AVNVPLSSLSLPPLPLlellekLLELLKDKPIVVYCNSGNRAAAAAALLKALGYK 79

                          90
                  ....*....|...
gi 446375420   92 NIYYLAGGMKAWS 104
Cdd:pfam00581  80 NVYVLDGGFEAWK 92
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 131-279 9.81e-14

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 70.56  E-value: 9.81e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420 131 CL----SYMVV--SNGEAAVIDAIRtVEAYEQFAKENGVTITNVMDTHLHADHISGGRKLAEKV------GGTywlppkd 198
Cdd:PLN02469   8 CLednyAYLIIdeSTKDAAVVDPVD-PEKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIKKLVpgikvyGGS------- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420 199 AEEVVFSYEPLVEGSVITVGGTkIEIDALYSPGHTIGSTSFIVDN-----SYLLSGDILFVDSIGRpDLAGKAEDWVSDL 273
Cdd:PLN02469  80 LDNVKGCTHPVENGDKLSLGKD-VNILALHTPCHTKGHISYYVTGkegedPAVFTGDTLFIAGCGK-FFEGTAEQMYQSL 157


                 ....*.
gi 446375420 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 2.19e-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: 62.86  E-value: 2.19e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420    18 GELFILDVRNETDYEDWKIEGkqisSINKPYFDLLDGVDQIVS----------ELPKDKDVLVVCAKEGSSIFVAEQLTE 87
Cdd:smart00450   3 EKVVLLDVRSPEEYEGGHIPG----AVNIPLSELLDRRGELDIlefeellkrlGLDKDKPVVVYCRSGNRSAKAAWLLRE 78

                           90       100
                   ....*....|....*....|..
gi 446375420    88 AGLENIYYLAGGMKAWSEYVKP 109
Cdd:smart00450  79 LGFKNVYLLDGGYKEWSAAGPP 100
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
130-294 1.12e-11

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 63.16  E-value: 1.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420  130 GCLSYMVVSNGEAAVIDA----IRTVEAYEQFAKENGVTITNVMDTHLHADHISGGRKLAEKVGGTYWLPPKDAEE---- 201
Cdd:pfam00753   5 QVNSYLIEGGGGAVLIDTggsaEAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEAREllde 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420  202 ---VVFSYEPLV-EGSVITVGGTKIEIDALYS---------PGHTIGSTSFIV---DNSYLLSGDILFVDSIGRPDL-AG 264
Cdd:pfam00753  85 elgLAASRLGLPgPPVVPLPPDVVLEEGDGILggglgllvtHGPGHGPGHVVVyygGGKVLFTGDLLFAGEIGRLDLpLG 164

                         170       180       190
                  ....*....|....*....|....*....|..
gi 446375420  265 KAEDWVSDLRNTLYSRYKELSQS--LIVLPAH 294
Cdd:pfam00753 165 GLLVLHPSSAESSLESLLKLAKLkaAVIVPGH 196
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
2-112 6.93e-07

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 50.78  E-value: 6.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420   2 EVKSLQAKDVAEKVLFGELFIlDVRNETDYEDWKIEGKQisSINKPYFDLldgvdQIVSELP-KDKDVLVVCAKEGSSIF 80
Cdd:PRK08762   1 SIREISPAEARARAAQGAVLI-DVREAHERASGQAEGAL--RIPRGFLEL-----RIETHLPdRDREIVLICASGTRSAH 72

                         90       100       110
                 ....*....|....*....|....*....|..
gi 446375420  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 3.44e-64

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: 202.24  E-value: 3.44e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420 122 YQFNRLGKGCLSYMVVSN--GEAAVIDAIR-TVEAYEQFAKENGVTITNVMDTHLHADHISGGRKLAEKVGGTYWLPPKD 198
Cdd:cd07724    3 RQFFDPGLGTLSYLVGDPetGEAAVIDPVRdSVDRYLDLAAELGLKITYVLETHVHADHVSGARELAERTGAPIVIGEGA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420 199 aeEVVFSYEPLVEGSVITVGGTKIEidALYSPGHTIGSTSFIV-DNSYLLSGDILFVDSIGRPDLAGKAEDWVSDLRNTL 277
Cdd:cd07724   83 --PASFFDRLLKDGDVLELGNLTLE--VLHTPGHTPESVSYLVgDPDAVFTGDTLFVGDVGRPDLPGEAEGLARQLYDSL 158

                        170
                 ....*....|....*....
gi 446375420 278 YSRYKELSQSLIVLPAHYS 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 1.51e-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: 151.49  E-value: 1.51e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420   6 LQAKDVAEKVLFGE-LFILDVRNETDYEDWKIEGKQISSINKPYFDLLDGVDQIVSELPKDKDVLVVCAKEGSSIFVAEQ 84
Cdd:cd01523    1 LDPEDLYARLLAGQpLFILDVRNESDYERWKIDGENNTPYFDPYFDFLEIEEDILDQLPDDQEVTVICAKEGSSQFVAEL 80

                         90       100
                 ....*....|....*....|.
gi 446375420  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 9.59e-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: 124.42  E-value: 9.59e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420 126 RLGKGCLSYMVVSNGEAAVIDA---IRTVEAYEQFAKENGVTITNVMDTHLHADHISGGRKLAEKVGGTYWLPPKDAE-- 200
Cdd:COG0491   10 GAGLGVNSYLIVGGDGAVLIDTglgPADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFGAPVYAHAAEAEal 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420 201 -----------EVVFSYEPLVEGSVITVGGTKIEIdaLYSPGHTIGSTSFIV-DNSYLLSGDILFVDSIGRPDLAGK-AE 267
Cdd:COG0491   90 eapaagalfgrEPVPPDRTLEDGDTLELGGPGLEV--IHTPGHTPGHVSFYVpDEKVLFTGDALFSGGVGRPDLPDGdLA 167

                        170       180
                 ....*....|....*....|....*..
gi 446375420 268 DWVSDLRntlysRYKELSQSlIVLPAH 294
Cdd:COG0491  168 QWLASLE-----RLLALPPD-LVIPGH 188
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 139-294 1.63e-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: 109.68  E-value: 1.63e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420 139 NGEAAVIDA-IRTVEAYEQFAKENGVTITNVMDTHLHADHISGGRKLAEKVGGTYWLPPKDAE----------------- 200
Cdd:cd06262   19 EGEAILIDPgAGALEKILEAIEELGLKIKAILLTHGHFDHIGGLAELKEAPGAPVYIHEADAElledpelnlaffgggpl 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420 201 EVVFSYEPLVEGSVITVGGTKIEIdaLYSPGHTIGSTSFIVDNS-YLLSGDILFVDSIGRPDLAGKAEDwvsDLRNTLYS 279
Cdd:cd06262   99 PPPEPDILLEDGDTIELGGLELEV--IHTPGHTPGSVCFYIEEEgVLFTGDTLFAGSIGRTDLPGGDPE---QLIESIKK 173

                        170
                 ....*....|....*
gi 446375420 280 RYKELSQSLIVLPAH 294
Cdd:cd06262  174 LLLLLPDDTVVYPGH 188
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 1-114 1.08e-25

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: 99.66  E-value: 1.08e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420   1 MEVKSLQAKDVAEKVLFGELFILDVRNETDYEDWKIEGkqisSINKPYFDLldgvDQIVSELPKDKDVLVVCAKEGSSIF 80
Cdd:COG0607    1 ASVKEISPAELAELLESEDAVLLDVREPEEFAAGHIPG----AINIPLGEL----AERLDELPKDKPIVVYCASGGRSAQ 72

                         90       100       110
                 ....*....|....*....|....*....|....
gi 446375420  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 1.54e-24

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: 98.76  E-value: 1.54e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420 133 SYMVV--SNGEAAVIDAIRTVEAYEQFAKENGVTITNVMDTHLHADHISGGRKLAEKVGGTYWLPPKDAEEVVFSYEPLV 210
Cdd:cd16275   14 SYIIIdkATREAAVVDPAWDIEKILAKLNELGLTLTGILLTHSHFDHVNLVEPLLAKYDAPVYMSKEEIDYYGFRCPNLI 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420 211 E---GSVITVGGTKIEidALYSPGHTIGSTSFIVDNSyLLSGDILFVDSIGRPDLAGKAedwVSDLRNTLYSRYKELSQS 287
Cdd:cd16275   94 PledGDTIKIGDTEIT--CLLTPGHTPGSMCYLLGDS-LFTGDTLFIEGCGRCDLPGGD---PEEMYESLQRLKKLPPPN 167


                 ....*..
gi 446375420 288 LIVLPAH 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 3.92e-21

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: 89.53  E-value: 3.92e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420   133 SYMVVSNGEAAVIDA-IRTVEAYEQFAKENGV-TITNVMDTHLHADHISGGRKLAEKVGGTYWLPPKDAE---------- 200
Cdd:smart00849   2 SYLVRDDGGAILIDTgPGEAEDLLAELKKLGPkKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAEllkdllallg 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420   201 ------EVVFSYEPLVEGSVITVGGTKIEIdaLYSPGHTIGSTSFIV-DNSYLLSGDILFVDSIGRPDLagkaeDWVSDL 273
Cdd:smart00849  82 elgaeaEPAPPDRTLKDGDELDLGGGELEV--IHTPGHTPGSIVLYLpEGKILFTGDLLFAGGDGRTLV-----DGGDAA 154

                          170       180
                   ....*....|....*....|...
gi 446375420   274 RNTLYSRYKELSQSL--IVLPAH 294
Cdd:smart00849 155 ASDALESLLKLLKLLpkLVVPGH 177
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 133-294 1.06e-19

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: 85.20  E-value: 1.06e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420 133 SYMVVSN--GEAAVIDAirtVEAYE--QFAKENGVTITNVMDTHLHADHISGGRKLAEKVGGtywLP---PKDaEEVVFS 205
Cdd:cd07723   11 IYLIVDEatGEAAVVDP---GEAEPvlAALEKNGLTLTAILTTHHHWDHTGGNAELKALFPD---APvygPAE-DRIPGL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420 206 YEPLVEGSVITVGGTKIEIdaLYSPGHTIGSTSFIVDNS-YLLSGDILFVDSIGRPDLaGKAEdwvsDLRNTLySRYKEL 284
Cdd:cd07723   84 DHPVKDGDEIKLGGLEVKV--LHTPGHTLGHICYYVPDEpALFTGDTLFSGGCGRFFE-GTAE----QMYASL-QKLLAL 155

                        170
                 ....*....|
gi 446375420 285 SQSLIVLPAH 294
Cdd:cd07723  156 PDDTLVYCGH 165
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 10-103 1.12e-19

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: 82.73  E-value: 1.12e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420  10 DVAEKVLFGELFILDVRNETDYEDWKIEGkqisSINKPYFDLLDgvDQIVSELPKDKDVLVVCAKEGSSIFVAEQLTEAG 89
Cdd:cd00158    1 ELKELLDDEDAVLLDVREPEEYAAGHIPG----AINIPLSELEE--RAALLELDKDKPIVVYCRSGNRSARAAKLLRKAG 74

                         90
                 ....*....|....
gi 446375420  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 3.39e-18

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: 82.01  E-value: 3.39e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420 140 GEAAVIDAIRTVEAYEQFAKENGVTITNVMDTHLHADHISGGRKLAEKVGGTYWLPPKDAE--------------EVVFS 205
Cdd:cd16322   22 GEAVLVDPGDESEKLLARFGTTGLTLLYILLTHAHFDHVGGVADLRRHPGAPVYLHPDDLPlyeaadlgakafglGIEPL 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420 206 YEP---LVEGSVITVGGTKIEIdaLYSPGHTIGSTSFIV-DNSYLLSGDILFVDSIGRPDLAGKAEdwvsdlrNTLYSRY 281
Cdd:cd16322  102 PPPdrlLEDGQTLTLGGLEFKV--LHTPGHSPGHVCFYVeEEGLLFSGDLLFQGSIGRTDLPGGDP-------KAMAASL 172

                        170
                 ....*....|....*.
gi 446375420 282 KELSQSL---IVLPAH 294
Cdd:cd16322  173 RRLLTLPdetRVFPGH 188
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 139-294 3.56e-18

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: 81.45  E-value: 3.56e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420 139 NGEAAVIDAIRTVEAYEQFAKENGVTITNVMDTHLHADHISGGRKLAEKVGGTYWLPPKDAEEVVFS------------Y 206
Cdd:cd07737   21 TKEAAVIDPGGDADKILQAIEDLGLTLKKILLTHGHLDHVGGAAELAEHYGVPIIGPHKEDKFLLENlpeqsqmfgfppA 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420 207 EPLV------EGSVITVGGTKIEIdaLYSPGHTIGSTSFIVD-NSYLLSGDILFVDSIGRPDLA-GKAEDWVSDLRNTLY 278
Cdd:cd07737  101 EAFTpdrwleEGDTVTVGNLTLEV--LHCPGHTPGHVVFFNReSKLAIVGDVLFKGSIGRTDFPgGNHAQLIASIKEKLL 178

                        170
                 ....*....|....*.
gi 446375420 279 SrykeLSQSLIVLPAH 294
Cdd:cd07737  179 P----LGDDVTFIPGH 190
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 18-104 5.43e-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: 67.12  E-value: 5.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420   18 GELFILDVRNETDYEDWKIEGkqisSINKPYFDLLDGVDQI------VSELPKDKDVLVVCAKEGSSIFVAEQLTEAGLE 91
Cdd:pfam00581   4 GKVVLIDVRPPEEYAKGHIPG----AVNVPLSSLSLPPLPLlellekLLELLKDKPIVVYCNSGNRAAAAAALLKALGYK 79

                          90
                  ....*....|...
gi 446375420   92 NIYYLAGGMKAWS 104
Cdd:pfam00581  80 NVYVLDGGFEAWK 92
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 131-279 9.81e-14

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 70.56  E-value: 9.81e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420 131 CL----SYMVV--SNGEAAVIDAIRtVEAYEQFAKENGVTITNVMDTHLHADHISGGRKLAEKV------GGTywlppkd 198
Cdd:PLN02469   8 CLednyAYLIIdeSTKDAAVVDPVD-PEKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIKKLVpgikvyGGS------- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420 199 AEEVVFSYEPLVEGSVITVGGTkIEIDALYSPGHTIGSTSFIVDN-----SYLLSGDILFVDSIGRpDLAGKAEDWVSDL 273
Cdd:PLN02469  80 LDNVKGCTHPVENGDKLSLGKD-VNILALHTPCHTKGHISYYVTGkegedPAVFTGDTLFIAGCGK-FFEGTAEQMYQSL 157


                 ....*.
gi 446375420 274 RNTLYS 279
Cdd:PLN02469 158 CVTLGS 163
GlpE_ST cd01444
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ...
 18-103 8.51e-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: 63.82  E-value: 8.51e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420  18 GELFILDVRNETDYEDWK--IEGKQISSinkpyfdlLDGVDQIVSELPKDKDVLVVCAKEGSSIFVAEQLTEAGLENIYY 95
Cdd:cd01444   15 EAPVLLDVRDPASYAALPdhIPGAIHLD--------EDSLDDWLGDLDRDRPVVVYCYHGNSSAQLAQALREAGFTDVRS 86


                 ....*...
gi 446375420  96 LAGGMKAW 103
Cdd:cd01444   87 LAGGFEAW 94
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 18-109 2.19e-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: 62.86  E-value: 2.19e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420    18 GELFILDVRNETDYEDWKIEGkqisSINKPYFDLLDGVDQIVS----------ELPKDKDVLVVCAKEGSSIFVAEQLTE 87
Cdd:smart00450   3 EKVVLLDVRSPEEYEGGHIPG----AVNIPLSELLDRRGELDIlefeellkrlGLDKDKPVVVYCRSGNRSAKAAWLLRE 78

                           90       100
                   ....*....|....*....|..
gi 446375420    88 AGLENIYYLAGGMKAWSEYVKP 109
Cdd:smart00450  79 LGFKNVYLLDGGYKEWSAAGPP 100
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 133-250 8.28e-12

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: 63.47  E-value: 8.28e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420 133 SYMVVSNGEAAVIDA-IRTVEAYEQFA---KENGVT---ITNVMDTHLHADHISGGRKLAEKVGGTYWLPPkdaeevvfs 205
Cdd:cd07725   17 VYLLRDGDETTLIDTgLATEEDAEALWeglKELGLKpsdIDRVLLTHHHPDHIGLAGKLQEKSGATVYILD--------- 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 446375420 206 YEPLVEGSVITVGGTKIEidALYSPGHTIGSTSFI-VDNSYLLSGD 250
Cdd:cd07725   88 VTPVKDGDKIDLGGLRLK--VIETPGHTPGHIVLYdEDRRELFVGD 131
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
130-294 1.12e-11

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 63.16  E-value: 1.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420  130 GCLSYMVVSNGEAAVIDA----IRTVEAYEQFAKENGVTITNVMDTHLHADHISGGRKLAEKVGGTYWLPPKDAEE---- 201
Cdd:pfam00753   5 QVNSYLIEGGGGAVLIDTggsaEAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEAREllde 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420  202 ---VVFSYEPLV-EGSVITVGGTKIEIDALYS---------PGHTIGSTSFIV---DNSYLLSGDILFVDSIGRPDL-AG 264
Cdd:pfam00753  85 elgLAASRLGLPgPPVVPLPPDVVLEEGDGILggglgllvtHGPGHGPGHVVVyygGGKVLFTGDLLFAGEIGRLDLpLG 164

                         170       180       190
                  ....*....|....*....|....*....|..
gi 446375420  265 KAEDWVSDLRNTLYSRYKELSQS--LIVLPAH 294
Cdd:pfam00753 165 GLLVLHPSSAESSLESLLKLAKLkaAVIVPGH 196
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 133-294 1.83e-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: 62.51  E-value: 1.83e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420 133 SYMVVSNGEAAVID----------AIrtVEAYEqfakenGVTITNVMDTHLHADHISGGRKLAEKVGG-TYWLPPKDAEE 201
Cdd:cd16278   20 TYLLGAPDGVVVIDpgpddpahldAL--LAALG------GGRVSAILVTHTHRDHSPGAARLAERTGApVRAFGPHRAGG 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420 202 VVFSYEP---LVEGSVITVGGTKIEidALYSPGHTIGSTSFIVDNS-YLLSGDILFVDS---IGRPDlaGKAEDWVSDLR 274
Cdd:cd16278   92 QDTDFAPdrpLADGEVIEGGGLRLT--VLHTPGHTSDHLCFALEDEgALFTGDHVMGWSttvIAPPD--GDLGDYLASLE 167

                        170       180
                 ....*....|....*....|
gi 446375420 275 ntlysRYKELSQSLIvLPAH 294
Cdd:cd16278  168 -----RLLALDDRLL-LPGH 181
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 142-338 8.18e-11

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 61.74  E-value: 8.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420 142 AAVIDAI-RTVEAYEQFAKENGVTITNVMDTHLHADHISGGRKLAEKVGGTYWLPPKDAEEvvfSYEPLVE-GSVITVGG 219
Cdd:PLN02962  38 ALLIDPVdKTVDRDLSLVKELGLKLIYAMNTHVHADHVTGTGLLKTKLPGVKSIISKASGS---KADLFVEpGDKIYFGD 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420 220 TKIEIDAlySPGHTIGSTSFIVDNS-------YLLSGDILFVDSIGRPDLAGKAEDwvsDLRNTLYSRYKELSQSLIVLP 292
Cdd:PLN02962 115 LYLEVRA--TPGHTAGCVTYVTGEGpdqpqprMAFTGDALLIRGCGRTDFQGGSSD---QLYKSVHSQIFTLPKDTLIYP 189

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 446375420 293 AHyskisemDESGIVSAKLKDLFEHNAGLNiEDEGEFRKVVTE-NLP 338
Cdd:PLN02962 190 AH-------DYKGFTVSTVGEEMLYNPRLT-KDEETFKTIMENlNLP 228
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 136-274 4.53e-09

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: 56.03  E-value: 4.53e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420 136 VVSNGEAAVIDA----IRTVEAYEQFAKENGVTITNVMDTHLHADHISG----------------GRKLAEKVGGTYWLP 195
Cdd:cd16282   20 IVGDDGVVVIDTgaspRLARALLAAIRKVTDKPVRYVVNTHYHGDHTLGnaafadagapiiahenTREELAARGEAYLEL 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420 196 PKDAEEVVFSYEPLV-------EGSVITVGGTKIEIDALySPGHTIGSTS-FIVDNSYLLSGDILFVDSIGrPDLAGKAE 267
Cdd:cd16282  100 MRRLGGDAMAGTELVlpdrtfdDGLTLDLGGRTVELIHL-GPAHTPGDLVvWLPEEGVLFAGDLVFNGRIP-FLPDGSLA 177


                 ....*..
gi 446375420 268 DWVSDLR 274
Cdd:cd16282  178 GWIAALD 184
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 171-294 5.29e-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: 5.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420 171 THLHADHISGGRKLA-----------EKVGGTYWLPPKDAEEVVFSYEPLVEGSVITVGGTkIE----IDALYSPGHTIG 235
Cdd:cd07729   95 SHLHFDHAGGLDLFPnatiivqraelEYATGPDPLAAGYYEDVLALDDDLPGGRVRLVDGD-YDlfpgVTLIPTPGHTPG 173

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446375420 236 STSFIVDN---SYLLSGD-ILFVDSIGRPDLAGkaedWVSDLRNTLYS--RYKELSQSL--IVLPAH 294
Cdd:cd07729  174 HQSVLVRLpegTVLLAGDaAYTYENLEEGRPPG----INYDPEAALASleRLKALAEREgaRVIPGH 236
RHOD_2 cd01528
Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes ...
 22-107 8.19e-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: 52.78  E-value: 8.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420  22 ILDVRnetdyEDWKIEGKQI-SSINKPyfdlLDGVDQIVSELP---KDKDVLVVCAKEGSSIFVAEQLTEAGLENIYYLA 97
Cdd:cd01528   20 LIDVR-----EPEELEIAFLpGFLHLP----MSEIPERSKELDsdnPDKDIVVLCHHGGRSMQVAQWLLRQGFENVYNLQ 90

                         90
                 ....*....|
gi 446375420  98 GGMKAWSEYV 107
Cdd:cd01528   91 GGIDAWSLEV 100
RHOD_Pyr_redox cd01524
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ...
 19-104 2.35e-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: 2.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420  19 ELFILDVRNETDYEDWKIEGkqisSINKPyfdlLDGVDQIVSELPKDKDVLVVCAKEGSSIFVAEQLTEAGLeNIYYLAG 98
Cdd:cd01524   13 GVTLIDVRTPQEFEKGHIKG----AINIP----LDELRDRLNELPKDKEIIVYCAVGLRGYIAARILTQNGF-KVKNLDG 83


                 ....*.
gi 446375420  99 GMKAWS 104
Cdd:cd01524   84 GYKTYS 89
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 103-294 4.41e-08

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: 53.61  E-value: 4.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420 103 WSEYVKPIKVGDlknggSMYQFNRLGKGclSYMVVSNGEAAVIDAI--RTVEAYEQFAKENGVTITNV---MDTHLHADH 177
Cdd:cd16310    1 WTAPTEPFRIVD-----NIYYVGTKGIG--SYLITSNHGAILLDGGleENAALIEQNIKALGFKLSDIkiiINTHAHYDH 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420 178 ISGGRKLAEKVGGTYWLPPKDAEEVV------------FSYEP------LVEGSVITVGgtKIEIDALYSPGHTIGSTSF 239
Cdd:cd16310   74 AGGLAQLKADTGAKLWASRGDRPALEagkhigdnitqpAPFPAvkvdriLGDGEKIKLG--DITLTATLTPGHTKGCTTW 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446375420 240 ---IVDN----------SYLLSGDILfVDSIGRPDLagkaedwVSDLRNTlYSRYKELSQSlIVLPAH 294
Cdd:cd16310  152 sttVKENgrplrvvfpcSLSVAGNVL-VGNKTYPTI-------VEDYRAS-FARLRAMKAD-IVLTSH 209
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 161-242 2.04e-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: 51.43  E-value: 2.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420 161 NGVTITNVMDTHLHADHISGGRKLAEKVGGTYWLPPKDAEEVVFSYEP---------------LVEGSVITVGGTKIEId 225
Cdd:cd16280   58 DPADIKYILITHGHGDHYGGAAYLKDLYGAKVVMSEADWDMMEEPPEEgdnprwgppperdivIKDGDTLTLGDTTITV- 136

                         90
                 ....*....|....*..
gi 446375420 226 aLYSPGHTIGSTSFIVD 242
Cdd:cd16280  137 -YLTPGHTPGTLSLIFP 152
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 140-257 6.20e-07

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: 49.07  E-value: 6.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420 140 GEAAVIDAIRTVeayeqFAKENGVTITNVMDTHLHADHIsGG----RKLAEKVGGTYW---LPPKDAEEVVFS--YEPLV 210
Cdd:cd07722   37 GRPSYIPLLKSV-----LDSEGNATISDILLTHWHHDHV-GGlpdvLDLLRGPSPRVYkfpRPEEDEDPDEDGgdIHDLQ 110

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 446375420 211 EGSVITVGGTKIEidALYSPGHTIGSTSFivdnsYLLSGDILFV-DSI 257
Cdd:cd07722  111 DGQVFKVEGATLR--VIHTPGHTTDHVCF-----LLEEENALFTgDCV 151
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
2-112 6.93e-07

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 50.78  E-value: 6.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420   2 EVKSLQAKDVAEKVLFGELFIlDVRNETDYEDWKIEGKQisSINKPYFDLldgvdQIVSELP-KDKDVLVVCAKEGSSIF 80
Cdd:PRK08762   1 SIREISPAEARARAAQGAVLI-DVREAHERASGQAEGAL--RIPRGFLEL-----RIETHLPdRDREIVLICASGTRSAH 72

                         90       100       110
                 ....*....|....*....|....*....|..
gi 446375420  81 VAEQLTEAGLENIYYLAGGMKAWSEYVKPIKV 112
Cdd:PRK08762  73 AAATLRELGYTRVASVAGGFSAWKDAGLPLER 104
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 134-259 1.88e-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: 47.99  E-value: 1.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420 134 YMVVSNGEAAVIDA--IRTVEAYEQFAKENGVT---ITNVMDTHLHADHISGGRKLAEK--------------------- 187
Cdd:cd07721   14 YLIEDDDGLTLIDTglPGSAKRILKALRELGLSpkdIRRILLTHGHIDHIGSLAALKEApgapvyahereapylegekpy 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420 188 --------VGGTYWLPPKDAEEVVfsyEPLVEGSVITVGGtkiEIDALYSPGHTIGSTSFIV-DNSYLLSGDiLFVDSIG 258
Cdd:cd07721   94 pppvrlglLGLLSPLLPVKPVPVD---RTLEDGDTLDLAG---GLRVIHTPGHTPGHISLYLeEDGVLIAGD-ALVTVGG 166


                 .
gi 446375420 259 R 259
Cdd:cd07721  167 E 167
YmaE-like_MBL-fold cd07727
uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold ...
 130-256 4.61e-06

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: 46.42  E-value: 4.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420 130 GCLSYMVVSNGEAAVIDAIRTVEAYEQFAKENG----VTITnvmdthlHADHISGGRKLAEKVGGTYWLPPKDAEEVVFS 205
Cdd:cd07727   14 GAASYLILRPEGNILVDSPRYSPPLAKRIEALGgiryIFLT-------HRDDVADHAKWAERFGAKRIIHEDDVNAVTRP 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446375420 206 YEPLVEGSVITVGGTKiEIDALYSPGHTIGSTSFIVDNS-YLLSGDILFVDS 256
Cdd:cd07727   87 DEVIVLWGGDPWELDP-DLTLIPVPGHTRGSVVLLYKEKgVLFTGDHLAWSR 137
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 168-257 4.87e-06

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: 46.47  E-value: 4.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420 168 VMDTHLHADHIsGGRKLAEKVggtyWLPPKDAE------------EVVFSYE--------PLVEGSVITVGGTKIEIdaL 227
Cdd:cd07712   46 VVATHGHFDHI-GGLHEFEEV----YVHPADAEilaapdnfetltWDAATYSvppagptlPLRDGDVIDLGDRQLEV--I 118

                         90       100       110
                 ....*....|....*....|....*....|.
gi 446375420 228 YSPGHTIGSTSFI-VDNSYLLSGDILFVDSI 257
Cdd:cd07712  119 HTPGHTPGSIALLdRANRLLFSGDVVYDGPL 149
Polysulfide_ST cd01447
Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as ...
 6-105 2.49e-05

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: 42.80  E-value: 2.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420   6 LQAKDVAEKVLFGELFILDVRNETDYE-DWKIEG-KQI------------SSINKPYFDlldgvdqivselpKDKDVLVV 71
Cdd:cd01447    1 LSPEDARALLGSPGVLLVDVRDPRELErTGMIPGaFHAprgmlefwadpdSPYHKPAFA-------------EDKPFVFY 67

                         90       100       110
                 ....*....|....*....|....*....|....
gi 446375420  72 CAKEGSSIFVAEQLTEAGLENIYYLAGGMKAWSE 105
Cdd:cd01447   68 CASGWRSALAGKTLQDMGLKPVYNIEGGFKDWKE 101
RHOD_ThiF cd01526
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ...
 22-109 3.12e-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: 43.07  E-value: 3.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420  22 ILDVRNETDYEDWKIEGkqisSINKPYFDLLDGVDQIVSELP------KDKDVLVVCAKEGSSIFVAEQLTEAGLE-NIY 94
Cdd:cd01526   27 LLDVRPKVHFEICRLPE----AINIPLSELLSKAAELKSLQElpldndKDSPIYVVCRRGNDSQTAVRKLKELGLErFVR 102

                         90
                 ....*....|....*
gi 446375420  95 YLAGGMKAWSEYVKP 109
Cdd:cd01526  103 DIIGGLKAWADKVDP 117
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 136-259 4.66e-05

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 44.83  E-value: 4.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420 136 VVSNGEAA-VIDAIrtveayeqfaKENGVTITNVMDTHLHADHISGGRKLAEKVGGTYWLPPKDAEEVVFSYEPLVEGSV 214
Cdd:PLN02398 102 VVDPSEAVpVIDAL----------SRKNRNLTYILNTHHHYDHTGGNLELKARYGAKVIGSAVDKDRIPGIDIVLKDGDK 171

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 446375420 215 ITVGGTKIEIdaLYSPGHTIGSTSFIVDNS-YLLSGDILFVDSIGR 259
Cdd:PLN02398 172 WMFAGHEVLV--METPGHTRGHISFYFPGSgAIFTGDTLFSLSCGK 215
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
22-109 4.68e-05

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 45.11  E-value: 4.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420  22 ILDVRNETDYEDWKIEGKQIssINKPYFDLLDGVDQiVSELPKDKDVLVVCAKEGSSIFVAEQLTEAGLENIYyLAGGMK 101
Cdd:PRK07411 302 LIDVRNPNEYEIARIPGSVL--VPLPDIENGPGVEK-VKELLNGHRLIAHCKMGGRSAKALGILKEAGIEGTN-VKGGIT 377


                 ....*...
gi 446375420 102 AWSEYVKP 109
Cdd:PRK07411 378 AWSREVDP 385
RHOD_1 cd01522
Member of the Rhodanese Homology Domain superfamily, subgroup 1. This CD includes the putative ...
 21-94 6.75e-05

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: 41.93  E-value: 6.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420  21 FILDVRNEtdyEDWKIEGKQISSINKPYFDLLDG------VDQIVSELPKDKDVLVVCAKEGSSIFVAEQLTEAGLENIY 94
Cdd:cd01522   17 VLVDVRTE---AEWKFVGGVPDAVHVAWQVYPDMeinpnfLAELEEKVGKDRPVLLLCRSGNRSIAAAEAAAQAGFTNVY 93
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 139-251 7.10e-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: 43.69  E-value: 7.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420 139 NGEAAVIDA---------IRTVEAYeqfAKENGVT-ITNVMDTHLHADHISGGRKLAEKVG-GTYWLPPKDAEEVVF--- 204
Cdd:COG2333   20 DGKTILIDTgprpsfdagERVVLPY---LRALGIRrLDLLVLTHPDADHIGGLAAVLEAFPvGRVLVSGPPDTSETYerl 96

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446375420 205 ---------SYEPLVEGSVITVGGTKIEIdaLYSPGHTIGSTSF----IV------DNSYLLSGDI 251
Cdd:COG2333   97 lealkekgiPVRPCRAGDTWQLGGVRFEV--LWPPEDLLEGSDEnnnsLVlrltygGFSFLLTGDA 160
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 136-253 8.69e-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: 42.90  E-value: 8.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420 136 VVSNGEAAVIDA----IRTVEAYEQFaKENGVTITNVMDTHLHADHISGGRKLAEKVGGTYWLPPKDAE-------EVVF 204
Cdd:cd07743   14 VFGDKEALLIDSgldeDAGRKIRKIL-EELGWKLKAIINTHSHADHIGGNAYLQKKTGCKVYAPKIEKAfienpllEPSY 92

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446375420 205 SY--------------------EPLVEGSVITVGGTKIEIDALysPGHTIGSTSFIVDNSYLLSGDILF 253
Cdd:cd07743   93 LGgayppkelrnkflmakpskvDDIIEEGELELGGVGLEIIPL--PGHSFGQIGILTPDGVLFAGDALF 159
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 128-251 9.90e-05

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: 42.51  E-value: 9.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420 128 GKGcLSYMVVSNGEAAVIDAIRTVEAYEQ----FAKENGVT-ITNVMDTHLHADHISGGRKLAEKV-GGTYWLPPKDAEE 201
Cdd:cd07731    8 GQG-DAILIQTPGKTILIDTGPRDSFGEDvvvpYLKARGIKkLDYLILTHPDADHIGGLDAVLKNFpVKEVYMPGVTHTT 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446375420 202 VVF------------SYEPLVEGSVITVGGTKIEIdalYSPGHTIGST----SfIV------DNSYLLSGDI 251
Cdd:cd07731   87 KTYedlldaikekgiPVTPCKAGDRWQLGGVSFEV---LSPPKDDYDDlnnnS-CVlrltygGTSFLLTGDA 154
GOB1-like_MBL-B3 cd16308
Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; ...
 171-242 1.37e-04

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: 42.84  E-value: 1.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420 171 THLHADHISGGRKLAEKVGGTYWLPPKDAEEVV-------------FSYEP------LVEGSVITVGGTKIEIdaLYSPG 231
Cdd:cd16308   67 TQAHYDHVGAMAAIKQQTGAKMMVDEKDAKVLAdggksdyemggygSTFAPvkadklLHDGDTIKLGGTKLTL--LHHPG 144

                         90
                 ....*....|.
gi 446375420 232 HTIGSTSFIVD 242
Cdd:cd16308  145 HTKGSCSFLFD 155
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 1.45e-04

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: 43.08  E-value: 1.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420 171 THLHADHISGGRKLAEKVGGTYWLPPKDAEEV-------------VFSYEP------LVEGSVITVGGTKIEidALYSPG 231
Cdd:cd16288   67 SHAHLDHAGGLAALKKLTGAKLMASAEDAALLasggksdfhygddSLAFPPvkvdrvLKDGDRVTLGGTTLT--AHLTPG 144

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446375420 232 HTIGSTSFIVDNSYllSG---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 4.28e-04

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: 39.20  E-value: 4.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420  19 ELFILDVRNETDYEDWKIEGKqissINKPYFDLLDGVD--QIVSELPKDKDVLVVCAKEGSSIFVAEQLTEAGLENIYYL 96
Cdd:cd01529   12 GTALLDVRAEDEYAAGHLPGK----RSIPGAALVLRSQelQALEAPGRATRYVLTCDGSLLARFAAQELLALGGKPVALL 87


                 ....*..
gi 446375420  97 AGGMKAW 103
Cdd:cd01529   88 DGGTSAW 94
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 19-109 5.24e-04

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 41.62  E-value: 5.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420  19 ELFILDVRNETDYEDWKIEGKQIssINKPYFDLLDGVdqivSELPKDKDVLVVCAKEGSSIFVAEQLTEAGLENIYYLAG 98
Cdd:PRK07878 303 KIALIDVREPVEWDIVHIPGAQL--IPKSEILSGEAL----AKLPQDRTIVLYCKTGVRSAEALAALKKAGFSDAVHLQG 376

                         90
                 ....*....|.
gi 446375420  99 GMKAWSEYVKP 109
Cdd:PRK07878 377 GVVAWAKQVDP 387
DdPDE5-like_MBL-fold cd07738
Dictyostelium discoideum phosphodiesterase 5 and related proteins; MBL-fold metallo hydrolase ...
 157-250 9.02e-04

Dictyostelium discoideum phosphodiesterase 5 and related proteins; MBL-fold metallo hydrolase domain; Includes Dictyostelium discoideum cAMP/cGMP-dependent 3',5'-cAMP/cGMP phosphodiesterase A (also known as cyclic GMP-binding protein A, phosphodiesterase 5, phosphodiesterase D, and PDE5) and cAMP/cGMP-dependent 3',5'-cAMP/cGMP phosphodiesterase B (also known as cyclic GMP-binding protein B, phosphodiesterase 6, phosphodiesterase E, and PDE6. 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: 293824  Cd Length: 189  Bit Score: 39.97  E-value: 9.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420 157 FAKENGV---TITNVMDTHLHADHISG-------GRKLA------------EKVGGTYWLPPKDAEEvVFSYEPLVEGSV 214
Cdd:cd07738   38 YLRQNGIsprLVDHVILTHCHADHDAGtfqkileEEKITlyttrtinesflRKYAALTGLPPDFLEE-LFDFRPVIIGEK 116

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 446375420 215 ITVGGTKIEIDalYSPgHTIGSTSFIV---DNSYLLSGD 250
Cdd:cd07738  117 TKINGAEFEFD--YSF-HSIPTIRFKVsygGKSIAYSGD 152
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
133-257 1.12e-03

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 40.18  E-value: 1.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420 133 SYMVVSNGEAAVIDA-----IRTVEAYEQFAKengvtITNVMDTHLHADHISGgrklaekVGG---TYWLP--------- 195
Cdd:COG1234   21 SYLLEAGGERLLIDCgegtqRQLLRAGLDPRD-----IDAIFITHLHGDHIAG-------LPGllsTRSLAgrekpltiy 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420 196 -PKDAEEVV--------------FSYEPLVEGSVITVGGTKIEIDALYspgHTIGSTSFIVD---NSYLLSGDILFVDSI 257
Cdd:COG1234   89 gPPGTKEFLeallkasgtdldfpLEFHEIEPGEVFEIGGFTVTAFPLD---HPVPAYGYRFEepgRSLVYSGDTRPCEAL 165
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 22-106 1.18e-03

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 40.63  E-value: 1.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420  22 ILDVRNETDYEDWKIEGkqisSINKPYFDLLDGVDQIVSELPKDkdVLVVCAKEGSSIFVAEQLTEAGLENIYYLAGGMK 101
Cdd:PRK05597 277 LIDVREPSEFAAYSIPG----AHNVPLSAIREGANPPSVSAGDE--VVVYCAAGVRSAQAVAILERAGYTGMSSLDGGIE 350


                 ....*
gi 446375420 102 AWSEY 106
Cdd:PRK05597 351 GWLDS 355
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 133-256 2.54e-03

Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism];


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 39.11  E-value: 2.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420 133 SYMVVSNGEAAVIDA---IRtveayeQFAKENGVTITNVmD----THLHADHISGGRKLAEKVGG---TYWLPPKDAEEV 202
Cdd:COG1235   37 SILVEADGTRLLIDAgpdLR------EQLLRLGLDPSKI-DaillTHEHADHIAGLDDLRPRYGPnpiPVYATPGTLEAL 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420 203 -------------VFSYEPLVEGSVITVGGTKIE-IDALYSPGHTIG--------STSFIVDNSY-------LLSG-DIL 252
Cdd:COG1235  110 errfpylfapypgKLEFHEIEPGEPFEIGGLTVTpFPVPHDAGDPVGyriedggkKLAYATDTGYipeevleLLRGaDLL 189


                 ....
gi 446375420 253 FVDS 256
Cdd:COG1235  190 ILDA 193
RHOD_YceA cd01518
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, ...
 4-108 9.28e-03

Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, Bacillus subtilis YbfQ, and similar uncharacterized proteins.


Pssm-ID: 238776 [Multi-domain]  Cd Length: 101  Bit Score: 35.25  E-value: 9.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375420   4 KSLQAKDVAEKVLFGELFILDVRNetDYEdWKIeGKQISSIN---KPYFDLLDGVDQIVsELPKDKDVLVVCAK----EG 76
Cdd:cd01518    2 TYLSPAEWNELLEDPEVVLLDVRN--DYE-YDI-GHFKGAVNpdvDTFREFPFWLDENL-DLLKGKKVLMYCTGgircEK 76

                         90       100       110
                 ....*....|....*....|....*....|..
gi 446375420  77 SSIFVAEQlteaGLENIYYLAGGMkawSEYVK 108
Cdd:cd01518   77 ASAYLKER----GFKNVYQLKGGI---LKYLE 101
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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