NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2205866422|ref|WP_240950847|]
View 

MBL fold metallo-hydrolase [Methanobacterium subterraneum]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 10869930)

MBL fold metallo-hydrolase 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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 13-202 2.35e-62

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: 192.82  E-value: 2.35e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  13 VYALDSTQGNYTYLI-TGEENILVDTGRHGQGKGILKDLKAIGIKPDDVQHILITHHDVDHVGSLASLEKSTGAKVWASE 91
Cdd:cd07721     2 VYQLPLLPPVNAYLIeDDDGLTLIDTGLPGSAKRILKALRELGLSPKDIRRILLTHGHIDHIGSLAALKEAPGAPVYAHE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  92 KDIPYICGIKGRPGIKW-----LISVLMPLKKPEKITPYPEDQRI---GDIEIIPTPGHTPGHVALLYK--DVLMVGDLI 161
Cdd:cd07721    82 REAPYLEGEKPYPPPVRlgllgLLSPLLPVKPVPVDRTLEDGDTLdlaGGLRVIHTPGHTPGHISLYLEedGVLIAGDAL 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2205866422 162 KTSRGKIAPMSSFMNWDDEIIKESIHKINNYNFRWICPAHG 202
Cdd:cd07721   162 VTVGGELVPPPPPFTWDMEEALESLRKLAELDPEVLAPGHG 202
 
Name Accession Description Interval E-value
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 13-202 2.35e-62

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: 192.82  E-value: 2.35e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  13 VYALDSTQGNYTYLI-TGEENILVDTGRHGQGKGILKDLKAIGIKPDDVQHILITHHDVDHVGSLASLEKSTGAKVWASE 91
Cdd:cd07721     2 VYQLPLLPPVNAYLIeDDDGLTLIDTGLPGSAKRILKALRELGLSPKDIRRILLTHGHIDHIGSLAALKEAPGAPVYAHE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  92 KDIPYICGIKGRPGIKW-----LISVLMPLKKPEKITPYPEDQRI---GDIEIIPTPGHTPGHVALLYK--DVLMVGDLI 161
Cdd:cd07721    82 REAPYLEGEKPYPPPVRlgllgLLSPLLPVKPVPVDRTLEDGDTLdlaGGLRVIHTPGHTPGHISLYLEedGVLIAGDAL 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2205866422 162 KTSRGKIAPMSSFMNWDDEIIKESIHKINNYNFRWICPAHG 202
Cdd:cd07721   162 VTVGGELVPPPPPFTWDMEEALESLRKLAELDPEVLAPGHG 202
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 21-211 2.00e-33

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: 119.02  E-value: 2.00e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  21 GNYTYLI-TGEENILVDTGRHGQGKG-ILKDLKAIGikpDDVQHILITHHDVDHVGSLASLEKSTGAKVWASEKDIPYIC 98
Cdd:COG0491    14 GVNSYLIvGGDGAVLIDTGLGPADAEaLLAALAALG---LDIKAVLLTHLHPDHVGGLAALAEAFGAPVYAHAAEAEALE 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  99 GIKGRPGIKwlisvlMPLKKPEKITPYPEDQRIGD--IEIIPTPGHTPGHVALLYKD--VLMVGDLIKT-SRGKI-APMS 172
Cdd:COG0491    91 APAAGALFG------REPVPPDRTLEDGDTLELGGpgLEVIHTPGHTPGHVSFYVPDekVLFTGDALFSgGVGRPdLPDG 164

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2205866422 173 SFMNWddeiiKESIHKINNYNFRWICPAHGEPLMTQEVR 211
Cdd:COG0491   165 DLAQW-----LASLERLLALPPDLVIPGHGPPTTAEAID 198
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 23-201 1.16e-28

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: 105.71  E-value: 1.16e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422   23 YTYLI-TGEENILVDTGrHGQGKGILKDLKAIGikPDDVQHILITHHDVDHVGSLASLEKSTGAKVWASEKDIPYICGIK 101
Cdd:smart00849   1 NSYLVrDDGGAILIDTG-PGEAEDLLAELKKLG--PKKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELLKDLL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  102 GRPGIKWLIsvlmpLKKPEKITPYPEDQRI----GDIEIIPTPGHTPGHVALLYKD--VLMVGDLIKtSRGKIAPMSSFM 175
Cdd:smart00849  78 ALLGELGAE-----AEPAPPDRTLKDGDELdlggGELEVIHTPGHTPGSIVLYLPEgkILFTGDLLF-AGGDGRTLVDGG 151

                          170       180
                   ....*....|....*....|....*.
gi 2205866422  176 NWDDEIIKESIHKINNYNFRWICPAH 201
Cdd:smart00849 152 DAAASDALESLLKLLKLLPKLVVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
20-201 1.14e-21

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 88.19  E-value: 1.14e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  20 QGNYTYLITGEENILVDTGRHGQgKGILKDLKAIGIKPDDVQHILITHHDVDHVGSLASLEKSTGAKVWASEKDIPYICG 99
Cdd:pfam00753   5 QVNSYLIEGGGGAVLIDTGGSAE-AALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARELLD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422 100 ---IKGRPGIKWLISVLMPLKKPEKITPYPE-DQRIGDIEIIPTPGHTPGHVALLYKD--VLMVGDLIKTsrGKIAPMSS 173
Cdd:pfam00753  84 eelGLAASRLGLPGPPVVPLPPDVVLEEGDGiLGGGLGLLVTHGPGHGPGHVVVYYGGgkVLFTGDLLFA--GEIGRLDL 161

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2205866422 174 FM-------NWDDEIIKESIHKINNYNFRWICPAH 201
Cdd:pfam00753 162 PLggllvlhPSSAESSLESLLKLAKLKAAVIVPGH 196
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 22-159 6.27e-13

hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione hydrolase, a detoxification enzyme known as glyoxalase II. It follows lactoylglutathione lyase, or glyoxalase I, and acts to remove the toxic metabolite methylglyoxal and related compounds. This protein belongs to the broader metallo-beta-lactamase family (pfam00753). [Cellular processes, Detoxification]


Pssm-ID: 274569 [Multi-domain]  Cd Length: 248  Bit Score: 65.64  E-value: 6.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  22 NYTYLITGEEN--ILVDTGrhgQGKGILKDLKAIGIKPDdvqHILITHHDVDHVGSLASLEKSTGAKVWASEKDipyicG 99
Cdd:TIGR03413  10 NYIWLLHDPDGqaAVVDPG---EAEPVLDALEARGLTLT---AILLTHHHHDHVGGVAELLEAFPAPVYGPAEE-----R 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2205866422 100 IKGrpgikwlISVlmPLKKPEKITpypedqrIGD--IEIIPTPGHTPGHVALLYKD--VLMVGD 159
Cdd:TIGR03413  79 IPG-------ITH--PVKDGDTVT-------LGGleFEVLAVPGHTLGHIAYYLPDspALFCGD 126
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 20-161 1.88e-07

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 50.23  E-value: 1.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  20 QGNYTYLITGEenilvDTGRHG-----QGKGILKDLKAigiKPDDVQHILITHHDVDHVGSLASLEKSTGAKVWASEKDI 94
Cdd:PLN02398   85 KDNYAYLLHDE-----DTGTVGvvdpsEAVPVIDALSR---KNRNLTYILNTHHHYDHTGGNLELKARYGAKVIGSAVDK 156

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2205866422  95 PYICGIKG--RPGIKWLISvlmplkkpekitpypedqriG-DIEIIPTPGHTPGHVALLY--KDVLMVGDLI 161
Cdd:PLN02398  157 DRIPGIDIvlKDGDKWMFA--------------------GhEVLVMETPGHTRGHISFYFpgSGAIFTGDTL 208
 
Name Accession Description Interval E-value
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 13-202 2.35e-62

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: 192.82  E-value: 2.35e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  13 VYALDSTQGNYTYLI-TGEENILVDTGRHGQGKGILKDLKAIGIKPDDVQHILITHHDVDHVGSLASLEKSTGAKVWASE 91
Cdd:cd07721     2 VYQLPLLPPVNAYLIeDDDGLTLIDTGLPGSAKRILKALRELGLSPKDIRRILLTHGHIDHIGSLAALKEAPGAPVYAHE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  92 KDIPYICGIKGRPGIKW-----LISVLMPLKKPEKITPYPEDQRI---GDIEIIPTPGHTPGHVALLYK--DVLMVGDLI 161
Cdd:cd07721    82 REAPYLEGEKPYPPPVRlgllgLLSPLLPVKPVPVDRTLEDGDTLdlaGGLRVIHTPGHTPGHISLYLEedGVLIAGDAL 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2205866422 162 KTSRGKIAPMSSFMNWDDEIIKESIHKINNYNFRWICPAHG 202
Cdd:cd07721   162 VTVGGELVPPPPPFTWDMEEALESLRKLAELDPEVLAPGHG 202
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 21-211 2.00e-33

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: 119.02  E-value: 2.00e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  21 GNYTYLI-TGEENILVDTGRHGQGKG-ILKDLKAIGikpDDVQHILITHHDVDHVGSLASLEKSTGAKVWASEKDIPYIC 98
Cdd:COG0491    14 GVNSYLIvGGDGAVLIDTGLGPADAEaLLAALAALG---LDIKAVLLTHLHPDHVGGLAALAEAFGAPVYAHAAEAEALE 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  99 GIKGRPGIKwlisvlMPLKKPEKITPYPEDQRIGD--IEIIPTPGHTPGHVALLYKD--VLMVGDLIKT-SRGKI-APMS 172
Cdd:COG0491    91 APAAGALFG------REPVPPDRTLEDGDTLELGGpgLEVIHTPGHTPGHVSFYVPDekVLFTGDALFSgGVGRPdLPDG 164

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2205866422 173 SFMNWddeiiKESIHKINNYNFRWICPAHGEPLMTQEVR 211
Cdd:COG0491   165 DLAQW-----LASLERLLALPPDLVIPGHGPPTTAEAID 198
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 23-201 1.16e-28

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: 105.71  E-value: 1.16e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422   23 YTYLI-TGEENILVDTGrHGQGKGILKDLKAIGikPDDVQHILITHHDVDHVGSLASLEKSTGAKVWASEKDIPYICGIK 101
Cdd:smart00849   1 NSYLVrDDGGAILIDTG-PGEAEDLLAELKKLG--PKKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELLKDLL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  102 GRPGIKWLIsvlmpLKKPEKITPYPEDQRI----GDIEIIPTPGHTPGHVALLYKD--VLMVGDLIKtSRGKIAPMSSFM 175
Cdd:smart00849  78 ALLGELGAE-----AEPAPPDRTLKDGDELdlggGELEVIHTPGHTPGSIVLYLPEgkILFTGDLLF-AGGDGRTLVDGG 151

                          170       180
                   ....*....|....*....|....*.
gi 2205866422  176 NWDDEIIKESIHKINNYNFRWICPAH 201
Cdd:smart00849 152 DAAASDALESLLKLLKLLPKLVVPGH 177
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 2-205 9.71e-27

uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized human MBLAC1 and related proteins. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293797 [Multi-domain]  Cd Length: 190  Bit Score: 101.12  E-value: 9.71e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422   2 QEGFFLRVTDEVYALDSTqgnYTYLITGEENILVDTGRHGQGKGILKDLKAIGIKPDDVQHILITHHDVDHVGSLASLEK 81
Cdd:cd07711     6 VEGYARRDSDGGFRASST---VTLIKDGGKNILVDTGTPWDRDLLLKALAEHGLSPEDIDYVVLTHGHPDHIGNLNLFPN 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  82 stgAKVWASEKdipyicgIKGRPGIKWLISVLmplkKPEKITPypedqrigDIEIIPTPGHTPGHVALLYKD-----VLM 156
Cdd:cd07711    83 ---ATVIVGWD-------ICGDSYDDHSLEEG----DGYEIDE--------NVEVIPTPGHTPEDVSVLVETekkgtVAV 140

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2205866422 157 VGDLIKTSRGKIAPM-SSFMNWDDEIIKESIHKINNyNFRWICPAHGEPL 205
Cdd:cd07711   141 AGDLFEREEDLEDPIlWDPLSEDPELQEESRKRILA-LADWIIPGHGPPF 189
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 24-201 1.36e-26

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: 100.44  E-value: 1.36e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  24 TYLITGE--ENILVDTGrHGQGKGILKDLKAIGIKPDdvqHILITHHDVDHVGSLASLEKSTGAKVWASEKDIPYIcgik 101
Cdd:cd06262    12 CYLVSDEegEAILIDPG-AGALEKILEAIEELGLKIK---AILLTHGHFDHIGGLAELKEAPGAPVYIHEADAELL---- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422 102 GRPGIKWLISVLMPLKKPEKITPYPEDQRIG----DIEIIPTPGHTPGHVALLYKD--VLMVGDLI-KTSRGKiapmSSF 174
Cdd:cd06262    84 EDPELNLAFFGGGPLPPPEPDILLEDGDTIElgglELEVIHTPGHTPGSVCFYIEEegVLFTGDTLfAGSIGR----TDL 159

                         170       180
                  ....*....|....*....|....*....
gi 2205866422 175 MNWDDEIIKESIHKI--NNYNFRWICPAH 201
Cdd:cd06262   160 PGGDPEQLIESIKKLllLLPDDTVVYPGH 188
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 25-201 7.51e-24

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: 93.75  E-value: 7.51e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  25 YLITGEENILVDTG-RHGQGKGILKDLKAIGIKPddvQHILITHHDVDHVGSLASLEKSTGAKVWASEKDIPYI------ 97
Cdd:cd07743    13 YVFGDKEALLIDSGlDEDAGRKIRKILEELGWKL---KAIINTHSHADHIGGNAYLQKKTGCKVYAPKIEKAFIenplle 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  98 -CGIKGRPGIKWLIS-VLMPlkKPEKITPYPEDQRI----GDIEIIPTPGHTPGHVALLYKD-VLMVGDLIktsrgkiap 170
Cdd:cd07743    90 pSYLGGAYPPKELRNkFLMA--KPSKVDDIIEEGELelggVGLEIIPLPGHSFGQIGILTPDgVLFAGDAL--------- 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2205866422 171 mssFmnwDDEIIK--------------ESIHKINNYNFRWICPAH 201
Cdd:cd07743   159 ---F---GEEVLEkygipflydveeqlETLEKLEELDADYYVPGH 197
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 8-145 5.94e-23

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: 92.51  E-value: 5.94e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422   8 RVTDEVYALdSTQGNYTYLIT-GEENILVDTGRHGQGKGILKDLKAIGIKPDDVQHILITHHDVDHVGSLASLEKSTGAK 86
Cdd:cd16310     9 RIVDNIYYV-GTKGIGSYLITsNHGAILLDGGLEENAALIEQNIKALGFKLSDIKIIINTHAHYDHAGGLAQLKADTGAK 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2205866422  87 VWASEKDIPYICgiKGRP-GIKWLISVLMPLKKPEKITPYPEDQRIGDIEIIP--TPGHTPG 145
Cdd:cd16310    88 LWASRGDRPALE--AGKHiGDNITQPAPFPAVKVDRILGDGEKIKLGDITLTAtlTPGHTKG 147
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 23-189 1.21e-22

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: 91.51  E-value: 1.21e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  23 YTYLI-TGEENILVDTG------------------RHGQGKGILKDLKAIGIKPDDVQHILITHHDVDHVGSLASLeksT 83
Cdd:cd07729    33 YAYLIeHPEGTILVDTGfhpdaaddpgglelafppGVTEEQTLEEQLARLGLDPEDIDYVILSHLHFDHAGGLDLF---P 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  84 GAKVWASEKDIPYICG-IKGRPGIKWLISVLMPLKKPEKITPYPEDQRI-GDIEIIPTPGHTPGHVALLYK----DVLMV 157
Cdd:cd07729   110 NATIIVQRAELEYATGpDPLAAGYYEDVLALDDDLPGGRVRLVDGDYDLfPGVTLIPTPGHTPGHQSVLVRlpegTVLLA 189

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2205866422 158 GDLIKTSRGKIAPMSSFMNWDDEIIKESIHKI 189
Cdd:cd07729   190 GDAAYTYENLEEGRPPGINYDPEAALASLERL 221
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 24-161 2.02e-22

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: 91.07  E-value: 2.02e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  24 TYLI-TGEENILVDTG---RHGQGKG-ILKDLKAIGIKPDDVQHILITHHDVDHVGSLASLEKST---GAKVWASEKDIP 95
Cdd:cd07720    51 AFLVrTGGRLILVDTGaggLFGPTAGkLLANLAAAGIDPEDIDDVLLTHLHPDHIGGLVDAGGKPvfpNAEVHVSEAEWD 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  96 YicgikgrpgikWL----ISVLMPLKKP------EKITPYPEDQRIGD-------IEIIPTPGHTPGHVALL----YKDV 154
Cdd:cd07720   131 F-----------WLddanAAKAPEGAKRffdaarDRLRPYAAAGRFEDgdevlpgITAVPAPGHTPGHTGYRiesgGERL 199


                  ....*..
gi 2205866422 155 LMVGDLI 161
Cdd:cd07720   200 LIWGDIV 206
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
20-201 1.14e-21

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 88.19  E-value: 1.14e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  20 QGNYTYLITGEENILVDTGRHGQgKGILKDLKAIGIKPDDVQHILITHHDVDHVGSLASLEKSTGAKVWASEKDIPYICG 99
Cdd:pfam00753   5 QVNSYLIEGGGGAVLIDTGGSAE-AALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARELLD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422 100 ---IKGRPGIKWLISVLMPLKKPEKITPYPE-DQRIGDIEIIPTPGHTPGHVALLYKD--VLMVGDLIKTsrGKIAPMSS 173
Cdd:pfam00753  84 eelGLAASRLGLPGPPVVPLPPDVVLEEGDGiLGGGLGLLVTHGPGHGPGHVVVYYGGgkVLFTGDLLFA--GEIGRLDL 161

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2205866422 174 FM-------NWDDEIIKESIHKINNYNFRWICPAH 201
Cdd:pfam00753 162 PLggllvlhPSSAESSLESLLKLAKLKAAVIVPGH 196
YmaE-like_MBL-fold cd07727
uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold ...
 25-204 1.05e-20

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: 84.94  E-value: 1.05e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  25 YLITGEE-NILVDTGRHGqgKGILKDLKAIGikpdDVQHILITHhdVDHVGSLASLEKSTGAKVWASEKDIpyiCGIKGR 103
Cdd:cd07727    18 YLILRPEgNILVDSPRYS--PPLAKRIEALG----GIRYIFLTH--RDDVADHAKWAERFGAKRIIHEDDV---NAVTRP 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422 104 PGIKWLISvlmplkkpekiTPYPEDQriGDIEIIPTPGHTPGHVALLYKD--VLMVGDLIKTSRGKIApMSSFM--NWDD 179
Cdd:cd07727    87 DEVIVLWG-----------GDPWELD--PDLTLIPVPGHTRGSVVLLYKEkgVLFTGDHLAWSRRRGW-LSAFRyvCWYS 152

                         170       180
                  ....*....|....*....|....*.
gi 2205866422 180 -EIIKESIHKINNYNFRWICPAHGEP 204
Cdd:cd07727   153 wPEQAESVERLADLDFEWVLPGHGRR 178
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 8-145 3.39e-20

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


Pssm-ID: 293867 [Multi-domain]  Cd Length: 252  Bit Score: 85.23  E-value: 3.39e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422   8 RVTDEVYALdSTQGNYTYLITGEE-NILVDTGRHGQGKGILKDLKAIGIKPDDVQHILITHHDVDHVGSLASLEKSTGAK 86
Cdd:cd16309     9 KLIGNIYYV-GTAGLGVFLITTPEgHILIDGAMPQSTPLIKDNIKKLGFDVKDVKYLLNTHAHFDHAGGLAELKKATGAQ 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2205866422  87 VWASEKDIPYICGikGRPGIKWLISVLMPLKKPEKITPYPEDQRIGDIEIIP--TPGHTPG 145
Cdd:cd16309    88 LVASAADKPLLES--GYVGSGDTKNLQFPPVRVDRVIGDGDKVTLGGTTLTAhlTPGHSPG 146
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 24-201 6.69e-19

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: 81.00  E-value: 6.69e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  24 TYLITGE-ENILVDTGRHGQGKGILKDLKAIGIKPDDVQHILITHHDVDHVGSLASL-EKSTGAKVWASEKdipyicgik 101
Cdd:cd07726    18 SYLLDGEgRPALIDTGPSSSVPRLLAALEALGIAPEDVDYIILTHIHLDHAGGAGLLaEALPNAKVYVHPR--------- 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422 102 grpGIKWLISvlmplkkPEK-------------------ITPYPEDQ----------RIGD--IEIIPTPGHTPGHVALL 150
Cdd:cd07726    89 ---GARHLID-------PSKlwasaravygdeadrlggeILPVPEERvivledgetlDLGGrtLEVIDTPGHAPHHLSFL 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422 151 YK--DVLMVGD-------LIKTSRGKIAPMSSFmnwDDEIIKESIHKINNYNFRWICPAH 201
Cdd:cd07726   159 DEesDGLFTGDaagvrypELDVVGPPSTPPPDF---DPEAWLESLDRLLSLKPERIYLTH 215
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 25-206 7.52e-19

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: 80.04  E-value: 7.52e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  25 YLIT-GEENILVDTG--RHGQGKGILKDLKAIGIKPDDVQHILITHHDVDHVGSLASLEKSTGAKVwasekdipyicgik 101
Cdd:cd07725    18 YLLRdGDETTLIDTGlaTEEDAEALWEGLKELGLKPSDIDRVLLTHHHPDHIGLAGKLQEKSGATV-------------- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422 102 grpgikwLISVLMPLKKPEKItpypedqRIGDI--EIIPTPGHTPGHVALLYKD--VLMVGDLIktsRGKIAPMSSFmnW 177
Cdd:cd07725    84 -------YILDVTPVKDGDKI-------DLGGLrlKVIETPGHTPGHIVLYDEDrrELFVGDAV---LPKITPNVSL--W 144

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2205866422 178 DDEIIK------ESIHKINNYNFRWICPAHGEPLM 206
Cdd:cd07725   145 AVRVEDplgaylESLDKLEKLDVDLAYPGHGGPIK 179
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 24-161 4.06e-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: 76.23  E-value: 4.06e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  24 TYLIT---GEENILVDTGrhgqgKGILKDLKAIGIKPDDVQHILITHHDVDHVGSLASLEKSTGAKVWASEKDIPYICGI 100
Cdd:cd16322    13 TYLVAdegGGEAVLVDPG-----DESEKLLARFGTTGLTLLYILLTHAHFDHVGGVADLRRHPGAPVYLHPDDLPLYEAA 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2205866422 101 KGRpGIKWLISVlmpLKKPEKITPYPEDQRIG----DIEIIPTPGHTPGHVALLY--KDVLMVGDLI 161
Cdd:cd16322    88 DLG-AKAFGLGI---EPLPPPDRLLEDGQTLTlgglEFKVLHTPGHSPGHVCFYVeeEGLLFSGDLL 150
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 7-153 4.96e-17

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. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. B3 MBLs include Fluoribacter gormanii FEZ-1, Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) GOB-1, Stenotrophomonas Maltophilia L1, and Bradyrhizobium diazoefficiens BJP-1, Serratia marcescens SMB-1, and Pseudomonas Aeruginosa AIM-1. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293794 [Multi-domain]  Cd Length: 248  Bit Score: 76.82  E-value: 4.96e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422   7 LRVTDEVYALdSTQGNYTYLI-TGEENILVDTGRHgQGKGILKD-LKAIGIKPDDVQHILITHHDVDHVGSLASLEKSTG 84
Cdd:cd07708     8 FQIAGNTYYV-GTDDLAAYLIvTPQGNILIDGDME-QNAPMIKAnIKKLGFKFSDTKLILISHAHFDHAGGSAEIKKQTG 85

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2205866422  85 AKVWASEKDIPYI-CGIKGRPGIKWLISVLMPLKKPEKITPYPEDQRIGDIEIIP--TPGHTPGHVALLYKD 153
Cdd:cd07708    86 AKVMAGAEDVSLLlSGGSSDFHYANDSSTYFPQSTVDRAVHDGERVTLGGTVLTAhaTPGHTPGCTTWTMTL 157
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 8-145 9.91e-17

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: 75.82  E-value: 9.91e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422   8 RVTDEVYALdSTQGNYTYLI-TGEENILVDTGRHGQGKGILKDLKAIGIKPDDVQHILITHHDVDHVGSLASLEKSTGAK 86
Cdd:cd16288     9 RIAGNVYYV-GTSGLASYLItTPQGLILIDTGLESSAPMIKANIRKLGFKPSDIKILLNSHAHLDHAGGLAALKKLTGAK 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2205866422  87 VWASEKDIPYIC-GIKG--RPGIKWLIsvlMPLKKPEKITPYPEDQRIGDIEIIP--TPGHTPG 145
Cdd:cd16288    88 LMASAEDAALLAsGGKSdfHYGDDSLA---FPPVKVDRVLKDGDRVTLGGTTLTAhlTPGHTRG 148
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 24-205 1.99e-16

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: 73.68  E-value: 1.99e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  24 TYLI-TGEENILVDTG----RHgqgkgilkdLKAI--GIKPDDVQHILITHHDVDHVGSLASLEKSTGAKVWAsekdipy 96
Cdd:cd16278    20 TYLLgAPDGVVVIDPGpddpAH---------LDALlaALGGGRVSAILVTHTHRDHSPGAARLAERTGAPVRA------- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  97 iCGIKGRPGIKWLISVLMPLkkpekitpyPEDQRI----GDIEIIPTPGHTPGHVALLYKD--VLMVGDLIkTSRGK--I 168
Cdd:cd16278    84 -FGPHRAGGQDTDFAPDRPL---------ADGEVIegggLRLTVLHTPGHTSDHLCFALEDegALFTGDHV-MGWSTtvI 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2205866422 169 AP----MSSFMnwddeiikESIHKINNYNFRWICPAHGEPL 205
Cdd:cd16278   153 APpdgdLGDYL--------ASLERLLALDDRLLLPGHGPPI 185
AIM-1-like_MBL-B3 cd16314
Pseudomonas Aeruginosa AIM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 26-145 2.14e-16

Pseudomonas Aeruginosa AIM-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 AIM-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: 293872 [Multi-domain]  Cd Length: 255  Bit Score: 75.31  E-value: 2.14e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  26 LITGEE-NILVDTGRHGQGKGILKDLKAIGIKPDDVQHILITHHDVDHVGSLASLEKSTGAKVWASEKDIPYI-CGIKGR 103
Cdd:cd16314    26 LVTSDAgHILIDGGTDKAAPLIEANIRALGFRPEDVRYIVSSHEHFDHAGGIARLQRATGAPVVAREPAATTLeRGRSDR 105

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2205866422 104 PGIKWLISvlmplkkpEKITPYPEDQRIGDIEII----------PTPGHTPG 145
Cdd:cd16314   106 SDPQFLVV--------EKFPPVASVQRIGDGEVLrvgplaltahATPGHTPG 149
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 8-151 1.94e-15

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: 72.23  E-value: 1.94e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422   8 RVTDEVYALdSTQGNYTYLI-TGEENILVDTGRHGQGKGILKD-LKAIGIKPDDVQHILITHHDVDHVGSLASLEKSTGA 85
Cdd:cd16280     9 QVFDNLYYV-GNKWVSAWAIdTGDGLILIDALNNNEAADLIVDgLEKLGLDPADIKYILITHGHGDHYGGAAYLKDLYGA 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2205866422  86 KVWASEKDipyicgikgrpgIKWLISVLMPLKKPEKITPYPEDQRIGD----------IEIIPTPGHTPGHVALLY 151
Cdd:cd16280    88 KVVMSEAD------------WDMMEEPPEEGDNPRWGPPPERDIVIKDgdtltlgdttITVYLTPGHTPGTLSLIF 151
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 24-161 4.76e-15

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: 293835 [Multi-domain]  Cd Length: 222  Bit Score: 71.01  E-value: 4.76e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  24 TYLI-TGEENILVDTGrHGQGK-------------GILKDLKAIGIKPDDVQHILITHHDVDHVGSLASLEKST------ 83
Cdd:cd16277    15 SWLVrTPGRTILVDTG-IGNDKprpgppafhnlntPYLERLAAAGVRPEDVDYVLCTHLHVDHVGWNTRLVDGRwvptfp 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  84 GAKVWASEKDIPYICGIKGRPGIKWLI---SVLmPLKKPEKITPYPEDQRIGD-IEIIPTPGHTPGHVALLYKD----VL 155
Cdd:cd16277    94 NARYLFSRAEYDHWSSPDAGGPPNRGVfedSVL-PVIEAGLADLVDDDHEILDgIRLEPTPGHTPGHVSVELESggerAL 172


                  ....*.
gi 2205866422 156 MVGDLI 161
Cdd:cd16277   173 FTGDVM 178
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 22-159 1.30e-14

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: 68.64  E-value: 1.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  22 NYTYLITGEEN---ILVDTGRHGQgkgILKDLKAIGIKPDdvqHILITHHDVDHVGSLASLEKSTG-AKVWASEKD-IPY 96
Cdd:cd07723     9 NYIYLIVDEATgeaAVVDPGEAEP---VLAALEKNGLTLT---AILTTHHHWDHTGGNAELKALFPdAPVYGPAEDrIPG 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2205866422  97 icgikgrpgikwlisVLMPLKKPEKITpypedqrIGDIEI--IPTPGHTPGHVALLYKD--VLMVGD 159
Cdd:cd07723    83 ---------------LDHPVKDGDEIK-------LGGLEVkvLHTPGHTLGHICYYVPDepALFTGD 127
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 20-203 6.10e-14

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: 67.17  E-value: 6.10e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  20 QGNYTYLI-TGEENILVDTGrhgQGKGILKD-----LKAIGIKPddVQHILITHHDVDHVGSLASlekstgakvwasekd 93
Cdd:cd07722    16 QGTNTYLVgTGKRRILIDTG---EGRPSYIPllksvLDSEGNAT--ISDILLTHWHHDHVGGLPD--------------- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  94 ipyICGIKGRPGIKwlISVLMPLKKPEKITPYPEDQR-IGD----------IEIIPTPGHTPGHVALLYK--DVLMVGDL 160
Cdd:cd07722    76 ---VLDLLRGPSPR--VYKFPRPEEDEDPDEDGGDIHdLQDgqvfkvegatLRVIHTPGHTTDHVCFLLEeeNALFTGDC 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2205866422 161 I---KTSrgKIAPMSSFMNwddeiikeSIHKINNYNFRWICPAHGE 203
Cdd:cd07722   151 VlghGTA--VFEDLAAYMA--------SLKKLLSLGPGRIYPGHGP 186
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 22-161 1.05e-13

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: 66.41  E-value: 1.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  22 NYTYLItgeenilVDtgrHGQGKGILKD--------LKAIGIKPDDVQHILITHHDVDHVGSLASLEKSTGAKVWASEKD 93
Cdd:cd16275    12 NYSYII-------ID---KATREAAVVDpawdiekiLAKLNELGLTLTGILLTHSHFDHVNLVEPLLAKYDAPVYMSKEE 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  94 IPYIcGIKGRPgikwlisvLMPLKKPEKItpypedqRIGDIEI--IPTPGHTPGHVALLYKDVLMVGDLI 161
Cdd:cd16275    82 IDYY-GFRCPN--------LIPLEDGDTI-------KIGDTEItcLLTPGHTPGSMCYLLGDSLFTGDTL 135
EVM-1-like_MBL-B3 cd16315
Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 26-145 1.24e-13

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


Pssm-ID: 293873 [Multi-domain]  Cd Length: 248  Bit Score: 67.37  E-value: 1.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  26 LITGEE-NILVDTGRHGQGKGILKDLKAIGIKPDDVQHILITHHDVDHVGSLASLEKSTGAKVWASEKDIPYICGIKGRP 104
Cdd:cd16315    26 LITGDDgHVLIDSGTEEAAPLVLANIRKLGFDPKDVRWLLSSHEHFDHVGGLAALQRATGARVAASAAAAPVLESGKPAP 105

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2205866422 105 GikwlisvlmplkKP-----EKITPYPEDQRIGDIEI----------IPTPGHTPG 145
Cdd:cd16315   106 D------------DPqaglhEPFPPVRVDRIVEDGDTvalgslrltaHATPGHTPG 149
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 50-201 5.19e-13

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: 65.75  E-value: 5.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  50 LKAIGIKPDDVQHILITHHDVDHVGSLASLeksTGAKVWASEKDIPYICGIKGRPGIK-------WLISVLMPLKKPEKI 122
Cdd:cd07730    74 LAAGGIDPEDIDAVILSHLHWDHIGGLSDF---PNARLIVGPGAKEALRPPGYPSGFLpellpsdFEGRLVRWEEDDFLW 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422 123 TPYPEDQR----IGD--IEIIPTPGHTPGHVALLY-----KDVLMVGDLIKTSRGKIAPMSSFMNWDDEII------KES 185
Cdd:cd07730   151 VPLGPFPRaldlFGDgsLYLVDLPGHAPGHLGLLArttsgTWVFLAGDACHHRIGLLRPSPLLPLPDLDDGadreaaRET 230

                         170       180
                  ....*....|....*....|
gi 2205866422 186 IHKI----NNYNFRwICPAH 201
Cdd:cd07730   231 LARLreldAAPDVR-VVLAH 249
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 25-161 6.03e-13

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: 64.57  E-value: 6.03e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  25 YLITG-EENILVDTGrHGQGKgILKDLKAIGIKPDDVqhiLITHHDVDHVGSLASLEKstgakVWASEKDIPYICGIKGR 103
Cdd:cd07712    12 YLLRGrDRALLIDTG-LGIGD-LKEYVRTLTDLPLLV---VATHGHFDHIGGLHEFEE-----VYVHPADAEILAAPDNF 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2205866422 104 PGIKWLiSVLMPLKKPEKITPYPEDQRI--GD--IEIIPTPGHTPGHVALLYKD--VLMVGDLI 161
Cdd:cd07712    82 ETLTWD-AATYSVPPAGPTLPLRDGDVIdlGDrqLEVIHTPGHTPGSIALLDRAnrLLFSGDVV 144
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 22-159 6.27e-13

hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione hydrolase, a detoxification enzyme known as glyoxalase II. It follows lactoylglutathione lyase, or glyoxalase I, and acts to remove the toxic metabolite methylglyoxal and related compounds. This protein belongs to the broader metallo-beta-lactamase family (pfam00753). [Cellular processes, Detoxification]


Pssm-ID: 274569 [Multi-domain]  Cd Length: 248  Bit Score: 65.64  E-value: 6.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  22 NYTYLITGEEN--ILVDTGrhgQGKGILKDLKAIGIKPDdvqHILITHHDVDHVGSLASLEKSTGAKVWASEKDipyicG 99
Cdd:TIGR03413  10 NYIWLLHDPDGqaAVVDPG---EAEPVLDALEARGLTLT---AILLTHHHHDHVGGVAELLEAFPAPVYGPAEE-----R 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2205866422 100 IKGrpgikwlISVlmPLKKPEKITpypedqrIGD--IEIIPTPGHTPGHVALLYKD--VLMVGD 159
Cdd:TIGR03413  79 IPG-------ITH--PVKDGDTVT-------LGGleFEVLAVPGHTLGHIAYYLPDspALFCGD 126
AIM-1_SMB-1-like_MBL-B3 cd16290
AIM-1, SMB-1, EVM-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 19-145 8.46e-13

AIM-1, SMB-1, EVM-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; This subgroup of B3 subclass MBLs includes Pseudomonas Aeruginosa AIM-1, Serratia marcescens SMB-1, Erythrobacter vulgaris EVM-1, and Janthinobacterium lividum THIN-B. 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 AIM-1-,SMB-1-, EVM-1-, THIN-B-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: 293848 [Multi-domain]  Cd Length: 256  Bit Score: 65.06  E-value: 8.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  19 TQGNYTYLITGEEN-ILVDTGRHGQGKGILKDLKAIGIKPDDVQHILITHHDVDHVGSLASLEKSTGAKVWASEkdipyi 97
Cdd:cd16290    19 TGGLSAVLITSPQGlILIDGALPQSAPQIEANIRALGFRLEDVKLILNSHAHFDHAGGIAALQRDSGATVAASP------ 92

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2205866422  98 cgikgrPGIKWLISVLMPLKKP-----EKITPYPEDQRIGDIEIIP----------TPGHTPG 145
Cdd:cd16290    93 ------AGAAALRSGGVDPDDPqagaaDPFPPVAKVRVVADGEVVKlgplavtahaTPGHTPG 149
GOB1-like_MBL-B3 cd16308
Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; ...
 25-176 1.13e-12

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: 64.80  E-value: 1.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  25 YLI-TGEENILVDTGRHGQGKGILKDLKAIGIKPDDVQHILITHHDVDHVGSLASLEKSTGAKVWASEKDIP-------- 95
Cdd:cd16308    25 YLIvTPKGNILINTGLAESVPLIKKNIQALGFKFKDIKILLTTQAHYDHVGAMAAIKQQTGAKMMVDEKDAKvladggks 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  96 -YICGIKGrpgikwliSVLMPLkKPEKITPYPEDQRIGDIEI--IPTPGHTPGHVALLYKdvlmVGDLIKTSRGKIAPMS 172
Cdd:cd16308   105 dYEMGGYG--------STFAPV-KADKLLHDGDTIKLGGTKLtlLHHPGHTKGSCSFLFD----VKDEKRTYRVLIANMP 171


                  ....
gi 2205866422 173 SFMN 176
Cdd:cd16308   172 TILP 175
L1_POM-1-like_MBL-B3 cd16289
Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-1 and related ...
 7-153 1.21e-11

Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-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 L1- and Pom-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: 293847  Cd Length: 239  Bit Score: 61.76  E-value: 1.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422   7 LRVTDEVYALDSTQGNYTYLITGEENILVDTGRHGQGKGILKDLKAIGIKPDDVQHILITHHDVDHVGSLASLEKSTGAK 86
Cdd:cd16289     8 LQIADHTWYIGTESLTALLVKTPDGAVLLDGGMPQAADMLLDNMRALGVAPGDLKLILHSHAHADHAGPLAALKRATGAR 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2205866422  87 VwASEKDIPYICGIKGRPGIKWLISVLMPLKKPEKITPYPEDQRIGDIEIIP--TPGHTPGHVALLYKD 153
Cdd:cd16289    88 V-AANAESAVLLARGGSDDIHFGDGITFPPVQADRIVMDGEVVTLGGVTFTAhfTPGHTPGSTSWTWTD 155
SMB-1-like_MBL-B3 cd16313
SMB-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase ...
 19-145 1.43e-11

SMB-1, THIN-B 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 SMB-1- and THIN-B-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: 293871 [Multi-domain]  Cd Length: 254  Bit Score: 61.80  E-value: 1.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  19 TQGNYTYLITGEE-NILVDTGRHGQGKGILKDLKAIGIKPDDVQHILITHHDVDHVGSLASLEKSTGAKVWASEKDIPYI 97
Cdd:cd16313    19 TGGISAVLITSPQgHILIDGGFPKSPEQIAASIRQLGFKLEDVKYILSSHDHWDHAGGIAALQKLTGAQVLASPATVAVL 98

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2205866422  98 cgikgRPGIkwlisvlMPLKKPE-----KITPYPEDQRIGDIEIIP----------TPGHTPG 145
Cdd:cd16313    99 -----RSGS-------MGKDDPQfggltPMPPVASVRAVRDGEVVKlgplavtahaTPGHTTG 149
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 20-92 1.55e-11

uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold metallo hydrolase domain; Includes the uncharacterized Bacillus subtilis YycJ 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: 293819 [Multi-domain]  Cd Length: 151  Bit Score: 59.97  E-value: 1.55e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2205866422  20 QGNYTYLITGEENILVDTGRhgQGKGILKDLKAIGIKPDDVQHILITHHDVDHVGSLASLEKSTGAKVWASEK 92
Cdd:cd07733     8 KGNCTYLETEDGKLLIDAGL--SGRKITGRLAEIGRDPEDIDAILVTHEHADHIKGLGVLARKYNVPIYATAG 78
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 21-211 2.13e-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: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 60.66  E-value: 2.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  21 GNYTYLITGEENILVDTG-RHGQGKGILKDLKAIGIKPddVQHILITHHDVDHVGSLASLeKSTGAKVWASEKDIPYicg 99
Cdd:cd16282    15 SNIGFIVGDDGVVVIDTGaSPRLARALLAAIRKVTDKP--VRYVVNTHYHGDHTLGNAAF-ADAGAPIIAHENTREE--- 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422 100 IKGRPGIKWLISVLMPLKKPEKITPYPEDQ--------RIGD--IEIIPT-PGHTPGHVALLYKD--VLMVGDLIKTSRG 166
Cdd:cd16282    89 LAARGEAYLELMRRLGGDAMAGTELVLPDRtfddgltlDLGGrtVELIHLgPAHTPGDLVVWLPEegVLFAGDLVFNGRI 168

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2205866422 167 KIAPMSSFMNWddeiiKESIHKINNYNFRWICPAHGEPLMTQEVR 211
Cdd:cd16282   169 PFLPDGSLAGW-----IAALDRLLALDATVVVPGHGPVGDKADLR 208
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 21-161 2.50e-11

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: 59.72  E-value: 2.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  21 GNYTYLITGEEN---ILVDTGRHgQGKGILKDLKAIGIKpddVQHILITHHDVDHVGSLASLEKSTGAKVWASEKDIPYI 97
Cdd:cd07724    11 GTLSYLVGDPETgeaAVIDPVRD-SVDRYLDLAAELGLK---ITYVLETHVHADHVSGARELAERTGAPIVIGEGAPASF 86

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2205866422  98 CGIkgrpgikwlisvlmPLKKPEKItpypedqRIGDIEI--IPTPGHTPGHVALLYKDVLMV--GDLI 161
Cdd:cd07724    87 FDR--------------LLKDGDVL-------ELGNLTLevLHTPGHTPESVSYLVGDPDAVftGDTL 133
NorV COG0426
Flavorubredoxin [Energy production and conversion];
25-202 1.63e-10

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 59.46  E-value: 1.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  25 YLITGEENILVDTGRHGQGKGILKDLKAIgIKPDDVQHILITHHDVDHVGSLAS-LEKSTGAKVWASEKDIPYICGIKGR 103
Cdd:COG0426    37 YLIVDEKTALIDTVGESFFEEFLENLSKV-IDPKKIDYIIVNHQEPDHSGSLPElLELAPNAKIVCSKKAARFLPHFYGI 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422 104 PGIKwlisvLMPLKKPEKItpypedqRIGD--IEIIPTPG-HTPGH-VALLYKD-VLMVGDLiktsrgkiapMSSFM--- 175
Cdd:COG0426   116 PDFR-----FIVVKEGDTL-------DLGGhtLQFIPAPMlHWPDTmFTYDPEDkILFSGDA----------FGSHGasd 173

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2205866422 176 -----NWDDEIIKES------------------IHKINNYNFRWICPAHG 202
Cdd:COG0426   174 elfddEVDEHLEEEArryyanimmpfskqvlkaLKKVRGLDIDMIAPSHG 223
THIN-B-like_MBL-B3 cd16312
Janthinobacterium lividum THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 19-145 1.14e-09

Janthinobacterium lividum THIN-B 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 THIN-B-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: 293870 [Multi-domain]  Cd Length: 258  Bit Score: 56.53  E-value: 1.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  19 TQGNYTYLITGEE-NILVDTGRHGQGKGILKDLKAIGIKPDDVQHILITHHDVDHVGSLASLEKSTGAKVWASEKDIPYI 97
Cdd:cd16312    19 TAGLSAVLVTSPQgHVLLDGALPQSAPLIIANIEALGFRIEDVKLILNSHAHWDHAGGIAALQKASGATVAASAHGAQVL 98

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2205866422  98 -CGIKGRPGIKWLISVLMPLKKPEKITPYPEDQ--RIGDIEIIP--TPGHTPG 145
Cdd:cd16312    99 qSGTNGKDDPQYQAKPVVHVAKVAKVKEVGEGDtlKVGPLRLTAhmTPGHTPG 151
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 33-161 1.70e-09

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: 55.25  E-value: 1.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  33 ILVDTGrhGQGKGILKDLKAIGIKpddVQHILITHHDVDHVGSLASLEKSTGAKVWASEKD-------IPYICGIKGRPG 105
Cdd:cd07737    25 AVIDPG--GDADKILQAIEDLGLT---LKKILLTHGHLDHVGGAAELAEHYGVPIIGPHKEdkfllenLPEQSQMFGFPP 99

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2205866422 106 IkwliSVLMP---LKKPEKITpypedqrIGDI--EIIPTPGHTPGHVALLYKD--VLMVGDLI 161
Cdd:cd07737   100 A----EAFTPdrwLEEGDTVT-------VGNLtlEVLHCPGHTPGHVVFFNREskLAIVGDVL 151
metallo-hydrolase-like_MBL-fold cd07742
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 50-159 2.00e-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) 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: 293828 [Multi-domain]  Cd Length: 249  Bit Score: 55.71  E-value: 2.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  50 LKAIGIKPDDVQHILITHHDVDHVGSLASLEKSTgAKVWASEKDIpyicGIKGRPGIKWLISVLMPLKKPEKITPYPE-- 127
Cdd:cd07742    71 IEALGFDPSDVRHIVLTHLDLDHAGGLADFPHAT-VHVHAAELDA----ATSPRTRYERRRYRPQQLAHGPWWVTYAAgg 145

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2205866422 128 ------------DQRIGDIEIIPTPGHTPGHVALLYKD----VLMVGD 159
Cdd:cd07742   146 erwfgfeavrplDGLPPEILLVPLPGHTRGHCGVAVRTgdrwLLHAGD 193
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 24-144 2.40e-09

Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as tRNase Z or 3' tRNase) catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors. Two forms of RNase Z exist in eukaryotes, one long (ELAC2) and one short form (ELAC1), the former may have resulted from a duplication of the shorter enzyme. Only the short form exists in bacteria. It includes the C-terminus of human ELAC2 and Escherichia coli zinc phosphodiesterase (ZiPD, also known as ecoZ, tRNase Z, or RNase BN) is a 3' tRNA-processing endonuclease, encoded by the elaC gene. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293830 [Multi-domain]  Cd Length: 180  Bit Score: 54.58  E-value: 2.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  24 TYLITGEENILVDTGRHGQGKgilkdLKAIGIKPDDVQHILITHHDVDHVGSLASLEKSTGakvWASEKDIPYICgikGR 103
Cdd:cd16272    20 YLLETGGTRILLDCGEGTVYR-----LLKAGVDPDKLDAIFLSHFHLDHIGGLPTLLFARR---YGGRKKPLTIY---GP 88

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2205866422 104 PGIKWLISVLMPLKKPEKITPYP----------EDQRIGDIEIIPTPG-HTP 144
Cdd:cd16272    89 KGIKEFLEKLLNFPVEILPLGFPleieeleeggEVLELGDLKVEAFPVkHSV 140
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 12-93 4.43e-09

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: 53.68  E-value: 4.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  12 EVYALDSTQGNYTYLITGEENILVDTGRHGQGKG--ILKDLKAIGIKpdDVQHILITHHDVDHVGSLASLEKS-TGAKVW 88
Cdd:cd07731     1 RVHFLDVGQGDAILIQTPGKTILIDTGPRDSFGEdvVVPYLKARGIK--KLDYLILTHPDADHIGGLDAVLKNfPVKEVY 78


                  ....*
gi 2205866422  89 ASEKD 93
Cdd:cd07731    79 MPGVT 83
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 24-140 1.46e-08

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 53.36  E-value: 1.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  24 TYLITGEENILVDTGRhgqgkGILKDLKAIGIKPDDVQHILITHHDVDHVGSLASLEKSTGAK---VWASEKDIPYIcgi 100
Cdd:COG1235    38 ILVEADGTRLLIDAGP-----DLREQLLRLGLDPSKIDAILLTHEHADHIAGLDDLRPRYGPNpipVYATPGTLEAL--- 109

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2205866422 101 kgRPGIKWLISVLMPLKKPEKITPYpEDQRIGDIEIIPTP 140
Cdd:COG1235   110 --ERRFPYLFAPYPGKLEFHEIEPG-EPFEIGGLTVTPFP 146
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 25-133 3.78e-08

Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, and related proteins; MBL-fold metallo hydrolase domain; This subgroup includes Methanocaldococcus jannaschii 7,8-dihydropterin-6-methyl-4-(beta-D-ribofuranosyl)-aminobenzene-5'-phosphate synthase (EC 2.5.1.15), a folate biosynthetic enzyme also known as dihydropteroate synthase and 7,8 dihydropteroate synthase. Thermoanaerobacter tengcongensis Tflp is a ferredoxin-like member. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293799  Cd Length: 269  Bit Score: 52.24  E-value: 3.78e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  25 YLI-TGEENILVDTGrhgQGKGILKDLKAIGIKPDDVQHILITHHDVDHVGSLAS-LEKSTGAKVWASeKDIP---YICG 99
Cdd:cd07713    23 LLIeTEGKKILFDTG---QSGVLLHNAKKLGIDLSDIDAVVLSHGHYDHTGGLKAlLELNPKAPVYAH-PDAFeprYSKR 98

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2205866422 100 IKGRPGIKWLISVLmpLKKPEKITPYPEDQRIGD 133
Cdd:cd07713    99 GGGKKGIGIGREEL--EKAGARLVLVEEPTEIAP 130
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 26-79 3.83e-08

Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold metallo-hydrolase domain; Arylsulfatase (also known as aryl-sulfate sulfohydrolase, EC 3.1.6.1). Pseudoalteromonas carrageenovora arylsulfatase AtsA may function as a glycosulfohydrolase involved with desulfation of sulfated polysaccharides, which catalyzes hydrolysis of the arylsulfate ester bond, producing the aryl compounds and inorganic sulfate. CD also includes some sequences annotated as ribonucleases. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily.


Pssm-ID: 293805 [Multi-domain]  Cd Length: 193  Bit Score: 51.36  E-value: 3.83e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2205866422  26 LITGEENILVDTGRhgqgkGILKDLKAIGIKPDDVQHILITHHDVDHVGSLASL 79
Cdd:cd07719    23 VVVGGRVYLVDAGS-----GVVRRLAQAGLPLGDLDAVFLTHLHSDHVADLPAL 71
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 25-202 6.06e-08

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


Pssm-ID: 293795 [Multi-domain]  Cd Length: 238  Bit Score: 51.33  E-value: 6.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  25 YLITGEENILVDTGRHGQGKGILKDLKAIgIKPDDVQHILITHHDVDHVGSLAS-LEKSTGAKVWASEKDIPYICGIKGR 103
Cdd:cd07709    35 YLIKDEKTALIDTVKEPFFDEFLENLEEV-IDPRKIDYIVVNHQEPDHSGSLPElLELAPNAKIVCSKKAARFLKHFYPG 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422 104 PGIKWLisvlmPLKKPEKITpypedqrIGD--IEIIPTPG-HTPG--------------------HVAL--LYKDvlMVG 158
Cdd:cd07709   114 IDERFV-----VVKDGDTLD-------LGKhtLKFIPAPMlHWPDtmvtydpedkilfsgdafgaHGASgeLFDD--EVE 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2205866422 159 DLIKTSRGK----IAPMSSFmnwddeiIKESIHKINNYNFRWICPAHG 202
Cdd:cd07709   180 DYLEEARRYyaniMGPFSKQ-------VRKALEKLEALDIKMIAPSHG 220
THIN-B2-like_MBL-B3 cd16311
Janthinobacterium lividum THIN-B2 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 19-145 1.47e-07

Janthinobacterium lividum THIN-B2 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 THIN-B2-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: 293869  Cd Length: 257  Bit Score: 50.37  E-value: 1.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  19 TQGNYTYLITGEE-NILVDTGRHGQGKGILKDLKAIGIKPDDVQHILITHHDVDHVGSLASLEKSTGAKVWASEKdipyi 97
Cdd:cd16311    19 VKGLSSVLVTSPQgHVLVDGGLPESAPKIIANIEALGFRIEDVKLILNSHGHIDHAGGLAELQRRSGALVAASPS----- 93

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2205866422  98 cgikgrpGIKWLISVLMPLKKPE-----KITPYPeDQRI----GDIEIIP-------TPGHTPG 145
Cdd:cd16311    94 -------AALDLASGEVGPDDPQyhalpKYPPVK-DMRLardgGQFNVGPvsltahaTPGHTPG 149
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 20-161 1.88e-07

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 50.23  E-value: 1.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  20 QGNYTYLITGEenilvDTGRHG-----QGKGILKDLKAigiKPDDVQHILITHHDVDHVGSLASLEKSTGAKVWASEKDI 94
Cdd:PLN02398   85 KDNYAYLLHDE-----DTGTVGvvdpsEAVPVIDALSR---KNRNLTYILNTHHHYDHTGGNLELKARYGAKVIGSAVDK 156

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2205866422  95 PYICGIKG--RPGIKWLISvlmplkkpekitpypedqriG-DIEIIPTPGHTPGHVALLY--KDVLMVGDLI 161
Cdd:PLN02398  157 DRIPGIDIvlKDGDKWMFA--------------------GhEVLVMETPGHTRGHISFYFpgSGAIFTGDTL 208
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 12-93 2.11e-07

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: 49.86  E-value: 2.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  12 EVYALDSTQGNYTYLITGE-ENILVDTGRHGQ---GKGILKD-LKAIGIkpDDVQHILITHHDVDHVGSLAS-LEKSTGA 85
Cdd:COG2333     2 RVTFLDVGQGDAILIRTPDgKTILIDTGPRPSfdaGERVVLPyLRALGI--RRLDLLVLTHPDADHIGGLAAvLEAFPVG 79


                  ....*...
gi 2205866422  86 KVWASEKD 93
Cdd:COG2333    80 RVLVSGPP 87
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
25-79 1.89e-06

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 47.11  E-value: 1.89e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2205866422  25 YLIT-GEENILVDTGRhgqgkGILKDLKAIGIKPDDVQHILITHHDVDHVGSLASL 79
Cdd:COG1234    22 YLLEaGGERLLIDCGE-----GTQRQLLRAGLDPRDIDAIFITHLHGDHIAGLPGL 72
metallo-hydrolase-like_MBL-fold cd16276
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 13-209 3.44e-06

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily.Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293834 [Multi-domain]  Cd Length: 188  Bit Score: 45.65  E-value: 3.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  13 VYALDSTQGNYTYLITGEENILVD---TGrhgqGKGILKDLKAIGIKPddVQHILITHHDVDHVGSlASLEKSTGAKVWA 89
Cdd:cd16276     2 VYWVTDGGYQSMFLVTDKGVIVVDappSL----GENLLAAIRKVTDKP--VTHVVYSHNHADHIGG-ASIFKDEGATIIA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  90 SE--KDIpyicgIKGRPGIKwlisVLMP---LKKPEKITpyPEDQRigdIEII-PTPGHTPGHVALLYKD--VLMVGDLI 161
Cdd:cd16276    75 HEatAEL-----LKRNPDPK----RPVPtvtFDDEYTLE--VGGQT---LELSyFGPNHGPGNIVIYLPKqkVLMAVDLI 140

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2205866422 162 ktsRGKIAPMSSFMnwDDEIIKESIH---KINNYNFRWICPAHGEPLMTQE 209
Cdd:cd16276   141 ---NPGWVPFFNFA--GSEDIPGYIEaldELLEYDFDTFVGGHGNRLGTRE 186
YtnP-like_MBL-fold cd07728
Bacillus subtilis YtnP and related proteins; MBL-fold metallo hydrolase domain; Bacillus ...
 28-163 3.64e-06

Bacillus subtilis YtnP and related proteins; MBL-fold metallo hydrolase domain; Bacillus subtilis YtnP inhibits the signaling pathway required for the streptomycin production and development of aerial mycelium in Streptomyces griseus. 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: 293814  Cd Length: 249  Bit Score: 46.10  E-value: 3.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  28 TGEENILVDTGrHGQGK---------------GILKDLKAIGIKPDDVQHILITHHDVDHVGSLASLEKST------GAK 86
Cdd:cd07728    50 YQGKNYLIDAG-IGNGKltekqkrnfgvteesSIEESLAELGLTPEDIDYVLMTHLHFDHASGLTKVKGEQlvsvfpNAT 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  87 VWASEkdipyicgikgrpgIKWlisvlMPLKKP---EKITPYPE------DQRI---GDIEIIP------TPGHTPGHVA 148
Cdd:cd07728   129 IYVSE--------------IEW-----EEMRNPnirSKNTYWKEnwepieDQVKtfsDEIEIVPgitmihTGGHSDGHSI 189

                         170
                  ....*....|....*....
gi 2205866422 149 LLYKD----VLMVGDLIKT 163
Cdd:cd07728   190 IEIEQggetAIHMADLMPT 208
metallo-hydrolase-like_MBL-fold cd16281
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 26-164 7.84e-06

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: 293839  Cd Length: 252  Bit Score: 45.18  E-value: 7.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  26 LI-TGEENILVDTG--------------RHGQGkGILKDLKAIGIKPDDVQHILITHHDVDHVGSLASLEKSTG------ 84
Cdd:cd16281    47 LIeTGGRNILIDTGigdkqdpkfrsiyvQHSEH-SLLKSLARLGLSPEDITDVILTHLHFDHCGGATRADDDGLvellfp 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  85 -AKVWASEKdipyicgikgrpgiKWLISvLMPLKK------PEKITPYPE----------DQRIG-DIEIIPTPGHTPG- 145
Cdd:cd16281   126 nATYWVQKR--------------HWEWA-LNPNPRerasflPENIEPLEEsgrlklidgsDAELGpGIRFHLSDGHTPGq 190

                         170       180
                  ....*....|....*....|..
gi 2205866422 146 -HVALLYKD--VLMVGDLIKTS 164
Cdd:cd16281   191 mLPEISTPGgtVVFAADLIPTS 212
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 32-142 6.04e-05

Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and is related to pfam00753.


Pssm-ID: 432732 [Multi-domain]  Cd Length: 196  Bit Score: 42.30  E-value: 6.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  32 NILVDTG--RHGQGKGILKDLKAigiKPDDVQHILITHHDVDHVGSLASLEKSTGAKVWASEKDIPYICgikgrpgiKWL 109
Cdd:pfam12706   2 RILIDPGpdLRQQALPALQPGRL---RDDPIDAVLLTHDHYDHLAGLLDLREGRPRPLYAPLGVLAHLR--------RNF 70

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2205866422 110 ISVLMPLKKPEKITPYPEDQRI----GDIEIIPTPGH 142
Cdd:pfam12706  71 PYLFLLEHYGVRVHEIDWGESFtvgdGGLTVTATPAR 107
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 25-91 1.01e-04

Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; MBL-fold metallo-hydrolase domain; Includes the archaeal cleavage and polyadenylation specificity factors (CPSFs) such as Methanothermobacter thermautotrophicus MTH1203, and Pyrococcus horikoshii PH1404. In addition to the MBL-fold metallo-hydrolase nuclease and the beta-CASP domains, members of this subgroup contain two contiguous KH domains. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293853 [Multi-domain]  Cd Length: 197  Bit Score: 41.68  E-value: 1.01e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2205866422  25 YLI-TGEENILVDTGRHgQGKGILKDL--KAIGIKPDDVQHILITHHDVDHVGSLASLEKSTG-AKVWASE 91
Cdd:cd16295    15 YLLeTGGKRILLDCGLF-QGGKELEELnnEPFPFDPKEIDAVILTHAHLDHSGRLPLLVKEGFrGPIYATP 84
PRK05452 PRK05452
anaerobic nitric oxide reductase flavorubredoxin; Provisional
 24-99 3.57e-04

anaerobic nitric oxide reductase flavorubredoxin; Provisional


Pssm-ID: 235475 [Multi-domain]  Cd Length: 479  Bit Score: 40.90  E-value: 3.57e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2205866422  24 TYLITGEENILVDTGRHGQGKGILKDLKAiGIKPDDVQHILITHHDVDHVGSLASL-EKSTGAKVWASEKDIPYICG 99
Cdd:PRK05452   37 SYLIREEKNVLIDTVDHKFSREFVQNLRN-EIDLADIDYIVINHAEEDHAGALTELmAQIPDTPIYCTANAIDSING 112
FEZ-1-like_MBL-B3 cd16307
Fluoribacter gormanii FEZ-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 24-97 4.97e-04

Fluoribacter gormanii FEZ-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 FEZ-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: 293865  Cd Length: 255  Bit Score: 40.12  E-value: 4.97e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2205866422  24 TYLI-TGEENILVDTGRHGQGKGILKDLKAIGIKPDDVQHILITHHDVDHVGSLASLEKSTGAKVWASEKDIPYI 97
Cdd:cd16307    24 SYLItTPRGNILINSNLESSVPQIKASIEKLGFKFSDTKILLISHAHFDHAAGSALIKRETHAKYMVMDGDVDVV 98
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 23-76 8.52e-04

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293826 [Multi-domain]  Cd Length: 194  Bit Score: 38.78  E-value: 8.52e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2205866422  23 YTYLITGEENILVDTGrhgqgKGILKDLKAIGIKPDDVQHILITHHDVDHVGSL 76
Cdd:cd07740    18 CFHVASEAGRFLIDCG-----ASSLIALKRAGIDPNAIDAIFITHLHGDHFGGL 66
PRK11921 PRK11921
anaerobic nitric oxide reductase flavorubredoxin;
25-81 2.53e-03

anaerobic nitric oxide reductase flavorubredoxin;


Pssm-ID: 237023 [Multi-domain]  Cd Length: 394  Bit Score: 38.13  E-value: 2.53e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2205866422  25 YLITGEENILVDTGRHGQGKGILKDLKAIgIKPDDVQHILITHHDVDHVGSLASLEK 81
Cdd:PRK11921   36 YLIKDEKTVLIDTVWQPFAKEFVENLKKE-IDLDKIDYIVANHGEIDHSGALPELMK 91
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 24-146 4.86e-03

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 36.82  E-value: 4.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  24 TYLI-TGEENILVD---TGRHGQGKGILKDLKAIgikpDDVQHILITHHDVDHVG--SLASLeKSTGAKVWASEKDIPYI 97
Cdd:COG2220    13 TFLIeTGGKRILIDpvfSGRASPVNPLPLDPEDL----PKIDAVLVTHDHYDHLDdaTLRAL-KRTGATVVAPLGVAAWL 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2205866422  98 cgikgrpgIKWLISVLMPLKKPEKITpypedqrIGDIEIIPTPG-HTPGH 146
Cdd:COG2220    88 --------RAWGFPRVTELDWGESVE-------LGGLTVTAVPArHSSGR 122
arylsulfatase_Sdsa1-like_MBL-fold cd07710
Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and ...
 9-92 5.91e-03

Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and related proteins; MBL-fold metallo-hydrolase domain; Arylsulfatase (also known as aryl-sulfate sulfohydrolase, EC 3.1.6.1). Pseudomonas aeruginosa SdsA1 is a secreted SDS hydrolase that allows the bacterium to use primary sulfates such as the detergent SDS common in commercial personal hygiene products as a sole carbon or sulfur source. Pseudomonas inverting secondary alkylsulfatase 1 (Pisa1) is specific for secondary alkyl sulfates. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293796 [Multi-domain]  Cd Length: 239  Bit Score: 36.71  E-value: 5.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422   9 VTDEVY-ALDSTQGNYTYLITGEENILVDTGRH-GQGKGILKDLKAI-GIKPddVQHILITHHDVDH---VGSLASLEKS 82
Cdd:cd07710     5 VTDGVYqVRGYDLSNMTFIEGDTGLIIIDTLESaEAAKAALELFRKHtGDKP--VKAIIYTHSHPDHfggAGGFVEEEDS 82

                          90
                  ....*....|
gi 2205866422  83 TGAKVWASEK 92
Cdd:cd07710    83 GKVPIIAPEG 92
metallo-hydrolase-like_MBL-fold cd07739
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 26-92 6.00e-03

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293825 [Multi-domain]  Cd Length: 201  Bit Score: 36.33  E-value: 6.00e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  26 LITGEEN-ILVDTG-RHGQGKGILKDLKAIGiKPddVQHILITHHDVDHVGSLASL-EKSTGAKVWASEK 92
Cdd:cd07739    20 LIYGETEaVLVDAQfTRADAERLADWIKASG-KT--LTTIYITHGHPDHYFGLEVLlEAFPDAKVVATPA 86
PRK00685 PRK00685
metal-dependent hydrolase; Provisional
 25-100 6.76e-03

metal-dependent hydrolase; Provisional


Pssm-ID: 234811 [Multi-domain]  Cd Length: 228  Bit Score: 36.33  E-value: 6.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  25 YLITGEENILVD---TGRHgqgkgiLKDLKAIGIKPDdvqHILITHHDVDHVGSLASLEKSTGAKV--------WASEKD 93
Cdd:PRK00685   12 LIETGGKKILIDpfiTGNP------LADLKPEDVKVD---YILLTHGHGDHLGDTVEIAKRTGATVianaelanYLSEKG 82


                  ....*..
gi 2205866422  94 IPYICGI 100
Cdd:PRK00685   83 VEKTHPM 89
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 25-140 7.33e-03

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily.Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry. Some members of this subgroup are named as octanoyltransferase (also known as lipoate-protein ligase B).


Pssm-ID: 293837 [Multi-domain]  Cd Length: 193  Bit Score: 35.91  E-value: 7.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205866422  25 YLITGEENILVDTGrhgqgkgilKDLK--AIGIKPDDVQHILITHHDVDHVGSL-----ASLEKSTGAKVWASEKDIPYI 97
Cdd:cd16279    39 LIETGGKNILIDTG---------PDFRqqALRAGIRKLDAVLLTHAHADHIHGLddlrpFNRLQQRPIPVYASEETLDDL 109

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2205866422  98 C----------GIKGRPGIKWLIsvlmplkkpekITPYpEDQRIGDIEIIPTP 140
Cdd:cd16279   110 KrrfpyffaatGGGGVPKLDLHI-----------IEPD-EPFTIGGLEITPLP 150
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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