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Conserved domains on  [gi|81884571|sp|Q6AYD1|]
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RecName: Full=Metallo-beta-lactamase domain-containing protein 1; AltName: Full=Endoribonuclease MBLAC1

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 10869770)

MBL fold metallo-hydrolase similar to uncharacterized human metallo-beta-lactamase domain-containing protein 1 (MBLAC1 )

Gene Ontology:  GO:0016787
PubMed:  17597585

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
24-240 1.28e-71

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: 217.45  E-value: 1.28e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884571  24 SVVVLLRGYAEPQGvGDAVRADGTVTLVlprgwvsdtsrrlapsaDGGAKTaleeavrgpILVDTGGPWTRDALLEALAT 103
Cdd:cd07711   1 EVKVLVEGYARRDS-DGGFRASSTVTLI-----------------KDGGKN---------ILVDTGTPWDRDLLLKALAE 53
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884571 104 QGVAPGDVTLVVGTHGHSDHIGNLGLFPQAALLVSHDFClpGGLYLPHGLCETQPLILGSGLQVWATPGHGGQrDVSVVV 183
Cdd:cd07711  54 HGLSPEDIDYVVLTHGHPDHIGNLNLFPNATVIVGWDIC--GDSYDDHSLEEGDGYEIDENVEVIPTPGHTPE-DVSVLV 130
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884571 184 EGTSLGTVVVVGDVFERLGDEDS---WQDLSEDPVAQQRSRERILSVADVVVPGHGAPFR 240
Cdd:cd07711 131 ETEKKGTVAVAGDLFEREEDLEDpilWDPLSEDPELQEESRKRILALADWIIPGHGPPFK 190
 
Name Accession Description Interval E-value
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
24-240 1.28e-71

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: 217.45  E-value: 1.28e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884571  24 SVVVLLRGYAEPQGvGDAVRADGTVTLVlprgwvsdtsrrlapsaDGGAKTaleeavrgpILVDTGGPWTRDALLEALAT 103
Cdd:cd07711   1 EVKVLVEGYARRDS-DGGFRASSTVTLI-----------------KDGGKN---------ILVDTGTPWDRDLLLKALAE 53
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884571 104 QGVAPGDVTLVVGTHGHSDHIGNLGLFPQAALLVSHDFClpGGLYLPHGLCETQPLILGSGLQVWATPGHGGQrDVSVVV 183
Cdd:cd07711  54 HGLSPEDIDYVVLTHGHPDHIGNLNLFPNATVIVGWDIC--GDSYDDHSLEEGDGYEIDENVEVIPTPGHTPE-DVSVLV 130
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884571 184 EGTSLGTVVVVGDVFERLGDEDS---WQDLSEDPVAQQRSRERILSVADVVVPGHGAPFR 240
Cdd:cd07711 131 ETEKKGTVAVAGDLFEREEDLEDpilWDPLSEDPELQEESRKRILALADWIIPGHGPPFK 190
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
81-243 2.13e-15

Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];


Pssm-ID: 440257 [Multi-domain]  Cd Length: 215  Bit Score: 72.42  E-value: 2.13e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884571  81 RGPILVDTG-GPWTRDALLEALATQGVapgDVTLVVGTHGHSDHIGNLGLFPQA--ALLVSHDFCLP-------GGLYLP 150
Cdd:COG0491  24 DGAVLIDTGlGPADAEALLAALAALGL---DIKAVLLTHLHPDHVGGLAALAEAfgAPVYAHAAEAEaleapaaGALFGR 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884571 151 HGLCETQPL-------ILGSGLQVWATPGH--GgqrDVSVVVEGtslGTVVVVGDVF--ERLGDEDSWQdlsEDPVAQQR 219
Cdd:COG0491 101 EPVPPDRTLedgdtleLGGPGLEVIHTPGHtpG---HVSFYVPD---EKVLFTGDALfsGGVGRPDLPD---GDLAQWLA 171
                       170       180
                ....*....|....*....|....*
gi 81884571 220 SRERILSV-ADVVVPGHGAPFRVVR 243
Cdd:COG0491 172 SLERLLALpPDLVIPGHGPPTTAEA 196
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
84-235 4.26e-12

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: 62.96  E-value: 4.26e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884571     84 ILVDTGGPWTRDALLEALAtqgVAPGDVTLVVGTHGHSDHIGNLGLFPQA------------ALLVSHDFCLPGGLYLPH 151
Cdd:smart00849  12 ILIDTGPGEAEDLLAELKK---LGPKKIDAIILTHGHPDHIGGLPELLEApgapvyapegtaELLKDLLALLGELGAEAE 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884571    152 GLCETQPL-------ILGSGLQVWATPGHGGQrDVSVVVEGtslGTVVVVGDVFERLGDEDSWQDLSEDPVAQQRS--RE 222
Cdd:smart00849  89 PAPPDRTLkdgdeldLGGGELEVIHTPGHTPG-SIVLYLPE---GKILFTGDLLFAGGDGRTLVDGGDAAASDALEslLK 164
                          170
                   ....*....|...
gi 81884571    223 RILSVADVVVPGH 235
Cdd:smart00849 165 LLKLLPKLVVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
84-235 2.63e-09

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 55.45  E-value: 2.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884571    84 ILVDTGGPWTRDALLEaLATQGVAPGDVTLVVGTHGHSDHIGNLGLFPQA---------ALLVSHDFCLPGGLYLPHGLC 154
Cdd:pfam00753  18 VLIDTGGSAEAALLLL-LAALGLGPKDIDAVILTHGHFDHIGGLGELAEAtdvpvivvaEEARELLDEELGLAASRLGLP 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884571   155 ETQPLILGSGLQVW---------------ATPGHGGqrdvSVVVEGTSLGTVVVVGDVFER--LGDEDSWQDLSEDP--- 214
Cdd:pfam00753  97 GPPVVPLPPDVVLEegdgilggglgllvtHGPGHGP----GHVVVYYGGGKVLFTGDLLFAgeIGRLDLPLGGLLVLhps 172
                         170       180
                  ....*....|....*....|....
gi 81884571   215 ---VAQQRSRERILSVADVVVPGH 235
Cdd:pfam00753 173 saeSSLESLLKLAKLKAAVIVPGH 196
 
Name Accession Description Interval E-value
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
24-240 1.28e-71

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: 217.45  E-value: 1.28e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884571  24 SVVVLLRGYAEPQGvGDAVRADGTVTLVlprgwvsdtsrrlapsaDGGAKTaleeavrgpILVDTGGPWTRDALLEALAT 103
Cdd:cd07711   1 EVKVLVEGYARRDS-DGGFRASSTVTLI-----------------KDGGKN---------ILVDTGTPWDRDLLLKALAE 53
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884571 104 QGVAPGDVTLVVGTHGHSDHIGNLGLFPQAALLVSHDFClpGGLYLPHGLCETQPLILGSGLQVWATPGHGGQrDVSVVV 183
Cdd:cd07711  54 HGLSPEDIDYVVLTHGHPDHIGNLNLFPNATVIVGWDIC--GDSYDDHSLEEGDGYEIDENVEVIPTPGHTPE-DVSVLV 130
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884571 184 EGTSLGTVVVVGDVFERLGDEDS---WQDLSEDPVAQQRSRERILSVADVVVPGHGAPFR 240
Cdd:cd07711 131 ETEKKGTVAVAGDLFEREEDLEDpilWDPLSEDPELQEESRKRILALADWIIPGHGPPFK 190
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
82-235 3.28e-18

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: 80.72  E-value: 3.28e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884571  82 GPILVDTG---------------GPWTR---DALLEALATQGVAPGDVTLVVGTHGHSDHIGNLGLFPQAALLVS---HD 140
Cdd:cd07729  42 GTILVDTGfhpdaaddpgglelaFPPGVteeQTLEEQLARLGLDPEDIDYVILSHLHFDHAGGLDLFPNATIIVQraeLE 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884571 141 FCLpGGLYLPHGLCETQPLI-----------------LGSGLQVWATPGH--GGQrdvSVVVEgTSLGTVVVVGDV--FE 199
Cdd:cd07729 122 YAT-GPDPLAAGYYEDVLALdddlpggrvrlvdgdydLFPGVTLIPTPGHtpGHQ---SVLVR-LPEGTVLLAGDAayTY 196
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 81884571 200 RLGDEDSWQDLSEDPVAQQRSRERILSVAD----VVVPGH 235
Cdd:cd07729 197 ENLEEGRPPGINYDPEAALASLERLKALAEregaRVIPGH 236
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
81-243 2.13e-15

Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];


Pssm-ID: 440257 [Multi-domain]  Cd Length: 215  Bit Score: 72.42  E-value: 2.13e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884571  81 RGPILVDTG-GPWTRDALLEALATQGVapgDVTLVVGTHGHSDHIGNLGLFPQA--ALLVSHDFCLP-------GGLYLP 150
Cdd:COG0491  24 DGAVLIDTGlGPADAEALLAALAALGL---DIKAVLLTHLHPDHVGGLAALAEAfgAPVYAHAAEAEaleapaaGALFGR 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884571 151 HGLCETQPL-------ILGSGLQVWATPGH--GgqrDVSVVVEGtslGTVVVVGDVF--ERLGDEDSWQdlsEDPVAQQR 219
Cdd:COG0491 101 EPVPPDRTLedgdtleLGGPGLEVIHTPGHtpG---HVSFYVPD---EKVLFTGDALfsGGVGRPDLPD---GDLAQWLA 171
                       170       180
                ....*....|....*....|....*
gi 81884571 220 SRERILSV-ADVVVPGHGAPFRVVR 243
Cdd:COG0491 172 SLERLLALpPDLVIPGHGPPTTAEA 196
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
81-236 3.67e-15

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: 71.48  E-value: 3.67e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884571  81 RGPILVDTGGPWTRDALLEALATQGVAPGDVTLVVGTHGHSDHIGNLGLF---PQAALLVSHD----------------F 141
Cdd:cd07721  20 DGLTLIDTGLPGSAKRILKALRELGLSPKDIRRILLTHGHIDHIGSLAALkeaPGAPVYAHEReapylegekpypppvrL 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884571 142 CLPGGLY--LP-------HGLCETQPLILGSGLQVWATPGH-GGQrdVSVVVEGTSlgtVVVVGDVFERLGDEDSWQD-- 209
Cdd:cd07721 100 GLLGLLSplLPvkpvpvdRTLEDGDTLDLAGGLRVIHTPGHtPGH--ISLYLEEDG---VLIAGDALVTVGGELVPPPpp 174
                       170       180
                ....*....|....*....|....*...
gi 81884571 210 LSEDPVAQQRSRERILSV-ADVVVPGHG 236
Cdd:cd07721 175 FTWDMEEALESLRKLAELdPEVLAPGHG 202
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
84-245 2.52e-12

uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized Thermus thermophilus TTHA1429 and related proteins. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293811 [Multi-domain]  Cd Length: 184  Bit Score: 63.47  E-value: 2.52e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884571  84 ILVDTG--GPWTRDALLEALATQGVAPGDVTLVVGTHGHSDHIGNLGLF-PQAALLVSHDFCLPgglyLPHGlcetQPLI 160
Cdd:cd07725  27 TLIDTGlaTEEDAEALWEGLKELGLKPSDIDRVLLTHHHPDHIGLAGKLqEKSGATVYILDVTP----VKDG----DKID 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884571 161 LGS-GLQVWATPGHG-GQrdVSVVVEGtslGTVVVVGD-VFERLGDEDSWQDLS-EDPVAQ-QRSRERILSV-ADVVVPG 234
Cdd:cd07725  99 LGGlRLKVIETPGHTpGH--IVLYDED---RRELFVGDaVLPKITPNVSLWAVRvEDPLGAyLESLDKLEKLdVDLAYPG 173
                       170
                ....*....|.
gi 81884571 235 HGAPFRVVREA 245
Cdd:cd07725 174 HGGPIKDPKAR 184
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
84-235 4.26e-12

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: 62.96  E-value: 4.26e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884571     84 ILVDTGGPWTRDALLEALAtqgVAPGDVTLVVGTHGHSDHIGNLGLFPQA------------ALLVSHDFCLPGGLYLPH 151
Cdd:smart00849  12 ILIDTGPGEAEDLLAELKK---LGPKKIDAIILTHGHPDHIGGLPELLEApgapvyapegtaELLKDLLALLGELGAEAE 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884571    152 GLCETQPL-------ILGSGLQVWATPGHGGQrDVSVVVEGtslGTVVVVGDVFERLGDEDSWQDLSEDPVAQQRS--RE 222
Cdd:smart00849  89 PAPPDRTLkdgdeldLGGGELEVIHTPGHTPG-SIVLYLPE---GKILFTGDLLFAGGDGRTLVDGGDAAASDALEslLK 164
                          170
                   ....*....|...
gi 81884571    223 RILSVADVVVPGH 235
Cdd:smart00849 165 LLKLLPKLVVPGH 177
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
84-138 1.22e-10

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: 59.87  E-value: 1.22e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 81884571  84 ILVDTG-----GPWTrDALLEALATQGVAPGDVTLVVGTHGHSDHIGNL------GLFPQAALLVS 138
Cdd:cd07720  61 ILVDTGagglfGPTA-GKLLANLAAAGIDPEDIDDVLLTHLHPDHIGGLvdaggkPVFPNAEVHVS 125
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
84-235 6.79e-10

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: 57.15  E-value: 6.79e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884571  84 ILVDTG----------GPWTR--DALLEALATQGVAPGDVTLVVGTHGHSDHIG-NLGL--------FPQAALLVSH--- 139
Cdd:cd16277  25 ILVDTGigndkprpgpPAFHNlnTPYLERLAAAGVRPEDVDYVLCTHLHVDHVGwNTRLvdgrwvptFPNARYLFSRaey 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884571 140 DFCLPGGLYLP--HGLCE--TQPLI-------------LGSGLQVWATPGHG-GQrdVSVVVEGTSlGTVVVVGDV---- 197
Cdd:cd16277 105 DHWSSPDAGGPpnRGVFEdsVLPVIeagladlvdddheILDGIRLEPTPGHTpGH--VSVELESGG-ERALFTGDVmhhp 181
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 81884571 198 --FERLgdedswqDLS----EDPVAQQRSRERILS-VAD---VVVPGH 235
Cdd:cd16277 182 iqVARP-------DWSsvfdEDPAQAAATRRRLLErAADtdtLLFPAH 222
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
84-235 2.63e-09

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 55.45  E-value: 2.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884571    84 ILVDTGGPWTRDALLEaLATQGVAPGDVTLVVGTHGHSDHIGNLGLFPQA---------ALLVSHDFCLPGGLYLPHGLC 154
Cdd:pfam00753  18 VLIDTGGSAEAALLLL-LAALGLGPKDIDAVILTHGHFDHIGGLGELAEAtdvpvivvaEEARELLDEELGLAASRLGLP 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884571   155 ETQPLILGSGLQVW---------------ATPGHGGqrdvSVVVEGTSLGTVVVVGDVFER--LGDEDSWQDLSEDP--- 214
Cdd:pfam00753  97 GPPVVPLPPDVVLEegdgilggglgllvtHGPGHGP----GHVVVYYGGGKVLFTGDLLFAgeIGRLDLPLGGLLVLhps 172
                         170       180
                  ....*....|....*....|....
gi 81884571   215 ---VAQQRSRERILSVADVVVPGH 235
Cdd:pfam00753 173 saeSSLESLLKLAKLKAAVIVPGH 196
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
84-235 3.14e-09

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: 54.98  E-value: 3.14e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884571  84 ILVDTGGPwTRDALLEALATQGVapgDVTLVVGTHGHSDHIGNLGLFPQ------------AALLVSHDFCLPGGLYLP- 150
Cdd:cd06262  23 ILIDPGAG-ALEKILEAIEELGL---KIKAILLTHGHFDHIGGLAELKEapgapvyiheadAELLEDPELNLAFFGGGPl 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884571 151 ------HGLCETQPLILGS-GLQVWATPGH--GGqrdVSVVVEGtslGTVVVVGDV-FE----RLGDEDSwqdlseDPVA 216
Cdd:cd06262  99 pppepdILLEDGDTIELGGlELEVIHTPGHtpGS---VCFYIEE---EGVLFTGDTlFAgsigRTDLPGG------DPEQ 166
                       170       180
                ....*....|....*....|..
gi 81884571 217 QQRSRERILSVAD---VVVPGH 235
Cdd:cd06262 167 LIESIKKLLLLLPddtVVYPGH 188
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
82-137 1.55e-07

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: 50.57  E-value: 1.55e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884571  82 GPILVDTGGPWTRDALLEALATQGVAPGDVTLVVGTHGHSDHIGNLGL----FPQAALLV 137
Cdd:cd07726  26 RPALIDTGPSSSVPRLLAALEALGIAPEDVDYIILTHIHLDHAGGAGLlaeaLPNAKVYV 85
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
81-142 2.15e-07

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


Pssm-ID: 293816 [Multi-domain]  Cd Length: 250  Bit Score: 50.34  E-value: 2.15e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884571  81 RGPILVDTG---------------------GPWTRDALLEALATQGVAPGDVTLVVGTHGHSDHIGNLGLFPQAALLVSH 139
Cdd:cd07730  33 GGKILFDLGyrkdfeeytprvperlyrtpvPLEVEEDVAEQLAAGGIDPEDIDAVILSHLHWDHIGGLSDFPNARLIVGP 112

                ...
gi 81884571 140 DFC 142
Cdd:cd07730 113 GAK 115
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
84-127 8.82e-07

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: 47.90  E-value: 8.82e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 81884571  84 ILVDTGGPWT--RDALLEALATQGVapGDVTLVVGTHGHSDHIGNL 127
Cdd:cd07731  22 ILIDTGPRDSfgEDVVVPYLKARGI--KKLDYLILTHPDADHIGGL 65
L1_POM-1-like_MBL-B3 cd16289
Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-1 and related ...
82-127 9.10e-07

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: 48.66  E-value: 9.10e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 81884571  82 GPILVDTGGPWTRDALLEALATQGVAPGDVTLVVGTHGHSDHIGNL 127
Cdd:cd16289  32 GAVLLDGGMPQAADMLLDNMRALGVAPGDLKLILHSHAHADHAGPL 77
metallo-hydrolase-like_MBL-fold cd16281
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
84-139 9.62e-07

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


Pssm-ID: 293839  Cd Length: 252  Bit Score: 48.65  E-value: 9.62e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 81884571  84 ILVDTG-------------GPWTRDALLEALATQGVAPGDVTLVVGTHGHSDHIGNLG----------LFPQAALLVSH 139
Cdd:cd16281  55 ILIDTGigdkqdpkfrsiyVQHSEHSLLKSLARLGLSPEDITDVILTHLHFDHCGGATradddglvelLFPNATYWVQK 133
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
84-173 1.39e-06

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: 47.07  E-value: 1.39e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884571  84 ILVDTGGPwtrDALLEALATQGVapgDVTLVVGTHGHSDHI-GNLGL---FPQAALLVSHDFCLPGglyLPHGLCETQPL 159
Cdd:cd07723  23 AVVDPGEA---EPVLAALEKNGL---TLTAILTTHHHWDHTgGNAELkalFPDAPVYGPAEDRIPG---LDHPVKDGDEI 93
                        90
                ....*....|....*
gi 81884571 160 ILGSG-LQVWATPGH 173
Cdd:cd07723  94 KLGGLeVKVLHTPGH 108
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
84-133 1.92e-06

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


Pssm-ID: 440850  Cd Length: 273  Bit Score: 47.57  E-value: 1.92e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 81884571  84 ILVDTGGPwtrDALLEALATQGVAPGDVTLVVGTHGHSDHIGNLGLFPQA 133
Cdd:COG1237  34 ILFDTGQS---DVLLKNAEKLGIDLSDIDAVVLSHGHYDHTGGLPALLEL 80
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
84-138 2.37e-06

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: 47.16  E-value: 2.37e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 81884571  84 ILVDTGGPWTRDA----LLEALATQGVapGDVTLVVGTHGHSDHIGNL----GLFPQAALLVS 138
Cdd:COG2333  24 ILIDTGPRPSFDAgervVLPYLRALGI--RRLDLLVLTHPDADHIGGLaavlEAFPVGRVLVS 84
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
81-238 4.80e-05

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


Pssm-ID: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 42.94  E-value: 4.80e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884571  81 RGPILVDTGGPWTR-DALLEALATqgVAPGDVTLVVGTHGHSDHI-GNLGLFPQAALLVSHDFCL-----PGGLYLPHGL 153
Cdd:cd16282  24 DGVVVIDTGASPRLaRALLAAIRK--VTDKPVRYVVNTHYHGDHTlGNAAFADAGAPIIAHENTReelaaRGEAYLELMR 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884571 154 CETQPLILGSGLqVWAT----------------------PGH-GGqrDVSVVVEGTSlgtVVVVGD-VFERLGDEDSWQD 209
Cdd:cd16282 102 RLGGDAMAGTEL-VLPDrtfddgltldlggrtvelihlgPAHtPG--DLVVWLPEEG---VLFAGDlVFNGRIPFLPDGS 175
                       170       180
                ....*....|....*....|....*....
gi 81884571 210 LSEDPVAQQRSRERIlsvADVVVPGHGAP 238
Cdd:cd16282 176 LAGWIAALDRLLALD---ATVVVPGHGPV 201
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
84-127 6.00e-05

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: 43.38  E-value: 6.00e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 81884571  84 ILVDTGgpwTRDALLEALATQGVAPGDVTLVVGTHGHSDHIGNL 127
Cdd:cd07713  32 ILFDTG---QSGVLLHNAKKLGIDLSDIDAVVLSHGHYDHTGGL 72
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
82-125 6.51e-05

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


Pssm-ID: 293838 [Multi-domain]  Cd Length: 251  Bit Score: 42.96  E-value: 6.51e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 81884571  82 GPILVDTGgpWTRDA---LLEALATQGVAPGDVTLVVGTHGHSDHIG 125
Cdd:cd16280  32 GLILIDAL--NNNEAadlIVDGLEKLGLDPADIKYILITHGHGDHYG 76
metallo-hydrolase-like_MBL-fold cd07742
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
82-138 1.64e-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: 293828 [Multi-domain]  Cd Length: 249  Bit Score: 41.84  E-value: 1.64e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884571  82 GPILVDTG-------------GPWTRDAL-------------LEALatqGVAPGDVTLVVGTHGHSDHIGNLGLFPQAAL 135
Cdd:cd07742  29 GLVLVDTGfgladvadpkrrlGGPFRRLLrprldedetavrqIEAL---GFDPSDVRHIVLTHLDLDHAGGLADFPHATV 105

                ...
gi 81884571 136 LVS 138
Cdd:cd07742 106 HVH 108
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
82-133 4.11e-04

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


Pssm-ID: 293867 [Multi-domain]  Cd Length: 252  Bit Score: 40.55  E-value: 4.11e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 81884571  82 GPILVDTGGPWTRDALLEALATQGVAPGDVTLVVGTHGHSDHIGNLGLFPQA 133
Cdd:cd16309  32 GHILIDGAMPQSTPLIKDNIKKLGFDVKDVKYLLNTHAHFDHAGGLAELKKA 83
EVM-1-like_MBL-B3 cd16315
Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
82-133 4.28e-04

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


Pssm-ID: 293873 [Multi-domain]  Cd Length: 248  Bit Score: 40.41  E-value: 4.28e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 81884571  82 GPILVDTGGPWTRDALLEALATQGVAPGDVTLVVGTHGHSDHIGNLGLFPQA 133
Cdd:cd16315  32 GHVLIDSGTEEAAPLVLANIRKLGFDPKDVRWLLSSHEHFDHVGGLAALQRA 83
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
82-244 4.51e-04

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: 40.02  E-value: 4.51e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884571  82 GPILVDTGgpwtrDALLEALATQGVAPGDVTLVVGTHGHSDHIGNLG----------LFPQAALLVSHDFCLPGGLYLPH 151
Cdd:cd16322  23 EAVLVDPG-----DESEKLLARFGTTGLTLLYILLTHAHFDHVGGVAdlrrhpgapvYLHPDDLPLYEAADLGAKAFGLG 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884571 152 G---------LCETQPLILGS-GLQVWATPGHG-GQrdVSVVVEGtslGTVVVVGD-VFER-LGDEDSWQDlseDPVAQQ 218
Cdd:cd16322  98 IeplpppdrlLEDGQTLTLGGlEFKVLHTPGHSpGH--VCFYVEE---EGLLFSGDlLFQGsIGRTDLPGG---DPKAMA 169
                       170       180
                ....*....|....*....|....*...
gi 81884571 219 RSRERILSVAD--VVVPGHGAPFRVVRE 244
Cdd:cd16322 170 ASLRRLLTLPDetRVFPGHGPPTTLGEE 197
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
81-125 8.30e-04

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: 39.84  E-value: 8.30e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 81884571  81 RGPILVDTGGPWTRDALLEALATQGVAPGDVTLVVGTHGHSDHIG 125
Cdd:cd07708  31 QGNILIDGDMEQNAPMIKANIKKLGFKFSDTKLILISHAHFDHAG 75
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
84-173 8.36e-04

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: 39.05  E-value: 8.36e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884571  84 ILVDTG--GPWTRDALLEALATQGVAPgdVTLVVGTHGHSDHIGNL----GLFPQAAL------LVSHDFCLPGGLYLPH 151
Cdd:cd07722  30 ILIDTGegRPSYIPLLKSVLDSEGNAT--ISDILLTHWHHDHVGGLpdvlDLLRGPSPrvykfpRPEEDEDPDEDGGDIH 107
                        90       100
                ....*....|....*....|...
gi 81884571 152 GLCETQPL-ILGSGLQVWATPGH 173
Cdd:cd07722 108 DLQDGQVFkVEGATLRVIHTPGH 130
THIN-B2-like_MBL-B3 cd16311
Janthinobacterium lividum THIN-B2 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
71-127 1.97e-03

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: 38.81  E-value: 1.97e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 81884571  71 GAKTALEEAVRGPILVDTGGPWTRDALLEALATQGVAPGDVTLVVGTHGHSDHIGNL 127
Cdd:cd16311  21 GLSSVLVTSPQGHVLVDGGLPESAPKIIANIEALGFRIEDVKLILNSHGHIDHAGGL 77
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
78-130 2.00e-03

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: 37.63  E-value: 2.00e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 81884571  78 EAVRGPILVDTGgpWTRDALLEALATQGVAPGDVTLVVGTHGHSDHIGNLGLF 130
Cdd:cd07733  15 ETEDGKLLIDAG--LSGRKITGRLAEIGRDPEDIDAILVTHEHADHIKGLGVL 65
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
95-173 2.71e-03

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


Pssm-ID: 293836 [Multi-domain]  Cd Length: 185  Bit Score: 37.86  E-value: 2.71e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884571  95 DALLEALAtqgvaPGDVTLVVGTHGHSDHIGNLGLFPQA----------ALLVSHDFCLPGGLYLPHGLCETQPlilGSG 164
Cdd:cd16278  43 DALLAALG-----GGRVSAILVTHTHRDHSPGAARLAERtgapvrafgpHRAGGQDTDFAPDRPLADGEVIEGG---GLR 114

                ....*....
gi 81884571 165 LQVWATPGH 173
Cdd:cd16278 115 LTVLHTPGH 123
MBL-B1 cd16285
metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
84-238 2.91e-03

metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. Subclass B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. Includes chromosomally-encoded MBLs such as Bacillus cereus BcII, Bacteroides fragilis CcrA, and Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) BlaB and acquired MBLs including IMP-1, VIM-1, VIM-2, GIM-1, NDM-1 and FIM-1.


Pssm-ID: 293843 [Multi-domain]  Cd Length: 210  Bit Score: 37.65  E-value: 2.91e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884571  84 ILVDTggPWTRD---ALLEALATQGVAPgdVTLVVGTHGHSDHIGNLGLF----------PQAALLVSHDfclpGGLYLP 150
Cdd:cd16285  38 VLIDT--PWTEAqtaTLLDWIEKKLGKP--VTAAISTHSHDDRTGGIKALnargiptyatALTNELAKKE----GKPVPT 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884571 151 HGLCETQPLILGSgLQVWaTPGHGGQRDVSVVVEGTSlgtVVVVGDVFERLGDEDSWQDLSE-DPVAQQRSRERIL---S 226
Cdd:cd16285 110 HSLKGALTLGFGP-LEVF-YPGPGHTPDNIVVWLPKS---KILFGGCLVKSASATSLGNVGDaDVEAWPKSIENLKakyP 184
                       170
                ....*....|..
gi 81884571 227 VADVVVPGHGAP 238
Cdd:cd16285 185 EARMVVPGHGAP 196
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
80-135 2.96e-03

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: 37.61  E-value: 2.96e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 81884571  80 VRGP---ILVDTGGPwTRDaLLEALATQGVAPgdvTLVVGTHGHSDHIGNLGLFPQAAL 135
Cdd:cd07712  14 LRGRdraLLIDTGLG-IGD-LKEYVRTLTDLP---LLVVATHGHFDHIGGLHEFEEVYV 67
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
81-173 5.23e-03

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: 37.30  E-value: 5.23e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884571  81 RGPILVDTGGPWTRDALLEALATQGVAPGDVTLVVGTHGHSDHIGNLGLFPQ---AALLVS------------HDFCL-- 143
Cdd:cd16288  31 QGLILIDTGLESSAPMIKANIRKLGFKPSDIKILLNSHAHLDHAGGLAALKKltgAKLMASaedaallasggkSDFHYgd 110
                        90       100       110
                ....*....|....*....|....*....|....*
gi 81884571 144 PGGLYLP----HGLCETQPLILG-SGLQVWATPGH 173
Cdd:cd16288 111 DSLAFPPvkvdRVLKDGDRVTLGgTTLTAHLTPGH 145
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 ...
82-127 5.76e-03

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: 37.33  E-value: 5.76e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 81884571  82 GPILVDTGGPWTRDALLEALATQGVAPGDVTLVVGTHGHSDHIGNL 127
Cdd:cd16290  32 GLILIDGALPQSAPQIEANIRALGFRLEDVKLILNSHAHFDHAGGI 77
metallo-hydrolase-like_MBL-fold cd16276
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
82-140 8.50e-03

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


Pssm-ID: 293834 [Multi-domain]  Cd Length: 188  Bit Score: 36.41  E-value: 8.50e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884571  82 GPILVDTGgPWTRDALLEALatQGVAPGDVTLVVGTHGHSDHIGNLGLFP-QAALLVSHD 140
Cdd:cd16276  20 GVIVVDAP-PSLGENLLAAI--RKVTDKPVTHVVYSHNHADHIGGASIFKdEGATIIAHE 76
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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