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Conserved domains on  [gi|723626132|gb|AIY19608|]
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hypothetical protein KR76_00190 [Pimelobacter simplex]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 10870238)

uncharacterized member of the MBL fold metallo-hydrolase superfamily

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold cd07742
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 4-247 4.90e-123

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: 350.39  E-value: 4.90e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723626132   4 HHLNCATMRPALGP-TMVAHVLLLERPDGLALVDTGFGTEDLAR-RRRLGRPFLLTVRPDLDPAETALAQVKARGFAPSD 81
Cdd:cd07742    1 HHLNCGTMRPPGGDlRLVCHCLLVETDDGLVLVDTGFGLADVADpKRRLGGPFRRLLRPRLDEDETAVRQIEALGFDPSD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723626132  82 VTDIVLTHLDLDHAGGIGDFPQARVHVHAREHAAAT-TPTAREKARYVAGQWAHGPRWTPHTEGSDAWFGFASVTALD-- 158
Cdd:cd07742   81 VRHIVLTHLDLDHAGGLADFPHATVHVHAAELDAATsPRTRYERRRYRPQQLAHGPWWVTYAAGGERWFGFEAVRPLDgl 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723626132 159 -DDVLIIPLPGHTRGHAGVAVRRDDGtWLLHAGDAFFHGGQLDVPARCPASLTAFQRLMAVDNRRRLDNLARLQELAQGR 237
Cdd:cd07742  161 pPEILLVPLPGHTRGHCGVAVRTGDR-WLLHAGDAYFHHGELDPLPPPPPPLRLFQRLLAVDRSARLANLARLRELARDH 239

                        250
                 ....*....|
gi 723626132 238 SGEVTVICAH 247
Cdd:cd07742  240 GDEVEVFCAH 249
 
Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold cd07742
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 4-247 4.90e-123

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: 350.39  E-value: 4.90e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723626132   4 HHLNCATMRPALGP-TMVAHVLLLERPDGLALVDTGFGTEDLAR-RRRLGRPFLLTVRPDLDPAETALAQVKARGFAPSD 81
Cdd:cd07742    1 HHLNCGTMRPPGGDlRLVCHCLLVETDDGLVLVDTGFGLADVADpKRRLGGPFRRLLRPRLDEDETAVRQIEALGFDPSD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723626132  82 VTDIVLTHLDLDHAGGIGDFPQARVHVHAREHAAAT-TPTAREKARYVAGQWAHGPRWTPHTEGSDAWFGFASVTALD-- 158
Cdd:cd07742   81 VRHIVLTHLDLDHAGGLADFPHATVHVHAAELDAATsPRTRYERRRYRPQQLAHGPWWVTYAAGGERWFGFEAVRPLDgl 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723626132 159 -DDVLIIPLPGHTRGHAGVAVRRDDGtWLLHAGDAFFHGGQLDVPARCPASLTAFQRLMAVDNRRRLDNLARLQELAQGR 237
Cdd:cd07742  161 pPEILLVPLPGHTRGHCGVAVRTGDR-WLLHAGDAYFHHGELDPLPPPPPPLRLFQRLLAVDRSARLANLARLRELARDH 239

                        250
                 ....*....|
gi 723626132 238 SGEVTVICAH 247
Cdd:cd07742  240 GDEVEVFCAH 249
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 3-197 3.76e-18

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: 80.50  E-value: 3.76e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723626132   3 IHHLNCATMRPALGptmvAHVLLLERPDGLALVDTGFGTEDlarrrrlgrpflltvrpdldpAETALAQVKARGfapSDV 82
Cdd:COG0491    1 VYVLPGGTPGAGLG----VNSYLIVGGDGAVLIDTGLGPAD---------------------AEALLAALAALG---LDI 52

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723626132  83 TDIVLTHLDLDHAGGIGDFPQ---ARVHVHAREHAAATTPTAREKARYVAGQWAHgprwtPHTEGSDAWFGfasvtalDD 159
Cdd:COG0491   53 KAVLLTHLHPDHVGGLAALAEafgAPVYAHAAEAEALEAPAAGALFGREPVPPDR-----TLEDGDTLELG-------GP 120

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 723626132 160 DVLIIPLPGHTRGHAGVAVRRDdgtWLLHAGDAFFHGG 197
Cdd:COG0491  121 GLEVIHTPGHTPGHVSFYVPDE---KVLFTGDALFSGG 155
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 22-225 1.50e-15

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: 72.59  E-value: 1.50e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723626132    22 HVLLLERPDGLALVDTGFGTedlarrrrlgrpflltvrpdldpAETALAQVKARGfaPSDVTDIVLTHLDLDHAGGIGDF 101
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGE-----------------------AEDLLAELKKLG--PKKIDAIILTHGHPDHIGGLPEL 55

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723626132   102 ---PQARVHVHAREHAAATTPTAREKARYVAGQWAhgPRWTPHTEGSDAWFGfasvtalDDDVLIIPLPGHTRGHAGVav 178
Cdd:smart00849  56 leaPGAPVYAPEGTAELLKDLLALLGELGAEAEPA--PPDRTLKDGDELDLG-------GGELEVIHTPGHTPGSIVL-- 124

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 723626132   179 rRDDGTWLLHAGDAFFHGGQLDvPARCPASLTAFQRLMAVDNRRRLD 225
Cdd:smart00849 125 -YLPEGKILFTGDLLFAGGDGR-TLVDGGDAAASDALESLLKLLKLL 169
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
23-230 3.14e-15

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 72.02  E-value: 3.14e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723626132   23 VLLLERPDGLALVDTGFGTEdlarrrrlgrpflltvrpdldpaETALAQVKARGFAPSDVTDIVLTHLDLDHAGGIGDFP 102
Cdd:pfam00753   8 SYLIEGGGGAVLIDTGGSAE-----------------------AALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELA 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723626132  103 QARVHVHAREHAAATTPTAREKARYvAGQWAHGPRWTPHTEGSDAWFGFASVTALDDDVLIIPLPGHTRGHAGVAVRRDD 182
Cdd:pfam00753  65 EATDVPVIVVAEEARELLDEELGLA-ASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGK 143

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 723626132  183 gtwLLHAGDAFFHGGQLDVPARCPASLTAFQRLMAvDNRRRLDNLARL 230
Cdd:pfam00753 144 ---VLFTGDLLFAGEIGRLDLPLGGLLVLHPSSAE-SSLESLLKLAKL 187
 
Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold cd07742
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 4-247 4.90e-123

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: 350.39  E-value: 4.90e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723626132   4 HHLNCATMRPALGP-TMVAHVLLLERPDGLALVDTGFGTEDLAR-RRRLGRPFLLTVRPDLDPAETALAQVKARGFAPSD 81
Cdd:cd07742    1 HHLNCGTMRPPGGDlRLVCHCLLVETDDGLVLVDTGFGLADVADpKRRLGGPFRRLLRPRLDEDETAVRQIEALGFDPSD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723626132  82 VTDIVLTHLDLDHAGGIGDFPQARVHVHAREHAAAT-TPTAREKARYVAGQWAHGPRWTPHTEGSDAWFGFASVTALD-- 158
Cdd:cd07742   81 VRHIVLTHLDLDHAGGLADFPHATVHVHAAELDAATsPRTRYERRRYRPQQLAHGPWWVTYAAGGERWFGFEAVRPLDgl 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723626132 159 -DDVLIIPLPGHTRGHAGVAVRRDDGtWLLHAGDAFFHGGQLDVPARCPASLTAFQRLMAVDNRRRLDNLARLQELAQGR 237
Cdd:cd07742  161 pPEILLVPLPGHTRGHCGVAVRTGDR-WLLHAGDAYFHHGELDPLPPPPPPLRLFQRLLAVDRSARLANLARLRELARDH 239

                        250
                 ....*....|
gi 723626132 238 SGEVTVICAH 247
Cdd:cd07742  240 GDEVEVFCAH 249
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 2-248 1.32e-37

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: 132.34  E-value: 1.32e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723626132   2 RIHHLNCATM-----------RPALGP-TMVAHVLLLERPDGLALVDTGFGtEDLARRRRLGRPFLLTVRPDLDPAETAL 69
Cdd:cd07729    1 KLYALDYGTVtvdksslfyygRGPGEPiDLPVYAYLIEHPEGTILVDTGFH-PDAADDPGGLELAFPPGVTEEQTLEEQL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723626132  70 AQVkarGFAPSDVTDIVLTHLDLDHAGGIGDFPQARVHVHAREHAAATTPTAREKARYVAGQWA----HGPRWTPHTEGS 145
Cdd:cd07729   80 ARL---GLDPEDIDYVILSHLHFDHAGGLDLFPNATIIVQRAELEYATGPDPLAAGYYEDVLALdddlPGGRVRLVDGDY 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723626132 146 DawfgfasvtaLDDDVLIIPLPGHTRGHAGVAVRRDDGTWLLhAGDAFFHGGQLDvpARCPASLTafqrlmaVDNRRRLD 225
Cdd:cd07729  157 D----------LFPGVTLIPTPGHTPGHQSVLVRLPEGTVLL-AGDAAYTYENLE--EGRPPGIN-------YDPEAALA 216

                        250       260
                 ....*....|....*....|...
gi 723626132 226 NLARLQELAqgRSGEVTVICAHD 248
Cdd:cd07729  217 SLERLKALA--EREGARVIPGHD 237
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 18-248 3.37e-32

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: 118.52  E-value: 3.37e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723626132  18 TMVAHVLLLERPD-GLALVDTGFGTeDLARRRRLGRPFLLTVRPDLDPAETALAQVKARGFAPSDVTDIVLTHLDLDHAG 96
Cdd:cd07730   20 TFPALAFLIEHPTgGKILFDLGYRK-DFEEYTPRVPERLYRTPVPLEVEEDVAEQLAAGGIDPEDIDAVILSHLHWDHIG 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723626132  97 GIGDFPQARVHVHAREHAAATTPTAREK--ARYVAGQWAHGPRWTPHTEGSDAWFG-FASvtALD--DD--VLIIPLPGH 169
Cdd:cd07730   99 GLSDFPNARLIVGPGAKEALRPPGYPSGflPELLPSDFEGRLVRWEEDDFLWVPLGpFPR--ALDlfGDgsLYLVDLPGH 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723626132 170 TRGHAGVAVRRDDGTWLLHAGDAFFHGgqldVPARCPASLTAFQRLMAVDNRRR-LDNLARLQELAqgRSGEVTVICAHD 248
Cdd:cd07730  177 APGHLGLLARTTSGTWVFLAGDACHHR----IGLLRPSPLLPLPDLDDGADREAaRETLARLRELD--AAPDVRVVLAHD 250
metallo-hydrolase-like_MBL-fold cd16281
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 18-191 4.52e-20

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: 86.39  E-value: 4.52e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723626132  18 TMVAHVLLLERPDGLALVDTGFGT--EDLARRRRlgrpflltVRPDLDPAETALAQVkarGFAPSDVTDIVLTHLDLDHA 95
Cdd:cd16281   40 TLAMRCLLIETGGRNILIDTGIGDkqDPKFRSIY--------VQHSEHSLLKSLARL---GLSPEDITDVILTHLHFDHC 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723626132  96 GGI----GD------FPQARVHVHAREHAAATTPTAREKARYV---------AGQWahgpRWtphTEGSDAWfgfasvta 156
Cdd:cd16281  109 GGAtradDDglvellFPNATYWVQKRHWEWALNPNPRERASFLpeniepleeSGRL----KL---IDGSDAE-------- 173

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 723626132 157 LDDDVLIIPLPGHTRGHAGVAVRRDDGTwLLHAGD 191
Cdd:cd16281  174 LGPGIRFHLSDGHTPGQMLPEISTPGGT-VVFAAD 207
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 23-237 1.51e-19

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: 84.91  E-value: 1.51e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723626132  23 VLLLERPDGLALVDTGFGTedlARRRRLGRpflltvrpdldpaetALAQVKARGFAPSDVTDIVLTHLDLDHAGGIGD-- 100
Cdd:cd07720   51 AFLVRTGGRLILVDTGAGG---LFGPTAGK---------------LLANLAAAGIDPEDIDDVLLTHLHPDHIGGLVDag 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723626132 101 ----FPQARVHVHAREHAAATTPTAREKARYVAGQWAHGPRWTPHTegsdawFGFASVTALDDDVL----IIPLPGHTRG 172
Cdd:cd07720  113 gkpvFPNAEVHVSEAEWDFWLDDANAAKAPEGAKRFFDAARDRLRP------YAAAGRFEDGDEVLpgitAVPAPGHTPG 186

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 723626132 173 HAGVAVRRDDGTwLLHAGDAFFHGgqlDVPARCPASLTAF--QRLMAVDNRRRLdnlarLQELAQGR 237
Cdd:cd07720  187 HTGYRIESGGER-LLIWGDIVHHP---ALQFAHPDWTIAFdvDPEQAAATRRRL-----LDRAAAEG 244
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 23-207 2.45e-19

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: 83.02  E-value: 2.45e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723626132  23 VLLLERPDGLALVDTGFGTedlarrrrlGRPFLLTvrpdldpaetALAQvkaRGFAPSDVTDIVLTHLDLDHAGGIGDFP 102
Cdd:cd07711   24 VTLIKDGGKNILVDTGTPW---------DRDLLLK----------ALAE---HGLSPEDIDYVVLTHGHPDHIGNLNLFP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723626132 103 QARVHVHarehaaattptarekaryvagQWAHGPRWTPHTEGSDawFGFasvtALDDDVLIIPLPGHTRGHAGVAVRRDD 182
Cdd:cd07711   82 NATVIVG---------------------WDICGDSYDDHSLEEG--DGY----EIDENVEVIPTPGHTPEDVSVLVETEK 134

                        170       180
                 ....*....|....*....|....*.
gi 723626132 183 -GTWLLhAGDAFFHGGQLDVPARCPA 207
Cdd:cd07711  135 kGTVAV-AGDLFEREEDLEDPILWDP 159
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 15-247 7.11e-19

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: 81.88  E-value: 7.11e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723626132  15 LGPTMVAHVLLLERPDGLALVDTGFgtedlarrrrlgrPFlltvrpdldPAETALAQVKARGFAPSDVTDIVLTHLDLDH 94
Cdd:cd07721    5 LPLLPPVNAYLIEDDDGLTLIDTGL-------------PG---------SAKRILKALRELGLSPKDIRRILLTHGHIDH 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723626132  95 AGGIGDF---PQARVHVHAREhaaattptarekARYVAGQWAHGPRWTPHTEGSDAWF-----GFASVTALDDDVL---- 162
Cdd:cd07721   63 IGSLAALkeaPGAPVYAHERE------------APYLEGEKPYPPPVRLGLLGLLSPLlpvkpVPVDRTLEDGDTLdlag 130

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723626132 163 ---IIPLPGHTRGHAGVaVRRDDGTwlLHAGDAFFHGGQLDVPArcPASLTAfqrlmavDNRRRLDNLARLQELAQgrsg 239
Cdd:cd07721  131 glrVIHTPGHTPGHISL-YLEEDGV--LIAGDALVTVGGELVPP--PPPFTW-------DMEEALESLRKLAELDP---- 194


                 ....*...
gi 723626132 240 eVTVICAH 247
Cdd:cd07721  195 -EVLAPGH 201
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 3-197 3.76e-18

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: 80.50  E-value: 3.76e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723626132   3 IHHLNCATMRPALGptmvAHVLLLERPDGLALVDTGFGTEDlarrrrlgrpflltvrpdldpAETALAQVKARGfapSDV 82
Cdd:COG0491    1 VYVLPGGTPGAGLG----VNSYLIVGGDGAVLIDTGLGPAD---------------------AEALLAALAALG---LDI 52

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723626132  83 TDIVLTHLDLDHAGGIGDFPQ---ARVHVHAREHAAATTPTAREKARYVAGQWAHgprwtPHTEGSDAWFGfasvtalDD 159
Cdd:COG0491   53 KAVLLTHLHPDHVGGLAALAEafgAPVYAHAAEAEALEAPAAGALFGREPVPPDR-----TLEDGDTLELG-------GP 120

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 723626132 160 DVLIIPLPGHTRGHAGVAVRRDdgtWLLHAGDAFFHGG 197
Cdd:COG0491  121 GLEVIHTPGHTPGHVSFYVPDE---KVLFTGDALFSGG 155
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 22-225 1.50e-15

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: 72.59  E-value: 1.50e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723626132    22 HVLLLERPDGLALVDTGFGTedlarrrrlgrpflltvrpdldpAETALAQVKARGfaPSDVTDIVLTHLDLDHAGGIGDF 101
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGE-----------------------AEDLLAELKKLG--PKKIDAIILTHGHPDHIGGLPEL 55

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723626132   102 ---PQARVHVHAREHAAATTPTAREKARYVAGQWAhgPRWTPHTEGSDAWFGfasvtalDDDVLIIPLPGHTRGHAGVav 178
Cdd:smart00849  56 leaPGAPVYAPEGTAELLKDLLALLGELGAEAEPA--PPDRTLKDGDELDLG-------GGELEVIHTPGHTPGSIVL-- 124

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 723626132   179 rRDDGTWLLHAGDAFFHGGQLDvPARCPASLTAFQRLMAVDNRRRLD 225
Cdd:smart00849 125 -YLPEGKILFTGDLLFAGGDGR-TLVDGGDAAASDALESLLKLLKLL 169
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
23-230 3.14e-15

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 72.02  E-value: 3.14e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723626132   23 VLLLERPDGLALVDTGFGTEdlarrrrlgrpflltvrpdldpaETALAQVKARGFAPSDVTDIVLTHLDLDHAGGIGDFP 102
Cdd:pfam00753   8 SYLIEGGGGAVLIDTGGSAE-----------------------AALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELA 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723626132  103 QARVHVHAREHAAATTPTAREKARYvAGQWAHGPRWTPHTEGSDAWFGFASVTALDDDVLIIPLPGHTRGHAGVAVRRDD 182
Cdd:pfam00753  65 EATDVPVIVVAEEARELLDEELGLA-ASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGK 143

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 723626132  183 gtwLLHAGDAFFHGGQLDVPARCPASLTAFQRLMAvDNRRRLDNLARL 230
Cdd:pfam00753 144 ---VLFTGDLLFAGEIGRLDLPLGGLLVLHPSSAE-SSLESLLKLAKL 187
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 22-247 7.38e-14

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: 68.70  E-value: 7.38e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723626132  22 HVLLLERPDGLALVDTGFGtEDLARRRRlgrpflltvrPDLDPAETA-LAQVKARGFAPSDVTDIVLTHLDLDHAGG--- 97
Cdd:cd16277   14 HSWLVRTPGRTILVDTGIG-NDKPRPGP----------PAFHNLNTPyLERLAAAGVRPEDVDYVLCTHLHVDHVGWntr 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723626132  98 -IGD-----FPQARVHVHAREHAaattptarekarYVAGQWAHGPRWTPHTEGS-----DAwfGFASV----TALDDDVL 162
Cdd:cd16277   83 lVDGrwvptFPNARYLFSRAEYD------------HWSSPDAGGPPNRGVFEDSvlpviEA--GLADLvdddHEILDGIR 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723626132 163 IIPLPGHTRGHAGVAVRRDDGTWLLhAGDAFFHGGQLDVPARCPASLTAFQRlmAVDNRRRLdnlarlqeLAQGRSGEVT 242
Cdd:cd16277  149 LEPTPGHTPGHVSVELESGGERALF-TGDVMHHPIQVARPDWSSVFDEDPAQ--AAATRRRL--------LERAADTDTL 217


                 ....*
gi 723626132 243 VICAH 247
Cdd:cd16277  218 LFPAH 222
YtnP-like_MBL-fold cd07728
Bacillus subtilis YtnP and related proteins; MBL-fold metallo hydrolase domain; Bacillus ...
 18-193 1.21e-11

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: 63.05  E-value: 1.21e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723626132  18 TMVAHVLLLERPDGLALVDTGFGTEDLARRRRlgRPFLLTVRPDLDPAetaLAQVkarGFAPSDVTDIVLTHLDLDHAGG 97
Cdd:cd07728   40 ELRTDPILIQYQGKNYLIDAGIGNGKLTEKQK--RNFGVTEESSIEES---LAEL---GLTPEDIDYVLMTHLHFDHASG 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723626132  98 I----GD-----FPQARVHVHAREHAAATTPTAREKARYvagqWahgprwtphtegSDAWFGFAS-VTALDDDVLIIP-- 165
Cdd:cd07728  112 LtkvkGEqlvsvFPNATIYVSEIEWEEMRNPNIRSKNTY----W------------KENWEPIEDqVKTFSDEIEIVPgi 175

                        170       180       190
                 ....*....|....*....|....*....|..
gi 723626132 166 ----LPGHTRGHAgVAVRRDDGTWLLHAGDAF 193
Cdd:cd07728  176 tmihTGGHSDGHS-IIEIEQGGETAIHMADLM 206
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 63-197 2.72e-11

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: 60.76  E-value: 2.72e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723626132  63 DPAETALAQVKARGFA-PSDVTDIVLTHLDLDHAGGIGDF---PQARVHVHAREHAAATTPTARekARYVAGQWAHGPRW 138
Cdd:cd06262   26 DPGAGALEKILEAIEElGLKIKAILLTHGHFDHIGGLAELkeaPGAPVYIHEADAELLEDPELN--LAFFGGGPLPPPEP 103

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 723626132 139 TPHTEGSDawfgfaSVTALDDDVLIIPLPGHTRGHAGVAVRRDDgtwLLHAGDAFFHGG 197
Cdd:cd06262  104 DILLEDGD------TIELGGLELEVIHTPGHTPGSVCFYIEEEG---VLFTGDTLFAGS 153
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 20-111 1.13e-09

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: 56.73  E-value: 1.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723626132  20 VAHVLLLERPDGLALVDTGFGTEdlarrrrlgrpflltvrpdldpAETALAQVKARGFAPSDVTDIVLTHLDLDHAGGIG 99
Cdd:cd07726   15 RIASYLLDGEGRPALIDTGPSSS----------------------VPRLLAALEALGIAPEDVDYIILTHIHLDHAGGAG 72

                         90
                 ....*....|....*.
gi 723626132 100 D----FPQARVHVHAR 111
Cdd:cd07726   73 LlaeaLPNAKVYVHPR 88
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 29-222 3.03e-08

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


Pssm-ID: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 52.57  E-value: 3.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723626132  29 PDGLALVDTGFgTEDLARRrrlgrpflltvrpdldpaetALAQVKARGFAPsdVTDIVLTHLDLDHAGGIGDFPQARVHV 108
Cdd:cd16282   23 DDGVVVIDTGA-SPRLARA--------------------LLAAIRKVTDKP--VRYVVNTHYHGDHTLGNAAFADAGAPI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723626132 109 HA----REHAAATTPTAREKARYVAGQWAHGPRWTPHTEgsdawfGFASVTALD---DDVLIIPL-PGHTRGHAGVAVRR 180
Cdd:cd16282   80 IAhentREELAARGEAYLELMRRLGGDAMAGTELVLPDR------TFDDGLTLDlggRTVELIHLgPAHTPGDLVVWLPE 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 723626132 181 DDgtwLLHAGDAFFHGGQLDVP-ARCPASLTAFQRLMAVDNRR 222
Cdd:cd16282  154 EG---VLFAGDLVFNGRIPFLPdGSLAGWIAALDRLLALDATV 193
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 23-192 4.90e-08

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: 51.53  E-value: 4.90e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723626132  23 VLLLERPDGLALVDTGFGTEDlarrrrlgrpflltvrpdldPAETALAQVKARGFAPSDVTDIVLTHLDLDHAGGIGDFp 102
Cdd:cd07725   17 VYLLRDGDETTLIDTGLATEE--------------------DAEALWEGLKELGLKPSDIDRVLLTHHHPDHIGLAGKL- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723626132 103 qarvhvhaREHAAATtptarekaryVAgqwahGPRWTPHTEGSDawfgfasVTALDDDVLIIPLPGHTRGHAGVAVRRDD 182
Cdd:cd07725   76 --------QEKSGAT----------VY-----ILDVTPVKDGDK-------IDLGGLRLKVIETPGHTPGHIVLYDEDRR 125

                        170
                 ....*....|
gi 723626132 183 gtwLLHAGDA 192
Cdd:cd07725  126 ---ELFVGDA 132
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 21-209 3.72e-07

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: 49.16  E-value: 3.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723626132  21 AHVLLLERPDGLALVDTGFGTEDLARRRRLgrpflLTVRPDLdpaetalaqvkargfapsdvtdIVLTHLDLDHAGGIGD 100
Cdd:cd07712    9 VNIYLLRGRDRALLIDTGLGIGDLKEYVRT-----LTDLPLL----------------------VVATHGHFDHIGGLHE 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723626132 101 FPqaRVHVHAREHAAATTPTAREKARYVAGQWAH--GPRWTPHTEGsdawfgfaSVTALDDDVL-IIPLPGHTRGHagVA 177
Cdd:cd07712   62 FE--EVYVHPADAEILAAPDNFETLTWDAATYSVppAGPTLPLRDG--------DVIDLGDRQLeVIHTPGHTPGS--IA 129

                        170       180       190
                 ....*....|....*....|....*....|..
gi 723626132 178 VrRDDGTWLLHAGDAFFHGGQLDVPARCPASL 209
Cdd:cd07712  130 L-LDRANRLLFSGDVVYDGPLIMDLPHSDLDD 160
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 63-197 7.66e-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: 45.14  E-value: 7.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723626132  63 DPAETA--LAQVKARGFapsDVTDIVLTHLDLDHAGGIGD----FPQARVHVHAREHAAATTptarekaRYVAgqwahgp 136
Cdd:cd07723   26 DPGEAEpvLAALEKNGL---TLTAILTTHHHWDHTGGNAElkalFPDAPVYGPAEDRIPGLD-------HPVK------- 88

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 723626132 137 rwtphtEGSDAWFGFASVTALDddvliipLPGHTRGHagVAVRRDDGTWLLhAGDAFFHGG 197
Cdd:cd07723   89 ------DGDEIKLGGLEVKVLH-------TPGHTLGH--ICYYVPDEPALF-TGDTLFSGG 133
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 23-172 3.44e-05

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: 44.07  E-value: 3.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723626132  23 VLLLERPDGLALVDTGfgTEDLArrrrlgrpflltvrpdldpaETALAQVKARGFAPSDVTDIVLTHLDLDHAGGIGDFP 102
Cdd:cd07708   24 AYLIVTPQGNILIDGD--MEQNA--------------------PMIKANIKKLGFKFSDTKLILISHAHFDHAGGSAEIK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723626132 103 QarvhvharehaaattptaREKARYVAGQ-----WAHGPRWTPHTEGSD--AWFGFASVTALDDDVLII---------PL 166
Cdd:cd07708   82 K------------------QTGAKVMAGAedvslLLSGGSSDFHYANDSstYFPQSTVDRAVHDGERVTlggtvltahAT 143


                 ....*.
gi 723626132 167 PGHTRG 172
Cdd:cd07708  144 PGHTPG 149
YmaE-like_MBL-fold cd07727
uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold ...
 21-191 4.77e-05

uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold metallo hydrolase domain; Includes the uncharacterized Bacillus subtilis YmaE and Nostoc all1228 proteins.Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293813 [Multi-domain]  Cd Length: 181  Bit Score: 42.95  E-value: 4.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723626132  21 AHVLLLERPDGLALVDTGFGTEDLARRrrlgrpflltvrpdldpaetalaqVKARGfapsDVTDIVLTHLDldHAGGIGD 100
Cdd:cd07727   15 AASYLILRPEGNILVDSPRYSPPLAKR------------------------IEALG----GIRYIFLTHRD--DVADHAK 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723626132 101 F---PQARVHVHAREHAAATTPTAREkaryvagqwahgprwtpHTEGSDAWfgfasvtALDDDVLIIPLPGHTRGHAgVA 177
Cdd:cd07727   65 WaerFGAKRIIHEDDVNAVTRPDEVI-----------------VLWGGDPW-------ELDPDLTLIPVPGHTRGSV-VL 119

                        170
                 ....*....|....
gi 723626132 178 VRRDDGtwLLHAGD 191
Cdd:cd07727  120 LYKEKG--VLFTGD 131
SMB-1-like_MBL-B3 cd16313
SMB-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase ...
 63-172 8.27e-05

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: 42.93  E-value: 8.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723626132  63 DPAETALAQVKARGFAPSDVTDIVLTHLDLDHAGGIGDFPQ-ARVHVHArehAAATTPTARekaryvAGQwahGPRWTPH 141
Cdd:cd16313   42 KSPEQIAASIRQLGFKLEDVKYILSSHDHWDHAGGIAALQKlTGAQVLA---SPATVAVLR------SGS---MGKDDPQ 109

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 723626132 142 TEGSDAWFGFASVTALDDD--VLIIPL-------PGHTRG 172
Cdd:cd16313  110 FGGLTPMPPVASVRAVRDGevVKLGPLavtahatPGHTTG 149
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 158-194 3.44e-04

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


Pssm-ID: 293829 [Multi-domain]  Cd Length: 197  Bit Score: 40.59  E-value: 3.44e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 723626132 158 DDDVLIIPLPGHTRGHAGVAVrrDDGTwlLHAGDAFF 194
Cdd:cd07743  127 GVGLEIIPLPGHSFGQIGILT--PDGV--LFAGDALF 159
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 63-172 5.24e-04

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: 39.83  E-value: 5.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723626132  63 DPA---ETALAQVKARGFapsDVTDIVLTHLDLDHAGGIGDFP---QARVHVHAREhaaattptaREKARYvagqwaHGP 136
Cdd:cd16275   29 DPAwdiEKILAKLNELGL---TLTGILLTHSHFDHVNLVEPLLakyDAPVYMSKEE---------IDYYGF------RCP 90

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 723626132 137 RWTPHTEGSDAWFGfasvtalddDVLIIPL--PGHTRG 172
Cdd:cd16275   91 NLIPLEDGDTIKIG---------DTEITCLltPGHTPG 119
AIM-1-like_MBL-B3 cd16314
Pseudomonas Aeruginosa AIM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 69-117 1.29e-03

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: 39.10  E-value: 1.29e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 723626132  69 LAQVKARGFAPSDVTDIVLTHLDLDHAGGIGDFPQAR-VHVHAREHAAAT 117
Cdd:cd16314   48 EANIRALGFRPEDVRYIVSSHEHFDHAGGIARLQRATgAPVVAREPAATT 97
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 23-172 2.03e-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: 38.84  E-value: 2.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723626132  23 VLLLERPDGLALVDTGFgtedlarrrrlgrpflltvrpdldpAETA---LAQVKARGFAPSDVTDIVLTHLDLDHAGGIG 99
Cdd:cd16288   24 SYLITTPQGLILIDTGL-------------------------ESSApmiKANIRKLGFKPSDIKILLNSHAHLDHAGGLA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723626132 100 DFPQ---ARVHVHAREhaaattptarekaryvAGQWAHGPRWTPHTEgsDAWFGFASVTA-----------LDDDVLIIP 165
Cdd:cd16288   79 ALKKltgAKLMASAED----------------AALLASGGKSDFHYG--DDSLAFPPVKVdrvlkdgdrvtLGGTTLTAH 140


                 ....*...
gi 723626132 166 L-PGHTRG 172
Cdd:cd16288  141 LtPGHTRG 148
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
62-105 2.59e-03

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 38.25  E-value: 2.59e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 723626132  62 LDPAETALAQVKARGFAPSDVTDIVLTHLDLDHAGGIGDFPQAR 105
Cdd:COG1234   33 IDCGEGTQRQLLRAGLDPRDIDAIFITHLHGDHIAGLPGLLSTR 76
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 69-136 5.32e-03

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


Pssm-ID: 293867 [Multi-domain]  Cd Length: 252  Bit Score: 37.46  E-value: 5.32e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 723626132  69 LAQVKARGFAPSDVTDIVLTHLDLDHAGGIGDFpqarvhvhAREHAAATTPTAREKARYVAGQWAHGP 136
Cdd:cd16309   48 KDNIKKLGFDVKDVKYLLNTHAHFDHAGGLAEL--------KKATGAQLVASAADKPLLESGYVGSGD 107
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 70-172 9.39e-03

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: 36.66  E-value: 9.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723626132  70 AQVKARGFAPSDVTDIVLTHLDLDHAGGIGdfpQARVHVHAREHAAATTPTAREKARYVAGQWAHGPRWTPHTegSDAWF 149
Cdd:cd16310   49 QNIKALGFKLSDIKIIINTHAHYDHAGGLA---QLKADTGAKLWASRGDRPALEAGKHIGDNITQPAPFPAVK--VDRIL 123

                         90       100
                 ....*....|....*....|....
gi 723626132 150 GFASVTALDDDVLIIPL-PGHTRG 172
Cdd:cd16310  124 GDGEKIKLGDITLTATLtPGHTKG 147
 
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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