NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2075269700|ref|WP_219774839|]
View 

subclass B3 metallo-beta-lactamase [Polymorphobacter sp. PAMC 29334]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 581040)

MBL fold metallo-hydrolase is most likely a hydrolytic enzyme

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold super family cl23716
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 24-275 5.71e-130

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.


The actual alignment was detected with superfamily member cd16310:

Pssm-ID: 451500  Cd Length: 252  Bit Score: 369.09  E-value: 5.71e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700  24 WSEPTPPFRIVGNIYYVGTKGLAAYLIASPRGLILLDATLEGNVRQIEASIVSLGFRLRDIRILLNSHAHFDHAAGLARL 103
Cdd:cd16310     1 WTAPTEPFRIVDNIYYVGTKGIGSYLITSNHGAILLDGGLEENAALIEQNIKALGFKLSDIKIIINTHAHYDHAGGLAQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700 104 KRDTGATMLASAGDRGALESGTPPSVVDYGVVAFPPVKIDRVLVDGEPVRLGDIAMTPVITPGHTPGCTTWTMTAVERER 183
Cdd:cd16310    81 KADTGAKLWASRGDRPALEAGKHIGDNITQPAPFPAVKVDRILGDGEKIKLGDITLTATLTPGHTKGCTTWSTTVKENGR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700 184 RLRVVFPCSLTVAGNALIGNTGYPGIVADFRRSFVSLAALKADVVLPAHPDIAGVLARKARRDAGDLDAFIAPESLGHIV 263
Cdd:cd16310   161 PLRVVFPCSLSVAGNVLVGNKTYPTIVEDYRASFARLRAMKADIVLTSHPEVADLLARKAKQDAGQANAFVDPGELARIV 240

                         250
                  ....*....|..
gi 2075269700 264 ADAAKAFDVELA 275
Cdd:cd16310   241 DQSEAAFNKELA 252
 
Name Accession Description Interval E-value
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 24-275 5.71e-130

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: 369.09  E-value: 5.71e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700  24 WSEPTPPFRIVGNIYYVGTKGLAAYLIASPRGLILLDATLEGNVRQIEASIVSLGFRLRDIRILLNSHAHFDHAAGLARL 103
Cdd:cd16310     1 WTAPTEPFRIVDNIYYVGTKGIGSYLITSNHGAILLDGGLEENAALIEQNIKALGFKLSDIKIIINTHAHYDHAGGLAQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700 104 KRDTGATMLASAGDRGALESGTPPSVVDYGVVAFPPVKIDRVLVDGEPVRLGDIAMTPVITPGHTPGCTTWTMTAVERER 183
Cdd:cd16310    81 KADTGAKLWASRGDRPALEAGKHIGDNITQPAPFPAVKVDRILGDGEKIKLGDITLTATLTPGHTKGCTTWSTTVKENGR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700 184 RLRVVFPCSLTVAGNALIGNTGYPGIVADFRRSFVSLAALKADVVLPAHPDIAGVLARKARRDAGDLDAFIAPESLGHIV 263
Cdd:cd16310   161 PLRVVFPCSLSVAGNVLVGNKTYPTIVEDYRASFARLRAMKADIVLTSHPEVADLLARKAKQDAGQANAFVDPGELARIV 240

                         250
                  ....*....|..
gi 2075269700 264 ADAAKAFDVELA 275
Cdd:cd16310   241 DQSEAAFNKELA 252
B3_Acin_new1 NF033184
putative subclass B3 metallo-beta-lactamase; This is one of two families of putative ...
 17-274 3.25e-93

putative subclass B3 metallo-beta-lactamase; This is one of two families of putative metallo-beta-lactamases of subclass B3 that are restricted to the genus Acinetobacter, and undescribed as of January 2017.


Pssm-ID: 439394  Cd Length: 283  Bit Score: 276.99  E-value: 3.25e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700  17 KAPDApaWSEPTPPFRIVGNIYYVGTKGLAAYLIASPRGLILLDATLEGNVRQIEASIVSLGFRLRDIRILLNSHAHFDH 96
Cdd:NF033184   23 KLPDD--WTQNTQPFQITENIYYVGTHGLAAYLLASGHQALLIDTGLPENTEQIEQNIKQLGFKLSDVKIMVTSHAHWDH 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700  97 AAGLARLKRDTGATMLASAGDRGALESGTPPSVVDYGVVAFPPVKIDRVLVDGEPVRLGDIAMTPVITPGHTPGCTTWTM 176
Cdd:NF033184  101 VGALARIKQDTGAKLIAMQQDVKALEIGKPIGENTFQTIPFTPVKVDKVIHDGEVVKLGKFKLKATLTPGHTPGCTTWST 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700 177 TAVERERRLRVVFPCSLTVAGNALIGNTGYPGIVADFRRSFVSLAALKADVVLPAHPDIAGVLARKARRDAGDLDAFIAP 256
Cdd:NF033184  181 EVKSNGKNLNVVFPCSLSVAGNVLQNNHQYPNIVADYRKSFERLKNMKADIVLTSHPEVADVLGNKARKDAGQTNAFIQP 260

                         250
                  ....*....|....*...
gi 2075269700 257 ESLGHIVADAAKAFDVEL 274
Cdd:NF033184  261 EKLSSIVKDAEMAFEKSL 278
B3_Acin_new2 NF033185
putative subclass B3 metallo-beta-lactamase; This is one of two families of putative ...
 22-277 1.00e-79

putative subclass B3 metallo-beta-lactamase; This is one of two families of putative metallo-beta-lactamases of subclass B3 that are restricted to the genus Acinetobacter, and undescribed as of January 2017.


Pssm-ID: 380189  Cd Length: 285  Bit Score: 242.71  E-value: 1.00e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700  22 PA-WSEPTPPFRIVGNIYYVGTKGLAAYLIASPRGLILLDATLEGNVRQIEASIVSLGFRLRDIRILLNSHAHFDHAAGL 100
Cdd:NF033185   27 PAeWTQSIEPFRIAGSIYYVGTRGLGSYLLVSGSKAILIDTGLTENAALIEQNILKLGLNLSDVKIILVSHAHWDHVGAL 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700 101 ARLKRDTGATMLASAGDRGALESGTPPSVVDYGVVAFPPVKIDRVLVDGEPVRLGDIAMTPVITPGHTPGCTTWTMTAVE 180
Cdd:NF033185  107 AQIQKNTGAKVFAMDKEVTALTTGKPKGDNILQSFSYTPVKVDHILRDKEVIKMGKIHLKATLTPGHTPGCTTWSTSLKE 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700 181 RERRLRVVFPCSLTVAGNALIGNTGYPGIVADFRRSFVSLAALKADVVLPAHPDIAGVLARKARRDAGDLDAFIAPESLG 260
Cdd:NF033185  187 HGKTLNVVFPCSLSVAGNVLSNNQTYPGIVQDYQLSFHRLSKMPADIVLTSHPEAADLMNRKAKSEAGQLDAFTDRKLLE 266

                         250
                  ....*....|....*..
gi 2075269700 261 HIVADAAKAFDVELARQ 277
Cdd:NF033185  267 KIIKDAEFSFNQSLDNQ 283
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 47-232 2.48e-26

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: 102.85  E-value: 2.48e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700  47 AYLIASPRGLILLDATLEGN-VRQIEASIVSLGfrlRDIRILLNSHAHFDHAAGLARLKRDTGATMLASAGDRGALESGT 125
Cdd:COG0491    17 SYLIVGGDGAVLIDTGLGPAdAEALLAALAALG---LDIKAVLLTHLHPDHVGGLAALAEAFGAPVYAHAAEAEALEAPA 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700 126 PPSvvdygVVAFPPVKIDRVLVDGEPVRLGDIAMTPVITPGHTPGCTTWtmtaveRERRLRVVFpcsltvAGNAL----I 201
Cdd:COG0491    94 AGA-----LFGREPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSF------YVPDEKVLF------TGDALfsggV 156

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2075269700 202 GNTGYPGI-VADFRRSFVSLAALKADVVLPAH 232
Cdd:COG0491   157 GRPDLPDGdLAQWLASLERLLALPPDLVIPGH 188
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 47-232 2.98e-26

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: 101.48  E-value: 2.98e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700   47 AYLIASPRGLILLDaTLEGNVRQIEASIVSLGfrLRDIRILLNSHAHFDHAAGLARLKRDTGATMLASAGDRGALESGTP 126
Cdd:smart00849   2 SYLVRDDGGAILID-TGPGEAEDLLAELKKLG--PKKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELLKDLLA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700  127 PSVVDYGVvaFPPVKIDRVLVDGEPVRLGDIAMTPVITPGHTPGCTTWTMtavereRRLRVVFP-CSLTVAGNALIGNTG 205
Cdd:smart00849  79 LLGELGAE--AEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYL------PEGKILFTgDLLFAGGDGRTLVDG 150

                          170       180
                   ....*....|....*....|....*..
gi 2075269700  206 YPGIVADFRRSFVSLAALKADVVLPAH 232
Cdd:smart00849 151 GDAAASDALESLLKLLKLLPKLVVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
47-232 4.68e-19

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 82.80  E-value: 4.68e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700  47 AYLIASPRGLILLDaTLEGNVRQIEASIVSLGFRLRDIRILLNSHAHFDHAAGLARLKRDTGATMLASAGDRGAL---ES 123
Cdd:pfam00753   8 SYLIEGGGGAVLID-TGGSAEAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARELldeEL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700 124 GTPPSVVDYGVVAFPPVKIDRVLVDGEPVRLGDIAMTPVITPGHTPGCttwtmtAVERERRLRVVF-------PCSLTVA 196
Cdd:pfam00753  87 GLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGH------VVVYYGGGKVLFtgdllfaGEIGRLD 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2075269700 197 GNALIGNTGYPGIVADFRRSFVSLAALKADVVLPAH 232
Cdd:pfam00753 161 LPLGGLLVLHPSSAESSLESLLKLAKLKAAVIVPGH 196
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 74-170 1.16e-04

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 42.91  E-value: 1.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700  74 IVSLGFRLRDIRILLNSHAHFDHAAGLARLKRDTGATMLASAGDRGALESgtppsvvdygvvafppvkIDRVLVDGEPVR 153
Cdd:PLN02398  112 IDALSRKNRNLTYILNTHHHYDHTGGNLELKARYGAKVIGSAVDKDRIPG------------------IDIVLKDGDKWM 173

                          90
                  ....*....|....*..
gi 2075269700 154 LGDIAMTPVITPGHTPG 170
Cdd:PLN02398  174 FAGHEVLVMETPGHTRG 190
 
Name Accession Description Interval E-value
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 24-275 5.71e-130

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: 369.09  E-value: 5.71e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700  24 WSEPTPPFRIVGNIYYVGTKGLAAYLIASPRGLILLDATLEGNVRQIEASIVSLGFRLRDIRILLNSHAHFDHAAGLARL 103
Cdd:cd16310     1 WTAPTEPFRIVDNIYYVGTKGIGSYLITSNHGAILLDGGLEENAALIEQNIKALGFKLSDIKIIINTHAHYDHAGGLAQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700 104 KRDTGATMLASAGDRGALESGTPPSVVDYGVVAFPPVKIDRVLVDGEPVRLGDIAMTPVITPGHTPGCTTWTMTAVERER 183
Cdd:cd16310    81 KADTGAKLWASRGDRPALEAGKHIGDNITQPAPFPAVKVDRILGDGEKIKLGDITLTATLTPGHTKGCTTWSTTVKENGR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700 184 RLRVVFPCSLTVAGNALIGNTGYPGIVADFRRSFVSLAALKADVVLPAHPDIAGVLARKARRDAGDLDAFIAPESLGHIV 263
Cdd:cd16310   161 PLRVVFPCSLSVAGNVLVGNKTYPTIVEDYRASFARLRAMKADIVLTSHPEVADLLARKAKQDAGQANAFVDPGELARIV 240

                         250
                  ....*....|..
gi 2075269700 264 ADAAKAFDVELA 275
Cdd:cd16310   241 DQSEAAFNKELA 252
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 24-275 8.03e-108

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: 313.10  E-value: 8.03e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700  24 WSEPTPPFRIVGNIYYVGTKGLAAYLIASPRGLILLDATLEGNVRQIEASIVSLGFRLRDIRILLNSHAHFDHAAGLARL 103
Cdd:cd16288     1 WNAPFEPFRIAGNVYYVGTSGLASYLITTPQGLILIDTGLESSAPMIKANIRKLGFKPSDIKILLNSHAHLDHAGGLAAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700 104 KRDTGATMLASAGDRGALESGTpPSVVDYG--VVAFPPVKIDRVLVDGEPVRLGDIAMTPVITPGHTPGCTTWTMTAVER 181
Cdd:cd16288    81 KKLTGAKLMASAEDAALLASGG-KSDFHYGddSLAFPPVKVDRVLKDGDRVTLGGTTLTAHLTPGHTRGCTTWTMTVKDD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700 182 ERRLRVVFPCSLTVA-GNALIGNTGYPGIVADFRRSFVSLAALKADVVLPAHPDIAGVLARKARRDAGDLDAFIAPESLG 260
Cdd:cd16288   160 GKVYQVVFADSLTVNpGYKLVGNPTYPGIAEDYRHSFATLRALQCDIFLASHAEYFDLKEKRARLAAGQPNAFIDPEGYR 239

                         250
                  ....*....|....*
gi 2075269700 261 HIVADAAKAFDVELA 275
Cdd:cd16288   240 NFIEKAKADFEKQLA 254
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 24-275 2.22e-105

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: 306.72  E-value: 2.22e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700  24 WSEPTPPFRIVGNIYYVGTKGLAAYLIASPRGLILLDATLEGNVRQIEASIVSLGFRLRDIRILLNSHAHFDHAAGLARL 103
Cdd:cd16309     1 WNEPMEPFKLIGNIYYVGTAGLGVFLITTPEGHILIDGAMPQSTPLIKDNIKKLGFDVKDVKYLLNTHAHFDHAGGLAEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700 104 KRDTGATMLASAGDRGALESGtppsVVDYG---VVAFPPVKIDRVLVDGEPVRLGDIAMTPVITPGHTPGCTTWTMTAVE 180
Cdd:cd16309    81 KKATGAQLVASAADKPLLESG----YVGSGdtkNLQFPPVRVDRVIGDGDKVTLGGTTLTAHLTPGHSPGCTSWTTTVKD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700 181 RERRLR-VVFPCSLTVAGNALIGNTGYPGIVADFRRSFVSLAALKADVVLPAHPDIAGVLARKARRDAGDLDAFIAPESL 259
Cdd:cd16309   157 TAGPPReVLFFCSATVAGNQLVGPPTYPGIVDDYRATFAKARAMKADVFLANHPEFFGLVAKRARQSAGEPDAFVDAGEL 236

                         250
                  ....*....|....*.
gi 2075269700 260 GHIVADAAKAFDVELA 275
Cdd:cd16309   237 QRFNTKMEDDFEKALA 252
B3_Acin_new1 NF033184
putative subclass B3 metallo-beta-lactamase; This is one of two families of putative ...
 17-274 3.25e-93

putative subclass B3 metallo-beta-lactamase; This is one of two families of putative metallo-beta-lactamases of subclass B3 that are restricted to the genus Acinetobacter, and undescribed as of January 2017.


Pssm-ID: 439394  Cd Length: 283  Bit Score: 276.99  E-value: 3.25e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700  17 KAPDApaWSEPTPPFRIVGNIYYVGTKGLAAYLIASPRGLILLDATLEGNVRQIEASIVSLGFRLRDIRILLNSHAHFDH 96
Cdd:NF033184   23 KLPDD--WTQNTQPFQITENIYYVGTHGLAAYLLASGHQALLIDTGLPENTEQIEQNIKQLGFKLSDVKIMVTSHAHWDH 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700  97 AAGLARLKRDTGATMLASAGDRGALESGTPPSVVDYGVVAFPPVKIDRVLVDGEPVRLGDIAMTPVITPGHTPGCTTWTM 176
Cdd:NF033184  101 VGALARIKQDTGAKLIAMQQDVKALEIGKPIGENTFQTIPFTPVKVDKVIHDGEVVKLGKFKLKATLTPGHTPGCTTWST 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700 177 TAVERERRLRVVFPCSLTVAGNALIGNTGYPGIVADFRRSFVSLAALKADVVLPAHPDIAGVLARKARRDAGDLDAFIAP 256
Cdd:NF033184  181 EVKSNGKNLNVVFPCSLSVAGNVLQNNHQYPNIVADYRKSFERLKNMKADIVLTSHPEVADVLGNKARKDAGQTNAFIQP 260

                         250
                  ....*....|....*...
gi 2075269700 257 ESLGHIVADAAKAFDVEL 274
Cdd:NF033184  261 EKLSSIVKDAEMAFEKSL 278
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 24-268 1.90e-90

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: 268.64  E-value: 1.90e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700  24 WSEPTPPFRIVGNIYYVGTKGLAAYLIASPRGLILLDATLEGNVRQIEASIVSLGFRLRDIRILLNSHAHFDHAAGLARL 103
Cdd:cd07708     1 WPNPFPPFQIAGNTYYVGTDDLAAYLIVTPQGNILIDGDMEQNAPMIKANIKKLGFKFSDTKLILISHAHFDHAGGSAEI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700 104 KRDTGATMLASAGDRGALESGTPPSVVDYG--VVAFPPVKIDRVLVDGEPVRLGDIAMTPVITPGHTPGCTTWTMTAVER 181
Cdd:cd07708    81 KKQTGAKVMAGAEDVSLLLSGGSSDFHYANdsSTYFPQSTVDRAVHDGERVTLGGTVLTAHATPGHTPGCTTWTMTLKDH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700 182 ERRLRVVFPCSLTVA-GNALIGNTGYPGIVADFRRSFVSLAALKADVVLPAHPDIAGVLARKARRDAGDLDAFIAPESLG 260
Cdd:cd07708   161 GKQYQVVFADSLTVNpGYRLVDNPTYPKIVEDYRHSFAVVEAMRCDILLGPHPGVFDMKNKYVLLSKGQNNPFVDPGGCK 240


                  ....*...
gi 2075269700 261 HIVADAAK 268
Cdd:cd07708   241 AYAEAKAN 248
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 ...
 24-256 2.20e-81

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: 246.11  E-value: 2.20e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700  24 WSEPTPPFRIVGNIYYVGTKGLAAYLIASPRGLILLDATLEGNVRQIEASIVSLGFRLRDIRILLNSHAHFDHAAGLARL 103
Cdd:cd16290     1 WNQPQAPFRIHGNTYYVGTGGLSAVLITSPQGLILIDGALPQSAPQIEANIRALGFRLEDVKLILNSHAHFDHAGGIAAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700 104 KRDTGATMLASAGDRGALESGTP-PSVVDYGVV-AFPPVKIDRVLVDGEPVRLGDIAMTPVITPGHTPGCTTWTMTAVER 181
Cdd:cd16290    81 QRDSGATVAASPAGAAALRSGGVdPDDPQAGAAdPFPPVAKVRVVADGEVVKLGPLAVTAHATPGHTPGGTSWTWRSCEG 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2075269700 182 ERRLRVVFPCSLTV--AGNALIGNTGYPGIVADFRRSFVSLAALKADVVLPAHPDIAGVLARKARRDAG-DLDAFIAP 256
Cdd:cd16290   161 GRCLDIVYADSLTAvsADGFRFSDDAHPARVAAFRRSIATVAALPCDILISAHPDASGLWEKLARRAREpGPNPFIDP 238
FEZ-1-like_MBL-B3 cd16307
Fluoribacter gormanii FEZ-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 24-275 4.66e-81

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


Pssm-ID: 293865  Cd Length: 255  Bit Score: 245.05  E-value: 4.66e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700  24 WSEPTPPFRIVGNIYYVGTKGLAAYLIASPRGLILLDATLEGNVRQIEASIVSLGFRLRDIRILLNSHAHFDHAAGLARL 103
Cdd:cd16307     1 WTTPFPPFRIAGNLYYVGSRDLASYLITTPRGNILINSNLESSVPQIKASIEKLGFKFSDTKILLISHAHFDHAAGSALI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700 104 KRDTGATMLASAGDRGALESGTpPSVVDYG---VVAFPPVKIDRVLVDGEPVRLGDIAMTPVITPGHTPGCTTWTMTAVE 180
Cdd:cd16307    81 KRETHAKYMVMDGDVDVVESGG-KSDFFYGndpSTYFPPAHVDKVLHDGEQVELGGTVLTAHLTAGHTKGCTTWTMKVKD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700 181 RERRLRVVFPCSLTV-AGNALIGNTGYPGIVADFRRSFVSLAALKADVVLPAHPDIAGVLARKARRDAGDLDAFIAPESL 259
Cdd:cd16307   160 HGKTYDVVIVGSPNVnPGAKLVNNITYPGIAEDYAHTFAVLRSLPCDIFLGAHGGYFDLKNKYVRLQKGGANPFIDPEGY 239

                         250
                  ....*....|....*.
gi 2075269700 260 GHIVADAAKAFDVELA 275
Cdd:cd16307   240 KAYVAEKEQAFRTELE 255
B3_Acin_new2 NF033185
putative subclass B3 metallo-beta-lactamase; This is one of two families of putative ...
 22-277 1.00e-79

putative subclass B3 metallo-beta-lactamase; This is one of two families of putative metallo-beta-lactamases of subclass B3 that are restricted to the genus Acinetobacter, and undescribed as of January 2017.


Pssm-ID: 380189  Cd Length: 285  Bit Score: 242.71  E-value: 1.00e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700  22 PA-WSEPTPPFRIVGNIYYVGTKGLAAYLIASPRGLILLDATLEGNVRQIEASIVSLGFRLRDIRILLNSHAHFDHAAGL 100
Cdd:NF033185   27 PAeWTQSIEPFRIAGSIYYVGTRGLGSYLLVSGSKAILIDTGLTENAALIEQNILKLGLNLSDVKIILVSHAHWDHVGAL 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700 101 ARLKRDTGATMLASAGDRGALESGTPPSVVDYGVVAFPPVKIDRVLVDGEPVRLGDIAMTPVITPGHTPGCTTWTMTAVE 180
Cdd:NF033185  107 AQIQKNTGAKVFAMDKEVTALTTGKPKGDNILQSFSYTPVKVDHILRDKEVIKMGKIHLKATLTPGHTPGCTTWSTSLKE 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700 181 RERRLRVVFPCSLTVAGNALIGNTGYPGIVADFRRSFVSLAALKADVVLPAHPDIAGVLARKARRDAGDLDAFIAPESLG 260
Cdd:NF033185  187 HGKTLNVVFPCSLSVAGNVLSNNQTYPGIVQDYQLSFHRLSKMPADIVLTSHPEAADLMNRKAKSEAGQLDAFTDRKLLE 266

                         250
                  ....*....|....*..
gi 2075269700 261 HIVADAAKAFDVELARQ 277
Cdd:NF033185  267 KIIKDAEFSFNQSLDNQ 283
THIN-B-like_MBL-B3 cd16312
Janthinobacterium lividum THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 24-275 1.12e-70

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


Pssm-ID: 293870 [Multi-domain]  Cd Length: 258  Bit Score: 218.70  E-value: 1.12e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700  24 WSEPTPPFRIVGNIYYVGTKGLAAYLIASPRGLILLDATLEGNVRQIEASIVSLGFRLRDIRILLNSHAHFDHAAGLARL 103
Cdd:cd16312     1 WNQPVKPFNVFGNTWYVGTAGLSAVLVTSPQGHVLLDGALPQSAPLIIANIEALGFRIEDVKLILNSHAHWDHAGGIAAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700 104 KRDTGATMLASAGDRGALESGTP----PSVVDYGVVAFPPVKIDRVLVDGEPVRLGDIAMTPVITPGHTPGCTTWTMTAV 179
Cdd:cd16312    81 QKASGATVAASAHGAQVLQSGTNgkddPQYQAKPVVHVAKVAKVKEVGEGDTLKVGPLRLTAHMTPGHTPGGTTWTWTSC 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700 180 ERERRLRVVFPCSLT---VAGNALIGNTGYPGIVADFRRSFVSLAALKADVVLPAHPDIAGVLArKARRDAGDLDAFIAP 256
Cdd:cd16312   161 EGQRCLDVVYADSLNpysSGDFYYTGKGGYPDISASFRASIAKVAALPCDIIIAVHPGFTDVLD-KAKRRSGDTNPFIDA 239

                         250
                  ....*....|....*....
gi 2075269700 257 ESLGHIVADAAKAFDVELA 275
Cdd:cd16312   240 EACRAYAAGAAKSLEKRLA 258
SMB-1-like_MBL-B3 cd16313
SMB-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase ...
 24-275 9.15e-69

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: 213.96  E-value: 9.15e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700  24 WSEPTPPFRIVGNIYYVGTKGLAAYLIASPRGLILLDATLEGNVRQIEASIVSLGFRLRDIRILLNSHAHFDHAAGLARL 103
Cdd:cd16313     1 WNAPQEPFQIYGNTYYVGTGGISAVLITSPQGHILIDGGFPKSPEQIAASIRQLGFKLEDVKYILSSHDHWDHAGGIAAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700 104 KRDTGATMLASAGDRGALESGTPP-SVVDY-GVVAFPPVKIDRVLVDGEPVRLGDIAMTPVITPGHTPGCTTWTMTAVER 181
Cdd:cd16313    81 QKLTGAQVLASPATVAVLRSGSMGkDDPQFgGLTPMPPVASVRAVRDGEVVKLGPLAVTAHATPGHTTGGTSWTWQSCEQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700 182 ERRLRVVFPCSLTVAGNALIGNTGYPGIVADFRRSFVSLAALKADVVLPAHPDIAGVLARKARRDAGDLDAFIAPESLGH 261
Cdd:cd16313   161 GRCANMVFADSLTAVSADGYRFSAHPAVLADVEQSIAAVEKLACDILVSAHPEFSDMWTRVKRGAAEGNAAFIDGGGCRA 240

                         250
                  ....*....|....
gi 2075269700 262 IVADAAKAFDVELA 275
Cdd:cd16313   241 YAAKAREKLNKRLA 254
EVM-1-like_MBL-B3 cd16315
Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 24-274 1.43e-65

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: 205.28  E-value: 1.43e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700  24 WSEPTPPFRIVGNIYYVGTKGLAAYLIASPRGLILLDATLEGNVRQIEASIVSLGFRLRDIRILLNSHAHFDHAAGLARL 103
Cdd:cd16315     1 WDKPAPPARIFGNTYYVGTCGISAILITGDDGHVLIDSGTEEAAPLVLANIRKLGFDPKDVRWLLSSHEHFDHVGGLAAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700 104 KRDTGATMLASAGDRGALESGTP-PSVVDYGVV-AFPPVKIDRVLVDGEPVRLGDIAMTPVITPGHTPGCTTWTMTAVER 181
Cdd:cd16315    81 QRATGARVAASAAAAPVLESGKPaPDDPQAGLHePFPPVRVDRIVEDGDTVALGSLRLTAHATPGHTPGALSWTWRSCEG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700 182 ERRLRVVFPCSLTVAGNALIGNTGYPGIVADFRRSFVSLAALKADVVLPAHPDIAGVLARKARRdagdlDAFIAPESLGH 261
Cdd:cd16315   161 ADCRTIVYADSLSPVSADGYRFSDHPDYVAAYRAGLAKVAALPCDILLTPHPSASDMFERLSGG-----APLADPDACAA 235

                         250
                  ....*....|...
gi 2075269700 262 IVADAAKAFDVEL 274
Cdd:cd16315   236 YAAGAEKRLDERL 248
THIN-B2-like_MBL-B3 cd16311
Janthinobacterium lividum THIN-B2 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 24-275 4.64e-62

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: 196.75  E-value: 4.64e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700  24 WSEPTPPFRIVGNIYYVGTKGLAAYLIASPRGLILLDATLEGNVRQIEASIVSLGFRLRDIRILLNSHAHFDHAAGLARL 103
Cdd:cd16311     1 WNADQAPFRIFGNTYYVGVKGLSSVLVTSPQGHVLVDGGLPESAPKIIANIEALGFRIEDVKLILNSHGHIDHAGGLAEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700 104 KRDTGATMLASAGDRGALESG-TPPSVVDYGVV-AFPPVKIDRVLVDGEPVRLGDIAMTPVITPGHTPGCTTWTMTAVER 181
Cdd:cd16311    81 QRRSGALVAASPSAALDLASGeVGPDDPQYHALpKYPPVKDMRLARDGGQFNVGPVSLTAHATPGHTPGGLSWTWQSCDG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700 182 ERRLRVVFPCSLTVA---GNALIGNTGYPGIVADFRRSFVSLAALKADVVLPAHPDIAGVLARKARRDAGDLDAFIAPES 258
Cdd:cd16311   161 PRCLNMVYADSQNAVsrpGFKFSASSEYPNAVADLRRSFETLEKLPCDVLISAHPEASQLWERLEASDRSARPALVDREA 240

                         250
                  ....*....|....*..
gi 2075269700 259 LGHIVADAAKAFDVELA 275
Cdd:cd16311   241 CRRYASRAREALEKRIA 257
GOB1-like_MBL-B3 cd16308
Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; ...
 24-275 6.42e-62

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


Pssm-ID: 293866 [Multi-domain]  Cd Length: 254  Bit Score: 196.15  E-value: 6.42e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700  24 WSEPTPPFRIVGNIYYVGTKGLAAYLIASPRGLILLDATLEGNVRQIEASIVSLGFRLRDIRILLNSHAHFDHAAGLARL 103
Cdd:cd16308     1 WSQPYAPFRIAGNLYYVGTYDLACYLIVTPKGNILINTGLAESVPLIKKNIQALGFKFKDIKILLTTQAHYDHVGAMAAI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700 104 KRDTGATMLASAGDRGALESGtppSVVDYGV----VAFPPVKIDRVLVDGEPVRLGDIAMTPVITPGHTPGCTTWTMTAV 179
Cdd:cd16308    81 KQQTGAKMMVDEKDAKVLADG---GKSDYEMggygSTFAPVKADKLLHDGDTIKLGGTKLTLLHHPGHTKGSCSFLFDVK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700 180 ERERRLRVVFPCSLTV-AGNALIGNTGYPGIVADFRRSFVSLAALKADVVLPAHPDIAGVLARKARRDAGDLDAFIAPES 258
Cdd:cd16308   158 DEKRTYRVLIANMPTIlPDTKLSGMPGYPGIAKDYAYTFEAMKALSFDIWLASHASQFDLHQKHKPGAPYNPAAFADRAG 237

                         250
                  ....*....|....*..
gi 2075269700 259 LGHIVADAAKAFDVELA 275
Cdd:cd16308   238 YDKALAGLEKSYDKKIK 254
AIM-1-like_MBL-B3 cd16314
Pseudomonas Aeruginosa AIM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 24-241 3.38e-57

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: 184.32  E-value: 3.38e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700  24 WSEPTPPFRIVGNIYYVGTKGLAAYLIASPRGLILLDATLEGNVRQIEASIVSLGFRLRDIRILLNSHAHFDHAAGLARL 103
Cdd:cd16314     1 WDDPAPPRRIYGNTWYVGTCGISALLVTSDAGHILIDGGTDKAAPLIEANIRALGFRPEDVRYIVSSHEHFDHAGGIARL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700 104 KRDTGATMLASAGDRGALESGTPP-SVVDYGVVA-FPPVKIDRVLVDGEPVRLGDIAMTPVITPGHTPGCTTWTMTAVER 181
Cdd:cd16314    81 QRATGAPVVAREPAATTLERGRSDrSDPQFLVVEkFPPVASVQRIGDGEVLRVGPLALTAHATPGHTPGGTSWTWRSCEG 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700 182 ERRLRVVFPCSLTVAGNALIGNTGYPGIVADFRRSFVSLAALKADVVLPAHPDIAGVLAR 241
Cdd:cd16314   161 AVCRDMVYADSVTAISDDIYRYSDHPGMVAAFRNTLDTVAALPCDILVTPHPSASGLWER 220
L1_POM-1-like_MBL-B3 cd16289
Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-1 and related ...
 24-237 6.99e-54

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: 175.00  E-value: 6.99e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700  24 WSEPTPPFRIVGNIYYVGTKGLAAYLIASPRGLILLDATLEGNVRQIEASIVSLGFRLRDIRILLNSHAHFDHAAGLARL 103
Cdd:cd16289     1 WLQPMAPLQIADHTWYIGTESLTALLVKTPDGAVLLDGGMPQAADMLLDNMRALGVAPGDLKLILHSHAHADHAGPLAAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700 104 KRDTGATMLASAGDRGALESGTPPSVVDYGVVAFPPVKIDRVLVDGEPVRLGDIAMTPVITPGHTPGCTTWTMTAVERER 183
Cdd:cd16289    81 KRATGARVAANAESAVLLARGGSDDIHFGDGITFPPVQADRIVMDGEVVTLGGVTFTAHFTPGHTPGSTSWTWTDTRDGK 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2075269700 184 RLRVVFPCSLTVAGNALIGNTGYPGIVADFRRSFVSLAALKADVVLPAHPDIAG 237
Cdd:cd16289   161 PVRIAYADSLSAPGYQLLGNPRYPRIVEDYRRTFATVRALPCDVLLTPHPGASG 214
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 24-257 6.26e-42

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: 144.65  E-value: 6.26e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700  24 WSEPTPPFRIVGNIYYVGTKGLAAYLIASPRGLILLDaTLEGN--VRQIEASIVSLGFRLRDIRILLNSHAHFDHAAGLA 101
Cdd:cd16280     1 KKGYVEPFQVFDNLYYVGNKWVSAWAIDTGDGLILID-ALNNNeaADLIVDGLEKLGLDPADIKYILITHGHGDHYGGAA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700 102 RLKRDTGATMLASAgdRGALESGTPPSVVDyGVVAFPPVKIDRVLVDGEPVRLGDIAMTPVITPGHTPGCTTWTMTAVER 181
Cdd:cd16280    80 YLKDLYGAKVVMSE--ADWDMMEEPPEEGD-NPRWGPPPERDIVIKDGDTLTLGDTTITVYLTPGHTPGTLSLIFPVKDG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700 182 ERRLRVvfpcsltvagnALIGNTGYPGI-----VADFRRSFVSLAALK----ADVVLPAHPDIAGVLARKAR---RDAGD 249
Cdd:cd16280   157 GKTHRA-----------GLWGGTGLNTGpnlerREQYIASLERFKKIAeeagVDVFLSNHPFQDGSLEKREAlrnRKPGE 225


                  ....*...
gi 2075269700 250 LDAFIAPE 257
Cdd:cd16280   226 PNPFVDGQ 233
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 47-232 1.26e-29

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: 111.16  E-value: 1.26e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700  47 AYLIASPRGLILLDATLEGNVRQIEASIVSLGFRLRDI-RILLnSHAHFDHAAGLARLKRDTGATMLASAGDRGALESGT 125
Cdd:cd07721    13 AYLIEDDDGLTLIDTGLPGSAKRILKALRELGLSPKDIrRILL-THGHIDHIGSLAALKEAPGAPVYAHEREAPYLEGEK 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700 126 PPSVVDYGVVA--------FPPVKIDRVLVDGEPVRLGdIAMTPVITPGHTPGCttwtmTAVERERRlRVVFpcsltvAG 197
Cdd:cd07721    92 PYPPPVRLGLLgllspllpVKPVPVDRTLEDGDTLDLA-GGLRVIHTPGHTPGH-----ISLYLEED-GVLI------AG 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2075269700 198 NALIGNTGYPGIVADF--------RRSFVSLAALKADVVLPAH 232
Cdd:cd07721   159 DALVTVGGELVPPPPPftwdmeeaLESLRKLAELDPEVLAPGH 201
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 47-232 2.48e-26

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: 102.85  E-value: 2.48e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700  47 AYLIASPRGLILLDATLEGN-VRQIEASIVSLGfrlRDIRILLNSHAHFDHAAGLARLKRDTGATMLASAGDRGALESGT 125
Cdd:COG0491    17 SYLIVGGDGAVLIDTGLGPAdAEALLAALAALG---LDIKAVLLTHLHPDHVGGLAALAEAFGAPVYAHAAEAEALEAPA 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700 126 PPSvvdygVVAFPPVKIDRVLVDGEPVRLGDIAMTPVITPGHTPGCTTWtmtaveRERRLRVVFpcsltvAGNAL----I 201
Cdd:COG0491    94 AGA-----LFGREPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSF------YVPDEKVLF------TGDALfsggV 156

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2075269700 202 GNTGYPGI-VADFRRSFVSLAALKADVVLPAH 232
Cdd:COG0491   157 GRPDLPDGdLAQWLASLERLLALPPDLVIPGH 188
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 47-232 2.98e-26

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: 101.48  E-value: 2.98e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700   47 AYLIASPRGLILLDaTLEGNVRQIEASIVSLGfrLRDIRILLNSHAHFDHAAGLARLKRDTGATMLASAGDRGALESGTP 126
Cdd:smart00849   2 SYLVRDDGGAILID-TGPGEAEDLLAELKKLG--PKKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELLKDLLA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700  127 PSVVDYGVvaFPPVKIDRVLVDGEPVRLGDIAMTPVITPGHTPGCTTWTMtavereRRLRVVFP-CSLTVAGNALIGNTG 205
Cdd:smart00849  79 LLGELGAE--AEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYL------PEGKILFTgDLLFAGGDGRTLVDG 150

                          170       180
                   ....*....|....*....|....*..
gi 2075269700  206 YPGIVADFRRSFVSLAALKADVVLPAH 232
Cdd:smart00849 151 GDAAASDALESLLKLLKLLPKLVVPGH 177
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 47-232 3.42e-21

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: 88.50  E-value: 3.42e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700  47 AYLIASPRG-LILLDATLeGNVRQIEASIVSLGFRLRDIrilLNSHAHFDHAAGLARLKRDTGATMLASAGDRGALESGt 125
Cdd:cd06262    12 CYLVSDEEGeAILIDPGA-GALEKILEAIEELGLKIKAI---LLTHGHFDHIGGLAELKEAPGAPVYIHEADAELLEDP- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700 126 PPSVVDYGVVAFPPVKIDRVLVDGEPVRLGDIAMTPVITPGHTPGCTTWtmtaveRERRLRVVFpcsltvAGNAL----I 201
Cdd:cd06262    87 ELNLAFFGGGPLPPPEPDILLEDGDTIELGGLELEVIHTPGHTPGSVCF------YIEEEGVLF------TGDTLfagsI 154

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2075269700 202 GNTGYPGivADFRRSFVSLAALKA-----DVVLPAH 232
Cdd:cd06262   155 GRTDLPG--GDPEQLIESIKKLLLllpddTVVYPGH 188
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
47-232 4.68e-19

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 82.80  E-value: 4.68e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700  47 AYLIASPRGLILLDaTLEGNVRQIEASIVSLGFRLRDIRILLNSHAHFDHAAGLARLKRDTGATMLASAGDRGAL---ES 123
Cdd:pfam00753   8 SYLIEGGGGAVLID-TGGSAEAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARELldeEL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700 124 GTPPSVVDYGVVAFPPVKIDRVLVDGEPVRLGDIAMTPVITPGHTPGCttwtmtAVERERRLRVVF-------PCSLTVA 196
Cdd:pfam00753  87 GLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGH------VVVYYGGGKVLFtgdllfaGEIGRLD 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2075269700 197 GNALIGNTGYPGIVADFRRSFVSLAALKADVVLPAH 232
Cdd:pfam00753 161 LPLGGLLVLHPSSAESSLESLLKLAKLKAAVIVPGH 196
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 83-232 5.03e-15

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: 72.00  E-value: 5.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700  83 DIRILLNSHAHFDHAAGLARLKRDTGATMLASAGDRGALESGtPPSVVDYGVVAFPPVKIDRVLVDGEPVRLGDIAMTPV 162
Cdd:cd16322    46 TLLYILLTHAHFDHVGGVADLRRHPGAPVYLHPDDLPLYEAA-DLGAKAFGLGIEPLPPPDRLLEDGQTLTLGGLEFKVL 124

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2075269700 163 ITPGHTPGCTTWtmtAVERErrlRVVFPCSLTVAGNalIGNTGYPGIV-ADFRRSFVSLAALKADV-VLPAH 232
Cdd:cd16322   125 HTPGHSPGHVCF---YVEEE---GLLFSGDLLFQGS--IGRTDLPGGDpKAMAASLRRLLTLPDETrVFPGH 188
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 36-232 1.91e-13

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) 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: 67.56  E-value: 1.91e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700  36 NIYYVGTKGLAAYLIASPrglilLDatlEGNVRQIEASIVSLGFRLRDIrilLNSHAHFDHAAGLARLKRDTGATMLASA 115
Cdd:cd07743     9 NIGVYVFGDKEALLIDSG-----LD---EDAGRKIRKILEELGWKLKAI---INTHSHADHIGGNAYLQKKTGCKVYAPK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700 116 GDRGALE----------SGTPPSVVDYGVVAFPPVKIDRVLVDGEpVRLGDIAMTPVITPGHTPGcttwtMTAVERERrl 185
Cdd:cd07743    78 IEKAFIEnpllepsylgGAYPPKELRNKFLMAKPSKVDDIIEEGE-LELGGVGLEIIPLPGHSFG-----QIGILTPD-- 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2075269700 186 RVVFpcsltvAGNALIG-----NTGYPGI--VADFRRSFVSLAALKADVVLPAH 232
Cdd:cd07743   150 GVLF------AGDALFGeevleKYGIPFLydVEEQLETLEKLEELDADYYVPGH 197
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 38-174 6.57e-12

ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; MBL-fold metallo-hydrolase domain; Persulfide dioxygenase (PDO, also known as sulfur dioxygenase, SDO, EC 1.13.11.18) is a non-heme iron-dependent oxygenase which catalyzes the oxidation of glutathione persulfide to glutathione and persulfite in the mitochondria. Mutations in ethe1 (the human PDO gene) are responsible for a rare autosomal recessive metabolic disorder called ethylmalonic encephalopathy. Arabidopsis thaliana ETHE1 is essential for embryo and endosperm development. Bacterial ETHE1-type PDOs are also called Type 1 PDOs. Type II PDOs (also called PDOAs), are mainly proteobacterial. These enzymes belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293810 [Multi-domain]  Cd Length: 177  Bit Score: 62.80  E-value: 6.57e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700  38 YYVGTKGLAAYLIASPRGL--ILLDATLEgNVRQIEASIVSLGFRLRDIrilLNSHAHFDHAAGLARLKRDTGATMLASA 115
Cdd:cd07724     5 FFDPGLGTLSYLVGDPETGeaAVIDPVRD-SVDRYLDLAAELGLKITYV---LETHVHADHVSGARELAERTGAPIVIGE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2075269700 116 GDRGALEsgtppsvvdygvvafppvkiDRVLVDGEPVRLGDIAMTPVITPGHTPGCTTW 174
Cdd:cd07724    81 GAPASFF--------------------DRLLKDGDVLELGNLTLEVLHTPGHTPESVSY 119
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 47-241 2.24e-11

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


Pssm-ID: 293811 [Multi-domain]  Cd Length: 184  Bit Score: 61.55  E-value: 2.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700  47 AYLIASPRGLILLDATL--EGNVRQIEASIVSLGFRLRDI-RILLnSHAHFDHAAGLARLKRDTGATmlasagdrgales 123
Cdd:cd07725    17 VYLLRDGDETTLIDTGLatEEDAEALWEGLKELGLKPSDIdRVLL-THHHPDHIGLAGKLQEKSGAT------------- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700 124 gtppsvvdygvVAFPPVKIdrvLVDGEPVRLGDIAMTPVITPGHTPGcttWTMTAVERERRLrvvfpcsltVAGNALIGN 203
Cdd:cd07725    83 -----------VYILDVTP---VKDGDKIDLGGLRLKVIETPGHTPG---HIVLYDEDRREL---------FVGDAVLPK 136

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2075269700 204 -----TGYPGIV----ADFRRSFVSLAALKADVVLPAHPD-IAGVLAR 241
Cdd:cd07725   137 itpnvSLWAVRVedplGAYLESLDKLEKLDVDLAYPGHGGpIKDPKAR 184
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 38-169 2.81e-11

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: 61.74  E-value: 2.81e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700  38 YYVGTKGL-AAYLIASPRGLILLDATLEGNVRQIEASIVSLGFRLRDIRILLNSHAHFDHAAGLARL-KRDTGATMLASA 115
Cdd:cd07726     8 GFLGFPGRiASYLLDGEGRPALIDTGPSSSVPRLLAALEALGIAPEDVDYIILTHIHLDHAGGAGLLaEALPNAKVYVHP 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700 116 gdRGA--------LESGTppSVVdYGVVAFP------PVKIDRVLV--DGEPVRLGDIAMTPVITPGHTP 169
Cdd:cd07726    88 --RGArhlidpskLWASA--RAV-YGDEADRlggeilPVPEERVIVleDGETLDLGGRTLEVIDTPGHAP 152
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 47-232 3.51e-11

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: 61.85  E-value: 3.51e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700  47 AYLIASPRGLILLD--------------ATLEGNVRQIEASIVS----LGFRLRDIRILLNSHAHFDHAAGLARLKrdtG 108
Cdd:cd07729    34 AYLIEHPEGTILVDtgfhpdaaddpgglELAFPPGVTEEQTLEEqlarLGLDPEDIDYVILSHLHFDHAGGLDLFP---N 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700 109 ATMLASagdRGALESGTPPSVVDYGVvaFPPVKIDRVLVDGEPVRL--GDIAMTPVI----TPGHTPGcttwtMTAVere 182
Cdd:cd07729   111 ATIIVQ---RAELEYATGPDPLAAGY--YEDVLALDDDLPGGRVRLvdGDYDLFPGVtlipTPGHTPG-----HQSV--- 177

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2075269700 183 rRLRvvfpcslTVAGNALI-GNTGY----------PGIVADFRRSFVSLAALKA------DVVLPAH 232
Cdd:cd07729   178 -LVR-------LPEGTVLLaGDAAYtyenleegrpPGINYDPEAALASLERLKAlaeregARVIPGH 236
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 48-232 4.74e-11

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


Pssm-ID: 293836 [Multi-domain]  Cd Length: 185  Bit Score: 60.58  E-value: 4.74e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700  48 YLIASPRGLILLD--ATLEGNVRQIEASIVslGFRLRdiRILLnSHAHFDHAAGLARLKRDTGATMLASagdrgalesgt 125
Cdd:cd16278    21 YLLGAPDGVVVIDpgPDDPAHLDALLAALG--GGRVS--AILV-THTHRDHSPGAARLAERTGAPVRAF----------- 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700 126 PPSVVDYGVVAFPPvkiDRVLVDGEPVRLGDIAMTPVITPGHTPG--CTTWtmtavereRRLRVVFpCSLTVAGnaliGN 203
Cdd:cd16278    85 GPHRAGGQDTDFAP---DRPLADGEVIEGGGLRLTVLHTPGHTSDhlCFAL--------EDEGALF-TGDHVMG----WS 148

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2075269700 204 T---GYP-GIVADFRRSFVSLAALKADVVLPAH 232
Cdd:cd16278   149 TtviAPPdGDLGDYLASLERLLALDDRLLLPGH 181
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 48-232 2.40e-09

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: 55.71  E-value: 2.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700  48 YLIASPRGLILLDATL-EGNVRQIEASIVSLGFrlrdirILLNSHAHFDHAAGLARLKRdtgatMLASAGDRGALESGTP 126
Cdd:cd07712    12 YLLRGRDRALLIDTGLgIGDLKEYVRTLTDLPL------LVVATHGHFDHIGGLHEFEE-----VYVHPADAEILAAPDN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700 127 PS-----VVDYGVVAFPPVKIdrvLVDGEPVRLGDIAMTPVITPGHTPGCttwtMTAVERERRLrvvfpcsltvagnaLI 201
Cdd:cd07712    81 FEtltwdAATYSVPPAGPTLP---LRDGDVIDLGDRQLEVIHTPGHTPGS----IALLDRANRL--------------LF 139

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2075269700 202 -GNTGYPGIV---------ADFRRSFVSLAALK--ADVVLPAH 232
Cdd:cd07712   140 sGDVVYDGPLimdlphsdlDDYLASLEKLSKLPdeFDKVLPGH 182
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 47-170 5.27e-09

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: 54.39  E-value: 5.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700  47 AYLIASP--RGLILLDAtleGNVRQIEASIVSLGFRLRDIrilLNSHAHFDHAAGLARLKRDTG-ATMLASAGDRgales 123
Cdd:cd07723    11 IYLIVDEatGEAAVVDP---GEAEPVLAALEKNGLTLTAI---LTTHHHWDHTGGNAELKALFPdAPVYGPAEDR----- 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2075269700 124 gtppsvvdygvvaFPPVkiDRVLVDGEPVRLGDIAMTpVI-TPGHTPG 170
Cdd:cd07723    80 -------------IPGL--DHPVKDGDEIKLGGLEVK-VLhTPGHTLG 111
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 65-170 4.09e-08

Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase domain; This subgroup includes Salmonella enterica serovar typhimurium YcbL which has type II hydroxyacylglutathione hydrolase (EC 3.1.2.6, also known as glyoxalase II) activity, and has a single metal ion binding site, and Thermus thermophilus TTHA1623 which does not have GLX2 activity and has two metal ion binding sites with a glyoxalase II-type metal coordination. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293823 [Multi-domain]  Cd Length: 190  Bit Score: 52.17  E-value: 4.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700  65 GNVRQIEASIVSLGFRLrdIRILLnSHAHFDHAAGLARLKRDTGATMLAS-AGDRGALESgTPPSVVDYGVVAFPPVKID 143
Cdd:cd07737    31 GDADKILQAIEDLGLTL--KKILL-THGHLDHVGGAAELAEHYGVPIIGPhKEDKFLLEN-LPEQSQMFGFPPAEAFTPD 106

                          90       100
                  ....*....|....*....|....*..
gi 2075269700 144 RVLVDGEPVRLGDIAMTPVITPGHTPG 170
Cdd:cd07737   107 RWLEEGDTVTVGNLTLEVLHCPGHTPG 133
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 66-172 8.01e-08

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: 51.00  E-value: 8.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700  66 NVRQIEASIVSLGFRLRDIriLLnSHAHFDHAAGLARLKRDTGATMLASAGDRGAlesgtppsvvdYGvvaFPPVKIdRV 145
Cdd:cd16275    33 DIEKILAKLNELGLTLTGI--LL-THSHFDHVNLVEPLLAKYDAPVYMSKEEIDY-----------YG---FRCPNL-IP 94

                          90       100
                  ....*....|....*....|....*..
gi 2075269700 146 LVDGEPVRLGDIAMTPVITPGHTPGCT 172
Cdd:cd16275    95 LEDGDTIKIGDTEITCLLTPGHTPGSM 121
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 46-172 2.64e-06

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 47.58  E-value: 2.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700  46 AAYLIASPRGLILLDATLEGnvRQIEASivsLGFRLRDIRILLNSHAHFDHAAG---LARLKRDTGATMLASAGDRGALE 122
Cdd:COG1235    36 SSILVEADGTRLLIDAGPDL--REQLLR---LGLDPSKIDAILLTHEHADHIAGlddLRPRYGPNPIPVYATPGTLEALE 110

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2075269700 123 SGtppsvVDYGVVAFPPVKIDRVLVDGEPVRLGDIAMTPVITPGHTPGCT 172
Cdd:COG1235   111 RR-----FPYLFAPYPGKLEFHEIEPGEPFEIGGLTVTPFPVPHDAGDPV 155
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 47-170 3.74e-05

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: 44.08  E-value: 3.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700  47 AYLIASPRGLILLDA----TLEGNVRQIEASIVSLGFRLRDIRILLNSHAHFDHAAGL---ARLKRDTGATMLASAGDRG 119
Cdd:cd07720    51 AFLVRTGGRLILVDTgaggLFGPTAGKLLANLAAAGIDPEDIDDVLLTHLHPDHIGGLvdaGGKPVFPNAEVHVSEAEWD 130

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2075269700 120 ALESGTPPSVVDYGVVAFPPVKIDRV--------LVDGEPVrLGDIamTPVITPGHTPG 170
Cdd:cd07720   131 FWLDDANAAKAPEGAKRFFDAARDRLrpyaaagrFEDGDEV-LPGI--TAVPAPGHTPG 186
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 41-165 4.08e-05

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: 42.64  E-value: 4.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700  41 GTKGLAAYlIASPRGLILLDATLEGnvRQIEASIVSLGFRLRDIRILLNSHAHFDHAAGLARLKRDTGATMLASAGDRGA 120
Cdd:cd07733     6 GSKGNCTY-LETEDGKLLIDAGLSG--RKITGRLAEIGRDPEDIDAILVTHEHADHIKGLGVLARKYNVPIYATAGTLRA 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2075269700 121 LESGTPPSvvdygvvafpPVKIDRVLVDGEPVRLGDIAMTPVITP 165
Cdd:cd07733    83 MERKVGLI----------DVDQKQIFEPGETFSIGDFDVESFGVS 117
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 47-232 6.96e-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: 6.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700  47 AYLIASPRGLILLDATL-EGNVRQIEASIVSLGFRLrdIRILLNSHAHFDHAAGLARLKrDTGATMLASAGDRGALESGT 125
Cdd:cd16282    17 IGFIVGDDGVVVIDTGAsPRLARALLAAIRKVTDKP--VRYVVNTHYHGDHTLGNAAFA-DAGAPIIAHENTREELAARG 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700 126 PPSVVDYGVVA------FPPVKIDRVLVDGEPVRLGDIAMTpVIT--PGHTPGcttwtMTAVERERRlRVVFpcsltvAG 197
Cdd:cd16282    94 EAYLELMRRLGgdamagTELVLPDRTFDDGLTLDLGGRTVE-LIHlgPAHTPG-----DLVVWLPEE-GVLF------AG 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2075269700 198 NAL-IGNTGYP--GIVADFRRSFVSLAALKADVVLPAH 232
Cdd:cd16282   161 DLVfNGRIPFLpdGSLAGWIAALDRLLALDATVVVPGH 198
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 74-170 1.16e-04

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 42.91  E-value: 1.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700  74 IVSLGFRLRDIRILLNSHAHFDHAAGLARLKRDTGATMLASAGDRGALESgtppsvvdygvvafppvkIDRVLVDGEPVR 153
Cdd:PLN02398  112 IDALSRKNRNLTYILNTHHHYDHTGGNLELKARYGAKVIGSAVDKDRIPG------------------IDIVLKDGDKWM 173

                          90
                  ....*....|....*..
gi 2075269700 154 LGDIAMTPVITPGHTPG 170
Cdd:PLN02398  174 FAGHEVLVMETPGHTRG 190
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 57-167 1.88e-04

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


Pssm-ID: 432732 [Multi-domain]  Cd Length: 196  Bit Score: 41.53  E-value: 1.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700  57 ILLDATLeGNVRQIEASIVSLGFRLRDIRILLNSHAHFDHAAGLARLKRDTGATMLASAGDRGALESGTPPSVVD--YGV 134
Cdd:pfam12706   3 ILIDPGP-DLRQQALPALQPGRLRDDPIDAVLLTHDHYDHLAGLLDLREGRPRPLYAPLGVLAHLRRNFPYLFLLehYGV 81

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2075269700 135 VAFPpvkidrvLVDGEPVRLGDIAMTPVITPGH 167
Cdd:pfam12706  82 RVHE-------IDWGESFTVGDGGLTVTATPAR 107
YtnP-like_MBL-fold cd07728
Bacillus subtilis YtnP and related proteins; MBL-fold metallo hydrolase domain; Bacillus ...
 70-107 3.67e-04

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: 41.09  E-value: 3.67e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2075269700  70 IEASIVSLGFRLRDIRILLNSHAHFDHAAGLARLKRDT 107
Cdd:cd07728    82 IEESLAELGLTPEDIDYVLMTHLHFDHASGLTKVKGEQ 119
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 44-103 5.31e-04

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: 40.68  E-value: 5.31e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2075269700  44 GLAAYlIASPRGLILLDA----TLEGNVRQieasivsLGFRLRDIRILLNSHAHFDHAAGLARL 103
Cdd:cd07713    20 GLSLL-IETEGKKILFDTgqsgVLLHNAKK-------LGIDLSDIDAVVLSHGHYDHTGGLKAL 75
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 48-168 6.31e-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: 39.82  E-value: 6.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700  48 YLIASPRGLILLDATlEGNVRQIE----ASIVSLGFRLRDIrILlnSHAHFDHAAGLARLkrdtgatmlasagdRGALES 123
Cdd:cd07722    21 YLVGTGKRRILIDTG-EGRPSYIPllksVLDSEGNATISDI-LL--THWHHDHVGGLPDV--------------LDLLRG 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2075269700 124 GTP-----PSVVDYGVVAFPPVKIDRvLVDGEPVRLGDIAMTPVITPGHT 168
Cdd:cd07722    83 PSPrvykfPRPEEDEDPDEDGGDIHD-LQDGQVFKVEGATLRVIHTPGHT 131
YmaE-like_MBL-fold cd07727
uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold ...
 36-172 7.10e-04

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


Pssm-ID: 293813 [Multi-domain]  Cd Length: 181  Bit Score: 39.49  E-value: 7.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700  36 NIYYVGTK-----GLAAYLIASPRGLILLDAT--LEGNVRQIEAsivslgfrLRDIRILLNSHAhfDHAAGLARLKRDTG 108
Cdd:cd07727     1 GVYYCGFHseksfGAASYLILRPEGNILVDSPrySPPLAKRIEA--------LGGIRYIFLTHR--DDVADHAKWAERFG 70

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2075269700 109 ATMLASAGDRGALESGTPPSVVDygvvafppvkidrvlvDGEPVRLGDiAMTPVITPGHTPGCT 172
Cdd:cd07727    71 AKRIIHEDDVNAVTRPDEVIVLW----------------GGDPWELDP-DLTLIPVPGHTRGSV 117
metallo-hydrolase-like_MBL-fold cd07742
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 67-101 7.11e-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: 40.30  E-value: 7.11e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2075269700  67 VRQIEAsivsLGFRLRDIR-ILLnSHAHFDHAAGLA 101
Cdd:cd07742    68 VRQIEA----LGFDPSDVRhIVL-THLDLDHAGGLA 98
PDE1 COG5212
cAMP phosphodiesterase [Signal transduction mechanisms];
41-101 9.39e-04

cAMP phosphodiesterase [Signal transduction mechanisms];


Pssm-ID: 444071 [Multi-domain]  Cd Length: 300  Bit Score: 39.94  E-value: 9.39e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2075269700  41 GTKG------LAAYLIASP--RGLILLDA-TLEGNV---RQIEASIVSLGFRLRDIRILLNSHAHFDHAAGLA 101
Cdd:COG5212    18 GCSGgisdgnLTTYLLRPLgsDDYVLLDAgTVVSGLelaEQKGAFKGRQGYVLEHIKGYLISHAHLDHIAGLP 90
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 37-145 9.67e-04

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 39.52  E-value: 9.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700  37 IYYVGTkglAAYLIASPRGLILLDATLEGNVRQIEASIVSLgFRLRDIRILLNSHAHFDHA--AGLARLKRdTGATMLAS 114
Cdd:COG2220     6 ITWLGH---ATFLIETGGKRILIDPVFSGRASPVNPLPLDP-EDLPKIDAVLVTHDHYDHLddATLRALKR-TGATVVAP 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2075269700 115 AGDRGALESGTPPSVV---DYGVVAFPPVKIDRV 145
Cdd:COG2220    81 LGVAAWLRAWGFPRVTeldWGESVELGGLTVTAV 114
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
39-116 1.98e-03

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


Pssm-ID: 440850  Cd Length: 273  Bit Score: 39.10  E-value: 1.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700  39 YVGTKGLAA-----YLIASPRGLILLDA----TLEGNVRQieasivsLGFRLRDIRILLNSHAHFDHAAGLAR-LKRDTG 108
Cdd:COG1237    11 TAGDEGLLAehglsALIETEGKRILFDTgqsdVLLKNAEK-------LGIDLSDIDAVVLSHGHYDHTGGLPAlLELNPK 83


                  ....*...
gi 2075269700 109 ATMLASAG 116
Cdd:COG1237    84 APVYAHPD 91
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 42-101 2.51e-03

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


Pssm-ID: 293830 [Multi-domain]  Cd Length: 180  Bit Score: 38.01  E-value: 2.51e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700  42 TKGLAAYLIASPRGLILLDATlEGNVRQIEASIVSLgfrLRDIRILLnSHAHFDHAAGLA 101
Cdd:cd16272    14 TRNTSSYLLETGGTRILLDCG-EGTVYRLLKAGVDP---DKLDAIFL-SHFHLDHIGGLP 68
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
44-171 5.39e-03

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 37.48  E-value: 5.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700  44 GLAAYLIASPRGLILLDATlEGNVRQIEASivslGFRLRDIRILLNSHAHFDHAAGLARL-------KRDTGATMLASAG 116
Cdd:COG1234    18 ATSSYLLEAGGERLLIDCG-EGTQRQLLRA----GLDPRDIDAIFITHLHGDHIAGLPGLlstrslaGREKPLTIYGPPG 92

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2075269700 117 DRGALES--GTPPSVVDYgvvafpPVKIdRVLVDGEPVRLGDIAMTPVITPgHTPGC 171
Cdd:COG1234    93 TKEFLEAllKASGTDLDF------PLEF-HEIEPGEVFEIGGFTVTAFPLD-HPVPA 141
metallo-hydrolase-like_MBL-fold cd16281
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 70-112 5.66e-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: 293839  Cd Length: 252  Bit Score: 37.47  E-value: 5.66e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2075269700  70 IEASIVSLGFRLRDIRILLNSHAHFDHAAGLARLKRDTGATML 112
Cdd:cd16281    81 LLKSLARLGLSPEDITDVILTHLHFDHCGGATRADDDGLVELL 123
class_II_PDE_MBL-fold cd07735
class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium ...
 44-100 7.29e-03

class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium discoideum PDE1 and PDE7, and related proteins; MBL-fold metallo-hydrolase domain; Cyclic nucleotide phosphodiesterases (PDEs) decompose the second messengers cyclic adenosine and guanosine 3',5'-monophosphate (cAMP and cGMP, respectively). Saccharomyces cerevisiae PDE1 and Dictyostelium discoideum PDE1 and PDE7, have dual cAMP/cGMP specificity. 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: 293821  Cd Length: 259  Bit Score: 37.19  E-value: 7.29e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2075269700  44 GLAAYLI--ASPRGLILLDA-------TLEGNVRQIEASIVSLGFRLRD-IR-ILLnSHAHFDHAAGL 100
Cdd:cd07735    16 NTSSFLLdpAGSDGDILLDAgtgvgalSLEEMFNDILFPSQKAAYELYQrIRhYLI-THAHLDHIAGL 82
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 77-170 9.50e-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. Some members of this subgroup are annotated as GumP protein.


Pssm-ID: 293816 [Multi-domain]  Cd Length: 250  Bit Score: 36.86  E-value: 9.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269700  77 LGFRLRDIRILLNSHAHFDHAAGLARLkrdTGATMLASAGDRGALESGTPPSVVDYGVVA--FPPVKIDRVLVDGEPVRL 154
Cdd:cd07730    77 GGIDPEDIDAVILSHLHWDHIGGLSDF---PNARLIVGPGAKEALRPPGYPSGFLPELLPsdFEGRLVRWEEDDFLWVPL 153

                          90       100
                  ....*....|....*....|....*....
gi 2075269700 155 ----------GD---IAmtpVITPGHTPG 170
Cdd:cd07730   154 gpfpraldlfGDgslYL---VDLPGHAPG 179
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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