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Conserved domains on  [gi|446436140|ref|WP_000513995|]
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MULTISPECIES: FprA family A-type flavoprotein [Bacillus cereus group]

Protein Classification

FprA family A-type flavoprotein( domain architecture ID 11417996)

FprA family A-type flavoprotein contains an MBL fold metallo-hydrolase domain having a binuclear iron center, and a flavodoxin-like domain containing one FMN moiety; similar to Desulfovibrio gigas rubredoxin-oxygen oxidoreductase, which catalyzes the four-electron reduction of one oxygen molecule to two water molecules

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NorV COG0426
Flavorubredoxin [Energy production and conversion];
5-403 3.51e-150

Flavorubredoxin [Energy production and conversion];


:

Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 430.79  E-value: 3.51e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140   5 IQLTKDIYWVGKVDNREVPFHRLI-LAKGTTYNAYLLKTEKPTVIDTVDIEFGREFVESLSKLIDPQEIQYIVVNHTEPD 83
Cdd:COG0426    3 VEIAHGVYWVGVLDWDRRLFEGEYpTPRGTTYNSYLIVDEKTALIDTVGESFFEEFLENLSKVIDPKKIDYIIVNHQEPD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140  84 HSGGLAALASRATNATIVCTEIAVPEIQEMYKLHNRKFLVVKDGDTLDIGGKTLKFKETPYLHTEETMITYCVEDKILFP 163
Cdd:COG0426   83 HSGSLPELLELAPNAKIVCSKKAARFLPHFYGIPDFRFIVVKEGDTLDLGGHTLQFIPAPMLHWPDTMFTYDPEDKILFS 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140 164 CDIFSTHIANDEIFSDKANVDITEDFIGYYNAIIHPHRRYVRTLIEALKDLDVQMIAPSHGYILRQDIQKYIKLYADMSR 243
Cdd:COG0426  163 GDAFGSHGASDELFDDEVDEHLEEEARRYYANIMMPFSKQVLKALKKVRGLDIDMIAPSHGPIWRGNPKEILDWYRKWSS 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140 244 DTnQDKKVTIVYTTIKNNTKKVANIIKETLEADNIHVTVFNADKSKKLEVLKSIQEADAVFIGSSTRYADMIGNLEEILK 323
Cdd:COG0426  243 YQ-PEKKVVIVYASMYGNTEKMAEAIAEGLTEEGVKVKLYDLEKTDPSEIITEIFDAKGIVIGSPTYNGGAFPPIADLLG 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140 324 EMTEMNLEGKIAASFGSYGWSGEAIEVIQDYLNETNMNVqstskvikstgmthVEFPIRIRFSPKDEGKVKKIQHATTFV 403
Cdd:COG0426  322 YLKGLAPKNKLAGAFGSYGWSGEAVKLLEEKLEDAGFEV--------------VFEPLRVKFKPTEEDLKKCEELGTDLA 387
 
Name Accession Description Interval E-value
NorV COG0426
Flavorubredoxin [Energy production and conversion];
5-403 3.51e-150

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 430.79  E-value: 3.51e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140   5 IQLTKDIYWVGKVDNREVPFHRLI-LAKGTTYNAYLLKTEKPTVIDTVDIEFGREFVESLSKLIDPQEIQYIVVNHTEPD 83
Cdd:COG0426    3 VEIAHGVYWVGVLDWDRRLFEGEYpTPRGTTYNSYLIVDEKTALIDTVGESFFEEFLENLSKVIDPKKIDYIIVNHQEPD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140  84 HSGGLAALASRATNATIVCTEIAVPEIQEMYKLHNRKFLVVKDGDTLDIGGKTLKFKETPYLHTEETMITYCVEDKILFP 163
Cdd:COG0426   83 HSGSLPELLELAPNAKIVCSKKAARFLPHFYGIPDFRFIVVKEGDTLDLGGHTLQFIPAPMLHWPDTMFTYDPEDKILFS 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140 164 CDIFSTHIANDEIFSDKANVDITEDFIGYYNAIIHPHRRYVRTLIEALKDLDVQMIAPSHGYILRQDIQKYIKLYADMSR 243
Cdd:COG0426  163 GDAFGSHGASDELFDDEVDEHLEEEARRYYANIMMPFSKQVLKALKKVRGLDIDMIAPSHGPIWRGNPKEILDWYRKWSS 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140 244 DTnQDKKVTIVYTTIKNNTKKVANIIKETLEADNIHVTVFNADKSKKLEVLKSIQEADAVFIGSSTRYADMIGNLEEILK 323
Cdd:COG0426  243 YQ-PEKKVVIVYASMYGNTEKMAEAIAEGLTEEGVKVKLYDLEKTDPSEIITEIFDAKGIVIGSPTYNGGAFPPIADLLG 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140 324 EMTEMNLEGKIAASFGSYGWSGEAIEVIQDYLNETNMNVqstskvikstgmthVEFPIRIRFSPKDEGKVKKIQHATTFV 403
Cdd:COG0426  322 YLKGLAPKNKLAGAFGSYGWSGEAVKLLEEKLEDAGFEV--------------VFEPLRVKFKPTEEDLKKCEELGTDLA 387
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 5-242 4.06e-105

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


Pssm-ID: 293795 [Multi-domain]  Cd Length: 238  Bit Score: 310.19  E-value: 4.06e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140   5 IQLTKDIYWVGKVDNREVPFHRLI-LAKGTTYNAYLLKTEKPTVIDTVDIEFGREFVESLSKLIDPQEIQYIVVNHTEPD 83
Cdd:cd07709    1 VEIADDIYWVGVNDWDLRLFEGEYpTPRGTSYNSYLIKDEKTALIDTVKEPFFDEFLENLEEVIDPRKIDYIVVNHQEPD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140  84 HSGGLAALASRATNATIVCTEIAVPEIQEMYKLHNRKFLVVKDGDTLDIGGKTLKFKETPYLHTEETMITYCVEDKILFP 163
Cdd:cd07709   81 HSGSLPELLELAPNAKIVCSKKAARFLKHFYPGIDERFVVVKDGDTLDLGKHTLKFIPAPMLHWPDTMVTYDPEDKILFS 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446436140 164 CDIFSTHIANDEIFSDKANvDITEDFIGYYNAIIHPHRRYVRTLIEALKDLDVQMIAPSHGYILRQDIQKYIKLYADMS 242
Cdd:cd07709  161 GDAFGAHGASGELFDDEVE-DYLEEARRYYANIMGPFSKQVRKALEKLEALDIKMIAPSHGPIWRKDPGEIIDLYRDWS 238
PRK11921 PRK11921
anaerobic nitric oxide reductase flavorubredoxin;
6-403 4.78e-90

anaerobic nitric oxide reductase flavorubredoxin;


Pssm-ID: 237023 [Multi-domain]  Cd Length: 394  Bit Score: 277.34  E-value: 4.78e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140   6 QLTKDIYWVGKVDNREVPFH--RLILAKGTTYNAYLLKTEKPTVIDTVDIEFGREFVESLSKLIDPQEIQYIVVNHTEPD 83
Cdd:PRK11921   2 KINDNVTWVGKIDWELRKFHgeEYSTHRGSSYNSYLIKDEKTVLIDTVWQPFAKEFVENLKKEIDLDKIDYIVANHGEID 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140  84 HSGGLAALASRATNATIVCTEIAVPEIQEMYKlHNRKFLVVKDGDTLDIGGKTLKFKETPYLHTEETMITYCVEDKILFP 163
Cdd:PRK11921  82 HSGALPELMKEIPDTPIYCTKNGAKSLKGHYH-QDWNFVVVKTGDRLEIGSNELIFIEAPMLHWPDSMFTYLTGDNILFS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140 164 CDIFSTHIANDEIFSDKanVDITEDF---IGYYNAIIHPHRRYVRTLIEALKDLD--VQMIAPSHGYILRQD----IQKY 234
Cdd:PRK11921 161 NDAFGQHYASELMYNDL--VDQGELYqeaIKYYANILTPFSPLVIKKIEEILSLNlpVDMICPSHGVIWRDNplqiVEKY 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140 235 IKLYADMsrdtnQDKKVTIVYTTIKNNTKKVANIIKETLEADNIHVTV--FNADKSKKLEVLKSIQEADAVFIGSSTRYA 312
Cdd:PRK11921 239 LEWAANY-----QENQVTILYDTMWNSTRRMAEAIAEGIKKANKDVTVklYNSAKSDKNDIITEVFKSKAILVGSSTINR 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140 313 DMIGNLEEILKEMTEMNLEGKIAASFGSYGWSGEAIEVIQDYLnetnmnvqstskviKSTGMTHVEFPIRIRFSPKDEGK 392
Cdd:PRK11921 314 GILSSTAAILEEIKGLGFKNKKAAAFGSYGWSGESVKIITERL--------------KKAGFEIVNDGIRELWNPDDEAL 379

                        410
                 ....*....|.
gi 446436140 393 VKKIQHATTFV 403
Cdd:PRK11921 380 DRCRSFGENFA 390
ODP pfam19583
ODP family beta lactamase; The ODP (Oxygen-binding Di-iron Protein) domain is a distinct ...
 60-224 3.10e-23

ODP family beta lactamase; The ODP (Oxygen-binding Di-iron Protein) domain is a distinct member of the metallo-beta-lactamase superfamily recruited to various bacterial and archaeal signal transduction pathways, including chemotaxis, to function as oxygen and iron sensors (1). ODP was shown to act as a sensor for chemotactic responses to both iron and oxygen in the human pathogen Treponema denticola (Td). The ODP di-iron site binds oxygen at high affinity to reversibly form an unusually stable peroxo adduct.


Pssm-ID: 437415  Cd Length: 194  Bit Score: 96.01  E-value: 3.10e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140   60 VESLSKLIDPQEIQYIVVNHTEPDHSGGLAALASRATNATIVCTEIA---VPEiqemYKLHNRKFLVVKD-GDTLDIG-G 134
Cdd:pfam19583  29 LAKVSKYIDPEKIKYIFASHQDPDICSSLPLWLDVIPDAKIVISELWerfLPH----YGLKKSRFIPIPDeGGRITLGsG 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140  135 KTLKFKETPYLHTEETMITYCVEDKILFPCDIFSThiandeIFSDKANVDITEDFIGYYNAIIHPHRRY------VRTLI 208
Cdd:pfam19583 105 RRLEFIPAHFLHSPGNFVTYDPVSKILFSGDIGAA------LFPGKDWSLFVEDFDAHIPYMEGFHRRYmpsnkaLRLWV 178

                         170
                  ....*....|....*.
gi 446436140  209 EALKDLDVQMIAPSHG 224
Cdd:pfam19583 179 EMVRKLDIEMIAPQHG 194
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 36-223 6.24e-20

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: 86.45  E-value: 6.24e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140    36 NAYLLKTEKPTV-IDTVdIEFGREFVESLSKLiDPQEIQYIVVNHTEPDHSGGLAALAsRATNATIVCTEIAVPEIQEMY 114
Cdd:smart00849   1 NSYLVRDDGGAIlIDTG-PGEAEDLLAELKKL-GPKKIDAIILTHGHPDHIGGLPELL-EAPGAPVYAPEGTAELLKDLL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140   115 KLH---------NRKFLVVKDGDTLDIGGKTLKFKETPyLHTEETMITYCVEDKILFPCDIFSTHIandeifsdkanvDI 185
Cdd:smart00849  78 ALLgelgaeaepAPPDRTLKDGDELDLGGGELEVIHTP-GHTPGSIVLYLPEGKILFTGDLLFAGG------------DG 144

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 446436140   186 TEDFIGYYnaiiHPHRRYVRTLIEALKdLDVQMIAPSH 223
Cdd:smart00849 145 RTLVDGGD----AAASDALESLLKLLK-LLPKLVVPGH 177
flav_short TIGR01753
flavodoxin, short chain; Flavodoxins are small redox-active proteins with a flavin ...
 251-403 2.72e-16

flavodoxin, short chain; Flavodoxins are small redox-active proteins with a flavin mononucleotide (FMN) prosthetic group. They can act in nitrogen fixation by nitrogenase, in sulfite reduction, and light-dependent NADP+ reduction in during photosynthesis, among other roles. This model describes the short chain type. Many of these are involved in sulfite reduction. [Energy metabolism, Electron transport]


Pssm-ID: 273789 [Multi-domain]  Cd Length: 140  Bit Score: 75.07  E-value: 2.72e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140  251 VTIVYTTIKNNTKKVANIIKETLEADNIHVTVFNADKSKKLEVLksiqEADAVFIGSSTrYADmiGNLEE-----ILKEM 325
Cdd:TIGR01753   1 ILIVYASMTGNTEEMANIIAEGLKEAGAEVDLLEVADADAEDLL----SYDAVLLGCST-WGD--EDLEQddfepFFEEL 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446436140  326 TEMNLEGKIAASFGSYGWSGEAIEVIQDYlnETNMnvqstskviKSTGMTHVEFPIRIRFSPKDEGKVKKIQHATTFV 403
Cdd:TIGR01753  74 EDIDLGGKKVALFGSGDWGYEFCEAVDDW--EERL---------KEAGATIIAEGLKVDGDPEEEDLDKCREFAKDLA 140
 
Name Accession Description Interval E-value
NorV COG0426
Flavorubredoxin [Energy production and conversion];
5-403 3.51e-150

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 430.79  E-value: 3.51e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140   5 IQLTKDIYWVGKVDNREVPFHRLI-LAKGTTYNAYLLKTEKPTVIDTVDIEFGREFVESLSKLIDPQEIQYIVVNHTEPD 83
Cdd:COG0426    3 VEIAHGVYWVGVLDWDRRLFEGEYpTPRGTTYNSYLIVDEKTALIDTVGESFFEEFLENLSKVIDPKKIDYIIVNHQEPD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140  84 HSGGLAALASRATNATIVCTEIAVPEIQEMYKLHNRKFLVVKDGDTLDIGGKTLKFKETPYLHTEETMITYCVEDKILFP 163
Cdd:COG0426   83 HSGSLPELLELAPNAKIVCSKKAARFLPHFYGIPDFRFIVVKEGDTLDLGGHTLQFIPAPMLHWPDTMFTYDPEDKILFS 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140 164 CDIFSTHIANDEIFSDKANVDITEDFIGYYNAIIHPHRRYVRTLIEALKDLDVQMIAPSHGYILRQDIQKYIKLYADMSR 243
Cdd:COG0426  163 GDAFGSHGASDELFDDEVDEHLEEEARRYYANIMMPFSKQVLKALKKVRGLDIDMIAPSHGPIWRGNPKEILDWYRKWSS 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140 244 DTnQDKKVTIVYTTIKNNTKKVANIIKETLEADNIHVTVFNADKSKKLEVLKSIQEADAVFIGSSTRYADMIGNLEEILK 323
Cdd:COG0426  243 YQ-PEKKVVIVYASMYGNTEKMAEAIAEGLTEEGVKVKLYDLEKTDPSEIITEIFDAKGIVIGSPTYNGGAFPPIADLLG 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140 324 EMTEMNLEGKIAASFGSYGWSGEAIEVIQDYLNETNMNVqstskvikstgmthVEFPIRIRFSPKDEGKVKKIQHATTFV 403
Cdd:COG0426  322 YLKGLAPKNKLAGAFGSYGWSGEAVKLLEEKLEDAGFEV--------------VFEPLRVKFKPTEEDLKKCEELGTDLA 387
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 5-242 4.06e-105

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


Pssm-ID: 293795 [Multi-domain]  Cd Length: 238  Bit Score: 310.19  E-value: 4.06e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140   5 IQLTKDIYWVGKVDNREVPFHRLI-LAKGTTYNAYLLKTEKPTVIDTVDIEFGREFVESLSKLIDPQEIQYIVVNHTEPD 83
Cdd:cd07709    1 VEIADDIYWVGVNDWDLRLFEGEYpTPRGTSYNSYLIKDEKTALIDTVKEPFFDEFLENLEEVIDPRKIDYIVVNHQEPD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140  84 HSGGLAALASRATNATIVCTEIAVPEIQEMYKLHNRKFLVVKDGDTLDIGGKTLKFKETPYLHTEETMITYCVEDKILFP 163
Cdd:cd07709   81 HSGSLPELLELAPNAKIVCSKKAARFLKHFYPGIDERFVVVKDGDTLDLGKHTLKFIPAPMLHWPDTMVTYDPEDKILFS 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446436140 164 CDIFSTHIANDEIFSDKANvDITEDFIGYYNAIIHPHRRYVRTLIEALKDLDVQMIAPSHGYILRQDIQKYIKLYADMS 242
Cdd:cd07709  161 GDAFGAHGASGELFDDEVE-DYLEEARRYYANIMGPFSKQVRKALEKLEALDIKMIAPSHGPIWRKDPGEIIDLYRDWS 238
PRK11921 PRK11921
anaerobic nitric oxide reductase flavorubredoxin;
6-403 4.78e-90

anaerobic nitric oxide reductase flavorubredoxin;


Pssm-ID: 237023 [Multi-domain]  Cd Length: 394  Bit Score: 277.34  E-value: 4.78e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140   6 QLTKDIYWVGKVDNREVPFH--RLILAKGTTYNAYLLKTEKPTVIDTVDIEFGREFVESLSKLIDPQEIQYIVVNHTEPD 83
Cdd:PRK11921   2 KINDNVTWVGKIDWELRKFHgeEYSTHRGSSYNSYLIKDEKTVLIDTVWQPFAKEFVENLKKEIDLDKIDYIVANHGEID 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140  84 HSGGLAALASRATNATIVCTEIAVPEIQEMYKlHNRKFLVVKDGDTLDIGGKTLKFKETPYLHTEETMITYCVEDKILFP 163
Cdd:PRK11921  82 HSGALPELMKEIPDTPIYCTKNGAKSLKGHYH-QDWNFVVVKTGDRLEIGSNELIFIEAPMLHWPDSMFTYLTGDNILFS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140 164 CDIFSTHIANDEIFSDKanVDITEDF---IGYYNAIIHPHRRYVRTLIEALKDLD--VQMIAPSHGYILRQD----IQKY 234
Cdd:PRK11921 161 NDAFGQHYASELMYNDL--VDQGELYqeaIKYYANILTPFSPLVIKKIEEILSLNlpVDMICPSHGVIWRDNplqiVEKY 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140 235 IKLYADMsrdtnQDKKVTIVYTTIKNNTKKVANIIKETLEADNIHVTV--FNADKSKKLEVLKSIQEADAVFIGSSTRYA 312
Cdd:PRK11921 239 LEWAANY-----QENQVTILYDTMWNSTRRMAEAIAEGIKKANKDVTVklYNSAKSDKNDIITEVFKSKAILVGSSTINR 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140 313 DMIGNLEEILKEMTEMNLEGKIAASFGSYGWSGEAIEVIQDYLnetnmnvqstskviKSTGMTHVEFPIRIRFSPKDEGK 392
Cdd:PRK11921 314 GILSSTAAILEEIKGLGFKNKKAAAFGSYGWSGESVKIITERL--------------KKAGFEIVNDGIRELWNPDDEAL 379

                        410
                 ....*....|.
gi 446436140 393 VKKIQHATTFV 403
Cdd:PRK11921 380 DRCRSFGENFA 390
PRK05452 PRK05452
anaerobic nitric oxide reductase flavorubredoxin; Provisional
 5-368 1.44e-86

anaerobic nitric oxide reductase flavorubredoxin; Provisional


Pssm-ID: 235475 [Multi-domain]  Cd Length: 479  Bit Score: 271.25  E-value: 1.44e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140   5 IQLTKDIYWVGKVDNREVPFH--RLILAKGTTYNAYLLKTEKPTVIDTVDIEFGREFVESLSKLIDPQEIQYIVVNHTEP 82
Cdd:PRK05452   3 IHVKNNIHWVGQRDWEVRDFHgtEYKTLRGSSYNSYLIREEKNVLIDTVDHKFSREFVQNLRNEIDLADIDYIVINHAEE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140  83 DHSGGLAALASRATNATIVCTEIAVPEIQEMYKLHNRKFLVVKDGDTLDIG-GKTLKFKETPYLHTEETMITYCVEDKIL 161
Cdd:PRK05452  83 DHAGALTELMAQIPDTPIYCTANAIDSINGHHHHPEWNFNVVKTGDTLDIGnGKQLIFVETPMLHWPDSMMTYLTGDAVL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140 162 FPCDIFSTHIANDEIFSDKanVDITEDF---IGYYNAIIHPHRRYVRTLI-EALK-DLDVQMIAPSHGYILRQDIQKYIK 236
Cdd:PRK05452 163 FSNDAFGQHYCDEHLFNDE--VDQTELFeqcQRYYANILTPFSRLVTPKItEILGfNLPVDMIATSHGVVWRDNPTQIVE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140 237 LYADMSrDTNQDKKVTIVYTTIKNNTKKVANIIKETL-EAD-NIHVTVFNADKSKKLEVLKSIQEADAVFIGSSTRYADM 314
Cdd:PRK05452 241 LYLKWA-ADYQEDRITIFYDTMSNNTRMMADAIAQGIaEVDpRVAVKIFNVARSDKNEILTNVFRSKGVLVGSSTMNNVM 319

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446436140 315 IGNLEEILKEMTEMNLEGKIAASFGSYGWSGEAIEVIQDYLNETNMNVQSTSKV 368
Cdd:PRK05452 320 MPKIAGLLEEITGLRFRNKRASAFGSHGWSGGAVDRLSTRLQDAGFEMSLSLKA 373
ODP pfam19583
ODP family beta lactamase; The ODP (Oxygen-binding Di-iron Protein) domain is a distinct ...
 60-224 3.10e-23

ODP family beta lactamase; The ODP (Oxygen-binding Di-iron Protein) domain is a distinct member of the metallo-beta-lactamase superfamily recruited to various bacterial and archaeal signal transduction pathways, including chemotaxis, to function as oxygen and iron sensors (1). ODP was shown to act as a sensor for chemotactic responses to both iron and oxygen in the human pathogen Treponema denticola (Td). The ODP di-iron site binds oxygen at high affinity to reversibly form an unusually stable peroxo adduct.


Pssm-ID: 437415  Cd Length: 194  Bit Score: 96.01  E-value: 3.10e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140   60 VESLSKLIDPQEIQYIVVNHTEPDHSGGLAALASRATNATIVCTEIA---VPEiqemYKLHNRKFLVVKD-GDTLDIG-G 134
Cdd:pfam19583  29 LAKVSKYIDPEKIKYIFASHQDPDICSSLPLWLDVIPDAKIVISELWerfLPH----YGLKKSRFIPIPDeGGRITLGsG 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140  135 KTLKFKETPYLHTEETMITYCVEDKILFPCDIFSThiandeIFSDKANVDITEDFIGYYNAIIHPHRRY------VRTLI 208
Cdd:pfam19583 105 RRLEFIPAHFLHSPGNFVTYDPVSKILFSGDIGAA------LFPGKDWSLFVEDFDAHIPYMEGFHRRYmpsnkaLRLWV 178

                         170
                  ....*....|....*.
gi 446436140  209 EALKDLDVQMIAPSHG 224
Cdd:pfam19583 179 EMVRKLDIEMIAPQHG 194
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 36-223 6.24e-20

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: 86.45  E-value: 6.24e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140    36 NAYLLKTEKPTV-IDTVdIEFGREFVESLSKLiDPQEIQYIVVNHTEPDHSGGLAALAsRATNATIVCTEIAVPEIQEMY 114
Cdd:smart00849   1 NSYLVRDDGGAIlIDTG-PGEAEDLLAELKKL-GPKKIDAIILTHGHPDHIGGLPELL-EAPGAPVYAPEGTAELLKDLL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140   115 KLH---------NRKFLVVKDGDTLDIGGKTLKFKETPyLHTEETMITYCVEDKILFPCDIFSTHIandeifsdkanvDI 185
Cdd:smart00849  78 ALLgelgaeaepAPPDRTLKDGDELDLGGGELEVIHTP-GHTPGSIVLYLPEGKILFTGDLLFAGG------------DG 144

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 446436140   186 TEDFIGYYnaiiHPHRRYVRTLIEALKdLDVQMIAPSH 223
Cdd:smart00849 145 RTLVDGGD----AAASDALESLLKLLK-LLPKLVVPGH 177
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 36-236 6.54e-19

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: 84.74  E-value: 6.54e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140  36 NAYLLKT-EKPTVIDT-VDIEFGREFVESLSKLIDPqeIQYIVVNHTEPDHSGGLAALAsRATNATIVCTEIAVPEI--- 110
Cdd:COG0491   16 NSYLIVGgDGAVLIDTgLGPADAEALLAALAALGLD--IKAVLLTHLHPDHVGGLAALA-EAFGAPVYAHAAEAEALeap 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140 111 --QEMYKLHNRKF-LVVKDGDTLDIGGKTLKFKETPYlHTEETMITYCVEDKILFPCD-IFSTHIANDEIFSdkanvdit 186
Cdd:COG0491   93 aaGALFGREPVPPdRTLEDGDTLELGGPGLEVIHTPG-HTPGHVSFYVPDEKVLFTGDaLFSGGVGRPDLPD-------- 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 446436140 187 edfigyynaiiHPHRRYVRTLiEALKDLDVQMIAPSHGYILRQDIQKYIK 236
Cdd:COG0491  164 -----------GDLAQWLASL-ERLLALPPDLVIPGHGPPTTAEAIDYLE 201
flav_short TIGR01753
flavodoxin, short chain; Flavodoxins are small redox-active proteins with a flavin ...
 251-403 2.72e-16

flavodoxin, short chain; Flavodoxins are small redox-active proteins with a flavin mononucleotide (FMN) prosthetic group. They can act in nitrogen fixation by nitrogenase, in sulfite reduction, and light-dependent NADP+ reduction in during photosynthesis, among other roles. This model describes the short chain type. Many of these are involved in sulfite reduction. [Energy metabolism, Electron transport]


Pssm-ID: 273789 [Multi-domain]  Cd Length: 140  Bit Score: 75.07  E-value: 2.72e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140  251 VTIVYTTIKNNTKKVANIIKETLEADNIHVTVFNADKSKKLEVLksiqEADAVFIGSSTrYADmiGNLEE-----ILKEM 325
Cdd:TIGR01753   1 ILIVYASMTGNTEEMANIIAEGLKEAGAEVDLLEVADADAEDLL----SYDAVLLGCST-WGD--EDLEQddfepFFEEL 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446436140  326 TEMNLEGKIAASFGSYGWSGEAIEVIQDYlnETNMnvqstskviKSTGMTHVEFPIRIRFSPKDEGKVKKIQHATTFV 403
Cdd:TIGR01753  74 EDIDLGGKKVALFGSGDWGYEFCEAVDDW--EERL---------KEAGATIIAEGLKVDGDPEEEDLDKCREFAKDLA 140
FldA COG0716
Flavodoxin [Energy production and conversion]; Flavodoxin is part of the Pathway/BioSystem: ...
 251-362 4.00e-16

Flavodoxin [Energy production and conversion]; Flavodoxin is part of the Pathway/BioSystem: Heme biosynthesis


Pssm-ID: 440480 [Multi-domain]  Cd Length: 135  Bit Score: 74.55  E-value: 4.00e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140 251 VTIVYTTIKNNTKKVANIIKETLEADNihVTVFNADKSKklevLKSIQEADAVFIGSSTRYADMIGNLEEILKEMTEmNL 330
Cdd:COG0716    1 ILIVYGSTTGNTEKVAEAIAEALGAAG--VDLFEIEDAD----LDDLEDYDLLILGTPTWAGELPDDWEDFLEELKE-DL 73

                         90       100       110
                 ....*....|....*....|....*....|....
gi 446436140 331 EGKIAASFGSYGWS--GEAIEVIQDYLNETNMNV 362
Cdd:COG0716   74 SGKKVALFGTGDSSgyGDALGELKELLEEKGAKV 107
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 36-224 1.78e-14

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: 71.18  E-value: 1.78e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140  36 NAYLLKTEKPTV-IDT--VDIEFGREFVESLSKL-IDPQEIQYIVVNHTEPDHSGGLAALASRAtnatiVCTEIAVPeiq 111
Cdd:cd07725   16 NVYLLRDGDETTlIDTglATEEDAEALWEGLKELgLKPSDIDRVLLTHHHPDHIGLAGKLQEKS-----GATVYILD--- 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140 112 emyklhnrkFLVVKDGDTLDIGGKTLKFKETPYlHTEETMITYCVEDKILFPCDifstHIANdeifsdkanvDITEDFIG 191
Cdd:cd07725   88 ---------VTPVKDGDKIDLGGLRLKVIETPG-HTPGHIVLYDEDRRELFVGD----AVLP----------KITPNVSL 143

                        170       180       190
                 ....*....|....*....|....*....|...
gi 446436140 192 YYNAIIHPHRRYVRTLiEALKDLDVQMIAPSHG 224
Cdd:cd07725  144 WAVRVEDPLGAYLESL-DKLEKLDVDLAYPGHG 175
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 37-151 2.01e-13

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


Pssm-ID: 293838 [Multi-domain]  Cd Length: 251  Bit Score: 69.54  E-value: 2.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140  37 AYLLKT-EKPTVIDTVD-IEFGREFVESLSKL-IDPQEIQYIVVNHTEPDHSGGLAALASRaTNATIVCTEIAVPEIQEM 113
Cdd:cd16280   24 AWAIDTgDGLILIDALNnNEAADLIVDGLEKLgLDPADIKYILITHGHGDHYGGAAYLKDL-YGAKVVMSEADWDMMEEP 102

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 446436140 114 YKLHN--------RKFLVVKDGDTLDIGGKTLKFKETPYlHTEETM 151
Cdd:cd16280  103 PEEGDnprwgpppERDIVIKDGDTLTLGDTTITVYLTPG-HTPGTL 147
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 36-162 2.94e-12

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: 65.00  E-value: 2.94e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140  36 NAYLLKTEKPT--VIDTvdiefGREFVESLSKLID--PQEIQYIVVNHTEPDHSGGLAALAsRATNATIVCTEIAVPEIQ 111
Cdd:cd06262   11 NCYLVSDEEGEaiLIDP-----GAGALEKILEAIEelGLKIKAILLTHGHFDHIGGLAELK-EAPGAPVYIHEADAELLE 84

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446436140 112 EMYKLHNRKFLV----------VKDGDTLDIGGKTLKFKETPyLHTEETMITYCVEDKILF 162
Cdd:cd06262   85 DPELNLAFFGGGplpppepdilLEDGDTIELGGLELEVIHTP-GHTPGSVCFYIEEEGVLF 144
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 37-143 1.20e-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: 63.67  E-value: 1.20e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140  37 AYLLKTE-KPTVIDT---VDIEFGREFVESLSklIDPQEIQYIVVNHTEPDHSGGLAALASRATNATIVCTEIAVPEI-- 110
Cdd:cd07726   18 SYLLDGEgRPALIDTgpsSSVPRLLAALEALG--IAPEDVDYIILTHIHLDHAGGAGLLAEALPNAKVYVHPRGARHLid 95

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446436140 111 -------------QEMYKLHNR-------KFLVVKDGDTLDIGGKTLKFKETP 143
Cdd:cd07726   96 psklwasaravygDEADRLGGEilpvpeeRVIVLEDGETLDLGGRTLEVIDTP 148
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
36-223 1.46e-11

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 63.16  E-value: 1.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140   36 NAYLLKTEKPTV-IDT-VDIEFGREFvESLSKLIDPQEIQYIVVNHTEPDHSGGLAALASRATNATIVCTEIAVP----- 108
Cdd:pfam00753   7 NSYLIEGGGGAVlIDTgGSAEAALLL-LLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARElldee 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140  109 -EIQEMYKLHNRKFLVVK-------DGDTLDIGGKTLKFKETPyLHTEETMITYCVEDKILFPCDifsTHIANDEIFSDK 180
Cdd:pfam00753  86 lGLAASRLGLPGPPVVPLppdvvleEGDGILGGGLGLLVTHGP-GHGPGHVVVYYGGGKVLFTGD---LLFAGEIGRLDL 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 446436140  181 ANVDITEDFIGYYNAiihphrryVRTLIEALKDLDVQMIAPSH 223
Cdd:pfam00753 162 PLGGLLVLHPSSAES--------SLESLLKLAKLKAAVIVPGH 196
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 47-224 1.84e-10

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


Pssm-ID: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 60.27  E-value: 1.84e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140  47 VIDT-VDIEFGREFVESLSKLIDpQEIQYIVVNHTEPDHSGGLAALAsrATNATIVCTEIAVPEIQE--------MYKLH 117
Cdd:cd16282   28 VIDTgASPRLARALLAAIRKVTD-KPVRYVVNTHYHGDHTLGNAAFA--DAGAPIIAHENTREELAArgeaylelMRRLG 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140 118 NRKF---------LVVKDGDTLDIGGKTLKFKETPYLHTEETMITYCVEDKILFPCDIFsthiandeiFSDkaNVDITED 188
Cdd:cd16282  105 GDAMagtelvlpdRTFDDGLTLDLGGRTVELIHLGPAHTPGDLVVWLPEEGVLFAGDLV---------FNG--RIPFLPD 173

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 446436140 189 fiGYYnaiihphRRYVRTLiEALKDLDVQMIAPSHG 224
Cdd:cd16282  174 --GSL-------AGWIAAL-DRLLALDATVVVPGHG 199
PRK06703 PRK06703
flavodoxin; Provisional
 250-404 2.73e-10

flavodoxin; Provisional


Pssm-ID: 235854 [Multi-domain]  Cd Length: 151  Bit Score: 58.23  E-value: 2.73e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140 250 KVTIVYTTIKNNTKKVANIIKETLEADNIHVTVFNADKSKKLEVLksiqEADAVFIGSSTrYADmiGNL----EEILKEM 325
Cdd:PRK06703   3 KILIAYASMSGNTEDIADLIKVSLDAFDHEVVLQEMDGMDAEELL----AYDGIILGSYT-WGD--GDLpyeaEDFHEDL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140 326 TEMNLEGKIAASFGS----YGWSGEAIEVIQDYLNETNMNV-QSTSKvikstgmthvefpirIRFSPKDEGKVKKIQH-A 399
Cdd:PRK06703  76 ENIDLSGKKVAVFGSgdtaYPLFCEAVTIFEERLVERGAELvQEGLK---------------IELAPETDEDVEKCSNfA 140


                 ....*
gi 446436140 400 TTFVT 404
Cdd:PRK06703 141 IAFAE 145
PRK05568 PRK05568
flavodoxin; Provisional
 249-372 3.40e-10

flavodoxin; Provisional


Pssm-ID: 235508 [Multi-domain]  Cd Length: 142  Bit Score: 57.90  E-value: 3.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140 249 KKVTIVYTTIKNNTKKVANIIKETLEADNIHVTVFNADKSKKLEVlksiQEADAVFIGSSTRYADMI--GNLEEILKEMT 326
Cdd:PRK05568   2 KKINIIYWSGTGNTEAMANLIAEGAKENGAEVKLLNVSEASVDDV----KGADVVALGSPAMGDEVLeeGEMEPFVESIS 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 446436140 327 EMnLEGKIAASFGSYGW-SGEAIEVIQDYLNETNMNVQSTSKVIKST 372
Cdd:PRK05568  78 SL-VKGKKLVLFGSYGWgDGEWMRDWVERMEGYGANLVNEGLIVNNT 123
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 25-224 1.05e-09

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: 58.00  E-value: 1.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140  25 HRLILAKGTtyNAYLLKTEKP-TVIDTVDIEFGREFVESLSKL-IDPQEIQYIVVNHTEPDHSGGLAALAsRATNATIVC 102
Cdd:cd07721    3 YQLPLLPPV--NAYLIEDDDGlTLIDTGLPGSAKRILKALRELgLSPKDIRRILLTHGHIDHIGSLAALK-EAPGAPVYA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140 103 TEIAVPEIQ--EMYKLHNRKFL-----------------VVKDGDTLDIGG--KTLkfkETP--------YLHTeetmit 153
Cdd:cd07721   80 HEREAPYLEgeKPYPPPVRLGLlgllspllpvkpvpvdrTLEDGDTLDLAGglRVI---HTPghtpghisLYLE------ 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446436140 154 ycvEDKILFPCDIFSTHIANDEIFSDKANVDItedfigyynaiihphRRYVRTlIEALKDLDVQMIAPSHG 224
Cdd:cd07721  151 ---EDGVLIAGDALVTVGGELVPPPPPFTWDM---------------EEALES-LRKLAELDPEVLAPGHG 202
PRK05569 PRK05569
flavodoxin; Provisional
 249-362 2.09e-08

flavodoxin; Provisional


Pssm-ID: 135442 [Multi-domain]  Cd Length: 141  Bit Score: 52.91  E-value: 2.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140 249 KKVTIVYTTIKNNTKKVANIIKETLEADNIHVTVFNADKSKKLEVLksiqEADAVFIGSSTRYADMIG--NLEEILKEMT 326
Cdd:PRK05569   2 KKVSIIYWSCGGNVEVLANTIADGAKEAGAEVTIKHVADAKVEDVL----EADAVAFGSPSMDNNNIEqeEMAPFLDQFK 77

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 446436140 327 EMNLEGKIAASFGSYGW-SGEAIEVIQDYLNETNMNV 362
Cdd:PRK05569  78 LTPNENKKCILFGSYGWdNGEFMKLWKDRMKDYGFNV 114
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 38-143 6.22e-08

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: 53.26  E-value: 6.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140  38 YLLKT-EKPTVIDTVDIEFGREFVESLSKL-IDPQEIQYIVVNHTEPDHSGGLAALaSRATNATIVCTEIAVPEIQEMYK 115
Cdd:cd16309   25 FLITTpEGHILIDGAMPQSTPLIKDNIKKLgFDVKDVKYLLNTHAHFDHAGGLAEL-KKATGAQLVASAADKPLLESGYV 103

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 446436140 116 LH-NRKFL---------VVKDGDTLDIGGKTLKFKETP 143
Cdd:cd16309  104 GSgDTKNLqfppvrvdrVIGDGDKVTLGGTTLTAHLTP 141
PRK09267 PRK09267
flavodoxin FldA; Validated
 249-339 8.52e-08

flavodoxin FldA; Validated


Pssm-ID: 236439 [Multi-domain]  Cd Length: 169  Bit Score: 51.75  E-value: 8.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140 249 KKVTIVYTTIKNNTKKVANIIKETLEADNihVTVFNADKSKKLEvlksIQEADAVFIGSSTRYadmIGNL----EEILKE 324
Cdd:PRK09267   2 AKIGIFFGSDTGNTEDIAKMIQKKLGKDV--ADVVDIAKASKED----FEAYDLLILGIPTWG---YGELqcdwDDFLPE 72

                         90
                 ....*....|....*
gi 446436140 325 MTEMNLEGKIAASFG 339
Cdd:PRK09267  73 LEEIDFSGKKVALFG 87
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 32-224 8.63e-08

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: 51.77  E-value: 8.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140  32 GTtyNAYLLKTEKPTV-IDTVDiefGR-EFVESLSKLID---PQEIQYIVVNHTEPDHSGGLAALASRATNATIVCTEIA 106
Cdd:cd07722   17 GT--NTYLVGTGKRRIlIDTGE---GRpSYIPLLKSVLDsegNATISDILLTHWHHDHVGGLPDVLDLLRGPSPRVYKFP 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140 107 VPEIQEMYKLHNRKFLVVKDGDTLDIGGKTLKFKETPYlHTEETMITYCVEDKILFPCD--------IFsthiandeifs 178
Cdd:cd07722   92 RPEEDEDPDEDGGDIHDLQDGQVFKVEGATLRVIHTPG-HTTDHVCFLLEEENALFTGDcvlghgtaVF----------- 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 446436140 179 dkanvditEDFigyynaiihphRRYVRTLiEALKDLDVQMIAPSHG 224
Cdd:cd07722  160 --------EDL-----------AAYMASL-KKLLSLGPGRIYPGHG 185
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 26-227 6.43e-07

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


Pssm-ID: 293836 [Multi-domain]  Cd Length: 185  Bit Score: 49.41  E-value: 6.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140  26 RLILA--------KGTtyNAYLLKTEKP-TVIDT-VDIEfgrEFVESLSKLIDPQEIQYIVVNHTEPDHSGGLAALAsRA 95
Cdd:cd16278    3 RRVLApnpspmtlDGT--NTYLLGAPDGvVVIDPgPDDP---AHLDALLAALGGGRVSAILVTHTHRDHSPGAARLA-ER 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140  96 TNATIvcteIAVPEIQEMYKLHNRKF-LVVKDGDTLDIGGKTLKFKETPYlHTEETMityCV---EDKILFPCDI---FS 168
Cdd:cd16278   77 TGAPV----RAFGPHRAGGQDTDFAPdRPLADGEVIEGGGLRLTVLHTPG-HTSDHL---CFaleDEGALFTGDHvmgWS 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446436140 169 THIandeifsdkanvditedfigyynaIIHPH---RRYVRTLiEALKDLDVQMIAPSHGYIL 227
Cdd:cd16278  149 TTV------------------------IAPPDgdlGDYLASL-ERLLALDDRLLLPGHGPPI 185
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 36-167 6.63e-07

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: 49.65  E-value: 6.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140  36 NAYLL---KTEKPTVIDTVDIEfgrefvESLSKLIDPQE--IQYIVVNHTEPDHSGGLAALAsRATNATIVCTEIAVPeI 110
Cdd:cd16322   12 NTYLVadeGGGEAVLVDPGDES------EKLLARFGTTGltLLYILLTHAHFDHVGGVADLR-RHPGAPVYLHPDDLP-L 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446436140 111 QEMYKLHNRKFLV-----------VKDGDTLDIGGKTLKFKETPYlHTEETMITYCVEDKILFPCD-IF 167
Cdd:cd16322   84 YEAADLGAKAFGLgieplpppdrlLEDGQTLTLGGLEFKVLHTPG-HSPGHVCFYVEEEGLLFSGDlLF 151
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 28-134 1.20e-06

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: 48.03  E-value: 1.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140  28 ILAKGTTYNAYLLKTEKPTVIdtVDIEF-GREFVESLSKL-IDPQEIQYIVVNHTEPDHSGGLAALAsRATNATIVCTEI 105
Cdd:cd07733    2 VLASGSKGNCTYLETEDGKLL--IDAGLsGRKITGRLAEIgRDPEDIDAILVTHEHADHIKGLGVLA-RKYNVPIYATAG 78

                         90       100       110
                 ....*....|....*....|....*....|
gi 446436140 106 AVPEIQEMYKL-HNRKFLVVKDGDTLDIGG 134
Cdd:cd07733   79 TLRAMERKVGLiDVDQKQIFEPGETFSIGD 108
HemG COG4635
Protoporphyrinogen IX oxidase, menaquinone-dependent (flavodoxin domain) [Coenzyme transport ...
 249-311 1.89e-06

Protoporphyrinogen IX oxidase, menaquinone-dependent (flavodoxin domain) [Coenzyme transport and metabolism];


Pssm-ID: 443673  Cd Length: 179  Bit Score: 47.97  E-value: 1.89e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446436140 249 KKVTIVYTTIKNNTKKVANIIKETLEADNIHVTVFNADKSKKLEvlksIQEADAVFIGSSTRY 311
Cdd:COG4635    1 MKVLILYASRDGQTRKIAERIAEVLREAGHDVDLVDLEDAPDLD----LAGYDAVVIGASIRY 59
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 ...
 68-148 6.32e-06

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: 47.34  E-value: 6.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140  68 DPQEIQYIVVNHTEPDHSGGLAALAsRATNATIVCTEIAVPEIQEMYKLHN-------------RKFLVVKDGDTLDIGG 134
Cdd:cd16290   57 RLEDVKLILNSHAHFDHAGGIAALQ-RDSGATVAASPAGAAALRSGGVDPDdpqagaadpfppvAKVRVVADGEVVKLGP 135

                         90
                 ....*....|....
gi 446436140 135 KTLKFKETPYlHTE 148
Cdd:cd16290  136 LAVTAHATPG-HTP 148
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 6-189 6.47e-06

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: 47.32  E-value: 6.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140   6 QLTKDIYWVGkvdnrevpfhrlilakgtTYN--AYLLKTEKPTV-IDTVDIEFGREFVESLSKL-IDPQEIQYIVVNHTE 81
Cdd:cd16288    9 RIAGNVYYVG------------------TSGlaSYLITTPQGLIlIDTGLESSAPMIKANIRKLgFKPSDIKILLNSHAH 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140  82 PDHSGGLAALaSRATNATIVCTEIAVPEI----QEMYKLHNRKFL--------VVKDGDTLDIGGKTLKFKETPYlHTE- 148
Cdd:cd16288   71 LDHAGGLAAL-KKLTGAKLMASAEDAALLasggKSDFHYGDDSLAfppvkvdrVLKDGDRVTLGGTTLTAHLTPG-HTRg 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 446436140 149 -ETMITYCVEDK----ILFPCdifSTHIANDEIFSDKANV-DITEDF 189
Cdd:cd16288  149 cTTWTMTVKDDGkvyqVVFAD---SLTVNPGYKLVGNPTYpGIAEDY 192
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 33-101 1.05e-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: 46.39  E-value: 1.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140  33 TTYNAYLLKTEKPTV-IDTvdiEFGREFVESLSKL--------IDPQEIQYIVVNHTEPDHSGGLAALASRAT--NATIV 101
Cdd:cd07720   47 TSVNAFLVRTGGRLIlVDT---GAGGLFGPTAGKLlanlaaagIDPEDIDDVLLTHLHPDHIGGLVDAGGKPVfpNAEVH 123
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 47-158 1.37e-05

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: 45.08  E-value: 1.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140  47 VIDTVdiefgREFVESLSKLIDPQ--EIQYIVVNHTEPDH-SGGLAaLASRaTNATIVCTEIAVPEIqemyklhnrKFLV 123
Cdd:cd07724   27 VIDPV-----RDSVDRYLDLAAELglKITYVLETHVHADHvSGARE-LAER-TGAPIVIGEGAPASF---------FDRL 90

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 446436140 124 VKDGDTLDIGGKTLKFKETPYlHTEEtMITYCVED 158
Cdd:cd07724   91 LKDGDVLELGNLTLEVLHTPG-HTPE-SVSYLVGD 123
EVM-1-like_MBL-B3 cd16315
Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 68-148 1.80e-05

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: 45.80  E-value: 1.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140  68 DPQEIQYIVVNHTEPDHSGGLAALAsRATNATIVCTEIAVPEIQE--------MYKLHN-----RKFLVVKDGDTLDIGG 134
Cdd:cd16315   57 DPKDVRWLLSSHEHFDHVGGLAALQ-RATGARVAASAAAAPVLESgkpapddpQAGLHEpfppvRVDRIVEDGDTVALGS 135

                         90
                 ....*....|....
gi 446436140 135 KTLKFKETPyLHTE 148
Cdd:cd16315  136 LRLTAHATP-GHTP 148
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 71-162 2.43e-05

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: 44.37  E-value: 2.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140  71 EIQYIVVNHTEPDHSGGLAALASRATNATIVC-TEIAVPEIQEmyklhnrkflVVKDGDTLDIGGKTLKFKETPYlHTEE 149
Cdd:cd07723   43 TLTAILTTHHHWDHTGGNAELKALFPDAPVYGpAEDRIPGLDH----------PVKDGDEIKLGGLEVKVLHTPG-HTLG 111

                         90
                 ....*....|...
gi 446436140 150 TMITYCVEDKILF 162
Cdd:cd07723  112 HICYYVPDEPALF 124
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 36-167 2.85e-05

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: 44.54  E-value: 2.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140  36 NAYLLK-TEKPTVIDT----VDIefgREFVESLSKLidPqeiqYIVVN-HTEPDHSGGL------------AALASRATN 97
Cdd:cd07712   10 NIYLLRgRDRALLIDTglgiGDL---KEYVRTLTDL--P----LLVVAtHGHFDHIGGLhefeevyvhpadAEILAAPDN 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140  98 ATIVCTEIAVPEIQEMyklhnRKFLVVKDGDTLDIGGKTLKFKETPYlHTEETMITYCVEDKILFPCDIF 167
Cdd:cd07712   81 FETLTWDAATYSVPPA-----GPTLPLRDGDVIDLGDRQLEVIHTPG-HTPGSIALLDRANRLLFSGDVV 144
WrbA COG0655
Multimeric flavodoxin WrbA, includes NAD(P)H:quinone oxidoreductase [Energy production and ...
 250-364 8.81e-05

Multimeric flavodoxin WrbA, includes NAD(P)H:quinone oxidoreductase [Energy production and conversion];


Pssm-ID: 440420 [Multi-domain]  Cd Length: 181  Bit Score: 42.99  E-value: 8.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140 250 KVTIVYTTIKN--NTKKVANIIKETLEADNIHVTVFN-ADKSKK-----------------LEVLKSIQEADAVFIGSST 309
Cdd:COG0655    1 KILVINGSPRKngNTAALAEAVAEGAEEAGAEVELIRlADLDIKpcigcggtgkcvikddmNAIYEKLLEADGIIFGSPT 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446436140 310 RYADMIGnleeILK---------EMTEMNLEGKIAASF--GSYGWSGEAIEVIQDYLNETNMNVQS 364
Cdd:COG0655   81 YFGNMSA----QLKafidrlyalWAKGKLLKGKVGAVFttGGHGGAEATLLSLNTFLLHHGMIVVG 142
THIN-B-like_MBL-B3 cd16312
Janthinobacterium lividum THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 70-143 1.93e-04

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: 42.67  E-value: 1.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140  70 QEIQYIVVNHTEPDHSGGLAALaSRATNATIVCTEIAVPEIQE---------------MYKLHNRKFLVVKDGDTLDIGG 134
Cdd:cd16312   59 EDVKLILNSHAHWDHAGGIAAL-QKASGATVAASAHGAQVLQSgtngkddpqyqakpvVHVAKVAKVKEVGEGDTLKVGP 137


                 ....*....
gi 446436140 135 KTLKFKETP 143
Cdd:cd16312  138 LRLTAHMTP 146
AIM-1-like_MBL-B3 cd16314
Pseudomonas Aeruginosa AIM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 68-107 2.50e-04

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: 42.57  E-value: 2.50e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 446436140  68 DPQEIQYIVVNHTEPDHSGGLAALaSRATNATIVCTEIAV 107
Cdd:cd16314   57 RPEDVRYIVSSHEHFDHAGGIARL-QRATGAPVVAREPAA 95
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 35-140 2.88e-04

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: 42.20  E-value: 2.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140  35 YNAYLLKT-EKPTVIDT------------------VDIEFGREFVESLSKL-IDPQEIQYIVVNHTEPDHSGGLAALasr 94
Cdd:cd07729   32 VYAYLIEHpEGTILVDTgfhpdaaddpgglelafpPGVTEEQTLEEQLARLgLDPEDIDYVILSHLHFDHAGGLDLF--- 108

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 446436140  95 aTNATIVCTEiavPEIQEMYKLHNRKFLVVKDGDTLDIGGKTLKFK 140
Cdd:cd07729  109 -PNATIIVQR---AELEYATGPDPLAAGYYEDVLALDDDLPGGRVR 150
Flavodoxin_1 pfam00258
Flavodoxin;
253-345 7.58e-04

Flavodoxin;


Pssm-ID: 425562 [Multi-domain]  Cd Length: 142  Bit Score: 39.66  E-value: 7.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140  253 IVYTTIKNNTKKVANIIKETLEADNIHVTVFNADKSKklEVLKSIQEADAVFIGSSTRY-----ADMIGNLEEILKEMT- 326
Cdd:pfam00258   1 IFYGSQTGNTEKLAEAIAEGLGEAGFEVDVVDLDDVD--ETLSEIEEEDLLLVVVSTWGegeppDNAKPFVDWLLLFGTl 78

                          90       100
                  ....*....|....*....|..
gi 446436140  327 -EMNLEGKIAASF--GSYGWSG 345
Cdd:pfam00258  79 eDGDLSGLKYAVFglGDSGYEG 100
metallo-hydrolase-like_MBL-fold cd07741
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 67-154 1.58e-03

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


Pssm-ID: 293827 [Multi-domain]  Cd Length: 212  Bit Score: 39.48  E-value: 1.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140  67 IDPQEIQYIVVNHTEPDHSGGLAALASRATNA------TIVCTEIAVPEIQEMYKLHNRKFL----VVKDGDTLDIGGkt 136
Cdd:cd07741   49 LDPTKLDAIILSHRHLDHSNDANVLIEAMTEGgfkkrgTLLAPEDALNGEPVVLLYYHRRKLeeieILEEGDEYELGG-- 126

                         90
                 ....*....|....*...
gi 446436140 137 LKFKETPYLHTEETmiTY 154
Cdd:cd07741  127 IKIEATRHKHSDPT--TY 142
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
59-126 2.04e-03

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


Pssm-ID: 440850  Cd Length: 273  Bit Score: 39.87  E-value: 2.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140  59 FVESLSKL-IDPQEIQYIVVNHTEPDHSGGLAALASRATNATIVC---------------TEIAVPEIQEMYKLHNRKFL 122
Cdd:COG1237   44 LLKNAEKLgIDLSDIDAVVLSHGHYDHTGGLPALLELNPKAPVYAhpdafekryskrpggKYIGIPFSREELEKLGARLI 123


                 ....
gi 446436140 123 VVKD 126
Cdd:COG1237  124 LVKE 127
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 51-104 2.34e-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: 39.56  E-value: 2.34e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446436140  51 VDIEFGREFVESLSKL-IDPQEIQYIVVNHTEPDHSGGLAALasraTNATIVCTE 104
Cdd:cd07730   62 VPLEVEEDVAEQLAAGgIDPEDIDAVILSHLHWDHIGGLSDF----PNARLIVGP 112
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 6-189 2.51e-03

Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of Mbl1b-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293868  Cd Length: 252  Bit Score: 39.36  E-value: 2.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140   6 QLTKDIYWVGkvdnrevpfhrlilAKGTtyNAYLLKT-EKPTVIDTVDIEFGREFVESLSKL-IDPQEIQYIVVNHTEPD 83
Cdd:cd16310    9 RIVDNIYYVG--------------TKGI--GSYLITSnHGAILLDGGLEENAALIEQNIKALgFKLSDIKIIINTHAHYD 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140  84 HSGGLAALaSRATNATIVCTEIAVPEIQEMYKLHNRKF-----------LVVKDGDTLDIGGKTLKFKETPYlHTEE-TM 151
Cdd:cd16310   73 HAGGLAQL-KADTGAKLWASRGDRPALEAGKHIGDNITqpapfpavkvdRILGDGEKIKLGDITLTATLTPG-HTKGcTT 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 446436140 152 ITYCVED-----KILFPCdifSTHIANDEIFSDKANVDITEDF 189
Cdd:cd16310  151 WSTTVKEngrplRVVFPC---SLSVAGNVLVGNKTYPTIVEDY 190
SMB-1-like_MBL-B3 cd16313
SMB-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase ...
 69-108 2.74e-03

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: 39.08  E-value: 2.74e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 446436140  69 PQEIQYIVVNHTEPDHSGGLAALaSRATNATIVCTEIAVP 108
Cdd:cd16313   58 LEDVKYILSSHDHWDHAGGIAAL-QKLTGAQVLASPATVA 96
PRK06242 PRK06242
flavodoxin; Provisional
 250-342 3.60e-03

flavodoxin; Provisional


Pssm-ID: 180484 [Multi-domain]  Cd Length: 150  Bit Score: 37.59  E-value: 3.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140 250 KVTIVYTTIKN-NTKKVANIIKETLEADNIHVTVFNADKskklevlksIQEADAVFIGSSTRYADMIGNLEEILKEMteM 328
Cdd:PRK06242   2 KALIVYASVHHgNTEKIAKAIAEVLDAEVIDPGDVNPED---------LSEYDLIGFGSGIYFGKFHKSLLKLIEKL--P 70

                         90
                 ....*....|....
gi 446436140 329 NLEGKIAASFGSYG 342
Cdd:PRK06242  71 PVSGKKAFIFSTSG 84
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 37-155 4.33e-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: 4.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140  37 AYLLKTEKPTVIdtvdIEFGREFVESLSKL-IDPQEIQYIVVNHTEPDHSGGLAAL------ASRATNATIVCTE----- 104
Cdd:cd16272   19 SYLLETGGTRIL----LDCGEGTVYRLLKAgVDPDKLDAIFLSHFHLDHIGGLPTLlfarryGGRKKPLTIYGPKgikef 94

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446436140 105 ------IAVPEIQEMYKLHNRkfLVVKDGDTLDIGGKTLKFKETpyLHTEETM----------ITYC 155
Cdd:cd16272   95 lekllnFPVEILPLGFPLEIE--ELEEGGEVLELGDLKVEAFPV--KHSVESLgyrieaegksIVYS 157
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 70-166 4.65e-03

DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 441904 [Multi-domain]  Cd Length: 253  Bit Score: 38.30  E-value: 4.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140  70 QEIQYIVVNHTEPDHSGGLAALASRATNATIVCTEIAVP-----EIQEMYKLHNRKFLVVKDGDTLDIGGKTLKFketpy 144
Cdd:COG2333   51 RRLDLLVLTHPDADHIGGLAAVLEAFPVGRVLVSGPPDTsetyeRLLEALKEKGIPVRPCRAGDTWQLGGVRFEV----- 125

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 446436140 145 LHTEETMITY-------CV------EDKILFPCDI 166
Cdd:COG2333  126 LWPPEDLLEGsdennnsLVlrltygGFSFLLTGDA 160
Flavodoxin_5 pfam12724
Flavodoxin domain; This is a family of flavodoxins. Flavodoxins are electron transfer proteins ...
 253-324 7.51e-03

Flavodoxin domain; This is a family of flavodoxins. Flavodoxins are electron transfer proteins that carry a molecule of non-covalently bound FMN.


Pssm-ID: 463681 [Multi-domain]  Cd Length: 144  Bit Score: 36.86  E-value: 7.51e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446436140  253 IVYTTIKNNTKKVANIIKETLEADNIHVTVFNADKSKKLEvlksiqEADAVFIGSSTRYADMIGNLEEILKE 324
Cdd:pfam12724   2 ILYSSRDGQTKKIAERIAEELREEGELVDVEDVEAGEDLS------SYDAVVIGASIYYGKHLPELRQFVTK 67
metallo-hydrolase-like_MBL-fold cd16276
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 69-231 8.27e-03

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


Pssm-ID: 293834 [Multi-domain]  Cd Length: 188  Bit Score: 37.18  E-value: 8.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140  69 PQEIQYIVVNHTEPDHSGGLAALASRatNATIVCTEIAVpEIQEMYKLHNRKF--LVVKDGDTLDIGGKTLKFKETPYLH 146
Cdd:cd16276   43 DKPVTHVVYSHNHADHIGGASIFKDE--GATIIAHEATA-ELLKRNPDPKRPVptVTFDDEYTLEVGGQTLELSYFGPNH 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446436140 147 TEETMITYCVEDKILFPCDIfsthiandeIFSDKA---NVDITEDFIGYYNAiihpHRRyvrtlieaLKDLDVQMIAPSH 223
Cdd:cd16276  120 GPGNIVIYLPKQKVLMAVDL---------INPGWVpffNFAGSEDIPGYIEA----LDE--------LLEYDFDTFVGGH 178

                        170
                 ....*....|
gi 446436140 224 GYIL--RQDI 231
Cdd:cd16276  179 GNRLgtREDV 188
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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