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Conserved domains on  [gi|489523693|ref|WP_003428474|]
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FprA family A-type flavoprotein [Clostridioides difficile]

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];
3-396 3.04e-171

Flavorubredoxin [Energy production and conversion];


:

Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 483.56  E-value: 3.04e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523693   3 KVFEVKKDIYFTGVVDEGLKVFDIIMETEFGTTYNSYLIKDEKTVLFDTVKANFKDEFLSNLSEVTDIAKIDYVVIHHTE 82
Cdd:COG0426    1 QAVEIAHGVYWVGVLDWDRRLFEGEYPTPRGTTYNSYLIVDEKTALIDTVGESFFEEFLENLSKVIDPKKIDYIIVNHQE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523693  83 PDHAGSLKYLLDINPNIEVYCTKAAKLYLDGQINRP-FNCHVIKDGEILNIGKRNLRFITAPFLHWVDTMFTYIEEDKTL 161
Cdd:COG0426   81 PDHSGSLPELLELAPNAKIVCSKKAARFLPHFYGIPdFRFIVVKEGDTLDLGGHTLQFIPAPMLHWPDTMFTYDPEDKIL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523693 162 LTCDAFGCHFAS---VDAEVvnSEDYLKSAKHYYDCIVKPFAKHVLSAVDKVVGLNIefDTILTSHGPMLTKDPMAAVKR 238
Cdd:COG0426  161 FSGDAFGSHGASdelFDDEV--DEHLEEEARRYYANIMMPFSKQVLKALKKVRGLDI--DMIAPSHGPIWRGNPKEILDW 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523693 239 YVEWSTEAVnttnQNQVSIFYLSAYSNTLEMAKKIKEGLDKEGAKAELYDLEDMTLTEMHDTLVVSKVILLGSPTINKTM 318
Cdd:COG0426  237 YRKWSSYQP----EKKVVIVYASMYGNTEKMAEAIAEGLTEEGVKVKLYDLEKTDPSEIITEIFDAKGIVIGSPTYNGGA 312
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489523693 319 VKPMWDLFSVIDPMANQGKIAGVFGSFGWSGEGITMAETLLKSMSFKMPVESLKKKFFPSEETLKECMAFGAEFAKLV 396
Cdd:COG0426  313 FPPIADLLGYLKGLAPKNKLAGAFGSYGWSGEAVKLLEEKLEDAGFEVVFEPLRVKFKPTEEDLKKCEELGTDLAQKL 390
 
Name Accession Description Interval E-value
NorV COG0426
Flavorubredoxin [Energy production and conversion];
3-396 3.04e-171

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 483.56  E-value: 3.04e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523693   3 KVFEVKKDIYFTGVVDEGLKVFDIIMETEFGTTYNSYLIKDEKTVLFDTVKANFKDEFLSNLSEVTDIAKIDYVVIHHTE 82
Cdd:COG0426    1 QAVEIAHGVYWVGVLDWDRRLFEGEYPTPRGTTYNSYLIVDEKTALIDTVGESFFEEFLENLSKVIDPKKIDYIIVNHQE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523693  83 PDHAGSLKYLLDINPNIEVYCTKAAKLYLDGQINRP-FNCHVIKDGEILNIGKRNLRFITAPFLHWVDTMFTYIEEDKTL 161
Cdd:COG0426   81 PDHSGSLPELLELAPNAKIVCSKKAARFLPHFYGIPdFRFIVVKEGDTLDLGGHTLQFIPAPMLHWPDTMFTYDPEDKIL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523693 162 LTCDAFGCHFAS---VDAEVvnSEDYLKSAKHYYDCIVKPFAKHVLSAVDKVVGLNIefDTILTSHGPMLTKDPMAAVKR 238
Cdd:COG0426  161 FSGDAFGSHGASdelFDDEV--DEHLEEEARRYYANIMMPFSKQVLKALKKVRGLDI--DMIAPSHGPIWRGNPKEILDW 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523693 239 YVEWSTEAVnttnQNQVSIFYLSAYSNTLEMAKKIKEGLDKEGAKAELYDLEDMTLTEMHDTLVVSKVILLGSPTINKTM 318
Cdd:COG0426  237 YRKWSSYQP----EKKVVIVYASMYGNTEKMAEAIAEGLTEEGVKVKLYDLEKTDPSEIITEIFDAKGIVIGSPTYNGGA 312
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489523693 319 VKPMWDLFSVIDPMANQGKIAGVFGSFGWSGEGITMAETLLKSMSFKMPVESLKKKFFPSEETLKECMAFGAEFAKLV 396
Cdd:COG0426  313 FPPIADLLGYLKGLAPKNKLAGAFGSYGWSGEAVKLLEEKLEDAGFEVVFEPLRVKFKPTEEDLKKCEELGTDLAQKL 390
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
6-243 2.10e-114

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: 333.30  E-value: 2.10e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523693   6 EVKKDIYFTGVVDEGLKVFDIIMETEFGTTYNSYLIKDEKTVLFDTVKANFKDEFLSNLSEVTDIAKIDYVVIHHTEPDH 85
Cdd:cd07709    2 EIADDIYWVGVNDWDLRLFEGEYPTPRGTSYNSYLIKDEKTALIDTVKEPFFDEFLENLEEVIDPRKIDYIVVNHQEPDH 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523693  86 AGSLKYLLDINPNIEVYCTKAAKLYLDGQ-INRPFNCHVIKDGEILNIGKRNLRFITAPFLHWVDTMFTYIEEDKTLLTC 164
Cdd:cd07709   82 SGSLPELLELAPNAKIVCSKKAARFLKHFyPGIDERFVVVKDGDTLDLGKHTLKFIPAPMLHWPDTMVTYDPEDKILFSG 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489523693 165 DAFGCHFASVDAEVVNSEDYLKSAKHYYDCIVKPFAKHVLSAVDKVVGLNIEfdTILTSHGPMLTKDPMAAVKRYVEWS 243
Cdd:cd07709  162 DAFGAHGASGELFDDEVEDYLEEARRYYANIMGPFSKQVRKALEKLEALDIK--MIAPSHGPIWRKDPGEIIDLYRDWS 238
PRK11921 PRK11921
anaerobic nitric oxide reductase flavorubredoxin;
5-397 1.53e-106

anaerobic nitric oxide reductase flavorubredoxin;


Pssm-ID: 237023 [Multi-domain]  Cd Length: 394  Bit Score: 319.33  E-value: 1.53e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523693   5 FEVKKDIYFTGVVDEGLKVFD-IIMETEFGTTYNSYLIKDEKTVLFDTVKANFKDEFLSNLSEVTDIAKIDYVVIHHTEP 83
Cdd:PRK11921   1 FKINDNVTWVGKIDWELRKFHgEEYSTHRGSSYNSYLIKDEKTVLIDTVWQPFAKEFVENLKKEIDLDKIDYIVANHGEI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523693  84 DHAGSLKYLLDINPNIEVYCTKAAKLYLDGQINRPFNCHVIKDGEILNIGKRNLRFITAPFLHWVDTMFTYIEEDKTLLT 163
Cdd:PRK11921  81 DHSGALPELMKEIPDTPIYCTKNGAKSLKGHYHQDWNFVVVKTGDRLEIGSNELIFIEAPMLHWPDSMFTYLTGDNILFS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523693 164 CDAFGCHFAS--VDAEVVNSEDYLKSAKHYYDCIVKPFAKHVLSAVDKVVGLNIEFDTILTSHGPMLTKDPMAAVKRYVE 241
Cdd:PRK11921 161 NDAFGQHYASelMYNDLVDQGELYQEAIKYYANILTPFSPLVIKKIEEILSLNLPVDMICPSHGVIWRDNPLQIVEKYLE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523693 242 WSteavNTTNQNQVSIFYLSAYSNTLEMAKKIKEGLDK--EGAKAELYDLEDMTLTEMHDTLVVSKVILLGSPTINKTMV 319
Cdd:PRK11921 241 WA----ANYQENQVTILYDTMWNSTRRMAEAIAEGIKKanKDVTVKLYNSAKSDKNDIITEVFKSKAILVGSSTINRGIL 316
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489523693 320 KPMWDLFSVIDPMANQGKIAGVFGSFGWSGEGITMAETLLKSMSFKMPVESLKKKFFPSEETLKECMAFGAEFAKLVK 397
Cdd:PRK11921 317 SSTAAILEEIKGLGFKNKKAAAFGSYGWSGESVKIITERLKKAGFEIVNDGIRELWNPDDEALDRCRSFGENFAESLK 394
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
37-189 2.59e-23

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: 95.70  E-value: 2.59e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523693    37 NSYLIKDE-KTVLFDTVkANFKDEFLSNLSEVtDIAKIDYVVIHHTEPDHAGSLKYLLDInPNIEVYCTKAAKLYLDGQI 115
Cdd:smart00849   1 NSYLVRDDgGAILIDTG-PGEAEDLLAELKKL-GPKKIDAIILTHGHPDHIGGLPELLEA-PGAPVYAPEGTAELLKDLL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523693   116 NRPFNC----------HVIKDGEILNIGKRNLRFITAPfLHWVDTMFTYIEEDKTLLTCDAFGCHFAS---VDAEVVNSE 182
Cdd:smart00849  78 ALLGELgaeaepappdRTLKDGDELDLGGGELEVIHTP-GHTPGSIVLYLPEGKILFTGDLLFAGGDGrtlVDGGDAAAS 156

                   ....*..
gi 489523693   183 DYLKSAK 189
Cdd:smart00849 157 DALESLL 163
flav_short TIGR01753
flavodoxin, short chain; Flavodoxins are small redox-active proteins with a flavin ...
255-393 7.44e-18

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: 79.30  E-value: 7.44e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523693  255 VSIFYLSAYSNTLEMAKKIKEGLDKEGAKAELYDLEDMTLTEmhdtLVVSKVILLGSPTINKTMVKP--MWDLFSVIDPM 332
Cdd:TIGR01753   1 ILIVYASMTGNTEEMANIIAEGLKEAGAEVDLLEVADADAED----LLSYDAVLLGCSTWGDEDLEQddFEPFFEELEDI 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489523693  333 ANQGKIAGVFGSFGWSGEG---ITMAETLLKSMSFKMPVESLKKKFFPSEETLKECMAFGAEFA 393
Cdd:TIGR01753  77 DLGGKKVALFGSGDWGYEFceaVDDWEERLKEAGATIIAEGLKVDGDPEEEDLDKCREFAKDLA 140
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
37-224 8.07e-11

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 60.85  E-value: 8.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523693   37 NSYLIK-DEKTVLFDTVKANFKDEFLSNLSEVTDIAKIDYVVIHHTEPDHAGSLKYLLDINPNIEVYCTKAAKLYLDGQ- 114
Cdd:pfam00753   7 NSYLIEgGGGAVLIDTGGSAEAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARELLDEEl 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523693  115 ------------INRPFNCHVIKDGEILNIGKRNLRFITAPFLHWVDTMFTYIEEDKTLLTCDA-FGCHFASVDAEVVNS 181
Cdd:pfam00753  87 glaasrlglpgpPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLlFAGEIGRLDLPLGGL 166
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 489523693  182 EDYLKSAKhyydcivkpfaKHVLSAVDKVVGLNIEfdTILTSH 224
Cdd:pfam00753 167 LVLHPSSA-----------ESSLESLLKLAKLKAA--VIVPGH 196
 
Name Accession Description Interval E-value
NorV COG0426
Flavorubredoxin [Energy production and conversion];
3-396 3.04e-171

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 483.56  E-value: 3.04e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523693   3 KVFEVKKDIYFTGVVDEGLKVFDIIMETEFGTTYNSYLIKDEKTVLFDTVKANFKDEFLSNLSEVTDIAKIDYVVIHHTE 82
Cdd:COG0426    1 QAVEIAHGVYWVGVLDWDRRLFEGEYPTPRGTTYNSYLIVDEKTALIDTVGESFFEEFLENLSKVIDPKKIDYIIVNHQE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523693  83 PDHAGSLKYLLDINPNIEVYCTKAAKLYLDGQINRP-FNCHVIKDGEILNIGKRNLRFITAPFLHWVDTMFTYIEEDKTL 161
Cdd:COG0426   81 PDHSGSLPELLELAPNAKIVCSKKAARFLPHFYGIPdFRFIVVKEGDTLDLGGHTLQFIPAPMLHWPDTMFTYDPEDKIL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523693 162 LTCDAFGCHFAS---VDAEVvnSEDYLKSAKHYYDCIVKPFAKHVLSAVDKVVGLNIefDTILTSHGPMLTKDPMAAVKR 238
Cdd:COG0426  161 FSGDAFGSHGASdelFDDEV--DEHLEEEARRYYANIMMPFSKQVLKALKKVRGLDI--DMIAPSHGPIWRGNPKEILDW 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523693 239 YVEWSTEAVnttnQNQVSIFYLSAYSNTLEMAKKIKEGLDKEGAKAELYDLEDMTLTEMHDTLVVSKVILLGSPTINKTM 318
Cdd:COG0426  237 YRKWSSYQP----EKKVVIVYASMYGNTEKMAEAIAEGLTEEGVKVKLYDLEKTDPSEIITEIFDAKGIVIGSPTYNGGA 312
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489523693 319 VKPMWDLFSVIDPMANQGKIAGVFGSFGWSGEGITMAETLLKSMSFKMPVESLKKKFFPSEETLKECMAFGAEFAKLV 396
Cdd:COG0426  313 FPPIADLLGYLKGLAPKNKLAGAFGSYGWSGEAVKLLEEKLEDAGFEVVFEPLRVKFKPTEEDLKKCEELGTDLAQKL 390
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
6-243 2.10e-114

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: 333.30  E-value: 2.10e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523693   6 EVKKDIYFTGVVDEGLKVFDIIMETEFGTTYNSYLIKDEKTVLFDTVKANFKDEFLSNLSEVTDIAKIDYVVIHHTEPDH 85
Cdd:cd07709    2 EIADDIYWVGVNDWDLRLFEGEYPTPRGTSYNSYLIKDEKTALIDTVKEPFFDEFLENLEEVIDPRKIDYIVVNHQEPDH 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523693  86 AGSLKYLLDINPNIEVYCTKAAKLYLDGQ-INRPFNCHVIKDGEILNIGKRNLRFITAPFLHWVDTMFTYIEEDKTLLTC 164
Cdd:cd07709   82 SGSLPELLELAPNAKIVCSKKAARFLKHFyPGIDERFVVVKDGDTLDLGKHTLKFIPAPMLHWPDTMVTYDPEDKILFSG 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489523693 165 DAFGCHFASVDAEVVNSEDYLKSAKHYYDCIVKPFAKHVLSAVDKVVGLNIEfdTILTSHGPMLTKDPMAAVKRYVEWS 243
Cdd:cd07709  162 DAFGAHGASGELFDDEVEDYLEEARRYYANIMGPFSKQVRKALEKLEALDIK--MIAPSHGPIWRKDPGEIIDLYRDWS 238
PRK11921 PRK11921
anaerobic nitric oxide reductase flavorubredoxin;
5-397 1.53e-106

anaerobic nitric oxide reductase flavorubredoxin;


Pssm-ID: 237023 [Multi-domain]  Cd Length: 394  Bit Score: 319.33  E-value: 1.53e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523693   5 FEVKKDIYFTGVVDEGLKVFD-IIMETEFGTTYNSYLIKDEKTVLFDTVKANFKDEFLSNLSEVTDIAKIDYVVIHHTEP 83
Cdd:PRK11921   1 FKINDNVTWVGKIDWELRKFHgEEYSTHRGSSYNSYLIKDEKTVLIDTVWQPFAKEFVENLKKEIDLDKIDYIVANHGEI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523693  84 DHAGSLKYLLDINPNIEVYCTKAAKLYLDGQINRPFNCHVIKDGEILNIGKRNLRFITAPFLHWVDTMFTYIEEDKTLLT 163
Cdd:PRK11921  81 DHSGALPELMKEIPDTPIYCTKNGAKSLKGHYHQDWNFVVVKTGDRLEIGSNELIFIEAPMLHWPDSMFTYLTGDNILFS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523693 164 CDAFGCHFAS--VDAEVVNSEDYLKSAKHYYDCIVKPFAKHVLSAVDKVVGLNIEFDTILTSHGPMLTKDPMAAVKRYVE 241
Cdd:PRK11921 161 NDAFGQHYASelMYNDLVDQGELYQEAIKYYANILTPFSPLVIKKIEEILSLNLPVDMICPSHGVIWRDNPLQIVEKYLE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523693 242 WSteavNTTNQNQVSIFYLSAYSNTLEMAKKIKEGLDK--EGAKAELYDLEDMTLTEMHDTLVVSKVILLGSPTINKTMV 319
Cdd:PRK11921 241 WA----ANYQENQVTILYDTMWNSTRRMAEAIAEGIKKanKDVTVKLYNSAKSDKNDIITEVFKSKAILVGSSTINRGIL 316
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489523693 320 KPMWDLFSVIDPMANQGKIAGVFGSFGWSGEGITMAETLLKSMSFKMPVESLKKKFFPSEETLKECMAFGAEFAKLVK 397
Cdd:PRK11921 317 SSTAAILEEIKGLGFKNKKAAAFGSYGWSGESVKIITERLKKAGFEIVNDGIRELWNPDDEALDRCRSFGENFAESLK 394
PRK05452 PRK05452
anaerobic nitric oxide reductase flavorubredoxin; Provisional
7-394 1.02e-83

anaerobic nitric oxide reductase flavorubredoxin; Provisional


Pssm-ID: 235475 [Multi-domain]  Cd Length: 479  Bit Score: 263.54  E-value: 1.02e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523693   7 VKKDIYFTGVVDEGLKVFDiimETEF----GTTYNSYLIKDEKTVLFDTVKANFKDEFLSNLSEVTDIAKIDYVVIHHTE 82
Cdd:PRK05452   5 VKNNIHWVGQRDWEVRDFH---GTEYktlrGSSYNSYLIREEKNVLIDTVDHKFSREFVQNLRNEIDLADIDYIVINHAE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523693  83 PDHAGSLKYLLDINPNIEVYCTKAAKLYLDGQINRP-FNCHVIKDGEILNIGK-RNLRFITAPFLHWVDTMFTYIEEDKT 160
Cdd:PRK05452  82 EDHAGALTELMAQIPDTPIYCTANAIDSINGHHHHPeWNFNVVKTGDTLDIGNgKQLIFVETPMLHWPDSMMTYLTGDAV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523693 161 LLTCDAFGCHFAsvDAEVVNSE----DYLKSAKHYYDCIVKPFAKHVLSAVDKVVGLNIEFDTILTSHGPMLTKDPMAAV 236
Cdd:PRK05452 162 LFSNDAFGQHYC--DEHLFNDEvdqtELFEQCQRYYANILTPFSRLVTPKITEILGFNLPVDMIATSHGVVWRDNPTQIV 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523693 237 KRYVEWSteavNTTNQNQVSIFYLSAYSNTLEMAKKIKEGLDK--EGAKAELYDLEDMTLTEMHDTLVVSKVILLGSPTI 314
Cdd:PRK05452 240 ELYLKWA----ADYQEDRITIFYDTMSNNTRMMADAIAQGIAEvdPRVAVKIFNVARSDKNEILTNVFRSKGVLVGSSTM 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523693 315 NKTMVKPMWDLFSVIDPMANQGKIAGVFGSFGWSGEGITMAETLLKSMSFKMPVeSLKKKFFPSEETLKECMAFGAEFAK 394
Cdd:PRK05452 316 NNVMMPKIAGLLEEITGLRFRNKRASAFGSHGWSGGAVDRLSTRLQDAGFEMSL-SLKAKWRPDQDALELCREHGREIAR 394
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
37-189 2.59e-23

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: 95.70  E-value: 2.59e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523693    37 NSYLIKDE-KTVLFDTVkANFKDEFLSNLSEVtDIAKIDYVVIHHTEPDHAGSLKYLLDInPNIEVYCTKAAKLYLDGQI 115
Cdd:smart00849   1 NSYLVRDDgGAILIDTG-PGEAEDLLAELKKL-GPKKIDAIILTHGHPDHIGGLPELLEA-PGAPVYAPEGTAELLKDLL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523693   116 NRPFNC----------HVIKDGEILNIGKRNLRFITAPfLHWVDTMFTYIEEDKTLLTCDAFGCHFAS---VDAEVVNSE 182
Cdd:smart00849  78 ALLGELgaeaepappdRTLKDGDELDLGGGELEVIHTP-GHTPGSIVLYLPEGKILFTGDLLFAGGDGrtlVDGGDAAAS 156

                   ....*..
gi 489523693   183 DYLKSAK 189
Cdd:smart00849 157 DALESLL 163
flav_short TIGR01753
flavodoxin, short chain; Flavodoxins are small redox-active proteins with a flavin ...
255-393 7.44e-18

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: 79.30  E-value: 7.44e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523693  255 VSIFYLSAYSNTLEMAKKIKEGLDKEGAKAELYDLEDMTLTEmhdtLVVSKVILLGSPTINKTMVKP--MWDLFSVIDPM 332
Cdd:TIGR01753   1 ILIVYASMTGNTEEMANIIAEGLKEAGAEVDLLEVADADAED----LLSYDAVLLGCSTWGDEDLEQddFEPFFEELEDI 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489523693  333 ANQGKIAGVFGSFGWSGEG---ITMAETLLKSMSFKMPVESLKKKFFPSEETLKECMAFGAEFA 393
Cdd:TIGR01753  77 DLGGKKVALFGSGDWGYEFceaVDDWEERLKEAGATIIAEGLKVDGDPEEEDLDKCREFAKDLA 140
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
37-248 3.41e-13

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: 68.18  E-value: 3.41e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523693  37 NSYLIKD-EKTVLFDT-VKANFKDEFLSNLSEVTdiAKIDYVVIHHTEPDHAGSLKYLLDiNPNIEVYCTKAAKLYLDGQ 114
Cdd:COG0491   16 NSYLIVGgDGAVLIDTgLGPADAEALLAALAALG--LDIKAVLLTHLHPDHVGGLAALAE-AFGAPVYAHAAEAEALEAP 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523693 115 INRPFNC-------HVIKDGEILNIGKRNLRFITAP--------FlhwvdtmftYIEEDKTLLTCDA-FGCHFASVDAEV 178
Cdd:COG0491   93 AAGALFGrepvppdRTLEDGDTLELGGPGLEVIHTPghtpghvsF---------YVPDEKVLFTGDAlFSGGVGRPDLPD 163
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523693 179 VNSEDYLKSakhyydcivkpfakhvlsaVDKVvgLNIEFDTILTSHGPMLTKDPMAAVKRYVEWSTEAVN 248
Cdd:COG0491  164 GDLAQWLAS-------------------LERL--LALPPDLVIPGHGPPTTAEAIDYLEELLAALGERAN 212
FldA COG0716
Flavodoxin [Energy production and conversion]; Flavodoxin is part of the Pathway/BioSystem: ...
257-392 9.43e-13

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


Pssm-ID: 440480 [Multi-domain]  Cd Length: 135  Bit Score: 64.92  E-value: 9.43e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523693 257 IFYLSAYSNTLEMAKKIKEGLDKEGakAELYDLEDMTLTEMHDtlvvSKVILLGSPTINKTMVKPMWDLFSVIDPMANqG 336
Cdd:COG0716    3 IVYGSTTGNTEKVAEAIAEALGAAG--VDLFEIEDADLDDLED----YDLLILGTPTWAGELPDDWEDFLEELKEDLS-G 75
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489523693 337 KIAGVFGSFGWS--GEGITMAETLLKSMSFKMpVESL--KKKFFP-SEETLKECMAFGAEF 392
Cdd:COG0716   76 KKVALFGTGDSSgyGDALGELKELLEEKGAKV-VGGYdfEGSKAPdAEDTEERAEEWLKQL 135
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
37-163 6.18e-11

mainly hydrolytic enzymes and related proteins which carry out various biological functions; MBL-fold metallohydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases which can catalyze the hydrolysis of a wide range of beta-lactam antibiotics, hydroxyacylglutathione hydrolases (also called glyoxalase II) which hydrolyze S-d-lactoylglutathione to d-lactate in the second step of the glycoxlase system, AHL lactonases which catalyze the hydrolysis and opening of the homoserine lactone rings of acyl homoserine lactones (AHLs), persulfide dioxygenase which catalyze the oxidation of glutathione persulfide to glutathione and persulfite in the mitochondria, flavodiiron proteins which catalyze the reduction of oxygen and/or nitric oxide to water or nitrous oxide respectively, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J which has both 5'-3' exoribonucleolytic and endonucleolytic activity and ribonuclease Z which catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors, cyclic nucleotide phosphodiesterases which decompose cyclic adenosine and guanosine 3', 5'-monophosphate (cAMP and cGMP) respectively, insecticide hydrolases, and proteins required for natural transformation competence. The diversity of biological roles is reflected in variations in the active site metallo-chemistry, for example classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, human persulfide dioxygenase ETHE1 is a mono-iron binding member of the superfamily; Arabidopsis thaliana hydroxyacylglutathione hydrolases incorporates iron, manganese, and zinc in its dinuclear metal binding site, and flavodiiron proteins contains a diiron site.


Pssm-ID: 293792 [Multi-domain]  Cd Length: 188  Bit Score: 61.15  E-value: 6.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523693  37 NSYLIKDE--KTVLFDTVkANFKDEFLSNLSEvtDIAKIDYVVIHHTEPDHAGSLKYLLDiNPNIEVYCTKAAKLYLD-- 112
Cdd:cd06262   11 NCYLVSDEegEAILIDPG-AGALEKILEAIEE--LGLKIKAILLTHGHFDHIGGLAELKE-APGAPVYIHEADAELLEdp 86
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523693 113 ---------GQINRPFNCHVIKDGEILNIGKRNLRFITAPfLHWVDTMFTYIEEDKTLLT 163
Cdd:cd06262   87 elnlaffggGPLPPPEPDILLEDGDTIELGGLELEVIHTP-GHTPGSVCFYIEEEGVLFT 145
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
37-224 8.07e-11

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 60.85  E-value: 8.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523693   37 NSYLIK-DEKTVLFDTVKANFKDEFLSNLSEVTDIAKIDYVVIHHTEPDHAGSLKYLLDINPNIEVYCTKAAKLYLDGQ- 114
Cdd:pfam00753   7 NSYLIEgGGGAVLIDTGGSAEAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARELLDEEl 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523693  115 ------------INRPFNCHVIKDGEILNIGKRNLRFITAPFLHWVDTMFTYIEEDKTLLTCDA-FGCHFASVDAEVVNS 181
Cdd:pfam00753  87 glaasrlglpgpPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLlFAGEIGRLDLPLGGL 166
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 489523693  182 EDYLKSAKhyydcivkpfaKHVLSAVDKVVGLNIEfdTILTSH 224
Cdd:pfam00753 167 LVLHPSSA-----------ESSLESLLKLAKLKAA--VIVPGH 196
Flavodoxin_1 pfam00258
Flavodoxin;
257-389 1.21e-09

Flavodoxin;


Pssm-ID: 425562 [Multi-domain]  Cd Length: 142  Bit Score: 56.22  E-value: 1.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523693  257 IFYLSAYSNTLEMAKKIKEGLDKEGAKAELYDL--EDMTLTEMHDTLVVSKVILL---GSPTINKtmvKPMWD---LFSV 328
Cdd:pfam00258   1 IFYGSQTGNTEKLAEAIAEGLGEAGFEVDVVDLddVDETLSEIEEEDLLLVVVSTwgeGEPPDNA---KPFVDwllLFGT 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489523693  329 IDPMANQGKIAGVFGSFGWSGEG----ITMAETLLKSMSFKMPVESLKKKFFPSEETLKECMAFG 389
Cdd:pfam00258  78 LEDGDLSGLKYAVFGLGDSGYEGfcgaAKKLDEKLSELGASRVGPLGEGDEDPQEDGLEEAFEAW 142
PRK05568 PRK05568
flavodoxin; Provisional
254-394 4.71e-09

flavodoxin; Provisional


Pssm-ID: 235508 [Multi-domain]  Cd Length: 142  Bit Score: 54.43  E-value: 4.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523693 254 QVSIFYLSAYSNTLEMAKKIKEGLDKEGAKAELYDLEDMTLTEMHDtlvvSKVILLGSP-----TINKTMVKPMwdlfsv 328
Cdd:PRK05568   3 KINIIYWSGTGNTEAMANLIAEGAKENGAEVKLLNVSEASVDDVKG----ADVVALGSPamgdeVLEEGEMEPF------ 72
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489523693 329 IDPMAN--QGKIAGVFGSFGW-SGEGITMAETLLKSMSFKMPVESLKKKFFPSEETLKECMAFGAEFAK 394
Cdd:PRK05568  73 VESISSlvKGKKLVLFGSYGWgDGEWMRDWVERMEGYGANLVNEGLIVNNTPEGEGIEKCKALGEALAK 141
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
38-143 5.05e-09

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


Pssm-ID: 293799  Cd Length: 269  Bit Score: 56.86  E-value: 5.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523693  38 SYLIK-DEKTVLFDTvkaNFKDEFLSNLSE--VtDIAKIDYVVIHHTEPDHAGSLKYLLDINPNIEVYCTKAAKLYLDGQ 114
Cdd:cd07713   22 SLLIEtEGKKILFDT---GQSGVLLHNAKKlgI-DLSDIDAVVLSHGHYDHTGGLKALLELNPKAPVYAHPDAFEPRYSK 97
                         90       100
                 ....*....|....*....|....*....
gi 489523693 115 INRPFNCHVIKDGEILNIGKRnLRFITAP 143
Cdd:cd07713   98 RGGGKKGIGIGREELEKAGAR-LVLVEEP 125
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
37-166 6.78e-09

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: 55.00  E-value: 6.78e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523693  37 NSYLIKD-EKTVLFDTVKANFKD--EFLSNLSE-VTDIAKIDYVVIHHTEPDHAGSLKYLLDINpNIEVYC--TKAakly 110
Cdd:cd07725   16 NVYLLRDgDETTLIDTGLATEEDaeALWEGLKElGLKPSDIDRVLLTHHHPDHIGLAGKLQEKS-GATVYIldVTP---- 90
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489523693 111 ldgqinrpfnchvIKDGEILNIGKRNLRFITAPFlHWVDTMFTYIEEDKTLLTCDA 166
Cdd:cd07725   91 -------------VKDGDKIDLGGLRLKVIETPG-HTPGHIVLYDEDRRELFVGDA 132
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
31-225 1.50e-08

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: 54.53  E-value: 1.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523693  31 EFGTTYNSYLIKDEK-TVLFDTVKANFKDEFLSNLSEV-TDIAKIDYVVIHHTEPDHAGSLKYLLDInPNIEVYCTKAAK 108
Cdd:cd07721    6 PLLPPVNAYLIEDDDgLTLIDTGLPGSAKRILKALRELgLSPKDIRRILLTHGHIDHIGSLAALKEA-PGAPVYAHEREA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523693 109 LYLDGQINRPFNC--------------------HVIKDGEILNIGKRnlrfitapfLHWVDT--------MFtYIEEDKT 160
Cdd:cd07721   85 PYLEGEKPYPPPVrlgllgllspllpvkpvpvdRTLEDGDTLDLAGG---------LRVIHTpghtpghiSL-YLEEDGV 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489523693 161 LLTCDAfgchFASVDAEVVnsedyLKSAKHYYDcivkpfAKHVLSAVDKVvgLNIEFDTILTSHG 225
Cdd:cd07721  155 LIAGDA----LVTVGGELV-----PPPPPFTWD------MEEALESLRKL--AELDPEVLAPGHG 202
PRK06756 PRK06756
flavodoxin; Provisional
254-396 7.68e-08

flavodoxin; Provisional


Pssm-ID: 168663 [Multi-domain]  Cd Length: 148  Bit Score: 51.42  E-value: 7.68e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523693 254 QVSIFYLSAYSNTLEMAKKIKEGLDKEGAKAELYDLED---MTLTEMHDTlvvskvILLGSPTI-NKTMVKPMWDLFSVI 329
Cdd:PRK06756   3 KLVMIFASMSGNTEEMADHIAGVIRETENEIEVIDIMDspeASILEQYDG------IILGAYTWgDGDLPDDFLDFYDAM 76
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489523693 330 DPMANQGKIAGVFGSFGWSGEGITMAETLL----KSMSFKMPVESLKKKFFPSEETLKECMAFGAEFAKLV 396
Cdd:PRK06756  77 DSIDLTGKKAAVFGSCDSAYPKYGVAVDILieklQERGAAVVLEGLKVELTPEDEDVEKCLQFGAEFVKHL 147
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
38-168 1.95e-07

uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo hydrolase domain; This subgroup includes the uncharacterized Sulfolobus tokodaii ST1585 protein. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293812 [Multi-domain]  Cd Length: 215  Bit Score: 51.34  E-value: 1.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523693  38 SYLIKDE-KTVLFDTVKANFKDEFLSNLSEVT-DIAKIDYVVIHHTEPDHAGSLKYLLDINPNIEVYC-TKAAK------ 108
Cdd:cd07726   18 SYLLDGEgRPALIDTGPSSSVPRLLAALEALGiAPEDVDYIILTHIHLDHAGGAGLLAEALPNAKVYVhPRGARhlidps 97
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489523693 109 --------------LYLDGQInRPF---NCHVIKDGEILNIGKRNLRFITAPFlHWVDTMFTYIEEDKTLLTCDAFG 168
Cdd:cd07726   98 klwasaravygdeaDRLGGEI-LPVpeeRVIVLEDGETLDLGGRTLEVIDTPG-HAPHHLSFLDEESDGLFTGDAAG 172
PRK05569 PRK05569
flavodoxin; Provisional
254-394 2.69e-07

flavodoxin; Provisional


Pssm-ID: 135442 [Multi-domain]  Cd Length: 141  Bit Score: 49.45  E-value: 2.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523693 254 QVSIFYLSAYSNTLEMAKKIKEGLDKEGAKAELYDLEDMTLtemHDTLVVSKVIlLGSPTINKTMV-----KPMWDLFSV 328
Cdd:PRK05569   3 KVSIIYWSCGGNVEVLANTIADGAKEAGAEVTIKHVADAKV---EDVLEADAVA-FGSPSMDNNNIeqeemAPFLDQFKL 78
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489523693 329 idpMANQGKIAGVFGSFGW-SGEGITMAETLLKSMSFKMpVESLKKKFFPSEETLKECMAFGAEFAK 394
Cdd:PRK05569  79 ---TPNENKKCILFGSYGWdNGEFMKLWKDRMKDYGFNV-IGDLAVNESPNKEELNSAKELGKKLAK 141
WrbA COG0655
Multimeric flavodoxin WrbA, includes NAD(P)H:quinone oxidoreductase [Energy production and ...
257-397 1.18e-06

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


Pssm-ID: 440420 [Multi-domain]  Cd Length: 181  Bit Score: 48.39  E-value: 1.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523693 257 IFY-LSAYSNTLEMAKKIKEGLDKEGAKAELYDLEDMT------------------LTEMHDTLVVSKVILLGSPTINKT 317
Cdd:COG0655    5 INGsPRKNGNTAALAEAVAEGAEEAGAEVELIRLADLDikpcigcggtgkcvikddMNAIYEKLLEADGIIFGSPTYFGN 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523693 318 M---VKPMWD-LFSVIDPMAN-QGKIAGVFGSfGWSGEGITMAETLLKSMS-FKMPVESL---------KKKFFPSEETL 382
Cdd:COG0655   85 MsaqLKAFIDrLYALWAKGKLlKGKVGAVFTT-GGHGGAEATLLSLNTFLLhHGMIVVGLppygavgggGPGDVLDEEGL 163
                        170
                 ....*....|....*
gi 489523693 383 KECMAFGAEFAKLVK 397
Cdd:COG0655  164 ATARELGKRLAELAK 178
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
37-147 8.47e-06

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 46.45  E-value: 8.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523693  37 NSYLIK-DEKTVLFDTVKANFKDEFLSNLSEVTDIAKIDYVVIHHTEPDHAG--SLKYLLDinPNIEVYCTKAAKLYLDG 113
Cdd:COG2220   12 ATFLIEtGGKRILIDPVFSGRASPVNPLPLDPEDLPKIDAVLVTHDHYDHLDdaTLRALKR--TGATVVAPLGVAAWLRA 89
                         90       100       110
                 ....*....|....*....|....*....|....
gi 489523693 114 QinRPFNCHVIKDGEILNIGkrNLRFITAPFLHW 147
Cdd:COG2220   90 W--GFPRVTELDWGESVELG--GLTVTAVPARHS 119
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
32-162 9.66e-05

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Includes functionally uncharacterized Enterococcus faecalis EF2904. 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: 293818 [Multi-domain]  Cd Length: 202  Bit Score: 42.98  E-value: 9.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523693  32 FGTTYN------SYLIKDEKTVLFDTVKANFKDEFLSNLSEVTDIAKIDYVVIHHTEPDHAGSLKYLldiNPNIEVYCTK 105
Cdd:cd07732   29 FGLPLDpeskyfDEVLDFLELGLLPDIVGLYRDPLLLGGLRSEEDPSVDAVLLSHAHLDHYGLLNYL---RPDIPVYMGE 105
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489523693 106 AAKLYL-------DGQINRPFNCHVIKDGEILNIGKrnlrFITAPFLhwVD------TMFtYIE-EDKTLL 162
Cdd:cd07732  106 ATKRILkallpffGEGDPVPRNIRVFESGKSFTIGD----FTVTPYL--VDhsapgaYAF-LIEaPGKRIF 169
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
36-106 2.57e-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: 2.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523693  36 YNSYLIK-DEKTVLFDT-----VKANFKDEFLSNLSEVT--------------DIAKIDYVVIHHTEPDHAGSLKYLldi 95
Cdd:cd07729   32 VYAYLIEhPEGTILVDTgfhpdAADDPGGLELAFPPGVTeeqtleeqlarlglDPEDIDYVILSHLHFDHAGGLDLF--- 108
                         90
                 ....*....|.
gi 489523693  96 nPNIEVYCTKA 106
Cdd:cd07729  109 -PNATIIVQRA 118
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
38-143 2.94e-04

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: 40.91  E-value: 2.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523693  38 SYLIKDEKT---VLFDTVKANfkdeflsnlsEVTDIAK-----IDYVVIHHTEPDHAGSLKYLLDINPNIEVYCTKAAKL 109
Cdd:cd07723   11 IYLIVDEATgeaAVVDPGEAE----------PVLAALEkngltLTAILTTHHHWDHTGGNAELKALFPDAPVYGPAEDRI 80
                         90       100       110
                 ....*....|....*....|....*....|....
gi 489523693 110 yldgqinrPFNCHVIKDGEILNIGKRNLRFITAP 143
Cdd:cd07723   81 --------PGLDHPVKDGDEIKLGGLEVKVLHTP 106
PRK06703 PRK06703
flavodoxin; Provisional
257-393 5.89e-04

flavodoxin; Provisional


Pssm-ID: 235854 [Multi-domain]  Cd Length: 151  Bit Score: 40.13  E-value: 5.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523693 257 IFYLSAYSNTLEMAKKIKEGLDKEGAKAELYDLEDMTLTEmhdtLVVSKVILLGSPTinktmvkpmW----------DLF 326
Cdd:PRK06703   6 IAYASMSGNTEDIADLIKVSLDAFDHEVVLQEMDGMDAEE----LLAYDGIILGSYT---------WgdgdlpyeaeDFH 72
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489523693 327 SVIDPMANQGKIAGVFGSFGWS----GEGITMAETLLKSMSFKMPVESLKKKFFP-SEETLKECMAFGAEFA 393
Cdd:PRK06703  73 EDLENIDLSGKKVAVFGSGDTAyplfCEAVTIFEERLVERGAELVQEGLKIELAPeTDEDVEKCSNFAIAFA 144
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
37-224 1.25e-03

uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized human MBLAC2 and related proteins. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293798 [Multi-domain]  Cd Length: 182  Bit Score: 39.53  E-value: 1.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523693  37 NSYLIK-DEKTVLFDTvkaNFKDEFL-SNLSEVTDIAKIdyVVIHHTEPDHAGSLKYLLD--INP----NIEVYC--TKA 106
Cdd:cd07712   10 NIYLLRgRDRALLIDT---GLGIGDLkEYVRTLTDLPLL--VVATHGHFDHIGGLHEFEEvyVHPadaeILAAPDnfETL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523693 107 AKLYLDGQINRPFNCHVIKDGEILNIGKRNLRFITAPFlHWVDTMFTYIEEDKTLLTCDAFGchfasvDAEVV------N 180
Cdd:cd07712   85 TWDAATYSVPPAGPTLPLRDGDVIDLGDRQLEVIHTPG-HTPGSIALLDRANRLLFSGDVVY------DGPLImdlphsD 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 489523693 181 SEDYLKSAKhyydcivkpfakhvlsavdKVVGLNIEFDTILTSH 224
Cdd:cd07712  158 LDDYLASLE-------------------KLSKLPDEFDKVLPGH 182
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
46-158 1.44e-03

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


Pssm-ID: 432732 [Multi-domain]  Cd Length: 196  Bit Score: 39.60  E-value: 1.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523693   46 TVLFDTVKaNFKDEFLSNLSEVTDIA-KIDYVVIHHTEPDH-AGslkyLLDINP--NIEVYCTKAAKLYLDGQINRPF-- 119
Cdd:pfam12706   2 RILIDPGP-DLRQQALPALQPGRLRDdPIDAVLLTHDHYDHlAG----LLDLREgrPRPLYAPLGVLAHLRRNFPYLFll 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 489523693  120 -----NCHVIKDGEILNIGKRNLRFITAPFLHWVDTMFTYIEED 158
Cdd:pfam12706  77 ehygvRVHEIDWGESFTVGDGGLTVTATPARHGSPRGLDPNPGD 120
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
38-111 3.04e-03

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


Pssm-ID: 293853 [Multi-domain]  Cd Length: 197  Bit Score: 38.59  E-value: 3.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523693  38 SYLIK-DEKTVLFDT-VKANFKDEFLSNLSEVT-DIAKIDYVVIHHTEPDHAGSLKYLLDINPNIEVYCTKA----AKLY 110
Cdd:cd16295   14 CYLLEtGGKRILLDCgLFQGGKELEELNNEPFPfDPKEIDAVILTHAHLDHSGRLPLLVKEGFRGPIYATPAtkdlAELL 93

                 .
gi 489523693 111 L 111
Cdd:cd16295   94 L 94
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
40-89 3.13e-03

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


Pssm-ID: 293797 [Multi-domain]  Cd Length: 190  Bit Score: 38.34  E-value: 3.13e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489523693  40 LIKDE-KTVLFDTVKANFKDEFLSNLSE----VTDIakiDYVVIHHTEPDHAGSL 89
Cdd:cd07711   26 LIKDGgKNILVDTGTPWDRDLLLKALAEhglsPEDI---DYVVLTHGHPDHIGNL 77
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
38-143 6.19e-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: 293838 [Multi-domain]  Cd Length: 251  Bit Score: 37.95  E-value: 6.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523693  38 SYLIK-DEKTVLFDTVKAN-FKDEFLSNLSEV-TDIAKIDYVVIHHTEPDHAGSLKYLLDiNPNIEVYCTKAAKLYLDGQ 114
Cdd:cd16280   24 AWAIDtGDGLILIDALNNNeAADLIVDGLEKLgLDPADIKYILITHGHGDHYGGAAYLKD-LYGAKVVMSEADWDMMEEP 102
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 489523693 115 INRPFNCH---------VIKDGEILNIGKRNLRFITAP 143
Cdd:cd16280  103 PEEGDNPRwgppperdiVIKDGDTLTLGDTTITVYLTP 140
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
34-89 6.58e-03

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: 37.91  E-value: 6.58e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489523693  34 TTYNSYLIKD-EKTVLFDT-VKANFKDE---FLSNLSEV-TDIAKIDYVVIHHTEPDHAGSL 89
Cdd:cd07720   47 TSVNAFLVRTgGRLILVDTgAGGLFGPTagkLLANLAAAgIDPEDIDDVLLTHLHPDHIGGL 108
 
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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