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Conserved domains on  [gi|16130617|ref|NP_417190|]
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anaerobic nitric oxide reductase flavorubredoxin [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

anaerobic nitric oxide reductase flavorubredoxin( domain architecture ID 11481010)

anaerobic nitric oxide reductase flavorubredoxin is involved in nitric oxide detoxification as part of bacterial defense mechanisms against reactive nitrogen species; a FprA family A-type flavoprotein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK05452 PRK05452
anaerobic nitric oxide reductase flavorubredoxin; Provisional
 1-479 0e+00

anaerobic nitric oxide reductase flavorubredoxin; Provisional


:

Pssm-ID: 235475 [Multi-domain]  Cd Length: 479  Bit Score: 1113.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617    1 MSIVVKNNIHWVGQRDWEVRDFHGTEYKTLRGSSYNSYLIREEKNVLIDTVDHKFSREFVQNLRNEIDLADIDYIVINHA 80
Cdd:PRK05452   1 MSIHVKNNIHWVGQRDWEVRDFHGTEYKTLRGSSYNSYLIREEKNVLIDTVDHKFSREFVQNLRNEIDLADIDYIVINHA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617   81 EEDHAGALTELMAQIPDTPIYCTANAIDSINGHHHHPEWNFNVVKTGDTLDIGNGKQLIFVETPMLHWPDSMMTYLTGDA 160
Cdd:PRK05452  81 EEDHAGALTELMAQIPDTPIYCTANAIDSINGHHHHPEWNFNVVKTGDTLDIGNGKQLIFVETPMLHWPDSMMTYLTGDA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617  161 VLFSNDAFGQHYCDEHLFNDEVDQTELFEQCQRYYANILTPFSRLVTPKITEILGFNLPVDMIATSHGVVWRDNPTQIVE 240
Cdd:PRK05452 161 VLFSNDAFGQHYCDEHLFNDEVDQTELFEQCQRYYANILTPFSRLVTPKITEILGFNLPVDMIATSHGVVWRDNPTQIVE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617  241 LYLKWAADYQEDRITIFYDTMSNNTRMMADAIAQGIAETDPRVAVKIFNVARSDKNEILTNVFRSKGVLVGTSTMNNVMM 320
Cdd:PRK05452 241 LYLKWAADYQEDRITIFYDTMSNNTRMMADAIAQGIAEVDPRVAVKIFNVARSDKNEILTNVFRSKGVLVGSSTMNNVMM 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617  321 PKIAGLVEEMTGLRFRNKRASAFGSHGWSGGAVDRLSTRLQDAGFEMSLSLKAKWRPDQDALKLCREHGREIARQWALAP 400
Cdd:PRK05452 321 PKIAGLLEEITGLRFRNKRASAFGSHGWSGGAVDRLSTRLQDAGFEMSLSLKAKWRPDQDALELCREHGREIARQWALAP 400

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130617  401 LPQSTVNTVVKEETSATTTADLGPRMQCSVCQWIYDPAKGEPMQDVAPGTPWSEVPDNFLCPECSLGKDVFEELASEAK 479
Cdd:PRK05452 401 LPQSTVNTVVKEETSATTTADLGPRMQCSVCQWIYDPAKGEPMQDVAPGTPWSEVPDNFLCPECSLGKDVFDELASEAK 479
 
Name Accession Description Interval E-value
PRK05452 PRK05452
anaerobic nitric oxide reductase flavorubredoxin; Provisional
 1-479 0e+00

anaerobic nitric oxide reductase flavorubredoxin; Provisional


Pssm-ID: 235475 [Multi-domain]  Cd Length: 479  Bit Score: 1113.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617    1 MSIVVKNNIHWVGQRDWEVRDFHGTEYKTLRGSSYNSYLIREEKNVLIDTVDHKFSREFVQNLRNEIDLADIDYIVINHA 80
Cdd:PRK05452   1 MSIHVKNNIHWVGQRDWEVRDFHGTEYKTLRGSSYNSYLIREEKNVLIDTVDHKFSREFVQNLRNEIDLADIDYIVINHA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617   81 EEDHAGALTELMAQIPDTPIYCTANAIDSINGHHHHPEWNFNVVKTGDTLDIGNGKQLIFVETPMLHWPDSMMTYLTGDA 160
Cdd:PRK05452  81 EEDHAGALTELMAQIPDTPIYCTANAIDSINGHHHHPEWNFNVVKTGDTLDIGNGKQLIFVETPMLHWPDSMMTYLTGDA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617  161 VLFSNDAFGQHYCDEHLFNDEVDQTELFEQCQRYYANILTPFSRLVTPKITEILGFNLPVDMIATSHGVVWRDNPTQIVE 240
Cdd:PRK05452 161 VLFSNDAFGQHYCDEHLFNDEVDQTELFEQCQRYYANILTPFSRLVTPKITEILGFNLPVDMIATSHGVVWRDNPTQIVE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617  241 LYLKWAADYQEDRITIFYDTMSNNTRMMADAIAQGIAETDPRVAVKIFNVARSDKNEILTNVFRSKGVLVGTSTMNNVMM 320
Cdd:PRK05452 241 LYLKWAADYQEDRITIFYDTMSNNTRMMADAIAQGIAEVDPRVAVKIFNVARSDKNEILTNVFRSKGVLVGSSTMNNVMM 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617  321 PKIAGLVEEMTGLRFRNKRASAFGSHGWSGGAVDRLSTRLQDAGFEMSLSLKAKWRPDQDALKLCREHGREIARQWALAP 400
Cdd:PRK05452 321 PKIAGLLEEITGLRFRNKRASAFGSHGWSGGAVDRLSTRLQDAGFEMSLSLKAKWRPDQDALELCREHGREIARQWALAP 400

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130617  401 LPQSTVNTVVKEETSATTTADLGPRMQCSVCQWIYDPAKGEPMQDVAPGTPWSEVPDNFLCPECSLGKDVFEELASEAK 479
Cdd:PRK05452 401 LPQSTVNTVVKEETSATTTADLGPRMQCSVCQWIYDPAKGEPMQDVAPGTPWSEVPDNFLCPECSLGKDVFDELASEAK 479
NorV COG0426
Flavorubredoxin [Energy production and conversion];
1-394 0e+00

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 559.83  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617   1 MSIVVKNNIHWVGQRDWEVRDFHGtEYKTLRGSSYNSYLIREEKNVLIDTVDHKFSREFVQNLRNEIDLADIDYIVINHA 80
Cdd:COG0426   1 QAVEIAHGVYWVGVLDWDRRLFEG-EYPTPRGTTYNSYLIVDEKTALIDTVGESFFEEFLENLSKVIDPKKIDYIIVNHQ 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617  81 EEDHAGALTELMAQIPDTPIYCTANAIDSINGHHHHPEWNFNVVKTGDTLDIGnGKQLIFVETPMLHWPDSMMTYLTGDA 160
Cdd:COG0426  80 EPDHSGSLPELLELAPNAKIVCSKKAARFLPHFYGIPDFRFIVVKEGDTLDLG-GHTLQFIPAPMLHWPDTMFTYDPEDK 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617 161 VLFSNDAFGQHYCDEHLFNDEVDQtELFEQCQRYYANILTPFSRLVTPKITEILGfnLPVDMIATSHGVVWRDNPTQIVE 240
Cdd:COG0426 159 ILFSGDAFGSHGASDELFDDEVDE-HLEEEARRYYANIMMPFSKQVLKALKKVRG--LDIDMIAPSHGPIWRGNPKEILD 235

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617 241 LYLKWAADYQEDRITIFYDTMSNNTRMMADAIAQGIAETDprVAVKIFNVARSDKNEILTNVFRSKGVLVGTSTMNNVMM 320
Cdd:COG0426 236 WYRKWSSYQPEKKVVIVYASMYGNTEKMAEAIAEGLTEEG--VKVKLYDLEKTDPSEIITEIFDAKGIVIGSPTYNGGAF 313

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130617 321 PKIAGLVEEMTGLRFRNKRASAFGSHGWSGGAVDRLSTRLQDAGFEMSL-SLKAKWRPDQDALKLCREHGREIAR 394
Cdd:COG0426 314 PPIADLLGYLKGLAPKNKLAGAFGSYGWSGEAVKLLEEKLEDAGFEVVFePLRVKFKPTEEDLKKCEELGTDLAQ 388
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 5-246 3.39e-116

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: 341.00  E-value: 3.39e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617   5 VKNNIHWVGQRDWEVRDFHGtEYKTLRGSSYNSYLIREEKNVLIDTVDHKFSREFVQNLRNEIDLADIDYIVINHAEEDH 84
Cdd:cd07709   3 IADDIYWVGVNDWDLRLFEG-EYPTPRGTSYNSYLIKDEKTALIDTVKEPFFDEFLENLEEVIDPRKIDYIVVNHQEPDH 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617  85 AGALTELMAQIPDTPIYCTANAIDSINGHHHHPEWNFNVVKTGDTLDIGNgKQLIFVETPMLHWPDSMMTYLTGDAVLFS 164
Cdd:cd07709  82 SGSLPELLELAPNAKIVCSKKAARFLKHFYPGIDERFVVVKDGDTLDLGK-HTLKFIPAPMLHWPDTMVTYDPEDKILFS 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617 165 NDAFGQHYCDEHLFNDEVDqtELFEQCQRYYANILTPFSRLVTPKITEILGfnLPVDMIATSHGVVWRDNPTQIVELYLK 244
Cdd:cd07709 161 GDAFGAHGASGELFDDEVE--DYLEEARRYYANIMGPFSKQVRKALEKLEA--LDIKMIAPSHGPIWRKDPGEIIDLYRD 236


                ..
gi 16130617 245 WA 246
Cdd:cd07709 237 WS 238
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 36-178 4.13e-27

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: 107.25  E-value: 4.13e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617     36 NSYLIR-EEKNVLIDTVdHKFSREFVQNLRnEIDLADIDYIVINHAEEDHAGALTELmAQIPDTPIYCTANAIDSINGHH 114
Cdd:smart00849   1 NSYLVRdDGGAILIDTG-PGEAEDLLAELK-KLGPKKIDAIILTHGHPDHIGGLPEL-LEAPGAPVYAPEGTAELLKDLL 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130617    115 H---------HPEWNFNVVKTGDTLDIGNGKqLIFVETPMlHWPDSMMTYLTGDAVLFSNDAFGQHYCDEHLF 178
Cdd:smart00849  78 AllgelgaeaEPAPPDRTLKDGDELDLGGGE-LEVIHTPG-HTPGSIVLYLPEGKILFTGDLLFAGGDGRTLV 148
Rubredoxin pfam00301
Rubredoxin;
426-471 1.40e-22

Rubredoxin;


Pssm-ID: 459752 [Multi-domain]  Cd Length: 46  Bit Score: 90.38  E-value: 1.40e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 16130617   426 MQCSVCQWIYDPAKGEPMQDVAPGTPWSEVPDNFLCPECSLGKDVF 471
Cdd:pfam00301   1 YECKVCGYVYDPAKGDPDNGIPPGTPFEDLPDDWVCPDCGAGKDQF 46
flav_short TIGR01753
flavodoxin, short chain; Flavodoxins are small redox-active proteins with a flavin ...
 254-393 1.61e-20

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: 87.39  E-value: 1.61e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617   254 ITIFYDTMSNNTRMMADAIAQGIAETDPRVavKIFNVARSDKNEILTnvfrSKGVLVGTSTMNNVMMPK--IAGLVEEMT 331
Cdd:TIGR01753   1 ILIVYASMTGNTEEMANIIAEGLKEAGAEV--DLLEVADADAEDLLS----YDAVLLGCSTWGDEDLEQddFEPFFEELE 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16130617   332 GLRFRNKRASAFGSHGWS---GGAVDRLSTRLQDAGFEMSL-SLKAKWRPDQDALKLCREHGREIA 393
Cdd:TIGR01753  75 DIDLGGKKVALFGSGDWGyefCEAVDDWEERLKEAGATIIAeGLKVDGDPEEEDLDKCREFAKDLA 140
 
Name Accession Description Interval E-value
PRK05452 PRK05452
anaerobic nitric oxide reductase flavorubredoxin; Provisional
 1-479 0e+00

anaerobic nitric oxide reductase flavorubredoxin; Provisional


Pssm-ID: 235475 [Multi-domain]  Cd Length: 479  Bit Score: 1113.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617    1 MSIVVKNNIHWVGQRDWEVRDFHGTEYKTLRGSSYNSYLIREEKNVLIDTVDHKFSREFVQNLRNEIDLADIDYIVINHA 80
Cdd:PRK05452   1 MSIHVKNNIHWVGQRDWEVRDFHGTEYKTLRGSSYNSYLIREEKNVLIDTVDHKFSREFVQNLRNEIDLADIDYIVINHA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617   81 EEDHAGALTELMAQIPDTPIYCTANAIDSINGHHHHPEWNFNVVKTGDTLDIGNGKQLIFVETPMLHWPDSMMTYLTGDA 160
Cdd:PRK05452  81 EEDHAGALTELMAQIPDTPIYCTANAIDSINGHHHHPEWNFNVVKTGDTLDIGNGKQLIFVETPMLHWPDSMMTYLTGDA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617  161 VLFSNDAFGQHYCDEHLFNDEVDQTELFEQCQRYYANILTPFSRLVTPKITEILGFNLPVDMIATSHGVVWRDNPTQIVE 240
Cdd:PRK05452 161 VLFSNDAFGQHYCDEHLFNDEVDQTELFEQCQRYYANILTPFSRLVTPKITEILGFNLPVDMIATSHGVVWRDNPTQIVE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617  241 LYLKWAADYQEDRITIFYDTMSNNTRMMADAIAQGIAETDPRVAVKIFNVARSDKNEILTNVFRSKGVLVGTSTMNNVMM 320
Cdd:PRK05452 241 LYLKWAADYQEDRITIFYDTMSNNTRMMADAIAQGIAEVDPRVAVKIFNVARSDKNEILTNVFRSKGVLVGSSTMNNVMM 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617  321 PKIAGLVEEMTGLRFRNKRASAFGSHGWSGGAVDRLSTRLQDAGFEMSLSLKAKWRPDQDALKLCREHGREIARQWALAP 400
Cdd:PRK05452 321 PKIAGLLEEITGLRFRNKRASAFGSHGWSGGAVDRLSTRLQDAGFEMSLSLKAKWRPDQDALELCREHGREIARQWALAP 400

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130617  401 LPQSTVNTVVKEETSATTTADLGPRMQCSVCQWIYDPAKGEPMQDVAPGTPWSEVPDNFLCPECSLGKDVFEELASEAK 479
Cdd:PRK05452 401 LPQSTVNTVVKEETSATTTADLGPRMQCSVCQWIYDPAKGEPMQDVAPGTPWSEVPDNFLCPECSLGKDVFDELASEAK 479
PRK11921 PRK11921
anaerobic nitric oxide reductase flavorubredoxin;
5-395 0e+00

anaerobic nitric oxide reductase flavorubredoxin;


Pssm-ID: 237023 [Multi-domain]  Cd Length: 394  Bit Score: 665.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617    5 VKNNIHWVGQRDWEVRDFHGTEYKTLRGSSYNSYLIREEKNVLIDTVDHKFSREFVQNLRNEIDLADIDYIVINHAEEDH 84
Cdd:PRK11921   3 INDNVTWVGKIDWELRKFHGEEYSTHRGSSYNSYLIKDEKTVLIDTVWQPFAKEFVENLKKEIDLDKIDYIVANHGEIDH 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617   85 AGALTELMAQIPDTPIYCTANAIDSINGHHHHpEWNFNVVKTGDTLDIGNgKQLIFVETPMLHWPDSMMTYLTGDAVLFS 164
Cdd:PRK11921  83 SGALPELMKEIPDTPIYCTKNGAKSLKGHYHQ-DWNFVVVKTGDRLEIGS-NELIFIEAPMLHWPDSMFTYLTGDNILFS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617  165 NDAFGQHYCDEHLFNDEVDQTELFEQCQRYYANILTPFSRLVTPKITEILGFNLPVDMIATSHGVVWRDNPTQIVELYLK 244
Cdd:PRK11921 161 NDAFGQHYASELMYNDLVDQGELYQEAIKYYANILTPFSPLVIKKIEEILSLNLPVDMICPSHGVIWRDNPLQIVEKYLE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617  245 WAADYQEDRITIFYDTMSNNTRMMADAIAQGIAETDPRVAVKIFNVARSDKNEILTNVFRSKGVLVGTSTMNNVMMPKIA 324
Cdd:PRK11921 241 WAANYQENQVTILYDTMWNSTRRMAEAIAEGIKKANKDVTVKLYNSAKSDKNDIITEVFKSKAILVGSSTINRGILSSTA 320

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130617  325 GLVEEMTGLRFRNKRASAFGSHGWSGGAVDRLSTRLQDAGFE-MSLSLKAKWRPDQDALKLCREHGREIARQ 395
Cdd:PRK11921 321 AILEEIKGLGFKNKKAAAFGSYGWSGESVKIITERLKKAGFEiVNDGIRELWNPDDEALDRCRSFGENFAES 392
NorV COG0426
Flavorubredoxin [Energy production and conversion];
1-394 0e+00

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 559.83  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617   1 MSIVVKNNIHWVGQRDWEVRDFHGtEYKTLRGSSYNSYLIREEKNVLIDTVDHKFSREFVQNLRNEIDLADIDYIVINHA 80
Cdd:COG0426   1 QAVEIAHGVYWVGVLDWDRRLFEG-EYPTPRGTTYNSYLIVDEKTALIDTVGESFFEEFLENLSKVIDPKKIDYIIVNHQ 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617  81 EEDHAGALTELMAQIPDTPIYCTANAIDSINGHHHHPEWNFNVVKTGDTLDIGnGKQLIFVETPMLHWPDSMMTYLTGDA 160
Cdd:COG0426  80 EPDHSGSLPELLELAPNAKIVCSKKAARFLPHFYGIPDFRFIVVKEGDTLDLG-GHTLQFIPAPMLHWPDTMFTYDPEDK 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617 161 VLFSNDAFGQHYCDEHLFNDEVDQtELFEQCQRYYANILTPFSRLVTPKITEILGfnLPVDMIATSHGVVWRDNPTQIVE 240
Cdd:COG0426 159 ILFSGDAFGSHGASDELFDDEVDE-HLEEEARRYYANIMMPFSKQVLKALKKVRG--LDIDMIAPSHGPIWRGNPKEILD 235

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617 241 LYLKWAADYQEDRITIFYDTMSNNTRMMADAIAQGIAETDprVAVKIFNVARSDKNEILTNVFRSKGVLVGTSTMNNVMM 320
Cdd:COG0426 236 WYRKWSSYQPEKKVVIVYASMYGNTEKMAEAIAEGLTEEG--VKVKLYDLEKTDPSEIITEIFDAKGIVIGSPTYNGGAF 313

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130617 321 PKIAGLVEEMTGLRFRNKRASAFGSHGWSGGAVDRLSTRLQDAGFEMSL-SLKAKWRPDQDALKLCREHGREIAR 394
Cdd:COG0426 314 PPIADLLGYLKGLAPKNKLAGAFGSYGWSGEAVKLLEEKLEDAGFEVVFePLRVKFKPTEEDLKKCEELGTDLAQ 388
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 5-246 3.39e-116

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: 341.00  E-value: 3.39e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617   5 VKNNIHWVGQRDWEVRDFHGtEYKTLRGSSYNSYLIREEKNVLIDTVDHKFSREFVQNLRNEIDLADIDYIVINHAEEDH 84
Cdd:cd07709   3 IADDIYWVGVNDWDLRLFEG-EYPTPRGTSYNSYLIKDEKTALIDTVKEPFFDEFLENLEEVIDPRKIDYIVVNHQEPDH 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617  85 AGALTELMAQIPDTPIYCTANAIDSINGHHHHPEWNFNVVKTGDTLDIGNgKQLIFVETPMLHWPDSMMTYLTGDAVLFS 164
Cdd:cd07709  82 SGSLPELLELAPNAKIVCSKKAARFLKHFYPGIDERFVVVKDGDTLDLGK-HTLKFIPAPMLHWPDTMVTYDPEDKILFS 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617 165 NDAFGQHYCDEHLFNDEVDqtELFEQCQRYYANILTPFSRLVTPKITEILGfnLPVDMIATSHGVVWRDNPTQIVELYLK 244
Cdd:cd07709 161 GDAFGAHGASGELFDDEVE--DYLEEARRYYANIMGPFSKQVRKALEKLEA--LDIKMIAPSHGPIWRKDPGEIIDLYRD 236


                ..
gi 16130617 245 WA 246
Cdd:cd07709 237 WS 238
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 36-178 4.13e-27

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: 107.25  E-value: 4.13e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617     36 NSYLIR-EEKNVLIDTVdHKFSREFVQNLRnEIDLADIDYIVINHAEEDHAGALTELmAQIPDTPIYCTANAIDSINGHH 114
Cdd:smart00849   1 NSYLVRdDGGAILIDTG-PGEAEDLLAELK-KLGPKKIDAIILTHGHPDHIGGLPEL-LEAPGAPVYAPEGTAELLKDLL 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130617    115 H---------HPEWNFNVVKTGDTLDIGNGKqLIFVETPMlHWPDSMMTYLTGDAVLFSNDAFGQHYCDEHLF 178
Cdd:smart00849  78 AllgelgaeaEPAPPDRTLKDGDELDLGGGE-LEVIHTPG-HTPGSIVLYLPEGKILFTGDLLFAGGDGRTLV 148
NorV COG1773
Flavorubredoxin [Inorganic ion transport and metabolism];
425-474 1.43e-23

Flavorubredoxin [Inorganic ion transport and metabolism];


Pssm-ID: 441379 [Multi-domain]  Cd Length: 53  Bit Score: 93.31  E-value: 1.43e-23
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 16130617 425 RMQCSVCQWIYDPAKGEPMQDVAPGTPWSEVPDNFLCPECSLGKDVFEEL 474
Cdd:COG1773   3 KYQCKVCGYVYDPAEGDPENGIPPGTPFEDLPDDWVCPVCGAGKEDFEPV 52
rubredoxin cd00730
Rubredoxin; nonheme iron binding domains containing a [Fe(SCys)4] center. Rubredoxins are ...
 425-474 7.45e-23

Rubredoxin; nonheme iron binding domains containing a [Fe(SCys)4] center. Rubredoxins are small nonheme iron proteins. The iron atom is coordinated by four cysteine residues (Fe(S-Cys)4), but iron can also be replaced by cobalt, nickel or zinc. They are believed to be involved in electron transfer.


Pssm-ID: 238372 [Multi-domain]  Cd Length: 50  Bit Score: 91.21  E-value: 7.45e-23
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 16130617 425 RMQCSVCQWIYDPAKGEPMQDVAPGTPWSEVPDNFLCPECSLGKDVFEEL 474
Cdd:cd00730   1 KYECRICGYIYDPAEGDPDEGIPPGTPFEDLPDDWVCPVCGAGKDDFEPL 50
Rubredoxin pfam00301
Rubredoxin;
426-471 1.40e-22

Rubredoxin;


Pssm-ID: 459752 [Multi-domain]  Cd Length: 46  Bit Score: 90.38  E-value: 1.40e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 16130617   426 MQCSVCQWIYDPAKGEPMQDVAPGTPWSEVPDNFLCPECSLGKDVF 471
Cdd:pfam00301   1 YECKVCGYVYDPAKGDPDNGIPPGTPFEDLPDDWVCPDCGAGKDQF 46
flav_short TIGR01753
flavodoxin, short chain; Flavodoxins are small redox-active proteins with a flavin ...
 254-393 1.61e-20

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: 87.39  E-value: 1.61e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617   254 ITIFYDTMSNNTRMMADAIAQGIAETDPRVavKIFNVARSDKNEILTnvfrSKGVLVGTSTMNNVMMPK--IAGLVEEMT 331
Cdd:TIGR01753   1 ILIVYASMTGNTEEMANIIAEGLKEAGAEV--DLLEVADADAEDLLS----YDAVLLGCSTWGDEDLEQddFEPFFEELE 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16130617   332 GLRFRNKRASAFGSHGWS---GGAVDRLSTRLQDAGFEMSL-SLKAKWRPDQDALKLCREHGREIA 393
Cdd:TIGR01753  75 DIDLGGKKVALFGSGDWGyefCEAVDDWEERLKEAGATIIAeGLKVDGDPEEEDLDKCREFAKDLA 140
Flavodoxin_1 pfam00258
Flavodoxin;
256-389 2.75e-17

Flavodoxin;


Pssm-ID: 425562 [Multi-domain]  Cd Length: 142  Bit Score: 78.57  E-value: 2.75e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617   256 IFYDTMSNNTRMMADAIAQGIAETDPRV-AVKIFNVARsDKNEILTNVFRSKGVL---VGTSTMNNVmmPKIAGLVEEMT 331
Cdd:pfam00258   1 IFYGSQTGNTEKLAEAIAEGLGEAGFEVdVVDLDDVDE-TLSEIEEEDLLLVVVStwgEGEPPDNAK--PFVDWLLLFGT 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130617   332 --GLRFRNKR--ASAFGSHGWSG--GAVDRLSTRLQDAGFEMSLS-LKAKWRPDQDALKLCREHG 389
Cdd:pfam00258  78 leDGDLSGLKyaVFGLGDSGYEGfcGAAKKLDEKLSELGASRVGPlGEGDEDPQEDGLEEAFEAW 142
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 36-166 1.76e-16

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: 77.33  E-value: 1.76e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617  36 NSYLIREEKN--VLIDTVDHkfSREFVQNLRNEIDLaDIDYIVINHAEEDHAGALTELmAQIPDTPIYCTANAID----- 108
Cdd:cd06262  11 NCYLVSDEEGeaILIDPGAG--ALEKILEAIEELGL-KIKAILLTHGHFDHIGGLAEL-KEAPGAPVYIHEADAElledp 86

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130617 109 -----SINGHHHHPEWNFNVVKTGDTLDIGNGKqLIFVETPMlHWPDSMMTYLTGDAVLFSND 166
Cdd:cd06262  87 elnlaFFGGGPLPPPEPDILLEDGDTIELGGLE-LEVIHTPG-HTPGSVCFYIEEEGVLFTGD 147
FldA COG0716
Flavodoxin [Energy production and conversion]; Flavodoxin is part of the Pathway/BioSystem: ...
 254-392 6.57e-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: 74.17  E-value: 6.57e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617 254 ITIFYDTMSNNTRMMADAIAQGIAETDprvaVKIFNVARSDKNEILtnvfRSKGVLVGTSTMNNVMMPKIAGLVEEMTGl 333
Cdd:COG0716   1 ILIVYGSTTGNTEKVAEAIAEALGAAG----VDLFEIEDADLDDLE----DYDLLILGTPTWAGELPDDWEDFLEELKE- 71

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130617 334 RFRNKRASAFGSHGWSGG--AVDRLSTRLQDAGFEM--SLSLKAKWRPD-QDALKLCREHGREI 392
Cdd:COG0716  72 DLSGKKVALFGTGDSSGYgdALGELKELLEEKGAKVvgGYDFEGSKAPDaEDTEERAEEWLKQL 135
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 36-254 6.53e-14

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: 70.87  E-value: 6.53e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617  36 NSYLIR-EEKNVLIDT-VDHKFSREFVQNLRnEIDLaDIDYIVINHAEEDHAGALTELMAQiPDTPIYCTANAIDSINGH 113
Cdd:COG0491  16 NSYLIVgGDGAVLIDTgLGPADAEALLAALA-ALGL-DIKAVLLTHLHPDHVGGLAALAEA-FGAPVYAHAAEAEALEAP 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617 114 HHHPEWNFN------VVKTGDTLDIGNGKqLIFVETPMlHWPDSMMTYLTGDAVLFSNDafgqhycdeHLFNDEVDQTEL 187
Cdd:COG0491  93 AAGALFGREpvppdrTLEDGDTLELGGPG-LEVIHTPG-HTPGHVSFYVPDEKVLFTGD---------ALFSGGVGRPDL 161

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130617 188 FEQC-QRYYANIltpfSRLvtpkiteilgFNLPVDMIATSHGVVWRDNPTQIVELYLKWAADYQEDRI 254
Cdd:COG0491 162 PDGDlAQWLASL----ERL----------LALPPDLVIPGHGPPTTAEAIDYLEELLAALGERANPFL 215
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
36-171 7.39e-13

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 67.39  E-value: 7.39e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617    36 NSYLIR-EEKNVLIDTVDHKFSREFVQNLRNEIDLADIDYIVINHAEEDHAGALTELMAQIPDTPIYCTANAIDSINGHH 114
Cdd:pfam00753   7 NSYLIEgGGGAVLIDTGGSAEAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARELLDEEL 86

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130617   115 HHPEWNFN------------VVKTGDTLDIGNGKQLIFVETPmLHWPDSMMTYLTGDAVLFSNDAFGQH 171
Cdd:pfam00753  87 GLAASRLGlpgppvvplppdVVLEEGDGILGGGLGLLVTHGP-GHGPGHVVVYYGGGKVLFTGDLLFAG 154
PRK06756 PRK06756
flavodoxin; Provisional
 253-394 4.46e-11

flavodoxin; Provisional


Pssm-ID: 168663 [Multi-domain]  Cd Length: 148  Bit Score: 60.66  E-value: 4.46e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617  253 RITIFYDTMSNNTRMMADAIAQGIAETDPRVAVKifNVARSDKNEILTnvfRSKGVLVGTSTMNNVMMP-KIAGLVEEMT 331
Cdd:PRK06756   3 KLVMIFASMSGNTEEMADHIAGVIRETENEIEVI--DIMDSPEASILE---QYDGIILGAYTWGDGDLPdDFLDFYDAMD 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130617  332 GLRFRNKRASAFGSHGWS----GGAVDRLSTRLQDAGFEMSLS-LKAKWRPDQDALKLCREHGREIAR 394
Cdd:PRK06756  78 SIDLTGKKAAVFGSCDSAypkyGVAVDILIEKLQERGAAVVLEgLKVELTPEDEDVEKCLQFGAEFVK 145
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 36-168 9.04e-11

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: 61.08  E-value: 9.04e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617  36 NSYLIREEKN-VLIDTVDHKFSREFVQNLRNE-IDLADIDYIVINHAEEDHAGALTELmAQIPDTPIYCTANAIDSING- 112
Cdd:cd07721  12 NAYLIEDDDGlTLIDTGLPGSAKRILKALRELgLSPKDIRRILLTHGHIDHIGSLAAL-KEAPGAPVYAHEREAPYLEGe 90

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130617 113 ---------------HHHHPEWNFNVVKT---GDTLDIGNGkqLIFVETPMlHWPDSMMTYLTGDAVLFSNDAF 168
Cdd:cd07721  91 kpypppvrlgllgllSPLLPVKPVPVDRTledGDTLDLAGG--LRVIHTPG-HTPGHISLYLEEDGVLIAGDAL 161
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 37-159 1.06e-10

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: 62.25  E-value: 1.06e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617  37 SYLIR-EEKNVLIDT----VdhkfsreFVQNLRN-EIDLADIDYIVINHAEEDHAGALTELMAQIPDTPIYCTANAIDSi 110
Cdd:cd07713  22 SLLIEtEGKKILFDTgqsgV-------LLHNAKKlGIDLSDIDAVVLSHGHYDHTGGLKALLELNPKAPVYAHPDAFEP- 93

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 16130617 111 ngHHHHPEWNFNVVKTGDTLDIGNGKQLIFVETPMLHWPDsmmTYLTGD 159
Cdd:cd07713  94 --RYSKRGGGKKGIGIGREELEKAGARLVLVEEPTEIAPG---VYLTGE 137
PRK05569 PRK05569
flavodoxin; Provisional
 253-394 7.55e-10

flavodoxin; Provisional


Pssm-ID: 135442 [Multi-domain]  Cd Length: 141  Bit Score: 57.15  E-value: 7.55e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617  253 RITIFYDTMSNNTRMMADAIAQGIAETDPRVAVKifNVARSDKNEILtnvfRSKGVLVGTSTM--NNVMMPKIAGLVEEM 330
Cdd:PRK05569   3 KVSIIYWSCGGNVEVLANTIADGAKEAGAEVTIK--HVADAKVEDVL----EADAVAFGSPSMdnNNIEQEEMAPFLDQF 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130617  331 TGLRFRNKRASAFGSHGWSGGA-VDRLSTRLQDAGFEMSLSLKAKWRPDQDALKLCREHGREIAR 394
Cdd:PRK05569  77 KLTPNENKKCILFGSYGWDNGEfMKLWKDRMKDYGFNVIGDLAVNESPNKEELNSAKELGKKLAK 141
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 36-167 2.90e-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: 56.54  E-value: 2.90e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617  36 NSYLIR-EEKNVLIDT-VDHKFSREFVQNLRNE--IDLADIDYIVINHAEEDHAGALTELmaqipdtpiyCTANAIDSIn 111
Cdd:cd07725  16 NVYLLRdGDETTLIDTgLATEEDAEALWEGLKElgLKPSDIDRVLLTHHHPDHIGLAGKL----------QEKSGATVY- 84

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 16130617 112 ghhhHPEWNFnvVKTGDTLDIGnGKQLIFVETPMlHWPDSMMTYLTGDAVLFSNDA 167
Cdd:cd07725  85 ----ILDVTP--VKDGDKIDLG-GLRLKVIETPG-HTPGHIVLYDEDRRELFVGDA 132
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 37-176 5.78e-08

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: 53.27  E-value: 5.78e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617  37 SYLIREE-KNVLIDT-----VDHkfSREFVQNLRneIDLADIDYIVINHAEEDHAGALTELMAQIPDTPIYCTANA---- 106
Cdd:cd07726  18 SYLLDGEgRPALIDTgpsssVPR--LLAALEALG--IAPEDVDYIILTHIHLDHAGGAGLLAEALPNAKVYVHPRGarhl 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617 107 ID---------SINGHHHHPEW---------NFNVVKTGDTLDIGnGKQLIFVETPMlHWPDSMMTYLTGDAVLFSNDAF 168
Cdd:cd07726  94 IDpsklwasarAVYGDEADRLGgeilpvpeeRVIVLEDGETLDLG-GRTLEVIDTPG-HAPHHLSFLDEESDGLFTGDAA 171


                ....*...
gi 16130617 169 GQHYCDEH 176
Cdd:cd07726 172 GVRYPELD 179
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 37-166 7.60e-08

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: 51.69  E-value: 7.60e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617  37 SYLIREEKN---VLIDTVDHKFSREFVQNLRneidlADIDYIVINHAEEDHAGALTELMAQIPDTPIYctANAIDSINGH 113
Cdd:cd07723  11 IYLIVDEATgeaAVVDPGEAEPVLAALEKNG-----LTLTAILTTHHHWDHTGGNAELKALFPDAPVY--GPAEDRIPGL 83

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 16130617 114 HHhpewnfnVVKTGDTLDIGNGKqLIFVETPMlHWPDSMMTYLTGDAVLFSND 166
Cdd:cd07723  84 DH-------PVKDGDEIKLGGLE-VKVLHTPG-HTLGHICYYVPDEPALFTGD 127
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 29-166 1.50e-07

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: 51.38  E-value: 1.50e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617  29 TLRGSsyNSYLIREEKN-VLIDTVDHKfsREFVQNLRNEID---LADIDYIVINHAEEDHAGALTELMAQIPDTPIycta 104
Cdd:cd07722  14 TLQGT--NTYLVGTGKRrILIDTGEGR--PSYIPLLKSVLDsegNATISDILLTHWHHDHVGGLPDVLDLLRGPSP---- 85

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617 105 naidSINGHHHHPEWNFNVVKTGDTLDIGNGkQLIFVE--------TPMlHWPDSMMTYLTGDAVLFSND 166
Cdd:cd07722  86 ----RVYKFPRPEEDEDPDEDGGDIHDLQDG-QVFKVEgatlrvihTPG-HTTDHVCFLLEEENALFTGD 149
RnjA COG0595
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];
67-134 4.12e-07

mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 52.37  E-value: 4.12e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617  67 IDL--ADIDY----------IVINHAEEDHAGALTELMAQIpDTPIYCTANAIDSING----HHHHPEWNFNVVKTGDTL 130
Cdd:COG0595  47 VDLviPDISYleenkdkikgIVLTHGHEDHIGALPYLLKEL-NVPVYGTPLTLALLEAklkeHGLLKKVKLHVVKPGDRI 125


                ....
gi 16130617 131 DIGN 134
Cdd:COG0595 126 KFGP 129
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 32-104 6.64e-07

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: 49.76  E-value: 6.64e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130617  32 GSSYnsyLIR-EEKNVLIDT-VdhKFSREFVQNLRNE---IDLADIDYIVINHAEEDHAGALTELMAQIPDTPIYCTA 104
Cdd:cd16295  12 GSCY---LLEtGGKRILLDCgL--FQGGKELEELNNEpfpFDPKEIDAVILTHAHLDHSGRLPLLVKEGFRGPIYATP 84
PRK05568 PRK05568
flavodoxin; Provisional
 253-394 7.88e-07

flavodoxin; Provisional


Pssm-ID: 235508 [Multi-domain]  Cd Length: 142  Bit Score: 48.27  E-value: 7.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617  253 RITIFYDTMSNNTRMMADAIAQGIAETDprVAVKIFNVARSDKNEiltnVFRSKGVLVGTSTM------NNVMMPkiagL 326
Cdd:PRK05568   3 KINIIYWSGTGNTEAMANLIAEGAKENG--AEVKLLNVSEASVDD----VKGADVVALGSPAMgdevleEGEMEP----F 72

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617  327 VEEMTGLrFRNKRASAFGSHGW-SGGAVDRLSTRLQDAGFEM-SLSLKAKWRPDQDALKLCREHGREIAR 394
Cdd:PRK05568  73 VESISSL-VKGKKLVLFGSYGWgDGEWMRDWVERMEGYGANLvNEGLIVNNTPEGEGIEKCKALGEALAK 141
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 36-166 1.12e-06

RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a prokaryotic ribonuclease which plays a key part in RNA processing and in RNA degradation. It can act as an endonuclease which is specific for single-stranded regions of RNA irrespective of their sequence or location, and as a processive 5' exonuclease which only acts on substrates having a single phosphate or a hydroxyl at the 5' end. Many bacterial species have only one RNase J, but some, such as Bacillus subtilis, have two. 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: 293800 [Multi-domain]  Cd Length: 248  Bit Score: 49.71  E-value: 1.12e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617  36 NSYLIREEKNVLIdtVDH--KFSREFVqnlrNEID--LADIDY----------IVINHAEEDHAGALTELMAQIpDTPIY 101
Cdd:cd07714  12 NMYVVEYDDDIII--IDCglKFPDEDM----PGVDyiIPDFSYleenkdkikgIFITHGHEDHIGALPYLLPEL-NVPIY 84

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130617 102 CTANAI----DSINGHHHHPEWNFNVVKTGDTLDIGNgkqlIFVET-PMLH-WPDSMMTYLTGDA--VLFSND 166
Cdd:cd07714  85 ATPLTLalikKKLEEFKLIKKVKLNEIKPGERIKLGD----FEVEFfRVTHsIPDSVGLAIKTPEgtIVHTGD 153
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 32-133 1.75e-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: 47.64  E-value: 1.75e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617  32 GSSYNSYLIREEKNVLIdtVDHKFSREFVQNLRNEI--DLADIDYIVINHAEEDHAGALtELMAQIPDTPIYCTANAIDS 109
Cdd:cd07733   6 GSKGNCTYLETEDGKLL--IDAGLSGRKITGRLAEIgrDPEDIDAILVTHEHADHIKGL-GVLARKYNVPIYATAGTLRA 82

                        90       100
                ....*....|....*....|....*
gi 16130617 110 INGHHH-HPEWNFNVVKTGDTLDIG 133
Cdd:cd07733  83 MERKVGlIDVDQKQIFEPGETFSIG 107
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 36-104 3.92e-06

RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 49.03  E-value: 3.92e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617  36 NSYLIR-EEKNVLIDTVDHkFSREFVQNLRNEIDLADIDYIVINHAEEDHAGALTELMAQIPDTPIYCTA 104
Cdd:COG1236  15 SCYLLEtGGTRILIDCGLF-QGGKERNWPPFPFRPSDVDAVVLTHAHLDHSGALPLLVKEGFRGPIYATP 83
rubredoxin_like cd00350
Rubredoxin_like; nonheme iron binding domain containing a [Fe(SCys)4] center. The family ...
 425-474 5.34e-06

Rubredoxin_like; nonheme iron binding domain containing a [Fe(SCys)4] center. The family includes rubredoxins, a small electron transfer protein, and a slightly smaller modular rubredoxin domain present in rubrerythrin and nigerythrin and detected either N- or C-terminal to such proteins as flavin reductase, NAD(P)H-nitrite reductase, and ferredoxin-thioredoxin reductase. In rubredoxin, the iron atom is coordinated by four cysteine residues (Fe(S-Cys)4), but iron can also be replaced by cobalt, nickel or zinc and believed to be involved in electron transfer. Rubrerythrins and nigerythrins are small homodimeric proteins, generally consisting of 2 domains: a rubredoxin domain C-terminal to a non-sulfur, oxo-bridged diiron site in the N-terminal rubrerythrin domain. Rubrerythrins and nigerythrins have putative peroxide activity.


Pssm-ID: 238210 [Multi-domain]  Cd Length: 33  Bit Score: 42.93  E-value: 5.34e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 16130617 425 RMQCSVCQWIYDPAKgepmqdvapgtpwsevpDNFLCPECSLGKDVFEEL 474
Cdd:cd00350   1 KYVCPVCGYIYDGEE-----------------APWVCPVCGAPKDKFEKL 33
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 37-147 6.69e-06

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; 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 named as octanoyltransferase (also known as lipoate-protein ligase B).


Pssm-ID: 293837 [Multi-domain]  Cd Length: 193  Bit Score: 46.70  E-value: 6.69e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617  37 SYLIR-EEKNVLIDTvdhkfSREF-VQNLRNEIDlaDIDYIVINHAEEDHAGALTEL----MAQIPDTPIYCTANAIDSI 110
Cdd:cd16279  37 SILIEtGGKNILIDT-----GPDFrQQALRAGIR--KLDAVLLTHAHADHIHGLDDLrpfnRLQQRPIPVYASEETLDDL 109

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 16130617 111 ----------NGHHHHPEWNFNVVKTGDTLDIGnGKQLIFVetPMLH 147
Cdd:cd16279 110 krrfpyffaaTGGGGVPKLDLHIIEPDEPFTIG-GLEITPL--PVLH 153
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 29-166 7.76e-06

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: 46.33  E-value: 7.76e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617  29 TLRGSsyNSYLIREEKNVLI-----DTVDHkfsrefVQNLRNEIDLADIDYIVINHAEEDHAGALTELmAQIPDTPIYCT 103
Cdd:cd16278  14 TLDGT--NTYLLGAPDGVVVidpgpDDPAH------LDALLAALGGGRVSAILVTHTHRDHSPGAARL-AERTGAPVRAF 84

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130617 104 ANAIDSINGHHHHPEwnfNVVKTGDTLDIGnGKQLIFVETPMlHWPDSMMTYLTGDAVLFSND 166
Cdd:cd16278  85 GPHRAGGQDTDFAPD---RPLADGEVIEGG-GLRLTVLHTPG-HTSDHLCFALEDEGALFTGD 142
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 37-160 4.83e-05

Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This subgroup includes proteins required for natural transformation competence including Neisseria gonorrhoeae ComA, Pseudomonas stutzeri ComA, Bacillus subtilis ComEC (also known as ComE operon protein 3) and Haemophilus influenza ORF2 encoded by the rec-2 gene, as well as Escherichia coli YcaI which does not mediate spontaneous plasmid transformation on nutrient-containing agar plates. It also includes the phosphorylcholine esterase (Pce) domain of choline-binding protein e from streptococcus pneumonia. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293817 [Multi-domain]  Cd Length: 179  Bit Score: 44.05  E-value: 4.83e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617  37 SYLIR-EEKNVLIDT--VDHKFSREFVQNLRNE-IDlaDIDYIVINHAEEDHAGALTELMAQIP-----------DTPIY 101
Cdd:cd07731  12 AILIQtPGKTILIDTgpRDSFGEDVVVPYLKARgIK--KLDYLILTHPDADHIGGLDAVLKNFPvkevympgvthTTKTY 89

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130617 102 ctANAIDSINGHHHHpewnFNVVKTGDTLDIGNgkqlIFVEtpMLHWP---------DS---MMTY------LTGDA 160
Cdd:cd07731  90 --EDLLDAIKEKGIP----VTPCKAGDRWQLGG----VSFE--VLSPPkddyddlnnNScvlRLTYggtsflLTGDA 154
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 34-89 5.54e-05

Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold metallo hydrolase domain; Pseudomonas pseudoalcaligenes OPHC2 is a thermostable organophosphorus hydrolase which a broad substrate activity spectrum: it hydrolyzes various phosphotriesters, esters, and a lactone. This subgroup also includes Pseudomonas oleovorans PoOPH which exhibits high lactonase and esterase activities, and latent PTE activity. However, double mutations His250Ile/Ile263Trp switch PoOPH into an efficient and thermostable PTE. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293806 [Multi-domain]  Cd Length: 251  Bit Score: 44.46  E-value: 5.54e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130617  34 SYNSYLIR-EEKNVLIDT-----VDHKFSReFVQNLRNE-IDLADIDYIVINHAEEDHAGALT 89
Cdd:cd07720  48 SVNAFLVRtGGRLILVDTgagglFGPTAGK-LLANLAAAgIDPEDIDDVLLTHLHPDHIGGLV 109
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 36-164 5.88e-05

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 44.14  E-value: 5.88e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617  36 NSYLIR-EEKNVLID-TVDHKFSREFVQNLRNEiDLADIDYIVINHAEEDHAGALTELMAQIPDTPIYCTANAIDSINGH 113
Cdd:COG2220  12 ATFLIEtGGKRILIDpVFSGRASPVNPLPLDPE-DLPKIDAVLVTHDHYDHLDDATLRALKRTGATVVAPLGVAAWLRAW 90

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130617 114 HHHpewNFNVVKTGDTLDIGNGKqlifVE-TPMLHWP---DSMMT--------------YLTGDAVLFS 164
Cdd:COG2220  91 GFP---RVTELDWGESVELGGLT----VTaVPARHSSgrpDRNGGlwvgfvietdgktiYHAGDTGYFP 152
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 37-133 9.53e-05

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: 43.98  E-value: 9.53e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617  37 SYLI-REEKNVLIDTVDHKFSREFVQNLRN-EIDLADIDYIVINHAEEDHAGAL--------TELMAQIPDTPIYCTANA 106
Cdd:cd16310  24 SYLItSNHGAILLDGGLEENAALIEQNIKAlGFKLSDIKIIINTHAHYDHAGGLaqlkadtgAKLWASRGDRPALEAGKH 103

                        90       100
                ....*....|....*....|....*....
gi 16130617 107 I-DSINGHHHHPEWNFN-VVKTGDTLDIG 133
Cdd:cd16310 104 IgDNITQPAPFPAVKVDrILGDGEKIKLG 132
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 24-183 1.06e-04

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: 43.02  E-value: 1.06e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617  24 GTEYKTLRGSSyNSYLIR-EEKNVLIDT---VDHKFsrefvqnLRNEIDLADIDYIVINHAEEDHAGALTELMAQI---- 95
Cdd:cd16272   7 GGAVPSLTRNT-SSYLLEtGGTRILLDCgegTVYRL-------LKAGVDPDKLDAIFLSHFHLDHIGGLPTLLFARrygg 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617  96 PDTP--IYC---TANAIDSINGHHHHPEW---NFNVV---KTGDTLDIGNGKqlifVET-PMLHWPDSMMTYLT--GDAV 161
Cdd:cd16272  79 RKKPltIYGpkgIKEFLEKLLNFPVEILPlgfPLEIEeleEGGEVLELGDLK----VEAfPVKHSVESLGYRIEaeGKSI 154

                       170       180
                ....*....|....*....|...
gi 16130617 162 LFSNDAfgqHYCDEHL-FNDEVD 183
Cdd:cd16272 155 VYSGDT---GPCENLVeLAKGAD 174
WrbA COG0655
Multimeric flavodoxin WrbA, includes NAD(P)H:quinone oxidoreductase [Energy production and ...
 253-394 1.07e-04

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: 1.07e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617 253 RITIFYDTMSN--NTRMMADAIAQGIAETDprVAVKIFNVAR------------------SDKNEILTNVFRSKGVLVGT 312
Cdd:COG0655   1 KILVINGSPRKngNTAALAEAVAEGAEEAG--AEVELIRLADldikpcigcggtgkcvikDDMNAIYEKLLEADGIIFGS 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617 313 STMNNVMMPKIAGLVEEMTGL-----RFRNKRASAF--GSHGWSGGAVDRLSTRLQDAGFE--------MSLSLKAKWRP 377
Cdd:COG0655  79 PTYFGNMSAQLKAFIDRLYALwakgkLLKGKVGAVFttGGHGGAEATLLSLNTFLLHHGMIvvglppygAVGGGGPGDVL 158

                       170
                ....*....|....*..
gi 16130617 378 DQDALKLCREHGREIAR 394
Cdd:COG0655 159 DEEGLATARELGKRLAE 175
PRK06703 PRK06703
flavodoxin; Provisional
 253-397 1.62e-04

flavodoxin; Provisional


Pssm-ID: 235854 [Multi-domain]  Cd Length: 151  Bit Score: 42.05  E-value: 1.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617  253 RITIFYDTMSNNTRMMADAIAQGIAETDprVAVKIFNVARSDKNEILTnvfrSKGVLVGTSTMNNVMMPKIA-GLVEEMT 331
Cdd:PRK06703   3 KILIAYASMSGNTEDIADLIKVSLDAFD--HEVVLQEMDGMDAEELLA----YDGIILGSYTWGDGDLPYEAeDFHEDLE 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130617  332 GLRFRNKRASAFGSHGWS----GGAVDRLSTRLQDAGFEM-SLSLKAKWRPDQDA-LKLCREHGREIARqWA 397
Cdd:PRK06703  77 NIDLSGKKVAVFGSGDTAyplfCEAVTIFEERLVERGAELvQEGLKIELAPETDEdVEKCSNFAIAFAE-KF 147
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 39-134 2.57e-04

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: 42.54  E-value: 2.57e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617  39 LIR--EEKNVLIDT----VDHKFSREFVQNLRnEIDLADIDYIVINHAEEDHAGALTELMAQIP-----------DTPIY 101
Cdd:COG2333  15 LIRtpDGKTILIDTgprpSFDAGERVVLPYLR-ALGIRRLDLLVLTHPDADHIGGLAAVLEAFPvgrvlvsgppdTSETY 93

                        90       100       110
                ....*....|....*....|....*....|...
gi 16130617 102 CTANAIDSINGHHHHPewnfnvVKTGDTLDIGN 134
Cdd:COG2333  94 ERLLEALKEKGIPVRP------CRAGDTWQLGG 120
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 36-188 3.73e-04

uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized Thermus thermophilus TTHA1623 and related proteins. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. This family includes homologs present in a wide range of bacteria and archaea and some eukaryota. Members of the MBL-fold metallo-hydrolase superfamily exhibit a variety of active site metallo-chemistry, TTHA1623 exhibiting a uniquely shaped putative substrate-binding pocket with a glyoxalase II-type metal-coordination mode.


Pssm-ID: 293877 [Multi-domain]  Cd Length: 204  Bit Score: 41.57  E-value: 3.73e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617  36 NSYLIREEKN---VLIDTVDhkfsrEFVQNLRNEIDLA-DIDYIVINHAEEDHAGALTELMAQiPDTPIYCtaNAIDSin 111
Cdd:cd16322  12 NTYLVADEGGgeaVLVDPGD-----ESEKLLARFGTTGlTLLYILLTHAHFDHVGGVADLRRH-PGAPVYL--HPDDL-- 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617 112 GHHHHPE-----WNFNVVKT---------GDTLDIGNgkqLIF--VETPMlHWPDSMMTYLTGDAVLFSNDAFGQ----- 170
Cdd:cd16322  82 PLYEAADlgakaFGLGIEPLpppdrlledGQTLTLGG---LEFkvLHTPG-HSPGHVCFYVEEEGLLFSGDLLFQgsigr 157

                       170       180
                ....*....|....*....|....*...
gi 16130617 171 ---HYCDEHLFN-------DEVDQTELF 188
Cdd:cd16322 158 tdlPGGDPKAMAaslrrllTLPDETRVF 185
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 35-142 5.97e-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: 41.43  E-value: 5.97e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617  35 YNSYLIR-EEKNVLIDT--------------VDHKFSREFVQNLRNE-----IDLADIDYIVINHAEEDHAGALTELmaq 94
Cdd:cd07729  32 VYAYLIEhPEGTILVDTgfhpdaaddpggleLAFPPGVTEEQTLEEQlarlgLDPEDIDYVILSHLHFDHAGGLDLF--- 108

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 16130617  95 iPDTPIYCTANAIDSINGHHHHPEWNFNVVKTGDTLDigNGKQLIFVE 142
Cdd:cd07729 109 -PNATIIVQRAELEYATGPDPLAAGYYEDVLALDDDL--PGGRVRLVD 153
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 37-166 8.25e-04

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 41.29  E-value: 8.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617   37 SYLIREE---KNVLIDTVDhkfsREFVQNLRNEIDlADIDYIVINHAEEDHAGALTELMAQIPDTPIYctANAIDSINGH 113
Cdd:PLN02469  14 AYLIIDEstkDAAVVDPVD----PEKVLQAAHEHG-AKIKLVLTTHHHWDHAGGNEKIKKLVPGIKVY--GGSLDNVKGC 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 16130617  114 HHHpewnfnvVKTGDTLDIGNGKQLIFVETPmLHWPDSMMTYLTG----DAVLFSND 166
Cdd:PLN02469  87 THP-------VENGDKLSLGKDVNILALHTP-CHTKGHISYYVTGkegeDPAVFTGD 135
MG423 TIGR00649
beta-CASP ribonuclease, RNase J family; This family of metalloenzymes includes RNase J1 and ...
 75-159 1.06e-03

beta-CASP ribonuclease, RNase J family; This family of metalloenzymes includes RNase J1 and RNase J2, involved in mRNA degradation in a wide range of organism. [Transcription, Degradation of RNA]


Pssm-ID: 273195 [Multi-domain]  Cd Length: 422  Bit Score: 41.18  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617    75 IVINHAEEDHAGALTELMAQIPDTPIYCTANAI----DSINGHHHHPEWNFNVVKTGDTLDIGNGKQLIFVET------- 143
Cdd:TIGR00649  62 IFITHGHEDHIGAVPYLLHQVGFFPIYGTPLTIalikSKIKEHGLNVRTDLLEIHEGEPVEFGENTAIEFFRIthsipds 141

                          90
                  ....*....|....*...
gi 16130617   144 --PMLHWPDSMMTYlTGD 159
Cdd:TIGR00649 142 vgFALHTPLGYIVY-TGD 158
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 45-148 1.58e-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: 1.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617    45 NVLIDTV----DHKFSREFVQNLRNEidlaDIDYIVINHAEEDH-AGALTelMAQIPDTPIYCTANAIDSINGH------ 113
Cdd:pfam12706   2 RILIDPGpdlrQQALPALQPGRLRDD----PIDAVLLTHDHYDHlAGLLD--LREGRPRPLYAPLGVLAHLRRNfpylfl 75

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 16130617   114 HHHPEWNFNVVKTGDTLDIGNGkQLIFVETPMLHW 148
Cdd:pfam12706  76 LEHYGVRVHEIDWGESFTVGDG-GLTVTATPARHG 109
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 39-144 2.16e-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: 39.11  E-value: 2.16e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617  39 LIR-EEKNVLIDTvDHKFSREF-VQNLRNE-IDLADIDYIVINHAEEDHAGalteLMAQIPDtpiyctANAIDSINGHHH 115
Cdd:cd07711  26 LIKdGGKNILVDT-GTPWDRDLlLKALAEHgLSPEDIDYVVLTHGHPDHIG----NLNLFPN------ATVIVGWDICGD 94

                        90       100
                ....*....|....*....|....*....
gi 16130617 116 HpeWNFNVVKTGDTLDIGNGKQLIfvETP 144
Cdd:cd07711  95 S--YDDHSLEEGDGYEIDENVEVI--PTP 119
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 46-144 2.51e-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: 39.49  E-value: 2.51e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617  46 VLIDTVD-HKFSREFVQNLRN-EIDLADIDYIVINHAEEDHAGAlTELMAQIPDTPIYCTANAIDSINGhhhHPEWNFN- 122
Cdd:cd16280  34 ILIDALNnNEAADLIVDGLEKlGLDPADIKYILITHGHGDHYGG-AAYLKDLYGAKVVMSEADWDMMEE---PPEEGDNp 109

                        90       100       110
                ....*....|....*....|....*....|..
gi 16130617 123 ----------VVKTGDTLDIGNgKQLIFVETP 144
Cdd:cd16280 110 rwgppperdiVIKDGDTLTLGD-TTITVYLTP 140
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 21-163 4.62e-03

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: 38.36  E-value: 4.62e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130617  21 DFhGTEYKtlRGSSYNSYLIREEKNVLIDTVDHKFSREFVQNLRNEIDLADIDYIVINHAEEDHAGALTELMaqiPDTPI 100
Cdd:cd07732  28 DF-GLPLD--PESKYFDEVLDFLELGLLPDIVGLYRDPLLLGGLRSEEDPSVDAVLLSHAHLDHYGLLNYLR---PDIPV 101

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130617 101 YCTA------NAIDSINGHHHHPEWNFNVVKTGDTLDIGNgkqliFVETPML--H-WPDSMMTYL-TGDAVLF 163
Cdd:cd07732 102 YMGEatkrilKALLPFFGEGDPVPRNIRVFESGKSFTIGD-----FTVTPYLvdHsAPGAYAFLIeAPGKRIF 169
Int9-11_CPSF2-3-like_MBL-fold cd07734
Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; ...
 39-103 8.65e-03

Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; MBL-fold metallo-hydrolase domain; CPSF3 (cleavage and polyadenylation specificity factor subunit 3; also known as cleavage and polyadenylation specificity factor 73 kDa subunit, CPSF-73) and CPSF2 (also known as cleavage and polyadenylation specificity factor 100 kDa subunit /CPSF-100) are components of the CPSF complex, which plays a role in 3' end processing of pre-mRNAs during cleavage/polyadenylation, and during processing of metazoan histone pre-mRNAs. CPSF3 functions as a 3' endonuclease. Int11 (also known as cleavage and polyadenylation-specific factor (CPSF) 3-like protein, and protein related to CPSF subunits of 68 kDa (RC-68)), and Int9, also known as protein related to CPSF subunits of 74 kDa (RC-74) are subunits of Integrator, a metazoan-specific multifunctional protein complex composed of 14 subunits. Integrator has been implicated in a variety of Pol II transcription events including 3' end processing of snRNA, transcription initiation, promoter-proximal pausing, termination of protein-coding transcripts, and in HVS pre-miRNA 3' end processing. 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: 293820 [Multi-domain]  Cd Length: 193  Bit Score: 37.31  E-value: 8.65e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130617  39 LIREEKNVLIDTVDHKFSREFVQNL-RNEIDLADIDYIVINHAEEDHAGALTELMAQ-IPDTPIYCT 103
Cdd:cd07734  16 VEFKGRTVLLDCGMNPGKEDPEACLpQFELLPPEIDAILISHFHLDHCGALPYLFRGfIFRGPIYAT 82
 
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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