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Conserved domains on  [gi|490247618|ref|WP_004145759|]
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MULTISPECIES: anaerobic nitric oxide reductase flavorubredoxin [Klebsiella]

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
 1-482 0e+00

anaerobic nitric oxide reductase flavorubredoxin; Provisional


:

Pssm-ID: 235475 [Multi-domain]  Cd Length: 479  Bit Score: 1090.18  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618   1 MSIVVKNNILWVGQRDWEVRDFHGTEYKTLRGSSYNSYLIREEKNVLIDTVDHKFSREFVQNLRREIDLADLDYIVINHA 80
Cdd:PRK05452   1 MSIHVKNNIHWVGQRDWEVRDFHGTEYKTLRGSSYNSYLIREEKNVLIDTVDHKFSREFVQNLRNEIDLADIDYIVINHA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618  81 EEDHAGALTELMMQIPDTPIYCTANAIDSINGHHHHPEWNFHVVKTGDTLDIGNGKQLIFVETPMLHWPDSMMTYLTGDA 160
Cdd:PRK05452  81 EEDHAGALTELMAQIPDTPIYCTANAIDSINGHHHHPEWNFNVVKTGDTLDIGNGKQLIFVETPMLHWPDSMMTYLTGDA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618 161 VLFSNDAFGQHYCDEHLFNDEVDQTELYEQCQRYYANILTPFSRLVTPKITEILGFNLPVEMIATSHGVVWRDNPTQIVE 240
Cdd:PRK05452 161 VLFSNDAFGQHYCDEHLFNDEVDQTELFEQCQRYYANILTPFSRLVTPKITEILGFNLPVDMIATSHGVVWRDNPTQIVE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618 241 KYLEWAADYQEDRITIFYDTMSNNTRMMADAIAQGITEVDPRVAVKIFNVARSDKNDILTNVFRSKGVLVGTSTMNNVMM 320
Cdd:PRK05452 241 LYLKWAADYQEDRITIFYDTMSNNTRMMADAIAQGIAEVDPRVAVKIFNVARSDKNEILTNVFRSKGVLVGSSTMNNVMM 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618 321 PKIAGLVEEMTGLRFRNKRASAFGSHGWSGGAVDRLSTRLQDAGFEMSLSLKAKWRPDIDALELCRQHGRDIARQWALSP 400
Cdd:PRK05452 321 PKIAGLLEEITGLRFRNKRASAFGSHGWSGGAVDRLSTRLQDAGFEMSLSLKAKWRPDQDALELCREHGREIARQWALAP 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618 401 LPVAEAATTPEPQDcacAAAAAADLGPMMQCSVCQWVYDPAKGEPNQDVQPGTPWSEVPDNFLCPECSLGKDVFDVLATE 480
Cdd:PRK05452 401 LPQSTVNTVVKEET---SATTTADLGPRMQCSVCQWIYDPAKGEPMQDVAPGTPWSEVPDNFLCPECSLGKDVFDELASE 477


                 ..
gi 490247618 481 AK 482
Cdd:PRK05452 478 AK 479
 
Name Accession Description Interval E-value
PRK05452 PRK05452
anaerobic nitric oxide reductase flavorubredoxin; Provisional
 1-482 0e+00

anaerobic nitric oxide reductase flavorubredoxin; Provisional


Pssm-ID: 235475 [Multi-domain]  Cd Length: 479  Bit Score: 1090.18  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618   1 MSIVVKNNILWVGQRDWEVRDFHGTEYKTLRGSSYNSYLIREEKNVLIDTVDHKFSREFVQNLRREIDLADLDYIVINHA 80
Cdd:PRK05452   1 MSIHVKNNIHWVGQRDWEVRDFHGTEYKTLRGSSYNSYLIREEKNVLIDTVDHKFSREFVQNLRNEIDLADIDYIVINHA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618  81 EEDHAGALTELMMQIPDTPIYCTANAIDSINGHHHHPEWNFHVVKTGDTLDIGNGKQLIFVETPMLHWPDSMMTYLTGDA 160
Cdd:PRK05452  81 EEDHAGALTELMAQIPDTPIYCTANAIDSINGHHHHPEWNFNVVKTGDTLDIGNGKQLIFVETPMLHWPDSMMTYLTGDA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618 161 VLFSNDAFGQHYCDEHLFNDEVDQTELYEQCQRYYANILTPFSRLVTPKITEILGFNLPVEMIATSHGVVWRDNPTQIVE 240
Cdd:PRK05452 161 VLFSNDAFGQHYCDEHLFNDEVDQTELFEQCQRYYANILTPFSRLVTPKITEILGFNLPVDMIATSHGVVWRDNPTQIVE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618 241 KYLEWAADYQEDRITIFYDTMSNNTRMMADAIAQGITEVDPRVAVKIFNVARSDKNDILTNVFRSKGVLVGTSTMNNVMM 320
Cdd:PRK05452 241 LYLKWAADYQEDRITIFYDTMSNNTRMMADAIAQGIAEVDPRVAVKIFNVARSDKNEILTNVFRSKGVLVGSSTMNNVMM 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618 321 PKIAGLVEEMTGLRFRNKRASAFGSHGWSGGAVDRLSTRLQDAGFEMSLSLKAKWRPDIDALELCRQHGRDIARQWALSP 400
Cdd:PRK05452 321 PKIAGLLEEITGLRFRNKRASAFGSHGWSGGAVDRLSTRLQDAGFEMSLSLKAKWRPDQDALELCREHGREIARQWALAP 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618 401 LPVAEAATTPEPQDcacAAAAAADLGPMMQCSVCQWVYDPAKGEPNQDVQPGTPWSEVPDNFLCPECSLGKDVFDVLATE 480
Cdd:PRK05452 401 LPQSTVNTVVKEET---SATTTADLGPRMQCSVCQWIYDPAKGEPMQDVAPGTPWSEVPDNFLCPECSLGKDVFDELASE 477


                 ..
gi 490247618 481 AK 482
Cdd:PRK05452 478 AK 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: 555.60  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618   1 MSIVVKNNILWVGQRDWEVRDFHGtEYKTLRGSSYNSYLIREEKNVLIDTVDHKFSREFVQNLRREIDLADLDYIVINHA 80
Cdd:COG0426    1 QAVEIAHGVYWVGVLDWDRRLFEG-EYPTPRGTTYNSYLIVDEKTALIDTVGESFFEEFLENLSKVIDPKKIDYIIVNHQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618  81 EEDHAGALTELMMQIPDTPIYCTANAIDSINGHHHHPEWNFHVVKTGDTLDIGnGKQLIFVETPMLHWPDSMMTYLTGDA 160
Cdd:COG0426   80 EPDHSGSLPELLELAPNAKIVCSKKAARFLPHFYGIPDFRFIVVKEGDTLDLG-GHTLQFIPAPMLHWPDTMFTYDPEDK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618 161 VLFSNDAFGQHYCDEHLFNDEVDQtELYEQCQRYYANILTPFSRLVTPKITEILGfnLPVEMIATSHGVVWRDNPTQIVE 240
Cdd:COG0426  159 ILFSGDAFGSHGASDELFDDEVDE-HLEEEARRYYANIMMPFSKQVLKALKKVRG--LDIDMIAPSHGPIWRGNPKEILD 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618 241 KYLEWAADYQEDRITIFYDTMSNNTRMMADAIAQGITEVDprVAVKIFNVARSDKNDILTNVFRSKGVLVGTSTMNNVMM 320
Cdd:COG0426  236 WYRKWSSYQPEKKVVIVYASMYGNTEKMAEAIAEGLTEEG--VKVKLYDLEKTDPSEIITEIFDAKGIVIGSPTYNGGAF 313

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490247618 321 PKIAGLVEEMTGLRFRNKRASAFGSHGWSGGAVDRLSTRLQDAGFEMSL-SLKAKWRPDIDALELCRQHGRDIAR 394
Cdd:COG0426  314 PPIADLLGYLKGLAPKNKLAGAFGSYGWSGEAVKLLEEKLEDAGFEVVFePLRVKFKPTEEDLKKCEELGTDLAQ 388
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 5-246 1.15e-115

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: 339.85  E-value: 1.15e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618   5 VKNNILWVGQRDWEVRDFHGtEYKTLRGSSYNSYLIREEKNVLIDTVDHKFSREFVQNLRREIDLADLDYIVINHAEEDH 84
Cdd:cd07709    3 IADDIYWVGVNDWDLRLFEG-EYPTPRGTSYNSYLIKDEKTALIDTVKEPFFDEFLENLEEVIDPRKIDYIVVNHQEPDH 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618  85 AGALTELMMQIPDTPIYCTANAIDSINGHHHHPEWNFHVVKTGDTLDIGNgKQLIFVETPMLHWPDSMMTYLTGDAVLFS 164
Cdd:cd07709   82 SGSLPELLELAPNAKIVCSKKAARFLKHFYPGIDERFVVVKDGDTLDLGK-HTLKFIPAPMLHWPDTMVTYDPEDKILFS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618 165 NDAFGQHYCDEHLFNDEVDqtELYEQCQRYYANILTPFSRLVTPKITEILGfnLPVEMIATSHGVVWRDNPTQIVEKYLE 244
Cdd:cd07709  161 GDAFGAHGASGELFDDEVE--DYLEEARRYYANIMGPFSKQVRKALEKLEA--LDIKMIAPSHGPIWRKDPGEIIDLYRD 236


                 ..
gi 490247618 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 7.66e-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: 106.48  E-value: 7.66e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618    36 NSYLIR-EEKNVLIDTVdHKFSREFVQNLRReIDLADLDYIVINHAEEDHAGALTELmMQIPDTPIYCTANAIDSINGHH 114
Cdd:smart00849   1 NSYLVRdDGGAILIDTG-PGEAEDLLAELKK-LGPKKIDAIILTHGHPDHIGGLPEL-LEAPGAPVYAPEGTAELLKDLL 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490247618   115 H---------HPEWNFHVVKTGDTLDIGNGKqLIFVETPMlHWPDSMMTYLTGDAVLFSNDAFGQHYCDEHLF 178
Cdd:smart00849  78 AllgelgaeaEPAPPDRTLKDGDELDLGGGE-LEVIHTPG-HTPGSIVLYLPEGKILFTGDLLFAGGDGRTLV 148
Rubredoxin pfam00301
Rubredoxin;
429-474 6.22e-21

Rubredoxin;


Pssm-ID: 459752 [Multi-domain]  Cd Length: 46  Bit Score: 85.76  E-value: 6.22e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 490247618  429 MQCSVCQWVYDPAKGEPNQDVQPGTPWSEVPDNFLCPECSLGKDVF 474
Cdd:pfam00301   1 YECKVCGYVYDPAKGDPDNGIPPGTPFEDLPDDWVCPDCGAGKDQF 46
flav_short TIGR01753
flavodoxin, short chain; Flavodoxins are small redox-active proteins with a flavin ...
 254-393 5.05e-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: 86.24  E-value: 5.05e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618  254 ITIFYDTMSNNTRMMADAIAQGITEVDPRVavKIFNVARSDKNDILTnvfrSKGVLVGTSTMNNVMMPK--IAGLVEEMT 331
Cdd:TIGR01753   1 ILIVYASMTGNTEEMANIIAEGLKEAGAEV--DLLEVADADAEDLLS----YDAVLLGCSTWGDEDLEQddFEPFFEELE 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490247618  332 GLRFRNKRASAFGSHGWS---GGAVDRLSTRLQDAGFEMSL-SLKAKWRPDIDALELCRQHGRDIA 393
Cdd:TIGR01753  75 DIDLGGKKVALFGSGDWGyefCEAVDDWEERLKEAGATIIAeGLKVDGDPEEEDLDKCREFAKDLA 140
 
Name Accession Description Interval E-value
PRK05452 PRK05452
anaerobic nitric oxide reductase flavorubredoxin; Provisional
 1-482 0e+00

anaerobic nitric oxide reductase flavorubredoxin; Provisional


Pssm-ID: 235475 [Multi-domain]  Cd Length: 479  Bit Score: 1090.18  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618   1 MSIVVKNNILWVGQRDWEVRDFHGTEYKTLRGSSYNSYLIREEKNVLIDTVDHKFSREFVQNLRREIDLADLDYIVINHA 80
Cdd:PRK05452   1 MSIHVKNNIHWVGQRDWEVRDFHGTEYKTLRGSSYNSYLIREEKNVLIDTVDHKFSREFVQNLRNEIDLADIDYIVINHA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618  81 EEDHAGALTELMMQIPDTPIYCTANAIDSINGHHHHPEWNFHVVKTGDTLDIGNGKQLIFVETPMLHWPDSMMTYLTGDA 160
Cdd:PRK05452  81 EEDHAGALTELMAQIPDTPIYCTANAIDSINGHHHHPEWNFNVVKTGDTLDIGNGKQLIFVETPMLHWPDSMMTYLTGDA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618 161 VLFSNDAFGQHYCDEHLFNDEVDQTELYEQCQRYYANILTPFSRLVTPKITEILGFNLPVEMIATSHGVVWRDNPTQIVE 240
Cdd:PRK05452 161 VLFSNDAFGQHYCDEHLFNDEVDQTELFEQCQRYYANILTPFSRLVTPKITEILGFNLPVDMIATSHGVVWRDNPTQIVE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618 241 KYLEWAADYQEDRITIFYDTMSNNTRMMADAIAQGITEVDPRVAVKIFNVARSDKNDILTNVFRSKGVLVGTSTMNNVMM 320
Cdd:PRK05452 241 LYLKWAADYQEDRITIFYDTMSNNTRMMADAIAQGIAEVDPRVAVKIFNVARSDKNEILTNVFRSKGVLVGSSTMNNVMM 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618 321 PKIAGLVEEMTGLRFRNKRASAFGSHGWSGGAVDRLSTRLQDAGFEMSLSLKAKWRPDIDALELCRQHGRDIARQWALSP 400
Cdd:PRK05452 321 PKIAGLLEEITGLRFRNKRASAFGSHGWSGGAVDRLSTRLQDAGFEMSLSLKAKWRPDQDALELCREHGREIARQWALAP 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618 401 LPVAEAATTPEPQDcacAAAAAADLGPMMQCSVCQWVYDPAKGEPNQDVQPGTPWSEVPDNFLCPECSLGKDVFDVLATE 480
Cdd:PRK05452 401 LPQSTVNTVVKEET---SATTTADLGPRMQCSVCQWIYDPAKGEPMQDVAPGTPWSEVPDNFLCPECSLGKDVFDELASE 477


                 ..
gi 490247618 481 AK 482
Cdd:PRK05452 478 AK 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: 662.93  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618   5 VKNNILWVGQRDWEVRDFHGTEYKTLRGSSYNSYLIREEKNVLIDTVDHKFSREFVQNLRREIDLADLDYIVINHAEEDH 84
Cdd:PRK11921   3 INDNVTWVGKIDWELRKFHGEEYSTHRGSSYNSYLIKDEKTVLIDTVWQPFAKEFVENLKKEIDLDKIDYIVANHGEIDH 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618  85 AGALTELMMQIPDTPIYCTANAIDSINGHHHHpEWNFHVVKTGDTLDIGNgKQLIFVETPMLHWPDSMMTYLTGDAVLFS 164
Cdd:PRK11921  83 SGALPELMKEIPDTPIYCTKNGAKSLKGHYHQ-DWNFVVVKTGDRLEIGS-NELIFIEAPMLHWPDSMFTYLTGDNILFS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618 165 NDAFGQHYCDEHLFNDEVDQTELYEQCQRYYANILTPFSRLVTPKITEILGFNLPVEMIATSHGVVWRDNPTQIVEKYLE 244
Cdd:PRK11921 161 NDAFGQHYASELMYNDLVDQGELYQEAIKYYANILTPFSPLVIKKIEEILSLNLPVDMICPSHGVIWRDNPLQIVEKYLE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618 245 WAADYQEDRITIFYDTMSNNTRMMADAIAQGITEVDPRVAVKIFNVARSDKNDILTNVFRSKGVLVGTSTMNNVMMPKIA 324
Cdd:PRK11921 241 WAANYQENQVTILYDTMWNSTRRMAEAIAEGIKKANKDVTVKLYNSAKSDKNDIITEVFKSKAILVGSSTINRGILSSTA 320

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490247618 325 GLVEEMTGLRFRNKRASAFGSHGWSGGAVDRLSTRLQDAGFE-MSLSLKAKWRPDIDALELCRQHGRDIARQ 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: 555.60  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618   1 MSIVVKNNILWVGQRDWEVRDFHGtEYKTLRGSSYNSYLIREEKNVLIDTVDHKFSREFVQNLRREIDLADLDYIVINHA 80
Cdd:COG0426    1 QAVEIAHGVYWVGVLDWDRRLFEG-EYPTPRGTTYNSYLIVDEKTALIDTVGESFFEEFLENLSKVIDPKKIDYIIVNHQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618  81 EEDHAGALTELMMQIPDTPIYCTANAIDSINGHHHHPEWNFHVVKTGDTLDIGnGKQLIFVETPMLHWPDSMMTYLTGDA 160
Cdd:COG0426   80 EPDHSGSLPELLELAPNAKIVCSKKAARFLPHFYGIPDFRFIVVKEGDTLDLG-GHTLQFIPAPMLHWPDTMFTYDPEDK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618 161 VLFSNDAFGQHYCDEHLFNDEVDQtELYEQCQRYYANILTPFSRLVTPKITEILGfnLPVEMIATSHGVVWRDNPTQIVE 240
Cdd:COG0426  159 ILFSGDAFGSHGASDELFDDEVDE-HLEEEARRYYANIMMPFSKQVLKALKKVRG--LDIDMIAPSHGPIWRGNPKEILD 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618 241 KYLEWAADYQEDRITIFYDTMSNNTRMMADAIAQGITEVDprVAVKIFNVARSDKNDILTNVFRSKGVLVGTSTMNNVMM 320
Cdd:COG0426  236 WYRKWSSYQPEKKVVIVYASMYGNTEKMAEAIAEGLTEEG--VKVKLYDLEKTDPSEIITEIFDAKGIVIGSPTYNGGAF 313

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490247618 321 PKIAGLVEEMTGLRFRNKRASAFGSHGWSGGAVDRLSTRLQDAGFEMSL-SLKAKWRPDIDALELCRQHGRDIAR 394
Cdd:COG0426  314 PPIADLLGYLKGLAPKNKLAGAFGSYGWSGEAVKLLEEKLEDAGFEVVFePLRVKFKPTEEDLKKCEELGTDLAQ 388
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 5-246 1.15e-115

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: 339.85  E-value: 1.15e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618   5 VKNNILWVGQRDWEVRDFHGtEYKTLRGSSYNSYLIREEKNVLIDTVDHKFSREFVQNLRREIDLADLDYIVINHAEEDH 84
Cdd:cd07709    3 IADDIYWVGVNDWDLRLFEG-EYPTPRGTSYNSYLIKDEKTALIDTVKEPFFDEFLENLEEVIDPRKIDYIVVNHQEPDH 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618  85 AGALTELMMQIPDTPIYCTANAIDSINGHHHHPEWNFHVVKTGDTLDIGNgKQLIFVETPMLHWPDSMMTYLTGDAVLFS 164
Cdd:cd07709   82 SGSLPELLELAPNAKIVCSKKAARFLKHFYPGIDERFVVVKDGDTLDLGK-HTLKFIPAPMLHWPDTMVTYDPEDKILFS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618 165 NDAFGQHYCDEHLFNDEVDqtELYEQCQRYYANILTPFSRLVTPKITEILGfnLPVEMIATSHGVVWRDNPTQIVEKYLE 244
Cdd:cd07709  161 GDAFGAHGASGELFDDEVE--DYLEEARRYYANIMGPFSKQVRKALEKLEA--LDIKMIAPSHGPIWRKDPGEIIDLYRD 236


                 ..
gi 490247618 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 7.66e-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: 106.48  E-value: 7.66e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618    36 NSYLIR-EEKNVLIDTVdHKFSREFVQNLRReIDLADLDYIVINHAEEDHAGALTELmMQIPDTPIYCTANAIDSINGHH 114
Cdd:smart00849   1 NSYLVRdDGGAILIDTG-PGEAEDLLAELKK-LGPKKIDAIILTHGHPDHIGGLPEL-LEAPGAPVYAPEGTAELLKDLL 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490247618   115 H---------HPEWNFHVVKTGDTLDIGNGKqLIFVETPMlHWPDSMMTYLTGDAVLFSNDAFGQHYCDEHLF 178
Cdd:smart00849  78 AllgelgaeaEPAPPDRTLKDGDELDLGGGE-LEVIHTPG-HTPGSIVLYLPEGKILFTGDLLFAGGDGRTLV 148
NorV COG1773
Flavorubredoxin [Inorganic ion transport and metabolism];
429-477 1.68e-21

Flavorubredoxin [Inorganic ion transport and metabolism];


Pssm-ID: 441379 [Multi-domain]  Cd Length: 53  Bit Score: 87.53  E-value: 1.68e-21
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 490247618 429 MQCSVCQWVYDPAKGEPNQDVQPGTPWSEVPDNFLCPECSLGKDVFDVL 477
Cdd:COG1773    4 YQCKVCGYVYDPAEGDPENGIPPGTPFEDLPDDWVCPVCGAGKEDFEPV 52
Rubredoxin pfam00301
Rubredoxin;
429-474 6.22e-21

Rubredoxin;


Pssm-ID: 459752 [Multi-domain]  Cd Length: 46  Bit Score: 85.76  E-value: 6.22e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 490247618  429 MQCSVCQWVYDPAKGEPNQDVQPGTPWSEVPDNFLCPECSLGKDVF 474
Cdd:pfam00301   1 YECKVCGYVYDPAKGDPDNGIPPGTPFEDLPDDWVCPDCGAGKDQF 46
rubredoxin cd00730
Rubredoxin; nonheme iron binding domains containing a [Fe(SCys)4] center. Rubredoxins are ...
 428-477 7.90e-21

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: 85.44  E-value: 7.90e-21
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 490247618 428 MMQCSVCQWVYDPAKGEPNQDVQPGTPWSEVPDNFLCPECSLGKDVFDVL 477
Cdd:cd00730    1 KYECRICGYIYDPAEGDPDEGIPPGTPFEDLPDDWVCPVCGAGKDDFEPL 50
flav_short TIGR01753
flavodoxin, short chain; Flavodoxins are small redox-active proteins with a flavin ...
 254-393 5.05e-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: 86.24  E-value: 5.05e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618  254 ITIFYDTMSNNTRMMADAIAQGITEVDPRVavKIFNVARSDKNDILTnvfrSKGVLVGTSTMNNVMMPK--IAGLVEEMT 331
Cdd:TIGR01753   1 ILIVYASMTGNTEEMANIIAEGLKEAGAEV--DLLEVADADAEDLLS----YDAVLLGCSTWGDEDLEQddFEPFFEELE 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490247618  332 GLRFRNKRASAFGSHGWS---GGAVDRLSTRLQDAGFEMSL-SLKAKWRPDIDALELCRQHGRDIA 393
Cdd:TIGR01753  75 DIDLGGKKVALFGSGDWGyefCEAVDDWEERLKEAGATIIAeGLKVDGDPEEEDLDKCREFAKDLA 140
Flavodoxin_1 pfam00258
Flavodoxin;
256-389 1.13e-16

Flavodoxin;


Pssm-ID: 425562 [Multi-domain]  Cd Length: 142  Bit Score: 76.64  E-value: 1.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618  256 IFYDTMSNNTRMMADAIAQGITEVDPRV-AVKIFNVARsDKNDILTNVFRSKGVL---VGTSTMNNVmmPKIAGLVEEMT 331
Cdd:pfam00258   1 IFYGSQTGNTEKLAEAIAEGLGEAGFEVdVVDLDDVDE-TLSEIEEEDLLLVVVStwgEGEPPDNAK--PFVDWLLLFGT 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490247618  332 --GLRFRNKR--ASAFGSHGWSG--GAVDRLSTRLQDAGFEMSLS-LKAKWRPDIDALELCRQHG 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 2.46e-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: 76.94  E-value: 2.46e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618  36 NSYLIREEKN--VLIDTVDHkfSREFVQNLRREIDLaDLDYIVINHAEEDHAGALTELmMQIPDTPIYCTANAID----- 108
Cdd:cd06262   11 NCYLVSDEEGeaILIDPGAG--ALEKILEAIEELGL-KIKAILLTHGHFDHIGGLAEL-KEAPGAPVYIHEADAElledp 86

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490247618 109 -----SINGHHHHPEWNFHVVKTGDTLDIGNGKqLIFVETPMlHWPDSMMTYLTGDAVLFSND 166
Cdd:cd06262   87 elnlaFFGGGPLPPPEPDILLEDGDTIELGGLE-LEVIHTPG-HTPGSVCFYIEEEGVLFTGD 147
FldA COG0716
Flavodoxin [Energy production and conversion]; Flavodoxin is part of the Pathway/BioSystem: ...
 254-397 4.28e-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: 74.94  E-value: 4.28e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618 254 ITIFYDTMSNNTRMMADAIAQGITEVDprvaVKIFNVARSDKNDILtnvfRSKGVLVGTSTMNNVMMPKIAGLVEEMTGl 333
Cdd:COG0716    1 ILIVYGSTTGNTEKVAEAIAEALGAAG----VDLFEIEDADLDDLE----DYDLLILGTPTWAGELPDDWEDFLEELKE- 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490247618 334 RFRNKRASAFGSHGWSGG--AVDRLSTRLQDAGFEM--SLSLKAKWRPDIDALElcrqhgrDIARQWA 397
Cdd:COG0716   72 DLSGKKVALFGTGDSSGYgdALGELKELLEEKGAKVvgGYDFEGSKAPDAEDTE-------ERAEEWL 132
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 36-254 5.00e-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: 5.00e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618  36 NSYLIR-EEKNVLIDTVDHKFSREFVQNLRREIDLaDLDYIVINHAEEDHAGALTELmMQIPDTPIYCTANAIDSINGHH 114
Cdd:COG0491   16 NSYLIVgGDGAVLIDTGLGPADAEALLAALAALGL-DIKAVLLTHLHPDHVGGLAAL-AEAFGAPVYAHAAEAEALEAPA 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618 115 HHPEWNF------HVVKTGDTLDIGNGKqLIFVETPMlHWPDSMMTYLTGDAVLFSNDAFGQHYCDeHLFNDEVDQTELY 188
Cdd:COG0491   94 AGALFGRepvppdRTLEDGDTLELGGPG-LEVIHTPG-HTPGHVSFYVPDEKVLFTGDALFSGGVG-RPDLPDGDLAQWL 170

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490247618 189 EQCQRYYAniltpfsrlvtpkiteilgfnLPVEMIATSHGVVWRDNPTQIVEKYLEWAADYQEDRI 254
Cdd:COG0491  171 ASLERLLA---------------------LPPDLVIPGHGPPTTAEAIDYLEELLAALGERANPFL 215
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
36-171 3.87e-12

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 65.08  E-value: 3.87e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618   36 NSYLIR-EEKNVLIDTVDHKFSREFVQNLRREIDLADLDYIVINHAEEDHAGALTELmMQIPDTPIYCTANAIDSINGHH 114
Cdd:pfam00753   7 NSYLIEgGGGAVLIDTGGSAEAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGEL-AEATDVPVIVVAEEARELLDEE 85

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618  115 HHPEWNFH-------------VVKTGDTLDIGNGKQLIFVETPmLHWPDSMMTYLTGDAVLFSNDAFGQH 171
Cdd:pfam00753  86 LGLAASRLglpgppvvplppdVVLEEGDGILGGGLGLLVTHGP-GHGPGHVVVYYGGGKVLFTGDLLFAG 154
PRK06756 PRK06756
flavodoxin; Provisional
 253-394 3.11e-11

flavodoxin; Provisional


Pssm-ID: 168663 [Multi-domain]  Cd Length: 148  Bit Score: 61.43  E-value: 3.11e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618 253 RITIFYDTMSNNTRMMADAIAQGITEVDPRVAVKifNVARSDKNDILTnvfRSKGVLVGTSTMNNVMMP-KIAGLVEEMT 331
Cdd:PRK06756   3 KLVMIFASMSGNTEEMADHIAGVIRETENEIEVI--DIMDSPEASILE---QYDGIILGAYTWGDGDLPdDFLDFYDAMD 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490247618 332 GLRFRNKRASAFGSHGWS----GGAVDRLSTRLQDAGFEMSLS-LKAKWRPDIDALELCRQHGRDIAR 394
Cdd:PRK06756  78 SIDLTGKKAAVFGSCDSAypkyGVAVDILIEKLQERGAAVVLEgLKVELTPEDEDVEKCLQFGAEFVK 145
PRK05569 PRK05569
flavodoxin; Provisional
 253-394 4.65e-10

flavodoxin; Provisional


Pssm-ID: 135442 [Multi-domain]  Cd Length: 141  Bit Score: 57.92  E-value: 4.65e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618 253 RITIFYDTMSNNTRMMADAIAQGITEVDPRVAVKifNVARSDKNDILtnvfRSKGVLVGTSTM--NNVMMPKIAGLVEEM 330
Cdd:PRK05569   3 KVSIIYWSCGGNVEVLANTIADGAKEAGAEVTIK--HVADAKVEDVL----EADAVAFGSPSMdnNNIEQEEMAPFLDQF 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490247618 331 TGLRFRNKRASAFGSHGWSGGA-VDRLSTRLQDAGFEMSLSLKAKWRPDIDALELCRQHGRDIAR 394
Cdd:PRK05569  77 KLTPNENKKCILFGSYGWDNGEfMKLWKDRMKDYGFNVIGDLAVNESPNKEELNSAKELGKKLAK 141
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 37-159 7.81e-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: 59.56  E-value: 7.81e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618  37 SYLIR-EEKNVLIDT----VdhkfsreFVQNLRR-EIDLADLDYIVINHAEEDHAGALTELMMQIPDTPIYCTANAIDSi 110
Cdd:cd07713   22 SLLIEtEGKKILFDTgqsgV-------LLHNAKKlGIDLSDIDAVVLSHGHYDHTGGLKALLELNPKAPVYAHPDAFEP- 93

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 490247618 111 ngHHHHPEWNFHVVKTGDTLDIGNGKQLIFVETPMLHWPDsmmTYLTGD 159
Cdd:cd07713   94 --RYSKRGGGKKGIGIGREELEKAGARLVLVEEPTEIAPG---VYLTGE 137
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 36-168 9.79e-10

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


Pssm-ID: 293807 [Multi-domain]  Cd Length: 202  Bit Score: 58.00  E-value: 9.79e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618  36 NSYLIREEKN-VLIDTVDHKFSREFVQNLRRE-IDLADLDYIVINHAEEDHAGALTELmMQIPDTPIYCTANAIDSING- 112
Cdd:cd07721   12 NAYLIEDDDGlTLIDTGLPGSAKRILKALRELgLSPKDIRRILLTHGHIDHIGSLAAL-KEAPGAPVYAHEREAPYLEGe 90

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490247618 113 ---------------HHHHPEWNFHVVKT---GDTLDIGNGkqLIFVETPMlHWPDSMMTYLTGDAVLFSNDAF 168
Cdd:cd07721   91 kpypppvrlgllgllSPLLPVKPVPVDRTledGDTLDLAGG--LRVIHTPG-HTPGHISLYLEEDGVLIAGDAL 161
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 37-176 6.52e-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: 52.88  E-value: 6.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618  37 SYLIREE-KNVLIDT-----VDHkfSREFVQNLRreIDLADLDYIVINHAEEDHAGALTELMMQIPDTPIYCTANA---- 106
Cdd:cd07726   18 SYLLDGEgRPALIDTgpsssVPR--LLAALEALG--IAPEDVDYIILTHIHLDHAGGAGLLAEALPNAKVYVHPRGarhl 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618 107 ID---------SINGHHHHPEW---------NFHVVKTGDTLDIGnGKQLIFVETPMlHWPDSMMTYLTGDAVLFSNDAF 168
Cdd:cd07726   94 IDpsklwasarAVYGDEADRLGgeilpvpeeRVIVLEDGETLDLG-GRTLEVIDTPG-HAPHHLSFLDEESDGLFTGDAA 171


                 ....*...
gi 490247618 169 GQHYCDEH 176
Cdd:cd07726  172 GVRYPELD 179
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 36-167 1.11e-07

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


Pssm-ID: 293811 [Multi-domain]  Cd Length: 184  Bit Score: 51.92  E-value: 1.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618  36 NSYLIR-EEKNVLIDT-VDHKFSREFVQNLRRE--IDLADLDYIVINHAEEDHAGALTELmmqipdtpiyCTANAIDSIn 111
Cdd:cd07725   16 NVYLLRdGDETTLIDTgLATEEDAEALWEGLKElgLKPSDIDRVLLTHHHPDHIGLAGKL----------QEKSGATVY- 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 490247618 112 ghhhHPEWNFhvVKTGDTLDIGnGKQLIFVETPMlHWPDSMMTYLTGDAVLFSNDA 167
Cdd:cd07725   85 ----ILDVTP--VKDGDKIDLG-GLRLKVIETPG-HTPGHIVLYDEDRRELFVGDA 132
PRK05568 PRK05568
flavodoxin; Provisional
 253-394 1.86e-07

flavodoxin; Provisional


Pssm-ID: 235508 [Multi-domain]  Cd Length: 142  Bit Score: 50.19  E-value: 1.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618 253 RITIFYDTMSNNTRMMADAIAQGITEVDprVAVKIFNVARSDKNDiltnVFRSKGVLVGTSTM------NNVMMPkiagL 326
Cdd:PRK05568   3 KINIIYWSGTGNTEAMANLIAEGAKENG--AEVKLLNVSEASVDD----VKGADVVALGSPAMgdevleEGEMEP----F 72

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618 327 VEEMTGLrFRNKRASAFGSHGW-SGGAVDRLSTRLQDAGFEM-SLSLKAKWRPDIDALELCRQHGRDIAR 394
Cdd:PRK05568  73 VESISSL-VKGKKLVLFGSYGWgDGEWMRDWVERMEGYGANLvNEGLIVNNTPEGEGIEKCKALGEALAK 141
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 37-166 3.76e-07

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: 49.77  E-value: 3.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618  37 SYLIREEKN---VLIDTVDHKFSREFVQNLRreidlADLDYIVINHAEEDHAGALTELMMQIPDTPIYctANAIDSINGH 113
Cdd:cd07723   11 IYLIVDEATgeaAVVDPGEAEPVLAALEKNG-----LTLTAILTTHHHWDHTGGNAELKALFPDAPVY--GPAEDRIPGL 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 490247618 114 HhhpewnfHVVKTGDTLDIGNGKqLIFVETPMlHWPDSMMTYLTGDAVLFSND 166
Cdd:cd07723   84 D-------HPVKDGDEIKLGGLE-VKVLHTPG-HTLGHICYYVPDEPALFTGD 127
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 75-166 6.07e-07

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: 50.48  E-value: 6.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618  75 IVINHAEEDHAGALTELMMQIpDTPIYCTANAI----DSINGHHHHPEWNFHVVKTGDTLDIGNgkqlIFVET-PMLH-W 148
Cdd:cd07714   59 IFITHGHEDHIGALPYLLPEL-NVPIYATPLTLalikKKLEEFKLIKKVKLNEIKPGERIKLGD----FEVEFfRVTHsI 133

                         90       100
                 ....*....|....*....|
gi 490247618 149 PDSMMTYLTGDA--VLFSND 166
Cdd:cd07714  134 PDSVGLAIKTPEgtIVHTGD 153
RnjA COG0595
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];
67-134 7.92e-07

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


Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 51.60  E-value: 7.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618  67 IDL--ADLDY----------IVINHAEEDHAGALTELMMQIpDTPIYCTANAIDSING----HHHHPEWNFHVVKTGDTL 130
Cdd:COG0595   47 VDLviPDISYleenkdkikgIVLTHGHEDHIGALPYLLKEL-NVPVYGTPLTLALLEAklkeHGLLKKVKLHVVKPGDRI 125


                 ....
gi 490247618 131 DIGN 134
Cdd:COG0595  126 KFGP 129
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 36-164 1.31e-06

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 49.15  E-value: 1.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618  36 NSYLIR-EEKNVLID-TVDHKFSREFVQNLRREiDLADLDYIVINHAEEDHAGALTELMMQIPDTPIYCTANAIDSINGH 113
Cdd:COG2220   12 ATFLIEtGGKRILIDpVFSGRASPVNPLPLDPE-DLPKIDAVLVTHDHYDHLDDATLRALKRTGATVVAPLGVAAWLRAW 90

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490247618 114 HHHpewNFHVVKTGDTLDIGNGKqlifVE-TPMLHWP---DSMMT--------------YLTGDAVLFS 164
Cdd:COG2220   91 GFP---RVTELDWGESVELGGLT----VTaVPARHSSgrpDRNGGlwvgfvietdgktiYHAGDTGYFP 152
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 29-166 7.40e-06

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: 46.37  E-value: 7.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618  29 TLRGSsyNSYLIREEKN-VLIDTVDHKfsREFVQNLRREID---LADLDYIVINHAEEDHAGALTELMMQIPDTPIycta 104
Cdd:cd07722   14 TLQGT--NTYLVGTGKRrILIDTGEGR--PSYIPLLKSVLDsegNATISDILLTHWHHDHVGGLPDVLDLLRGPSP---- 85

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618 105 naidSINGHHHHPEWNFHVVKTGDTLDIGNGkQLIFVE--------TPMlHWPDSMMTYLTGDAVLFSND 166
Cdd:cd07722   86 ----RVYKFPRPEEDEDPDEDGGDIHDLQDG-QVFKVEgatlrvihTPG-HTTDHVCFLLEEENALFTGD 149
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 32-104 1.28e-05

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: 45.91  E-value: 1.28e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490247618  32 GSSYnsyLIR-EEKNVLIDTVDHKFSREFVQNLRRE--IDLADLDYIVINHAEEDHAGALTELMMQIPDTPIYCTA 104
Cdd:cd16295   12 GSCY---LLEtGGKRILLDCGLFQGGKELEELNNEPfpFDPKEIDAVILTHAHLDHSGRLPLLVKEGFRGPIYATP 84
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 36-104 1.56e-05

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 47.10  E-value: 1.56e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618  36 NSYLIR-EEKNVLIDTVDHkFSREFVQNLRREIDLADLDYIVINHAEEDHAGALTELMMQIPDTPIYCTA 104
Cdd:COG1236   15 SCYLLEtGGTRILIDCGLF-QGGKERNWPPFPFRPSDVDAVVLTHAHLDHSGALPLLVKEGFRGPIYATP 83
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 37-147 1.61e-05

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: 45.54  E-value: 1.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618  37 SYLIR-EEKNVLIDTvdhkfSREFVQNLRREiDLADLDYIVINHAEEDHAGALTEL----MMQIPDTPIYCTANAIDSI- 110
Cdd:cd16279   37 SILIEtGGKNILIDT-----GPDFRQQALRA-GIRKLDAVLLTHAHADHIHGLDDLrpfnRLQQRPIPVYASEETLDDLk 110

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 490247618 111 ---------NGHHHHPEWNFHVVKTGDTLDIGnGKQLIFVetPMLH 147
Cdd:cd16279  111 rrfpyffaaTGGGGVPKLDLHIIEPDEPFTIG-GLEITPL--PVLH 153
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 24-183 5.24e-05

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: 43.79  E-value: 5.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618  24 GTEYKTLRGSSyNSYLIR-EEKNVLIDTVDHKFSRefvqnLRRE-IDLADLDYIVINHAEEDHAGALTELMMQI----PD 97
Cdd:cd16272    7 GGAVPSLTRNT-SSYLLEtGGTRILLDCGEGTVYR-----LLKAgVDPDKLDAIFLSHFHLDHIGGLPTLLFARryggRK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618  98 TP--IYC---TANAIDSINGHHHHPEW-----NFHVVK-TGDTLDIGNGKqlifVET-PMLHWPDSMMTYLT--GDAVLF 163
Cdd:cd16272   81 KPltIYGpkgIKEFLEKLLNFPVEILPlgfplEIEELEeGGEVLELGDLK----VEAfPVKHSVESLGYRIEaeGKSIVY 156

                        170       180
                 ....*....|....*....|.
gi 490247618 164 SNDAfgqHYCDEHL-FNDEVD 183
Cdd:cd16272  157 SGDT---GPCENLVeLAKGAD 174
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 29-166 7.86e-05

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


Pssm-ID: 293836 [Multi-domain]  Cd Length: 185  Bit Score: 43.25  E-value: 7.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618  29 TLRGSsyNSYLIREEKNVLI-----DTVDHkfsrefVQNLRREIDLADLDYIVINHAEEDHAGALTELMmQIPDTPIYCT 103
Cdd:cd16278   14 TLDGT--NTYLLGAPDGVVVidpgpDDPAH------LDALLAALGGGRVSAILVTHTHRDHSPGAARLA-ERTGAPVRAF 84

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490247618 104 ANAIDSINGHHHHPEwnfHVVKTGDTLDIGnGKQLIFVETPMlHWPDSMMTYLTGDAVLFSND 166
Cdd:cd16278   85 GPHRAGGQDTDFAPD---RPLADGEVIEGG-GLRLTVLHTPG-HTSDHLCFALEDEGALFTGD 142
rubredoxin_like cd00350
Rubredoxin_like; nonheme iron binding domain containing a [Fe(SCys)4] center. The family ...
 428-474 1.25e-04

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: 39.07  E-value: 1.25e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 490247618 428 MMQCSVCQWVYDPAKgepnqdvqpgtpwsevpDNFLCPECSLGKDVF 474
Cdd:cd00350    1 KYVCPVCGYIYDGEE-----------------APWVCPVCGAPKDKF 30
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 37-134 1.39e-04

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: 42.51  E-value: 1.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618  37 SYLIR-EEKNVLIDT--VDHKFSREFVQNLRRE-IDlaDLDYIVINHAEEDHAGALTELMMQIP-----------DTPIY 101
Cdd:cd07731   12 AILIQtPGKTILIDTgpRDSFGEDVVVPYLKARgIK--KLDYLILTHPDADHIGGLDAVLKNFPvkevympgvthTTKTY 89

                         90       100       110
                 ....*....|....*....|....*....|...
gi 490247618 102 ctANAIDSINGHHHHpewnFHVVKTGDTLDIGN 134
Cdd:cd07731   90 --EDLLDAIKEKGIP----VTPCKAGDRWQLGG 116
PRK06703 PRK06703
flavodoxin; Provisional
 253-397 1.54e-04

flavodoxin; Provisional


Pssm-ID: 235854 [Multi-domain]  Cd Length: 151  Bit Score: 42.05  E-value: 1.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618 253 RITIFYDTMSNNTRMMADAIAQGITEVDprVAVKIFNVARSDKNDILTnvfrSKGVLVGTSTMNNVMMPKIA-GLVEEMT 331
Cdd:PRK06703   3 KILIAYASMSGNTEDIADLIKVSLDAFD--HEVVLQEMDGMDAEELLA----YDGIILGSYTWGDGDLPYEAeDFHEDLE 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490247618 332 GLRFRNKRASAFGSHGWS----GGAVDRLSTRLQDAGFEM-SLSLKAKWRPDIDA-LELCRQHGRDIARqWA 397
Cdd:PRK06703  77 NIDLSGKKVAVFGSGDTAyplfCEAVTIFEERLVERGAELvQEGLKIELAPETDEdVEKCSNFAIAFAE-KF 147
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 37-133 3.29e-04

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: 42.44  E-value: 3.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618  37 SYLI-REEKNVLIDTVDHKFSREFVQNLRR-EIDLADLDYIVINHAEEDHAGAL--------TELMMQIPDTPIYCTANA 106
Cdd:cd16310   24 SYLItSNHGAILLDGGLEENAALIEQNIKAlGFKLSDIKIIINTHAHYDHAGGLaqlkadtgAKLWASRGDRPALEAGKH 103

                         90       100
                 ....*....|....*....|....*....
gi 490247618 107 I-DSINGHHHHPEWNF-HVVKTGDTLDIG 133
Cdd:cd16310  104 IgDNITQPAPFPAVKVdRILGDGEKIKLG 132
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 39-134 9.48e-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: 41.00  E-value: 9.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618  39 LIR--EEKNVLIDT---VDHKFSREFVQNLRREIDLADLDYIVINHAEEDHAGALTELMMQIP-----------DTPIYc 102
Cdd:COG2333   15 LIRtpDGKTILIDTgprPSFDAGERVVLPYLRALGIRRLDLLVLTHPDADHIGGLAAVLEAFPvgrvlvsgppdTSETY- 93

                         90       100       110
                 ....*....|....*....|....*....|..
gi 490247618 103 tANAIDSINGHHHhpewNFHVVKTGDTLDIGN 134
Cdd:COG2333   94 -ERLLEALKEKGI----PVRPCRAGDTWQLGG 120
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 36-188 1.38e-03

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: 40.02  E-value: 1.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618  36 NSYLIREEKN---VLIDTVDhkfsrEFVQNLRREIDLA-DLDYIVINHAEEDHAGALTELMMQiPDTPIYCtaNAIDSin 111
Cdd:cd16322   12 NTYLVADEGGgeaVLVDPGD-----ESEKLLARFGTTGlTLLYILLTHAHFDHVGGVADLRRH-PGAPVYL--HPDDL-- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618 112 GHHHHPE-----WNFHVVKT---------GDTLDIGNgkqLIF--VETPMlHWPDSMMTYLTGDAVLFSNDAFGQ----- 170
Cdd:cd16322   82 PLYEAADlgakaFGLGIEPLpppdrlledGQTLTLGG---LEFkvLHTPG-HSPGHVCFYVEEEGLLFSGDLLFQgsigr 157

                        170       180
                 ....*....|....*....|....*...
gi 490247618 171 ---HYCDEHLFN-------DEVDQTELY 188
Cdd:cd16322  158 tdlPGGDPKAMAaslrrllTLPDETRVF 185
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 45-148 1.91e-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: 1.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618   45 NVLIDTVdhkFSReFVQNLRR----EIDLADLDYIVINHAEEDH-AGALTelMMQIPDTPIYCTANAIDSINGH------ 113
Cdd:pfam12706   2 RILIDPG---PDL-RQQALPAlqpgRLRDDPIDAVLLTHDHYDHlAGLLD--LREGRPRPLYAPLGVLAHLRRNfpylfl 75

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 490247618  114 HHHPEWNFHVVKTGDTLDIGNGkQLIFVETPMLHW 148
Cdd:pfam12706  76 LEHYGVRVHEIDWGESFTVGDG-GLTVTATPARHG 109
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 32-167 2.23e-03

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


Pssm-ID: 293810 [Multi-domain]  Cd Length: 177  Bit Score: 38.92  E-value: 2.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618  32 GSSYNSYLIREEKN---VLIDTVdhkfsREFVQnlrREIDLA-----DLDYIVINHAEEDHAGALTELMmQIPDTPIYCt 103
Cdd:cd07724    9 GLGTLSYLVGDPETgeaAVIDPV-----RDSVD---RYLDLAaelglKITYVLETHVHADHVSGARELA-ERTGAPIVI- 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490247618 104 anaidsingHHHHPEWNFHV-VKTGDTLDIGNgKQLIFVETPMlHWPDSmMTYLTGDAV-LFSNDA 167
Cdd:cd07724   79 ---------GEGAPASFFDRlLKDGDVLELGN-LTLEVLHTPG-HTPES-VSYLVGDPDaVFTGDT 132
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 46-144 2.44e-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: 2.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618  46 VLIDTVD-HKFSREFVQNLRR-EIDLADLDYIVINHAEEDHAGAlTELMMQIPDTPIYCTANAIDSINGHHHHPEWNFH- 122
Cdd:cd16280   34 ILIDALNnNEAADLIVDGLEKlGLDPADIKYILITHGHGDHYGG-AAYLKDLYGAKVVMSEADWDMMEEPPEEGDNPRWg 112

                         90       100
                 ....*....|....*....|....*....
gi 490247618 123 -------VVKTGDTLDIGNgKQLIFVETP 144
Cdd:cd16280  113 ppperdiVIKDGDTLTLGD-TTITVYLTP 140
MG423 TIGR00649
beta-CASP ribonuclease, RNase J family; This family of metalloenzymes includes RNase J1 and ...
 75-159 2.90e-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: 40.03  E-value: 2.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618   75 IVINHAEEDHAGALTELMMQIPDTPIYCTANAI----DSINGHHHHPEWNFHVVKTGDTLDIGNGKQLIFVET------- 143
Cdd:TIGR00649  62 IFITHGHEDHIGAVPYLLHQVGFFPIYGTPLTIalikSKIKEHGLNVRTDLLEIHEGEPVEFGENTAIEFFRIthsipds 141

                          90
                  ....*....|....*...
gi 490247618  144 --PMLHWPDSMMTYlTGD 159
Cdd:TIGR00649 142 vgFALHTPLGYIVY-TGD 158
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 37-166 3.76e-03

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 38.97  E-value: 3.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618  37 SYLIREE---KNVLIDTVDhkfsREFVQNLRREIDlADLDYIVINHAEEDHAGALTELMMQIPDTPIYctANAIDSINGH 113
Cdd:PLN02469  14 AYLIIDEstkDAAVVDPVD----PEKVLQAAHEHG-AKIKLVLTTHHHWDHAGGNEKIKKLVPGIKVY--GGSLDNVKGC 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 490247618 114 HHHpewnfhvVKTGDTLDIGNGKQLIFVETPmLHWPDSMMTYLTG----DAVLFSND 166
Cdd:PLN02469  87 THP-------VENGDKLSLGKDVNILALHTP-CHTKGHISYYVTGkegeDPAVFTGD 135
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 21-163 6.25e-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: 37.98  E-value: 6.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247618  21 DFhGTEYKtlRGSSYNSYLIREEKNVLIDTVDHKFSREFVQNLRREIDLADLDYIVINHAEEDHAGALTELMmqiPDTPI 100
Cdd:cd07732   28 DF-GLPLD--PESKYFDEVLDFLELGLLPDIVGLYRDPLLLGGLRSEEDPSVDAVLLSHAHLDHYGLLNYLR---PDIPV 101

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490247618 101 YCTA------NAIDSINGHHHHPEWNFHVVKTGDTLDIGNgkqliFVETPML--H-WPDSMMTYL-TGDAVLF 163
Cdd:cd07732  102 YMGEatkrilKALLPFFGEGDPVPRNIRVFESGKSFTIGD-----FTVTPYLvdHsAPGAYAFLIeAPGKRIF 169
PHD2_KDM5A_like cd15516
PHD finger 2 found in Lysine-specific demethylase KDM5A, KDM5B, KDM5C, KDM5D, and similar ...
 426-467 9.92e-03

PHD finger 2 found in Lysine-specific demethylase KDM5A, KDM5B, KDM5C, KDM5D, and similar proteins; The JARID subfamily within the JmjC proteins includes Lysine-specific demethylase KDM5A, KDM5B, KDM5C, KDM5D and a Drosophila homolog protein, little imaginal discs (Lid). KDM5A was originally identified as a retinoblastoma protein (Rb)-binding partner and its inactivation may be important for Rb to promote differentiation. It is involved in transcription through interacting with TBP, p107, nuclear receptors, Myc, Sin3/HDAC, Mad1, RBP-J, CLOCK, and BMAL1. KDM5B has a restricted expression pattern in the testis, ovary, and transiently in the mammary gland of the pregnant female and has been shown to be upregulated in breast cancer, prostate cancer, and lung cancer, suggesting a potential role in tumorigenesis. Both KDM5A and KDM5B function as trimethylated histone H3 lysine 4 (H3K4me3) demethylases. KDM5C is a H3K4 trimethyl-histone demethylase that catalyzes demethylation of H3K4me3 and H3K4me2 to H3K4me1. It plays a role in neuronal survival and dendrite development. KDM5C defects are associated with X-linked mental retardation (XLMR). KDM5D is a male-specific antigen that shows a demethylase activity specific for di- and tri-methylated histone H3K4 (H3K4me3 and H3K4me2), and has a male-specific function as a histone H3K4 demethylase by recruiting a meiosis-regulatory protein, MSH5, to condensed DNA. KDM5D directly interacts with a polycomb-like protein Ring6a/MBLR, and plays a role in regulation of transcriptional initiation through H3K4 demethylation. The family also includes Drosophila melanogaster protein little imaginal discs (Lid) that functions as a JmjC-dependent trimethyl histone H3K4 (H3K4me3) demethylase, which is required for dMyc-induced cell growth. It positively regulates Hox gene expression in S2 cells. Members in this family contain the catalytic JmjC domain, JmjN, the BRIGHT domain, which is an AT-rich interacting domain (ARID), and a Cys5HisCys2 zinc finger, as well as two or three plant homeodomain (PHD) fingers. This model corresponds to the second PHD finger.


Pssm-ID: 276991  Cd Length: 53  Bit Score: 34.21  E-value: 9.92e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 490247618 426 GPMMQCSVCQ-WVYDPAKGEPNQDVQP-GTPWSEVPDNFLCPEC 467
Cdd:cd15516   10 AGMLQCELCQdWFHGSCVAVPRISSSPrPLAWWEGDRKFLCPLC 53
 
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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