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Conserved domains on  [gi|1940529019|gb|KAF9894576|]
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hypothetical protein FE257_006462 [Aspergillus nanangensis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DUF455 pfam04305
Protein of unknown function (DUF455);
188-448 2.61e-135

Protein of unknown function (DUF455);


:

Pssm-ID: 461256  Cd Length: 247  Bit Score: 389.19  E-value: 2.61e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940529019 188 STSNPEHKIELTAHLFALFTEEgsTMALGDGKVTLPAIPPRQD-LEEVQPGRMPRPGRGGTLKSRVSMLHALANIELWAI 266
Cdd:pfam04305   1 LTADPEEKVALTRAAAAAWRAG--RLSEIPDAPPPPDRPGRPErPELVPPRDVPKRRKLGTLEGRAALLHALAHIELNAI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940529019 267 DLAIDICVRFvafqtnvpsdgisRTLPRAYFHDWLKVANDEAKHFSLLRARLEELGSYFGALPVHHGLWMSATDTAEDLR 346
Cdd:pfam04305  79 DLAWDAIARF-------------AGLPREFYDDWLKVADDEARHFSLLRERLEELGSEYGDLPAHNGLWEAAEKTAHDLL 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940529019 347 SRISIVSLVHEARGLDVNPMTIDKFRKAGDAESVQTLEIIHNDEITHVTTGHRWLTWICNEEDTDPVQVFRANVQKHFRG 426
Cdd:pfam04305 146 ARLALVPRVLEARGLDVTPGTIAKLRAAGDEESAAILEIILRDEIGHVAAGNRWFRYLCEQRGLDPVATFRELVRRYFRG 225

                         250       260
                  ....*....|....*....|..
gi 1940529019 427 PLREPFNAEARMQAGMDPRYYE 448
Cdd:pfam04305 226 ALKGPFNEEARLKAGFTEEEYE 247
NirD COG2146
Ferredoxin subunit of nitrite reductase or a ring-hydroxylating dioxygenase [Inorganic ion ...
 1-120 7.70e-13

Ferredoxin subunit of nitrite reductase or a ring-hydroxylating dioxygenase [Inorganic ion transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


:

Pssm-ID: 441749 [Multi-domain]  Cd Length: 103  Bit Score: 64.48  E-value: 7.70e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940529019   1 MAKVALGPLSDFKQARYVLHLSNGKRLVLFRlpsieprqgkkspakneTDDGwsYFAMEAECPHAGGPMqdSQVDIEDSa 80
Cdd:COG2146     1 MSEVKVCALDDLPEGGGVVVEVGGKQIAVFR-----------------TDGE--VYAYDNRCPHQGAPL--SEGIVDGG- 58

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1940529019  81 yIVSCPWHAYDFNVETGESSVGIKAC---TFPIDVRSESVTLE 120
Cdd:COG2146    59 -VVTCPLHGARFDLRTGECLGGPATEplkTYPVRVEDGDVYVD 100
 
Name Accession Description Interval E-value
DUF455 pfam04305
Protein of unknown function (DUF455);
188-448 2.61e-135

Protein of unknown function (DUF455);


Pssm-ID: 461256  Cd Length: 247  Bit Score: 389.19  E-value: 2.61e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940529019 188 STSNPEHKIELTAHLFALFTEEgsTMALGDGKVTLPAIPPRQD-LEEVQPGRMPRPGRGGTLKSRVSMLHALANIELWAI 266
Cdd:pfam04305   1 LTADPEEKVALTRAAAAAWRAG--RLSEIPDAPPPPDRPGRPErPELVPPRDVPKRRKLGTLEGRAALLHALAHIELNAI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940529019 267 DLAIDICVRFvafqtnvpsdgisRTLPRAYFHDWLKVANDEAKHFSLLRARLEELGSYFGALPVHHGLWMSATDTAEDLR 346
Cdd:pfam04305  79 DLAWDAIARF-------------AGLPREFYDDWLKVADDEARHFSLLRERLEELGSEYGDLPAHNGLWEAAEKTAHDLL 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940529019 347 SRISIVSLVHEARGLDVNPMTIDKFRKAGDAESVQTLEIIHNDEITHVTTGHRWLTWICNEEDTDPVQVFRANVQKHFRG 426
Cdd:pfam04305 146 ARLALVPRVLEARGLDVTPGTIAKLRAAGDEESAAILEIILRDEIGHVAAGNRWFRYLCEQRGLDPVATFRELVRRYFRG 225

                         250       260
                  ....*....|....*....|..
gi 1940529019 427 PLREPFNAEARMQAGMDPRYYE 448
Cdd:pfam04305 226 ALKGPFNEEARLKAGFTEEEYE 247
COG2833 COG2833
Uncharacterized protein, contains ferritin-like DUF455 domain [Function unknown];
178-452 4.37e-98

Uncharacterized protein, contains ferritin-like DUF455 domain [Function unknown];


Pssm-ID: 442081  Cd Length: 265  Bit Score: 295.16  E-value: 4.37e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940529019 178 TLCDWCGHILSTSNPEHKIELTAHLFALFTEEGSTMALGDGKVTLPAIPPRQD-LEEVQPGRMPRPgRGGTLKSRVSMLH 256
Cdd:COG2833     2 TLREAALAVLLTADPAEKLALTRALAAAWRAGRLALDPDPGPAAPPDRPGRPArPELVPPRDVPRR-SLGTPEGRAALLH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940529019 257 ALANIELWAIDLAIDICVRFvafqtnvpsdgisRTLPRAYFHDWLKVANDEAKHFSLLRARLEELGSYFGALPVHHGLWM 336
Cdd:COG2833    81 AIAHIEFNAINLALDAVLRF-------------PGMPRAFYDDWLRVAAEEARHFRLLRERLAELGYDYGDFPAHDGLWE 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940529019 337 SATDTAEDLRSRISIVSLVHEARGLDVNPMTIDKFRKAGDAESVQTLEIIHNDEITHVTTGHRWLTWICNEEDTDPVQVF 416
Cdd:COG2833   148 MAEKTAHDLLARMALVPRVLEARGLDVTPGMIEKLRAAGDEEAAAILDIILRDEIGHVAIGNRWFRYLCEQRGLDPEETY 227

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1940529019 417 RANVQKHFRGPLREPFNAEARMQAGMDPRYYENLDR 452
Cdd:COG2833   228 RELLRRYFPGRLKGPFNREARRAAGFSEDELDPLAA 263
Ferritin_like cd00657
Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, ...
 254-401 1.66e-13

Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, diiron-carboxylate proteins participate in a range of functions including iron regulation, mono-oxygenation, and reactive radical production. These proteins are characterized by the fact that they catalyze dioxygen-dependent oxidation-hydroxylation reactions within diiron centers; one exception is manganese catalase, which catalyzes peroxide-dependent oxidation-reduction within a dimanganese center. Diiron-carboxylate proteins are further characterized by the presence of duplicate metal ligands, glutamates and histidines (ExxH) and two additional glutamates within a four-helix bundle. Outside of these conserved residues there is little obvious homology. Members include bacterioferritin, ferritin, rubrerythrin, aromatic and alkene monooxygenase hydroxylases (AAMH), ribonucleotide reductase R2 (RNRR2), acyl-ACP-desaturases (Acyl_ACP_Desat), manganese (Mn) catalases, demethoxyubiquinone hydroxylases (DMQH), DNA protecting proteins (DPS), and ubiquinol oxidases (AOX), and the aerobic cyclase system, Fe-containing subunit (ACSF).


Pssm-ID: 153097  Cd Length: 130  Bit Score: 67.14  E-value: 1.66e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940529019 254 MLHALANIELWAIDLAIDIcvrfvafqtnvpsdgISRTLPRAYFHDWLKVANDEAKHFSLLRARLEELGSYFGALPVHHG 333
Cdd:cd00657     2 LLNDALAGEYAAIIAYGQL---------------AARAPDPDLKDELLEIADEERRHADALAERLRELGGTPPLPPAHLL 66

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1940529019 334 LWMSATDTAEDLRSRIsIVSLVHEARGLDVNPMTIDKFRkagDAESVQTLEIIHNDEITHVTTGHRWL 401
Cdd:cd00657    67 AAYALPKTSDDPAEAL-RAALEVEARAIAAYRELIEQAD---DPELRRLLERILADEQRHAAWFRKLL 130
NirD COG2146
Ferredoxin subunit of nitrite reductase or a ring-hydroxylating dioxygenase [Inorganic ion ...
 1-120 7.70e-13

Ferredoxin subunit of nitrite reductase or a ring-hydroxylating dioxygenase [Inorganic ion transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441749 [Multi-domain]  Cd Length: 103  Bit Score: 64.48  E-value: 7.70e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940529019   1 MAKVALGPLSDFKQARYVLHLSNGKRLVLFRlpsieprqgkkspakneTDDGwsYFAMEAECPHAGGPMqdSQVDIEDSa 80
Cdd:COG2146     1 MSEVKVCALDDLPEGGGVVVEVGGKQIAVFR-----------------TDGE--VYAYDNRCPHQGAPL--SEGIVDGG- 58

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1940529019  81 yIVSCPWHAYDFNVETGESSVGIKAC---TFPIDVRSESVTLE 120
Cdd:COG2146    59 -VVTCPLHGARFDLRTGECLGGPATEplkTYPVRVEDGDVYVD 100
Rieske cd03467
Rieske domain; a [2Fe-2S] cluster binding domain commonly found in Rieske non-heme iron ...
 4-98 4.29e-11

Rieske domain; a [2Fe-2S] cluster binding domain commonly found in Rieske non-heme iron oxygenase (RO) systems such as naphthalene and biphenyl dioxygenases, as well as in plant/cyanobacterial chloroplast b6f and mitochondrial cytochrome bc(1) complexes. The Rieske domain can be divided into two subdomains, with an incomplete six-stranded, antiparallel beta-barrel at one end, and an iron-sulfur cluster binding subdomain at the other. The Rieske iron-sulfur center contains a [2Fe-2S] cluster, which is involved in electron transfer, and is liganded to two histidine and two cysteine residues present in conserved sequences called Rieske motifs. In RO systems, the N-terminal Rieske domain of the alpha subunit acts as an electron shuttle that accepts electrons from a reductase or ferredoxin component and transfers them to the mononuclear iron in the alpha subunit C-terminal domain to be used for catalysis.


Pssm-ID: 239550 [Multi-domain]  Cd Length: 98  Bit Score: 59.42  E-value: 4.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940529019   4 VALGPLSDFKQARYVLHLSNGKRLVLFRlpsieprqgkkspaknetDDGWSYFAMEAECPHAGGPMqdSQVDIEDSayIV 83
Cdd:cd03467     2 VVVGALSELPPGGGRVVVVGGGPVVVVR------------------REGGEVYALSNRCTHQGCPL--SEGEGEDG--CI 59

                          90
                  ....*....|....*
gi 1940529019  84 SCPWHAYDFNVETGE 98
Cdd:cd03467    60 VCPCHGSRFDLRTGE 74
Rieske pfam00355
Rieske [2Fe-2S] domain; The rieske domain has a [2Fe-2S] centre. Two conserved cysteines ...
 2-98 6.24e-05

Rieske [2Fe-2S] domain; The rieske domain has a [2Fe-2S] centre. Two conserved cysteines coordinate one Fe ion, while the other Fe ion is coordinated by two conserved histidines. In hyperthermophilic archaea there is a SKTPCX(2-3)C motif at the C-terminus. The cysteines in this motif form a disulphide bridge, which stabilizes the protein.


Pssm-ID: 425632 [Multi-domain]  Cd Length: 89  Bit Score: 41.56  E-value: 6.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940529019   2 AKVALGPLSDFKQARYVLHLSNGKRLVLFRLPsieprqgkkspaknetdDGwSYFAMEAECPHAGGPMQDSQVdieDSAY 81
Cdd:pfam00355   1 SWYPVCHSSELPEGEPKVVEVGGEPLVVFRDE-----------------DG-ELYALEDRCPHRGAPLSEGKV---NGGG 59

                          90
                  ....*....|....*..
gi 1940529019  82 IVSCPWHAYDFNvETGE 98
Cdd:pfam00355  60 RLECPYHGWRFD-GTGK 75
 
Name Accession Description Interval E-value
DUF455 pfam04305
Protein of unknown function (DUF455);
188-448 2.61e-135

Protein of unknown function (DUF455);


Pssm-ID: 461256  Cd Length: 247  Bit Score: 389.19  E-value: 2.61e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940529019 188 STSNPEHKIELTAHLFALFTEEgsTMALGDGKVTLPAIPPRQD-LEEVQPGRMPRPGRGGTLKSRVSMLHALANIELWAI 266
Cdd:pfam04305   1 LTADPEEKVALTRAAAAAWRAG--RLSEIPDAPPPPDRPGRPErPELVPPRDVPKRRKLGTLEGRAALLHALAHIELNAI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940529019 267 DLAIDICVRFvafqtnvpsdgisRTLPRAYFHDWLKVANDEAKHFSLLRARLEELGSYFGALPVHHGLWMSATDTAEDLR 346
Cdd:pfam04305  79 DLAWDAIARF-------------AGLPREFYDDWLKVADDEARHFSLLRERLEELGSEYGDLPAHNGLWEAAEKTAHDLL 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940529019 347 SRISIVSLVHEARGLDVNPMTIDKFRKAGDAESVQTLEIIHNDEITHVTTGHRWLTWICNEEDTDPVQVFRANVQKHFRG 426
Cdd:pfam04305 146 ARLALVPRVLEARGLDVTPGTIAKLRAAGDEESAAILEIILRDEIGHVAAGNRWFRYLCEQRGLDPVATFRELVRRYFRG 225

                         250       260
                  ....*....|....*....|..
gi 1940529019 427 PLREPFNAEARMQAGMDPRYYE 448
Cdd:pfam04305 226 ALKGPFNEEARLKAGFTEEEYE 247
COG2833 COG2833
Uncharacterized protein, contains ferritin-like DUF455 domain [Function unknown];
178-452 4.37e-98

Uncharacterized protein, contains ferritin-like DUF455 domain [Function unknown];


Pssm-ID: 442081  Cd Length: 265  Bit Score: 295.16  E-value: 4.37e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940529019 178 TLCDWCGHILSTSNPEHKIELTAHLFALFTEEGSTMALGDGKVTLPAIPPRQD-LEEVQPGRMPRPgRGGTLKSRVSMLH 256
Cdd:COG2833     2 TLREAALAVLLTADPAEKLALTRALAAAWRAGRLALDPDPGPAAPPDRPGRPArPELVPPRDVPRR-SLGTPEGRAALLH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940529019 257 ALANIELWAIDLAIDICVRFvafqtnvpsdgisRTLPRAYFHDWLKVANDEAKHFSLLRARLEELGSYFGALPVHHGLWM 336
Cdd:COG2833    81 AIAHIEFNAINLALDAVLRF-------------PGMPRAFYDDWLRVAAEEARHFRLLRERLAELGYDYGDFPAHDGLWE 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940529019 337 SATDTAEDLRSRISIVSLVHEARGLDVNPMTIDKFRKAGDAESVQTLEIIHNDEITHVTTGHRWLTWICNEEDTDPVQVF 416
Cdd:COG2833   148 MAEKTAHDLLARMALVPRVLEARGLDVTPGMIEKLRAAGDEEAAAILDIILRDEIGHVAIGNRWFRYLCEQRGLDPEETY 227

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1940529019 417 RANVQKHFRGPLREPFNAEARMQAGMDPRYYENLDR 452
Cdd:COG2833   228 RELLRRYFPGRLKGPFNREARRAAGFSEDELDPLAA 263
Ferritin_like cd00657
Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, ...
 254-401 1.66e-13

Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, diiron-carboxylate proteins participate in a range of functions including iron regulation, mono-oxygenation, and reactive radical production. These proteins are characterized by the fact that they catalyze dioxygen-dependent oxidation-hydroxylation reactions within diiron centers; one exception is manganese catalase, which catalyzes peroxide-dependent oxidation-reduction within a dimanganese center. Diiron-carboxylate proteins are further characterized by the presence of duplicate metal ligands, glutamates and histidines (ExxH) and two additional glutamates within a four-helix bundle. Outside of these conserved residues there is little obvious homology. Members include bacterioferritin, ferritin, rubrerythrin, aromatic and alkene monooxygenase hydroxylases (AAMH), ribonucleotide reductase R2 (RNRR2), acyl-ACP-desaturases (Acyl_ACP_Desat), manganese (Mn) catalases, demethoxyubiquinone hydroxylases (DMQH), DNA protecting proteins (DPS), and ubiquinol oxidases (AOX), and the aerobic cyclase system, Fe-containing subunit (ACSF).


Pssm-ID: 153097  Cd Length: 130  Bit Score: 67.14  E-value: 1.66e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940529019 254 MLHALANIELWAIDLAIDIcvrfvafqtnvpsdgISRTLPRAYFHDWLKVANDEAKHFSLLRARLEELGSYFGALPVHHG 333
Cdd:cd00657     2 LLNDALAGEYAAIIAYGQL---------------AARAPDPDLKDELLEIADEERRHADALAERLRELGGTPPLPPAHLL 66

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1940529019 334 LWMSATDTAEDLRSRIsIVSLVHEARGLDVNPMTIDKFRkagDAESVQTLEIIHNDEITHVTTGHRWL 401
Cdd:cd00657    67 AAYALPKTSDDPAEAL-RAALEVEARAIAAYRELIEQAD---DPELRRLLERILADEQRHAAWFRKLL 130
NirD COG2146
Ferredoxin subunit of nitrite reductase or a ring-hydroxylating dioxygenase [Inorganic ion ...
 1-120 7.70e-13

Ferredoxin subunit of nitrite reductase or a ring-hydroxylating dioxygenase [Inorganic ion transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441749 [Multi-domain]  Cd Length: 103  Bit Score: 64.48  E-value: 7.70e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940529019   1 MAKVALGPLSDFKQARYVLHLSNGKRLVLFRlpsieprqgkkspakneTDDGwsYFAMEAECPHAGGPMqdSQVDIEDSa 80
Cdd:COG2146     1 MSEVKVCALDDLPEGGGVVVEVGGKQIAVFR-----------------TDGE--VYAYDNRCPHQGAPL--SEGIVDGG- 58

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1940529019  81 yIVSCPWHAYDFNVETGESSVGIKAC---TFPIDVRSESVTLE 120
Cdd:COG2146    59 -VVTCPLHGARFDLRTGECLGGPATEplkTYPVRVEDGDVYVD 100
Rieske cd03467
Rieske domain; a [2Fe-2S] cluster binding domain commonly found in Rieske non-heme iron ...
 4-98 4.29e-11

Rieske domain; a [2Fe-2S] cluster binding domain commonly found in Rieske non-heme iron oxygenase (RO) systems such as naphthalene and biphenyl dioxygenases, as well as in plant/cyanobacterial chloroplast b6f and mitochondrial cytochrome bc(1) complexes. The Rieske domain can be divided into two subdomains, with an incomplete six-stranded, antiparallel beta-barrel at one end, and an iron-sulfur cluster binding subdomain at the other. The Rieske iron-sulfur center contains a [2Fe-2S] cluster, which is involved in electron transfer, and is liganded to two histidine and two cysteine residues present in conserved sequences called Rieske motifs. In RO systems, the N-terminal Rieske domain of the alpha subunit acts as an electron shuttle that accepts electrons from a reductase or ferredoxin component and transfers them to the mononuclear iron in the alpha subunit C-terminal domain to be used for catalysis.


Pssm-ID: 239550 [Multi-domain]  Cd Length: 98  Bit Score: 59.42  E-value: 4.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940529019   4 VALGPLSDFKQARYVLHLSNGKRLVLFRlpsieprqgkkspaknetDDGWSYFAMEAECPHAGGPMqdSQVDIEDSayIV 83
Cdd:cd03467     2 VVVGALSELPPGGGRVVVVGGGPVVVVR------------------REGGEVYALSNRCTHQGCPL--SEGEGEDG--CI 59

                          90
                  ....*....|....*
gi 1940529019  84 SCPWHAYDFNVETGE 98
Cdd:cd03467    60 VCPCHGSRFDLRTGE 74
Rieske_NirD_small_Bacillus cd03530
Small subunit of nitrite reductase (NirD) family, Rieske domain; composed of proteins similar ...
 31-119 6.55e-09

Small subunit of nitrite reductase (NirD) family, Rieske domain; composed of proteins similar to the Bacillus subtilis small subunit of assimilatory nitrite reductase containing a Rieske domain. The Rieske domain is a [2Fe-2S] cluster binding domain involved in electron transfer. Assimilatory nitrate and nitrite reductases convert nitrate through nitrite to ammonium.


Pssm-ID: 239606 [Multi-domain]  Cd Length: 98  Bit Score: 52.99  E-value: 6.55e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940529019  31 RLPSIEPRQGKKSPAKNE------TDDGwSYFAMEAECPHAGGPMqdSQVDIEDSAyiVSCPWHAYDFNVETGESSVGIK 104
Cdd:cd03530     6 ALEDIPPRGARKVQTGGGeiavfrTADD-EVFALENRCPHKGGPL--SEGIVHGEY--VTCPLHNWVIDLETGEAQGPDE 80

                          90
                  ....*....|....*..
gi 1940529019 105 AC--TFPIDVRSESVTL 119
Cdd:cd03530    81 GCvrTFPVKVEDGRVYL 97
Rieske_AIFL_N cd03478
AIFL (apoptosis-inducing factor like) family, N-terminal Rieske domain; members of this family ...
 55-98 1.93e-06

AIFL (apoptosis-inducing factor like) family, N-terminal Rieske domain; members of this family show similarity to human AIFL, containing an N-terminal Rieske domain and a C-terminal pyridine nucleotide-disulfide oxidoreductase domain (Pyr_redox). The Rieske domain is a [2Fe-2S] cluster binding domain involved in electron transfer. AIFL shares 35% homology with human AIF (apoptosis-inducing factor), mainly in the Pyr_redox domain. AIFL is predominantly localized to the mitochondria. AIFL induces apoptosis in a caspase-dependent manner.


Pssm-ID: 239560 [Multi-domain]  Cd Length: 95  Bit Score: 46.08  E-value: 1.93e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1940529019  55 YFAMEAECPHAGGPMQDSQVdiedSAYIVSCPWHAYDFNVETGE 98
Cdd:cd03478    33 VHAIGAKCPHYGAPLAKGVL----TDGRIRCPWHGACFNLRTGD 72
Rieske pfam00355
Rieske [2Fe-2S] domain; The rieske domain has a [2Fe-2S] centre. Two conserved cysteines ...
 2-98 6.24e-05

Rieske [2Fe-2S] domain; The rieske domain has a [2Fe-2S] centre. Two conserved cysteines coordinate one Fe ion, while the other Fe ion is coordinated by two conserved histidines. In hyperthermophilic archaea there is a SKTPCX(2-3)C motif at the C-terminus. The cysteines in this motif form a disulphide bridge, which stabilizes the protein.


Pssm-ID: 425632 [Multi-domain]  Cd Length: 89  Bit Score: 41.56  E-value: 6.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940529019   2 AKVALGPLSDFKQARYVLHLSNGKRLVLFRLPsieprqgkkspaknetdDGwSYFAMEAECPHAGGPMQDSQVdieDSAY 81
Cdd:pfam00355   1 SWYPVCHSSELPEGEPKVVEVGGEPLVVFRDE-----------------DG-ELYALEDRCPHRGAPLSEGKV---NGGG 59

                          90
                  ....*....|....*..
gi 1940529019  82 IVSCPWHAYDFNvETGE 98
Cdd:pfam00355  60 RLECPYHGWRFD-GTGK 75
Rieske_RO_ferredoxin cd03528
Rieske non-heme iron oxygenase (RO) family, Rieske ferredoxin component; composed of the ...
 55-120 3.13e-04

Rieske non-heme iron oxygenase (RO) family, Rieske ferredoxin component; composed of the Rieske ferredoxin component of some three-component RO systems including biphenyl dioxygenase (BPDO) and carbazole 1,9a-dioxygenase (CARDO). The RO family comprise a large class of aromatic ring-hydroxylating dioxygenases found predominantly in microorganisms. These enzymes enable microorganisms to tolerate and even exclusively utilize aromatic compounds for growth. ROs consist of two or three components: reductase, oxygenase, and ferredoxin (in some cases) components. The ferredoxin component contains either a plant-type or Rieske-type [2Fe-2S] cluster. The Rieske ferredoxin component in this family carries an electron from the RO reductase component to the terminal RO oxygenase component. BPDO degrades biphenyls and polychlorinated biphenyls. BPDO ferredoxin (BphF) has structural features consistent with a minimal and perhaps archetypical Rieske protein in that the insertions that give other Rieske proteins unique structural features are missing. CARDO catalyzes dihydroxylation at the C1 and C9a positions of carbazole. Rieske ferredoxins are found as subunits of membrane oxidase complexes, cis-dihydrodiol-forming aromatic dioxygenases, bacterial assimilatory nitrite reductases, and arsenite oxidase. Rieske ferredoxins are also found as soluble electron carriers in bacterial dioxygenase and monooxygenase complexes.


Pssm-ID: 239604 [Multi-domain]  Cd Length: 98  Bit Score: 39.78  E-value: 3.13e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1940529019  55 YFAMEAECPHAGGPMQDSQVDiedsAYIVSCPWHAYDFNVETGessvgiKACTFP--IDVRSESVTLE 120
Cdd:cd03528    34 FYATDDLCTHGDASLSEGYVE----GGVIECPLHGGRFDLRTG------KALSLPatEPLKTYPVKVE 91
 
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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