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Conserved domains on  [gi|447007217|ref|WP_001084473|]
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MULTISPECIES: Rieske 2Fe-2S domain-containing protein [Acinetobacter calcoaceticus/baumannii complex]

Protein Classification

Rieske_RO_Alpha_N and RHO_alpha_C_AntDO-like domain-containing protein( domain architecture ID 11468625)

Rieske_RO_Alpha_N and RHO_alpha_C_AntDO-like domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RHO_alpha_C_AntDO-like cd08879
C-terminal catalytic domain of the oxygenase alpha subunit of Pseudomonas resinovorans strain ...
 191-424 5.48e-87

C-terminal catalytic domain of the oxygenase alpha subunit of Pseudomonas resinovorans strain CA10 anthranilate 1,2-dioxygenase and related aromatic ring hydroxylating dioxygenases; C-terminal catalytic domain of the oxygenase alpha subunit of anthranilate 1,2-dioxygenase (AntDO) and related Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs, also known as aromatic ring hydroxylating dioxygenases). RHOs utilize non-heme Fe(II) to catalyze the addition of hydroxyl groups to the aromatic ring, an initial step in the oxidative degradation of aromatic compounds. RHOs are composed of either two or three protein components, and are comprised of an electron transport chain (ETC) and an oxygenase. The ETC transfers reducing equivalents from the electron donor to the oxygenase component, which in turn transfers electrons to the oxygen molecules. The oxygenase components are oligomers, either (alpha)n or (alpha)n(beta)n. The alpha subunits are the catalytic components and have an N-terminal domain, which binds a Rieske-like 2Fe-2S cluster, and the C-terminal catalytic domain which binds the non-heme Fe(II). The Fe(II) is co-ordinated by conserved His and Asp residues. Oxygenases belonging to this subgroup include the alpha subunits of AntDO, aniline dioxygenase, Acinetobacter calcoaceticus benzoate 1,2-dioxygenase, 2-halobenzoate 1,2-dioxygenase from Pseudomonas cepacia 2CBS, 2,4,5-trichlorophenoxyacetic acid oxygenase from Pseudomonas cepacia AC1100, 2,4-dichlorophenoxyacetic acid oxygenase from Bradyrhizobium sp. strain HW13, p-cumate 2,3-dioxygenase, 2-halobenzoate 1,2-dioxygenase form Pseudomonas cepacia 2CBS, and Pseudomonas putida IacC, which may be involved in the catabolism of the plant hormone indole 3-acetic acid. This subfamily belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket.


:

Pssm-ID: 176888 [Multi-domain]  Cd Length: 237  Bit Score: 264.59  E-value: 5.48e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447007217 191 GEHRFRFPGNWKIQLENTTDAYHFPLVHKSFL-----SSVDEKTEEL--FNFENQPGFVEDLGNGHSVMVMIPELVDLEE 263
Cdd:cd08879    2 GTHRYRYRGNWKLQLENGTDGYHPPFVHASYVattgaAAADATRGGLssFMTGPQGGGVRDLGNGHSVLDSRPEIPRLDA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447007217 264 DlmerPIQERFEDLAQALRDEGHEElEVRRIVRavgGSGFNLNLFPNIACSMAF--FRVLQPISVAETEIHHSVITMDGG 341
Cdd:cd08879   82 D----RPKPPIAEYRAALVAAHGEE-RARRILR---GRGRNLNIFPNLFIIDISqqIRVIRPIAVDETEVTSWALRPKGA 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447007217 342 PQIANQYRLRLHEHFQGPFGFGTPDDSEAWERVQHGANAGNDLWIMLNRGLPGEVKTEDGLKSD-VSAETGMRAAYQQWK 420
Cdd:cd08879  154 PDEVNRRRLRYSEDFFGPSGFATPDDLEAFERCQRGLAARGEEWVDLSRGLGREKADEDGVVTGaVTDELPMRNQWRAWK 233


                 ....
gi 447007217 421 KMMT 424
Cdd:cd08879  234 RLMT 237
HcaE COG4638
Phenylpropionate dioxygenase or related ring-hydroxylating dioxygenase, large terminal subunit ...
 21-422 8.52e-83

Phenylpropionate dioxygenase or related ring-hydroxylating dioxygenase, large terminal subunit [Inorganic ion transport and metabolism, General function prediction only];


:

Pssm-ID: 443676 [Multi-domain]  Cd Length: 298  Bit Score: 256.07  E-value: 8.52e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447007217  21 DRAHTSLYKDERIFDEEMEKIFYSTWVWVAHASEIPEGGSYKTINIGKQPVVVVRDRKKKVHVLLNRCRHRAATVCEHkK 100
Cdd:COG4638    2 SRLPAAFYTDPEIFELELERIFRRGWYYVGHSSELPEPGDYLTRTILGEPVVLVRDKDGEVRAFHNVCPHRGAPLSEG-R 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447007217 101 GKTNSFVCPYHGWSYALDGSLRGVPSPESYGDcLDKSELPLVSLRVEEYNGMIFASFKEDIQPLEEFLGPAKKWIDLFMK 180
Cdd:COG4638   81 GNGGRLVCPYHGWTYDLDGRLVGIPHMEGFPD-FDPARAGLRSVPVEEWGGLIFVWLGPDAPPLAEYLGPLAEYLDPYDF 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447007217 181 QGAgypiKVLGEHRFRFPGNWKIQLENTTDAYHFPLVHKsflssvdekteelfnfenqpgfvedlgnghsvmvmipelvd 260
Cdd:COG4638  160 GEL----KVAGRETYEVNANWKLVVENFLDGYHVPFVHP----------------------------------------- 194

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447007217 261 leedlmerpiqerfedlaqalrdegheelevrrivravggsGFNLNLFPNIAC----SMAFFRVLQPISVAETEIHHSVI 336
Cdd:COG4638  195 -----------------------------------------GIILFLFPNLMIldypDHLVVRTVTPVSPDRTRVFVTFY 233

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447007217 337 TMDGGPQIANQYRLRLhehfqgPFGFGTPDDSEAWERVQHGanagndlwiMLNRGLPGEVktedglKSDVSAETGMRAAY 416
Cdd:COG4638  234 VPKDALDPEARADLEA------FWGRVFEEDREIVERQQRG---------LRSLAYPGPY------LSRSPAEGGVRHFR 292


                 ....*.
gi 447007217 417 QQWKKM 422
Cdd:COG4638  293 RWLRRL 298
 
Name Accession Description Interval E-value
RHO_alpha_C_AntDO-like cd08879
C-terminal catalytic domain of the oxygenase alpha subunit of Pseudomonas resinovorans strain ...
 191-424 5.48e-87

C-terminal catalytic domain of the oxygenase alpha subunit of Pseudomonas resinovorans strain CA10 anthranilate 1,2-dioxygenase and related aromatic ring hydroxylating dioxygenases; C-terminal catalytic domain of the oxygenase alpha subunit of anthranilate 1,2-dioxygenase (AntDO) and related Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs, also known as aromatic ring hydroxylating dioxygenases). RHOs utilize non-heme Fe(II) to catalyze the addition of hydroxyl groups to the aromatic ring, an initial step in the oxidative degradation of aromatic compounds. RHOs are composed of either two or three protein components, and are comprised of an electron transport chain (ETC) and an oxygenase. The ETC transfers reducing equivalents from the electron donor to the oxygenase component, which in turn transfers electrons to the oxygen molecules. The oxygenase components are oligomers, either (alpha)n or (alpha)n(beta)n. The alpha subunits are the catalytic components and have an N-terminal domain, which binds a Rieske-like 2Fe-2S cluster, and the C-terminal catalytic domain which binds the non-heme Fe(II). The Fe(II) is co-ordinated by conserved His and Asp residues. Oxygenases belonging to this subgroup include the alpha subunits of AntDO, aniline dioxygenase, Acinetobacter calcoaceticus benzoate 1,2-dioxygenase, 2-halobenzoate 1,2-dioxygenase from Pseudomonas cepacia 2CBS, 2,4,5-trichlorophenoxyacetic acid oxygenase from Pseudomonas cepacia AC1100, 2,4-dichlorophenoxyacetic acid oxygenase from Bradyrhizobium sp. strain HW13, p-cumate 2,3-dioxygenase, 2-halobenzoate 1,2-dioxygenase form Pseudomonas cepacia 2CBS, and Pseudomonas putida IacC, which may be involved in the catabolism of the plant hormone indole 3-acetic acid. This subfamily belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket.


Pssm-ID: 176888 [Multi-domain]  Cd Length: 237  Bit Score: 264.59  E-value: 5.48e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447007217 191 GEHRFRFPGNWKIQLENTTDAYHFPLVHKSFL-----SSVDEKTEEL--FNFENQPGFVEDLGNGHSVMVMIPELVDLEE 263
Cdd:cd08879    2 GTHRYRYRGNWKLQLENGTDGYHPPFVHASYVattgaAAADATRGGLssFMTGPQGGGVRDLGNGHSVLDSRPEIPRLDA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447007217 264 DlmerPIQERFEDLAQALRDEGHEElEVRRIVRavgGSGFNLNLFPNIACSMAF--FRVLQPISVAETEIHHSVITMDGG 341
Cdd:cd08879   82 D----RPKPPIAEYRAALVAAHGEE-RARRILR---GRGRNLNIFPNLFIIDISqqIRVIRPIAVDETEVTSWALRPKGA 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447007217 342 PQIANQYRLRLHEHFQGPFGFGTPDDSEAWERVQHGANAGNDLWIMLNRGLPGEVKTEDGLKSD-VSAETGMRAAYQQWK 420
Cdd:cd08879  154 PDEVNRRRLRYSEDFFGPSGFATPDDLEAFERCQRGLAARGEEWVDLSRGLGREKADEDGVVTGaVTDELPMRNQWRAWK 233


                 ....
gi 447007217 421 KMMT 424
Cdd:cd08879  234 RLMT 237
HcaE COG4638
Phenylpropionate dioxygenase or related ring-hydroxylating dioxygenase, large terminal subunit ...
 21-422 8.52e-83

Phenylpropionate dioxygenase or related ring-hydroxylating dioxygenase, large terminal subunit [Inorganic ion transport and metabolism, General function prediction only];


Pssm-ID: 443676 [Multi-domain]  Cd Length: 298  Bit Score: 256.07  E-value: 8.52e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447007217  21 DRAHTSLYKDERIFDEEMEKIFYSTWVWVAHASEIPEGGSYKTINIGKQPVVVVRDRKKKVHVLLNRCRHRAATVCEHkK 100
Cdd:COG4638    2 SRLPAAFYTDPEIFELELERIFRRGWYYVGHSSELPEPGDYLTRTILGEPVVLVRDKDGEVRAFHNVCPHRGAPLSEG-R 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447007217 101 GKTNSFVCPYHGWSYALDGSLRGVPSPESYGDcLDKSELPLVSLRVEEYNGMIFASFKEDIQPLEEFLGPAKKWIDLFMK 180
Cdd:COG4638   81 GNGGRLVCPYHGWTYDLDGRLVGIPHMEGFPD-FDPARAGLRSVPVEEWGGLIFVWLGPDAPPLAEYLGPLAEYLDPYDF 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447007217 181 QGAgypiKVLGEHRFRFPGNWKIQLENTTDAYHFPLVHKsflssvdekteelfnfenqpgfvedlgnghsvmvmipelvd 260
Cdd:COG4638  160 GEL----KVAGRETYEVNANWKLVVENFLDGYHVPFVHP----------------------------------------- 194

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447007217 261 leedlmerpiqerfedlaqalrdegheelevrrivravggsGFNLNLFPNIAC----SMAFFRVLQPISVAETEIHHSVI 336
Cdd:COG4638  195 -----------------------------------------GIILFLFPNLMIldypDHLVVRTVTPVSPDRTRVFVTFY 233

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447007217 337 TMDGGPQIANQYRLRLhehfqgPFGFGTPDDSEAWERVQHGanagndlwiMLNRGLPGEVktedglKSDVSAETGMRAAY 416
Cdd:COG4638  234 VPKDALDPEARADLEA------FWGRVFEEDREIVERQQRG---------LRSLAYPGPY------LSRSPAEGGVRHFR 292


                 ....*.
gi 447007217 417 QQWKKM 422
Cdd:COG4638  293 RWLRRL 298
Rieske_RO_Alpha_N cd03469
Rieske non-heme iron oxygenase (RO) family, N-terminal Rieske domain of the oxygenase alpha ...
 46-164 1.14e-51

Rieske non-heme iron oxygenase (RO) family, N-terminal Rieske domain of the oxygenase alpha subunit; 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 oxygenase component may contain alpha and beta subunits, with the beta subunit having a purely structural function. Some oxygenase components contain only an alpha subunit. The oxygenase alpha subunit has two domains, an N-terminal Rieske domain with an [2Fe-2S] cluster and a C-terminal catalytic domain with a mononuclear Fe(II) binding site. The Rieske [2Fe-2S] cluster accepts electrons from the reductase or ferredoxin component and transfers them to the mononuclear iron for catalysis. Reduced pyridine nucleotide is used as the initial source of two electrons for dioxygen activation.


Pssm-ID: 239551 [Multi-domain]  Cd Length: 118  Bit Score: 169.31  E-value: 1.14e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447007217  46 WVWVAHASEIPEGGSYKTINIGKQPVVVVRDRKKKVHVLLNRCRHRAATVCEHKKGKTNSFVCPYHGWSYALDGSLRGVP 125
Cdd:cd03469    1 WYFVGHSSELPEPGDYVTLELGGEPLVLVRDRDGEVRAFHNVCPHRGARLCEGRGGNAGRLVCPYHGWTYDLDGKLVGVP 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 447007217 126 SPESYGDcLDKSELPLVSLRVEEYNGMIFASFKEDIQPL 164
Cdd:cd03469   81 REEGFPG-FDKEKLGLRTVPVEEWGGLIFVNLDPDAPPL 118
Rieske pfam00355
Rieske [2Fe-2S] domain; The rieske domain has a [2Fe-2S] centre. Two conserved cysteines ...
 45-127 2.51e-24

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: 95.88  E-value: 2.51e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447007217   45 TWVWVAHASEIPEGGSyKTINIGKQPVVVVRDRKKKVHVLLNRCRHRAATVCEHKKGKTNSFVCPYHGWSYALDGSLRGV 124
Cdd:pfam00355   1 SWYPVCHSSELPEGEP-KVVEVGGEPLVVFRDEDGELYALEDRCPHRGAPLSEGKVNGGGRLECPYHGWRFDGTGKVVKV 79


                  ...
gi 447007217  125 PSP 127
Cdd:pfam00355  80 PAP 82
Ring_hydroxyl_A pfam00848
Ring hydroxylating alpha subunit (catalytic domain); This family is the catalytic domain of ...
 188-381 2.98e-10

Ring hydroxylating alpha subunit (catalytic domain); This family is the catalytic domain of aromatic-ring- hydroxylating dioxygenase systems. The active site contains a non-heme ferrous ion coordinated by three ligands.


Pssm-ID: 425905  Cd Length: 210  Bit Score: 59.78  E-value: 2.98e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447007217  188 KVLGEHRFRFPGNWKIQLENTTDAYHFPLVHKSFLSSVDEKTEELFNfenqPGFVEDLGnGHSVMVMIPELVDLEEDLME 267
Cdd:pfam00848   5 RRVARITLDVAANWKLAAENFLECYHVPVLHPELLRASPPEDLPPSE----AAHFDGFG-PHGRLGQGGDLRLTPAAASM 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447007217  268 RPIQERFEDLAQALRDEGHeelevrrivravgGSGFNLNLFPNIACS----MAFFRVLQPISVAETEIHHSVITMdgGPQ 343
Cdd:pfam00848  80 TLDAEAGRPELPGLPEEQD-------------RGALFYTLFPNLSILlapdHVVVYQLIPTGPDTTRVEVYWYVP--PDA 144

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 447007217  344 IAN-QYRLRLHEHFQGPFGFGTpDDSEAWERVQHGANAG 381
Cdd:pfam00848 145 LAEpEFAEELEAVWDRTFGVNQ-EDAELCERVQRGLRSR 182
PLN02281 PLN02281
chlorophyllide a oxygenase
 68-220 1.96e-07

chlorophyllide a oxygenase


Pssm-ID: 177920 [Multi-domain]  Cd Length: 536  Bit Score: 53.19  E-value: 1.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447007217  68 KQPVVVVRDRKKKVHVLLNRCRHRAatvCEHKKGKTNS--FVCPYHGWSYALDGSLRGVPSPESYgdcldksELPLVSLR 145
Cdd:PLN02281 242 EQPWVIFRGEDGKPGCVRNTCAHRA---CPLDLGTVNEgrIQCPYHGWEYSTDGECKKMPSTKLL-------KVKIKSLP 311

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447007217 146 VEEYNGMIF--------ASFKEDIQPLEEFLGPAKKWIDLFMKQGagypikvlgehrfrfpgnwkIQLENTTDAYHFPLV 217
Cdd:PLN02281 312 CLEQEGMIWiwpgdeppAPILPSLQPPSGFLIHAELVMDLPVEHG--------------------LLLDNLLDLAHAPFT 371


                 ...
gi 447007217 218 HKS 220
Cdd:PLN02281 372 HTS 374
nirD_assim_sml TIGR02378
nitrite reductase [NAD(P)H], small subunit; This model describes NirD, the small subunit of ...
 45-153 4.38e-07

nitrite reductase [NAD(P)H], small subunit; This model describes NirD, the small subunit of nitrite reductase [NAD(P)H] (the assimilatory nitrite reductase), which associates with NirB, the large subunit (TIGR02374). In a few bacteria such as Klebsiella pneumoniae and in Fungi, the two regions are fused. [Central intermediary metabolism, Nitrogen metabolism]


Pssm-ID: 131431 [Multi-domain]  Cd Length: 105  Bit Score: 48.08  E-value: 4.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447007217   45 TWVWVAHASEIPEGGSyKTINIGKQPVVVVRDRKKKVHVLLNRCRHRAATVCEH-----KKGKTNSFvCPYHGWSYALDG 119
Cdd:TIGR02378   1 TWQDICAIDDIPEETG-VCVLLGDTQIAIFRVPGDQVFAIQNMCPHKRAFVLSRgivgdAQGELWVA-CPLHKRNFRLED 78

                          90       100       110
                  ....*....|....*....|....*....|....
gi 447007217  120 slrgvpspesyGDCLDKSELPLVSLRVEEYNGMI 153
Cdd:TIGR02378  79 -----------GRCLEDDSGSVRTYEVRVEDGRV 101
 
Name Accession Description Interval E-value
RHO_alpha_C_AntDO-like cd08879
C-terminal catalytic domain of the oxygenase alpha subunit of Pseudomonas resinovorans strain ...
 191-424 5.48e-87

C-terminal catalytic domain of the oxygenase alpha subunit of Pseudomonas resinovorans strain CA10 anthranilate 1,2-dioxygenase and related aromatic ring hydroxylating dioxygenases; C-terminal catalytic domain of the oxygenase alpha subunit of anthranilate 1,2-dioxygenase (AntDO) and related Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs, also known as aromatic ring hydroxylating dioxygenases). RHOs utilize non-heme Fe(II) to catalyze the addition of hydroxyl groups to the aromatic ring, an initial step in the oxidative degradation of aromatic compounds. RHOs are composed of either two or three protein components, and are comprised of an electron transport chain (ETC) and an oxygenase. The ETC transfers reducing equivalents from the electron donor to the oxygenase component, which in turn transfers electrons to the oxygen molecules. The oxygenase components are oligomers, either (alpha)n or (alpha)n(beta)n. The alpha subunits are the catalytic components and have an N-terminal domain, which binds a Rieske-like 2Fe-2S cluster, and the C-terminal catalytic domain which binds the non-heme Fe(II). The Fe(II) is co-ordinated by conserved His and Asp residues. Oxygenases belonging to this subgroup include the alpha subunits of AntDO, aniline dioxygenase, Acinetobacter calcoaceticus benzoate 1,2-dioxygenase, 2-halobenzoate 1,2-dioxygenase from Pseudomonas cepacia 2CBS, 2,4,5-trichlorophenoxyacetic acid oxygenase from Pseudomonas cepacia AC1100, 2,4-dichlorophenoxyacetic acid oxygenase from Bradyrhizobium sp. strain HW13, p-cumate 2,3-dioxygenase, 2-halobenzoate 1,2-dioxygenase form Pseudomonas cepacia 2CBS, and Pseudomonas putida IacC, which may be involved in the catabolism of the plant hormone indole 3-acetic acid. This subfamily belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket.


Pssm-ID: 176888 [Multi-domain]  Cd Length: 237  Bit Score: 264.59  E-value: 5.48e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447007217 191 GEHRFRFPGNWKIQLENTTDAYHFPLVHKSFL-----SSVDEKTEEL--FNFENQPGFVEDLGNGHSVMVMIPELVDLEE 263
Cdd:cd08879    2 GTHRYRYRGNWKLQLENGTDGYHPPFVHASYVattgaAAADATRGGLssFMTGPQGGGVRDLGNGHSVLDSRPEIPRLDA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447007217 264 DlmerPIQERFEDLAQALRDEGHEElEVRRIVRavgGSGFNLNLFPNIACSMAF--FRVLQPISVAETEIHHSVITMDGG 341
Cdd:cd08879   82 D----RPKPPIAEYRAALVAAHGEE-RARRILR---GRGRNLNIFPNLFIIDISqqIRVIRPIAVDETEVTSWALRPKGA 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447007217 342 PQIANQYRLRLHEHFQGPFGFGTPDDSEAWERVQHGANAGNDLWIMLNRGLPGEVKTEDGLKSD-VSAETGMRAAYQQWK 420
Cdd:cd08879  154 PDEVNRRRLRYSEDFFGPSGFATPDDLEAFERCQRGLAARGEEWVDLSRGLGREKADEDGVVTGaVTDELPMRNQWRAWK 233


                 ....
gi 447007217 421 KMMT 424
Cdd:cd08879  234 RLMT 237
HcaE COG4638
Phenylpropionate dioxygenase or related ring-hydroxylating dioxygenase, large terminal subunit ...
 21-422 8.52e-83

Phenylpropionate dioxygenase or related ring-hydroxylating dioxygenase, large terminal subunit [Inorganic ion transport and metabolism, General function prediction only];


Pssm-ID: 443676 [Multi-domain]  Cd Length: 298  Bit Score: 256.07  E-value: 8.52e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447007217  21 DRAHTSLYKDERIFDEEMEKIFYSTWVWVAHASEIPEGGSYKTINIGKQPVVVVRDRKKKVHVLLNRCRHRAATVCEHkK 100
Cdd:COG4638    2 SRLPAAFYTDPEIFELELERIFRRGWYYVGHSSELPEPGDYLTRTILGEPVVLVRDKDGEVRAFHNVCPHRGAPLSEG-R 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447007217 101 GKTNSFVCPYHGWSYALDGSLRGVPSPESYGDcLDKSELPLVSLRVEEYNGMIFASFKEDIQPLEEFLGPAKKWIDLFMK 180
Cdd:COG4638   81 GNGGRLVCPYHGWTYDLDGRLVGIPHMEGFPD-FDPARAGLRSVPVEEWGGLIFVWLGPDAPPLAEYLGPLAEYLDPYDF 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447007217 181 QGAgypiKVLGEHRFRFPGNWKIQLENTTDAYHFPLVHKsflssvdekteelfnfenqpgfvedlgnghsvmvmipelvd 260
Cdd:COG4638  160 GEL----KVAGRETYEVNANWKLVVENFLDGYHVPFVHP----------------------------------------- 194

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447007217 261 leedlmerpiqerfedlaqalrdegheelevrrivravggsGFNLNLFPNIAC----SMAFFRVLQPISVAETEIHHSVI 336
Cdd:COG4638  195 -----------------------------------------GIILFLFPNLMIldypDHLVVRTVTPVSPDRTRVFVTFY 233

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447007217 337 TMDGGPQIANQYRLRLhehfqgPFGFGTPDDSEAWERVQHGanagndlwiMLNRGLPGEVktedglKSDVSAETGMRAAY 416
Cdd:COG4638  234 VPKDALDPEARADLEA------FWGRVFEEDREIVERQQRG---------LRSLAYPGPY------LSRSPAEGGVRHFR 292


                 ....*.
gi 447007217 417 QQWKKM 422
Cdd:COG4638  293 RWLRRL 298
Rieske_RO_Alpha_N cd03469
Rieske non-heme iron oxygenase (RO) family, N-terminal Rieske domain of the oxygenase alpha ...
 46-164 1.14e-51

Rieske non-heme iron oxygenase (RO) family, N-terminal Rieske domain of the oxygenase alpha subunit; 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 oxygenase component may contain alpha and beta subunits, with the beta subunit having a purely structural function. Some oxygenase components contain only an alpha subunit. The oxygenase alpha subunit has two domains, an N-terminal Rieske domain with an [2Fe-2S] cluster and a C-terminal catalytic domain with a mononuclear Fe(II) binding site. The Rieske [2Fe-2S] cluster accepts electrons from the reductase or ferredoxin component and transfers them to the mononuclear iron for catalysis. Reduced pyridine nucleotide is used as the initial source of two electrons for dioxygen activation.


Pssm-ID: 239551 [Multi-domain]  Cd Length: 118  Bit Score: 169.31  E-value: 1.14e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447007217  46 WVWVAHASEIPEGGSYKTINIGKQPVVVVRDRKKKVHVLLNRCRHRAATVCEHKKGKTNSFVCPYHGWSYALDGSLRGVP 125
Cdd:cd03469    1 WYFVGHSSELPEPGDYVTLELGGEPLVLVRDRDGEVRAFHNVCPHRGARLCEGRGGNAGRLVCPYHGWTYDLDGKLVGVP 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 447007217 126 SPESYGDcLDKSELPLVSLRVEEYNGMIFASFKEDIQPL 164
Cdd:cd03469   81 REEGFPG-FDKEKLGLRTVPVEEWGGLIFVNLDPDAPPL 118
Rieske_RO_Alpha_OHBDO_like cd03545
Rieske non-heme iron oxygenase (RO) family, Ortho-halobenzoate-1,2-dioxygenase (OHBDO)-like ...
 28-164 5.63e-40

Rieske non-heme iron oxygenase (RO) family, Ortho-halobenzoate-1,2-dioxygenase (OHBDO)-like subfamily, N-terminal Rieske domain of the oxygenase alpha subunit; composed of the oxygenase alpha subunits of OHBDO, salicylate 5-hydroxylase (S5H), terephthalate 1,2-dioxygenase system (TERDOS) and similar proteins. ROs comprise a large class of aromatic ring-hydroxylating dioxygenases that enable microorganisms to tolerate and utilize aromatic compounds for growth. The oxygenase alpha subunit contains an N-terminal Rieske domain with an [2Fe-2S] cluster and a C-terminal catalytic domain with a mononuclear Fe(II) binding site. The Rieske [2Fe-2S] cluster accepts electrons from a reductase or ferredoxin component and transfers them to the mononuclear iron for catalysis. OHBDO converts 2-chlorobenzoate (2-CBA) to catechol as well as 2,4-dCBA and 2,5-dCBA to 4-chlorocatechol, as part of the chlorobenzoate degradation pathway. Although ortho-substituted chlorobenzoates appear to be particularly recalcitrant to biodegradation, several strains utilize 2-CBA and the dCBA derivatives as a sole carbon and energy source. S5H converts salicylate (2-hydroxybenzoate), a metabolic intermediate of phenanthrene, to gentisate (2,5-dihydroxybenzoate) as part of an alternate pathway for naphthalene catabolism. S5H is a multicomponent enzyme made up of NagGH (the oxygenase components), NagAa (the ferredoxin reductase component), and NagAb (the ferredoxin component). The oxygenase component is made up of alpha (NagG) and beta (NagH) subunits. TERDOS is present in gram-positive bacteria and proteobacteria where it converts terephthalate (1,4-dicarboxybenzene) to protocatechuate as part of the terephthalate degradation pathway. The oxygenase component of TERDOS, called TerZ, is a hetero-hexamer with 3 alpha (TerZalpha) and 3 beta (TerZbeta) subunits.


Pssm-ID: 239616 [Multi-domain]  Cd Length: 150  Bit Score: 139.89  E-value: 5.63e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447007217  28 YKDERIFDEEMEKIFY-STWVWVAHASEIPEGGSYKTINIGKQPVVVVRDRKKKVHVLLNRCRHRAATVCEHKKGKTNSF 106
Cdd:cd03545    7 FTDRAYFDREQERIFRgKTWSYVGLEAEIPNAGDFKSTFVGDTPVVVTRAEDGSLHAWVNRCAHRGALVCRERRGNDGSL 86

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447007217 107 VCPYHGWSYALDGSLRGVP------SPESYGDCLDKSELPLVSLRVEEYNGMIFASFKEDIQPL 164
Cdd:cd03545   87 TCVYHQWAYDLKGNLKGVPfrrglkGQGGMPKDFDMKQHGLEKLRVETVGGLVFASFSDEVEPL 150
Rieske_RO_Alpha_AntDO cd03538
Rieske non-heme iron oxygenase (RO) family, Anthranilate 1,2-dioxygenase (AntDO) subfamily, ...
 24-160 1.40e-36

Rieske non-heme iron oxygenase (RO) family, Anthranilate 1,2-dioxygenase (AntDO) subfamily, N-terminal Rieske domain of the oxygenase alpha subunit; ROs comprise a large class of aromatic ring-hydroxylating dioxygenases that enable microorganisms to tolerate and utilize aromatic compounds for growth. The oxygenase alpha subunit contains an N-terminal Rieske domain with an [2Fe-2S] cluster and a C-terminal catalytic domain with a mononuclear Fe(II) binding site. The Rieske [2Fe-2S] cluster accepts electrons from a reductase or ferredoxin component and transfers them to the mononuclear iron for catalysis. AntDO converts anthranilate to catechol, a naturally occurring compound formed through tryptophan degradation and an important intermediate in the metabolism of many N-heterocyclic compounds such as indole, o-nitrobenzoate, carbazole, and quinaldine.


Pssm-ID: 239612 [Multi-domain]  Cd Length: 146  Bit Score: 131.05  E-value: 1.40e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447007217  24 HTSLYKDERIFDEEMEKIFYSTWVWVAHASEIPEGGSYKTINIGKQPVVVVRDRKKKVHVLLNRCRHRAATVCEHKKGKT 103
Cdd:cd03538    1 HKDVYTDPEIFALEMERLFGNAWIYVGHESQVPNPGDYITTRIGDQPVVMVRHTDGSVHVLYNRCPHKGTKIVSDGCGNT 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447007217 104 NSFV-CPYHGWSYALDGSLRGVPSPESY-GDCLDKSE----LPLVSlRVEEYNGMIFASFKED 160
Cdd:cd03538   81 GKFFrCPYHAWSFKTDGSLLAIPLKKGYeGTGFDPSHadkgMQRVG-AVDIYRGFVFARLSPS 142
Rieske_RO_Alpha_NDO cd03535
Rieske non-heme iron oxygenase (RO) family, Nathphalene 1,2-dioxygenase (NDO) subfamily, ...
 45-164 1.07e-33

Rieske non-heme iron oxygenase (RO) family, Nathphalene 1,2-dioxygenase (NDO) subfamily, N-terminal Rieske domain of the oxygenase alpha subunit; ROs comprise a large class of aromatic ring-hydroxylating dioxygenases that enable microorganisms to tolerate and utilize aromatic compounds for growth. The oxygenase alpha subunit contains an N-terminal Rieske domain with an [2Fe-2S] cluster and a C-terminal catalytic domain with a mononuclear Fe(II) binding site. The Rieske [2Fe-2S] cluster accepts electrons from a reductase or ferredoxin component and transfers them to the mononuclear iron for catalysis. NDO is a three-component RO system consisting of a reductase, a ferredoxin, and a hetero-hexameric alpha-beta subunit oxygenase component. NDO catalyzes the oxidation of naphthalene to cis-(1R,2S)-dihydroxy-1,2-dihydronaphthalene (naphthalene cis-dihydrodiol) with the consumption of O2 and NAD(P)H. NDO has a relaxed substrate specificity and can oxidize almost 100 substrates. Included in its varied activities are the enantiospecific cis-dihydroxylation of polycyclic aromatic hydrocarbons and benzocycloalkenes, benzylic hydroxylation, N- and O-dealkylation, sulfoxidation and desaturation reactions.


Pssm-ID: 239609 [Multi-domain]  Cd Length: 123  Bit Score: 122.54  E-value: 1.07e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447007217  45 TWVWVAHASEIPEGGSYKTINIGKQPVVVVRDRKKKVHVLLNRCRHRAATVCEHKKGKTNSFVCPYHGWSYALDGSLRGV 124
Cdd:cd03535    2 AWVFLGHESEIPNAGDYVVRYIGDDSFIVCRDEDGEIRAMFNSCRHRGMQVCRAEMGNTSHFRCPYHGWTYRNTGRLVGV 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 447007217 125 PS-PESYGDCLDKSELPLVSL-RVEEYNGMIFASFKEDIQPL 164
Cdd:cd03535   82 PAqQEAYGGGFDKSQWGLRPApNLDSYNGLIFGSLDPKAPSL 123
Rieske_RO_Alpha_BPDO_like cd03472
Rieske non-heme iron oxygenase (RO) family, Biphenyl dioxygenase (BPDO)-like subfamily, ...
 38-160 1.41e-33

Rieske non-heme iron oxygenase (RO) family, Biphenyl dioxygenase (BPDO)-like subfamily, N-terminal Rieske domain of the oxygenase alpha subunit; composed of the oxygenase alpha subunits of BPDO and similar proteins including cumene dioxygenase (CumDO), nitrobenzene dioxygenase (NBDO), alkylbenzene dioxygenase (AkbDO) and dibenzofuran 4,4a-dioxygenase (DFDO). ROs comprise a large class of aromatic ring-hydroxylating dioxygenases that enable microorganisms to tolerate and utilize aromatic compounds for growth. The oxygenase alpha subunit contains an N-terminal Rieske domain with an [2Fe-2S] cluster and a C-terminal catalytic domain with a mononuclear Fe(II) binding site. The Rieske [2Fe-2S] cluster accepts electrons from a reductase or ferredoxin component and transfers them to the mononuclear iron for catalysis. BPDO degrades biphenyls and polychlorinated biphenyls (PCB's) while CumDO degrades cumene (isopropylbenzene), an aromatic hydrocarbon that is intermediate in size between ethylbenzene and biphenyl. NBDO catalyzes the initial reaction in nitrobenzene degradation, oxidizing the aromatic rings of mono- and dinitrotoluenes to form catechol and nitrite. NBDO belongs to the naphthalene subfamily of ROs. AkbDO is involved in alkylbenzene catabolism, converting o-xylene to 2,3- and 3,4-dimethylphenol and ethylbenzene to cis-dihydrodiol. DFDO is involved in dibenzofuran degradation.


Pssm-ID: 239554 [Multi-domain]  Cd Length: 128  Bit Score: 122.26  E-value: 1.41e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447007217  38 MEKIFYSTWVWVAHASEIPEGGSYKTINIGKQPVVVVRDRKKKVHVLLNRCRHRAATVCEHKKGKTNSFVCPYHGWSYAL 117
Cdd:cd03472    1 LERVFARSWLLLGHETHIPKAGDYLTTYMGEDPVIVVRQKDGSIRVFLNQCRHRGMRICRSDAGNAKAFTCTYHGWAYDT 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 447007217 118 DGSLRGVP-SPESYGDCLDKSELPLVSLRVEEYNGMIFASFKED 160
Cdd:cd03472   81 AGNLVNVPfEKEAFCDGLDKADWGPLQARVETYKGLIFANWDAE 124
Rieske_RO_Alpha_HBDO cd03542
Rieske non-heme iron oxygenase (RO) family, 2-Halobenzoate 1,2-dioxygenase (HBDO) subfamily, ...
 46-164 4.65e-33

Rieske non-heme iron oxygenase (RO) family, 2-Halobenzoate 1,2-dioxygenase (HBDO) subfamily, N-terminal Rieske domain of the oxygenase alpha subunit; ROs comprise a large class of aromatic ring-hydroxylating dioxygenases that enable microorganisms to tolerate and utilize aromatic compounds for growth. The oxygenase alpha subunit contains an N-terminal Rieske domain with an [2Fe-2S] cluster and a C-terminal catalytic domain with a mononuclear Fe(II) binding site. The Rieske [2Fe-2S] cluster accepts electrons from a reductase or ferredoxin component and transfers them to the mononuclear iron for catalysis. HBDO catalyzes the double hydroxylation of 2-halobenzoates with concomitant release of halogenide and carbon dioxide, yielding catechol.


Pssm-ID: 239615 [Multi-domain]  Cd Length: 123  Bit Score: 120.63  E-value: 4.65e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447007217  46 WVWVAHASEIPEGGSYKTINIGKQPVVVVRDRKKKVHVLLNRCRHRAATVCEHKKGKTNSFVCPYHGWSYALDGSLRGVP 125
Cdd:cd03542    1 WVYLAHESQIPNNNDYFTTTIGRQPVVITRDKDGELNAFINACSHRGAMLCRRKQGNKGTFTCPFHGWTFSNTGKLLKVK 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 447007217 126 SPES--YGDCLDKS---ELPLVSlRVEEYNGMIFASFKEDIQPL 164
Cdd:cd03542   81 DPKTagYPEGFNCDgshDLTKVA-RFESYRGFLFGSLNADVAPL 123
Rieske pfam00355
Rieske [2Fe-2S] domain; The rieske domain has a [2Fe-2S] centre. Two conserved cysteines ...
 45-127 2.51e-24

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: 95.88  E-value: 2.51e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447007217   45 TWVWVAHASEIPEGGSyKTINIGKQPVVVVRDRKKKVHVLLNRCRHRAATVCEHKKGKTNSFVCPYHGWSYALDGSLRGV 124
Cdd:pfam00355   1 SWYPVCHSSELPEGEP-KVVEVGGEPLVVFRDEDGELYALEDRCPHRGAPLSEGKVNGGGRLECPYHGWRFDGTGKVVKV 79


                  ...
gi 447007217  125 PSP 127
Cdd:pfam00355  80 PAP 82
Rieske_RO_Alpha_S5H cd03539
This alignment model represents the N-terminal rieske iron-sulfur domain of the oxygenase ...
 46-164 3.95e-24

This alignment model represents the N-terminal rieske iron-sulfur domain of the oxygenase alpha subunit (NagG) of salicylate 5-hydroxylase (S5H). S5H converts salicylate (2-hydroxybenzoate), a metabolic intermediate of phenanthrene, to gentisate (2,5-dihydroxybenzoate) as part of an alternate pathway for naphthalene catabolism. S5H is a multicomponent enzyme made up of NagGH (the oxygenase components), NagAa (the ferredoxin reductase component), and NagAb (the ferredoxin component). The oxygenase component is made up of alpha (NagG) and beta (NagH) subunits.


Pssm-ID: 239613 [Multi-domain]  Cd Length: 129  Bit Score: 96.92  E-value: 3.95e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447007217  46 WVWVAHASEIPEGGSYKTINIGKQPVVVVRDRKKKVHVLLNRCRHRAATVCEHKKGKTNSFVCPYHGWSYALDGSLRGVP 125
Cdd:cd03539    1 WCYVGLEAEIPNPGDFKRTLIGERSVIMTRDPDGGINVVENVCAHRGMRFCRERNGNAKDFVCPYHQWNYSLKGDLQGVP 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 447007217 126 --------------SPESYgdclDKSELPLVSLRVEEYNGMIFASFKEDIQPL 164
Cdd:cd03539   81 frrgvkkdgkvnggMPKDF----KTKDHGLTKLKVATRGGVVFASFDHDVESF 129
Rieske_RO_Alpha_DTDO cd03536
This alignment model represents the N-terminal rieske domain of the oxygenase alpha subunit ...
 46-166 2.94e-23

This alignment model represents the N-terminal rieske domain of the oxygenase alpha subunit (DitA) of diterpenoid dioxygenase (DTDO). DTDO is a novel aromatic-ring-hydroxylating dioxygenase found in Pseudomonas and other proteobacteria that degrades dehydroabietic acid (DhA). Specifically, DitA hydroxylates 7-oxodehydroabietic acid to 7-oxo-11,12-dihydroxy-8, 13-abietadien acid. The ditA1 and ditA2 genes encode the alpha and beta subunits of the oxygenase component of DTDO while the ditA3 gene encodes the ferredoxin component of DTDO. The organization of the genes encoding the various diterpenoid dioxygenase components, the phylogenetic distinctiveness of both the alpha subunit and the ferredoxin component, and the unusual iron-sulfur cluster of the ferredoxin all suggest that this enzyme belongs to a new class of aromatic ring-hydroxylating dioxygenases.


Pssm-ID: 239610 [Multi-domain]  Cd Length: 123  Bit Score: 94.23  E-value: 2.94e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447007217  46 WVWVAHASEIPEGGSYKTINIGKQPVVVVRDRKKKVHVLLNRCRHRAATVCEHKKGKTNSFVCPYHGWSYALDGSLRGVP 125
Cdd:cd03536    1 WVLLGHESEIPNKGDFMVRDMGSDSVIVARDKDGEIHVSLNVCPHRGMRISTTDGGNTQIHVCIYHGWAFRPNGDFIGAP 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 447007217 126 SPES--YGDCLDKSELPLVSLRVEEYNGMIFASFKEDIQPLEE 166
Cdd:cd03536   81 VEKEcmHGKMRTKAELGLHKARVTLYGGLIFATWNIDGPSFED 123
Rieske_RO_Alpha_CMO cd03541
Rieske non-heme iron oxygenase (RO) family, Choline monooxygenase (CMO) subfamily, N-terminal ...
 46-157 1.25e-19

Rieske non-heme iron oxygenase (RO) family, Choline monooxygenase (CMO) subfamily, N-terminal Rieske domain of the oxygenase alpha subunit; ROs comprise a large class of aromatic ring-hydroxylating dioxygenases that enable microorganisms to tolerate and utilize aromatic compounds for growth. The oxygenase alpha subunit contains an N-terminal Rieske domain with an [2Fe-2S] cluster and a C-terminal catalytic domain with a mononuclear Fe(II) binding site. The Rieske [2Fe-2S] cluster accepts electrons from a reductase or ferredoxin component and transfers them to the mononuclear iron for catalysis. CMO is a novel RO found in certain plants which catalyzes the first step in betaine synthesis. CMO is not found in animals or bacteria. In these organisms, the first step in betaine synthesis is catalyzed by either the membrane-bound choline dehydrogenase (CDH) or the soluble choline oxidase (COX).


Pssm-ID: 239614 [Multi-domain]  Cd Length: 118  Bit Score: 84.14  E-value: 1.25e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447007217  46 WVWVAHASEIPEGGSYKTINIGKQPVVVVRDRKKKVHVLLNRCRHRAaTVCEHKKGKTNSFVCPYHGWSYALDGSLRGVp 125
Cdd:cd03541    2 WQVAGYSDQVKEKNQYFTGRLGNVEYVVCRDGNGKLHAFHNVCTHRA-SILACGSGKKSCFVCPYHGWVYGLDGSLTKA- 79

                         90       100       110
                 ....*....|....*....|....*....|..
gi 447007217 126 SPESYGDCLDKSELPLVSLRVEEYNGMIFASF 157
Cdd:cd03541   80 TQATGIQNFNPKELGLVPLKVAEWGPFVLISV 111
Rieske cd03467
Rieske domain; a [2Fe-2S] cluster binding domain commonly found in Rieske non-heme iron ...
 46-154 8.92e-18

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: 78.30  E-value: 8.92e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447007217  46 WVWVAHASEIPEGGsYKTINIGKQPVVVVRDRKKKVHVLLNRCRHRAATVCEhKKGKTNSFVCPYHGWSYAL-DGSLRGV 124
Cdd:cd03467    1 WVVVGALSELPPGG-GRVVVVGGGPVVVVRREGGEVYALSNRCTHQGCPLSE-GEGEDGCIVCPCHGSRFDLrTGEVVSG 78

                         90       100       110
                 ....*....|....*....|....*....|.
gi 447007217 125 PSPesygdcldkseLPLVSLRV-EEYNGMIF 154
Cdd:cd03467   79 PAP-----------RPLPKYPVkVEGDGVVW 98
PobA COG5749
Chlorophyllide a oxygenase/letal leaf spot protein [Coenzyme transport and metabolism];
46-238 4.85e-17

Chlorophyllide a oxygenase/letal leaf spot protein [Coenzyme transport and metabolism];


Pssm-ID: 444459 [Multi-domain]  Cd Length: 349  Bit Score: 81.97  E-value: 4.85e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447007217  46 WVWVAHASEIPEGGSYKtINIGKQPVVVVRDRKKKVHVLLNRCRHRAATVCEhkkGK--TNSFVCPYHGWSYALDGSLRG 123
Cdd:COG5749   20 WYPVAPSEDLKPNKPKP-VTLLGEPLVIWRDSDGKVVALEDRCPHRGAPLSE---GRveGGNLRCPYHGWQFDGDGKCVH 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447007217 124 VPspesygdCLDKSELPLVSLRVEEY-----NGMIF-------ASFKEDIQPLEEFLGPAKKWIDLFmkqgagypikvlg 191
Cdd:COG5749   96 IP-------QLPENQPIPKNAKVKSYpvqerYGLIWvwlgdppQADETPIPDIPELDDPEWVATSSV------------- 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 447007217 192 ehrFRFPGNWKIQLENTTDAYHFPLVHKSFLSSVD---------EKTEELFNFENQ 238
Cdd:COG5749  156 ---RDLECHYSRLIENLIDPSHVPFVHHGTQGNRKqaqplemeiESTPNGITASYT 208
RHO_alpha_C_NDO-like cd08881
C-terminal catalytic domain of the oxygenase alpha subunit of naphthalene 1,2-dioxygenase (NDO) ...
 187-424 3.32e-15

C-terminal catalytic domain of the oxygenase alpha subunit of naphthalene 1,2-dioxygenase (NDO) and related aromatic ring hydroxylating dioxygenases; C-terminal catalytic domain of the oxygenase alpha subunit of naphthalene 1,2-dioxygenase (NDO) and related Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs, also known as aromatic ring hydroxylating dioxygenases). This domain binds non-heme Fe(II). RHOs utilize non-heme Fe(II) to catalyze the addition of hydroxyl groups to the aromatic ring, an initial step in the oxidative degradation of aromatic compounds. RHOs are composed of either two or three protein components, and are comprised of an electron transport chain (ETC) and an oxygenase. The ETC transfers reducing equivalents form the electron donor to the oxygenase component, which in turn transfers electrons to the oxygen molecules. The oxygenase components are oligomers, either (alpha)n or (alpha)n(beta)n. The alpha subunits are the catalytic components and have an N-terminal domain, which binds a Rieske-like 2Fe-2S cluster, and a C-terminal domain which binds the non-heme Fe(II). The Fe(II) is co-ordinated by conserved His and Asp residues. Proteins belonging to this subgroup include the terminal oxygenase alpha subunits of biphenyl dioxygenase, cumene dioxygenase from Pseudomonas fluorescens IP01, ethylbenzene dioxygenase, naphthalene 1,2-dioxygenase, nitrobenzene dioxygenase from Comamonas sp. strain JS765, toluene 2,3-dioxygenase from Pseudomonas putida F1, dioxin dioxygenase of Sphingomonas sp. Strain RW1, and the polycyclic aromatic hydrocarbons (PAHs)degrading ring-hydroxylating dioxygenase from Sphingomonas CHY-1. This subfamily belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket.


Pssm-ID: 176890 [Multi-domain]  Cd Length: 206  Bit Score: 73.82  E-value: 3.32e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447007217 187 IKVLGE-HRFRFPGNWKIQLEN-TTDAYHFPLVHKSFLSSvdekteeLFNFENQPGFVEDLGnghsvmvmipelvdleed 264
Cdd:cd08881    2 LEVVGGpQKWVIKANWKLAAENfAGDGYHTGTTHASALEA-------GLPPDAADLPPIDLG------------------ 56

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447007217 265 lmerpiqerfedLAQALRDEGHEelevrriVRAVGGSGFNLNLFPNiaCSMAF-----FRVLQPISVAETEIHHSVITMD 339
Cdd:cd08881   57 ------------LQFTAPWHGHG-------LGFFLDSPQHGTIFPN--LSFLPgyfntLRVWHPRGPDETEVWTWTLVDK 115

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447007217 340 GGPQ-IANQYRLRLHEHFqGPFGFGTPDDSEAWERVQH---GANAGNdlwIMLN--RGLPGEVKTEDGLKSDVSA----E 409
Cdd:cd08881  116 DAPEeVKDRVRRQYTRTF-GPAGTFEQDDGENWEEITRvarGYVARQ---VPLNyqMGLGVEPEPDPGGPGIVGPgfysE 191

                        250
                 ....*....|....*
gi 447007217 410 TGMRAAYQQWKKMMT 424
Cdd:cd08881  192 ANQRGFYRRWLELME 206
RHO_alpha_C cd00680
C-terminal catalytic domain of the oxygenase alpha subunit of Rieske-type non-heme iron ...
 193-423 2.40e-13

C-terminal catalytic domain of the oxygenase alpha subunit of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases; C-terminal catalytic domain of the oxygenase alpha subunit of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenase (RHO) family. RHOs, also known as aromatic ring hydroxylating dioxygenases, utilize non-heme Fe(II) to catalyze the addition of hydroxyl groups to the aromatic ring, an initial step in the oxidative degradation of aromatic compounds. RHOs are composed of either two or three protein components, and are comprised of an electron transport chain (ETC), and an oxygenase. The ETC transfers reducing equivalents from the electron donor to the oxygenase component, which in turn transfers electrons to the oxygen molecules. The oxygenase components are oligomers, either (alpha)n or (alpha)n(beta)n. The alpha subunits are the catalytic components and have an N-terminal domain, which binds a Rieske-like 2Fe-2S cluster, and a C-terminal domain which binds the non-heme Fe(II). The Fe(II) is co-ordinated by conserved His and Asp residues. Oxygenases belonging to this family include the alpha subunits of Pseudomonas resinovorans strain CA10 anthranilate 1,2-dioxygenase, Stenotrophomonas maltophilia dicamba O-demethylase, Ralstonia sp. U2 salicylate-5-hydroxylase, Cycloclasticus sp. strain A5 polycyclic aromatic hydrocarbon dioxygenase, toluene 2,3-dioxygenase from Pseudomonas putida F1, dioxin dioxygenase of Sphingomonas sp. Strain RW1, plant choline monooxygenase, and the polycyclic aromatic hydrocarbon (PAH)-degrading ring-hydroxylating dioxygenase from Sphingomonas CHY-1. This group also includes the C-terminal catalytic domains of MupW, part of the mupirocin biosynthetic gene cluster in Pseudomonas fluorescens, and Pseudomonas aeruginosa GbcA (glycine betaine catabolism A). This family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket.


Pssm-ID: 176852 [Multi-domain]  Cd Length: 188  Bit Score: 68.36  E-value: 2.40e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447007217 193 HRFRFPGNWKIQLENTTDAYHFPLVHKSFLSSVDEKTEELFNFENQPGFVEDLGNGHSVMVmipelvdleedlmerpiqe 272
Cdd:cd00680    3 YEYEVDCNWKLAVENFLECYHVPTVHPDTLATGLPLPLLFGDHYRVDDTGEGPGEGLSRHW------------------- 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447007217 273 rfedlaqalrdeGHEELEVRRIVRAVGGSGFNLNLFPN--IACSMAFFRVLQ--PISVAETEIHHSVITMDGGPqiANQY 348
Cdd:cd00680   64 ------------GDGKGPQSALPGLKPGGYLYLYLFPNlmIGLYPDSLQVQQfvPIGPNKTRLEVRLYRPKDED--AREE 129

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447007217 349 RLRLHEHFQGPFGFGTPDDSEAWERVQHGANAGNDLWIMLNRGlpgevktedglksdvsaETGMRAAYQQWKKMM 423
Cdd:cd00680  130 FDAELESLAGILRQVLDEDIELCERIQRGLRSGAFRGGPLSPL-----------------EEGIRHFHRWLRRAL 187
RHO_alpha_C_ahdA1c-like cd08880
C-terminal catalytic domain of the large/alpha subunit (ahdA1c) of a ring-hydroxylating ...
 190-423 8.26e-13

C-terminal catalytic domain of the large/alpha subunit (ahdA1c) of a ring-hydroxylating dioxygenase from Sphingomonas sp. strain P2 and related proteins; C-terminal catalytic domain of the large subunit (ahdA1c) of the AhdA3A4A2cA1c salicylate 1-hydroxylase complex from Sphingomonas sp. strain P2, and related Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs, also known as aromatic ring hydroxylating dioxygenases). AhdA3A4A2cA1c is one of three known isofunctional salicylate 1-hydroxylase complexes in strain P2, involved in phenanthrene degradation, which catalyze the monooxygenation of salicylate, the metabolite of phenanthene degradation, to produce catechol. This complex prefers salicylate over other substituted salicylates; the other two salicylate 1-hydroxylases have different substrate preferences. RHOs utilize non-heme Fe(II) to catalyze the addition of hydroxyl groups to the aromatic ring, an initial step in the oxidative degradation of aromatic compounds. RHOs are composed of either two or three protein components, and are comprised of an electron transport chain (ETC) and an oxygenase. The ETC transfers reducing equivalents from the electron donor to the oxygenase component, which in turn transfers electrons to the oxygen molecules. The oxygenase components are oligomers, either (alpha)n or (alpha)n(beta)n. The alpha subunits are the catalytic components and have an N-terminal domain, which binds a Rieske-like 2Fe-2S cluster, and a C-terminal domain which binds the non-heme Fe(II). The Fe(II) is co-ordinated by conserved His and Asp residues. Other oxygenases belonging to this subgroup include the alpha subunits of anthranilate 1,2-dioxygenase from Burkholderia cepacia DBO1, a polycyclic aromatic hydrocarbon dioxygenase from Cycloclasticus sp. strain A5 (PhnA dioxygenase), salicylate-5-hydroxylase from Ralstonia sp. U2, ortho-halobenzoate 1,2-dioxygenase from Pseudomonas aeruginosa strain JB2, and the terephthalate 1,2-dioxygenase system from Delftia tsuruhatensis strain T7. This subfamily belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket.


Pssm-ID: 176889  Cd Length: 222  Bit Score: 67.28  E-value: 8.26e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447007217 190 LGEHRFRFPGNWKIQLENTTDAYHFPLVHkSFLSsvdekTEELFNFENQPGFVEDLGNGHSVMV-MIPElvDLEEDLMER 268
Cdd:cd08880    1 LGYYRQRIPGNWKLYAENVKDPYHASLLH-LFFV-----TFGLWRADQKSSIIDDEHGRHSVMTsTKSG--DDEAAEKDS 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447007217 269 PIQERFEDLAQaLRDEgheelEVRRIVRAVGGSGFN--LNLFPN-----IACSMAfFRVLQPISVAETEIhhsVITM--- 338
Cdd:cd08880   73 EEIRSFRDDFT-LLDP-----SLLDGRAEFDDDITLviQSIFPSlvvqqIQNTLA-VRHIIPKGPDSFEL---VWTYfgy 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447007217 339 -DGGPQianQYRLRL-HEHFQGPFGFGTPDDSEAWERVQHGA-NAGNDLWIMLNRGlpGEVKTEDGLksdvSAETGMRAA 415
Cdd:cd08880  143 eDDDEE---MTRLRLrQANLVGPAGFVSMEDGEAIEFVQRGVeGDGGDRSVIEMGG--GDVESSDHM----VTEAAIRGF 213


                 ....*...
gi 447007217 416 YQQWKKMM 423
Cdd:cd08880  214 WKYYRKVM 221
NirD COG2146
Ferredoxin subunit of nitrite reductase or a ring-hydroxylating dioxygenase [Inorganic ion ...
 45-154 3.58e-11

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: 59.47  E-value: 3.58e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447007217  45 TWVWVAHASEIPEGGSyKTINIGKQPVVVVRDRKKkVHVLLNRCRHRAATVCEHK-KGKTnsFVCPYHGWSYAL-DGSLR 122
Cdd:COG2146    2 SEVKVCALDDLPEGGG-VVVEVGGKQIAVFRTDGE-VYAYDNRCPHQGAPLSEGIvDGGV--VTCPLHGARFDLrTGECL 77

                         90       100       110
                 ....*....|....*....|....*....|..
gi 447007217 123 GVPSPEsygdcldkselPLVSLRVEEYNGMIF 154
Cdd:COG2146   78 GGPATE-----------PLKTYPVRVEDGDVY 98
Ring_hydroxyl_A pfam00848
Ring hydroxylating alpha subunit (catalytic domain); This family is the catalytic domain of ...
 188-381 2.98e-10

Ring hydroxylating alpha subunit (catalytic domain); This family is the catalytic domain of aromatic-ring- hydroxylating dioxygenase systems. The active site contains a non-heme ferrous ion coordinated by three ligands.


Pssm-ID: 425905  Cd Length: 210  Bit Score: 59.78  E-value: 2.98e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447007217  188 KVLGEHRFRFPGNWKIQLENTTDAYHFPLVHKSFLSSVDEKTEELFNfenqPGFVEDLGnGHSVMVMIPELVDLEEDLME 267
Cdd:pfam00848   5 RRVARITLDVAANWKLAAENFLECYHVPVLHPELLRASPPEDLPPSE----AAHFDGFG-PHGRLGQGGDLRLTPAAASM 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447007217  268 RPIQERFEDLAQALRDEGHeelevrrivravgGSGFNLNLFPNIACS----MAFFRVLQPISVAETEIHHSVITMdgGPQ 343
Cdd:pfam00848  80 TLDAEAGRPELPGLPEEQD-------------RGALFYTLFPNLSILlapdHVVVYQLIPTGPDTTRVEVYWYVP--PDA 144

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 447007217  344 IAN-QYRLRLHEHFQGPFGFGTpDDSEAWERVQHGANAG 381
Cdd:pfam00848 145 LAEpEFAEELEAVWDRTFGVNQ-EDAELCERVQRGLRSR 182
Rieske_RO_Alpha_PhDO_like cd03479
Rieske non-heme iron oxygenase (RO) family, Phthalate 4,5-dioxygenase (PhDO)-like subfamily, ...
 38-155 1.08e-09

Rieske non-heme iron oxygenase (RO) family, Phthalate 4,5-dioxygenase (PhDO)-like subfamily, N-terminal Rieske domain of the oxygenase alpha subunit; composed of the oxygenase alpha subunits of PhDO and similar proteins including 3-chlorobenzoate 3,4-dioxygenase (CBDO), phenoxybenzoate dioxygenase (POB-dioxygenase) and 3-nitrobenzoate oxygenase (MnbA). ROs comprise a large class of aromatic ring-hydroxylating dioxygenases that enable microorganisms to tolerate and utilize aromatic compounds for growth. The oxygenase alpha subunit contains an N-terminal Rieske domain with an [2Fe-2S] cluster and a C-terminal catalytic domain with a mononuclear Fe(II) binding site. The Rieske [2Fe-2S] cluster accepts electrons from a reductase or ferredoxin component and transfers them to the mononuclear iron for catalysis. PhDO and CBDO are two-component RO systems, containing oxygenase and reductase components. PhDO catalyzes the dihydroxylation of phthalate to form the 4,5-dihydro-cis-dihydrodiol of phthalate (DHD). CBDO, together with CbaC dehydrogenase, converts the environmental pollutant 3CBA to protocatechuate (PCA) and 5-Cl-PCA, which are then metabolized by the chromosomal PCA meta (extradiol) ring fission pathway. POB-dioxygenase catalyzes the initial catabolic step in the angular dioxygenation of phenoxybenzoate, converting mono- and dichlorinated phenoxybenzoates to protocatechuate and chlorophenols. These phenoxybenzoates are metabolic products formed during the degradation of pyrethroid insecticides.


Pssm-ID: 239561 [Multi-domain]  Cd Length: 144  Bit Score: 56.49  E-value: 1.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447007217  38 MEKIFYSTWVWVAHASEIPEGGSYKTINIGKQPVVVVRDRKKKVHVLLNRCRHRAATV----CEHkkgktNSFVCPYHGW 113
Cdd:cd03479   14 MGELLRRYWQPVALSSELTEDGQPVRVRLLGEDLVAFRDTSGRVGLLDEHCPHRGASLvfgrVEE-----CGLRCCYHGW 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 447007217 114 SYALDGSLRGVPSpESYGDCLdKSELPLVSLRVEEYNGMIFA 155
Cdd:cd03479   89 KFDVDGQCLEMPS-EPPDSQL-KQKVRQPAYPVRERGGLVWA 128
Rieske_RO_Alpha_OMO_CARDO cd03548
Rieske non-heme iron oxygenase (RO) family, 2-Oxoquinoline 8-monooxygenase (OMO) and Carbazole ...
 42-166 1.28e-09

Rieske non-heme iron oxygenase (RO) family, 2-Oxoquinoline 8-monooxygenase (OMO) and Carbazole 1,9a-dioxygenase (CARDO) subfamily, N-terminal Rieske domain of the oxygenase alpha subunit; ROs comprise a large class of aromatic ring-hydroxylating dioxygenases that enable microorganisms to tolerate and utilize aromatic compounds for growth. The oxygenase alpha subunit contains an N-terminal Rieske domain with an [2Fe-2S] cluster and a C-terminal catalytic domain with a mononuclear Fe(II) binding site. The Rieske [2Fe-2S] cluster accepts electrons from a reductase or ferredoxin component and transfers them to the mononuclear iron for catalysis. OMO catalyzes the NADH-dependent oxidation of the N-heterocyclic aromatic compound 2-oxoquinoline to 8-hydroxy-2-oxoquinoline, the second step in the bacterial degradation of quinoline. OMO consists of a reductase component (OMR) and an oxygenase component (OMO) that together function to shuttle electrons from the reduced pyridine nucleotide to the active site of OMO, where O2 activation and 2-oxoquinoline hydroxylation occurs. CARDO, which contains oxygenase (CARDO-O), ferredoxin (CARDO-F) and ferredoxin reductase (CARDO-R) components, catalyzes the dihydroxylation at the C1 and C9a positions of carbazole. The oxygenase component of OMO and CARDO contain only alpha subunits arranged in a trimeric structure.


Pssm-ID: 239617 [Multi-domain]  Cd Length: 136  Bit Score: 56.28  E-value: 1.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447007217  42 FYSTWVWVAHASEIPEGgSYKTINIGKQPVVVVRDrKKKVHVLLNRCRHRAATVCEHKKGKTNSFV-CPYHGWSYAL-DG 119
Cdd:cd03548   11 FRNHWYPALFSHELEEG-EPKGIQLCGEPILLRRV-DGKVYALKDRCLHRGVPLSKKPECFTKGTItCWYHGWTYRLdDG 88

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 447007217 120 SLRG-VPSPESygdcldkselPLVSLR------VEEYNGMIFA----SFKEDIQPLEE 166
Cdd:cd03548   89 KLVTiLANPDD----------PLIGRTglktypVEEAKGMIFVfvgdGDYADPPPLAH 136
Rieske_RO_Alpha_Cao cd04337
Cao (chlorophyll a oxygenase) is a rieske non-heme iron-sulfur protein located within the ...
 46-154 8.68e-09

Cao (chlorophyll a oxygenase) is a rieske non-heme iron-sulfur protein located within the plastid-envelope inner and thylakoid membranes, that catalyzes the conversion of chlorophyllide a to chlorophyllide b. CAO is found not only in plants but also in chlorophytes and prochlorophytes. This domain represents the N-terminal rieske domain of the oxygenase alpha subunit. ROs comprise a large class of aromatic ring-hydroxylating dioxygenases that enable microorganisms to tolerate and utilize aromatic compounds for growth. The oxygenase alpha subunit contains an N-terminal Rieske domain with an [2Fe-2S] cluster and a C-terminal catalytic domain with a mononuclear Fe(II) binding site. The Rieske [2Fe-2S] cluster accepts electrons from a reductase or ferredoxin component and transfers them to the mononuclear iron for catalysis. Cao is closely related to several other plant RO's including Tic 55, a 55 kDa protein associated with protein transport through the inner chloroplast membrane; Ptc 52, a novel 52 kDa protein isolated from chloroplasts; and LLS1/Pao (Lethal-leaf spot 1/pheophorbide a oxygenase).


Pssm-ID: 239829 [Multi-domain]  Cd Length: 129  Bit Score: 53.65  E-value: 8.68e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447007217  46 WVWVAHASEIPEGgSYKTINIGKQPVVVVRDRKKKVHVLLNRCRHRAatvCEHKKGKTNS--FVCPYHGWSYALDGSLRG 123
Cdd:cd04337   18 WYPVEFSKDLKMD-TMVPFELFGQPWVLFRDEDGTPGCIRDECAHRA---CPLSLGKVIEgrIQCPYHGWEYDGDGECTK 93

                         90       100       110
                 ....*....|....*....|....*....|.
gi 447007217 124 VPSPESYGdcldkseLPLVSLRVEEYNGMIF 154
Cdd:cd04337   94 MPSTKCLN-------VGIAALPCMEQDGMIW 117
PLN02281 PLN02281
chlorophyllide a oxygenase
 68-220 1.96e-07

chlorophyllide a oxygenase


Pssm-ID: 177920 [Multi-domain]  Cd Length: 536  Bit Score: 53.19  E-value: 1.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447007217  68 KQPVVVVRDRKKKVHVLLNRCRHRAatvCEHKKGKTNS--FVCPYHGWSYALDGSLRGVPSPESYgdcldksELPLVSLR 145
Cdd:PLN02281 242 EQPWVIFRGEDGKPGCVRNTCAHRA---CPLDLGTVNEgrIQCPYHGWEYSTDGECKKMPSTKLL-------KVKIKSLP 311

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447007217 146 VEEYNGMIF--------ASFKEDIQPLEEFLGPAKKWIDLFMKQGagypikvlgehrfrfpgnwkIQLENTTDAYHFPLV 217
Cdd:PLN02281 312 CLEQEGMIWiwpgdeppAPILPSLQPPSGFLIHAELVMDLPVEHG--------------------LLLDNLLDLAHAPFT 371


                 ...
gi 447007217 218 HKS 220
Cdd:PLN02281 372 HTS 374
nirD_assim_sml TIGR02378
nitrite reductase [NAD(P)H], small subunit; This model describes NirD, the small subunit of ...
 45-153 4.38e-07

nitrite reductase [NAD(P)H], small subunit; This model describes NirD, the small subunit of nitrite reductase [NAD(P)H] (the assimilatory nitrite reductase), which associates with NirB, the large subunit (TIGR02374). In a few bacteria such as Klebsiella pneumoniae and in Fungi, the two regions are fused. [Central intermediary metabolism, Nitrogen metabolism]


Pssm-ID: 131431 [Multi-domain]  Cd Length: 105  Bit Score: 48.08  E-value: 4.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447007217   45 TWVWVAHASEIPEGGSyKTINIGKQPVVVVRDRKKKVHVLLNRCRHRAATVCEH-----KKGKTNSFvCPYHGWSYALDG 119
Cdd:TIGR02378   1 TWQDICAIDDIPEETG-VCVLLGDTQIAIFRVPGDQVFAIQNMCPHKRAFVLSRgivgdAQGELWVA-CPLHKRNFRLED 78

                          90       100       110
                  ....*....|....*....|....*....|....
gi 447007217  120 slrgvpspesyGDCLDKSELPLVSLRVEEYNGMI 153
Cdd:TIGR02378  79 -----------GRCLEDDSGSVRTYEVRVEDGRV 101
PLN00095 PLN00095
chlorophyllide a oxygenase; Provisional
 46-154 9.09e-07

chlorophyllide a oxygenase; Provisional


Pssm-ID: 165668 [Multi-domain]  Cd Length: 394  Bit Score: 50.83  E-value: 9.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447007217  46 WVWVAHASEIPEGGSYKTINIGKQPVVVVRDRKKKVHVLLNRCRHRAatvCEHKKGK-TNSFV-CPYHGWSYALDGSLRG 123
Cdd:PLN00095  73 WFPVAFAAGLRDEDALIAFDLFNVPWVLFRDADGEAGCIKDECAHRA---CPLSLGKlVDGKAqCPYHGWEYETGGECAK 149

                         90       100       110
                 ....*....|....*....|....*....|....
gi 447007217 124 VPSPESYgdcldkseLPLV---SLRVEEYNGMIF 154
Cdd:PLN00095 150 MPSCKKF--------LKGVfadAAPVIERDGFIF 175
Rieske_RO_Alpha_VanA_DdmC cd03532
Rieske non-heme iron oxygenase (RO) family, Vanillate-O-demethylase oxygenase (VanA) and ...
 45-128 1.68e-06

Rieske non-heme iron oxygenase (RO) family, Vanillate-O-demethylase oxygenase (VanA) and dicamba O-demethylase oxygenase (DdmC) subfamily, N-terminal Rieske domain of the oxygenase alpha subunit; ROs comprise a large class of aromatic ring-hydroxylating dioxygenases that enable microorganisms to tolerate and utilize aromatic compounds for growth. The oxygenase alpha subunit contains an N-terminal Rieske domain with an [2Fe-2S] cluster and a C-terminal catalytic domain with a mononuclear Fe(II) binding site. The Rieske [2Fe-2S] cluster accepts electrons from a reductase or ferredoxin component and transfers them to the mononuclear iron for catalysis. Vanillate-O-demethylase is a heterodimeric enzyme consisting of a terminal oxygenase (VanA) and reductase (VanB) components. This enzyme reductively catalyzes the conversion of vanillate into protocatechuate and formaldehyde. Protocatechuate and vanillate are important intermediate metabolites in the degradation pathway of lignin-derived compounds such as ferulic acid and vanillin by soil microbes. DDmC is the oxygenase component of a three-component dicamba O-demethylase found in Pseudomonas maltophila, that catalyzes the conversion of a widely used herbicide called herbicide dicamba (2-methoxy-3,6-dichlorobenzoic acid) to DCSA (3,6-dichlorosalicylic acid).


Pssm-ID: 239608 [Multi-domain]  Cd Length: 116  Bit Score: 46.59  E-value: 1.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447007217  45 TWVWVAHASEIPEGGSYKTInIGKqPVVVVRDRKKKVHVLLNRCRHRAATVcehKKGKT--NSFVCPYHGWSYALDGSLR 122
Cdd:cd03532    5 AWYVAAWADELGDKPLARTL-LGE-PVVLYRTQDGRVAALEDRCPHRSAPL---SKGSVegGGLVCGYHGLEFDSDGRCV 79


                 ....*.
gi 447007217 123 GVPSPE 128
Cdd:cd03532   80 HMPGQE 85
Rieske_RO_Alpha_KSH cd03531
The alignment model represents the N-terminal rieske iron-sulfur domain of KshA, the oxygenase ...
 63-125 1.11e-05

The alignment model represents the N-terminal rieske iron-sulfur domain of KshA, the oxygenase component of 3-ketosteroid 9-alpha-hydroxylase (KSH). The terminal oxygenase component of KSH is a key enzyme in the microbial steroid degradation pathway, catalyzing the 9 alpha-hydroxylation of 4-androstene-3,17-dione (AD) and 1,4-androstadiene-3,17-dione (ADD). KSH is a two-component class IA monooxygenase, with terminal oxygenase (KshA) and oxygenase reductase (KshB) components. KSH activity has been found in many actino- and proteo- bacterial genera including Rhodococcus, Nocardia, Arthrobacter, Mycobacterium, and Burkholderia.


Pssm-ID: 239607 [Multi-domain]  Cd Length: 115  Bit Score: 44.33  E-value: 1.11e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447007217  63 TINIGKQPVVVVRDRKKKVHVLLNRCRHRAATVcEHKKGKTNSFVCPYHGWSYALDGSLRGVP 125
Cdd:cd03531   18 GVEAFGTKLVVFADSDGALNVLDAYCRHMGGDL-SQGTVKGDEIACPFHDWRWGGDGRCKAIP 79
Rieske_RO_Alpha_Tic55 cd04338
Tic55 is a 55kDa LLS1-related non-heme iron oxygenase associated with protein transport ...
 46-125 5.83e-05

Tic55 is a 55kDa LLS1-related non-heme iron oxygenase associated with protein transport through the plant inner chloroplast membrane. This domain represents the N-terminal Rieske domain of the Tic55 oxygenase alpha subunit. Tic55 is closely related to the oxygenase alpha subunits of a small subfamily of enzymes found in plants as well as oxygenic cyanobacterial photosynthesizers including LLS1 (lethal leaf spot 1, also known as PaO), Ptc52, and ACD1 (accelerated cell death 1). ROs comprise a large class of aromatic ring-hydroxylating dioxygenases that enable microorganisms to tolerate and utilize aromatic compounds for growth. The oxygenase alpha subunit contains an N-terminal Rieske domain with an [2Fe-2S] cluster and a C-terminal catalytic domain with a mononuclear Fe(II) binding site. The Rieske [2Fe-2S] cluster accepts electrons from a reductase or ferredoxin component and transfers them to the mononuclear iron for catalysis.


Pssm-ID: 239830 [Multi-domain]  Cd Length: 134  Bit Score: 42.51  E-value: 5.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447007217  46 WVWVAHASEIPEGGSYkTINIGKQPVVVVRDRKKKVHVLLNRCRHRAATVCEHK--KGKTNsfvCPYHGWSYALDGSLRG 123
Cdd:cd04338   18 WYPLYLLKDVPTDAPL-GLSVYDEPFVLFRDQNGQLRCLEDRCPHRLAKLSEGQliDGKLE---CLYHGWQFGGEGKCVK 93


                 ..
gi 447007217 124 VP 125
Cdd:cd04338   94 IP 95
Rieske_YhfW_C cd03477
YhfW family, C-terminal Rieske domain; YhfW is a protein of unknown function with an ...
 59-121 9.91e-05

YhfW family, C-terminal Rieske domain; YhfW is a protein of unknown function with an N-terminal DadA-like (glycine/D-amino acid dehydrogenase) domain and a C-terminal Rieske domain. The Rieske domain is a [2Fe-2S] cluster binding domain involved in electron transfer. It is 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. YhfW is found in bacteria, some eukaryotes and archaea.


Pssm-ID: 239559 [Multi-domain]  Cd Length: 91  Bit Score: 40.75  E-value: 9.91e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447007217  59 GSYKTINIGKQPVVVVRDRKKKVHVLLNRCRHRAATVCEHKKGKTnsFVCPYHGWSYALDGSL 121
Cdd:cd03477   11 GEGGVVNIGGKRLAVYRDEDGVLHTVSATCTHLGCIVHWNDAEKS--WDCPCHGSRFSYDGEV 71
RHO_alpha_C_3 cd08887
C-terminal catalytic domain of the oxygenase alpha subunit of an uncharacterized subgroup of ...
 192-381 1.36e-04

C-terminal catalytic domain of the oxygenase alpha subunit of an uncharacterized subgroup of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases; C-terminal catalytic domain of the oxygenase alpha subunit of a functionally uncharacterized subgroup of the Rieske-type non-heme iron aromatic ring-hydroxylating oxygenase (RHO) family. RHOs, also known as aromatic ring hydroxylating dioxygenases, utilize non-heme Fe(II) to catalyze the addition of hydroxyl groups to the aromatic ring, an initial step in the oxidative degradation of aromatic compounds. RHOs are composed of either two or three protein components, and are comprised of an electron transport chain (ETC) and an oxygenase. The ETC transfers reducing equivalents from the electron donor to the oxygenase component, which in turn transfers electrons to the oxygen molecules. The oxygenase components are oligomers, either (alpha)n or (alpha)n(beta)n. The alpha subunits are the catalytic components and have an N-terminal domain, which binds a Rieske-like 2Fe-2S cluster, and a C-terminal domain which binds the non-heme Fe(II). The Fe(II) is co-ordinated by conserved His and Asp residues. This group contains a putative Parvibaculum lavamentivorans (T) DS-1 oxygenase; this organism catabolizes commercial linear alkylbenzenesulfonate surfactant (LAS) and other surfactants, by a pathway involving an undefined 'omega-oxygenation' and beta-oxidation of the LAS side chain. The nature of the LAS-oxygenase is unknown but is likely a multicomponent system. This subfamily belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket.


Pssm-ID: 176896  Cd Length: 185  Bit Score: 42.68  E-value: 1.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447007217 192 EHRFRFPGNWKIQLENTTDAYHFPLVHKSFLSSVdekteelfnFENQPGFVEDLGnGHSVMVmipelvdleedLMERPIQ 271
Cdd:cd08887    3 SRRFDVAANWKLALDGFLEGYHFKVLHKNTIAPY---------FYDNLSVYDAFG-PHSRIV-----------FPRKSIE 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447007217 272 ErfedlaqaLRDEGHEELEVRRivravgGSGFNLNLFPNIacSMAFFR------VLQPISVAETEIHHSVITmdggPQIA 345
Cdd:cd08887   62 S--------LRDLPEDEWDLRR------HLTVIYTLFPNV--SLLVQPdhleiiQIEPGSPDRTRVTVYLLI----PPPP 121

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 447007217 346 NQYRLRlhEHFQGPFGF----GTPDDSEAWERVQHGANAG 381
Cdd:cd08887  122 DTEEAR--AYWDKNWDFlmavVLDEDFEVAEEIQRGLASG 159
Rieske_NirD_small_Bacillus cd03530
Small subunit of nitrite reductase (NirD) family, Rieske domain; composed of proteins similar ...
 46-117 5.51e-04

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: 39.13  E-value: 5.51e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447007217  46 WVWVAHASEIPEGGSyKTINIGKQPVVVVRDRKKKVHVLLNRCRHRAATVCE---HkkgkTNSFVCPYHGWSYAL 117
Cdd:cd03530    1 WIDIGALEDIPPRGA-RKVQTGGGEIAVFRTADDEVFALENRCPHKGGPLSEgivH----GEYVTCPLHNWVIDL 70
Rieske_RO_Alpha_PaO cd03480
Rieske non-heme iron oxygenase (RO) family, Pheophorbide a oxygenase (PaO) subfamily, ...
 71-154 6.45e-04

Rieske non-heme iron oxygenase (RO) family, Pheophorbide a oxygenase (PaO) subfamily, N-terminal Rieske domain of the oxygenase alpha subunit; composed of the oxygenase alpha subunits of a small subfamily of enzymes found in plants as well as oxygenic cyanobacterial photosynthesizers including LLS1 (lethal leaf spot 1, also known as PaO) and ACD1 (accelerated cell death 1). ROs comprise a large class of aromatic ring-hydroxylating dioxygenases that enable microorganisms to tolerate and utilize aromatic compounds for growth. The oxygenase alpha subunit contains an N-terminal Rieske domain with an [2Fe-2S] cluster and a C-terminal catalytic domain with a mononuclear Fe(II) binding site. The Rieske [2Fe-2S] cluster accepts electrons from a reductase or ferredoxin component and transfers them to the mononuclear iron for catalysis. PaO expression increases upon physical wounding of plant leaves and is thought to catalyze a key step in chlorophyll degradation. The Arabidopsis-accelerated cell death gene ACD1 is involved in oxygenation of PaO.


Pssm-ID: 239562 [Multi-domain]  Cd Length: 138  Bit Score: 39.61  E-value: 6.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447007217  71 VVVVRDRK-KKVHVLLNRCRHRAATVCEHKKGKTNSFVCPYHGWSYALDGSLRGVPSPESYGDCLDKSELPLVSLRVEEY 149
Cdd:cd03480   42 LVIWWDRNsQQWRAFDDQCPHRLAPLSEGRIDEEGCLECPYHGWSFDGSGSCQRIPQAAEGGKAHTSPRACVASLPTAVR 121


                 ....*
gi 447007217 150 NGMIF 154
Cdd:cd03480  122 QGLLF 126
PLN02518 PLN02518
pheophorbide a oxygenase
 71-129 9.54e-04

pheophorbide a oxygenase


Pssm-ID: 215283 [Multi-domain]  Cd Length: 539  Bit Score: 41.39  E-value: 9.54e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447007217  71 VVVVRDRKK-KVHVLLNRCRHRAATVCEHKKGKTNSFVCPYHGWSYALDGSLRGVPS-----PES 129
Cdd:PLN02518 115 LVLWKDPNQgEWVAFDDKCPHRLAPLSEGRIDENGHLQCSYHGWSFDGCGSCTRIPQaapegPEA 179
Rieske_NirD cd03529
Assimilatory nitrite reductase (NirD) family, Rieske domain; Assimilatory nitrate and nitrite ...
 46-154 1.94e-03

Assimilatory nitrite reductase (NirD) family, Rieske domain; Assimilatory nitrate and nitrite reductases convert nitrate through nitrite to ammonium. Members include bacterial and fungal proteins. The bacterial NirD contains a single Rieske domain while fungal proteins have a C-terminal Rieske domain in addition to several other domains. The fungal NirD is involved in nutrient acquisition, functioning at the soil/fungus interface to control nutrient exchange between the fungus and the host plant. The Rieske domain is a [2Fe-2S] cluster binding domain involved in electron transfer. The Rieske [2Fe-2S] cluster is liganded to two histidine and two cysteine residues present in conserved sequences called Rieske motifs. In this family, only a few members contain these residues. Other members may have lost the ability to bind the Rieske [2Fe-2S] cluster.


Pssm-ID: 239605 [Multi-domain]  Cd Length: 103  Bit Score: 37.49  E-value: 1.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447007217  46 WVWVAHASEIPEGGSyKTINIGKQPVVVVRDRKKKVHVLLNRCRHRAATV------CEHKKgktNSFV-CPYHGWSYALD 118
Cdd:cd03529    1 WQTVCALDDLPPGSG-VAALVGDTQIAIFRLPGREVYAVQNMDPHSRANVlsrgivGDIGG---EPVVaSPLYKQHFSLK 76

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 447007217 119 GslrgvpspesyGDCLDKSELPLVSLRVEEYNGMIF 154
Cdd:cd03529   77 T-----------GRCLEDEDVSVATFPVRVEDGEVY 101
 
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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