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Conserved domains on  [gi|754524259|dbj|GAM98641|]
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pheophorbide a oxygenase [alpha proteobacterium U9-1i]

Protein Classification

aromatic ring-hydroxylating dioxygenase subunit alpha( domain architecture ID 11468605)

aromatic ring-hydroxylating dioxygenase subunit alpha is the catalytic component of a complex that catalyzes the addition of hydroxyl groups to the aromatic ring, an initial step in the oxidative degradation of aromatic compounds

CATH:  3.90.380.10|2.102.10.10
EC:  1.14.13.-
Gene Ontology:  GO:0051537|GO:0016491
PubMed:  11849939
SCOP:  4001667

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PobA super family cl47407
Chlorophyllide a oxygenase/letal leaf spot protein [Coenzyme transport and metabolism];
1-306 8.79e-56

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


The actual alignment was detected with superfamily member COG5749:

Pssm-ID: 444459 [Multi-domain]  Cd Length: 349  Bit Score: 185.59  E-value: 8.79e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754524259   1 MSELLRDLWYFAATSKEVTAGKMFRREILGEPVVLGRDGQGRAFALRDICPHRAVPLSAGRVtETDgvqTVECPYHGWRF 80
Cdd:COG5749   12 QPFIFRNHWYPVAPSEDLKPNKPKPVTLLGEPLVIWRDSDGKVVALEDRCPHRGAPLSEGRV-EGG---NLRCPYHGWQF 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754524259  81 GtADGVCKQIPSLVEGQAYEASrIRVRHYPTHEANGIVLVFVSSDPRFADAPPPApefgLAELSEPKFVID---RIFAAS 157
Cdd:COG5749   88 D-GDGKCVHIPQLPENQPIPKN-AKVKSYPVQERYGLIWVWLGDPPQADETPIPD----IPELDDPEWVATssvRDLECH 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754524259 158 MDNAVVGLMDPAHVPYVHNQWW-WRPPSTGKKLKEKRfvpRERGWAIERHAPASNSLAYKYLFGGAVTTEISFMLPGFRW 236
Cdd:COG5749  162 YSRLIENLIDPSHVPFVHHGTQgNRKQAQPLEMEIES---TPNGITASYTAQSYYQLFFPFLGNLDETLTITFIYPNTVS 238

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 754524259 237 EVVETPKSRLFTLTCL-TPENENSTRI-TQVT--YWRDAIWLDlikPILIPAGREFLDQDGRMVDLQNSGLKYS 306
Cdd:COG5749  239 VDIGSGLGGRFGIVLYaTPIDEGKTRAyAIFFrnFAKKPRWLR---HFLKLLRNGILEQDVIILESQQPALLQL 309
 
Name Accession Description Interval E-value
PobA COG5749
Chlorophyllide a oxygenase/letal leaf spot protein [Coenzyme transport and metabolism];
1-306 8.79e-56

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


Pssm-ID: 444459 [Multi-domain]  Cd Length: 349  Bit Score: 185.59  E-value: 8.79e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754524259   1 MSELLRDLWYFAATSKEVTAGKMFRREILGEPVVLGRDGQGRAFALRDICPHRAVPLSAGRVtETDgvqTVECPYHGWRF 80
Cdd:COG5749   12 QPFIFRNHWYPVAPSEDLKPNKPKPVTLLGEPLVIWRDSDGKVVALEDRCPHRGAPLSEGRV-EGG---NLRCPYHGWQF 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754524259  81 GtADGVCKQIPSLVEGQAYEASrIRVRHYPTHEANGIVLVFVSSDPRFADAPPPApefgLAELSEPKFVID---RIFAAS 157
Cdd:COG5749   88 D-GDGKCVHIPQLPENQPIPKN-AKVKSYPVQERYGLIWVWLGDPPQADETPIPD----IPELDDPEWVATssvRDLECH 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754524259 158 MDNAVVGLMDPAHVPYVHNQWW-WRPPSTGKKLKEKRfvpRERGWAIERHAPASNSLAYKYLFGGAVTTEISFMLPGFRW 236
Cdd:COG5749  162 YSRLIENLIDPSHVPFVHHGTQgNRKQAQPLEMEIES---TPNGITASYTAQSYYQLFFPFLGNLDETLTITFIYPNTVS 238

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 754524259 237 EVVETPKSRLFTLTCL-TPENENSTRI-TQVT--YWRDAIWLDlikPILIPAGREFLDQDGRMVDLQNSGLKYS 306
Cdd:COG5749  239 VDIGSGLGGRFGIVLYaTPIDEGKTRAyAIFFrnFAKKPRWLR---HFLKLLRNGILEQDVIILESQQPALLQL 309
Rieske_RO_Alpha_N cd03469
Rieske non-heme iron oxygenase (RO) family, N-terminal Rieske domain of the oxygenase alpha ...
 9-134 1.05e-33

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: 120.77  E-value: 1.05e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754524259   9 WYFAATSKEVT-AGKMFRREILGEPVVLGRDGQGRAFALRDICPHRAVPLSAGRVTETDgvqTVECPYHGWRFGtADGVC 87
Cdd:cd03469    1 WYFVGHSSELPePGDYVTLELGGEPLVLVRDRDGEVRAFHNVCPHRGARLCEGRGGNAG---RLVCPYHGWTYD-LDGKL 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 754524259  88 KQIPSLVEGQAYEASRIRVRHYPTHEANGivLVFVSSDPrfaDAPPP 134
Cdd:cd03469   77 VGVPREEGFPGFDKEKLGLRTVPVEEWGG--LIFVNLDP---DAPPL 118
Rieske pfam00355
Rieske [2Fe-2S] domain; The rieske domain has a [2Fe-2S] centre. Two conserved cysteines ...
 9-100 3.18e-25

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: 97.42  E-value: 3.18e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754524259    9 WYFAATSKEVTAGKMFRREILGEPVVLGRDGQGRAFALRDICPHRAVPLSAGRVTETDgvqTVECPYHGWRFGtADGVCK 88
Cdd:pfam00355   2 WYPVCHSSELPEGEPKVVEVGGEPLVVFRDEDGELYALEDRCPHRGAPLSEGKVNGGG---RLECPYHGWRFD-GTGKVV 77

                          90
                  ....*....|..
gi 754524259   89 QIPSLVEGQAYE 100
Cdd:pfam00355  78 KVPAPRPLKSYP 89
PLN02281 PLN02281
chlorophyllide a oxygenase
 5-189 5.97e-17

chlorophyllide a oxygenase


Pssm-ID: 177920 [Multi-domain]  Cd Length: 536  Bit Score: 81.70  E-value: 5.97e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754524259   5 LRDLWYFAATSKEVTAGKMFRREILGEPVVLGRDGQGRAFALRDICPHRAVPLSAGRVTETdgvqTVECPYHGWRFGTaD 84
Cdd:PLN02281 217 LKNFWYPVAFTADLKHDTMVPIECFEQPWVIFRGEDGKPGCVRNTCAHRACPLDLGTVNEG----RIQCPYHGWEYST-D 291

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754524259  85 GVCKQIPSLvegqayEASRIRVRHYPTHEANGIVLVFVSSDPRFADAPPPAPEFGLAELSEPKFVIDRIFAASMDNavvg 164
Cdd:PLN02281 292 GECKKMPST------KLLKVKIKSLPCLEQEGMIWIWPGDEPPAPILPSLQPPSGFLIHAELVMDLPVEHGLLLDN---- 361

                        170       180
                 ....*....|....*....|....*...
gi 754524259 165 LMDPAHVPYVHNQWW---WRPPSTGKKL 189
Cdd:PLN02281 362 LLDLAHAPFTHTSTFakgWSVPSLVKFL 389
nirD_assim_sml TIGR02378
nitrite reductase [NAD(P)H], small subunit; This model describes NirD, the small subunit of ...
 37-120 4.81e-12

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: 61.95  E-value: 4.81e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754524259   37 RDGQGRAFALRDICPH-RAVPLSAGRVTETDGVQTVECPYHGWRFGTADGVCKQIPSLvegqayeasriRVRHYPTHEAN 115
Cdd:TIGR02378  30 RVPGDQVFAIQNMCPHkRAFVLSRGIVGDAQGELWVACPLHKRNFRLEDGRCLEDDSG-----------SVRTYEVRVED 98


                  ....*
gi 754524259  116 GIVLV 120
Cdd:TIGR02378  99 GRVYV 103
 
Name Accession Description Interval E-value
PobA COG5749
Chlorophyllide a oxygenase/letal leaf spot protein [Coenzyme transport and metabolism];
1-306 8.79e-56

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


Pssm-ID: 444459 [Multi-domain]  Cd Length: 349  Bit Score: 185.59  E-value: 8.79e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754524259   1 MSELLRDLWYFAATSKEVTAGKMFRREILGEPVVLGRDGQGRAFALRDICPHRAVPLSAGRVtETDgvqTVECPYHGWRF 80
Cdd:COG5749   12 QPFIFRNHWYPVAPSEDLKPNKPKPVTLLGEPLVIWRDSDGKVVALEDRCPHRGAPLSEGRV-EGG---NLRCPYHGWQF 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754524259  81 GtADGVCKQIPSLVEGQAYEASrIRVRHYPTHEANGIVLVFVSSDPRFADAPPPApefgLAELSEPKFVID---RIFAAS 157
Cdd:COG5749   88 D-GDGKCVHIPQLPENQPIPKN-AKVKSYPVQERYGLIWVWLGDPPQADETPIPD----IPELDDPEWVATssvRDLECH 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754524259 158 MDNAVVGLMDPAHVPYVHNQWW-WRPPSTGKKLKEKRfvpRERGWAIERHAPASNSLAYKYLFGGAVTTEISFMLPGFRW 236
Cdd:COG5749  162 YSRLIENLIDPSHVPFVHHGTQgNRKQAQPLEMEIES---TPNGITASYTAQSYYQLFFPFLGNLDETLTITFIYPNTVS 238

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 754524259 237 EVVETPKSRLFTLTCL-TPENENSTRI-TQVT--YWRDAIWLDlikPILIPAGREFLDQDGRMVDLQNSGLKYS 306
Cdd:COG5749  239 VDIGSGLGGRFGIVLYaTPIDEGKTRAyAIFFrnFAKKPRWLR---HFLKLLRNGILEQDVIILESQQPALLQL 309
HcaE COG4638
Phenylpropionate dioxygenase or related ring-hydroxylating dioxygenase, large terminal subunit ...
 1-329 4.06e-46

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: 159.00  E-value: 4.06e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754524259   1 MSELLRDLWYFAATSKEVT-AGKMFRREILGEPVVLGRDGQGRAFALRDICPHRAVPLSAGRvtetdGVQ-TVECPYHGW 78
Cdd:COG4638   19 LERIFRRGWYYVGHSSELPePGDYLTRTILGEPVVLVRDKDGEVRAFHNVCPHRGAPLSEGR-----GNGgRLVCPYHGW 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754524259  79 RFGTaDGVCKQIPSLVEGQAYEASRIRVRHYPTHEANGivLVFVSSDPrfaDAPPPAPEFG-----LAELSEPKFVIDR- 152
Cdd:COG4638   94 TYDL-DGRLVGIPHMEGFPDFDPARAGLRSVPVEEWGG--LIFVWLGP---DAPPLAEYLGplaeyLDPYDFGELKVAGr 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754524259 153 ---IFAASMDNAVVGLMDPAHVPYVHNQWWWrppstgkklkekrfvprergwaierhapasnslaykylfggavtteisF 229
Cdd:COG4638  168 etyEVNANWKLVVENFLDGYHVPFVHPGIIL------------------------------------------------F 199

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754524259 230 MLPGFRWEVVetpkSRLFTLTCLTPENENSTRITQVTYWRDAIWLDLIKPILIPAGREFLDQDGRMVDLQNSGLK---YS 306
Cdd:COG4638  200 LFPNLMILDY----PDHLVVRTVTPVSPDRTRVFVTFYVPKDALDPEARADLEAFWGRVFEEDREIVERQQRGLRslaYP 275

                        330       340
                 ....*....|....*....|...
gi 754524259 307 PAMLWIDDIDVQAKWYLKLKREW 329
Cdd:COG4638  276 GPYLSRSPAEGGVRHFRRWLRRL 298
Rieske_RO_Alpha_N cd03469
Rieske non-heme iron oxygenase (RO) family, N-terminal Rieske domain of the oxygenase alpha ...
 9-134 1.05e-33

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: 120.77  E-value: 1.05e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754524259   9 WYFAATSKEVT-AGKMFRREILGEPVVLGRDGQGRAFALRDICPHRAVPLSAGRVTETDgvqTVECPYHGWRFGtADGVC 87
Cdd:cd03469    1 WYFVGHSSELPePGDYVTLELGGEPLVLVRDRDGEVRAFHNVCPHRGARLCEGRGGNAG---RLVCPYHGWTYD-LDGKL 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 754524259  88 KQIPSLVEGQAYEASRIRVRHYPTHEANGivLVFVSSDPrfaDAPPP 134
Cdd:cd03469   77 VGVPREEGFPGFDKEKLGLRTVPVEEWGG--LIFVNLDP---DAPPL 118
Rieske_RO_Alpha_VanA_DdmC cd03532
Rieske non-heme iron oxygenase (RO) family, Vanillate-O-demethylase oxygenase (VanA) and ...
 4-130 1.09e-27

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: 104.76  E-value: 1.09e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754524259   4 LLRDLWYFAATSKEVTaGKMFRREILGEPVVLGRDGQGRAFALRDICPHRAVPLSAGRVtETDGVQtveCPYHGWRFGtA 83
Cdd:cd03532    1 FPRNAWYVAAWADELG-DKPLARTLLGEPVVLYRTQDGRVAALEDRCPHRSAPLSKGSV-EGGGLV---CGYHGLEFD-S 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 754524259  84 DGVCKQIPslveGQAYEASRIRVRHYPTHEANGIVLVFVsSDPRFAD 130
Cdd:cd03532   75 DGRCVHMP----GQERVPAKACVRSYPVVERDALIWIWM-GDAALAD 116
Rieske_RO_Alpha_PhDO_like cd03479
Rieske non-heme iron oxygenase (RO) family, Phthalate 4,5-dioxygenase (PhDO)-like subfamily, ...
 1-138 1.34e-25

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: 100.01  E-value: 1.34e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754524259   1 MSELLRDLWYFAATSKEVTA-GKMFRREILGEPVVLGRDGQGRAFALRDICPHRAVPLSAGRVTEtDGVQtveCPYHGWR 79
Cdd:cd03479   14 MGELLRRYWQPVALSSELTEdGQPVRVRLLGEDLVAFRDTSGRVGLLDEHCPHRGASLVFGRVEE-CGLR---CCYHGWK 89

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 754524259  80 FGTaDGVCKQIPSLVEGQAYEaSRIRVRHYPTHEANGIVLVFVSSdprfADAPPPAPEF 138
Cdd:cd03479   90 FDV-DGQCLEMPSEPPDSQLK-QKVRQPAYPVRERGGLVWAYMGP----AEEAPEFPRY 142
Rieske pfam00355
Rieske [2Fe-2S] domain; The rieske domain has a [2Fe-2S] centre. Two conserved cysteines ...
 9-100 3.18e-25

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: 97.42  E-value: 3.18e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754524259    9 WYFAATSKEVTAGKMFRREILGEPVVLGRDGQGRAFALRDICPHRAVPLSAGRVTETDgvqTVECPYHGWRFGtADGVCK 88
Cdd:pfam00355   2 WYPVCHSSELPEGEPKVVEVGGEPLVVFRDEDGELYALEDRCPHRGAPLSEGKVNGGG---RLECPYHGWRFD-GTGKVV 77

                          90
                  ....*....|..
gi 754524259   89 QIPSLVEGQAYE 100
Cdd:pfam00355  78 KVPAPRPLKSYP 89
Rieske_RO_Alpha_PaO cd03480
Rieske non-heme iron oxygenase (RO) family, Pheophorbide a oxygenase (PaO) subfamily, ...
 6-129 9.42e-23

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: 92.39  E-value: 9.42e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754524259   6 RDLWYFAATSKEVTAGKMFRREILGEPVVLGRDGQG---RAFAlrDICPHRAVPLSAGRVTEtDGvqTVECPYHGWRFgT 82
Cdd:cd03480   15 REVWYPVAYVEDLDPSRPTPFTLLGRDLVIWWDRNSqqwRAFD--DQCPHRLAPLSEGRIDE-EG--CLECPYHGWSF-D 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 754524259  83 ADGVCKQIP-SLVEGQAYEASRIRVRHYPTHEANGIVLVFVSSDPRFA 129
Cdd:cd03480   89 GSGSCQRIPqAAEGGKAHTSPRACVASLPTAVRQGLLFVWPGEPENAK 136
Rieske_RO_Alpha_Cao cd04337
Cao (chlorophyll a oxygenase) is a rieske non-heme iron-sulfur protein located within the ...
 1-136 4.92e-22

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: 90.24  E-value: 4.92e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754524259   1 MSELLRDLWYFAATSKEVTAGKMFRREILGEPVVLGRDGQGRAFALRDICPHRAVPLSAGRVTETdgvqTVECPYHGWRF 80
Cdd:cd04337   10 LEPGLRNFWYPVEFSKDLKMDTMVPFELFGQPWVLFRDEDGTPGCIRDECAHRACPLSLGKVIEG----RIQCPYHGWEY 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 754524259  81 GTaDGVCKQIPSLvegqayEASRIRVRHYPTHEANGIVLVFVSSDPrfadaPPPAP 136
Cdd:cd04337   86 DG-DGECTKMPST------KCLNVGIAALPCMEQDGMIWVWPGDDP-----PAALP 129
Rieske_RO_Alpha_OMO_CARDO cd03548
Rieske non-heme iron oxygenase (RO) family, 2-Oxoquinoline 8-monooxygenase (OMO) and Carbazole ...
 5-135 5.45e-22

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: 90.17  E-value: 5.45e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754524259   5 LRDLWYFAATSKEVTAGKMFRREILGEPVVLGRDGqGRAFALRDICPHRAVPLSAGRVTETDGvqTVECPYHGWRFGTAD 84
Cdd:cd03548   11 FRNHWYPALFSHELEEGEPKGIQLCGEPILLRRVD-GKVYALKDRCLHRGVPLSKKPECFTKG--TITCWYHGWTYRLDD 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 754524259  85 GVCKQIpsLVEGQAYEASRIRVRHYPTHEANGIVLVFVsSDPRFADAPPPA 135
Cdd:cd03548   88 GKLVTI--LANPDDPLIGRTGLKTYPVEEAKGMIFVFV-GDGDYADPPPLA 135
Rieske cd03467
Rieske domain; a [2Fe-2S] cluster binding domain commonly found in Rieske non-heme iron ...
 9-91 2.35e-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: 79.07  E-value: 2.35e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754524259   9 WYFAATSKEVTAGKMFRREILGEPVVLGRDGQGRAFALRDICPHRAVPLSAGRVTEtdgvQTVECPYHGWRFGTADGVCK 88
Cdd:cd03467    1 WVVVGALSELPPGGGRVVVVGGGPVVVVRREGGEVYALSNRCTHQGCPLSEGEGED----GCIVCPCHGSRFDLRTGEVV 76


                 ...
gi 754524259  89 QIP 91
Cdd:cd03467   77 SGP 79
NirD COG2146
Ferredoxin subunit of nitrite reductase or a ring-hydroxylating dioxygenase [Inorganic ion ...
 9-120 5.09e-18

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: 78.34  E-value: 5.09e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754524259   9 WYFAATSKEVTAGKMFRREILGEPVVLGRDGqGRAFALRDICPHRAVPLSAGRVtetDGvQTVECPYHGWRFGTADGVCk 88
Cdd:COG2146    3 EVKVCALDDLPEGGGVVVEVGGKQIAVFRTD-GEVYAYDNRCPHQGAPLSEGIV---DG-GVVTCPLHGARFDLRTGEC- 76

                         90       100       110
                 ....*....|....*....|....*....|..
gi 754524259  89 qipslVEGQAYEasriRVRHYPTHEANGIVLV 120
Cdd:COG2146   77 -----LGGPATE----PLKTYPVRVEDGDVYV 99
PLN02281 PLN02281
chlorophyllide a oxygenase
 5-189 5.97e-17

chlorophyllide a oxygenase


Pssm-ID: 177920 [Multi-domain]  Cd Length: 536  Bit Score: 81.70  E-value: 5.97e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754524259   5 LRDLWYFAATSKEVTAGKMFRREILGEPVVLGRDGQGRAFALRDICPHRAVPLSAGRVTETdgvqTVECPYHGWRFGTaD 84
Cdd:PLN02281 217 LKNFWYPVAFTADLKHDTMVPIECFEQPWVIFRGEDGKPGCVRNTCAHRACPLDLGTVNEG----RIQCPYHGWEYST-D 291

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754524259  85 GVCKQIPSLvegqayEASRIRVRHYPTHEANGIVLVFVSSDPRFADAPPPAPEFGLAELSEPKFVIDRIFAASMDNavvg 164
Cdd:PLN02281 292 GECKKMPST------KLLKVKIKSLPCLEQEGMIWIWPGDEPPAPILPSLQPPSGFLIHAELVMDLPVEHGLLLDN---- 361

                        170       180
                 ....*....|....*....|....*...
gi 754524259 165 LMDPAHVPYVHNQWW---WRPPSTGKKL 189
Cdd:PLN02281 362 LLDLAHAPFTHTSTFakgWSVPSLVKFL 389
PLN02518 PLN02518
pheophorbide a oxygenase
 6-177 3.17e-16

pheophorbide a oxygenase


Pssm-ID: 215283 [Multi-domain]  Cd Length: 539  Bit Score: 79.53  E-value: 3.17e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754524259   6 RDLWYFAATSKEVTAGKMFRREILGEPVVLGRD-GQGRAFALRDICPHRAVPLSAGRVTETDGVQtveCPYHGWRFGtAD 84
Cdd:PLN02518  88 RDHWYPVSLVEDLDPSVPTPFQLLGRDLVLWKDpNQGEWVAFDDKCPHRLAPLSEGRIDENGHLQ---CSYHGWSFD-GC 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754524259  85 GVCKQIPSLV----EGQAYEASRIRVRHYPTHEANGivLVFVSSDPR-----FADAPPPAPefglAELSEPKF---VIDR 152
Cdd:PLN02518 164 GSCTRIPQAApegpEARAVKSPRACAIKFPTMVSQG--LLFVWPDENgweraQATKPPMLP----DEFDDPEFstvTIQR 237

                        170       180
                 ....*....|....*....|....*
gi 754524259 153 IFAASMDNAVVGLMDPAHVPYVHNQ 177
Cdd:PLN02518 238 DLFYGYDTLMENVSDPSHIDFAHHK 262
Rieske_RO_Alpha_Tic55 cd04338
Tic55 is a 55kDa LLS1-related non-heme iron oxygenase associated with protein transport ...
 6-137 6.26e-16

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: 73.71  E-value: 6.26e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754524259   6 RDLWYFAATSKEVTAGKMFRREILGEPVVLGRDGQGRAFALRDICPHRAVPLSAGRVteTDGvqTVECPYHGWRFGTaDG 85
Cdd:cd04338   15 REEWYPLYLLKDVPTDAPLGLSVYDEPFVLFRDQNGQLRCLEDRCPHRLAKLSEGQL--IDG--KLECLYHGWQFGG-EG 89

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 754524259  86 VCKQIPSLVEGQAYEASRIrVRHYPTHEANGIVLVFVSsdprfaDAPPPAPE 137
Cdd:cd04338   90 KCVKIPQLPADAKIPKNAC-VKSYEVRDSQGVVWMWMS------EATPPDEE 134
Rieske_RO_ferredoxin cd03528
Rieske non-heme iron oxygenase (RO) family, Rieske ferredoxin component; composed of the ...
 9-120 1.67e-13

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: 65.59  E-value: 1.67e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754524259   9 WYFAATSKEVTAGKMFRREILGEPVVLGRDGqGRAFALRDICPHRAVPLSAGRVTETdgvqTVECPYHGWRFGTADGVCK 88
Cdd:cd03528    1 WVRVCAVDELPEGEPKRVDVGGRPIAVYRVD-GEFYATDDLCTHGDASLSEGYVEGG----VIECPLHGGRFDLRTGKAL 75

                         90       100       110
                 ....*....|....*....|....*....|..
gi 754524259  89 QIPslvegqAYEAsrirVRHYPTHEANGIVLV 120
Cdd:cd03528   76 SLP------ATEP----LKTYPVKVEDGDVYV 97
nirD_assim_sml TIGR02378
nitrite reductase [NAD(P)H], small subunit; This model describes NirD, the small subunit of ...
 37-120 4.81e-12

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: 61.95  E-value: 4.81e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754524259   37 RDGQGRAFALRDICPH-RAVPLSAGRVTETDGVQTVECPYHGWRFGTADGVCKQIPSLvegqayeasriRVRHYPTHEAN 115
Cdd:TIGR02378  30 RVPGDQVFAIQNMCPHkRAFVLSRGIVGDAQGELWVACPLHKRNFRLEDGRCLEDDSG-----------SVRTYEVRVED 98


                  ....*
gi 754524259  116 GIVLV 120
Cdd:TIGR02378  99 GRVYV 103
Rieske_NirD_small_Bacillus cd03530
Small subunit of nitrite reductase (NirD) family, Rieske domain; composed of proteins similar ...
 30-121 1.33e-11

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: 60.31  E-value: 1.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754524259  30 GEPVVLGRDGQGRAFALRDICPHRAVPLSAGRVtetdGVQTVECPYHGWRFgtadgvckqipSLVEGQAYEASRIRVRHY 109
Cdd:cd03530   22 GGEIAVFRTADDEVFALENRCPHKGGPLSEGIV----HGEYVTCPLHNWVI-----------DLETGEAQGPDEGCVRTF 86

                         90
                 ....*....|..
gi 754524259 110 PTHEANGIVLVF 121
Cdd:cd03530   87 PVKVEDGRVYLG 98
PLN00095 PLN00095
chlorophyllide a oxygenase; Provisional
 6-137 6.51e-11

chlorophyllide a oxygenase; Provisional


Pssm-ID: 165668 [Multi-domain]  Cd Length: 394  Bit Score: 63.16  E-value: 6.51e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754524259   6 RDLWY---FAATSKEVTAgkMFRREILGEPVVLGRDGQGRAFALRDICPHRAVPLSAGRVteTDGvqTVECPYHGWRFgT 82
Cdd:PLN00095  70 RAHWFpvaFAAGLRDEDA--LIAFDLFNVPWVLFRDADGEAGCIKDECAHRACPLSLGKL--VDG--KAQCPYHGWEY-E 142

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 754524259  83 ADGVCKQIPSLVEgqayEASRIRVRHYPTHEANGIVLVFV-SSDPRFADAPPPAPE 137
Cdd:PLN00095 143 TGGECAKMPSCKK----FLKGVFADAAPVIERDGFIFLWAgESDPADFVGPEAACE 194
Rieske_RO_Alpha_KSH cd03531
The alignment model represents the N-terminal rieske iron-sulfur domain of KshA, the oxygenase ...
 9-134 9.59e-11

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: 58.58  E-value: 9.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754524259   9 WYFAATSKEVTAGKMFRREILGEPVVLGRDGQGRAFALRDICPHRAVPLSAGRVTEtdgvQTVECPYHGWRFGtADGVCK 88
Cdd:cd03531    2 WHCLGLARDFRDGKPHGVEAFGTKLVVFADSDGALNVLDAYCRHMGGDLSQGTVKG----DEIACPFHDWRWG-GDGRCK 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 754524259  89 QIPSlvegqayeASRI----RVRHYPTHEANGivLVFVSSDPRfADAPPP 134
Cdd:cd03531   77 AIPY--------ARRVpplaRTRAWPTLERNG--QLFVWHDPE-GNPPPP 115
Rieske_2 pfam13806
Rieske-like [2Fe-2S] domain;
30-120 1.59e-09

Rieske-like [2Fe-2S] domain;


Pssm-ID: 433491 [Multi-domain]  Cd Length: 103  Bit Score: 54.48  E-value: 1.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754524259   30 GEPVVLGRDGQGRAFALRDICP-HRAVPLSAGRVTETDGVQTVECPYHGWRFGTADGVCKqipslvegqayEASRIRVRH 108
Cdd:pfam13806  22 GRQVAVFRLEDGQVYAIDNRDPfSGANVLSRGIVGDLGGELVVASPLYKQHFDLKTGECL-----------EDPEVSVPV 90

                          90
                  ....*....|..
gi 754524259  109 YPTHEANGIVLV 120
Cdd:pfam13806  91 YPVRVRDGNVEV 102
Rieske_RO_Alpha_PrnD cd03537
This alignment model represents the N-terminal rieske domain of the oxygenase alpha subunit of ...
 9-124 5.91e-09

This alignment model represents the N-terminal rieske domain of the oxygenase alpha subunit of aminopyrrolnitrin oxygenase (PrnD). PrnD is a novel Rieske N-oxygenase that catalyzes the final step in the pyrrolnitrin biosynthetic pathway, the oxidation of the amino group in aminopyrrolnitrin to a nitro group, forming the antibiotic pyrrolnitrin. The biosynthesis of pyrrolnitrin is one of the best examples of enzyme-catalyzed arylamine oxidation. Although arylamine oxygenases are widely distributed within the microbial world and used in a variety of metabolic reactions, PrnD represents one of only two known examples of arylamine oxygenases or N-oxygenases involved in arylnitro group formation, the other being AurF involved in aureothin biosynthesis.


Pssm-ID: 239611 [Multi-domain]  Cd Length: 123  Bit Score: 53.78  E-value: 5.91e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754524259   9 WYFAATSKEVTaGKMFRREILGEPVVLGRDGQGRAFALRDICPHRAVPLSAGRVTETdgvqTVECPYHGWRFgTADGVCK 88
Cdd:cd03537    4 WYVAMRSDDLK-DKPTELTLFGRPCVAWRGATGRAVVMDRHCSHLGANLADGRVKDG----CIQCPFHHWRY-DEQGQCV 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 754524259  89 QIPslveGQAYEASRI-------RVRHYPTHEANGIVLVFVSS 124
Cdd:cd03537   78 HIP----GHSTAVRRLepvprgaRQPTLVTAERYGYVWVWYGS 116
Rieske_AIFL_N cd03478
AIFL (apoptosis-inducing factor like) family, N-terminal Rieske domain; members of this family ...
 21-93 1.88e-08

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: 51.47  E-value: 1.88e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 754524259  21 GKMFRREILGEPVVLGRDGqGRAFALRDICPHRAVPLSAGRVTetDGvqTVECPYHGWRFGTADGVCKQIPSL 93
Cdd:cd03478   12 GEMKEVDVGDGKVLLVRQG-GEVHAIGAKCPHYGAPLAKGVLT--DG--RIRCPWHGACFNLRTGDIEDAPAL 79
Rieske_RO_Alpha_NDO cd03535
Rieske non-heme iron oxygenase (RO) family, Nathphalene 1,2-dioxygenase (NDO) subfamily, ...
 9-133 2.15e-08

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: 52.05  E-value: 2.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754524259   9 WYFAATSKEV-TAGKMFRREILGEPVVLGRDGQGRAFALRDICPHRAVPLSAgrvTETDGVQTVECPYHGWRFGTaDGVC 87
Cdd:cd03535    3 WVFLGHESEIpNAGDYVVRYIGDDSFIVCRDEDGEIRAMFNSCRHRGMQVCR---AEMGNTSHFRCPYHGWTYRN-TGRL 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 754524259  88 KQIPSLVE--GQAYEASRIRVRHYPTHEA-NGivLVFVSSDPrfaDAPP 133
Cdd:cd03535   79 VGVPAQQEayGGGFDKSQWGLRPAPNLDSyNG--LIFGSLDP---KAPS 122
RHO_alpha_C_DMO-like cd08878
C-terminal catalytic domain of the oxygenase alpha subunit of dicamba O-demethylase and ...
 161-330 2.04e-07

C-terminal catalytic domain of the oxygenase alpha subunit of dicamba O-demethylase and related aromatic ring hydroxylating dioxygenases; C-terminal catalytic domain of the oxygenase alpha subunit of Stenotrophomonas maltophilia dicamba O-demethylase (DMO) 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 carbazole 1,9a-dioxygenase, phthalate dioxygenase, vanillate O-demethylase, Pseudomonas putida 2-oxoquinoline 8-monooxygenase, and Comamonas testosteroni T-2 p-toluenesulfonate dioxygenase. It also includes the C-terminal domain of the lignin biphenyl-specific O-demethylase (LigX) of the 5,5'-dehydrodivanillic acid O- demethylation system of Sphingomonas paucimobilis SYK-6. 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: 176887  Cd Length: 196  Bit Score: 50.89  E-value: 2.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754524259 161 AVVGLMDPAHVPYVHNQWWWRPPSTGKKLKEKRFVPRERGWAIERHAPASNSLAYKYLFGGAVTTEISFMLPGF-----R 235
Cdd:cd08878   15 VVENLMDPSHVSFVHRSSIGRDAADLPSGPPKEVEEVPRGVTYRRWREDEDPPPFGFEGPVDRWRVIEFLLPNVllidpG 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754524259 236 WEVVETPKS--RLFTLTCLTPENENSTRItqvtYWRDAIWLDLIKPI---------LIPAGREFLDQDGRMVDLQNSGLK 304
Cdd:cd08878   95 VAPAGTREQgvRMRVTHWITPIDETTTHY----FWFFVRNFAPDEEKkddeeltetLRSGLSGAFNEDKEAVEAQQRIID 170

                        170       180
                 ....*....|....*....|....*.
gi 754524259 305 YSPAMLWIDDIDVQAKWYLKLKREWA 330
Cdd:cd08878  171 RDPTREHLGLSDKGIVRFRRLLRRLL 196
VanA_C pfam19112
Vanillate O-demethylase oxygenase C-terminal domain; This domain is found in a wide variety of ...
 159-300 4.21e-07

Vanillate O-demethylase oxygenase C-terminal domain; This domain is found in a wide variety of oxygenases such as Vanillate O-demethylase oxygenase and Toluene-4-sulfonate monooxygenase.


Pssm-ID: 436978  Cd Length: 195  Bit Score: 49.72  E-value: 4.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754524259  159 DNavvgLMDPAHVPYVHNQWWWRPPSTGKKLKEKRFVPRERG---WAIERHAPASNSLAYKYLFGGAVT---TEISFMLP 232
Cdd:pfam19112  10 DN----LLDLSHVAFVHPGTLGGPGGAELLDARTVVEEGERSvvvTREIPGKPPPPGFRAVLGDDGEVVdrwVTVEWHAP 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754524259  233 GF------RWEV--VETPKSRLFTLTCLTPENENSTRitqvTYWRDAIWLDL----IKPILIPAGREFLDQDGRMVDLQN 300
Cdd:pfam19112  86 GLvilligATDAgaPRGPGVRLPILHAITPETETSTH----YFWALARNFDLddadLSARLAEANHKAFDEDKPVLEAQQ 161
Rieske_NirD cd03529
Assimilatory nitrite reductase (NirD) family, Rieske domain; Assimilatory nitrate and nitrite ...
 30-120 7.17e-07

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: 47.12  E-value: 7.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754524259  30 GEPVVLGRDGQGRAFALRDICPH-RAVPLSAGRVTETDGVQTVECPYHgwrfgtadgvcKQIPSLVEGQAYEASRIRVRH 108
Cdd:cd03529   22 DTQIAIFRLPGREVYAVQNMDPHsRANVLSRGIVGDIGGEPVVASPLY-----------KQHFSLKTGRCLEDEDVSVAT 90

                         90
                 ....*....|..
gi 754524259 109 YPTHEANGIVLV 120
Cdd:cd03529   91 FPVRVEDGEVYV 102
Rieske_RO_Alpha_CMO cd03541
Rieske non-heme iron oxygenase (RO) family, Choline monooxygenase (CMO) subfamily, N-terminal ...
 9-86 1.46e-06

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: 46.78  E-value: 1.46e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 754524259   9 WYFAATSKEVTAGKMFRREILGE-PVVLGRDGQGRAFALRDICPHRAVPLSAGRVTETDGVqtveCPYHGWRFGTaDGV 86
Cdd:cd03541    2 WQVAGYSDQVKEKNQYFTGRLGNvEYVVCRDGNGKLHAFHNVCTHRASILACGSGKKSCFV----CPYHGWVYGL-DGS 75
Rieske_RO_Alpha_AntDO cd03538
Rieske non-heme iron oxygenase (RO) family, Anthranilate 1,2-dioxygenase (AntDO) subfamily, ...
 1-91 1.52e-06

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: 47.07  E-value: 1.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754524259   1 MSELLRDLW-YFAATSKEVTAGKMFRREILGEPVVLGRDGQGRAFALRDICPHRAVPLsagrVTETDGV--QTVECPYHG 77
Cdd:cd03538   15 MERLFGNAWiYVGHESQVPNPGDYITTRIGDQPVVMVRHTDGSVHVLYNRCPHKGTKI----VSDGCGNtgKFFRCPYHA 90

                         90
                 ....*....|....
gi 754524259  78 WRFGTaDGVCKQIP 91
Cdd:cd03538   91 WSFKT-DGSLLAIP 103
Rieske_RO_Alpha_DTDO cd03536
This alignment model represents the N-terminal rieske domain of the oxygenase alpha subunit ...
 9-82 2.71e-06

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: 46.08  E-value: 2.71e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 754524259   9 WYFAATSKEVTA-GKMFRREILGEPVVLGRDGQGRAFALRDICPHRAVplsagRVTETDG--VQTVECPYHGWRFGT 82
Cdd:cd03536    1 WVLLGHESEIPNkGDFMVRDMGSDSVIVARDKDGEIHVSLNVCPHRGM-----RISTTDGgnTQIHVCIYHGWAFRP 72
Rieske_RO_Alpha_HBDO cd03542
Rieske non-heme iron oxygenase (RO) family, 2-Halobenzoate 1,2-dioxygenase (HBDO) subfamily, ...
 9-80 2.74e-04

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: 40.12  E-value: 2.74e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 754524259   9 W-YFAATSKEVTAGKMFRREILGEPVVLGRDGQGRAFALRDICPHRAVPLsAGRVTETDGVQTveCPYHGWRF 80
Cdd:cd03542    1 WvYLAHESQIPNNNDYFTTTIGRQPVVITRDKDGELNAFINACSHRGAML-CRRKQGNKGTFT--CPFHGWTF 70
Rieske_T4moC cd03474
Toluene-4-monooxygenase effector protein complex (T4mo), Rieske ferredoxin subunit; The Rieske ...
 9-128 2.86e-04

Toluene-4-monooxygenase effector protein complex (T4mo), Rieske ferredoxin subunit; The Rieske domain is a [2Fe-2S] cluster binding domain involved in electron transfer. T4mo is a four-protein complex that catalyzes the NADH- and O2-dependent hydroxylation of toluene to form p-cresol. T4mo consists of an NADH oxidoreductase (T4moF), a diiron hydroxylase (T4moH), a catalytic effector protein (T4moD), and a Rieske ferredoxin (T4moC). T4moC contains a Rieske domain and functions as an obligate electron carrier between T4moF and T4moH. 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: 239556 [Multi-domain]  Cd Length: 108  Bit Score: 39.63  E-value: 2.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754524259   9 WYFAATSKEVTAGKMFRREILGEPVVLGRDGQGRAFALRDICPHRAVPLSAGRVtetDGvQTVECPYHGWRFgtadgvck 88
Cdd:cd03474    1 FTKVCSLDDVWEGEMELVDVDGEEVLLVAPEGGEFRAFQGICPHQEIPLAEGGF---DG-GVLTCRAHLWQF-------- 68

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 754524259  89 qipSLVEGQAYEASRIRVRHYPTHEANGIVLVFVSSDPRF 128
Cdd:cd03474   69 ---DADTGEGLNPRDCRLARYPVKVEGGDILVDTEGVLPL 105
Rieske_RO_Alpha_S5H cd03539
This alignment model represents the N-terminal rieske iron-sulfur domain of the oxygenase ...
 9-80 6.28e-04

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: 39.53  E-value: 6.28e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 754524259   9 WYFAATSKEVTAGKMFRREILGE-PVVLGRDGQGRAFALRDICPHRAVPLSAGRvteTDGVQTVECPYHGWRF 80
Cdd:cd03539    1 WCYVGLEAEIPNPGDFKRTLIGErSVIMTRDPDGGINVVENVCAHRGMRFCRER---NGNAKDFVCPYHQWNY 70
PRK09965 PRK09965
3-phenylpropionate dioxygenase ferredoxin subunit; Provisional
 41-123 1.67e-03

3-phenylpropionate dioxygenase ferredoxin subunit; Provisional


Pssm-ID: 170182 [Multi-domain]  Cd Length: 106  Bit Score: 37.45  E-value: 1.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754524259  41 GRAFALRDICPHRAVPLSAGRVtetDGVQTVECPYHGWRFGTADGVCKQIPslvegqayeaSRIRVRHYPTHEANGIVLV 120
Cdd:PRK09965  33 GEFYAIDDRCSHGNASLSEGYL---EDDATVECPLHAASFCLRTGKALCLP----------ATDPLRTYPVHVEGGDIFI 99


                 ...
gi 754524259 121 FVS 123
Cdd:PRK09965 100 DLP 102
 
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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