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Conserved domains on  [gi|1896924563|ref|WP_186869256|]
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MULTISPECIES: tRNA epoxyqueuosine(34) reductase QueG [Ornithinibacillus]

Protein Classification

epoxyqueuosine reductase( domain architecture ID 11489056)

epoxyqueuosine reductase catalyzes the conversion of epoxyqueuosine (oQ) to queuosine (Q), which is a hypermodified base found in the wobble positions of tRNA(Asp), tRNA(Asn), tRNA(His) and tRNA(Tyr)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TIGR00276 TIGR00276
epoxyqueuosine reductase; This model was rebuilt to exclude archaeal homologs, now that there ...
 10-344 0e+00

epoxyqueuosine reductase; This model was rebuilt to exclude archaeal homologs, now that there is new information that bacterial members are epoxyqueuosine reductase, QueG, involved in queuosine biosynthesis for tRNA maturation. [Protein synthesis, tRNA and rRNA base modification]


:

Pssm-ID: 272993 [Multi-domain]  Cd Length: 337  Bit Score: 541.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924563  10 IIDYSKEIGIDKIGFTTADVFTELKERLKRQQELGYQS--GFEKGTNEERTEPKRLLPGAQSIISIAMAYPSRMrKDAPK 87
Cdd:TIGR00276   1 IKAWAKELGFDKIGITDADLFPEEKERLLAWLEAGYHGemGFMARHGEKRARPAELLPGTRSVISVRMDYLPKL-APPAK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924563  88 SRKEERRGFFCRASWGMDYHDVLRDRLQKLERFIHEKVTDAVTKVMVDTGELSDRAVAERAGVGFTGKNTLLITEEFGSF 167
Cdd:TIGR00276  80 SLKDPERGYISRYALGRDYHKVLRKRLKKLAEFIEEEVGDFGYRVFVDTAPVLERALAERAGLGWIGKHTLLINREAGSW 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924563 168 VYLGELITNIPFIPDSPIEDGCGDCRKCIDACPTGAIVQGGQLNAQRCIAFLT-QTKDFLPEEFRSKLGNRVYGCDTCQL 246
Cdd:TIGR00276 160 FFLGEIFTNLPLPPDAPVTDHCGSCTACLDACPTGAIVAPYQLDARRCISYLTiELKGPIPEEFRPLIGNRIYGCDDCQL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924563 247 VCPKNQKVDFHHHPEFEPEDDIAKPLLKPMLTISNREFKEQFGHISGSWRGKKPIQRNAIIGLGHYKDKTAVDELISIMN 326
Cdd:TIGR00276 240 VCPWNKFADATHEPDFQPRHELDAPSLIELLAWDEAEFLERFGGSAIRRIGKKRWLRNAAVALGNAPGSPAIIEALEALL 319

                         330
                  ....*....|....*...
gi 1896924563 327 NDPRPVIRGTAAWSLGKI 344
Cdd:TIGR00276 320 DDPSPLVREHAAWALGQL 337
EZ_HEAT smart00567
E-Z type HEAT repeats; Present in subunits of cyanobacterial phycocyanin lyase, and other ...
 331-360 2.82e-04

E-Z type HEAT repeats; Present in subunits of cyanobacterial phycocyanin lyase, and other proteins. Probable scaffolding role.


:

Pssm-ID: 128837 [Multi-domain]  Cd Length: 30  Bit Score: 37.78  E-value: 2.82e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1896924563  331 PVIRGTAAWSLGKIGTEEAFDAITKAMEKE 360
Cdd:smart00567   1 PLVRHEAAFALGQLGDEEAVPALIKALEDE 30
 
Name Accession Description Interval E-value
TIGR00276 TIGR00276
epoxyqueuosine reductase; This model was rebuilt to exclude archaeal homologs, now that there ...
 10-344 0e+00

epoxyqueuosine reductase; This model was rebuilt to exclude archaeal homologs, now that there is new information that bacterial members are epoxyqueuosine reductase, QueG, involved in queuosine biosynthesis for tRNA maturation. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 272993 [Multi-domain]  Cd Length: 337  Bit Score: 541.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924563  10 IIDYSKEIGIDKIGFTTADVFTELKERLKRQQELGYQS--GFEKGTNEERTEPKRLLPGAQSIISIAMAYPSRMrKDAPK 87
Cdd:TIGR00276   1 IKAWAKELGFDKIGITDADLFPEEKERLLAWLEAGYHGemGFMARHGEKRARPAELLPGTRSVISVRMDYLPKL-APPAK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924563  88 SRKEERRGFFCRASWGMDYHDVLRDRLQKLERFIHEKVTDAVTKVMVDTGELSDRAVAERAGVGFTGKNTLLITEEFGSF 167
Cdd:TIGR00276  80 SLKDPERGYISRYALGRDYHKVLRKRLKKLAEFIEEEVGDFGYRVFVDTAPVLERALAERAGLGWIGKHTLLINREAGSW 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924563 168 VYLGELITNIPFIPDSPIEDGCGDCRKCIDACPTGAIVQGGQLNAQRCIAFLT-QTKDFLPEEFRSKLGNRVYGCDTCQL 246
Cdd:TIGR00276 160 FFLGEIFTNLPLPPDAPVTDHCGSCTACLDACPTGAIVAPYQLDARRCISYLTiELKGPIPEEFRPLIGNRIYGCDDCQL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924563 247 VCPKNQKVDFHHHPEFEPEDDIAKPLLKPMLTISNREFKEQFGHISGSWRGKKPIQRNAIIGLGHYKDKTAVDELISIMN 326
Cdd:TIGR00276 240 VCPWNKFADATHEPDFQPRHELDAPSLIELLAWDEAEFLERFGGSAIRRIGKKRWLRNAAVALGNAPGSPAIIEALEALL 319

                         330
                  ....*....|....*...
gi 1896924563 327 NDPRPVIRGTAAWSLGKI 344
Cdd:TIGR00276 320 DDPSPLVREHAAWALGQL 337
QueG COG1600
Epoxyqueuosine reductase QueG (queuosine biosynthesis) [Translation, ribosomal structure and ...
 2-348 5.61e-178

Epoxyqueuosine reductase QueG (queuosine biosynthesis) [Translation, ribosomal structure and biogenesis]; Epoxyqueuosine reductase QueG (queuosine biosynthesis) is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 441208 [Multi-domain]  Cd Length: 345  Bit Score: 498.19  E-value: 5.61e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924563   2 NTDQLKQEIIDYSKEIGIDKIGFTTADVFTELKERLKRQQELGY--QSGFEKGTNEERTEPKRLLPGAQSIISIAMAYPS 79
Cdd:COG1600     3 DLMELKEEIKAWARELGFDLVGIAPADPLPEAEERLEEWLAAGYhgEMGYMERHIEKRADPRELLPGAKSVISLALNYLP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924563  80 RMRKDAPksrkeeRRGFFCRASWGMDYHDVLRDRLQKLERFIHEKVTDAVTKVMVDTGELSDRAVAERAGVGFTGKNTLL 159
Cdd:COG1600    83 EEEVSDP------DRGKISRYAWGRDYHKVLRKRLKKLAEFLEEEGPGVGYRVFVDTAPVLERALAERAGLGWIGKNTNL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924563 160 ITEEFGSFVYLGELITNIPFIPDSPIEDGCGDCRKCIDACPTGAIVQGGQLNAQRCIAFLT-QTKDFLPEEFRSKLGNRV 238
Cdd:COG1600   157 ITPEFGSWFFLGEILTDLELPPDEPVEDHCGSCTRCLDACPTGAIVAPYVLDARRCISYLTiELKGPIPEELRPKMGNRI 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924563 239 YGCDTCQLVCPKNQKVDFHHHPEFEPEDDIAKPLLKPMLTISNREFKEQFGHISGSWRGKKPIQRNAIIGLGHYKDKTAV 318
Cdd:COG1600   237 YGCDDCQDVCPWNRFAQPTREPDFQPRPELAAPDLEELLALDEAEFRERFGGSAIRRIGRERLLRNAAIALGNSGDPAAV 316

                         330       340       350
                  ....*....|....*....|....*....|
gi 1896924563 319 DELISIMnNDPRPVIRGTAAWSLGKIGTEE 348
Cdd:COG1600   317 PALEALL-DDPSPLVREHAAWALGRLGGRE 345
QueG_DUF1730 pfam08331
Epoxyqueuosine reductase QueG, DUF1730; This domain of unknown function occurs in ...
 57-136 7.35e-30

Epoxyqueuosine reductase QueG, DUF1730; This domain of unknown function occurs in Epoxyqueuosine reductase QueG, an iron-sulfur cluster-binding protein, together with the 4Fe-4S binding domain (pfam00037). QueG catalyzes the conversion of epoxyqueuosine (oQ) to queuosine (Q), which is a hypermodified base found in the wobble positions of tRNA(Asp), tRNA(Asn), tRNA(His) and tRNA(Tyr).


Pssm-ID: 462431 [Multi-domain]  Cd Length: 77  Bit Score: 109.93  E-value: 7.35e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924563  57 RTEPKRLLPGAQSIISIAMAYPSRmrkDAPKSRKEERRGFFCRASWGMDYHDVLRDRLQKLERFIHEKVTDAVTKVMVDT 136
Cdd:pfam08331   1 RADPRLLLPGARSVISLALNYYPP---KDPPALLDPDRGKISRYAWGRDYHDVLKKRLKALAAWLEAEVPGGEYRVFVDT 77
HycB_like cd10554
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ...
 192-249 2.20e-06

HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a membrane-associated formate hydrogenlyase system (FHL-1) in Escherichia coli that breaks down formate, produced during anaerobic fermentation, to H2 and CO2. FHL-1 consists of formate dehydrogenase H (FDH-H) and the hydrogenase 3 complex (Hyd-3). HycB is thought to code for the [4Fe-4S] ferredoxin subunit of hydrogenase 3, which functions as an intermediate electron carrier protein between hydrogenase 3 and formate dehydrogenase. HydN codes for the [4Fe-4S] ferredoxin subunit of FDH-H; a hydN in-frame deletion mutation causes only weak reduction in hydrogenase activity, but loss of more than 60% of FDH-H activity. This pathway is only active at low pH and high formate concentrations, and is thought to provide a detoxification/de-acidification system countering the buildup of formate during fermentation.


Pssm-ID: 319876 [Multi-domain]  Cd Length: 149  Bit Score: 46.87  E-value: 2.20e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1896924563 192 CRKCIDA-----CPTGAIVQGG---QLNAQRCIafltqtkdflpeefrsklgnrvyGCDTCQLVCP 249
Cdd:cd10554    56 CRQCEDApcanvCPVGAISQEDgvvQVDEERCI-----------------------GCKLCVLACP 98
EZ_HEAT smart00567
E-Z type HEAT repeats; Present in subunits of cyanobacterial phycocyanin lyase, and other ...
 331-360 2.82e-04

E-Z type HEAT repeats; Present in subunits of cyanobacterial phycocyanin lyase, and other proteins. Probable scaffolding role.


Pssm-ID: 128837 [Multi-domain]  Cd Length: 30  Bit Score: 37.78  E-value: 2.82e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1896924563  331 PVIRGTAAWSLGKIGTEEAFDAITKAMEKE 360
Cdd:smart00567   1 PLVRHEAAFALGQLGDEEAVPALIKALEDE 30
PRK12769 PRK12769
putative oxidoreductase Fe-S binding subunit; Reviewed
 192-249 6.90e-04

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183733 [Multi-domain]  Cd Length: 654  Bit Score: 41.66  E-value: 6.90e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1896924563 192 CRKCIDA-----CPTGAIVQGG---QLNAQRCIafltqtkdflpeefrsklgnrvyGCDTCQLVCP 249
Cdd:PRK12769   56 CHHCEDApcarsCPNGAISHVDdsiQVNQQKCI-----------------------GCKSCVVACP 98
HEAT_PBS pfam03130
PBS lyase HEAT-like repeat; This family contains a short bi-helical repeat that is related to ...
 333-358 8.47e-04

PBS lyase HEAT-like repeat; This family contains a short bi-helical repeat that is related to pfam02985. Cyanobacteria and red algae harvest light energy using macromolecular complexes known as phycobilisomes (PBS), peripherally attached to the photosynthetic membrane. The major components of PBS are the phycobiliproteins. These heterodimeric proteins are covalently attached to phycobilins: open-chain tetrapyrrole chromophores, which function as the photosynthetic light-harvesting pigments. Phycobiliproteins differ in sequence and in the nature and number of attached phycobilins to each of their subunits. This family includes the lyase enzymes that specifically attach particular phycobilins to apophycobiliprotein subunits. The most comprehensively studied of these is the CpcE/F lyase, which attaches phycocyanobilin (PCB) to the alpha subunit of apophycocyanin. Similarly, MpeU/V attaches phycoerythrobilin to phycoerythrin II, while CpeY/Z is thought to be involved in phycoerythrobilin (PEB) attachment to phycoerythrin (PE) I (PEs I and II differ in sequence and in the number of attached molecules of PEB: PE I has five, PE II has six). All the reactions of the above lyases involve an apoprotein cysteine SH addition to a terminal delta 3,3'-double bond. Such a reaction is not possible in the case of phycoviolobilin (PVB), the phycobilin of alpha-phycoerythrocyanin (alpha-PEC). It is thought that in this case, PCB, not PVB, is first added to apo-alpha-PEC, and is then isomerized to PVB. The addition reaction has been shown to occur in the presence of either of the components of alpha-PEC-PVB lyase PecE or PecF (or both). The isomerization reaction occurs only when both PecE and PecF components are present, i.e. the PecE/F phycobiliprotein lyase is also a phycobilin isomerase. Another member of this family is the NblB protein, whose similarity to the phycobiliprotein lyases was previously noted. This constitutively expressed protein is not known to have any lyase activity. It is thought to be involved in the coordination of PBS degradation with environmental nutrient limitation. It has been suggested that the similarity of NblB to the phycobiliprotein lyases is due to the ability to bind tetrapyrrole phycobilins via the common repeated motif.


Pssm-ID: 308641 [Multi-domain]  Cd Length: 27  Bit Score: 36.30  E-value: 8.47e-04
                          10        20
                  ....*....|....*....|....*.
gi 1896924563 333 IRGTAAWSLGKIGTEEAFDAITKAME 358
Cdd:pfam03130   1 VRRAAARALGALGDPEAIPALIEALD 26
 
Name Accession Description Interval E-value
TIGR00276 TIGR00276
epoxyqueuosine reductase; This model was rebuilt to exclude archaeal homologs, now that there ...
 10-344 0e+00

epoxyqueuosine reductase; This model was rebuilt to exclude archaeal homologs, now that there is new information that bacterial members are epoxyqueuosine reductase, QueG, involved in queuosine biosynthesis for tRNA maturation. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 272993 [Multi-domain]  Cd Length: 337  Bit Score: 541.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924563  10 IIDYSKEIGIDKIGFTTADVFTELKERLKRQQELGYQS--GFEKGTNEERTEPKRLLPGAQSIISIAMAYPSRMrKDAPK 87
Cdd:TIGR00276   1 IKAWAKELGFDKIGITDADLFPEEKERLLAWLEAGYHGemGFMARHGEKRARPAELLPGTRSVISVRMDYLPKL-APPAK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924563  88 SRKEERRGFFCRASWGMDYHDVLRDRLQKLERFIHEKVTDAVTKVMVDTGELSDRAVAERAGVGFTGKNTLLITEEFGSF 167
Cdd:TIGR00276  80 SLKDPERGYISRYALGRDYHKVLRKRLKKLAEFIEEEVGDFGYRVFVDTAPVLERALAERAGLGWIGKHTLLINREAGSW 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924563 168 VYLGELITNIPFIPDSPIEDGCGDCRKCIDACPTGAIVQGGQLNAQRCIAFLT-QTKDFLPEEFRSKLGNRVYGCDTCQL 246
Cdd:TIGR00276 160 FFLGEIFTNLPLPPDAPVTDHCGSCTACLDACPTGAIVAPYQLDARRCISYLTiELKGPIPEEFRPLIGNRIYGCDDCQL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924563 247 VCPKNQKVDFHHHPEFEPEDDIAKPLLKPMLTISNREFKEQFGHISGSWRGKKPIQRNAIIGLGHYKDKTAVDELISIMN 326
Cdd:TIGR00276 240 VCPWNKFADATHEPDFQPRHELDAPSLIELLAWDEAEFLERFGGSAIRRIGKKRWLRNAAVALGNAPGSPAIIEALEALL 319

                         330
                  ....*....|....*...
gi 1896924563 327 NDPRPVIRGTAAWSLGKI 344
Cdd:TIGR00276 320 DDPSPLVREHAAWALGQL 337
QueG COG1600
Epoxyqueuosine reductase QueG (queuosine biosynthesis) [Translation, ribosomal structure and ...
 2-348 5.61e-178

Epoxyqueuosine reductase QueG (queuosine biosynthesis) [Translation, ribosomal structure and biogenesis]; Epoxyqueuosine reductase QueG (queuosine biosynthesis) is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 441208 [Multi-domain]  Cd Length: 345  Bit Score: 498.19  E-value: 5.61e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924563   2 NTDQLKQEIIDYSKEIGIDKIGFTTADVFTELKERLKRQQELGY--QSGFEKGTNEERTEPKRLLPGAQSIISIAMAYPS 79
Cdd:COG1600     3 DLMELKEEIKAWARELGFDLVGIAPADPLPEAEERLEEWLAAGYhgEMGYMERHIEKRADPRELLPGAKSVISLALNYLP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924563  80 RMRKDAPksrkeeRRGFFCRASWGMDYHDVLRDRLQKLERFIHEKVTDAVTKVMVDTGELSDRAVAERAGVGFTGKNTLL 159
Cdd:COG1600    83 EEEVSDP------DRGKISRYAWGRDYHKVLRKRLKKLAEFLEEEGPGVGYRVFVDTAPVLERALAERAGLGWIGKNTNL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924563 160 ITEEFGSFVYLGELITNIPFIPDSPIEDGCGDCRKCIDACPTGAIVQGGQLNAQRCIAFLT-QTKDFLPEEFRSKLGNRV 238
Cdd:COG1600   157 ITPEFGSWFFLGEILTDLELPPDEPVEDHCGSCTRCLDACPTGAIVAPYVLDARRCISYLTiELKGPIPEELRPKMGNRI 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924563 239 YGCDTCQLVCPKNQKVDFHHHPEFEPEDDIAKPLLKPMLTISNREFKEQFGHISGSWRGKKPIQRNAIIGLGHYKDKTAV 318
Cdd:COG1600   237 YGCDDCQDVCPWNRFAQPTREPDFQPRPELAAPDLEELLALDEAEFRERFGGSAIRRIGRERLLRNAAIALGNSGDPAAV 316

                         330       340       350
                  ....*....|....*....|....*....|
gi 1896924563 319 DELISIMnNDPRPVIRGTAAWSLGKIGTEE 348
Cdd:COG1600   317 PALEALL-DDPSPLVREHAAWALGRLGGRE 345
QueG_DUF1730 pfam08331
Epoxyqueuosine reductase QueG, DUF1730; This domain of unknown function occurs in ...
 57-136 7.35e-30

Epoxyqueuosine reductase QueG, DUF1730; This domain of unknown function occurs in Epoxyqueuosine reductase QueG, an iron-sulfur cluster-binding protein, together with the 4Fe-4S binding domain (pfam00037). QueG catalyzes the conversion of epoxyqueuosine (oQ) to queuosine (Q), which is a hypermodified base found in the wobble positions of tRNA(Asp), tRNA(Asn), tRNA(His) and tRNA(Tyr).


Pssm-ID: 462431 [Multi-domain]  Cd Length: 77  Bit Score: 109.93  E-value: 7.35e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924563  57 RTEPKRLLPGAQSIISIAMAYPSRmrkDAPKSRKEERRGFFCRASWGMDYHDVLRDRLQKLERFIHEKVTDAVTKVMVDT 136
Cdd:pfam08331   1 RADPRLLLPGARSVISLALNYYPP---KDPPALLDPDRGKISRYAWGRDYHDVLKKRLKALAAWLEAEVPGGEYRVFVDT 77
Fer4_16 pfam13484
4Fe-4S double cluster binding domain;
189-251 2.83e-26

4Fe-4S double cluster binding domain;


Pssm-ID: 463893 [Multi-domain]  Cd Length: 65  Bit Score: 99.87  E-value: 2.83e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1896924563 189 CGDCRKCIDACPTGAIVQG-GQLNAQRCIAFLT-QTKDFLPEEFRSKLGNRVYGCDTCQLVCPKN 251
Cdd:pfam13484   1 CGSCGKCIDACPTGAIVGPeGVLDARRCISYLTiEKKGLIPDELRCLLGNRCYGCDICQDVCPWN 65
HEAT_2 pfam13646
HEAT repeats; This family includes multiple HEAT repeats.
 301-374 1.43e-12

HEAT repeats; This family includes multiple HEAT repeats.


Pssm-ID: 433376 [Multi-domain]  Cd Length: 88  Bit Score: 62.74  E-value: 1.43e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1896924563 301 IQRNAIIGLGHYKDKTAVDELISIMNnDPRPVIRGTAAWSLGKIGTEEAFDAITKAMEKESDQDVLFEMEKGLA 374
Cdd:pfam13646  16 VRAAAIRALGRIGDPEAVPALLELLK-DEDPAVRRAAAEALGKIGDPEALPALLELLRDDDDDVVRAAAAEALA 88
RDH TIGR02486
reductive dehalogenase; This model represents a family of corrin and 8-iron Fe-S ...
 143-255 1.93e-09

reductive dehalogenase; This model represents a family of corrin and 8-iron Fe-S cluster-containing reductive dehalogenases found primarily in halorespiring microorganisms such as dehalococcoides ethenogenes which contains as many as 17 enzymes of this type with varying substrate ranges. One example of a characterized species is the tetrachloroethene reductive dehalogenase (1.97.1.8) which also acts on trichloroethene converting it to dichloroethene.


Pssm-ID: 274158  Cd Length: 314  Bit Score: 58.21  E-value: 1.93e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924563 143 AVAERAGVGFTGKN-TLLITEEFGSFVYLGELI-TNIPFIPDSPIEDG----CGDCRKCIDACPTGAIVQGG-------- 208
Cdd:TIGR02486 155 AFAVLAGLGEHGRMgQAIISPEYGPRVRIAKVIlTDLPLVPTKPIDAGmakfCETCGKCADECPSGAISKGGeptwdped 234

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1896924563 209 ---------------QLNAQRCIAFltqtkdflpeefrSKLGNRVYGCDTCQLVCPKNQKVD 255
Cdd:TIGR02486 235 sngdppgennpglkwQYDGWRCLLF-------------RCYNEGGGGCGVCQAVCPFNKKPN 283
HEAT COG1413
HEAT repeat [General function prediction only];
301-365 5.97e-09

HEAT repeat [General function prediction only];


Pssm-ID: 441023 [Multi-domain]  Cd Length: 137  Bit Score: 54.25  E-value: 5.97e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1896924563 301 IQRNAIIGLGHYKDKTAVDELISIMNnDPRPVIRGTAAWSLGKIGTEEAFDAITKAMeKESDQDV 365
Cdd:COG1413     1 VRRAAARALGRLGDPAAVPALIAALA-DEDPDVRAAAARALGRLGDPRAVPALLEAL-KDPDPEV 63
HEAT COG1413
HEAT repeat [General function prediction only];
301-362 1.12e-08

HEAT repeat [General function prediction only];


Pssm-ID: 441023 [Multi-domain]  Cd Length: 137  Bit Score: 53.09  E-value: 1.12e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1896924563 301 IQRNAIIGLGHYKDKTAVDELISIMNnDPRPVIRGTAAWSLGKIGTEEAFDAITKAMEKESD 362
Cdd:COG1413    32 VRAAAARALGRLGDPRAVPALLEALK-DPDPEVRAAAAEALGRIGDPEAVPALIAALKDEDP 92
HEAT COG1413
HEAT repeat [General function prediction only];
301-363 2.64e-08

HEAT repeat [General function prediction only];


Pssm-ID: 441023 [Multi-domain]  Cd Length: 137  Bit Score: 52.32  E-value: 2.64e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1896924563 301 IQRNAIIGLGHYKDKTAVDELISIMNnDPRPVIRGTAAWSLGKIGTEEAFDAITKAMEKESDQ 363
Cdd:COG1413    63 VRAAAAEALGRIGDPEAVPALIAALK-DEDPEVRRAAAEALGRLGDPAAVPALLEALKDPDWE 124
HycB_like cd10554
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ...
 192-249 2.20e-06

HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a membrane-associated formate hydrogenlyase system (FHL-1) in Escherichia coli that breaks down formate, produced during anaerobic fermentation, to H2 and CO2. FHL-1 consists of formate dehydrogenase H (FDH-H) and the hydrogenase 3 complex (Hyd-3). HycB is thought to code for the [4Fe-4S] ferredoxin subunit of hydrogenase 3, which functions as an intermediate electron carrier protein between hydrogenase 3 and formate dehydrogenase. HydN codes for the [4Fe-4S] ferredoxin subunit of FDH-H; a hydN in-frame deletion mutation causes only weak reduction in hydrogenase activity, but loss of more than 60% of FDH-H activity. This pathway is only active at low pH and high formate concentrations, and is thought to provide a detoxification/de-acidification system countering the buildup of formate during fermentation.


Pssm-ID: 319876 [Multi-domain]  Cd Length: 149  Bit Score: 46.87  E-value: 2.20e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1896924563 192 CRKCIDA-----CPTGAIVQGG---QLNAQRCIafltqtkdflpeefrsklgnrvyGCDTCQLVCP 249
Cdd:cd10554    56 CRQCEDApcanvCPVGAISQEDgvvQVDEERCI-----------------------GCKLCVLACP 98
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 189-251 7.39e-06

4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.


Pssm-ID: 463724 [Multi-domain]  Cd Length: 51  Bit Score: 42.90  E-value: 7.39e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1896924563 189 CGDCRKCIDACPTGAIVQGGQLNAQRciaflTQTKDFLPEEFrsklgnrvYGCDTCQLVCPKN 251
Cdd:pfam12838   1 CIGCGACVAACPVGAITLDEVGEKKG-----TKTVVIDPERC--------VGCGACVAVCPTG 50
HEAT_2 pfam13646
HEAT repeats; This family includes multiple HEAT repeats.
 318-361 9.20e-06

HEAT repeats; This family includes multiple HEAT repeats.


Pssm-ID: 433376 [Multi-domain]  Cd Length: 88  Bit Score: 43.48  E-value: 9.20e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1896924563 318 VDELISIMNNDPRPVIRGTAAWSLGKIGTEEAFDAITKAMEKES 361
Cdd:pfam13646   1 LPALLQALLRDPDPEVRAAAIRALGRIGDPEAVPALLELLKDED 44
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 186-251 9.48e-06

Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion transport and metabolism];


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 43.12  E-value: 9.48e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1896924563 186 EDGCGDCRKCIDACPTGAI-VQGGQL--NAQRCIafltqtkdflpeefrsklgnrvyGCDTCQLVCPKN 251
Cdd:COG2221    14 EEKCIGCGLCVAVCPTGAIsLDDGKLviDEEKCI-----------------------GCGACIRVCPTG 59
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
189-249 1.79e-05

Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 44.26  E-value: 1.79e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1896924563 189 CGDcRKCIDACPTGAIVQGG---QLNAQRCIafltqtkdflpeefrsklgnrvyGCDTCQLVCP 249
Cdd:COG1142    55 CED-APCAEVCPVGAITRDDgavVVDEEKCI-----------------------GCGLCVLACP 94
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
185-251 2.05e-05

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 42.41  E-value: 2.05e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924563 185 IEDGCGDCRKCIDACPTGAIVQGG---QLNAQRCIafltqtkdflpeefrsklgnrvyGCDTCQLVCPKN 251
Cdd:COG2768     9 DEEKCIGCGACVKVCPVGAISIEDgkaVIDPEKCI-----------------------GCGACIEVCPVG 55
HEAT COG1413
HEAT repeat [General function prediction only];
301-345 2.25e-05

HEAT repeat [General function prediction only];


Pssm-ID: 441023 [Multi-domain]  Cd Length: 137  Bit Score: 43.85  E-value: 2.25e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1896924563 301 IQRNAIIGLGHYKDKTAVDELISIMNnDPRPVIRGTAAWSLGKIG 345
Cdd:COG1413    94 VRRAAAEALGRLGDPAAVPALLEALK-DPDWEVRRAAARALGRLG 137
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 186-251 2.43e-05

MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function prediction only];


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 42.02  E-value: 2.43e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924563 186 EDGCGDCRKCIDACPTGAIVQGG----QLNAQRCIafltqtkdflpeefrsklgnrvyGCDTCQLVCPKN 251
Cdd:COG1149    10 EEKCIGCGLCVEVCPEGAIKLDDggapVVDPDLCT-----------------------GCGACVGVCPTG 56
RnfB COG2878
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ...
 186-251 1.72e-04

Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and conversion]; Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit is part of the Pathway/BioSystem: Na+-translocating Fd:NADH oxidoreductase


Pssm-ID: 442125 [Multi-domain]  Cd Length: 254  Bit Score: 42.67  E-value: 1.72e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1896924563 186 EDGCGDCRKCIDACPTGAIVqGG--QL---NAQRCIafltqtkdflpeefrsklgnrvyGCDTCQLVCPKN 251
Cdd:COG2878   136 EYGCIGCGDCIKACPFDAIV-GAakGMhtvDEDKCT-----------------------GCGLCVEACPVD 182
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 191-249 2.63e-04

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319895 [Multi-domain]  Cd Length: 154  Bit Score: 41.09  E-value: 2.63e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924563 191 DCRKCIDACPTGAI---------VQGG--QLNAQRCIAFLTQTkdflpeefrsklgnrvyGCDTCQLVCP 249
Cdd:cd16373    58 CCDACVEVCPTGALrpldleeqkVKMGvaVIDKDRCLAWQGGT-----------------DCGVCVEACP 110
EZ_HEAT smart00567
E-Z type HEAT repeats; Present in subunits of cyanobacterial phycocyanin lyase, and other ...
 331-360 2.82e-04

E-Z type HEAT repeats; Present in subunits of cyanobacterial phycocyanin lyase, and other proteins. Probable scaffolding role.


Pssm-ID: 128837 [Multi-domain]  Cd Length: 30  Bit Score: 37.78  E-value: 2.82e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1896924563  331 PVIRGTAAWSLGKIGTEEAFDAITKAMEKE 360
Cdd:smart00567   1 PLVRHEAAFALGQLGDEEAVPALIKALEDE 30
rnfB TIGR01944
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in ...
 186-251 2.93e-04

electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in Rhodobacter capsulatus encodes an apparent NADH oxidoreductase responsible for electron transport to nitrogenase, necessary for nitrogen fixation. A closely related complex in E. coli, RsxABCDGE (Reducer of SoxR), reduces the 2Fe-2S-containing superoxide sensor SoxR, active as a transcription factor when oxidized. This family of putative NADH oxidoreductase complexes exists in many of the same species as the related NQR, a Na(+)-translocating NADH-quinone reductase, but is distinct. This model describes the B subunit. [Energy metabolism, Electron transport]


Pssm-ID: 273887 [Multi-domain]  Cd Length: 165  Bit Score: 40.94  E-value: 2.93e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1896924563 186 EDGCGDCRKCIDACPTGAIVQGgqlnaqrciafltqtkdflPEEFRSKLGNRVYGCDTCQLVCPKN 251
Cdd:TIGR01944 112 EDNCIGCTKCIQACPVDAIVGA-------------------AKAMHTVIADECTGCDLCVEPCPTD 158
NapH COG0348
Polyferredoxin NapH [Energy production and conversion];
189-251 4.11e-04

Polyferredoxin NapH [Energy production and conversion];


Pssm-ID: 440117 [Multi-domain]  Cd Length: 263  Bit Score: 41.59  E-value: 4.11e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1896924563 189 CGDCRKCIDACPTGAIVQGGQLNAQRCIafltqtkdflpeefrsklgnrvyGCDTCQLVCPKN 251
Cdd:COG0348   212 CIDCGLCVKVCPMGIDIRKGEINQSECI-----------------------NCGRCIDACPKD 251
NapF COG1145
Ferredoxin [Energy production and conversion];
21-251 5.87e-04

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 41.25  E-value: 5.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924563  21 KIGFTTADVFTELKERLKRQQELGYQSGFEKGTNEERTEPKRLLPGAQSIISIAMAYPSRMRKDAPKSRKEERRGFFCRA 100
Cdd:COG1145     5 LDLKEALSPKLKVLYAVVTGILGKIILNVIAGALLKAVALGGLLPIIGILAKEAFDALKDVLGILGAIVIGIGAGEIVRV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924563 101 SWGMDYHDVLRDRLQKLERFIHEKVTDAVTKVMVDTGELSDRAVAERAGVGFTGKNTLLITEEFGS-----------FVY 169
Cdd:COG1145    85 GIAAADLNLKAVALVLLLALAVAGAAKRLIISAVKLVAGLVVAAGEVLLVIAAALAEAGLAILGAAapvdalaisggKKI 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924563 170 LGELITNIPFIPDSPIEDGCGDCRKCIDACPTGAIVQGG-----QLNAQRCIafltqtkdflpeefrsklgnrvyGCDTC 244
Cdd:COG1145   165 EEELKIAIKKAKAVIDAEKCIGCGLCVKVCPTGAIRLKDgkpqiVVDPDKCI-----------------------GCGAC 221


                  ....*..
gi 1896924563 245 QLVCPKN 251
Cdd:COG1145   222 VKVCPVG 228
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 186-251 6.16e-04

Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy production and conversion]; Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) is part of the Pathway/BioSystem: NADH dehydrogenase


Pssm-ID: 440758 [Multi-domain]  Cd Length: 66  Bit Score: 37.80  E-value: 6.16e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1896924563 186 EDGCGDCRKCIDACPTGAIVQGG-------QLNAQRCIafltqtkdflpeefrsklgnrvyGCDTCQLVCPKN 251
Cdd:COG1143     1 EDKCIGCGLCVRVCPVDAITIEDgepgkvyVIDPDKCI-----------------------GCGLCVEVCPTG 50
PRK12769 PRK12769
putative oxidoreductase Fe-S binding subunit; Reviewed
 192-249 6.90e-04

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183733 [Multi-domain]  Cd Length: 654  Bit Score: 41.66  E-value: 6.90e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1896924563 192 CRKCIDA-----CPTGAIVQGG---QLNAQRCIafltqtkdflpeefrsklgnrvyGCDTCQLVCP 249
Cdd:PRK12769   56 CHHCEDApcarsCPNGAISHVDdsiQVNQQKCI-----------------------GCKSCVVACP 98
HEAT_PBS pfam03130
PBS lyase HEAT-like repeat; This family contains a short bi-helical repeat that is related to ...
 333-358 8.47e-04

PBS lyase HEAT-like repeat; This family contains a short bi-helical repeat that is related to pfam02985. Cyanobacteria and red algae harvest light energy using macromolecular complexes known as phycobilisomes (PBS), peripherally attached to the photosynthetic membrane. The major components of PBS are the phycobiliproteins. These heterodimeric proteins are covalently attached to phycobilins: open-chain tetrapyrrole chromophores, which function as the photosynthetic light-harvesting pigments. Phycobiliproteins differ in sequence and in the nature and number of attached phycobilins to each of their subunits. This family includes the lyase enzymes that specifically attach particular phycobilins to apophycobiliprotein subunits. The most comprehensively studied of these is the CpcE/F lyase, which attaches phycocyanobilin (PCB) to the alpha subunit of apophycocyanin. Similarly, MpeU/V attaches phycoerythrobilin to phycoerythrin II, while CpeY/Z is thought to be involved in phycoerythrobilin (PEB) attachment to phycoerythrin (PE) I (PEs I and II differ in sequence and in the number of attached molecules of PEB: PE I has five, PE II has six). All the reactions of the above lyases involve an apoprotein cysteine SH addition to a terminal delta 3,3'-double bond. Such a reaction is not possible in the case of phycoviolobilin (PVB), the phycobilin of alpha-phycoerythrocyanin (alpha-PEC). It is thought that in this case, PCB, not PVB, is first added to apo-alpha-PEC, and is then isomerized to PVB. The addition reaction has been shown to occur in the presence of either of the components of alpha-PEC-PVB lyase PecE or PecF (or both). The isomerization reaction occurs only when both PecE and PecF components are present, i.e. the PecE/F phycobiliprotein lyase is also a phycobilin isomerase. Another member of this family is the NblB protein, whose similarity to the phycobiliprotein lyases was previously noted. This constitutively expressed protein is not known to have any lyase activity. It is thought to be involved in the coordination of PBS degradation with environmental nutrient limitation. It has been suggested that the similarity of NblB to the phycobiliprotein lyases is due to the ability to bind tetrapyrrole phycobilins via the common repeated motif.


Pssm-ID: 308641 [Multi-domain]  Cd Length: 27  Bit Score: 36.30  E-value: 8.47e-04
                          10        20
                  ....*....|....*....|....*.
gi 1896924563 333 IRGTAAWSLGKIGTEEAFDAITKAME 358
Cdd:pfam03130   1 VRRAAARALGALGDPEAIPALIEALD 26
NapF_like cd10564
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ...
 185-249 1.54e-03

NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, the iron-sulfur subunit of periplasmic nitrate reductase. The periplasmic nitrate reductase NapABC of Escherichia coli likely functions during anaerobic growth in low-nitrate environments; napF operon expression is activated by cyclic AMP receptor protein (Crp). NapF is a subfamily of the beta subunit of DMSO reductase (DMSOR) family. DMSOR family members have a large, periplasmic molybdenum-containing alpha subunit as well as a small beta FeS subunit, and may also have a small gamma subunit. The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319886 [Multi-domain]  Cd Length: 139  Bit Score: 38.38  E-value: 1.54e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1896924563 185 IEDGC-----GDCRKCIDACPTGAI----VQGG----QLNAQRCIafltqtkdflpeefrsklgnrvyGCDTCQLVCP 249
Cdd:cd10564    76 IGDSClalqgVECRSCQDACPTQAIrfrpRLGGialpELDADACT-----------------------GCGACVSVCP 130
PRK07569 PRK07569
bidirectional hydrogenase complex protein HoxU; Validated
 187-208 1.60e-03

bidirectional hydrogenase complex protein HoxU; Validated


Pssm-ID: 181037 [Multi-domain]  Cd Length: 234  Bit Score: 39.64  E-value: 1.60e-03
                          10        20
                  ....*....|....*....|..
gi 1896924563 187 DGCGDCRKCIDACPTGAIVQGG 208
Cdd:PRK07569  190 ETCTSCGKCVQACPTGAIFRKG 211
DMSOR_beta_like cd16374
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 167-269 2.09e-03

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319896 [Multi-domain]  Cd Length: 139  Bit Score: 38.02  E-value: 2.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924563 167 FVYLGELITNIPFipdspiedGCGDCRK--CIDACPTGAIVQGGQ----LNAQRCIafltqtkdflpeefrsklgnrvyG 240
Cdd:cd16374    29 SVEVVEDLASVPV--------RCRHCEDapCMEVCPTGAIYRDEDgavlVDPDKCI-----------------------G 77

                          90       100
                  ....*....|....*....|....*....
gi 1896924563 241 CDTCQLVCPknqkvdFhHHPEFEPEDDIA 269
Cdd:cd16374    78 CGMCAMACP------F-GVPRFDPSLKVA 99
DMSOR_beta-like cd04410
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ...
 186-215 2.23e-03

Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319870 [Multi-domain]  Cd Length: 136  Bit Score: 38.14  E-value: 2.23e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1896924563 186 EDGCGDCRKCIDACPTGAIVQGGQLN-AQRC 215
Cdd:cd04410    79 EDKCIGCGSCVEACPYGAIVFDPEPGkAVKC 109
Fer4 pfam00037
4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to ...
 185-204 4.70e-03

4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich.


Pssm-ID: 459642 [Multi-domain]  Cd Length: 24  Bit Score: 34.15  E-value: 4.70e-03
                          10        20
                  ....*....|....*....|
gi 1896924563 185 IEDGCGDCRKCIDACPTGAI 204
Cdd:pfam00037   4 DEEKCIGCGACVEVCPVGAI 23
DMSOR_beta-like cd04410
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ...
 194-269 4.74e-03

Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319870 [Multi-domain]  Cd Length: 136  Bit Score: 36.98  E-value: 4.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924563 194 KCIDACPTGAIVQ--GG--QLNAQRCIafltqtkdflpeefrsklgnrvyGCDTCQLVCPknqkvdfHHHPEFEPEDDIA 269
Cdd:cd04410    57 PCVKACPTGAIYKdeDGivLIDEDKCI-----------------------GCGSCVEACP-------YGAIVFDPEPGKA 106
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 185-251 5.36e-03

TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and conversion];


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 35.40  E-value: 5.36e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924563 185 IEDGCGDCRKCIDACPTGAIVQGG---QLNAQRCIafltqtkdflpeefrsklgnrvyGCDTCQLVCPKN 251
Cdd:COG4231    20 DEDKCTGCGACVKVCPADAIEEGDgkaVIDPDLCI-----------------------GCGSCVQVCPVD 66
Fer4_6 pfam12837
4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to ...
 189-204 6.71e-03

4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich.


Pssm-ID: 432822 [Multi-domain]  Cd Length: 24  Bit Score: 33.74  E-value: 6.71e-03
                          10
                  ....*....|....*.
gi 1896924563 189 CGDCRKCIDACPTGAI 204
Cdd:pfam12837   9 CIGCGRCVVVCPYGAI 24
PRK08348 PRK08348
NADH-plastoquinone oxidoreductase subunit; Provisional
 187-250 7.07e-03

NADH-plastoquinone oxidoreductase subunit; Provisional


Pssm-ID: 181399 [Multi-domain]  Cd Length: 120  Bit Score: 36.35  E-value: 7.07e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1896924563 187 DGCGDCRKCIDACPTGAIVqggQLNAQRCIAFLTqtkdflpeefrsklGNRVYgCDTCQLVCPK 250
Cdd:PRK08348   42 DKCVGCRMCVTVCPAGVFV---YLPEIRKVALWT--------------GRCVF-CGQCVDVCPT 87
 
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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