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Conserved domains on  [gi|498232607|ref|WP_010546763|]
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hypothetical protein [Halobiforma lacisalsi]

Protein Classification

beta-propeller fold lactonase family protein( domain architecture ID 1009710)

beta-propeller fold lactonase family protein similar to hydrazine synthase beta subunit from Candidatus Kuenenia stuttgartiensis, a component of the hydrazine synthase complex that catalyzes the condensation of nitric oxide (NO) with ammonium to form hydrazine

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PQQ_ABC_repeats super family cl37339
PQQ-dependent catabolism-associated beta-propeller protein; Members of this protein family ...
 45-290 2.92e-31

PQQ-dependent catabolism-associated beta-propeller protein; Members of this protein family consist of seven repeats each of the YVTN family beta-propeller repeat (see TIGR02276). Members occur invariably as part of a transport operon that is associated with PQQ-dependent catabolism of alcohols such as phenylethanol.


The actual alignment was detected with superfamily member TIGR03866:

Pssm-ID: 274824 [Multi-domain]  Cd Length: 310  Bit Score: 118.60  E-value: 2.92e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607   45 EKAYVTCSLGDTLLAFDTETWERTAEIEHEgfDFPHGLAIRERAGELWLASTYSSRVYVIDLESDEILTDFPTHQDkSHM 124
Cdd:TIGR03866  11 ETAYVSNEKDNTISVIDTATLKVTRTFPVG--QRPRGITFSKDGKLLYVCASDSDTIQVIDPATGEVLHTLPSGPD-PEQ 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607  125 VALTPDEERAFVANIGSGNVTAIDCEERRILADPEVGEEPEGIEVHPEAGLLVANQE-DGMLSVLDPETLEKTGRALLGE 203
Cdd:TIGR03866  88 FALHPNGKILYIANEDDALVTVIDIETRKVLAQIDVGVEPEGMAVSPDGKIVVNTSEtTNMAHWIDTATYEIVDNTLVDA 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607  204 TPIRVVSSPDGRHVLVPNRESNDVSLIDTEHVRDGERQPWEIARI-PVGIWPGGTVFAPDGNRAFVANNKTNDVSVIDCE 282
Cdd:TIGR03866 168 RPRFAEFTADGKELWVSSEIGGTVTVIDVATRKVIKKITFAIPGVhPEKVQPVGIKLTKDGKTAFVALGPANRVAVVDAK 247


                  ....*...
gi 498232607  283 TWtETERY 290
Cdd:TIGR03866 248 TY-EVLDY 254
 
Name Accession Description Interval E-value
PQQ_ABC_repeats TIGR03866
PQQ-dependent catabolism-associated beta-propeller protein; Members of this protein family ...
 45-290 2.92e-31

PQQ-dependent catabolism-associated beta-propeller protein; Members of this protein family consist of seven repeats each of the YVTN family beta-propeller repeat (see TIGR02276). Members occur invariably as part of a transport operon that is associated with PQQ-dependent catabolism of alcohols such as phenylethanol.


Pssm-ID: 274824 [Multi-domain]  Cd Length: 310  Bit Score: 118.60  E-value: 2.92e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607   45 EKAYVTCSLGDTLLAFDTETWERTAEIEHEgfDFPHGLAIRERAGELWLASTYSSRVYVIDLESDEILTDFPTHQDkSHM 124
Cdd:TIGR03866  11 ETAYVSNEKDNTISVIDTATLKVTRTFPVG--QRPRGITFSKDGKLLYVCASDSDTIQVIDPATGEVLHTLPSGPD-PEQ 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607  125 VALTPDEERAFVANIGSGNVTAIDCEERRILADPEVGEEPEGIEVHPEAGLLVANQE-DGMLSVLDPETLEKTGRALLGE 203
Cdd:TIGR03866  88 FALHPNGKILYIANEDDALVTVIDIETRKVLAQIDVGVEPEGMAVSPDGKIVVNTSEtTNMAHWIDTATYEIVDNTLVDA 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607  204 TPIRVVSSPDGRHVLVPNRESNDVSLIDTEHVRDGERQPWEIARI-PVGIWPGGTVFAPDGNRAFVANNKTNDVSVIDCE 282
Cdd:TIGR03866 168 RPRFAEFTADGKELWVSSEIGGTVTVIDVATRKVIKKITFAIPGVhPEKVQPVGIKLTKDGKTAFVALGPANRVAVVDAK 247


                  ....*...
gi 498232607  283 TWtETERY 290
Cdd:TIGR03866 248 TY-EVLDY 254
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
42-233 5.83e-28

DNA-binding beta-propeller fold protein YncE [General function prediction only];


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 108.24  E-value: 5.83e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607  42 PDGEKAYVTCSLGDTLLAFDTETWERTAEIEHEGfdFPHGLAIRERAGELWLASTYSSRVYVIDLESDEILTDFPTHqDK 121
Cdd:COG3391   77 ADGRRLYVANSGSGRVSVIDLATGKVVATIPVGG--GPRGLAVDPDGGRLYVADSGNGRVSVIDTATGKVVATIPVG-AG 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607 122 SHMVALTPDEERAFVANIGSGNVTAIdceerriladpevgeepegievhpeagllvanqedgmLSVLDPETLEKTGRALL 201
Cdd:COG3391  154 PHGIAVDPDGKRLYVANSGSNTVSVI-------------------------------------VSVIDTATGKVVATIPV 196

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 498232607 202 GETPIRVVSSPDGRHVLVPNRESN-------DVSLIDTE 233
Cdd:COG3391  197 GGGPVGVAVSPDGRRLYVANRGSNtsnggsnTVSVIDLA 235
Lactonase pfam10282
Lactonase, 7-bladed beta-propeller; This entry contains bacterial 6-phosphogluconolactonases ...
 5-283 9.19e-10

Lactonase, 7-bladed beta-propeller; This entry contains bacterial 6-phosphogluconolactonases (6PGL)YbhE-type (EC:3.1.1.31) which hydrolyse 6-phosphogluconolactone to 6-phosphogluconate. The entry also contains the fungal muconate lactonising enzyme carboxy-cis,cis-muconate cyclase (EC:5.5.1.5) and muconate cycloisomerase (EC:5.5.1.1), which convert cis,cis-muconates to muconolactones and vice versa as part of the microbial beta-ketoadipate pathway. Structures of proteins in this family have revealed a 7-bladed beta-propeller fold.


Pssm-ID: 431196 [Multi-domain]  Cd Length: 340  Bit Score: 58.77  E-value: 9.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607    5 LLVLNKDSDTmsvidAEAGDTETVVETEfNPHEIAVTPDGEKAYVTCSLGDT--LLAF----DTETWERTAEIEHEGFDF 78
Cdd:pfam10282  15 IYVLTLDTET-----GALTLLGLVAEVG-NPSYLALSPDGRTLYAVNEEGDQggVAAFridpDSGALTLLNQVPTGGASP 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607   79 PHgLAIrERAGELWLASTYSS---RVYVIDLESD-EILTDFPTH---------QDKS--HMVALTPDEERAFVANIGSGN 143
Cdd:pfam10282  89 CH-LSV-DPDGRFLFVANYHGgsvSVFPLDADGSlGELSQVVQHegsgppperQESPhpHSVDLTPDGKFLVVPDLGTDR 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607  144 VT--AIDcEERRILADPEVGEEPEG-----IEVHPEAGLL-VANQEDGMLSVLD-----------------PETLEKTGR 198
Cdd:pfam10282 167 VRvyKLD-AGGGKLTPPASVQTPPGsgprhLAFHPNGKYAyVVNELSSTVTVFEydpatgtfeelqtvstlPEGFTGTNG 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607  199 AllGEtpIRVvsSPDGRHVLVPNRESNDVSLIDtehVRDGERQPWEIARIPV-GIWPGGTVFAPDGNRAFVANNKTNDVS 277
Cdd:pfam10282 246 A--AA--IRV--SPDGKFLYVSNRGHDSIAVFA---VDEAGGTLTLVERVSTeGDFPRDFNIDPDGKFLVVANQDSDNVT 316


                  ....*...
gi 498232607  278 V--IDCET 283
Cdd:pfam10282 317 VfrRDPET 324
8prop_heme_binding_protein cd20718
eight-bladed beta-propeller heme-binding domain in cytochrome cd1 and similar proteins; ...
 98-304 1.76e-08

eight-bladed beta-propeller heme-binding domain in cytochrome cd1 and similar proteins; Members here contain an 8-bladed beta-propeller heme-binding domain in cytochrome cd1 (nitrite reductase) and similar proteins including NirN and NirF. During denitrification, nitrate (Nar), nitrite (Nir), nitric oxide (Nor), and nitrous oxide (Nos) reductases catalyze the reaction cascade of NO(3-)-> NO(2-)-> NO -> N2O -> N2. The integral membrane proteins NorC, NorB, and NosR form the core assembly platform that binds the nitrate reductase NarGHI and the periplasmic nitrite reductase NirS via its maturation factor NirF. NirN and NirF form a stable complex with the nitrite reductase NirS during enzyme maturation. NirF is involved in heme d1 insertion.


Pssm-ID: 467720 [Multi-domain]  Cd Length: 380  Bit Score: 55.04  E-value: 1.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607  98 SSRVYVIDLESDEILTDFPTHQDKSHMVALTPDEERAFVanIG-SGNVTAIDCEERRILADPEVGEEPEGIEVHPEAGLL 176
Cdd:cd20718   37 AGSVLVIDGSTHEVLGRIDDGGAQVHVVVFSPDGRFAYV--ISrDGWLTKIDLYTLRPVASIRIGVNSRGIALSDDGKYV 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607 177 VA-NQEDGMLSVLDPETLE--KT--GRALLGETPIR-----VVSSPDGRHVLVPNRESNDVSLIDTehvRDGERQP-WEI 245
Cdd:cd20718  115 IAgNYEPGHVVILDADTLEplKVipTTGVNDDGIIEsrvgaILETPPGPYFLVALKDAGSVWVIDY---SDPDGNKvTDI 191

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498232607 246 arIPVGIWPGGTVFAPDGNRAFVANNKTNDVSVIDCETWTETERYGTEL--HPDGIAYLER 304
Cdd:cd20718  192 --GNIGRPLHDAFLDPDGRYFIVASQGSNTMWVLDLKTGKVVARIPTGKtpHPGPGATWGR 250
 
Name Accession Description Interval E-value
PQQ_ABC_repeats TIGR03866
PQQ-dependent catabolism-associated beta-propeller protein; Members of this protein family ...
 45-290 2.92e-31

PQQ-dependent catabolism-associated beta-propeller protein; Members of this protein family consist of seven repeats each of the YVTN family beta-propeller repeat (see TIGR02276). Members occur invariably as part of a transport operon that is associated with PQQ-dependent catabolism of alcohols such as phenylethanol.


Pssm-ID: 274824 [Multi-domain]  Cd Length: 310  Bit Score: 118.60  E-value: 2.92e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607   45 EKAYVTCSLGDTLLAFDTETWERTAEIEHEgfDFPHGLAIRERAGELWLASTYSSRVYVIDLESDEILTDFPTHQDkSHM 124
Cdd:TIGR03866  11 ETAYVSNEKDNTISVIDTATLKVTRTFPVG--QRPRGITFSKDGKLLYVCASDSDTIQVIDPATGEVLHTLPSGPD-PEQ 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607  125 VALTPDEERAFVANIGSGNVTAIDCEERRILADPEVGEEPEGIEVHPEAGLLVANQE-DGMLSVLDPETLEKTGRALLGE 203
Cdd:TIGR03866  88 FALHPNGKILYIANEDDALVTVIDIETRKVLAQIDVGVEPEGMAVSPDGKIVVNTSEtTNMAHWIDTATYEIVDNTLVDA 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607  204 TPIRVVSSPDGRHVLVPNRESNDVSLIDTEHVRDGERQPWEIARI-PVGIWPGGTVFAPDGNRAFVANNKTNDVSVIDCE 282
Cdd:TIGR03866 168 RPRFAEFTADGKELWVSSEIGGTVTVIDVATRKVIKKITFAIPGVhPEKVQPVGIKLTKDGKTAFVALGPANRVAVVDAK 247


                  ....*...
gi 498232607  283 TWtETERY 290
Cdd:TIGR03866 248 TY-EVLDY 254
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
42-233 5.83e-28

DNA-binding beta-propeller fold protein YncE [General function prediction only];


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 108.24  E-value: 5.83e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607  42 PDGEKAYVTCSLGDTLLAFDTETWERTAEIEHEGfdFPHGLAIRERAGELWLASTYSSRVYVIDLESDEILTDFPTHqDK 121
Cdd:COG3391   77 ADGRRLYVANSGSGRVSVIDLATGKVVATIPVGG--GPRGLAVDPDGGRLYVADSGNGRVSVIDTATGKVVATIPVG-AG 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607 122 SHMVALTPDEERAFVANIGSGNVTAIdceerriladpevgeepegievhpeagllvanqedgmLSVLDPETLEKTGRALL 201
Cdd:COG3391  154 PHGIAVDPDGKRLYVANSGSNTVSVI-------------------------------------VSVIDTATGKVVATIPV 196

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 498232607 202 GETPIRVVSSPDGRHVLVPNRESN-------DVSLIDTE 233
Cdd:COG3391  197 GGGPVGVAVSPDGRRLYVANRGSNtsnggsnTVSVIDLA 235
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
129-284 1.60e-27

DNA-binding beta-propeller fold protein YncE [General function prediction only];


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 107.09  E-value: 1.60e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607 129 PDEERAFVANIGSGNVTAIDCEERRILADPEVGEEPEGIEVHPEAG-LLVANQEDGMLSVLDPETLEKTGRALLGETPIR 207
Cdd:COG3391   77 ADGRRLYVANSGSGRVSVIDLATGKVVATIPVGGGPRGLAVDPDGGrLYVADSGNGRVSVIDTATGKVVATIPVGAGPHG 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607 208 VVSSPDGRHVLVPNRESNDVSLI----DTEhvrDGErqpwEIARIPVGIWPGGTVFAPDGNRAFVAN---NKTN----DV 276
Cdd:COG3391  157 IAVDPDGKRLYVANSGSNTVSVIvsviDTA---TGK----VVATIPVGGGPVGVAVSPDGRRLYVANrgsNTSNggsnTV 229


                 ....*...
gi 498232607 277 SVIDCETW 284
Cdd:COG3391  230 SVIDLATL 237
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
3-148 1.74e-24

DNA-binding beta-propeller fold protein YncE [General function prediction only];


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 99.00  E-value: 1.74e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607   3 DRLLVLNKDSDTMSVIDAEAGDTETVVETEFNPHEIAVTPDGEKAYVTCSLGDTLLAFDTETWERTAEIEHEgfDFPHGL 82
Cdd:COG3391   80 RRLYVANSGSGRVSVIDLATGKVVATIPVGGGPRGLAVDPDGGRLYVADSGNGRVSVIDTATGKVVATIPVG--AGPHGI 157

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607  83 AIRERAGELWLASTYSSR----VYVIDLESDEILTDFPTHQDkSHMVALTPDEERAFVANIGSGNVTAID 148
Cdd:COG3391  158 AVDPDGKRLYVANSGSNTvsviVSVIDTATGKVVATIPVGGG-PVGVAVSPDGRRLYVANRGSNTSNGGS 226
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
175-301 3.47e-24

DNA-binding beta-propeller fold protein YncE [General function prediction only];


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 98.23  E-value: 3.47e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607 175 LLVANQEDGMLSVLDPETLEKTGRALLGETPIRVVSSPDGRHVLVPNRESNDVSLIDTEhvrDGErqpwEIARIPVGIWP 254
Cdd:COG3391   82 LYVANSGSGRVSVIDLATGKVVATIPVGGGPRGLAVDPDGGRLYVADSGNGRVSVIDTA---TGK----VVATIPVGAGP 154

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 498232607 255 GGTVFAPDGNRAFVANNKTND----VSVIDCETWTETERYGTELHPDGIAY 301
Cdd:COG3391  155 HGIAVDPDGKRLYVANSGSNTvsviVSVIDTATGKVVATIPVGGGPVGVAV 205
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
25-283 2.96e-17

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 79.68  E-value: 2.96e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607  25 TETVVETEFN-PHEIAVTPDGEkAYVTCSLGDTLLAFDTETwERTAEIEHEGFDFPHGLAIrERAGELWLASTYSSRVYV 103
Cdd:COG4257    8 TEYPVPAPGSgPRDVAVDPDGA-VWFTDQGGGRIGRLDPAT-GEFTEYPLGGGSGPHGIAV-DPDGNLWFTDNGNNRIGR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607 104 IDLESDEILT-DFPTHQDKSHMVALTPDeERAFVANIGSGNVTAIDCEERRILAD--PEVGEEPEGIEVHPEAGLLVANQ 180
Cdd:COG4257   85 IDPKTGEITTfALPGGGSNPHGIAFDPD-GNLWFTDQGGNRIGRLDPATGEVTEFplPTGGAGPYGIAVDPDGNLWVTDF 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607 181 EDGMLSVLDPETLEKTGRAL--LGETPIRVVSSPDGRhVLVPNRESNDVSLIDTEhvrDGERQpwEIARIPVGIWPGGTV 258
Cdd:COG4257  164 GANAIGRIDPDTGTLTEYALptPGAGPRGLAVDPDGN-LWVADTGSGRIGRFDPK---TGTVT--EYPLPGGGARPYGVA 237

                        250       260
                 ....*....|....*....|....*
gi 498232607 259 FAPDGnRAFVANNKTNDVSVIDCET 283
Cdd:COG4257  238 VDGDG-RVWFAESGANRIVRFDPDT 261
Pgl COG2706
6-phosphogluconolactonase, cycloisomerase 2 family [Carbohydrate transport and metabolism];
9-283 9.73e-16

6-phosphogluconolactonase, cycloisomerase 2 family [Carbohydrate transport and metabolism];


Pssm-ID: 442025 [Multi-domain]  Cd Length: 352  Bit Score: 76.48  E-value: 9.73e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607   9 NKDSDTMSV--IDAEAGD---TETVVETEfNPHEIAVTPDGEKAYVTCSLGD-TLLAFDTETWERT-AEIEH--EGFDFP 79
Cdd:COG2706   17 SGESEGIYVfrLDTATGEltlLGLVAALG-NPSFLALSPDGRFLYAVNEVDDgGVSAFRIDPADGTlTLLNTvsSGGASP 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607  80 HGLAIRERAGELWLASTYSSRVYVIDLESDEILTD------------FPTHQDKS--HMVALTPDEERAFVANIGSGNVT 145
Cdd:COG2706   96 CHLSVDPDGRFLFVANYGGGSVSVFPIDADGSLGEpvqviqhegsgpNPERQEGPhaHSVVFDPDGRFLYVPDLGTDRIY 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607 146 --AIDCEERRILADPEV----GEEPEGIEVHPEAGLL-VANQEDGMLSVLDPEtlEKTGRAllgeTPIRVVS-------- 210
Cdd:COG2706  176 vyRLDPATGKLPEPPEVslppGSGPRHLAFHPNGRFAyVINELDSTVSVYAYD--AATGTL----TLIQTVStlpedftg 249

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607 211 ---------SPDGRHVLVPNRESNDVSL--IDTEhvrDGERQPweIARIPV-GIWPGGTVFAPDGNRAFVANNKTNDVSV 278
Cdd:COG2706  250 enwaadihiSPDGRFLYVSNRGHNSIAVfaIDAD---GGKLTL--VGHVPTgGKWPRDFAIDPDGRFLLVANQKSDNITV 324


                 ....*..
gi 498232607 279 --IDCET 283
Cdd:COG2706  325 frIDADT 331
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
3-233 1.68e-15

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 74.67  E-value: 1.68e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607   3 DRLLVLNKDSDTMSVIDAEAGDTETVVETEFN-PHEIAVTPDGeKAYVTCSLGDTLLAFDTETwERTAEIEH-EGFDFPH 80
Cdd:COG4257   28 GAVWFTDQGGGRIGRLDPATGEFTEYPLGGGSgPHGIAVDPDG-NLWFTDNGNNRIGRIDPKT-GEITTFALpGGGSNPH 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607  81 GLAIrERAGELWLASTYSSRVYVIDLESDEILT-DFPTHQDKSHMVALTPDeERAFVANIGSGNVTAIDCE--ERRILAD 157
Cdd:COG4257  106 GIAF-DPDGNLWFTDQGGNRIGRLDPATGEVTEfPLPTGGAGPYGIAVDPD-GNLWVTDFGANAIGRIDPDtgTLTEYAL 183

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498232607 158 PEVGEEPEGIEVHPEAGLLVANQEDGMLSVLDPETLEKTGRALLGET--PIRVVSSPDGRhVLVPNRESNDVSLIDTE 233
Cdd:COG4257  184 PTPGAGPRGLAVDPDGNLWVADTGSGRIGRFDPKTGTVTEYPLPGGGarPYGVAVDGDGR-VWFAESGANRIVRFDPD 260
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
197-301 4.18e-14

DNA-binding beta-propeller fold protein YncE [General function prediction only];


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 70.49  E-value: 4.18e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607 197 GRALLGETPIRVVSSPDGRHVLVPNRESNDVSLIDTEhvrDGErqpwEIARIPVGIWPGGTVFAPDGNRAFVANNKTNDV 276
Cdd:COG3391   62 LGAAAVADADGADAGADGRRLYVANSGSGRVSVIDLA---TGK----VVATIPVGGGPRGLAVDPDGGRLYVADSGNGRV 134

                         90       100
                 ....*....|....*....|....*
gi 498232607 277 SVIDCETWTETERYGTELHPDGIAY 301
Cdd:COG3391  135 SVIDTATGKVVATIPVGAGPHGIAV 159
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
18-192 4.63e-13

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 67.74  E-value: 4.63e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607  18 IDAEAGDTETVV--ETEFNPHEIAVTPDGeKAYVTCSLGDTLLAFDTETWERTAEIEHEGFDFPHGLAIrERAGELWLAS 95
Cdd:COG4257   85 IDPKTGEITTFAlpGGGSNPHGIAFDPDG-NLWFTDQGGNRIGRLDPATGEVTEFPLPTGGAGPYGIAV-DPDGNLWVTD 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607  96 TYSSRVYVIDLESDEIlTDFPTHQDKSHMVALTPDEE-RAFVANIGSGNVTAIDCEERRI--LADPEVGEEPEGIEVHPE 172
Cdd:COG4257  163 FGANAIGRIDPDTGTL-TEYALPTPGAGPRGLAVDPDgNLWVADTGSGRIGRFDPKTGTVteYPLPGGGARPYGVAVDGD 241

                        170       180
                 ....*....|....*....|
gi 498232607 173 AGLLVANQEDGMLSVLDPET 192
Cdd:COG4257  242 GRVWFAESGANRIVRFDPDT 261
PQQ_ABC_repeats TIGR03866
PQQ-dependent catabolism-associated beta-propeller protein; Members of this protein family ...
 35-171 2.10e-10

PQQ-dependent catabolism-associated beta-propeller protein; Members of this protein family consist of seven repeats each of the YVTN family beta-propeller repeat (see TIGR02276). Members occur invariably as part of a transport operon that is associated with PQQ-dependent catabolism of alcohols such as phenylethanol.


Pssm-ID: 274824 [Multi-domain]  Cd Length: 310  Bit Score: 60.44  E-value: 2.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607   35 PHEIAVTPDGEKAYVTCSLGDTLLAFDTETWERTAEIEhegFDF---------PHGLAIRERAGELWLASTYSSRVYVID 105
Cdd:TIGR03866 169 PRFAEFTADGKELWVSSEIGGTVTVIDVATRKVIKKIT---FAIpgvhpekvqPVGIKLTKDGKTAFVALGPANRVAVVD 245

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498232607  106 LESDEILTDFPTHQDKSHMvALTPDEERAFVANIGSGNVTAIDCEERRILADPEVGEEPEGIEVHP 171
Cdd:TIGR03866 246 AKTYEVLDYLLVGQRVWQL-AFTPDESRLLTTNGVSNDVSVIDVAALKVIKSIKVGRLPWGVVVRP 310
YvrE COG3386
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase ...
 3-219 3.98e-10

Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase YvrE is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 442613 [Multi-domain]  Cd Length: 266  Bit Score: 59.14  E-value: 3.98e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607   3 DRLLVLNKDSDTMSVIDAEAGDTETVVETEFNPHEIAVTPDGEkaYVTCSLGDTLLAFDTETWERT--AEIEHEGFDFPH 80
Cdd:COG3386   19 GRLYWVDIPGGRIHRYDPDGGAVEVFAEPSGRPNGLAFDPDGR--LLVADHGRGLVRFDPADGEVTvlADEYGKPLNRPN 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607  81 GLAIReRAGELWLASTY----SSRVYVI--DLESDEILTDFPThqdkSHMVALTPDEERAFVANIGSGNVTAIDCEE--- 151
Cdd:COG3386   97 DGVVD-PDGRLYFTDMGeylpTGALYRVdpDGSLRVLADGLTF----PNGIAFSPDGRTLYVADTGAGRIYRFDLDAdgt 171

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498232607 152 ---RRILADPEVGE-EPEGIEVHPEAGLLVANQEDGMLSVLDPetlekTGRaLLG--ETPIRVVSS-----PDGRHVLV 219
Cdd:COG3386  172 lgnRRVFADLPDGPgGPDGLAVDADGNLWVALWGGGGVVRFDP-----DGE-LLGriELPERRPTNvafggPDLRTLYV 244
Lactonase pfam10282
Lactonase, 7-bladed beta-propeller; This entry contains bacterial 6-phosphogluconolactonases ...
 5-283 9.19e-10

Lactonase, 7-bladed beta-propeller; This entry contains bacterial 6-phosphogluconolactonases (6PGL)YbhE-type (EC:3.1.1.31) which hydrolyse 6-phosphogluconolactone to 6-phosphogluconate. The entry also contains the fungal muconate lactonising enzyme carboxy-cis,cis-muconate cyclase (EC:5.5.1.5) and muconate cycloisomerase (EC:5.5.1.1), which convert cis,cis-muconates to muconolactones and vice versa as part of the microbial beta-ketoadipate pathway. Structures of proteins in this family have revealed a 7-bladed beta-propeller fold.


Pssm-ID: 431196 [Multi-domain]  Cd Length: 340  Bit Score: 58.77  E-value: 9.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607    5 LLVLNKDSDTmsvidAEAGDTETVVETEfNPHEIAVTPDGEKAYVTCSLGDT--LLAF----DTETWERTAEIEHEGFDF 78
Cdd:pfam10282  15 IYVLTLDTET-----GALTLLGLVAEVG-NPSYLALSPDGRTLYAVNEEGDQggVAAFridpDSGALTLLNQVPTGGASP 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607   79 PHgLAIrERAGELWLASTYSS---RVYVIDLESD-EILTDFPTH---------QDKS--HMVALTPDEERAFVANIGSGN 143
Cdd:pfam10282  89 CH-LSV-DPDGRFLFVANYHGgsvSVFPLDADGSlGELSQVVQHegsgppperQESPhpHSVDLTPDGKFLVVPDLGTDR 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607  144 VT--AIDcEERRILADPEVGEEPEG-----IEVHPEAGLL-VANQEDGMLSVLD-----------------PETLEKTGR 198
Cdd:pfam10282 167 VRvyKLD-AGGGKLTPPASVQTPPGsgprhLAFHPNGKYAyVVNELSSTVTVFEydpatgtfeelqtvstlPEGFTGTNG 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607  199 AllGEtpIRVvsSPDGRHVLVPNRESNDVSLIDtehVRDGERQPWEIARIPV-GIWPGGTVFAPDGNRAFVANNKTNDVS 277
Cdd:pfam10282 246 A--AA--IRV--SPDGKFLYVSNRGHDSIAVFA---VDEAGGTLTLVERVSTeGDFPRDFNIDPDGKFLVVANQDSDNVT 316


                  ....*...
gi 498232607  278 V--IDCET 283
Cdd:pfam10282 317 VfrRDPET 324
8prop_heme_binding_protein cd20718
eight-bladed beta-propeller heme-binding domain in cytochrome cd1 and similar proteins; ...
 98-304 1.76e-08

eight-bladed beta-propeller heme-binding domain in cytochrome cd1 and similar proteins; Members here contain an 8-bladed beta-propeller heme-binding domain in cytochrome cd1 (nitrite reductase) and similar proteins including NirN and NirF. During denitrification, nitrate (Nar), nitrite (Nir), nitric oxide (Nor), and nitrous oxide (Nos) reductases catalyze the reaction cascade of NO(3-)-> NO(2-)-> NO -> N2O -> N2. The integral membrane proteins NorC, NorB, and NosR form the core assembly platform that binds the nitrate reductase NarGHI and the periplasmic nitrite reductase NirS via its maturation factor NirF. NirN and NirF form a stable complex with the nitrite reductase NirS during enzyme maturation. NirF is involved in heme d1 insertion.


Pssm-ID: 467720 [Multi-domain]  Cd Length: 380  Bit Score: 55.04  E-value: 1.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607  98 SSRVYVIDLESDEILTDFPTHQDKSHMVALTPDEERAFVanIG-SGNVTAIDCEERRILADPEVGEEPEGIEVHPEAGLL 176
Cdd:cd20718   37 AGSVLVIDGSTHEVLGRIDDGGAQVHVVVFSPDGRFAYV--ISrDGWLTKIDLYTLRPVASIRIGVNSRGIALSDDGKYV 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607 177 VA-NQEDGMLSVLDPETLE--KT--GRALLGETPIR-----VVSSPDGRHVLVPNRESNDVSLIDTehvRDGERQP-WEI 245
Cdd:cd20718  115 IAgNYEPGHVVILDADTLEplKVipTTGVNDDGIIEsrvgaILETPPGPYFLVALKDAGSVWVIDY---SDPDGNKvTDI 191

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498232607 246 arIPVGIWPGGTVFAPDGNRAFVANNKTNDVSVIDCETWTETERYGTEL--HPDGIAYLER 304
Cdd:cd20718  192 --GNIGRPLHDAFLDPDGRYFIVASQGSNTMWVLDLKTGKVVARIPTGKtpHPGPGATWGR 250
8prop_hemeD1_NirF cd20778
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirF; ...
 185-304 3.27e-08

eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirF; Denitrification is a process that enables biofilm formation of the opportunistic human pathogen Pseudomonas aeruginosa, making it more resilient to antibiotics and highly adaptable to different habitats. During denitrification, nitrate (Nar), nitrite (Nir), nitric oxide (Nor), and nitrous oxide (Nos) reductases catalyze the reaction cascade of NO3- -> NO2- -> NO -> N2O -> N2. The integral membrane proteins NorC, NorB, and NosR form the core assembly platform that binds the nitrate reductase NarGHI and the periplasmic cytochrome cd1 (nitrite reductase) NirS via its maturation factor NirF. The nirFDLGHJE genes encode proteins required for heme d1 biosynthesis. NirS, NirF, and NirN, the monomeric dihydro-heme d1 dehydrogenase form a stable complex during nitrite reductase maturation. The nitrite reductase NirS is bound to the denitrification supercomplex via NorB, while the electron donor system NirM and the enzyme maturation machinery NirN-NirF-NirQ, interacting with NirS, are bound via NorC.


Pssm-ID: 467722 [Multi-domain]  Cd Length: 381  Bit Score: 54.21  E-value: 3.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607 185 LSVLDPETLEKTGRALLGETPIRVVSSPDGRHVLVPNRESND--VSLIDTEHVrdgerqpwEIARIpvgIWPGGTV---- 258
Cdd:cd20778  263 VLVYDTNDWKFIKSIPLAGQPVFAVARPDGRYVWVNFSGPDNdtVQVIDTKTL--------KVVKT---LEPGKRVlhme 331

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 498232607 259 FAPDGNRAFVANNKTNDVSVIDCETWTETERYGTElHPDGIAYLER 304
Cdd:cd20778  332 FTPRGEAVYISVNDDNKVVVYDTRTFREIKEVPAK-KPSGIFFTWR 376
8prop_heme_binding_protein cd20718
eight-bladed beta-propeller heme-binding domain in cytochrome cd1 and similar proteins; ...
 57-296 3.51e-08

eight-bladed beta-propeller heme-binding domain in cytochrome cd1 and similar proteins; Members here contain an 8-bladed beta-propeller heme-binding domain in cytochrome cd1 (nitrite reductase) and similar proteins including NirN and NirF. During denitrification, nitrate (Nar), nitrite (Nir), nitric oxide (Nor), and nitrous oxide (Nos) reductases catalyze the reaction cascade of NO(3-)-> NO(2-)-> NO -> N2O -> N2. The integral membrane proteins NorC, NorB, and NosR form the core assembly platform that binds the nitrate reductase NarGHI and the periplasmic nitrite reductase NirS via its maturation factor NirF. NirN and NirF form a stable complex with the nitrite reductase NirS during enzyme maturation. NirF is involved in heme d1 insertion.


Pssm-ID: 467720 [Multi-domain]  Cd Length: 380  Bit Score: 54.27  E-value: 3.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607  57 LLAFDTETWERTAEIeHEGFDFPHGLAIrERAGELWLASTYSSRVYVIDLESDEILTDFPTHQDkSHMVALTPDEERAFV 136
Cdd:cd20718   40 VLVIDGSTHEVLGRI-DDGGAQVHVVVF-SPDGRFAYVISRDGWLTKIDLYTLRPVASIRIGVN-SRGIALSDDGKYVIA 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607 137 ANIGSGNVTAIDCEERRILAD-PEVGEEPEGI---------EVHPEAGLLVANQEDGMLSVLD---PETLEKTGRALLGE 203
Cdd:cd20718  117 GNYEPGHVVILDADTLEPLKViPTTGVNDDGIiesrvgailETPPGPYFLVALKDAGSVWVIDysdPDGNKVTDIGNIGR 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607 204 TPIRVVSSPDGRHVLVPNRESNDVSLIDTEHVRdgerqpwEIARIPVGIWP---GGTVFaPDGNRAFVANNKTNDVSVID 280
Cdd:cd20718  197 PLHDAFLDPDGRYFIVASQGSNTMWVLDLKTGK-------VVARIPTGKTPhpgPGATW-GRKGVTATPHLGEGIVTVWD 268

                        250
                 ....*....|....*.
gi 498232607 281 CETWTETERYGTELHP 296
Cdd:cd20718  269 LDTWKPVKYIPTPGPG 284
Cytochrom_D1 pfam02239
Cytochrome D1 heme domain; Cytochrome cd1 (nitrite reductase) catalyzes the conversion of ...
 101-283 1.58e-06

Cytochrome D1 heme domain; Cytochrome cd1 (nitrite reductase) catalyzes the conversion of nitrite to nitric oxide in the nitrogen cycle. This family represents the d1 heme binding domain of cytochrome cd1, in which His/Tyr side chains ligate the d1 heme iron of the active site in the oxidized state.


Pssm-ID: 366994 [Multi-domain]  Cd Length: 368  Bit Score: 49.00  E-value: 1.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607  101 VYVIDLESDEILTDFPTHQDKSHMVALTPDEERAFVANiGSGNVTAIDCEERRILADPEVGEEPEGIEVHPEAGL-LVAN 179
Cdd:pfam02239  17 VALLDGDRKEILARVDTGYALHISRMFSSDGRYVYVIG-RDGGLTKIDLWNQEIVAEVRQGGNARSVATSYDGRYvIVGN 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607  180 QEDGMLSVLDPETLE-----KTGRALLGETPIRVVS---SPDGRHVLVPNRESNDVSLIDTEHVRdgerqPWEIARIPVG 251
Cdd:pfam02239  96 YWPGQYVIMDGRTLElvkviPARGMTGDSPESRVAAivaSPGRPEFVVNLKDTGEIWLVDYSDGK-----NLKTTFIEAA 170

                         170       180       190
                  ....*....|....*....|....*....|..
gi 498232607  252 IWPGGTVFAPDGNRAFVANNKTNDVSVIDCET 283
Cdd:pfam02239 171 KFLHDGGFDPDGRYFMAAANASDKIAVWDTKR 202
NHL_like_5 cd14963
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
 3-104 3.68e-06

Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.


Pssm-ID: 271333 [Multi-domain]  Cd Length: 268  Bit Score: 47.29  E-value: 3.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607   3 DRLLVLNKDSDTMSVIDAEAGDTETVVetefNPHEIAVTPDGeKAYVTCSLGDTLLAFDTETWERTA----EIEHEGFDF 78
Cdd:cd14963  169 GRIQVFDKNGKFIKELNGSPDGKSGFV----NPRGIAVDPDG-NLYVVDNLSHRVYVFDEQGKELFTfggrGKDDGQFNL 243

                         90       100
                 ....*....|....*....|....*.
gi 498232607  79 PHGLAIRERaGELWLASTYSSRVYVI 104
Cdd:cd14963  244 PNGLFIDDD-GRLYVTDRENNRVAVY 268
beta_rpt_yvtn TIGR02276
40-residue YVTN family beta-propeller repeat; This repeat of about 40 amino acids is found in ...
 212-259 4.64e-06

40-residue YVTN family beta-propeller repeat; This repeat of about 40 amino acids is found in up to 14 copies per protein. Archaea Methanosarcina mazei and Methanosarcina acetivorans each have over 10 genes that encode tandem copies of this repeat, which is also found in other species. PSIPRED predicts with high confidence that each 40-residue repeats contains four beta strands. This model overlaps somewhat with the NHL repeat (pfam01436) and also shows sequence similarity to the WD domain, G-beta repeat (pfam00400).


Pssm-ID: 213697 [Multi-domain]  Cd Length: 42  Bit Score: 42.67  E-value: 4.64e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 498232607  212 PDGRHVLVPNRESNDVSLID--TEHVrdgerqpweIARIPVGIWPGGTVF 259
Cdd:TIGR02276   1 PDGTKLYVTNSGSNTVSVIDtaTNKV---------IATIPVGGYPFGVAV 41
beta_rpt_yvtn TIGR02276
40-residue YVTN family beta-propeller repeat; This repeat of about 40 amino acids is found in ...
 261-301 8.79e-06

40-residue YVTN family beta-propeller repeat; This repeat of about 40 amino acids is found in up to 14 copies per protein. Archaea Methanosarcina mazei and Methanosarcina acetivorans each have over 10 genes that encode tandem copies of this repeat, which is also found in other species. PSIPRED predicts with high confidence that each 40-residue repeats contains four beta strands. This model overlaps somewhat with the NHL repeat (pfam01436) and also shows sequence similarity to the WD domain, G-beta repeat (pfam00400).


Pssm-ID: 213697 [Multi-domain]  Cd Length: 42  Bit Score: 41.90  E-value: 8.79e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 498232607  261 PDGNRAFVANNKTNDVSVIDCETWTETERYGTELHPDGIAY 301
Cdd:TIGR02276   1 PDGTKLYVTNSGSNTVSVIDTATNKVIATIPVGGYPFGVAV 41
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
18-117 1.84e-05

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 45.40  E-value: 1.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607  18 IDAEAGDTETV-VETEFN-PHEIAVTPDGeKAYVTCSLGDTLLAFDTETWERTAEIEHEGFDFPHGLAIrERAGELWLAS 95
Cdd:COG4257  171 IDPDTGTLTEYaLPTPGAgPRGLAVDPDG-NLWVADTGSGRIGRFDPKTGTVTEYPLPGGGARPYGVAV-DGDGRVWFAE 248

                         90       100
                 ....*....|....*....|..
gi 498232607  96 TYSSRVYVIDLESDEILTDFPT 117
Cdd:COG4257  249 SGANRIVRFDPDTELTEYVLPS 270
8prop_heme_binding_protein cd20718
eight-bladed beta-propeller heme-binding domain in cytochrome cd1 and similar proteins; ...
 3-256 5.87e-05

eight-bladed beta-propeller heme-binding domain in cytochrome cd1 and similar proteins; Members here contain an 8-bladed beta-propeller heme-binding domain in cytochrome cd1 (nitrite reductase) and similar proteins including NirN and NirF. During denitrification, nitrate (Nar), nitrite (Nir), nitric oxide (Nor), and nitrous oxide (Nos) reductases catalyze the reaction cascade of NO(3-)-> NO(2-)-> NO -> N2O -> N2. The integral membrane proteins NorC, NorB, and NosR form the core assembly platform that binds the nitrate reductase NarGHI and the periplasmic nitrite reductase NirS via its maturation factor NirF. NirN and NirF form a stable complex with the nitrite reductase NirS during enzyme maturation. NirF is involved in heme d1 insertion.


Pssm-ID: 467720 [Multi-domain]  Cd Length: 380  Bit Score: 44.25  E-value: 5.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607   3 DRLLVLNKDSDTMSVIDAEAGDTETVVE---TEFNPHEIAVTPDGEKAYVTCSLGDTLLAFDTETWERTAEIEHEGfdFP 79
Cdd:cd20718  163 PYFLVALKDAGSVWVIDYSDPDGNKVTDignIGRPLHDAFLDPDGRYFIVASQGSNTMWVLDLKTGKVVARIPTGK--TP 240

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607  80 H-GlairerAGELWlastyssrvyvidlesdeiltdfpthqdkshmvaltPDEERAFVANIGSGNVTAIDCEERRILADP 158
Cdd:cd20718  241 HpG------PGATW------------------------------------GRKGVTATPHLGEGIVTVWDLDTWKPVKYI 278

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607 159 EVGEEPEGIEVHPEAGLLVANQ-----EDGMLSVLDPETLE--KTGRALLGETPIRVVSSPDGRHVLVPNRESNDVSLID 231
Cdd:cd20718  279 PTPGPGRFVRTHPSSPYVWADTvfgpeNADEIYVIDKETLKvvKTLIPKPGKRALHPEFTRDGKYVYVSVWDGGEVVVYD 358

                        250       260
                 ....*....|....*....|....*
gi 498232607 232 TEHVRDGERQPweiARIPVGIWPGG 256
Cdd:cd20718  359 AETLELVKRIP---AETPTGIFNVG 380
WD40 COG2319
WD40 repeat [General function prediction only];
2-271 1.16e-04

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 43.36  E-value: 1.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607   2 SDRLLVLNKDSDTMSVIDAEAGDTETVVETEFNPHEIAVTPDGEKAyVTCSLGDTLLAFDTETWERTAEIEHegfdfpHG 81
Cdd:COG2319   48 GARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLL-ASASADGTVRLWDLATGLLLRTLTG------HT 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607  82 LAIRERA----GELWLASTYSSRVYVIDLESDEILTDFPTHQDKSHMVALTPDEERAFVANiGSGNVTAIDCEERRILAD 157
Cdd:COG2319  121 GAVRSVAfspdGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGS-DDGTVRLWDLATGKLLRT 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607 158 PEVGEEP-EGIEVHPEAGLLVANQEDGMLSVLDPETlEKTGRALLGET-PIRVVS-SPDGRHVLVpNRESNDVSLIDTeh 234
Cdd:COG2319  200 LTGHTGAvRSVAFSPDGKLLASGSADGTVRLWDLAT-GKLLRTLTGHSgSVRSVAfSPDGRLLAS-GSADGTVRLWDL-- 275

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 498232607 235 vrDGERQPWEIARIPVGIWpgGTVFAPDGNRAFVANN 271
Cdd:COG2319  276 --ATGELLRTLTGHSGGVN--SVAFSPDGKLLASGSD 308
8prop_hemeD1_NirF cd20778
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirF; ...
 10-91 1.75e-04

eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirF; Denitrification is a process that enables biofilm formation of the opportunistic human pathogen Pseudomonas aeruginosa, making it more resilient to antibiotics and highly adaptable to different habitats. During denitrification, nitrate (Nar), nitrite (Nir), nitric oxide (Nor), and nitrous oxide (Nos) reductases catalyze the reaction cascade of NO3- -> NO2- -> NO -> N2O -> N2. The integral membrane proteins NorC, NorB, and NosR form the core assembly platform that binds the nitrate reductase NarGHI and the periplasmic cytochrome cd1 (nitrite reductase) NirS via its maturation factor NirF. The nirFDLGHJE genes encode proteins required for heme d1 biosynthesis. NirS, NirF, and NirN, the monomeric dihydro-heme d1 dehydrogenase form a stable complex during nitrite reductase maturation. The nitrite reductase NirS is bound to the denitrification supercomplex via NorB, while the electron donor system NirM and the enzyme maturation machinery NirN-NirF-NirQ, interacting with NirS, are bound via NorC.


Pssm-ID: 467722 [Multi-domain]  Cd Length: 381  Bit Score: 42.66  E-value: 1.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607  10 KDSDTMSVIDAEagdTETVVETeFNP-----HeIAVTPDGEKAYVTCSLGDTLLAFDTETWERTAEIEHEGfdfPHGLAI 84
Cdd:cd20778  302 PDNDTVQVIDTK---TLKVVKT-LEPgkrvlH-MEFTPRGEAVYISVNDDNKVVVYDTRTFREIKEVPAKK---PSGIFF 373


                 ....*..
gi 498232607  85 RERAGEL 91
Cdd:cd20778  374 TWRAHKI 380
NHL_like_5 cd14963
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
 2-113 2.94e-04

Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.


Pssm-ID: 271333 [Multi-domain]  Cd Length: 268  Bit Score: 41.51  E-value: 2.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607   2 SDRLLVLNKDSDTMSVIDAE---------AGDTETvvetEFN-PHEIAVTPDGEkAYVTCSLGDTLLAFDTET----WER 67
Cdd:cd14963  111 DGKLYVSDVKKHKVIVFDLEgklllefgkPGSEPG----ELSyPNGIAVDEDGN-IYVADSGNGRIQVFDKNGkfikELN 185

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 498232607  68 TAEIEHEGFDFPHGLAIRERaGELWLASTYSSRVYVIDLESDEILT 113
Cdd:cd14963  186 GSPDGKSGFVNPRGIAVDPD-GNLYVVDNLSHRVYVFDEQGKELFT 230
8prop_hemeD1_cyt_cd1-like cd20782
cytochrome cd1 nitrate reductase eight-bladed heme d1-binding beta-propeller domain and ...
 57-264 3.09e-04

cytochrome cd1 nitrate reductase eight-bladed heme d1-binding beta-propeller domain and similar proteins; Cytochrome cd1 (cyt cd1) nitrite reductase catalyzes in vitro the reduction of molecular oxygen to water and the reduction of nitrite to nitric oxide). It is a dimer of two identical subunits of 60 kDa, each containing one c and one d1 heme group. The c heme is the electron accepting pole of the molecule and is reduced in vitro by either azurin or cytochrome c551. The d1 heme is the site where nitrite, and oxygen reduction occur. NiR is a key denitrification enzyme, which controls the rate of the production of toxic nitric oxide (NO) and ultimately regulates the release of NO into the atmosphere. The two types of heme are located in separate domains whose arrangement suggests a mechanism requiring domain movement during catalysis.


Pssm-ID: 467726 [Multi-domain]  Cd Length: 415  Bit Score: 42.08  E-value: 3.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607  57 LLAFDTETWERTAEIE-----HEGFDFPHGLaireragELWLASTYSSRVYVIDLESDEILTDFPT----HQDKShmvAL 127
Cdd:cd20782  204 LIDYTQDDFPVVDEIDcgrtlHDGFFTPDGR-------YFMLASQTDNCMSVLDVEEREVVDRIPTagvpHPGPG---AL 273

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607 128 TPDEERAFVANIGSGNVTAIDCEERRILADPEVGEEPEGIEVHPEAGLLVAN-------QEDGMLSVLDPETLEKtgral 200
Cdd:cd20782  274 DPDRGLAFTTHVGTDAVTAWDTETWEPEADIEVPGGGLFLRSHPDSDYVWGDvilddtdRLDQLIYAIDPDTLEV----- 348

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498232607 201 lgETPIRVVSSPDGRHvlvpnresndvslIDTEHVRDGErqpweiaRIPVGIWPGGTVFAPDGN 264
Cdd:cd20782  349 --ATVIDTSEWGEGRA-------------IHPEFSRDGE-------KVYVSHWDAGEILVFDSH 390
8prop_hemeD1_cyt_cd1-like cd20782
cytochrome cd1 nitrate reductase eight-bladed heme d1-binding beta-propeller domain and ...
 18-90 2.43e-03

cytochrome cd1 nitrate reductase eight-bladed heme d1-binding beta-propeller domain and similar proteins; Cytochrome cd1 (cyt cd1) nitrite reductase catalyzes in vitro the reduction of molecular oxygen to water and the reduction of nitrite to nitric oxide). It is a dimer of two identical subunits of 60 kDa, each containing one c and one d1 heme group. The c heme is the electron accepting pole of the molecule and is reduced in vitro by either azurin or cytochrome c551. The d1 heme is the site where nitrite, and oxygen reduction occur. NiR is a key denitrification enzyme, which controls the rate of the production of toxic nitric oxide (NO) and ultimately regulates the release of NO into the atmosphere. The two types of heme are located in separate domains whose arrangement suggests a mechanism requiring domain movement during catalysis.


Pssm-ID: 467726 [Multi-domain]  Cd Length: 415  Bit Score: 39.39  E-value: 2.43e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498232607  18 IDAEAGDTETVVETEFNPHEIAVTP----DGEKAYVTCSLGDTLLAFDTETWERTAEIehEGFDFPHGLAIRERAGE 90
Cdd:cd20782  341 IDPDTLEVATVIDTSEWGEGRAIHPefsrDGEKVYVSHWDAGEILVFDSHTGELIEEI--DGLETPTGKFLGNRAEK 415
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
158-301 2.54e-03

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 38.85  E-value: 2.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607 158 PEVGEEPEGIEVHPEAGLLVANQEDGMLSVLDPETLEKTGRAL-LGETPIRVVSSPDGRhVLVPNRESNDVSLIDTEhvr 236
Cdd:COG4257   13 PAPGSGPRDVAVDPDGAVWFTDQGGGRIGRLDPATGEFTEYPLgGGSGPHGIAVDPDGN-LWFTDNGNNRIGRIDPK--- 88

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607 237 DGerqpwEIARIPVGIW---PGGTVFAPDGNrAFVANNKTNDVSVIDCET--WTETERYGTELHPDGIAY 301
Cdd:COG4257   89 TG-----EITTFALPGGgsnPHGIAFDPDGN-LWFTDQGGNRIGRLDPATgeVTEFPLPTGGAGPYGIAV 152
8prop_heme_binding_protein cd20718
eight-bladed beta-propeller heme-binding domain in cytochrome cd1 and similar proteins; ...
 38-283 2.84e-03

eight-bladed beta-propeller heme-binding domain in cytochrome cd1 and similar proteins; Members here contain an 8-bladed beta-propeller heme-binding domain in cytochrome cd1 (nitrite reductase) and similar proteins including NirN and NirF. During denitrification, nitrate (Nar), nitrite (Nir), nitric oxide (Nor), and nitrous oxide (Nos) reductases catalyze the reaction cascade of NO(3-)-> NO(2-)-> NO -> N2O -> N2. The integral membrane proteins NorC, NorB, and NosR form the core assembly platform that binds the nitrate reductase NarGHI and the periplasmic nitrite reductase NirS via its maturation factor NirF. NirN and NirF form a stable complex with the nitrite reductase NirS during enzyme maturation. NirF is involved in heme d1 insertion.


Pssm-ID: 467720 [Multi-domain]  Cd Length: 380  Bit Score: 38.86  E-value: 2.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607  38 IAVTPDGEKAYVTCSLGDTLLAFDTETWERTAEIEHEGFDfpHGLAIRERAGELwLASTYSSR----------VYVIDLE 107
Cdd:cd20718  105 IALSDDGKYVIAGNYEPGHVVILDADTLEPLKVIPTTGVN--DDGIIESRVGAI-LETPPGPYflvalkdagsVWVIDYS 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607 108 --SDEILTDFPTHQDKSHMVALTPDEERAFVANIGSGNVTAIDCEERRILADPEVGEEPegievHPEAGLL--------V 177
Cdd:cd20718  182 dpDGNKVTDIGNIGRPLHDAFLDPDGRYFIVASQGSNTMWVLDLKTGKVVARIPTGKTP-----HPGPGATwgrkgvtaT 256

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607 178 ANQEDGMLSVLDPETLEKTGR-ALLGETPIrVVSSPDGRHVLV----PNRESNDVSLIDTEhvrdgerqPWEIAR--IPV 250
Cdd:cd20718  257 PHLGEGIVTVWDLDTWKPVKYiPTPGPGRF-VRTHPSSPYVWAdtvfGPENADEIYVIDKE--------TLKVVKtlIPK 327

                        250       260       270
                 ....*....|....*....|....*....|....
gi 498232607 251 -GIWPGGTVFAPDGNRAFVANNKTNDVSVIDCET 283
Cdd:cd20718  328 pGKRALHPEFTRDGKYVYVSVWDGGEVVVYDAET 361
NHL_like_3 cd14956
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
 32-146 3.17e-03

Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.


Pssm-ID: 271326 [Multi-domain]  Cd Length: 274  Bit Score: 38.42  E-value: 3.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607  32 EFN-PHEIAVTPDGeKAYVTCSLGDTLLAFDTE-----TWERTAeIEHEGFDFPHGLAIRErAGELWLASTYSSRVYVID 105
Cdd:cd14956  105 QFNaPRGVAVDADG-NLYVADFGNQRIQKFDPDgsflrQWGGTG-IEPGSFNYPRGVAVDP-DGTLYVADTYNDRIQVFD 181

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 498232607 106 LESDEILT---------DFPTHQDkshmVALTPDeERAFVANIGSGNVTA 146
Cdd:cd14956  182 NDGAFLRKwggrgtgpgQFNYPYG----IAIDPD-GNVFVADFGNNRIQK 226
beta_rpt_yvtn TIGR02276
40-residue YVTN family beta-propeller repeat; This repeat of about 40 amino acids is found in ...
 129-169 3.88e-03

40-residue YVTN family beta-propeller repeat; This repeat of about 40 amino acids is found in up to 14 copies per protein. Archaea Methanosarcina mazei and Methanosarcina acetivorans each have over 10 genes that encode tandem copies of this repeat, which is also found in other species. PSIPRED predicts with high confidence that each 40-residue repeats contains four beta strands. This model overlaps somewhat with the NHL repeat (pfam01436) and also shows sequence similarity to the WD domain, G-beta repeat (pfam00400).


Pssm-ID: 213697 [Multi-domain]  Cd Length: 42  Bit Score: 34.58  E-value: 3.88e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 498232607  129 PDEERAFVANIGSGNVTAIDCEERRILADPEVGEEPEGIEV 169
Cdd:TIGR02276   1 PDGTKLYVTNSGSNTVSVIDTATNKVIATIPVGGYPFGVAV 41
8prop_hemeD1_cyt_cd1-like cd20785
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase and ...
 29-164 4.19e-03

eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase and similar proteins; Cytochrome cd1 (cyt cd1) nitrite reductase catalyzes in vitro the reduction of molecular oxygen to water and the reduction of nitrite to nitric oxide). It is a dimer of two identical subunits of 60 kDa, each containing one c and one d1 heme group. The c heme is the electron accepting pole of the molecule and is reduced in vitro by either azurin or cytochrome c551. The d1 heme is the site where nitrite, and oxygen reduction occur. NiR is a key denitrification enzyme, which controls the rate of the production of toxic nitric oxide (NO) and ultimately regulates the release of NO into the atmosphere. The two types of heme are located in separate domains whose arrangement suggests a mechanism requiring domain movement during catalysis.


Pssm-ID: 467729 [Multi-domain]  Cd Length: 412  Bit Score: 38.43  E-value: 4.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498232607  29 VETEFNPHEIAVTPDGEkaYVTCS--LGDTLLAFDTETWERTAEIEHEGFDfPHGLAIRERAGELwLASTY--------- 97
Cdd:cd20785  114 VKAGLNGPSLAVSRDGK--YLAAGsfVPHTAVILDADTLEPLKYFELEGVD-PDGKMVESDSGMI-TGTPYanyfaiale 189

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498232607  98 -SSRVYVIDLESDeiltDFPTHQDKS-----HMVALTPDEERAFVANIGSGNVTAIDCEERRILADPEVGEEP 164
Cdd:cd20785  190 qAGQVWIVDLDKP----GMPVTKIKNvgrhlHDAFLSPDGRYLMVASYDDNKNAVIDLKEKKVVKKIPAGCQP 258
 
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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