|
Name |
Accession |
Description |
Interval |
E-value |
| 8prop_hemeD1_NirF |
cd20778 |
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirF; ... |
21-391 |
0e+00 |
|
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: 606.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021414 21 PPLRGSGDLGVLIERADGSVQILDGTAKTSLARVEGLGDLSHASLVFSRDQRYAYVFGRDGGLTRLDLLAQRIDKRLIQG 100
Cdd:cd20778 12 LAATGTGALGVVVEREAGSVFVVDRSKHESLGRIEGLGNLSHATMVFSRDGRYAYVIGRDGGLSKVDLLTLKVVARVKQS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021414 101 GNSIGGAISQDGRLVAVSNYEPGGVKVFDSRTLELVAEIPATRLPGQDRnSRVVGLVDAPGQRFVFSLFDSGEIWIADFS 180
Cdd:cd20778 92 GNSIGGAISQDGRYVAVANYDPGGVKILDADTLKVLADIPAGSKGGGQR-SRVVGLVDAPGNRFIFSLMDADEIWVLDAS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021414 181 QGDTPRLTRFRDVGKQPYDALISPDGRYYMAGLFGEDGMAQLDLWHPERGVRRVLGDYGRGQRKLPVYKMPHLEGWTIAS 260
Cdd:cd20778 171 DPDFPVVKKFKDIGRMPYDALITPDGRYYIAGLFNSDGVGLLDLWKPERGVRRILLDYGKGEEKLPVYKMPHLEGWAVAG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021414 261 DQAFVPAVGHHQVLVLDARDWKQTDAIDVAGQPVFVMTRPDDRQIWVNFAYPDNDKVQVIDSETHEVIETLRPGPGVLHM 340
Cdd:cd20778 251 DKAFVPAVGEHRVLVYDTNDWKFIKSIPLAGQPVFAVARPDGRYVWVNFSGPDNDTVQVIDTKTLKVVKTLEPGKRVLHM 330
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 501021414 341 EFSGRGDQVWISVRDADQVQVWDPYRLERIGSLPARSPSGIFFSHRAQHIG 391
Cdd:cd20778 331 EFTPRGEAVYISVNDDNKVVVYDTRTFREIKEVPAKKPSGIFFTWRAHKIG 381
|
|
| Cytochrom_D1 |
pfam02239 |
Cytochrome D1 heme domain; Cytochrome cd1 (nitrite reductase) catalyzes the conversion of ... |
24-387 |
0e+00 |
|
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: 526.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021414 24 RGSGDLGVLIERADGSVQILDGTAKTSLARVEGLGDLsHASLVFSRDQRYAYVFGRDGGLTRLDLLAQRIDKRLIQGGNS 103
Cdd:pfam02239 1 RDLGNLFVVTERDAGSVALLDGDRKEILARVDTGYAL-HISRMFSSDGRYVYVIGRDGGLTKIDLWNQEIVAEVRQGGNA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021414 104 IGGAISQDGRLVAVSNYEPGGVKVFDSRTLELVAEIPATRLPGQDRNSRVVGLVDAPGQR-FVFSLFDSGEIWIADFSQG 182
Cdd:pfam02239 80 RSVATSYDGRYVIVGNYWPGQYVIMDGRTLELVKVIPARGMTGDSPESRVAAIVASPGRPeFVVNLKDTGEIWLVDYSDG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021414 183 dTPRLTRFRDVGKQPYDALISPDGRYYMAGLFGEDgmaQLDLWHPERGVRRVLGDYGRGQRKLPVYKMPHLEG---WTIA 259
Cdd:pfam02239 160 -KNLKTTFIEAAKFLHDGGFDPDGRYFMAAANASD---KIAVWDTKRGKLVALLDYGKTPHPGPGANMPHLEGgpvWTTS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021414 260 SDQAFV-PAVGHHQVLVLDARDWKQTDAIDVAGQPVFVMTRPDDRQIWVN-FAYPDNDKVQVIDSETHEVIETLRPGPG- 336
Cdd:pfam02239 236 HLGDFVtPLIGTDPVLVHDLQAWKQVKEIDVAGGGLFVKTHPDSRYLWVDtFLNPDNDSVAVIDSETLEKVLTLAPWPGl 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 501021414 337 -VLHMEFSGRGDQVWISVRDAD-QVQVWDPYRLERIGSLPARSPSGIFFSHRA 387
Cdd:pfam02239 316 vVVHMEFNKRGDEVWLSVWDGKgALVVYDDKTLKLKKVIPLNTPSGKFNVYNT 368
|
|
| 8prop_heme_binding_protein |
cd20718 |
eight-bladed beta-propeller heme-binding domain in cytochrome cd1 and similar proteins; ... |
22-382 |
6.13e-116 |
|
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: 342.40 E-value: 6.13e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021414 22 PLRGSGDLGVLIERADGSVQILDGTAKTSLARVEGLGDLSHaSLVFSRDQRYAYVFGRDGGLTRLDLLAQRIDKRLIQGG 101
Cdd:cd20718 22 GIWDLENLMVVVERDAGSVLVIDGSTHEVLGRIDDGGAQVH-VVVFSPDGRFAYVISRDGWLTKIDLYTLRPVASIRIGV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021414 102 NSIGGAISQDGRLVAVSNYEPGGVKVFDSRTLELVAEIPATRLPGQDRN-SRVVGLVD-APGQRFVFSLFDSGEIWIADF 179
Cdd:cd20718 101 NSRGIALSDDGKYVIAGNYEPGHVVILDADTLEPLKVIPTTGVNDDGIIeSRVGAILEtPPGPYFLVALKDAGSVWVIDY 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021414 180 SQGDTPRLTRFRDVGKQPYDALISPDGRYYMAGLFGEDGMAQLDLWhpergvrrvlgdYGRGQRKLPVYKMPHLEGWTIA 259
Cdd:cd20718 181 SDPDGNKVTDIGNIGRPLHDAFLDPDGRYFIVASQGSNTMWVLDLK------------TGKVVARIPTGKTPHPGPGATW 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021414 260 SDQ--AFVPAVGHHQVLVLDARDWKQTDAIDVAGQPVFVMTRPDDRQIWVNFAYPD--NDKVQVIDSETHEVIETLRPGP 335
Cdd:cd20718 249 GRKgvTATPHLGEGIVTVWDLDTWKPVKYIPTPGPGRFVRTHPSSPYVWADTVFGPenADEIYVIDKETLKVVKTLIPKP 328
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 501021414 336 G--VLHMEFSGRGDQVWISVRDADQVQVWDPYRLERIGSLPARSPSGIF 382
Cdd:cd20718 329 GkrALHPEFTRDGKYVYVSVWDGGEVVVYDAETLELVKRIPAETPTGIF 377
|
|
| 8prop_hemeD1_cyt_cd1-like |
cd20782 |
cytochrome cd1 nitrate reductase eight-bladed heme d1-binding beta-propeller domain and ... |
28-388 |
9.66e-47 |
|
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: 164.96 E-value: 9.66e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021414 28 DLGVLIERADGSVQILDGTAKTSLARVEGLGDLSHaSLVF-------SRDQRYAYVFGRDGGLTRLDLLAQRIDKRLIQG 100
Cdd:cd20782 47 DLLVVAERRNASVSLVDTVNHERLGRIEDVGRAIH-VIEFhrdlpenEREGAYAYTQSRQGWVSKLDLFGGERVARVRAG 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021414 101 GNSIGGAISQDGRLVAVSNYEPGGVKVFDSRTLELVAEIP--ATRLPGQDRNSRVVGLVDAPGQR-FVFSLFDSGEIWIA 177
Cdd:cd20782 126 TDARDIAVSRDSNYLIAGYYNPNHLVVVDAETMEPLKRIPthGVDPDGQSVESRVCTLYDVPGEGcFLAALKEAGQVWLI 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021414 178 DFSQGDTPRLTRFrDVGKQPYDALISPDGRYYMAGLFGEDGMAQLDLwhPERGVrrvlgdygrgQRKLPVYKMPHLEGWT 257
Cdd:cd20782 206 DYTQDDFPVVDEI-DCGRTLHDGFFTPDGRYFMLASQTDNCMSVLDV--EEREV----------VDRIPTAGVPHPGPGA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021414 258 IASDQ--AFVPAVGHHQVLVLDARDWKQTDAIDVAGQPVFVMTRPDDRQIWVNFAYPDNDK----VQVIDSETHEV---I 328
Cdd:cd20782 273 LDPDRglAFTTHVGTDAVTAWDTETWEPEADIEVPGGGLFLRSHPDSDYVWGDVILDDTDRldqlIYAIDPDTLEVatvI 352
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501021414 329 ETLRPGPG-VLHMEFSGRGDQVWISVRDADQVQVWDPYR---LERIGSLPArsPSGIFFSHRAQ 388
Cdd:cd20782 353 DTSEWGEGrAIHPEFSRDGEKVYVSHWDAGEILVFDSHTgelIEEIDGLET--PTGKFLGNRAE 414
|
|
| 8prop_heme-binding_NirN |
cd20777 |
eight-bladed heme d1-binding beta-propeller domain in dihydro-heme d1 dehydrogenase NirN; The ... |
29-380 |
3.46e-42 |
|
eight-bladed heme d1-binding beta-propeller domain in dihydro-heme d1 dehydrogenase NirN; The monomeric dihydro-heme d1 dehydrogenase NirN is part of the denitrification process that enables biofilm formation of the opportunistic human pathogen Pseudomonas aeruginosa, making it more resilient to antibiotics and highly adaptable to different habitats. NirN, similar to the homodimeric cytochrome cd1 (nitrite reductase; NirS), consists of an eight-bladed heme d1-binding beta-propeller and a cytochrome c domain, but their relative orientation differs with respect to NirS. His147, His323 and Tyr461, but not His417 are essential for activity. All 8 blades of the propeller are included in this alignment.
Pssm-ID: 467721 [Multi-domain] Cd Length: 405 Bit Score: 152.52 E-value: 3.46e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021414 29 LGVLIERADGSVQILDGTAKTSLARVEGLGDLsHASLVFSRDQRYAYVFGRDGGLTRLDLLAQRIDKRLIQGGNSIGGAI 108
Cdd:cd20777 34 LFVVVESGDHHVTVLDGDRFEPLARFPTRFAL-HGGPKFSPDGRFVYFASRDGWVTKYDLWNLKVVAEVRAGLNTRNLAV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021414 109 SQDGRLVAVSNYEPGGVKVFDSRTLELVAEIPATRLPGqdRNSRVVGLVDAPGQR-FVFSLFDSGEIWiadfsqgdtprl 187
Cdd:cd20777 113 SSDGRYVAVANYLPHTLVLLDARDLSLLKVIPAADAQG--RSSRVSAVYDAPPRRsFVVALKDVPELW------------ 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021414 188 trfrdvgKQPYDalisPDGRYYMAGL----FGEDGMAQLDLWHPER--------------GVRRVLG------------- 236
Cdd:cd20777 179 -------ELSYD----EGADPVPIGLvhdfLYEEGAASPGFFAPRRialpaplddfffdpDYRNLLGasrqggggqvidl 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021414 237 DYGRGQRKLPVYKMPHL-EGWTIASDQAFV---PAVGHHQVLVLDARDWKQTDAIDVAGQPVFVMTRPDDRQIWVN-FAY 311
Cdd:cd20777 248 DVGRVIASLPLSGMPHLgSGIYWKRDGRRVmatPNLSRGVISVIDLQTWAIVKEIPTPGPGFFMRSHENSPYAWADvFMG 327
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501021414 312 PDNDKVQVIDSETHEVIETLRPGPG--VLHMEFSGRGDQVWISVRDAD-QVQVWDPYRLERIGSLPARSPSG 380
Cdd:cd20777 328 PKRDKLHLIDKQTLEIVKTLRPEPGktAAHVEFTRDGRYALASVWEDDgALIVYDAHTLKEVKRLPMNKPSG 399
|
|
| 8prop_hemeD1_cyt_cd1-like |
cd20783 |
eight-bladed heme d1-binding beta-propeller domain and similar proteins; Cytochrome cd1 (cyt ... |
27-389 |
3.62e-36 |
|
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: 467727 [Multi-domain] Cd Length: 388 Bit Score: 135.98 E-value: 3.62e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021414 27 GDLGVLIERADGSVQILDGTAKTSLARVEGlGDLSHASLVFSRDQRYAYVFGRDGGLTRLDLLAQRIDKRLIQGGNSIGG 106
Cdd:cd20783 27 DNLLLVTEREARSIAVIDGDTHTLLGHIEA-GYRAHGYTFSPTDGRWAYNLGRDGWLYKIDLYSLQPVAKVRVGLDARGI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021414 107 AISQDGRLVAVSNYEPGGVKVFDSRTLELVAEIP--ATRLPGQDRNSRVVGLVD-AP---GQRFVFSLFDSGEIWIADFS 180
Cdd:cd20783 106 AISDDGKYLIAGNYIPATAVILDAKTLEPLKVIDtsGVDPDGKMVDSRVASVNDvAPdlvGPYFLLALKEAGQVWRIDYS 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021414 181 QGDTPrLTRFRDVGKQPYDALISPDGRYYMAGLFGEDGMAQLDLWHPErgvrrVLgdygrgqRKLPVYKMPHL-EGWTIA 259
Cdd:cd20783 186 KPDFP-ITKVENVGHILHDGFLSPDNKTFYLASQTDNWMAAIDVATMK-----IV-------AKIPTGDKPHPgSGAVWE 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021414 260 SD---QAFVPAVGHHQVLVLDARDWKQTDAIDVAGQPVFVMTRPDDRQIWVN--FAyPDNDKVQVIDSET-HEVIETLRP 333
Cdd:cd20783 253 ADgkeYAATVHAGEGKVTIWDLDTNEIVGEVPTSGPGLFIRTTENMPYVWADsmFA-PEPNEITVHEKAPpFKVVKRITD 331
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 501021414 334 GPGVLHMEFSGRGDQVWISVRDADQVQVWDPYRLERIGSLPA-RSPSGIFFSHRAQH 389
Cdd:cd20783 332 GTRTLHPEPTADGKYVYVSDWDGNVVRVYDAETLELVKEITGiTTPTGIFNTSRRHE 388
|
|
| 8prop_hemeD1_cyt_cd1-like |
cd20785 |
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase and ... |
70-392 |
8.83e-35 |
|
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: 132.42 E-value: 8.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021414 70 DQRYAYVFGRDGGLTRLDLLAQRIDKRLIQGGNSIGGAISQDGRLVAVSNYEPGGVKVFDSRTLELVAEIpatRLPGQDR 149
Cdd:cd20785 87 NPRWAYVKTDTGEVYKIDLYSMQAVRSVKAGLNGPSLAVSRDGKYLAAGSFVPHTAVILDADTLEPLKYF---ELEGVDP 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021414 150 NSRVV----GLVDAP--GQRFVFSLFDSGEIWIADFSQGDTPrLTRFRDVGKQPYDALISPDGRYYMAGLFGEDGMAQLD 223
Cdd:cd20785 164 DGKMVesdsGMITGTpyANYFAIALEQAGQVWIVDLDKPGMP-VTKIKNVGRHLHDAFLSPDGRYLMVASYDDNKNAVID 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021414 224 LwhperGVRRVLgdygrgqRKLPVYKMPHLEGWTIASDQAFVPAVG--------HHQVLVLDARDWKQTDAIDVAGQPVF 295
Cdd:cd20785 243 L-----KEKKVV-------KKIPAGCQPHLGSGAVVKVGGRLLGFGtnigscddKTVVTVWDMDTFEVVKQIPVSGPTES 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021414 296 VMTRPDDRQIWVNF--AYPDNDKVQVIDSETHEVIETLRPGpGVLHM-EFSGRGDQVWISVR-DADQVQVWDPYRLERIG 371
Cdd:cd20785 311 PAAHPNAPYVAVDIvgKDPRARKIQLIDKNTLEVVKTLDVG-GHSHFpEYTADGDYLYVSAGyNGDRLVIYDSKTLKKVK 389
|
330 340
....*....|....*....|...
gi 501021414 372 SLPARSPSGIFFSHRAQH--IGL 392
Cdd:cd20785 390 EIPMESPAGIFSRARARWvtVGL 412
|
|
| 8prop_hemeD1_cyt_cd1-like |
cd20784 |
cytochrome cd1 nitrate reductase eight-bladed heme d1-binding beta-propeller domain and ... |
28-380 |
1.53e-29 |
|
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: 467728 [Multi-domain] Cd Length: 367 Bit Score: 117.33 E-value: 1.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021414 28 DLGVLIERADGSVQILDGTA---KTSLARVeglgdlsHASLVFSRDQRYAYVFGRDGGLTRLDLLAQRIDKRLIQGGNSI 104
Cdd:cd20784 30 NITLVVERGGGKVWVMEGFRvldKFDFGNV-------HGGIKFSPSGKKIYVPSRDGWIGKYDLKEGRETGKVRACINLR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021414 105 GGAISQDGRLVAVSNYEPGGVKVFDSRTLELVAEIPatrLPGqdrnsRVVGLVDAPGQ-RFVFSLFDSGEIWIADFSQGD 183
Cdd:cd20784 103 NIALSRDGKYLAAACLLPENLVILDTKTLKPVKVIK---LDG-----KISAVYELYSKdKAIFTFRDKPKLGFLDTKTLK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021414 184 TprltRFRDVgKQPY-DALISPDGRYYMAGLFGEDGMAQLDLwhpergvrrvlgDYGRGQRKLPVYKMPHLEGWTI-ASD 261
Cdd:cd20784 175 I----EYIKI-KEPFeDFFIDPFEEYIIGTSRKGKKLYVYSL------------KDLKKVFEHKMEGMPHLFSATFwYKK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021414 262 QAF---VPAVGHHQVLVLDARDWKQTDAIDVAGQPVFVMTRPDDRQIWVnfaypDN--DKVQVIDSETHEV-IETLRPGP 335
Cdd:cd20784 238 GKFyfaTPHIKKPYVSIWKMYDWKFVKEIDLGGDGFFVRTHPKTPYLWV-----DNgtDKLVLIDKKDLSVkKITPPKGK 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 501021414 336 GVLHMEFSGRGDQVWISVRDAD-QVQVWDPYRLERIGSLPARSPSG 380
Cdd:cd20784 313 KAIHTEFSGDGKYAYVSIYEKDgALVVYDTFTLKELKRYPANIPVG 358
|
|
| 8prop_hemeD1_NiR_alpha_gamma |
cd20781 |
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NiR ... |
31-391 |
1.11e-26 |
|
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NiR alpha and gamma proteobacteria subdivisions; Cytochrome cd1 (nitrite reductase) catalyzes in vitro the reduction of molecular oxygen to water and the reduction of nitrite to nitric oxide. Purification and characterization of NiR from several bacterial sources have shown that there are two distinct classes of dissimilatory NiRs that yield NO as the main reaction product, containing either copper or heme as cofactor, the heme-containing enzyme occurring more frequently. It forms a homodimer 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. Heme binding nitrite reductase from alphaproteobacteria and gammaproteobacteria are present here.
Pssm-ID: 467725 [Multi-domain] Cd Length: 433 Bit Score: 110.57 E-value: 1.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021414 31 VLIERADGSVQILDGTAKTSLARVEG------LGDLSHASLVFSRDQ-RYAYVFGRDGGLTRLDLLaQRIDKRLIQ---- 99
Cdd:cd20781 43 VVIERDAGKVAIIDGDKKEVVAHIDTgyavhvLKASEHHKVEKAKNPgRFWYTMGRDGKLTKIDLW-QTPDKMLVAevqi 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021414 100 GGNSIGGAISQDGRLVAVSNYEPGGVKVFDSRTLELVaEIPATR---LPGQDRN-SRVVGLVDAPGQ-RFVFSLFDSGEI 174
Cdd:cd20781 122 AYDARDVAVSGDGKYVIGGGYWPPHFVIVDAETMEPL-KVVSTRgvnVDGEYVNeSRVAAIYTTPNApTFLVAVKELGQM 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021414 175 WIADFSQGDTPRLTRFrDVGKQPYDALISPDGRYYMAGLFGEDGMAQLD--------------LWHPERGVRRVLGDYGr 240
Cdd:cd20781 201 WQVDYSDLDNLRIDQI-DTAKFLHDGFFDPTGRYFQIAANASNKMVVVDtktrkleamidtgkLPHPGPGANWIDPKCG- 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021414 241 gqrklPVYKMPHL-EGWTIA--------SDQAfvpavghhqvlvldardWKQTDAIDVAGQPVFVMTRPDDRQIWVNFA- 310
Cdd:cd20781 279 -----PVGGTTHLgEGKVTVwgndpkghPDQA-----------------WKICYEVETDGPGLFIRTHPNSDYVWADQTk 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021414 311 YPD---NDKVQVIDSETHEVIETLR----PGPGVLHMEFSGRGDQVWISV-------RDADQVQVWDPYRLE---RIGSL 373
Cdd:cd20781 337 HPEpevQQSVQVIDKKTREIVKTIRvteeEGYVAVHMEFNQDGTEVWVSVwnrkdskEPNGEIVVYDAKTLEekaRIKGL 416
|
410
....*....|....*....
gi 501021414 374 PArsPSGIF-FSHRAQHIG 391
Cdd:cd20781 417 YT--PTGKFnVYNRVNHVT 433
|
|
| 8prop_hemeD1_NiR_delta_epsilon |
cd20780 |
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NiR ... |
28-334 |
1.20e-26 |
|
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NiR delta/epsilon subdivisions; Cytochrome cd1 (nitrite reductase) catalyzes in vitro the reduction of molecular oxygen to water and the reduction of nitrite to nitric oxide. Purification and characterization of NiR from several bacterial sources have shown that there are two distinct classes of dissimilatory NiRs that yield NO as the main reaction product, containing either copper or heme as cofactor- the heme-containing enzyme occurring more frequently. It forms a homodimer with each subunit 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. The heme-binding nitrite reductase in delta and epsilon subdivisions are present here.
Pssm-ID: 467724 [Multi-domain] Cd Length: 436 Bit Score: 110.31 E-value: 1.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021414 28 DLGVLIERADGSVQILDGTAKTSLARVEGlGDLSHASLVFSRDQRYAYVFGRDGGLTRLDLLA--QRIDKRLIQGGNSIG 105
Cdd:cd20780 50 DITFATERDASLVDFIDGTTGKVLSRHKA-GFAVHVTVTNKRNPRYAYSISRSGRLTMFDLAApgQPALASVQVGQESRG 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021414 106 GAISQDGRLVAVSNYEPGGVKVFDSRTLELVAEIPATRL---PGQDRNSRVVGLVDAP-GQRFVFSLFDSGEIWIADFSQ 181
Cdd:cd20780 129 LAVSPDGKYVMAGNYNPGGAVLCDAMTLEPLKVYDTSSVidpDGQIGPSRVASIADTPyGPYFAFALKDAGHVYIVDYSK 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021414 182 GDTPRLTRFRDVGKQPYDALISPD---GRYYMAGLFGEDGMAQLDLW----------------HPERGVRRvlgdYGRGQ 242
Cdd:cd20780 209 PDFPIVGDIPNIGKILHDAFLNEGegfGRYLMIASQGSDVMGIVDFKtknlaakvytgpkskpHPGQGSSW----YNKGL 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021414 243 rklpvYKMPHLegwTIASDqafvpaVGhhQVLVLDArDWKQTDAIDVAGQPVFVMTRPDDRQIWVN--FAYPDN-DKVQV 319
Cdd:cd20780 285 -----GKQLHA---TVSMN------VG--DVVIWDS-NWDVVKHVPTAGGGLFVGTSEHTPYLWADcvLGGPDNyNKVHL 347
|
330
....*....|....*
gi 501021414 320 IDSETHEVIETLRPG 334
Cdd:cd20780 348 INKQTLETDRIIKVG 362
|
|
| 8prop_hemeD1_NirS |
cd20779 |
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirS; ... |
30-382 |
2.25e-16 |
|
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirS; Cytochrome cd1 nitrite reductase NiR is a key denitrification enzyme that catalyzes the conversion of nitrite to nitric oxide in the nitrogen cycle. The crystal structure of the oxidized enzyme shows that the d1 heme iron of the active site is ligated by His/Tyr side chains, and the c heme iron is ligated by a His/His ligand pair. Nitrite reductase from Pseudomonas aeruginosa 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. The two types of heme are located in separate domains whose arrangement suggests a mechanism requiring domain movement during catalysis.
Pssm-ID: 467723 [Multi-domain] Cd Length: 438 Bit Score: 80.37 E-value: 2.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021414 30 GVlIERADGSVQILDGTAKTSLARVeglgDLSHAS--LVFSRDQRYAYVFGRDGGLTRLDLLAQRIDK-RLIQGGNSigg 106
Cdd:cd20779 63 GV-ILRDAGQVAIIDGDTKEIVSIV----DTGFAVhiLRSSASGRYFYTIGRDGKVTMIDLWMKKPTVvAEVKGCLD--- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021414 107 AISQDG--------RLVAVSNYEPGGVKVFDSRTLELVAeIPATRLPGQDRN-----SRVVGLVDAPGQ-RFVFSLFDSG 172
Cdd:cd20779 135 ARSVDSskykgfedKYAIVGCYWPPQYVILDGLTLEPLK-VVSTRGYTYDTGeyhpePRVASIVASHFDpEWVVNVKETG 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021414 173 EIWIADFSQGDTPRLT-----RF-RDVGkqpYDAlispDGRYYMAGLFGEDGMAQLDLW--------------HPERGVR 232
Cdd:cd20779 214 QVWLVDYSDLKNLKVTmieaeRFlHDGG---WDH----TKRYFLVAANARNKVVVVDTKtkklvalvetgikpHPGRGAN 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021414 233 RVLGDYGrgqrklPVYKMPHLEGWTIA---SDqafvPAvGHHQVlvldarDWKQTDAIDVAGQ-PVFVMTRPDDRQIWVN 308
Cdd:cd20779 287 WVDPKYG------PVWATGHLGEGKIAligTD----PK-GHPQY------AWKVVRKIKLPGGgSLFIKTHPKSPWLWVD 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021414 309 FAYPDNDKVQ----VIDSETHEVIETLRPGPG---VLHMEFSGRGDQVWISVRDADQ--VQVWDPYRLE---RIGSLPAR 376
Cdd:cd20779 350 RTLNPDPKLArsvcVFDKKLLDKKYKCWPVADhgrAVHFEYNKAGDEVWVSVWDKKPgaIVVYDDKTLKekaRITGDWLV 429
|
....*.
gi 501021414 377 SPSGIF 382
Cdd:cd20779 430 TPTGKF 435
|
|
| YncE |
COG3391 |
DNA-binding beta-propeller fold protein YncE [General function prediction only]; |
1-325 |
2.34e-15 |
|
DNA-binding beta-propeller fold protein YncE [General function prediction only];
Pssm-ID: 442618 [Multi-domain] Cd Length: 237 Bit Score: 74.73 E-value: 2.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021414 1 MNLRPLAPLFLALLAGCSQQPPLRGSGDLGVLIERADGSVQILDGTAKTSLARVEGLGDLSHASLVFS-RDQRYAYVFGR 79
Cdd:COG3391 8 LVAVLLAVLALAALAVAVAALGLGGGGPLLAAASGGVVGAAVGGGGVALLAGLGLGAAAVADADGADAgADGRRLYVANS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021414 80 DGG-LTRLDLLAQRIDKRLIQGGNSIGGAISQDGRLVAVSNYEPGGVKVFDSRTLELVAEIPatrlpgqdrnsrvvglvd 158
Cdd:COG3391 88 GSGrVSVIDLATGKVVATIPVGGGPRGLAVDPDGGRLYVADSGNGRVSVIDTATGKVVATIP------------------ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021414 159 apgqrfvfslfdsgeiwiadfsqgdtprltrfrdVGKQPYDALISPDGRYYMAGLFGEDGMAQLdlwhpergvrrvlgdy 238
Cdd:COG3391 150 ----------------------------------VGAGPHGIAVDPDGKRLYVANSGSNTVSVI---------------- 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021414 239 grgqrklpvykmphlegwtiasdqafvpavghhqVLVLDARDWKQTDAIDVAGQPVFVMTRPDDRQIWV-----NFAYPD 313
Cdd:COG3391 180 ----------------------------------VSVIDTATGKVVATIPVGGGPVGVAVSPDGRRLYVanrgsNTSNGG 225
|
330
....*....|..
gi 501021414 314 NDKVQVIDSETH 325
Cdd:COG3391 226 SNTVSVIDLATL 237
|
|
| YncE |
COG3391 |
DNA-binding beta-propeller fold protein YncE [General function prediction only]; |
246-384 |
5.01e-14 |
|
DNA-binding beta-propeller fold protein YncE [General function prediction only];
Pssm-ID: 442618 [Multi-domain] Cd Length: 237 Bit Score: 70.88 E-value: 5.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021414 246 PVYKMPHLEGWTIASDQAFVPAVGHHQVLVLDARDWKQTDAIDVAGQPVFVMTRPDDRQIWVnfAYPDNDKVQVIDSETH 325
Cdd:COG3391 65 AAVADADGADAGADGRRLYVANSGSGRVSVIDLATGKVVATIPVGGGPRGLAVDPDGGRLYV--ADSGNGRVSVIDTATG 142
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501021414 326 EVIETLRPGPGVLHMEFSGRGDQVWISVRDADQ----VQVWDPYRLERIGSLP-ARSPSGIFFS 384
Cdd:COG3391 143 KVVATIPVGAGPHGIAVDPDGKRLYVANSGSNTvsviVSVIDTATGKVVATIPvGGGPVGVAVS 206
|
|
| YncE |
COG3391 |
DNA-binding beta-propeller fold protein YncE [General function prediction only]; |
239-364 |
1.89e-11 |
|
DNA-binding beta-propeller fold protein YncE [General function prediction only];
Pssm-ID: 442618 [Multi-domain] Cd Length: 237 Bit Score: 63.56 E-value: 1.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021414 239 GRGQRKLPVYKMPHLEGWTIASDQAFVPAVGHHQVLVLDARDWKQTDAIDVAGQPVFVMTRPDDRQIWVnfAYPDNDK-- 316
Cdd:COG3391 100 GKVVATIPVGGGPRGLAVDPDGGRLYVADSGNGRVSVIDTATGKVVATIPVGAGPHGIAVDPDGKRLYV--ANSGSNTvs 177
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 501021414 317 --VQVIDSETHEVIETLRPGPGVLHMEFSGRGDQVWI-------SVRDADQVQVWDP 364
Cdd:COG3391 178 viVSVIDTATGKVVATIPVGGGPVGVAVSPDGRRLYVanrgsntSNGGSNTVSVIDL 234
|
|
| YncE |
COG3391 |
DNA-binding beta-propeller fold protein YncE [General function prediction only]; |
255-390 |
9.31e-09 |
|
DNA-binding beta-propeller fold protein YncE [General function prediction only];
Pssm-ID: 442618 [Multi-domain] Cd Length: 237 Bit Score: 55.47 E-value: 9.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021414 255 GWTIASDQAFVPAVGHHQVLVLDARDWKQTDAIDVAGQPvfvmTRPDDRQIWVnfAYPDNDKVQVIDSETHEVIETLRPG 334
Cdd:COG3391 36 LLAAASGGVVGAAVGGGGVALLAGLGLGAAAVADADGAD----AGADGRRLYV--ANSGSGRVSVIDLATGKVVATIPVG 109
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 501021414 335 PGVLHMEFSGRGDQVWISVRDADQVQVWDPYRLERIGSLPA-RSPSGIFFSHRAQHI 390
Cdd:COG3391 110 GGPRGLAVDPDGGRLYVADSGNGRVSVIDTATGKVVATIPVgAGPHGIAVDPDGKRL 166
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
3-377 |
9.42e-09 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 56.84 E-value: 9.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021414 3 LRPLAPLFLALLAGCSQQPPLRGSGDLGVLIERADGSVQILDGTAKTSLARVEGLGDLSHASLVFSRDQRYAYVFGRDGG 82
Cdd:COG2319 22 AAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021414 83 LTRLDLLAQRIDKRLIQGGNSIGG-AISQDGRLVAVSNYEpGGVKVFDSRTLELVAEIPAtrlpgqdRNSRVVGLVDAPG 161
Cdd:COG2319 102 VRLWDLATGLLLRTLTGHTGAVRSvAFSPDGKTLASGSAD-GTVRLWDLATGKLLRTLTG-------HSGAVTSVAFSPD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021414 162 QRFVFSLFDSGEIWIADFSQGDtpRLTRFRDVGKQPYDALISPDGRYYMAGlfGEDGMAQldLWHPERG-VRRVLGDYGR 240
Cdd:COG2319 174 GKLLASGSDDGTVRLWDLATGK--LLRTLTGHTGAVRSVAFSPDGKLLASG--SADGTVR--LWDLATGkLLRTLTGHSG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021414 241 gqrklPVYKM---PhlEGWTIASdqafvpAVGHHQVLVLDARDWKQTDAIDVAGQPVF-VMTRPDDRQIwvnfAYPDNDK 316
Cdd:COG2319 248 -----SVRSVafsP--DGRLLAS------GSADGTVRLWDLATGELLRTLTGHSGGVNsVAFSPDGKLL----ASGSDDG 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501021414 317 -VQVIDSETHEVIETLRPGPG-VLHMEFSGRGDQVwISVRDADQVQVWDPYRLERIGSLPARS 377
Cdd:COG2319 311 tVRLWDLATGKLLRTLTGHTGaVRSVAFSPDGKTL-ASGSDDGTVRLWDLATGELLRTLTGHT 372
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
36-228 |
8.41e-08 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 53.76 E-value: 8.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021414 36 ADGSVQILDGTAKTSLARVEGLGDLSHaSLVFSRDQRYAYVFGRDGGLTRLDLLAQRIDKRLIQGGNSIGG-AISQDGRL 114
Cdd:COG2319 224 ADGTVRLWDLATGKLLRTLTGHSGSVR-SVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSvAFSPDGKL 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021414 115 VAVSNYEpGGVKVFDSRTLELVAEIPAtrlpgqdRNSRVVGLVDAPGQRFVFSLFDSGEIWIADFSQGdtPRLTRFRDVG 194
Cdd:COG2319 303 LASGSDD-GTVRLWDLATGKLLRTLTG-------HTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATG--ELLRTLTGHT 372
|
170 180 190
....*....|....*....|....*....|....
gi 501021414 195 KQPYDALISPDGRYYMAGlfGEDGMAQldLWHPE 228
Cdd:COG2319 373 GAVTSVAFSPDGRTLASG--SADGTVR--LWDLA 402
|
|
| PQQ_ABC_repeats |
TIGR03866 |
PQQ-dependent catabolism-associated beta-propeller protein; Members of this protein family ... |
259-380 |
2.12e-05 |
|
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: 45.80 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021414 259 ASDQAFVPAVGHHQVLVLDARDWKQTDAIDVAGQPVFVMTRPDDRQIWVnfAYPDNDKVQVIDSETHEVIETLRPGPGVL 338
Cdd:TIGR03866 9 AAETAYVSNEKDNTISVIDTATLKVTRTFPVGQRPRGITFSKDGKLLYV--CASDSDTIQVIDPATGEVLHTLPSGPDPE 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 501021414 339 HMEFSGRGDQVWISVRDADQVQVWDPYRLERIGSLP--------ARSPSG 380
Cdd:TIGR03866 87 QFALHPNGKILYIANEDDALVTVIDIETRKVLAQIDvgvepegmAVSPDG 136
|
|
| PQQ_ABC_repeats |
TIGR03866 |
PQQ-dependent catabolism-associated beta-propeller protein; Members of this protein family ... |
65-343 |
4.82e-04 |
|
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: 41.56 E-value: 4.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021414 65 LVFSRDQRYAYVFGRDGGLTR-LDLLAQRIDKRLIQGGNSIGGAISQDGRLVAVSNYEPGGVKVFDSRTLELVAEIPATR 143
Cdd:TIGR03866 46 ITFSKDGKLLYVCASDSDTIQvIDPATGEVLHTLPSGPDPEQFALHPNGKILYIANEDDALVTVIDIETRKVLAQIDVGV 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021414 144 LPGqdrnsrvvGLVDAPGQRFVFSLFDSGEI--WIadfsqgDTPRLTRFRD--VGKQPYDALISPDGRYymaglfgedgm 219
Cdd:TIGR03866 126 EPE--------GMAVSPDGKIVVNTSETTNMahWI------DTATYEIVDNtlVDARPRFAEFTADGKE----------- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021414 220 aqldLWhpergvrrvlgdygrgqrklpvykmphlegwtiASDQafvpaVGHhQVLVLD--ARDWKQTDAIDVAG------ 291
Cdd:TIGR03866 181 ----LW---------------------------------VSSE-----IGG-TVTVIDvaTRKVIKKITFAIPGvhpekv 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 501021414 292 QPVFVMTRPDDRQIWVNFAyPDNdKVQVIDSETHEVIETLRPGPGVLHMEFS 343
Cdd:TIGR03866 218 QPVGIKLTKDGKTAFVALG-PAN-RVAVVDAKTYEVLDYLLVGQRVWQLAFT 267
|
|
| Vgb |
COG4257 |
Streptogramin lyase [Defense mechanisms]; |
107-374 |
5.18e-04 |
|
Streptogramin lyase [Defense mechanisms];
Pssm-ID: 443399 [Multi-domain] Cd Length: 270 Bit Score: 41.54 E-value: 5.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021414 107 AISQDGRlVAVSNYEPGGVKVFDSRTLElVAEIPATRlpgqdrNSRVVGLVDAPgqrfvfslfdSGEIWIADFSQG---- 182
Cdd:COG4257 23 AVDPDGA-VWFTDQGGGRIGRLDPATGE-FTEYPLGG------GSGPHGIAVDP----------DGNLWFTDNGNNrigr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021414 183 ---DTPRLTRFR--DVGKQPYDALISPDGRYYMAGlFGEDGMAQLDlwhPERGVRRVLGDYGRGQRklpvykmPHleGWT 257
Cdd:COG4257 85 idpKTGEITTFAlpGGGSNPHGIAFDPDGNLWFTD-QGGNRIGRLD---PATGEVTEFPLPTGGAG-------PY--GIA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021414 258 IASDQA-FVPAVGHHQVLVLDARD--WKQTDAIDVAGQPVFVMTRPDDRqIWVnfAYPDNDKVQVIDSETHEVIETLRPG 334
Cdd:COG4257 152 VDPDGNlWVTDFGANAIGRIDPDTgtLTEYALPTPGAGPRGLAVDPDGN-LWV--ADTGSGRIGRFDPKTGTVTEYPLPG 228
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 501021414 335 PGVL--HMEFSGRGDqVWISVRDADQVQVWDPYRLERIGSLP 374
Cdd:COG4257 229 GGARpyGVAVDGDGR-VWFAESGANRIVRFDPDTELTEYVLP 269
|
|
| Pgl |
COG2706 |
6-phosphogluconolactonase, cycloisomerase 2 family [Carbohydrate transport and metabolism]; |
65-140 |
2.99e-03 |
|
6-phosphogluconolactonase, cycloisomerase 2 family [Carbohydrate transport and metabolism];
Pssm-ID: 442025 [Multi-domain] Cd Length: 352 Bit Score: 39.50 E-value: 2.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021414 65 LVFSRDQRYAYVFG-RDGGLTRLDLLAQRIDKRLIQ---------GGNSIGGAI--SQDGRLVAVSNYEPGGVKVF---- 128
Cdd:COG2706 203 LAFHPNGRFAYVINeLDSTVSVYAYDAATGTLTLIQtvstlpedfTGENWAADIhiSPDGRFLYVSNRGHNSIAVFaida 282
|
90
....*....|..
gi 501021414 129 DSRTLELVAEIP 140
Cdd:COG2706 283 DGGKLTLVGHVP 294
|
|
| Lactonase |
pfam10282 |
Lactonase, 7-bladed beta-propeller; This entry contains bacterial 6-phosphogluconolactonases ... |
43-129 |
5.55e-03 |
|
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: 38.36 E-value: 5.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021414 43 LDGTAK--TSLARVEGLGDLSHasLVFSRDQRYAYVFGR---DGGLTRLDLLAQR-----IDKRLIQGGNSIGGAISQDG 112
Cdd:pfam10282 20 LDTETGalTLLGLVAEVGNPSY--LALSPDGRTLYAVNEegdQGGVAAFRIDPDSgaltlLNQVPTGGASPCHLSVDPDG 97
|
90
....*....|....*..
gi 501021414 113 RLVAVSNYEPGGVKVFD 129
Cdd:pfam10282 98 RFLFVANYHGGSVSVFP 114
|
|
| |
