|
Name |
Accession |
Description |
Interval |
E-value |
| 8prop_heme-binding_NirN |
cd20777 |
eight-bladed heme d1-binding beta-propeller domain in dihydro-heme d1 dehydrogenase NirN; The ... |
100-483 |
0e+00 |
|
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: 709.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 100 PQWSAENIRASQVQPHPLATLPSRPRFEADPLNLFVVVESGDHHVTILDGDRFEPIARFPSRYALHGGPKFSPDGRLVYF 179
Cdd:cd20777 1 PQWTAADIRASREVPPPAATLPDRPVFGADPLNLFVVVESGDHHVTVLDGDRFEPLARFPTRFALHGGPKFSPDGRFVYF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 180 ASRDGWVTLYDLYNLKVVAEVRAGLNTRNLAVSDDGRWVLVGNYLPGNLVLLDARDLSLVQVIPAADAQGQASRVSAVYT 259
Cdd:cd20777 81 ASRDGWVTKYDLWNLKVVAEVRAGLNTRNLAVSSDGRYVAVANYLPHTLVLLDARDLSLLKVIPAADAQGRSSRVSAVYD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 260 APPRHSFVVALKDVHELWELPYANGK---------------------PVAPKRLAVADYLDDFSFSPDYRYLLGSSRQAR 318
Cdd:cd20777 161 APPRRSFVVALKDVPELWELSYDEGAdpvpiglvhdflyeegaaspgFFAPRRIALPAPLDDFFFDPDYRNLLGASRQGG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 319 GGEVIELDSGARVASIPLSGMPHLGSGIYWKRDGRWVFATPNISCGVISVIDLQNWKPLKEIVTDGPGFFMRSHADSPYA 398
Cdd:cd20777 241 GGQVIDLDVGRVIASLPLSGMPHLGSGIYWKRDGRRVMATPNLSRGVISVIDLQTWAIVKEIPTPGPGFFMRSHENSPYA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 399 WTDTFLGKKHDEILLIDKQTLEIAHRLRPSPGKVAGHVEFTRDGRYALLSVWDRDGALVVYDAHSLEEVKRLPMNKPSGK 478
Cdd:cd20777 321 WADVFMGPKRDKLHLIDKQTLEIVKTLRPEPGKTAAHVEFTRDGRYALASVWEDDGALIVYDAHTLKEVKRLPMNKPSGK 400
|
....*
gi 489175324 479 YNVGN 483
Cdd:cd20777 401 YNVWN 405
|
|
| Cytochrom_D1 |
pfam02239 |
Cytochrome D1 heme domain; Cytochrome cd1 (nitrite reductase) catalyzes the conversion of ... |
128-484 |
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: 564.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 128 ADPLNLFVVVESGDHHVTILDGDRFEPIARFPSRYALHGGPKFSPDGRLVYFASRDGWVTLYDLYNLKVVAEVRAGLNTR 207
Cdd:pfam02239 1 RDLGNLFVVTERDAGSVALLDGDRKEILARVDTGYALHISRMFSSDGRYVYVIGRDGGLTKIDLWNQEIVAEVRQGGNAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 208 NLAVSDDGRWVLVGNYLPGNLVLLDARDLSLVQVIPAADAQGQ--ASRVSAVYTAPPRHSFVVALKDVHELWELPYANGK 285
Cdd:pfam02239 81 SVATSYDGRYVIVGNYWPGQYVIMDGRTLELVKVIPARGMTGDspESRVAAIVASPGRPEFVVNLKDTGEIWLVDYSDGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 286 PVAPKRLAVADYLDDFSFSPDYRYLLG---------SSRQARGGEVIELDSGARVASIPLSGMPHLGSGIYWKRDGRWVF 356
Cdd:pfam02239 161 NLKTTFIEAAKFLHDGGFDPDGRYFMAaanasdkiaVWDTKRGKLVALLDYGKTPHPGPGANMPHLEGGPVWTTSHLGDF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 357 ATPNISCGVISVIDLQNWKPLKEIVTDGPGFFMRSHADSPYAWTDTFLGKKHDEILLIDKQTLEIAHRLRPSPGKVAGHV 436
Cdd:pfam02239 241 VTPLIGTDPVLVHDLQAWKQVKEIDVAGGGLFVKTHPDSRYLWVDTFLNPDNDSVAVIDSETLEKVLTLAPWPGLVVVHM 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 489175324 437 EFTRDGRYALLSVWDRDGALVVYDAHSLEEVKRLPMNKPSGKYNVGNK 484
Cdd:pfam02239 321 EFNKRGDEVWLSVWDGKGALVVYDDKTLKLKKVIPLNTPSGKFNVYNT 368
|
|
| YncE |
COG3391 |
DNA-binding beta-propeller fold protein YncE [General function prediction only]; |
115-374 |
1.95e-14 |
|
DNA-binding beta-propeller fold protein YncE [General function prediction only];
Pssm-ID: 442618 [Multi-domain] Cd Length: 237 Bit Score: 72.80 E-value: 1.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 115 HPLATLPSRPRFEADPLNLFVVVESGDHHVTILDGDRFEPIARFPSRYALHGGPKFSPDGRLVYFA-SRDGWVTLYDLYN 193
Cdd:COG3391 20 ALAVAVAALGLGGGGPLLAAASGGVVGAAVGGGGVALLAGLGLGAAAVADADGADAGADGRRLYVAnSGSGRVSVIDLAT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 194 LKVVAEVRAGLNTRNLAVSDDGRWVLVGNYLPGNLVLLDARDLSLVQVIPaadaqgqasrvsavytapprhsfvvalkdv 273
Cdd:COG3391 100 GKVVATIPVGGGPRGLAVDPDGGRLYVADSGNGRVSVIDTATGKVVATIP------------------------------ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 274 helwelpyangkpvapkrlaVADYLDDFSFSPDYRYLLGSSRQARGG----EVIELDSGARVASIPLSGMPHlgsGIYWK 349
Cdd:COG3391 150 --------------------VGAGPHGIAVDPDGKRLYVANSGSNTVsvivSVIDTATGKVVATIPVGGGPV---GVAVS 206
|
250 260 270
....*....|....*....|....*....|.
gi 489175324 350 RDGRWVFAT------PNISCGVISVIDLQNW 374
Cdd:COG3391 207 PDGRRLYVAnrgsntSNGGSNTVSVIDLATL 237
|
|
| CccA |
COG2010 |
Cytochrome c, mono- and diheme variants [Energy production and conversion]; |
21-79 |
4.30e-13 |
|
Cytochrome c, mono- and diheme variants [Energy production and conversion];
Pssm-ID: 441613 [Multi-domain] Cd Length: 169 Bit Score: 67.28 E-value: 4.30e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489175324 21 APGEALYRQHCQACHGAGRLGGSG--PTLLPESLSRLKPAQAREVILHGRPATQMAGFAGQ 79
Cdd:COG2010 90 ARGKALYEQNCAACHGADGKGGLGaaPNLTDDALYGGDPEALVETILNGRPGGAMPAFGGQ 150
|
|
| Cytochrome_CBB3 |
pfam13442 |
Cytochrome C oxidase, cbb3-type, subunit III; |
21-79 |
2.97e-08 |
|
Cytochrome C oxidase, cbb3-type, subunit III;
Pssm-ID: 463879 [Multi-domain] Cd Length: 67 Bit Score: 50.48 E-value: 2.97e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 489175324 21 APGEALYRQHCQACHGAgrlGGSGPTLLPESLSrlkPAQAREVILHGRPAtqMAGFAGQ 79
Cdd:pfam13442 4 AAGEALYAANCASCHGT---GGAGPSLAGRALP---PEALVDIIRNGKGA--MPAFGGD 54
|
|
| PQQ_ABC_repeats |
TIGR03866 |
PQQ-dependent catabolism-associated beta-propeller protein; Members of this protein family ... |
117-220 |
4.81e-07 |
|
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: 51.58 E-value: 4.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 117 LATLP--SRPR---FEADPLNLFVVVeSGDHHVTILDGDRFEPIARFPS-----RYALHggpkfsPDGRLVYFASR-DGW 185
Cdd:TIGR03866 34 TRTFPvgQRPRgitFSKDGKLLYVCA-SDSDTIQVIDPATGEVLHTLPSgpdpeQFALH------PNGKILYIANEdDAL 106
|
90 100 110
....*....|....*....|....*....|....*
gi 489175324 186 VTLYDLYNLKVVAEVRAGLNTRNLAVSDDGRWVLV 220
Cdd:TIGR03866 107 VTVIDIETRKVLAQIDVGVEPEGMAVSPDGKIVVN 141
|
|
| PRK14486 |
PRK14486 |
putative bifunctional cbb3-type cytochrome c oxidase subunit II/cytochrome c; Provisional |
21-78 |
1.70e-04 |
|
putative bifunctional cbb3-type cytochrome c oxidase subunit II/cytochrome c; Provisional
Pssm-ID: 184704 [Multi-domain] Cd Length: 294 Bit Score: 43.65 E-value: 1.70e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 489175324 21 APGEALYRQHCQACHGAGRLGGSGPTLLPESLSRLKPAQAREVILHGRPATQMAGFAG 78
Cdd:PRK14486 216 AKGKALYDANCAACHGDEAQGQEGVALNDIDDGDLPDAAYFGMIKGGSDAKGMPGFGG 273
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| 8prop_heme-binding_NirN |
cd20777 |
eight-bladed heme d1-binding beta-propeller domain in dihydro-heme d1 dehydrogenase NirN; The ... |
100-483 |
0e+00 |
|
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: 709.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 100 PQWSAENIRASQVQPHPLATLPSRPRFEADPLNLFVVVESGDHHVTILDGDRFEPIARFPSRYALHGGPKFSPDGRLVYF 179
Cdd:cd20777 1 PQWTAADIRASREVPPPAATLPDRPVFGADPLNLFVVVESGDHHVTVLDGDRFEPLARFPTRFALHGGPKFSPDGRFVYF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 180 ASRDGWVTLYDLYNLKVVAEVRAGLNTRNLAVSDDGRWVLVGNYLPGNLVLLDARDLSLVQVIPAADAQGQASRVSAVYT 259
Cdd:cd20777 81 ASRDGWVTKYDLWNLKVVAEVRAGLNTRNLAVSSDGRYVAVANYLPHTLVLLDARDLSLLKVIPAADAQGRSSRVSAVYD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 260 APPRHSFVVALKDVHELWELPYANGK---------------------PVAPKRLAVADYLDDFSFSPDYRYLLGSSRQAR 318
Cdd:cd20777 161 APPRRSFVVALKDVPELWELSYDEGAdpvpiglvhdflyeegaaspgFFAPRRIALPAPLDDFFFDPDYRNLLGASRQGG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 319 GGEVIELDSGARVASIPLSGMPHLGSGIYWKRDGRWVFATPNISCGVISVIDLQNWKPLKEIVTDGPGFFMRSHADSPYA 398
Cdd:cd20777 241 GGQVIDLDVGRVIASLPLSGMPHLGSGIYWKRDGRRVMATPNLSRGVISVIDLQTWAIVKEIPTPGPGFFMRSHENSPYA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 399 WTDTFLGKKHDEILLIDKQTLEIAHRLRPSPGKVAGHVEFTRDGRYALLSVWDRDGALVVYDAHSLEEVKRLPMNKPSGK 478
Cdd:cd20777 321 WADVFMGPKRDKLHLIDKQTLEIVKTLRPEPGKTAAHVEFTRDGRYALASVWEDDGALIVYDAHTLKEVKRLPMNKPSGK 400
|
....*
gi 489175324 479 YNVGN 483
Cdd:cd20777 401 YNVWN 405
|
|
| Cytochrom_D1 |
pfam02239 |
Cytochrome D1 heme domain; Cytochrome cd1 (nitrite reductase) catalyzes the conversion of ... |
128-484 |
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: 564.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 128 ADPLNLFVVVESGDHHVTILDGDRFEPIARFPSRYALHGGPKFSPDGRLVYFASRDGWVTLYDLYNLKVVAEVRAGLNTR 207
Cdd:pfam02239 1 RDLGNLFVVTERDAGSVALLDGDRKEILARVDTGYALHISRMFSSDGRYVYVIGRDGGLTKIDLWNQEIVAEVRQGGNAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 208 NLAVSDDGRWVLVGNYLPGNLVLLDARDLSLVQVIPAADAQGQ--ASRVSAVYTAPPRHSFVVALKDVHELWELPYANGK 285
Cdd:pfam02239 81 SVATSYDGRYVIVGNYWPGQYVIMDGRTLELVKVIPARGMTGDspESRVAAIVASPGRPEFVVNLKDTGEIWLVDYSDGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 286 PVAPKRLAVADYLDDFSFSPDYRYLLG---------SSRQARGGEVIELDSGARVASIPLSGMPHLGSGIYWKRDGRWVF 356
Cdd:pfam02239 161 NLKTTFIEAAKFLHDGGFDPDGRYFMAaanasdkiaVWDTKRGKLVALLDYGKTPHPGPGANMPHLEGGPVWTTSHLGDF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 357 ATPNISCGVISVIDLQNWKPLKEIVTDGPGFFMRSHADSPYAWTDTFLGKKHDEILLIDKQTLEIAHRLRPSPGKVAGHV 436
Cdd:pfam02239 241 VTPLIGTDPVLVHDLQAWKQVKEIDVAGGGLFVKTHPDSRYLWVDTFLNPDNDSVAVIDSETLEKVLTLAPWPGLVVVHM 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 489175324 437 EFTRDGRYALLSVWDRDGALVVYDAHSLEEVKRLPMNKPSGKYNVGNK 484
Cdd:pfam02239 321 EFNKRGDEVWLSVWDGKGALVVYDDKTLKLKKVIPLNTPSGKFNVYNT 368
|
|
| 8prop_heme_binding_protein |
cd20718 |
eight-bladed beta-propeller heme-binding domain in cytochrome cd1 and similar proteins; ... |
105-482 |
6.20e-179 |
|
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: 506.49 E-value: 6.20e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 105 ENIRASQVQPHPLATLPSRPRFEADPLNLFVVVESGDHHVTILDGDRFEPIARFPSRYALHGGPKFSPDGRLVYFASRDG 184
Cdd:cd20718 1 EDIKKSLEVLVPERELPPVAYGIWDLENLMVVVERDAGSVLVIDGSTHEVLGRIDDGGAQVHVVVFSPDGRFAYVISRDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 185 WVTLYDLYNLKVVAEVRAGLNTRNLAVSDDGRWVLVGNYLPGNLVLLDARDLSLVQVIPAADAQGQ---ASRVSAVYTAP 261
Cdd:cd20718 81 WLTKIDLYTLRPVASIRIGVNSRGIALSDDGKYVIAGNYEPGHVVILDADTLEPLKVIPTTGVNDDgiiESRVGAILETP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 262 PRHSFVVALKDVHELWELPYANGK-PVAPKRLAVADYLDDFSFSPDYRYLLGSSRQARGGEVIELDSGARVASIPLSGMP 340
Cdd:cd20718 161 PGPYFLVALKDAGSVWVIDYSDPDgNKVTDIGNIGRPLHDAFLDPDGRYFIVASQGSNTMWVLDLKTGKVVARIPTGKTP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 341 HLGSGIYWKRdgRWVFATPNISCGVISVIDLQNWKPLKEIVTDGPGFFMRSHADSPYAWTDTFLG-KKHDEILLIDKQTL 419
Cdd:cd20718 241 HPGPGATWGR--KGVTATPHLGEGIVTVWDLDTWKPVKYIPTPGPGRFVRTHPSSPYVWADTVFGpENADEIYVIDKETL 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489175324 420 EIAHRLRPSPGKVAGHVEFTRDGRYALLSVWDrDGALVVYDAHSLEEVKRLPMNKPSGKYNVG 482
Cdd:cd20718 319 KVVKTLIPKPGKRALHPEFTRDGKYVYVSVWD-GGEVVVYDAETLELVKRIPAETPTGIFNVG 380
|
|
| 8prop_hemeD1_cyt_cd1-like |
cd20784 |
cytochrome cd1 nitrate reductase eight-bladed heme d1-binding beta-propeller domain and ... |
100-484 |
2.62e-127 |
|
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: 374.65 E-value: 2.62e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 100 PQWSAENIRAS-QVQPHPLATLPSRprfeaDPLNLFVVVESGDHHVTILDGDRfePIARFPSRyALHGGPKFSPDGRLVY 178
Cdd:cd20784 2 IRWSKEDIKKSiTIFNDKPKPLEIK-----DIENITLVVERGGGKVWVMEGFR--VLDKFDFG-NVHGGIKFSPSGKKIY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 179 FASRDGWVTLYDLYNLKVVAEVRAGLNTRNLAVSDDGRWVLVGNYLPGNLVLLDARDLSLVQVIPaadaqgQASRVSAVY 258
Cdd:cd20784 74 VPSRDGWIGKYDLKEGRETGKVRACINLRNIALSRDGKYLAAACLLPENLVILDTKTLKPVKVIK------LDGKISAVY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 259 TAPPRHSFVVALKDVHELWELPYANGKPvapKRLAVADYLDDFSFSPDYRYLLGSSRQARGGEVIELDSGARVASIPLSG 338
Cdd:cd20784 148 ELYSKDKAIFTFRDKPKLGFLDTKTLKI---EYIKIKEPFEDFFIDPFEEYIIGTSRKGKKLYVYSLKDLKKVFEHKMEG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 339 MPHLGSGIYWKRDGRWVFATPNISCGVISVIDLQNWKPLKEIVTDGPGFFMRSHADSPYAWTDTflGKkhDEILLIDKQT 418
Cdd:cd20784 225 MPHLFSATFWYKKGKFYFATPHIKKPYVSIWKMYDWKFVKEIDLGGDGFFVRTHPKTPYLWVDN--GT--DKLVLIDKKD 300
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489175324 419 LEIAHRLrPSPGKVAGHVEFTRDGRYALLSVWDRDGALVVYDAHSLEEVKRLPMNKPSGKYNVGNK 484
Cdd:cd20784 301 LSVKKIT-PPKGKKAIHTEFSGDGKYAYVSIYEKDGALVVYDTFTLKELKRYPANIPVGKYNFVNK 365
|
|
| 8prop_hemeD1_cyt_cd1-like |
cd20783 |
eight-bladed heme d1-binding beta-propeller domain and similar proteins; Cytochrome cd1 (cyt ... |
105-482 |
7.85e-82 |
|
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: 258.86 E-value: 7.85e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 105 ENIRASQVQPHPLATLPSRPRFEADPLNLFVVVESGDHHVTILDGDRFEPIARFPSRYALHGgPKFSP-DGRLVYFASRD 183
Cdd:cd20783 1 EDIAASREVLVPESELPAEPTHDGNVDNLLLVTEREARSIAVIDGDTHTLLGHIEAGYRAHG-YTFSPtDGRWAYNLGRD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 184 GWVTLYDLYNLKVVAEVRAGLNTRNLAVSDDGRWVLVGNYLPGNLVLLDARDLSLVQVIPAADAQGQ----ASRVSAVY- 258
Cdd:cd20783 80 GWLYKIDLYSLQPVAKVRVGLDARGIAISDDGKYLIAGNYIPATAVILDAKTLEPLKVIDTSGVDPDgkmvDSRVASVNd 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 259 TAPPRHS--FVVALKDVHELWELPYAngKPVAP--KRLAVADYLDDFSFSPDYRYLLGSSRQARGGEVIELDSGARVASI 334
Cdd:cd20783 160 VAPDLVGpyFLLALKEAGQVWRIDYS--KPDFPitKVENVGHILHDGFLSPDNKTFYLASQTDNWMAAIDVATMKIVAKI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 335 PLSGMPHLGSGIYWKRDGRWVFATPNISCGVISVIDLQNWKPLKEIVTDGPGFFMRSHADSPYAWTDTFLGKKHDEILLI 414
Cdd:cd20783 238 PTGDKPHPGSGAVWEADGKEYAATVHAGEGKVTIWDLDTNEIVGEVPTSGPGLFIRTTENMPYVWADSMFAPEPNEITVH 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489175324 415 DKQTLEIAHRlRPSPGKVAGHVEFTRDGRYALLSVWDrDGALVVYDAHSLEEVKRLP-MNKPSGKYNVG 482
Cdd:cd20783 318 EKAPPFKVVK-RITDGTRTLHPEPTADGKYVYVSDWD-GNVVRVYDAETLELVKEITgITTPTGIFNTS 384
|
|
| 8prop_hemeD1_NiR_alpha_gamma |
cd20781 |
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NiR ... |
96-485 |
1.96e-67 |
|
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: 223.04 E-value: 1.96e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 96 PPREPQWSAENIRASQ---VQPhplATLPSRPRFEADPLNLFVVVESGDHHVTILDGDRFEPIARFPSRYALH------- 165
Cdd:cd20781 4 PPVPPEMSLALMKERHkvyVEP---KDYPTKPLHGRNWENFFVVIERDAGKVAIIDGDKKEVVAHIDTGYAVHvlkaseh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 166 -GGPKFSPDGRLVYFASRDGWVTLYDLY---NLKVVAEVRAGLNTRNLAVSDDGRWVLVGNYLPGNLVLLDARDLSLVQV 241
Cdd:cd20781 81 hKVEKAKNPGRFWYTMGRDGKLTKIDLWqtpDKMLVAEVQIAYDARDVAVSGDGKYVIGGGYWPPHFVIVDAETMEPLKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 242 IPA--ADAQGQ---ASRVSAVYTAPPRHSFVVALKDVHELWELPYANGKPVAPKRLAVADYLDDFSFSPDYRYLLGSSRQ 316
Cdd:cd20781 161 VSTrgVNVDGEyvnESRVAAIYTTPNAPTFLVAVKELGQMWQVDYSDLDNLRIDQIDTAKFLHDGFFDPTGRYFQIAANA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 317 ARGGEVIELDSGARVASIPLSGMPHLGSGIYW--KRDGRwVFATPNISCGVISVI--------DlQNWKPLKEIVTDGPG 386
Cdd:cd20781 241 SNKMVVVDTKTRKLEAMIDTGKLPHPGPGANWidPKCGP-VGGTTHLGEGKVTVWgndpkghpD-QAWKICYEVETDGPG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 387 FFMRSHADSPYAWTDTflgKKHDE------ILLIDKQTLEIA--HRLRPSPGKVAGHVEFTRDGRYALLSVWDR------ 452
Cdd:cd20781 319 LFIRTHPNSDYVWADQ---TKHPEpevqqsVQVIDKKTREIVktIRVTEEEGYVAVHMEFNQDGTEVWVSVWNRkdskep 395
|
410 420 430
....*....|....*....|....*....|....
gi 489175324 453 DGALVVYDAHSLEEVKRLP-MNKPSGKYNVGNKI 485
Cdd:cd20781 396 NGEIVVYDAKTLEEKARIKgLYTPTGKFNVYNRV 429
|
|
| 8prop_hemeD1_cyt_cd1-like |
cd20782 |
cytochrome cd1 nitrate reductase eight-bladed heme d1-binding beta-propeller domain and ... |
105-479 |
1.02e-61 |
|
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: 207.33 E-value: 1.02e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 105 ENIRASQVQPHPLATLPSRPRFEADPLNLFVVVESGDHHVTILDGDRFEPIARF------PSRYALHGG-PKFSPDGRLV 177
Cdd:cd20782 20 EDIADSHEIHKEEEELPQEPQHDDDLRDLLVVAERRNASVSLVDTVNHERLGRIedvgraIHVIEFHRDlPENEREGAYA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 178 YFASRDGWVTLYDLYNLKVVAEVRAGLNTRNLAVSDDGRWVLVGNYLPGNLVLLDARDLSLVQVIPA----ADAQGQASR 253
Cdd:cd20782 100 YTQSRQGWVSKLDLFGGERVARVRAGTDARDIAVSRDSNYLIAGYYNPNHLVVVDAETMEPLKRIPThgvdPDGQSVESR 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 254 VSAVYTAPPRHSFVVALKDVHELWELPYANGKPVAPKRLAVADYLDDFSFSPDYRYLLGSSRQARGGEVIELDSGARVAS 333
Cdd:cd20782 180 VCTLYDVPGEGCFLAALKEAGQVWLIDYTQDDFPVVDEIDCGRTLHDGFFTPDGRYFMLASQTDNCMSVLDVEEREVVDR 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 334 IPLSGMPHLGSG-IYWKRDGRWvfaTPNISCGVISVIDLQNWKPLKEIVTDGPGFFMRSHADSPYAWTDTFL--GKKHDE 410
Cdd:cd20782 260 IPTAGVPHPGPGaLDPDRGLAF---TTHVGTDAVTAWDTETWEPEADIEVPGGGLFLRSHPDSDYVWGDVILddTDRLDQ 336
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489175324 411 -ILLIDKQTLEIAHRLRPSPGKVAG--HVEFTRDGRYALLSVWDrDGALVVYDAHS---LEEVKRLpmNKPSGKY 479
Cdd:cd20782 337 lIYAIDPDTLEVATVIDTSEWGEGRaiHPEFSRDGEKVYVSHWD-AGEILVFDSHTgelIEEIDGL--ETPTGKF 408
|
|
| 8prop_hemeD1_NirF |
cd20778 |
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirF; ... |
132-477 |
1.08e-59 |
|
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: 200.97 E-value: 1.08e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 132 NLFVVVESGDHHVTILDGDRFEPIARFPSRYAL-HGGPKFSPDGRLVYFASRDGWVTLYDLYNLKVVAEVRAGLNTRNLA 210
Cdd:cd20778 19 ALGVVVEREAGSVFVVDRSKHESLGRIEGLGNLsHATMVFSRDGRYAYVIGRDGGLSKVDLLTLKVVARVKQSGNSIGGA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 211 VSDDGRWVLVGNYLPGNLVLLDARDLSLVQVIPA-ADAQGQASRVSAVYTAPPRHsFVVALKDVHELWELPYAN-GKPVA 288
Cdd:cd20778 99 ISQDGRYVAVANYDPGGVKILDADTLKVLADIPAgSKGGGQRSRVVGLVDAPGNR-FIFSLMDADEIWVLDASDpDFPVV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 289 PKRLAVADYLDDFSFSPDYRY----LLGSS--------RQARGGEVIELDSGARVASIPLSGMPHLGSgiyWKRDGRWVF 356
Cdd:cd20778 178 KKFKDIGRMPYDALITPDGRYyiagLFNSDgvglldlwKPERGVRRILLDYGKGEEKLPVYKMPHLEG---WAVAGDKAF 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 357 aTPNISCGVISVIDLQNWKPLKEIVTDGPGFFMRSHADSPYAWTdTFLGKKHDEILLIDKQTLEIAHRLRpsPGKVAGHV 436
Cdd:cd20778 255 -VPAVGEHRVLVYDTNDWKFIKSIPLAGQPVFAVARPDGRYVWV-NFSGPDNDTVQVIDTKTLKVVKTLE--PGKRVLHM 330
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 489175324 437 EFTRDGRYALLSVWDRDgALVVYDAHSLEEVKRLPMNKPSG 477
Cdd:cd20778 331 EFTPRGEAVYISVNDDN-KVVVYDTRTFREIKEVPAKKPSG 370
|
|
| 8prop_hemeD1_cyt_cd1-like |
cd20785 |
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase and ... |
96-477 |
4.24e-59 |
|
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: 200.21 E-value: 4.24e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 96 PPREPQWSAENIRAS-QVQPHPLATLPSRPRFEADPLN-LFVVVESGDH------HVTILDGDRFEPIARFPSRYALHGg 167
Cdd:cd20785 2 PKRNPSWGLEDIRKSlEVLVADESTLPSKPTYAIDDIDdLMAVMARGRYgrgkgsKVVFFDGKTNRKVGEIPTGFAPHI- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 168 PKFSP-DGRLVYFASRDGWVTLYDLYNLKVVAEVRAGLNTRNLAVSDDGRWVLVGNYLPGNLVLLDARDLSLVQVIPAA- 245
Cdd:cd20785 81 MDFHPvNPRWAYVKTDTGEVYKIDLYSMQAVRSVKAGLNGPSLAVSRDGKYLAAGSFVPHTAVILDADTLEPLKYFELEg 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 246 -DAQG-QASRVSAVYTAPP-RHSFVVALKDVHELWELPYAngKPVAP--KRLAVADYLDDFSFSPDYRYLLGSSRQARGG 320
Cdd:cd20785 161 vDPDGkMVESDSGMITGTPyANYFAIALEQAGQVWIVDLD--KPGMPvtKIKNVGRHLHDAFLSPDGRYLMVASYDDNKN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 321 EVIELDSGARVASIPLSGMPHLGSGIYWKRDGRWV-FATpNI-SCG---VISVIDLQNWKPLKEIVTDGPGFFMRSHADS 395
Cdd:cd20785 239 AVIDLKEKKVVKKIPAGCQPHLGSGAVVKVGGRLLgFGT-NIgSCDdktVVTVWDMDTFEVVKQIPVSGPTESPAAHPNA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 396 PYAWTDTF-LGKKHDEILLIDKQTLEIAHRLrpspgKVAGHV---EFTRDGRYALLSVWDRDGALVVYDAHSLEEVKRLP 471
Cdd:cd20785 318 PYVAVDIVgKDPRARKIQLIDKNTLEVVKTL-----DVGGHShfpEYTADGDYLYVSAGYNGDRLVIYDSKTLKKVKEIP 392
|
....*.
gi 489175324 472 MNKPSG 477
Cdd:cd20785 393 MESPAG 398
|
|
| 8prop_hemeD1_NirS |
cd20779 |
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirS; ... |
94-481 |
3.03e-47 |
|
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: 169.35 E-value: 3.03e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 94 QAPPREPQWSAENIRASQVQPHPLATLPSRPRFEADPLNLFVVVESGDHHVTILDGDRFEPIARFPSRYALHgGPKFSPD 173
Cdd:cd20779 22 LPPPAPPEFGMADMKASWKVIVPVAKRPTKPEHKRNWENFFGVILRDAGQVAIIDGDTKEIVSIVDTGFAVH-ILRSSAS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 174 GRLVYFASRDGWVTLYDLYNLK--VVAEVRAGLNTRNLAVSD----DGRWVLVGNYLPGNLVLLDARDLSLVQVIPAA-- 245
Cdd:cd20779 101 GRYFYTIGRDGKVTMIDLWMKKptVVAEVKGCLDARSVDSSKykgfEDKYAIVGCYWPPQYVILDGLTLEPLKVVSTRgy 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 246 --DAQG--QASRVSAVYTAPPRHSFVVALKDVHELWELPYANGKPVAPKRLAVADYLDDFSFSPDYRYLLGSSRQARGGE 321
Cdd:cd20779 181 tyDTGEyhPEPRVASIVASHFDPEWVVNVKETGQVWLVDYSDLKNLKVTMIEAERFLHDGGWDHTKRYFLVAANARNKVV 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 322 VIELDSGARVASIPLSGMPHLGSGIYWKRD--GrWVFATPNISCGVISVI--DLQN-----WKPLKEIVTDGPG-FFMRS 391
Cdd:cd20779 261 VVDTKTKKLVALVETGIKPHPGRGANWVDPkyG-PVWATGHLGEGKIALIgtDPKGhpqyaWKVVRKIKLPGGGsLFIKT 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 392 HADSPYAWTDTFL---GKKHDEILLIDKQTLEIAHRLRPSPGKV-AGHVEFTRDGRYALLSVWDRD-GALVVYDAHSLEE 466
Cdd:cd20779 340 HPKSPWLWVDRTLnpdPKLARSVCVFDKKLLDKKYKCWPVADHGrAVHFEYNKAGDEVWVSVWDKKpGAIVVYDDKTLKE 419
|
410
....*....|....*...
gi 489175324 467 VKRL---PMNKPSGKYNV 481
Cdd:cd20779 420 KARItgdWLVTPTGKFNV 437
|
|
| 8prop_hemeD1_NiR_delta_epsilon |
cd20780 |
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NiR ... |
144-481 |
5.81e-37 |
|
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: 141.13 E-value: 5.81e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 144 VTILDGDRFEPIARFPSRYALHGGPKFSPDGRLVYFASRDGWVTLYDL--YNLKVVAEVRAGLNTRNLAVSDDGRWVLVG 221
Cdd:cd20780 62 VDFIDGTTGKVLSRHKAGFAVHVTVTNKRNPRYAYSISRSGRLTMFDLaaPGQPALASVQVGQESRGLAVSPDGKYVMAG 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 222 NYLPGNLVLLDARDLSLVQVIPAA-----DAQGQASRVSAVYTAPPRHSFVVALKDVHELWELPYAngKPVAPkrlAVAD 296
Cdd:cd20780 142 NYNPGGAVLCDAMTLEPLKVYDTSsvidpDGQIGPSRVASIADTPYGPYFAFALKDAGHVYIVDYS--KPDFP---IVGD 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 297 ------YLDDFSFSPDY---RYLLGSSRQARGGEVIELDSGARVASIPL--SGMPHLGSGIYW--KRDGRWVFATPNISC 363
Cdd:cd20780 217 ipnigkILHDAFLNEGEgfgRYLMIASQGSDVMGIVDFKTKNLAAKVYTgpKSKPHPGQGSSWynKGLGKQLHATVSMNV 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 364 GVISVIDlQNWKPLKEIVTDGPGFFMRSHADSPYAWTDTFLGK--KHDEILLIDKQTLEI----------AHRLRPSPGK 431
Cdd:cd20780 297 GDVVIWD-SNWDVVKHVPTAGGGLFVGTSEHTPYLWADCVLGGpdNYNKVHLINKQTLETdriikvgktkGTLIDAKTKK 375
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 489175324 432 VAG------HVEFTRDGRYALLSVWDRdGALVVYDAHSLEEVKRLP-MNKPSGKYNV 481
Cdd:cd20780 376 VLQtwdrllHAEPANHGKWTMISEWTT-GRIGIYESKTGKFVKYIEnLTTPTFTYSV 431
|
|
| YncE |
COG3391 |
DNA-binding beta-propeller fold protein YncE [General function prediction only]; |
115-374 |
1.95e-14 |
|
DNA-binding beta-propeller fold protein YncE [General function prediction only];
Pssm-ID: 442618 [Multi-domain] Cd Length: 237 Bit Score: 72.80 E-value: 1.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 115 HPLATLPSRPRFEADPLNLFVVVESGDHHVTILDGDRFEPIARFPSRYALHGGPKFSPDGRLVYFA-SRDGWVTLYDLYN 193
Cdd:COG3391 20 ALAVAVAALGLGGGGPLLAAASGGVVGAAVGGGGVALLAGLGLGAAAVADADGADAGADGRRLYVAnSGSGRVSVIDLAT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 194 LKVVAEVRAGLNTRNLAVSDDGRWVLVGNYLPGNLVLLDARDLSLVQVIPaadaqgqasrvsavytapprhsfvvalkdv 273
Cdd:COG3391 100 GKVVATIPVGGGPRGLAVDPDGGRLYVADSGNGRVSVIDTATGKVVATIP------------------------------ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 274 helwelpyangkpvapkrlaVADYLDDFSFSPDYRYLLGSSRQARGG----EVIELDSGARVASIPLSGMPHlgsGIYWK 349
Cdd:COG3391 150 --------------------VGAGPHGIAVDPDGKRLYVANSGSNTVsvivSVIDTATGKVVATIPVGGGPV---GVAVS 206
|
250 260 270
....*....|....*....|....*....|.
gi 489175324 350 RDGRWVFAT------PNISCGVISVIDLQNW 374
Cdd:COG3391 207 PDGRRLYVAnrgsntSNGGSNTVSVIDLATL 237
|
|
| CccA |
COG2010 |
Cytochrome c, mono- and diheme variants [Energy production and conversion]; |
21-79 |
4.30e-13 |
|
Cytochrome c, mono- and diheme variants [Energy production and conversion];
Pssm-ID: 441613 [Multi-domain] Cd Length: 169 Bit Score: 67.28 E-value: 4.30e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489175324 21 APGEALYRQHCQACHGAGRLGGSG--PTLLPESLSRLKPAQAREVILHGRPATQMAGFAGQ 79
Cdd:COG2010 90 ARGKALYEQNCAACHGADGKGGLGaaPNLTDDALYGGDPEALVETILNGRPGGAMPAFGGQ 150
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
170-463 |
3.67e-11 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 64.93 E-value: 3.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 170 FSPDGRLVYFASRDGWVTLYDLYNLKVVAEVRAGLNT-RNLAVSDDGRWVLVGNYlPGNLVLLDARDLSLVQVIpaadaQ 248
Cdd:COG2319 128 FSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAvTSVAFSPDGKLLASGSD-DGTVRLWDLATGKLLRTL-----T 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 249 GQASRVSAVYTAPPRHSFVVALKD--VHeLWELpyANGKPVAPKRLAvADYLDDFSFSPDYRYLLGSS--RQARggeVIE 324
Cdd:COG2319 202 GHTGAVRSVAFSPDGKLLASGSADgtVR-LWDL--ATGKLLRTLTGH-SGSVRSVAFSPDGRLLASGSadGTVR---LWD 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 325 LDSGARVASipLSGMPHLGSGIYWKRDGRWVFATPNIscGVISVIDLQNWKPLKEIvtdgpgffmRSHADSPY--AWT-- 400
Cdd:COG2319 275 LATGELLRT--LTGHSGGVNSVAFSPDGKLLASGSDD--GTVRLWDLATGKLLRTL---------TGHTGAVRsvAFSpd 341
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489175324 401 DTFL--GKKHDEILLIDKQTLEIAHRLRPSPGKVAGhVEFTRDGRYaLLSVwDRDGALVVYDAHS 463
Cdd:COG2319 342 GKTLasGSDDGTVRLWDLATGELLRTLTGHTGAVTS-VAFSPDGRT-LASG-SADGTVRLWDLAT 403
|
|
| YncE |
COG3391 |
DNA-binding beta-propeller fold protein YncE [General function prediction only]; |
229-464 |
5.28e-09 |
|
DNA-binding beta-propeller fold protein YncE [General function prediction only];
Pssm-ID: 442618 [Multi-domain] Cd Length: 237 Bit Score: 56.63 E-value: 5.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 229 VLLDARDLSLVQVIPAADAQGQASRVSAVYTAPPRHSFVVALKDVHELWELPYANGKPVAPKRLAVADYLDDFSFSPDYR 308
Cdd:COG3391 1 ALVASSLLVAVLLAVLALAALAVAVAALGLGGGGPLLAAASGGVVGAAVGGGGVALLAGLGLGAAAVADADGADAGADGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 309 YLLGSSRQARGGEVIELDSGARVASIPLSGMPHlgsGIYWKRDGRWVFATpNISCGVISVIDLQNWKPLKEIVTDGPGFF 388
Cdd:COG3391 81 RLYVANSGSGRVSVIDLATGKVVATIPVGGGPR---GLAVDPDGGRLYVA-DSGNGRVSVIDTATGKVVATIPVGAGPHG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 389 MRSHADSPYAW-TDTFLGKKHDEILLIDKQTLEIAHRLrpSPGKVAGHVEFTRDGRYALLSVWD------RDGALVVYDA 461
Cdd:COG3391 157 IAVDPDGKRLYvANSGSNTVSVIVSVIDTATGKVVATI--PVGGGPVGVAVSPDGRRLYVANRGsntsngGSNTVSVIDL 234
|
...
gi 489175324 462 HSL 464
Cdd:COG3391 235 ATL 237
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
134-315 |
1.85e-08 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 56.46 E-value: 1.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 134 FVVVESGDHHVTILDGDRFEPIARFPSRYALHGGPKFSPDGRLVYFASRDGWVTLYDLYNLKVVAEVRAGLNTRN-LAVS 212
Cdd:COG2319 218 LLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNsVAFS 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 213 DDGRWVLVGNYlPGNLVLLDARDLSLVQVIpaadaQGQASRVSAVYTAPPRHSFVVALKD--VHeLWELpyANGKPVAPK 290
Cdd:COG2319 298 PDGKLLASGSD-DGTVRLWDLATGKLLRTL-----TGHTGAVRSVAFSPDGKTLASGSDDgtVR-LWDL--ATGELLRTL 368
|
170 180
....*....|....*....|....*
gi 489175324 291 RlAVADYLDDFSFSPDYRYLLGSSR 315
Cdd:COG2319 369 T-GHTGAVTSVAFSPDGRTLASGSA 392
|
|
| Cytochrome_CBB3 |
pfam13442 |
Cytochrome C oxidase, cbb3-type, subunit III; |
21-79 |
2.97e-08 |
|
Cytochrome C oxidase, cbb3-type, subunit III;
Pssm-ID: 463879 [Multi-domain] Cd Length: 67 Bit Score: 50.48 E-value: 2.97e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 489175324 21 APGEALYRQHCQACHGAgrlGGSGPTLLPESLSrlkPAQAREVILHGRPAtqMAGFAGQ 79
Cdd:pfam13442 4 AAGEALYAANCASCHGT---GGAGPSLAGRALP---PEALVDIIRNGKGA--MPAFGGD 54
|
|
| PQQ_ABC_repeats |
TIGR03866 |
PQQ-dependent catabolism-associated beta-propeller protein; Members of this protein family ... |
117-220 |
4.81e-07 |
|
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: 51.58 E-value: 4.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 117 LATLP--SRPR---FEADPLNLFVVVeSGDHHVTILDGDRFEPIARFPS-----RYALHggpkfsPDGRLVYFASR-DGW 185
Cdd:TIGR03866 34 TRTFPvgQRPRgitFSKDGKLLYVCA-SDSDTIQVIDPATGEVLHTLPSgpdpeQFALH------PNGKILYIANEdDAL 106
|
90 100 110
....*....|....*....|....*....|....*
gi 489175324 186 VTLYDLYNLKVVAEVRAGLNTRNLAVSDDGRWVLV 220
Cdd:TIGR03866 107 VTVIDIETRKVLAQIDVGVEPEGMAVSPDGKIVVN 141
|
|
| Pgl |
COG2706 |
6-phosphogluconolactonase, cycloisomerase 2 family [Carbohydrate transport and metabolism]; |
170-358 |
1.89e-05 |
|
6-phosphogluconolactonase, cycloisomerase 2 family [Carbohydrate transport and metabolism];
Pssm-ID: 442025 [Multi-domain] Cd Length: 352 Bit Score: 46.82 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 170 FSPDGRLVYFASR--DGWVTLYDLY----NLKVVAEVRA-GLNTRNLAVSDDGRWVLVGNYLPGNLVLLD-ARDLSL--- 238
Cdd:COG2706 52 LSPDGRFLYAVNEvdDGGVSAFRIDpadgTLTLLNTVSSgGASPCHLSVDPDGRFLFVANYGGGSVSVFPiDADGSLgep 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 239 VQVI------PAADAQGqASRVSAVYTAP-PRHSFVVALKD--VHeLWELPYANGKPVAPKRLAVADYLD--DFSFSPDY 307
Cdd:COG2706 132 VQVIqhegsgPNPERQE-GPHAHSVVFDPdGRFLYVPDLGTdrIY-VYRLDPATGKLPEPPEVSLPPGSGprHLAFHPNG 209
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489175324 308 RYL-----LGS-----SRQARGGEVIELDsgaRVASIP--LSGmPHLGSGIYWKRDGRWVFAT 358
Cdd:COG2706 210 RFAyvineLDStvsvyAYDAATGTLTLIQ---TVSTLPedFTG-ENWAADIHISPDGRFLYVS 268
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
129-314 |
1.62e-04 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 43.48 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 129 DPLNLFVVVESGDHHVTILDGDRFEPIARFPSryalHGGP----KFSPDGRLVYFASRDGWVTLYDLYNLKVVA------ 198
Cdd:cd00200 102 SPDGRILSSSSRDKTIKVWDVETGKCLTTLRG----HTDWvnsvAFSPDGTFVASSSQDGTIKLWDLRTGKCVAtltght 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 199 -EVRAglntrnLAVSDDGRWVLVGNyLPGNLVLLDARDLSLVQVIpaadaQGQASRVSAVYTAPPRHSFVVALKDVH-EL 276
Cdd:cd00200 178 gEVNS------VAFSPDGEKLLSSS-SDGTIKLWDLSTGKCLGTL-----RGHENGVNSVAFSPDGYLLASGSEDGTiRV 245
|
170 180 190
....*....|....*....|....*....|....*....
gi 489175324 277 WELpyANGKPVapKRL-AVADYLDDFSFSPDYRYLLGSS 314
Cdd:cd00200 246 WDL--RTGECV--QTLsGHTNSVTSLAWSPDGKRLASGS 280
|
|
| PRK14486 |
PRK14486 |
putative bifunctional cbb3-type cytochrome c oxidase subunit II/cytochrome c; Provisional |
21-78 |
1.70e-04 |
|
putative bifunctional cbb3-type cytochrome c oxidase subunit II/cytochrome c; Provisional
Pssm-ID: 184704 [Multi-domain] Cd Length: 294 Bit Score: 43.65 E-value: 1.70e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 489175324 21 APGEALYRQHCQACHGAGRLGGSGPTLLPESLSRLKPAQAREVILHGRPATQMAGFAG 78
Cdd:PRK14486 216 AKGKALYDANCAACHGDEAQGQEGVALNDIDDGDLPDAAYFGMIKGGSDAKGMPGFGG 273
|
|
| Pgl |
COG2706 |
6-phosphogluconolactonase, cycloisomerase 2 family [Carbohydrate transport and metabolism]; |
114-235 |
4.28e-04 |
|
6-phosphogluconolactonase, cycloisomerase 2 family [Carbohydrate transport and metabolism];
Pssm-ID: 442025 [Multi-domain] Cd Length: 352 Bit Score: 42.59 E-value: 4.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 114 PHPLATLP--SRPR-FEADP-LNLFVVVESGDHHVTILDGD----RFEPIARF---PSRYALHGGP---KFSPDGRLVYF 179
Cdd:COG2706 188 EPPEVSLPpgSGPRhLAFHPnGRFAYVINELDSTVSVYAYDaatgTLTLIQTVstlPEDFTGENWAadiHISPDGRFLYV 267
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489175324 180 ASR-DGWVTLY----DLYNLKVVAEVR-AGLNTRNLAVSDDGRWVLVGNYLPGNLVLLdARD 235
Cdd:COG2706 268 SNRgHNSIAVFaidaDGGKLTLVGHVPtGGKWPRDFAIDPDGRFLLVANQKSDNITVF-RID 328
|
|
| TolB |
COG0823 |
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, ... |
134-228 |
1.84e-03 |
|
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440585 [Multi-domain] Cd Length: 158 Bit Score: 38.88 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 134 FVVVESGDHHVTI--LDGDRFEPIARFPsryALHGGPKFSPDGRLVYFAS-RDGWVTLYdLYNL---KVVAEVRAGLNTR 207
Cdd:COG0823 3 FTLSRDGNSDIYVvdLDGGEPRRLTNSP---GIDTSPAWSPDGRRIAFTSdRGGGPQIY-VVDAdggEPRRLTFGGGYNA 78
|
90 100
....*....|....*....|.
gi 489175324 208 NLAVSDDGRWVLVGNYLPGNL 228
Cdd:COG0823 79 SPSWSPDGKRLAFVSRSDGRF 99
|
|
| COG4946 |
COG4946 |
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown] ... |
138-241 |
3.01e-03 |
|
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown];
Pssm-ID: 443973 [Multi-domain] Cd Length: 1072 Bit Score: 40.41 E-value: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175324 138 ESGDHHVTILDGDRFEPIARFPS-RYALHGGPKFSPDGRLVYFASRDGWVTLYDL--YNLKVVAEVRAGLNTRNLAVSDD 214
Cdd:COG4946 363 ASGEYELYIAPADGSGEPKQLTLgDLGRVFNPVWSPDGKKIAFTDNRGRLWVVDLasGKVRKVDTDGYGDGISDLAWSPD 442
|
90 100 110
....*....|....*....|....*....|
gi 489175324 215 GRWVLVGNYLP---GNLVLLDARDLSLVQV 241
Cdd:COG4946 443 SKWLAYSKPGPnqlSQIFLYDVETGKTVQL 472
|
|
| TsdA |
COG3258 |
Thiosulfate dehydrogenase TsdA, contains C-terminal cytochrome c domain [Inorganic ion ... |
23-49 |
5.97e-03 |
|
Thiosulfate dehydrogenase TsdA, contains C-terminal cytochrome c domain [Inorganic ion transport and metabolism];
Pssm-ID: 442489 [Multi-domain] Cd Length: 216 Bit Score: 38.30 E-value: 5.97e-03
10 20 30
....*....|....*....|....*....|
gi 489175324 23 GEALYRQHCQACHGA---GRLGGSGPTLLP 49
Cdd:COG3258 120 GKALYAERCASCHGAdgeGQGRADGQYGFP 149
|
|
| PQQ |
COG1520 |
Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell ... |
165-239 |
8.84e-03 |
|
Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441129 [Multi-domain] Cd Length: 370 Bit Score: 38.26 E-value: 8.84e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489175324 165 HGGPKFSP--DGRLVYFASRDGWVTLYDLYNLKVVAEVRAGlntRNLA--VSDDGRWVLVGNYLpGNLVLLDARDLSLV 239
Cdd:COG1520 46 KGYSRLAPavAGDRVYAADADGRVAALDAATGKELWRVDLG---EPLSggVGADGGLVVVGTED-GEVIALDADDGEEL 120
|
|
| |
