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Conserved domains on  [gi|1777535666|ref|NP_001363831|]
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THO complex subunit 3 isoform 2 [Homo sapiens]

Protein Classification

WD40 repeat domain-containing protein( domain architecture ID 11455410)

WD40 repeat domain-containing protein similar to proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly

CATH:  2.130.10.10
PubMed:  10322433|8090199
SCOP:  4002744

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
49-297 6.22e-53

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 178.95  E-value: 6.22e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535666  49 REFLAHSAKVHSVAWSCDGRRLASGSFDKTASVFLLEKDRLVKEnnYRGHGDSVDQLCWHPSNpDLFVTASGDKTIRIWD 128
Cdd:COG2319   156 RTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRT--LTGHTGAVRSVAFSPDG-KLLASGSADGTVRLWD 232

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535666 129 VRTTKCIATVNTKGENIN-ICWSPDGQTIAVGNKDDVVTFIDAKTHRSKAE-EQFKFEVNEISWNNDNNMFFLTNGNGCI 206
Cdd:COG2319   233 LATGKLLRTLTGHSGSVRsVAFSPDGRLLASGSADGTVRLWDLATGELLRTlTGHSGGVNSVAFSPDGKLLASGSDDGTV 312

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535666 207 NILSYPELKPVQSINAHPSNCICIKFDPMGKYFATGSADALVSLWDVDELVCVRCFSRLDWPVRTLSFSHDGKMLASASE 286
Cdd:COG2319   313 RLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSA 392

                         250
                  ....*....|.
gi 1777535666 287 DHFIDIAEVET 297
Cdd:COG2319   393 DGTVRLWDLAT 403
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
49-297 6.22e-53

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 178.95  E-value: 6.22e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535666  49 REFLAHSAKVHSVAWSCDGRRLASGSFDKTASVFLLEKDRLVKEnnYRGHGDSVDQLCWHPSNpDLFVTASGDKTIRIWD 128
Cdd:COG2319   156 RTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRT--LTGHTGAVRSVAFSPDG-KLLASGSADGTVRLWD 232

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535666 129 VRTTKCIATVNTKGENIN-ICWSPDGQTIAVGNKDDVVTFIDAKTHRSKAE-EQFKFEVNEISWNNDNNMFFLTNGNGCI 206
Cdd:COG2319   233 LATGKLLRTLTGHSGSVRsVAFSPDGRLLASGSADGTVRLWDLATGELLRTlTGHSGGVNSVAFSPDGKLLASGSDDGTV 312

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535666 207 NILSYPELKPVQSINAHPSNCICIKFDPMGKYFATGSADALVSLWDVDELVCVRCFSRLDWPVRTLSFSHDGKMLASASE 286
Cdd:COG2319   313 RLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSA 392

                         250
                  ....*....|.
gi 1777535666 287 DHFIDIAEVET 297
Cdd:COG2319   393 DGTVRLWDLAT 403
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 49-290 4.74e-47

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: 160.19  E-value: 4.74e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535666  49 REFLAHSAKVHSVAWSCDGRRLASGSFDKTASVFLLEKDRLVKEnnYRGHGDSVDQLCWHPSNPdLFVTASGDKTIRIWD 128
Cdd:cd00200    45 RTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRT--LTGHTSYVSSVAFSPDGR-ILSSSSRDKTIKVWD 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535666 129 VRTTKCIATVNTKGENIN-ICWSPDGQTIAVGNKDDVVTFIDAKTHRSKAE-EQFKFEVNEISWNNDNNMFFLTNGNGCI 206
Cdd:cd00200   122 VETGKCLTTLRGHTDWVNsVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATlTGHTGEVNSVAFSPDGEKLLSSSSDGTI 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535666 207 NILSYPELKPVQSINAHPSNCICIKFDPMGKYFATGSADALVSLWDVDELVCVRCFSRLDWPVRTLSFSHDGKMLASASE 286
Cdd:cd00200   202 KLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSA 281


                  ....
gi 1777535666 287 DHFI 290
Cdd:cd00200   282 DGTI 285
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 52-171 3.05e-07

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 52.01  E-value: 3.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535666  52 LAHSAKVHSVAW-SCDGRRLASGSFDKTASVFLLEKDRLVKEnnYRGHGDSVDQLCWHPSNPDLFVTASGDKTIRIWDVR 130
Cdd:PLN00181  529 LASRSKLSGICWnSYIKSQVASSNFEGVVQVWDVARSQLVTE--MKEHEKRVWSIDYSSADPTLLASGSDDGSVKLWSIN 606

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1777535666 131 TTKCIATVNTKGeniNICW----SPDGQTIAVGNKDDVVTFIDAK 171
Cdd:PLN00181  607 QGVSIGTIKTKA---NICCvqfpSESGRSLAFGSADHKVYYYDLR 648
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 215-252 2.88e-06

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 43.46  E-value: 2.88e-06
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1777535666  215 KPVQSINAHPSNCICIKFDPMGKYFATGSADALVSLWD 252
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
95-128 2.58e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 40.79  E-value: 2.58e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1777535666  95 YRGHGDSVDQLCWHPSNpDLFVTASGDKTIRIWD 128
Cdd:pfam00400   7 LEGHTGSVTSLAFSPDG-KLLASGSDDGTVKVWD 39
propeller_TolB TIGR02800
tol-pal system beta propeller repeat protein TolB; Members of this protein family are the TolB ...
 107-162 4.37e-03

tol-pal system beta propeller repeat protein TolB; Members of this protein family are the TolB periplasmic protein of Gram-negative bacteria. TolB is part of the Tol-Pal (peptidoglycan-associated lipoprotein) multiprotein complex, comprising five envelope proteins, TolQ, TolR, TolA, TolB and Pal, which form two complexes. The TolQ, TolR and TolA inner-membrane proteins interact via their transmembrane domains. The {beta}-propeller domain of the periplasmic protein TolB is responsible for its interaction with Pal. TolB also interacts with the outer-membrane peptidoglycan-associated proteins Lpp and OmpA. TolA undergoes a conformational change in response to changes in the proton-motive force, and interacts with Pal in an energy-dependent manner. The C-terminal periplasmic domain of TolA also interacts with the N-terminal domain of TolB. The Tol-PAL system is required for bacterial outer membrane integrity. E. coli TolB is involved in the tonB-independent uptake of group A colicins (colicins A, E1, E2, E3 and K), and is necessary for the colicins to reach their respective targets after initial binding to the bacteria. It is also involved in uptake of filamentous DNA. Study of its structure suggest that the TolB protein might be involved in the recycling of peptidoglycan or in its covalent linking with lipoproteins. The Tol-Pal system is also implicated in pathogenesis of E. coli, Haemophilus ducreyi , Salmonella enterica and Vibrio cholerae, but the mechanism(s) is unclear. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274305 [Multi-domain]  Cd Length: 417  Bit Score: 38.41  E-value: 4.37e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1777535666 107 WHPSNPDL-FVTASGDK-TIRIWDVRTTKCIATVNTKGENINICWSPDGQTIAV-----GNKD 162
Cdd:TIGR02800 197 WSPDGQKLaYVSFESGKpEIYVQDLATGQREKVASFPGMNGAPAFSPDGSKLAVslskdGNPD 259
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
49-297 6.22e-53

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 178.95  E-value: 6.22e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535666  49 REFLAHSAKVHSVAWSCDGRRLASGSFDKTASVFLLEKDRLVKEnnYRGHGDSVDQLCWHPSNpDLFVTASGDKTIRIWD 128
Cdd:COG2319   156 RTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRT--LTGHTGAVRSVAFSPDG-KLLASGSADGTVRLWD 232

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535666 129 VRTTKCIATVNTKGENIN-ICWSPDGQTIAVGNKDDVVTFIDAKTHRSKAE-EQFKFEVNEISWNNDNNMFFLTNGNGCI 206
Cdd:COG2319   233 LATGKLLRTLTGHSGSVRsVAFSPDGRLLASGSADGTVRLWDLATGELLRTlTGHSGGVNSVAFSPDGKLLASGSDDGTV 312

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535666 207 NILSYPELKPVQSINAHPSNCICIKFDPMGKYFATGSADALVSLWDVDELVCVRCFSRLDWPVRTLSFSHDGKMLASASE 286
Cdd:COG2319   313 RLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSA 392

                         250
                  ....*....|.
gi 1777535666 287 DHFIDIAEVET 297
Cdd:COG2319   393 DGTVRLWDLAT 403
WD40 COG2319
WD40 repeat [General function prediction only];
48-318 3.23e-50

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 171.63  E-value: 3.23e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535666  48 TREFLAHSAKVHSVAWSCDGRRLASGSFDKTASVFLLEKDRLVKEnnYRGHGDSVDQLCWHPSNpDLFVTASGDKTIRIW 127
Cdd:COG2319   113 LRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRT--LTGHSGAVTSVAFSPDG-KLLASGSDDGTVRLW 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535666 128 DVRTTKCIATVNTKGENIN-ICWSPDGQTIAVGNKDDVVTFIDAKTHRSKAEEQFK-FEVNEISWNNDNNMFFLTNGNGC 205
Cdd:COG2319   190 DLATGKLLRTLTGHTGAVRsVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHsGSVRSVAFSPDGRLLASGSADGT 269

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535666 206 INILSYPELKPVQSINAHPSNCICIKFDPMGKYFATGSADALVSLWDVDELVCVRCFSRLDWPVRTLSFSHDGKMLASAS 285
Cdd:COG2319   270 VRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGS 349

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1777535666 286 EDHFIDIAEVETGNFMRIYRLSPLAVrTSLVIS 318
Cdd:COG2319   350 DDGTVRLWDLATGELLRTLTGHTGAV-TSVAFS 381
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 49-290 4.74e-47

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: 160.19  E-value: 4.74e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535666  49 REFLAHSAKVHSVAWSCDGRRLASGSFDKTASVFLLEKDRLVKEnnYRGHGDSVDQLCWHPSNPdLFVTASGDKTIRIWD 128
Cdd:cd00200    45 RTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRT--LTGHTSYVSSVAFSPDGR-ILSSSSRDKTIKVWD 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535666 129 VRTTKCIATVNTKGENIN-ICWSPDGQTIAVGNKDDVVTFIDAKTHRSKAE-EQFKFEVNEISWNNDNNMFFLTNGNGCI 206
Cdd:cd00200   122 VETGKCLTTLRGHTDWVNsVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATlTGHTGEVNSVAFSPDGEKLLSSSSDGTI 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535666 207 NILSYPELKPVQSINAHPSNCICIKFDPMGKYFATGSADALVSLWDVDELVCVRCFSRLDWPVRTLSFSHDGKMLASASE 286
Cdd:cd00200   202 KLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSA 281


                  ....
gi 1777535666 287 DHFI 290
Cdd:cd00200   282 DGTI 285
WD40 COG2319
WD40 repeat [General function prediction only];
32-318 8.71e-45

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 157.38  E-value: 8.71e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535666  32 SRYVLGMQELFRGHSKTREFLAHSAKVHSVAWSCDGRRLASGSFDKTASVFLLEKDRLVKEnnYRGHGDSVDQLCWHPSN 111
Cdd:COG2319    55 AGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRT--LTGHTGAVRSVAFSPDG 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535666 112 pDLFVTASGDKTIRIWDVRTTKCIATVNTKGENIN-ICWSPDGQTIAVGNKDDVVTFIDAKTHRSKAE-EQFKFEVNEIS 189
Cdd:COG2319   133 -KTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTsVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTlTGHTGAVRSVA 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535666 190 WNNDNNMFFLTNGNGCINILSYPELKPVQSINAHPSNCICIKFDPMGKYFATGSADALVSLWDVDELVCVRCFSRLDWPV 269
Cdd:COG2319   212 FSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGV 291

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1777535666 270 RTLSFSHDGKMLASASEDHFIDIAEVETGNFMRIYRLSPLAVRtSLVIS 318
Cdd:COG2319   292 NSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVR-SVAFS 339
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 47-252 1.74e-34

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: 127.45  E-value: 1.74e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535666  47 KTREFLAHSAKVHSVAWSCDGRRLASGSFDKTASVFLLEKDRLVKEnnYRGHGDSVDQLCWHPSNpDLFVTASGDKTIRI 126
Cdd:cd00200    85 CVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTT--LRGHTDWVNSVAFSPDG-TFVASSSQDGTIKL 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535666 127 WDVRTTKCIATVNTKGENIN-ICWSPDGQTIAVGNKDDVVTFIDAKTHRSKAE-EQFKFEVNEISWNNDNNMFFLTNGNG 204
Cdd:cd00200   162 WDLRTGKCVATLTGHTGEVNsVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTlRGHENGVNSVAFSPDGYLLASGSEDG 241

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1777535666 205 CINILSYPELKPVQSINAHPSNCICIKFDPMGKYFATGSADALVSLWD 252
Cdd:cd00200   242 TIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
49-318 5.58e-30

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 117.70  E-value: 5.58e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535666  49 REFLAHSAKVHSVAWSCDGRRLASGSFDKTASVFLLEKDRLVKEnnYRGHGDSVDQLCWHPsNPDLFVTASGDKTIRIWD 128
Cdd:COG2319    30 LLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLAT--LLGHTAAVLSVAFSP-DGRLLASASADGTVRLWD 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535666 129 VRTTKCIATVNTKGENIN-ICWSPDGQTIAVGNKDDVVTFIDAKTHrskaeeqfkfevneiswnndnnmffltngngcin 207
Cdd:COG2319   107 LATGLLLRTLTGHTGAVRsVAFSPDGKTLASGSADGTVRLWDLATG---------------------------------- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535666 208 ilsypelKPVQSINAHPSNCICIKFDPMGKYFATGSADALVSLWDVDELVCVRCFSRLDWPVRTLSFSHDGKMLASASED 287
Cdd:COG2319   153 -------KLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSAD 225

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1777535666 288 HFIDIAEVETGNFMRIYRLSPLAVRtSLVIS 318
Cdd:COG2319   226 GTVRLWDLATGKLLRTLTGHSGSVR-SVAFS 255
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 48-305 9.63e-30

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: 114.74  E-value: 9.63e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535666  48 TREFLAHSAKVHSVAWSCDGRRLASGSFDKTASVFLLEKDRLVKENnyRGHGDSVDQLCWHPSNpDLFVTASGDKTIRIW 127
Cdd:cd00200     2 RRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTL--KGHTGPVRDVAASADG-TYLASGSSDKTIRLW 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535666 128 DVRTTKCIATVntkgeninicwspdgqtiavgnkddvvtfidakthrskaeEQFKFEVNEISWNNDNNMFFLTNGNGCIN 207
Cdd:cd00200    79 DLETGECVRTL----------------------------------------TGHTSYVSSVAFSPDGRILSSSSRDKTIK 118

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535666 208 ILSYPELKPVQSINAHPSNCICIKFDPMGKYFATGSADALVSLWDVDELVCVRCFSRLDWPVRTLSFSHDGKMLASASED 287
Cdd:cd00200   119 VWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSD 198

                         250
                  ....*....|....*...
gi 1777535666 288 HFIDIAEVETGNFMRIYR 305
Cdd:cd00200   199 GTIKLWDLSTGKCLGTLR 216
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 42-162 1.65e-20

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: 89.70  E-value: 1.65e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535666  42 FRGHSKTREFLAHSAKVHSVAWSCDGRRLASGSFDKTASVFLLEKDRLVKEnnYRGHGDSVDQLCWHPSNpDLFVTASGD 121
Cdd:cd00200   164 LRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGT--LRGHENGVNSVAFSPDG-YLLASGSED 240

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1777535666 122 KTIRIWDVRTTKCIATVNTKGENIN-ICWSPDGQTIAVGNKD 162
Cdd:cd00200   241 GTIRVWDLRTGECVQTLSGHTNSVTsLAWSPDGKRLASGSAD 282
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 216-305 8.70e-11

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: 61.58  E-value: 8.70e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535666 216 PVQSINAHPSNCICIKFDPMGKYFATGSADALVSLWDVDELVCVRCFSRLDWPVRTLSFSHDGKMLASASEDHFIDIAEV 295
Cdd:cd00200     1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDL 80

                          90
                  ....*....|
gi 1777535666 296 ETGNFMRIYR 305
Cdd:cd00200    81 ETGECVRTLT 90
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
66-207 1.23e-09

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


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 57.78  E-value: 1.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535666  66 DGRRL-ASGSFDKTASVFLLEKDRLVKENNyrgHGDSVDQLCWHPSNPDLFVTASGDKTIRIWDVRTTKCIATVNTKGEN 144
Cdd:COG3391    78 DGRRLyVANSGSGRVSVIDLATGKVVATIP---VGGGPRGLAVDPDGGRLYVADSGNGRVSVIDTATGKVVATIPVGAGP 154

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1777535666 145 INICWSPDGQTIAVGNKDD-----VVTFIDAKTHRSKAEEQFKFEVNEISWNNDNNMFFLTN-GNGCIN 207
Cdd:COG3391   155 HGIAVDPDGKRLYVANSGSntvsvIVSVIDTATGKVVATIPVGGGPVGVAVSPDGRRLYVANrGSNTSN 223
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 52-171 3.05e-07

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 52.01  E-value: 3.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535666  52 LAHSAKVHSVAW-SCDGRRLASGSFDKTASVFLLEKDRLVKEnnYRGHGDSVDQLCWHPSNPDLFVTASGDKTIRIWDVR 130
Cdd:PLN00181  529 LASRSKLSGICWnSYIKSQVASSNFEGVVQVWDVARSQLVTE--MKEHEKRVWSIDYSSADPTLLASGSDDGSVKLWSIN 606

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1777535666 131 TTKCIATVNTKGeniNICW----SPDGQTIAVGNKDDVVTFIDAK 171
Cdd:PLN00181  607 QGVSIGTIKTKA---NICCvqfpSESGRSLAFGSADHKVYYYDLR 648
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 215-252 2.88e-06

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 43.46  E-value: 2.88e-06
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1777535666  215 KPVQSINAHPSNCICIKFDPMGKYFATGSADALVSLWD 252
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 95-128 3.47e-06

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 43.07  E-value: 3.47e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1777535666   95 YRGHGDSVDQLCWHPSNpDLFVTASGDKTIRIWD 128
Cdd:smart00320   8 LKGHTGPVTSVAFSPDG-KYLASGSDDGTIKLWD 40
WD40 COG2319
WD40 repeat [General function prediction only];
48-79 5.18e-06

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 47.60  E-value: 5.18e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1777535666  48 TREFLAHSAKVHSVAWSCDGRRLASGSFDKTA 79
Cdd:COG2319   365 LRTLTGHTGAVTSVAFSPDGRTLASGSADGTV 396
WD40 pfam00400
WD domain, G-beta repeat;
95-128 2.58e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 40.79  E-value: 2.58e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1777535666  95 YRGHGDSVDQLCWHPSNpDLFVTASGDKTIRIWD 128
Cdd:pfam00400   7 LEGHTGSVTSLAFSPDG-KLLASGSDDGTVKVWD 39
WD40 pfam00400
WD domain, G-beta repeat;
215-252 4.39e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 40.02  E-value: 4.39e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1777535666 215 KPVQSINAHPSNCICIKFDPMGKYFATGSADALVSLWD 252
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
PTZ00421 PTZ00421
coronin; Provisional
 96-171 5.58e-05

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 44.50  E-value: 5.58e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1777535666  96 RGHGDSVDQLCWHPSNPDLFVTASGDKTIRIWDVRTTKCIATVNTKGENI-NICWSPDGQTIAVGNKDDVVTFIDAK 171
Cdd:PTZ00421  122 QGHTKKVGIVSFHPSAMNVLASAGADMVVNVWDVERGKAVEVIKCHSDQItSLEWNLDGSLLCTTSKDKKLNIIDPR 198
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 46-82 6.04e-05

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 39.60  E-value: 6.04e-05
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1777535666   46 SKTREFLAHSAKVHSVAWSCDGRRLASGSFDKTASVF 82
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLW 39
WD40 pfam00400
WD domain, G-beta repeat;
46-82 1.33e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 38.87  E-value: 1.33e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1777535666  46 SKTREFLAHSAKVHSVAWSCDGRRLASGSFDKTASVF 82
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVW 38
8prop_hemeD1_NirF cd20778
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirF; ...
 107-174 1.25e-03

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: 40.34  E-value: 1.25e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1777535666 107 WHPSNPDLFVTASGDKTIRIWDVRTTKCIATVNTKGENINICWSPDGQTIAV---GNKDDVVTFIDAKTHR 174
Cdd:cd20778   246 WAVAGDKAFVPAVGEHRVLVYDTNDWKFIKSIPLAGQPVFAVARPDGRYVWVnfsGPDNDTVQVIDTKTLK 316
COG4946 COG4946
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown] ...
 137-238 2.26e-03

Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown];


Pssm-ID: 443973 [Multi-domain]  Cd Length: 1072  Bit Score: 39.64  E-value: 2.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535666  137 TVNTKGENINICWSPDGQTIAVGNKDDVVTFIDAKTHRSK--AEEQFKFEVNEISWNNDNN----MFFLTNGNGCINILS 210
Cdd:COG4946    384 TLGDLGRVFNPVWSPDGKKIAFTDNRGRLWVVDLASGKVRkvDTDGYGDGISDLAWSPDSKwlaySKPGPNQLSQIFLYD 463

                           90       100
                   ....*....|....*....|....*...
gi 1777535666  211 YPELKPVQsINAHPSNCICIKFDPMGKY 238
Cdd:COG4946    464 VETGKTVQ-LTDGRYDDGSPAFSPDGKY 490
propeller_TolB TIGR02800
tol-pal system beta propeller repeat protein TolB; Members of this protein family are the TolB ...
 107-162 4.37e-03

tol-pal system beta propeller repeat protein TolB; Members of this protein family are the TolB periplasmic protein of Gram-negative bacteria. TolB is part of the Tol-Pal (peptidoglycan-associated lipoprotein) multiprotein complex, comprising five envelope proteins, TolQ, TolR, TolA, TolB and Pal, which form two complexes. The TolQ, TolR and TolA inner-membrane proteins interact via their transmembrane domains. The {beta}-propeller domain of the periplasmic protein TolB is responsible for its interaction with Pal. TolB also interacts with the outer-membrane peptidoglycan-associated proteins Lpp and OmpA. TolA undergoes a conformational change in response to changes in the proton-motive force, and interacts with Pal in an energy-dependent manner. The C-terminal periplasmic domain of TolA also interacts with the N-terminal domain of TolB. The Tol-PAL system is required for bacterial outer membrane integrity. E. coli TolB is involved in the tonB-independent uptake of group A colicins (colicins A, E1, E2, E3 and K), and is necessary for the colicins to reach their respective targets after initial binding to the bacteria. It is also involved in uptake of filamentous DNA. Study of its structure suggest that the TolB protein might be involved in the recycling of peptidoglycan or in its covalent linking with lipoproteins. The Tol-Pal system is also implicated in pathogenesis of E. coli, Haemophilus ducreyi , Salmonella enterica and Vibrio cholerae, but the mechanism(s) is unclear. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274305 [Multi-domain]  Cd Length: 417  Bit Score: 38.41  E-value: 4.37e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1777535666 107 WHPSNPDL-FVTASGDK-TIRIWDVRTTKCIATVNTKGENINICWSPDGQTIAV-----GNKD 162
Cdd:TIGR02800 197 WSPDGQKLaYVSFESGKpEIYVQDLATGQREKVASFPGMNGAPAFSPDGSKLAVslskdGNPD 259
PQQ_ABC_repeats TIGR03866
PQQ-dependent catabolism-associated beta-propeller protein; Members of this protein family ...
 114-178 4.46e-03

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: 38.48  E-value: 4.46e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1777535666 114 LFVTASGDKTIRIWDVRTTKCIATVNTKGENINICWSPDGQTIAVGNKDD-VVTFIDAKTHRSKAE 178
Cdd:TIGR03866  55 LYVCASDSDTIQVIDPATGEVLHTLPSGPDPEQFALHPNGKILYIANEDDaLVTVIDIETRKVLAQ 120
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
 105-172 4.52e-03

Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped WD40 domain.The N-terminus of Afi1 serves to stabilize the union between Apc4 and Apc5, both of which lie towards the bottom-front of the APC,


Pssm-ID: 403945 [Multi-domain]  Cd Length: 91  Bit Score: 35.72  E-value: 4.52e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1777535666 105 LCWHPSNpDLFVTASGDKTI--------RIWDvrttkcIATVNTKGENINICWSPDGQTIAVGNKDDVVTFIDAKT 172
Cdd:pfam12894   1 MSWCPTM-DLIALATEDGELllhrlnwqRVWT------LSPDKEDLEVTSLAWRPDGKLLAVGYSDGTVRLLDAEN 69
eIF2A pfam08662
Eukaryotic translation initiation factor eIF2A; This is a family of eukaryotic translation ...
 134-241 6.95e-03

Eukaryotic translation initiation factor eIF2A; This is a family of eukaryotic translation initiation factors.


Pssm-ID: 462552 [Multi-domain]  Cd Length: 194  Bit Score: 37.25  E-value: 6.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535666 134 CIATVNTKGENINICWSPDGQTIAV--GNKDDVVTFIDAKthrskAEEQFKFE---VNEISWNNDNNMFFLT---NGNGC 205
Cdd:pfam08662  52 CVVELDKEGPIHDVAWSPNGKEFAViyGYMPAKVSFFDLK-----GNVIHSFGeqpRNTIFWSPFGRLVLLAgfgNLAGD 126

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1777535666 206 INILSYPELKPVQSINAhpSNCICIKFDPMGKYFAT 241
Cdd:pfam08662 127 IEFWDVVNKKKIATAEA--SNATLCEWSPDGRYFLT 160
8prop_hemeD1_NirF cd20778
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirF; ...
 108-174 9.62e-03

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: 37.26  E-value: 9.62e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535666 108 HPSNPDLFVTASGDK--TIRIWDVRTTKCIATVNTKGENINICWSPDGQTIAVG-NKDDVVTFIDAKTHR 174
Cdd:cd20778   289 RPDGRYVWVNFSGPDndTVQVIDTKTLKVVKTLEPGKRVLHMEFTPRGEAVYISvNDDNKVVVYDTRTFR 358
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 258-290 9.81e-03

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 33.44  E-value: 9.81e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1777535666  258 CVRCFSRLDWPVRTLSFSHDGKMLASASEDHFI 290
Cdd:smart00320   4 LLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTI 36
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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