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Conserved domains on  [gi|1901852724|dbj|GGS17325|]
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desiccation/radiation resistance protein [Deinococcus knuensis]

Protein Classification

PQQ-binding-like beta-propeller repeat protein( domain architecture ID 11445572)

PQQ (pyrrolo-quinoline quinone)-like beta-propeller repeat protein contains several instances of a beta-propeller repeat; similar to Bacillus subtilis protein YxaL

Gene Ontology:  GO:0070968

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PQQ super family cl34291
Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell ...
72-347 1.53e-23

Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell wall/membrane/envelope biogenesis];


The actual alignment was detected with superfamily member COG1520:

Pssm-ID: 441129 [Multi-domain]  Cd Length: 370  Bit Score: 102.58  E-value: 1.53e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724  72 ATGSEKWSF-----LTGDIGRAYpvvtpqGVTIAASYDDTVYALDPA-GKLLWKTKLDGDIFATPALrADGSVIVATAGG 145
Cdd:COG1520    75 ATGKELWRVdlgepLSGGVGADG------GLVVVGTEDGEVIALDADdGEELWRARLSSEVLAAPAV-AGGRVVVRTGDG 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724 146 TVHALDTQ-GRTLWTYRVGAPVFS----SPAIAADGTIYFGAQNNRMHALTP-DGKLKWAYTAGS------L-----VFS 208
Cdd:COG1520   148 RVYALDAAtGERLWSYQRPVPALTlrgtSSPVIVGGAVLVGFANGKLVALDLaNGQPLWEQRVAQprgrteLerlvdVDG 227
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724 209 SPAIgADGTVYFGSSDRRIYALNP-DGTPRWSLPTGLFVNaspIVTSAGLVVVGSYDGSVYAVNP-TGEIEWT-----YR 281
Cdd:COG1520   228 TPVV-DGGVVYAVAYQGRLAALDLrSGRVLWSRDLSSYTG---LAVDGNNLYVTDDDGRVWALDRrNGAELWKqdallYR 303
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1901852724 282 agagiagsaaELS-----DGSVIVPDLAGTVHAIGKA-GQSLWQIKTGKKIDLGVSVSDQGSVYFTTEGGGL 347
Cdd:COG1520   304 ----------GLTapvvlGDYVVVGDFEGYLHWLSRDdGSLVARLRVDGSGIRAAPVVVGDTLYVQTRDGTL 365
 
Name Accession Description Interval E-value
PQQ COG1520
Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell ...
72-347 1.53e-23

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: 102.58  E-value: 1.53e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724  72 ATGSEKWSF-----LTGDIGRAYpvvtpqGVTIAASYDDTVYALDPA-GKLLWKTKLDGDIFATPALrADGSVIVATAGG 145
Cdd:COG1520    75 ATGKELWRVdlgepLSGGVGADG------GLVVVGTEDGEVIALDADdGEELWRARLSSEVLAAPAV-AGGRVVVRTGDG 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724 146 TVHALDTQ-GRTLWTYRVGAPVFS----SPAIAADGTIYFGAQNNRMHALTP-DGKLKWAYTAGS------L-----VFS 208
Cdd:COG1520   148 RVYALDAAtGERLWSYQRPVPALTlrgtSSPVIVGGAVLVGFANGKLVALDLaNGQPLWEQRVAQprgrteLerlvdVDG 227
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724 209 SPAIgADGTVYFGSSDRRIYALNP-DGTPRWSLPTGLFVNaspIVTSAGLVVVGSYDGSVYAVNP-TGEIEWT-----YR 281
Cdd:COG1520   228 TPVV-DGGVVYAVAYQGRLAALDLrSGRVLWSRDLSSYTG---LAVDGNNLYVTDDDGRVWALDRrNGAELWKqdallYR 303
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1901852724 282 agagiagsaaELS-----DGSVIVPDLAGTVHAIGKA-GQSLWQIKTGKKIDLGVSVSDQGSVYFTTEGGGL 347
Cdd:COG1520   304 ----------GLTapvvlGDYVVVGDFEGYLHWLSRDdGSLVARLRVDGSGIRAAPVVVGDTLYVQTRDGTL 365
PQQ_2 pfam13360
PQQ-like domain; This domain contains several repeats of the PQQ repeat.
63-280 7.05e-23

PQQ-like domain; This domain contains several repeats of the PQQ repeat.


Pssm-ID: 433144 [Multi-domain]  Cd Length: 233  Bit Score: 97.47  E-value: 7.05e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724  63 SDARLHRTDA-TGSEKWSFLTGDIGRAYPVVtPQGVTIAASYDDTVYALDPA-GKLLWKTKLDGDIFATPALrADGSVIV 140
Cdd:pfam13360   1 ADGVVTALDAaTGAELWRVDLETGLGGGVAV-DGGRLFVATGGGQLVALDAAtGKLLWRQTLSGEVLGAPLV-AGGRVFV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724 141 ATAGGTVHALDTQ-GRTLWTYRVGAPVF----SSPAIAADGTIYFGAQNNRMHALTP-DGKLKWAYTAGS---------- 204
Cdd:pfam13360  79 VAGDGSLIALDAAdGRRLWSYQRSGEPLalrsSGSPAVVGDTVVAGFSSGKLVALDPaTGKVRWEAPLAAprgtnelerl 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1901852724 205 -LVFSSPAIgADGTVYFGSSDRRIYALNPD-GTPRWSLPTGLFVnasPIVTSAGLVVVGSYDGSVYAVNP-TGEIEWTY 280
Cdd:pfam13360 159 vDITGTPVV-AGGRVFASAYQGRLVAFDAAtGRRLWTREISGPN---GPILDGDLLYVVSDDGELYALDRaTGAVVWKT 233
assembly_YfgL TIGR03300
outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a ...
72-351 1.14e-20

outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a lipoprotein component of a complex that acts protein insertion into the bacterial outer membrane. Other members of this complex are NlpB, YfiO, and YaeT. This protein contains multiple copies of a repeat that, in other contexts, are associated with binding of the coenzyme PQQ. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 274511 [Multi-domain]  Cd Length: 377  Bit Score: 93.84  E-value: 1.14e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724  72 ATGSEKWSF-----LTGDIGRAYpvvtpqGVTIAASYDDTVYALDPA-GKLLWKTKLDGDIFATPALrADGSVIVATAGG 145
Cdd:TIGR03300  83 ETGKRLWRVdlderLSGGVGADG------GLVFVGTEKGEVIALDAEdGKELWRAKLSSEVLSPPLV-ANGLVVVRTNDG 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724 146 TVHALDTQ-GRTLWTYRVGAPVF----SSPAIAADGTIYFGAQNNRMHALTP-DGKLKW----AYTAGSL-------VFS 208
Cdd:TIGR03300 156 RLTALDAAtGERLWTYSRVTPPLtlrgSASPVIADGGVLVGFAGGKLVALDLqTGQPLWeqrvALPKGRTelerlvdVDG 235
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724 209 SPAIgADGTVYFGSSDRRIYALNP-DGTPRWSLPTGlfvNASPIVTSAGLVVVGSYDGSVYAVNP-TGEIEWTYRAGAGI 286
Cdd:TIGR03300 236 DPVV-DGGQVYAVSYQGRVAALDLrSGRVLWKRDAS---SYQGPAVDDNRLYVTDADGVVVALDRrSGSELWKNDELKYR 311
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1901852724 287 AGSAAELSDGSVIVPDLAGTVHAIGKA-GQSLWQIKTGKKIDLGVSVSDQGSVYFTTEGGGLNIVQ 351
Cdd:TIGR03300 312 QLTAPAVLGGYLVVGDFEGYLHWLDRDdGSFVARLKTDGSGIASPPVVVGDGLLVQTRDGDLYAFR 377
BamB_YfgL cd10276
Beta-barrel assembly machinery (Bam) complex component B and related proteins; BamB (YflG) is ...
115-347 1.37e-19

Beta-barrel assembly machinery (Bam) complex component B and related proteins; BamB (YflG) is a non-essential component of the beta-barrel assembly machinery (Bam), a multi-subunit complex that inserts proteins with beta-barrel topology into the outer membrane. BamB has been found to interact with BamA, which in turn binds and stabilizes pre-folded beta-barrel proteins; it has been suggested that BamB participates in the stabilization.


Pssm-ID: 199834 [Multi-domain]  Cd Length: 358  Bit Score: 90.47  E-value: 1.37e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724 115 KLLWKTKLDGDIFA----TPALrADGSVIVATAGGTVHALD-TQGRTLWTYRVGAPVFSSPAIA-ADGTIYFGAQNNRMH 188
Cdd:cd10276    15 EVLWSKSVGNGGMAgidlTPVV-AGDMVYAADANGQVSAFNaTTGKIIWETSLSGKGFLGGTPAvGNGKIFVGTESGYLY 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724 189 AL-TPDGKLKWAYTAGSLVFSSPAIGADGTVYFGSSDRRIYALNPD-GTPRWS----LPTGLFVNASPIVTSAGLVVVGS 262
Cdd:cd10276    94 ALdAKDGSELWRTEVSDSQLLSPPTYADGKIYVGTGDGRLYYCNAEtGKVVWNrtstAPELSLRGGAAPVGAYDVVFVGD 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724 263 YDGSVYAVNP-TGEIEWTYRAGAGIAGSAAE-LSDGSVIVPDLAGTVHAI---GKA-------GQSLWQIKTGKKIDLgv 330
Cdd:cd10276   174 GNGTVVALNTgTGVDIWEFSVSEPRGRTELPrMIDSSVTYVVVGGYLYSTsyqGYLvaldfesGQFLWSRKASGGTST-- 251
                         250
                  ....*....|....*..
gi 1901852724 331 SVSDQGSVYFTTEGGGL 347
Cdd:cd10276   252 STDANGRVYVGDGEGSL 268
PRK11138 PRK11138
outer membrane biogenesis protein BamB; Provisional
72-276 4.19e-10

outer membrane biogenesis protein BamB; Provisional


Pssm-ID: 236857 [Multi-domain]  Cd Length: 394  Bit Score: 61.87  E-value: 4.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724  72 ATGSEKWSF----LTGDIGRAYPVVTPQGVTIA------ASYDDTVYALDPA-GKLLWKTKLDGDIFATPALrADGSVIV 140
Cdd:PRK11138   87 DTGKEIWSVdlseKDGWFSKNKSALLSGGVTVAggkvyiGSEKGQVYALNAEdGEVAWQTKVAGEALSRPVV-SDGLVLV 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724 141 ATAGGTVHALD-TQGRTLWTYRVGAPVF-----SSPAIAAdGTIYFGAQNNRMHALTPD-GKLKWA---YTA-GSL---- 205
Cdd:PRK11138  166 HTSNGMLQALNeSDGAVKWTVNLDVPSLtlrgeSAPATAF-GGAIVGGDNGRVSAVLMEqGQLIWQqriSQPtGATeidr 244
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724 206 ---VFSSPAIgADGTVY-----------------------FGS---------------SDRRIYALNPD-GTPRWSLPTG 243
Cdd:PRK11138  245 lvdVDTTPVV-VGGVVYalayngnlvaldlrsgqivwkreYGSvndfavdggriylvdQNDRVYALDTRgGVELWSQSDL 323
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1901852724 244 LFVNASPIVTSAGLVVVGSYDGSVYAVNP-TGEI 276
Cdd:PRK11138  324 LHRLLTAPVLYNGYLVVGDSEGYLHWINReDGRF 357
PQQ smart00564
beta-propeller repeat; Beta-propeller repeat occurring in enzymes with pyrrolo-quinoline ...
250-281 2.06e-05

beta-propeller repeat; Beta-propeller repeat occurring in enzymes with pyrrolo-quinoline quinone (PQQ) as cofactor, in Ire1p-like Ser/Thr kinases, and in prokaryotic dehydrogenases.


Pssm-ID: 128836 [Multi-domain]  Cd Length: 33  Bit Score: 41.37  E-value: 2.06e-05
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1901852724  250 PIVTSAGLVVVGSYDGSVYAVNP-TGEIEWTYR 281
Cdd:smart00564   1 PVVLSDGTVYVGSTDGTLYALDAkTGEILWTYK 33
 
Name Accession Description Interval E-value
PQQ COG1520
Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell ...
72-347 1.53e-23

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: 102.58  E-value: 1.53e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724  72 ATGSEKWSF-----LTGDIGRAYpvvtpqGVTIAASYDDTVYALDPA-GKLLWKTKLDGDIFATPALrADGSVIVATAGG 145
Cdd:COG1520    75 ATGKELWRVdlgepLSGGVGADG------GLVVVGTEDGEVIALDADdGEELWRARLSSEVLAAPAV-AGGRVVVRTGDG 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724 146 TVHALDTQ-GRTLWTYRVGAPVFS----SPAIAADGTIYFGAQNNRMHALTP-DGKLKWAYTAGS------L-----VFS 208
Cdd:COG1520   148 RVYALDAAtGERLWSYQRPVPALTlrgtSSPVIVGGAVLVGFANGKLVALDLaNGQPLWEQRVAQprgrteLerlvdVDG 227
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724 209 SPAIgADGTVYFGSSDRRIYALNP-DGTPRWSLPTGLFVNaspIVTSAGLVVVGSYDGSVYAVNP-TGEIEWT-----YR 281
Cdd:COG1520   228 TPVV-DGGVVYAVAYQGRLAALDLrSGRVLWSRDLSSYTG---LAVDGNNLYVTDDDGRVWALDRrNGAELWKqdallYR 303
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1901852724 282 agagiagsaaELS-----DGSVIVPDLAGTVHAIGKA-GQSLWQIKTGKKIDLGVSVSDQGSVYFTTEGGGL 347
Cdd:COG1520   304 ----------GLTapvvlGDYVVVGDFEGYLHWLSRDdGSLVARLRVDGSGIRAAPVVVGDTLYVQTRDGTL 365
PQQ_2 pfam13360
PQQ-like domain; This domain contains several repeats of the PQQ repeat.
63-280 7.05e-23

PQQ-like domain; This domain contains several repeats of the PQQ repeat.


Pssm-ID: 433144 [Multi-domain]  Cd Length: 233  Bit Score: 97.47  E-value: 7.05e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724  63 SDARLHRTDA-TGSEKWSFLTGDIGRAYPVVtPQGVTIAASYDDTVYALDPA-GKLLWKTKLDGDIFATPALrADGSVIV 140
Cdd:pfam13360   1 ADGVVTALDAaTGAELWRVDLETGLGGGVAV-DGGRLFVATGGGQLVALDAAtGKLLWRQTLSGEVLGAPLV-AGGRVFV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724 141 ATAGGTVHALDTQ-GRTLWTYRVGAPVF----SSPAIAADGTIYFGAQNNRMHALTP-DGKLKWAYTAGS---------- 204
Cdd:pfam13360  79 VAGDGSLIALDAAdGRRLWSYQRSGEPLalrsSGSPAVVGDTVVAGFSSGKLVALDPaTGKVRWEAPLAAprgtnelerl 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1901852724 205 -LVFSSPAIgADGTVYFGSSDRRIYALNPD-GTPRWSLPTGLFVnasPIVTSAGLVVVGSYDGSVYAVNP-TGEIEWTY 280
Cdd:pfam13360 159 vDITGTPVV-AGGRVFASAYQGRLVAFDAAtGRRLWTREISGPN---GPILDGDLLYVVSDDGELYALDRaTGAVVWKT 233
assembly_YfgL TIGR03300
outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a ...
72-351 1.14e-20

outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a lipoprotein component of a complex that acts protein insertion into the bacterial outer membrane. Other members of this complex are NlpB, YfiO, and YaeT. This protein contains multiple copies of a repeat that, in other contexts, are associated with binding of the coenzyme PQQ. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 274511 [Multi-domain]  Cd Length: 377  Bit Score: 93.84  E-value: 1.14e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724  72 ATGSEKWSF-----LTGDIGRAYpvvtpqGVTIAASYDDTVYALDPA-GKLLWKTKLDGDIFATPALrADGSVIVATAGG 145
Cdd:TIGR03300  83 ETGKRLWRVdlderLSGGVGADG------GLVFVGTEKGEVIALDAEdGKELWRAKLSSEVLSPPLV-ANGLVVVRTNDG 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724 146 TVHALDTQ-GRTLWTYRVGAPVF----SSPAIAADGTIYFGAQNNRMHALTP-DGKLKW----AYTAGSL-------VFS 208
Cdd:TIGR03300 156 RLTALDAAtGERLWTYSRVTPPLtlrgSASPVIADGGVLVGFAGGKLVALDLqTGQPLWeqrvALPKGRTelerlvdVDG 235
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724 209 SPAIgADGTVYFGSSDRRIYALNP-DGTPRWSLPTGlfvNASPIVTSAGLVVVGSYDGSVYAVNP-TGEIEWTYRAGAGI 286
Cdd:TIGR03300 236 DPVV-DGGQVYAVSYQGRVAALDLrSGRVLWKRDAS---SYQGPAVDDNRLYVTDADGVVVALDRrSGSELWKNDELKYR 311
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1901852724 287 AGSAAELSDGSVIVPDLAGTVHAIGKA-GQSLWQIKTGKKIDLGVSVSDQGSVYFTTEGGGLNIVQ 351
Cdd:TIGR03300 312 QLTAPAVLGGYLVVGDFEGYLHWLDRDdGSFVARLKTDGSGIASPPVVVGDGLLVQTRDGDLYAFR 377
BamB_YfgL cd10276
Beta-barrel assembly machinery (Bam) complex component B and related proteins; BamB (YflG) is ...
115-347 1.37e-19

Beta-barrel assembly machinery (Bam) complex component B and related proteins; BamB (YflG) is a non-essential component of the beta-barrel assembly machinery (Bam), a multi-subunit complex that inserts proteins with beta-barrel topology into the outer membrane. BamB has been found to interact with BamA, which in turn binds and stabilizes pre-folded beta-barrel proteins; it has been suggested that BamB participates in the stabilization.


Pssm-ID: 199834 [Multi-domain]  Cd Length: 358  Bit Score: 90.47  E-value: 1.37e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724 115 KLLWKTKLDGDIFA----TPALrADGSVIVATAGGTVHALD-TQGRTLWTYRVGAPVFSSPAIA-ADGTIYFGAQNNRMH 188
Cdd:cd10276    15 EVLWSKSVGNGGMAgidlTPVV-AGDMVYAADANGQVSAFNaTTGKIIWETSLSGKGFLGGTPAvGNGKIFVGTESGYLY 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724 189 AL-TPDGKLKWAYTAGSLVFSSPAIGADGTVYFGSSDRRIYALNPD-GTPRWS----LPTGLFVNASPIVTSAGLVVVGS 262
Cdd:cd10276    94 ALdAKDGSELWRTEVSDSQLLSPPTYADGKIYVGTGDGRLYYCNAEtGKVVWNrtstAPELSLRGGAAPVGAYDVVFVGD 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724 263 YDGSVYAVNP-TGEIEWTYRAGAGIAGSAAE-LSDGSVIVPDLAGTVHAI---GKA-------GQSLWQIKTGKKIDLgv 330
Cdd:cd10276   174 GNGTVVALNTgTGVDIWEFSVSEPRGRTELPrMIDSSVTYVVVGGYLYSTsyqGYLvaldfesGQFLWSRKASGGTST-- 251
                         250
                  ....*....|....*..
gi 1901852724 331 SVSDQGSVYFTTEGGGL 347
Cdd:cd10276   252 STDANGRVYVGDGEGSL 268
BamB_YfgL cd10276
Beta-barrel assembly machinery (Bam) complex component B and related proteins; BamB (YflG) is ...
48-348 4.16e-17

Beta-barrel assembly machinery (Bam) complex component B and related proteins; BamB (YflG) is a non-essential component of the beta-barrel assembly machinery (Bam), a multi-subunit complex that inserts proteins with beta-barrel topology into the outer membrane. BamB has been found to interact with BamA, which in turn binds and stabilizes pre-folded beta-barrel proteins; it has been suggested that BamB participates in the stabilization.


Pssm-ID: 199834 [Multi-domain]  Cd Length: 358  Bit Score: 83.15  E-value: 4.16e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724  48 SGVTVSP---NGDLTFMGSDARLHRTDA-TGSEKWSFLTGDIGRAY-PVVTPQGVTIAASYDDTVYALDPA-GKLLWKTK 121
Cdd:cd10276    28 AGIDLTPvvaGDMVYAADANGQVSAFNAtTGKIIWETSLSGKGFLGgTPAVGNGKIFVGTESGYLYALDAKdGSELWRTE 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724 122 LDGDIFATPALRADGSVIVATAGGTVHAL-DTQGRTLWTYRVGAPV----FSSPAIAADGTIYFGAQNNRMHALTP-DGK 195
Cdd:cd10276   108 VSDSQLLSPPTYADGKIYVGTGDGRLYYCnAETGKVVWNRTSTAPElslrGGAAPVGAYDVVFVGDGNGTVVALNTgTGV 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724 196 LKWAYTAGSLVFSSPAIGAD----------GTVYFGSSDRRIYALNPD-GTPRWSLPTGLFvnASPIVTSAGLVVVGSYD 264
Cdd:cd10276   188 DIWEFSVSEPRGRTELPRMIdssvtyvvvgGYLYSTSYQGYLVALDFEsGQFLWSRKASGG--TSTSTDANGRVYVGDGE 265
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724 265 GSVYAVNP-TGEIEWTYRAGAGIAGSAAELSDGSVIV--PDLAGTVHAIGKAGQSLW-QIKTGKK--IDLGVSVSDqGSV 338
Cdd:cd10276   266 GSLYCLDAsTGDELWSQTVLLGRVLSSPAIYVGVYIYvtDNAEGYLYCLKDNDGLTVaRVEVDYSqyILQGPAVSD-GWL 344
                         330
                  ....*....|
gi 1901852724 339 YFTTEGGGLN 348
Cdd:cd10276   345 YYGTDDGYLY 354
BamB_YfgL cd10276
Beta-barrel assembly machinery (Bam) complex component B and related proteins; BamB (YflG) is ...
57-230 1.44e-13

Beta-barrel assembly machinery (Bam) complex component B and related proteins; BamB (YflG) is a non-essential component of the beta-barrel assembly machinery (Bam), a multi-subunit complex that inserts proteins with beta-barrel topology into the outer membrane. BamB has been found to interact with BamA, which in turn binds and stabilizes pre-folded beta-barrel proteins; it has been suggested that BamB participates in the stabilization.


Pssm-ID: 199834 [Multi-domain]  Cd Length: 358  Bit Score: 72.36  E-value: 1.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724  57 DLTFMGSDARLH---RTDATGSEKWSFLTG------------DIGRAYPVVTpqGVTIAASYDDTVYALDPA-GKLLWKT 120
Cdd:cd10276   166 YDVVFVGDGNGTvvaLNTGTGVDIWEFSVSeprgrtelprmiDSSVTYVVVG--GYLYSTSYQGYLVALDFEsGQFLWSR 243
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724 121 KLdGDIFATPALrADGSVIVATAGGTVHALDTQ-GRTLWTYRVGAP-VFSSPAIAADGTIYFG-AQNNRMHALTPDGKL- 196
Cdd:cd10276   244 KA-SGGTSTSTD-ANGRVYVGDGEGSLYCLDAStGDELWSQTVLLGrVLSSPAIYVGVYIYVTdNAEGYLYCLKDNDGLt 321
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1901852724 197 ----KWAYTAGSLvfSSPAIgADGTVYFGSSDRRIYAL 230
Cdd:cd10276   322 varvEVDYSQYIL--QGPAV-SDGWLYYGTDDGYLYAL 356
PRK11138 PRK11138
outer membrane biogenesis protein BamB; Provisional
72-276 4.19e-10

outer membrane biogenesis protein BamB; Provisional


Pssm-ID: 236857 [Multi-domain]  Cd Length: 394  Bit Score: 61.87  E-value: 4.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724  72 ATGSEKWSF----LTGDIGRAYPVVTPQGVTIA------ASYDDTVYALDPA-GKLLWKTKLDGDIFATPALrADGSVIV 140
Cdd:PRK11138   87 DTGKEIWSVdlseKDGWFSKNKSALLSGGVTVAggkvyiGSEKGQVYALNAEdGEVAWQTKVAGEALSRPVV-SDGLVLV 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724 141 ATAGGTVHALD-TQGRTLWTYRVGAPVF-----SSPAIAAdGTIYFGAQNNRMHALTPD-GKLKWA---YTA-GSL---- 205
Cdd:PRK11138  166 HTSNGMLQALNeSDGAVKWTVNLDVPSLtlrgeSAPATAF-GGAIVGGDNGRVSAVLMEqGQLIWQqriSQPtGATeidr 244
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724 206 ---VFSSPAIgADGTVY-----------------------FGS---------------SDRRIYALNPD-GTPRWSLPTG 243
Cdd:PRK11138  245 lvdVDTTPVV-VGGVVYalayngnlvaldlrsgqivwkreYGSvndfavdggriylvdQNDRVYALDTRgGVELWSQSDL 323
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1901852724 244 LFVNASPIVTSAGLVVVGSYDGSVYAVNP-TGEI 276
Cdd:PRK11138  324 LHRLLTAPVLYNGYLVVGDSEGYLHWINReDGRF 357
PRK11138 PRK11138
outer membrane biogenesis protein BamB; Provisional
124-270 3.63e-09

outer membrane biogenesis protein BamB; Provisional


Pssm-ID: 236857 [Multi-domain]  Cd Length: 394  Bit Score: 58.79  E-value: 3.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724 124 GDIFA--TPALrADGSVIVATAGGTVHALD-TQGRTLWT--YRVGAPVFSS--PA------IAADGTIYFGAQNNRMHAL 190
Cdd:PRK11138   57 GDYYSrlHPAV-AYNKVYAADRAGLVKALDaDTGKEIWSvdLSEKDGWFSKnkSAllsggvTVAGGKVYIGSEKGQVYAL 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724 191 -TPDGKLKWAYTAGSLVFSSPAIGaDGTVYFGSSDRRIYALNP-DGTPRWS----LPTGLFVNASPIVTSAGLVVVGSYD 264
Cdd:PRK11138  136 nAEDGEVAWQTKVAGEALSRPVVS-DGLVLVHTSNGMLQALNEsDGAVKWTvnldVPSLTLRGESAPATAFGGAIVGGDN 214

                  ....*.
gi 1901852724 265 GSVYAV 270
Cdd:PRK11138  215 GRVSAV 220
Luminal_IRE1_like cd09213
The Luminal domain, a dimerization domain, of Inositol-requiring protein 1-like proteins; The ...
138-278 9.17e-09

The Luminal domain, a dimerization domain, of Inositol-requiring protein 1-like proteins; The Luminal domain is a dimerization domain present in Inositol-requiring protein 1 (IRE1), eukaryotic translation Initiation Factor 2-Alpha Kinase 3 (EIF2AK3), and similar proteins. IRE1 and EIF2AK3 are serine/threonine protein kinases (STKs) and are type I transmembrane proteins that are localized in the endoplasmic reticulum (ER). They are kinase receptors that are activated through the release of BiP, a chaperone bound to their luminal domains under unstressed conditions. This results in dimerization through their luminal domains, allowing trans-autophosphorylation of their kinase domains and activation. They play roles in the signaling of the unfolded protein response (UPR), which is activated when protein misfolding is detected in the ER in order to decrease the synthesis of new proteins and increase the capacity of the ER to cope with the stress. IRE1, also called Endoplasmic reticulum (ER)-to-nucleus signaling protein (or ERN), contains an endoribonuclease domain in its cytoplasmic side and acts as an ER stress sensor. It is the oldest and most conserved component of the UPR in eukaryotes. Its activation results in the cleavage of its mRNA substrate, HAC1 in yeast and Xbp1 in metazoans, promoting a splicing event that enables translation into a transcription factor which activates the UPR. EIF2AK3, also called PKR-like Endoplasmic Reticulum Kinase (PERK), phosphorylates the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. It functions as the central regulator of translational control during the UPR pathway. In addition to the eIF-2 alpha subunit, EIF2AK3 also phosphorylates Nrf2, a leucine zipper transcription factor which regulates cellular redox status and promotes cell survival during the UPR.


Pssm-ID: 188873 [Multi-domain]  Cd Length: 312  Bit Score: 57.12  E-value: 9.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724 138 VIVATAGGTVHALDTQ-GRTLWTYRVGAPVFSS-----------------PAIAADGTIY-FGAQNNRMHALtpdgklkw 198
Cdd:cd09213     2 LLVATLDGTIYAVDASsGEIQWSFDGGGPLYSSyqssrdgnaessstmliPSLDGDGNLYqHDKGHGSLQRL-------- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724 199 AYTAGSLVFSSPAIGA---DGTVYFGSSDRRIYALNP-----------DGTPRWSLPTGLFVNASPIV---TSAGLVVVG 261
Cdd:cd09213    74 PLTIEDLVEASPLVSDtneDDVVVVGSKRTSVFALDAktgkiiktyraDGLPSTGGSDSDGNSTPGPDelqEEEELLYIG 153
                         170
                  ....*....|....*...
gi 1901852724 262 SYDGSVYAVNP-TGEIEW 278
Cdd:cd09213   154 RTDYVLQAIDPrSGKELW 171
PQQ_DH_like cd00216
PQQ-dependent dehydrogenases and related proteins; This family is composed of dehydrogenases ...
49-281 7.64e-08

PQQ-dependent dehydrogenases and related proteins; This family is composed of dehydrogenases with pyrroloquinoline quinone (PQQ) as a cofactor, such as ethanol, methanol, and membrane-bound glucose dehydrogenases. The alignment model contains an 8-bladed beta-propeller, and the family also includes distantly related proteins which are not enzymatically active and do not bind PQQ.


Pssm-ID: 199833 [Multi-domain]  Cd Length: 434  Bit Score: 54.92  E-value: 7.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724  49 GVTVSpnGDLTFMGS-DARLHRTDA-TGSEKWSFLTGDIGRAY-----PVVTPQGVTIAASYDDT-----VYALDPA-GK 115
Cdd:cd00216    76 GVAVW--GGKVYIGVlDGRVYALNAeTGKVAWKVKNADVLGGYtatsaPVVVDGLVIIGSSGDEFgvrgyLTAYDVAtGE 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724 116 LLWKTKLD-GDIFATPAlrADGSVIVA-TAGGTVHALDTQGRTLWtyrvgapvfSSPAIAAD-GTIYFGAQN-------- 184
Cdd:cd00216   154 EKWRFYLVmPDPNLLPG--KDSTVTDRnTPTGDEHTWTSGGGTGW---------SSAAYDAElNLIYVGGGNptpwnwgg 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724 185 ----------NRMHALTPD-GKLKWAY---------------------------------------------TAGSLVFS 208
Cdd:cd00216   223 nrtpgdnlytSSIVAVNADtGEMKWQYqttphdawdydgdntpvladikvkgkkvkvlfapakngnfyvldrRNGELVSA 302
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1901852724 209 SP----AIGADGTVYFGSSDRRIYALNPD-GTPRWSLPTGLFVNASPIVTSAGLVVVGSYDGSVYAVN-PTGEIEWTYR 281
Cdd:cd00216   303 RPlvpdSYDPDRELFYVPANGRIMALDPVtGVVVWEKSELHPLLGGPLSTAGNLVFVGTSDGYLKAYNaDTGEKLWQQK 381
NHL_like_5 cd14963
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
89-246 2.43e-07

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


Pssm-ID: 271333 [Multi-domain]  Cd Length: 268  Bit Score: 52.29  E-value: 2.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724  89 YP---VVTPQG-VTIAASYDDTVYALDPAGKLLW---KTKLDGDIFATPALRAD-GSVIVATAG-GTVHALDTQGRTLwt 159
Cdd:cd14963    57 YPygiAVDSDGnIYVADLYNGRIQVFDPDGKFLKyfpEKKDRVKLISPAGLAIDdGKLYVSDVKkHKVIVFDLEGKLL-- 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724 160 YRVGAP-----VFSSP---AIAADGTIYFG-AQNNRMHALTPDGK-LKWAY--TAGSLVFSSP---AIGADGTVYFGSS- 223
Cdd:cd14963   135 LEFGKPgsepgELSYPngiAVDEDGNIYVAdSGNGRIQVFDKNGKfIKELNgsPDGKSGFVNPrgiAVDPDGNLYVVDNl 214
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1901852724 224 DRRIYALNPDGTPRWS------------LPTGLFV 246
Cdd:cd14963   215 SHRVYVFDEQGKELFTfggrgkddgqfnLPNGLFI 249
PQQ_DH_like cd00216
PQQ-dependent dehydrogenases and related proteins; This family is composed of dehydrogenases ...
76-281 4.40e-07

PQQ-dependent dehydrogenases and related proteins; This family is composed of dehydrogenases with pyrroloquinoline quinone (PQQ) as a cofactor, such as ethanol, methanol, and membrane-bound glucose dehydrogenases. The alignment model contains an 8-bladed beta-propeller, and the family also includes distantly related proteins which are not enzymatically active and do not bind PQQ.


Pssm-ID: 199833 [Multi-domain]  Cd Length: 434  Bit Score: 52.61  E-value: 4.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724  76 EKWSFLTGDIGRAYPVVTP---QGVTIAASYDDTVYALDPA-GKLLWKTKL---DGDIFATPALRADG------SVIVAT 142
Cdd:cd00216     9 PAWSFSTGDGGNRGSELTPivvDGVMYATTSFSRVFALDADdGKEIWSYDPalkDGWFEACCDLVNRGvavwggKVYIGV 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724 143 AGGTVHALDTQ-GRTLWTYRVGAPVFS----SPAIAADGTIYFGAQNN------RMHALTP-DGKLKWAYTA-----GSL 205
Cdd:cd00216    89 LDGRVYALNAEtGKVAWKVKNADVLGGytatSAPVVVDGLVIIGSSGDefgvrgYLTAYDVaTGEEKWRFYLvmpdpNLL 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724 206 VFSSPAIGADGTVYFGSSDRRIYALNPDGTPRWSLPTGLFV----NASPIVTSAGLVVVGS-YDGSVYAVNP-TGEIEWT 279
Cdd:cd00216   169 PGKDSTVTDRNTPTGDEHTWTSGGGTGWSSAAYDAELNLIYvgggNPTPWNWGGNRTPGDNlYTSSIVAVNAdTGEMKWQ 248

                  ..
gi 1901852724 280 YR 281
Cdd:cd00216   249 YQ 250
YvrE COG3386
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase ...
130-237 7.95e-07

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


Pssm-ID: 442613 [Multi-domain]  Cd Length: 266  Bit Score: 50.66  E-value: 7.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724 130 PALRADGSVIVA-TAGGTVHALDTQGRTLWTYRVGAPVFSSPAIAADGTIYFGAQNNRMHALTP-DGKLKWAYTAGSLVF 207
Cdd:COG3386    13 PVWDPDGRLYWVdIPGGRIHRYDPDGGAVEVFAEPSGRPNGLAFDPDGRLLVADHGRGLVRFDPaDGEVTVLADEYGKPL 92
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1901852724 208 SSP---AIGADGTVYFGSSDR-----RIYALNPDGTPR 237
Cdd:COG3386    93 NRPndgVVDPDGRLYFTDMGEylptgALYRVDPDGSLR 130
PQQ_DH_like cd00216
PQQ-dependent dehydrogenases and related proteins; This family is composed of dehydrogenases ...
153-280 2.41e-06

PQQ-dependent dehydrogenases and related proteins; This family is composed of dehydrogenases with pyrroloquinoline quinone (PQQ) as a cofactor, such as ethanol, methanol, and membrane-bound glucose dehydrogenases. The alignment model contains an 8-bladed beta-propeller, and the family also includes distantly related proteins which are not enzymatically active and do not bind PQQ.


Pssm-ID: 199833 [Multi-domain]  Cd Length: 434  Bit Score: 49.91  E-value: 2.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724 153 QGRTLWTYRVGAPV---FSSPAIAADGTIYFGAQNNRMHAL-TPDGKLKWAYT---------AGSLVFSSPAIGADGTVY 219
Cdd:cd00216     6 QLTPAWSFSTGDGGnrgSELTPIVVDGVMYATTSFSRVFALdADDGKEIWSYDpalkdgwfeACCDLVNRGVAVWGGKVY 85
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1901852724 220 FGSSDRRIYALNP-DGTPRWSLPT----GLFVNASPIVTSAGLVVVGS------YDGSVYAVNP-TGEIEWTY 280
Cdd:cd00216    86 IGVLDGRVYALNAeTGKVAWKVKNadvlGGYTATSAPVVVDGLVIIGSsgdefgVRGYLTAYDVaTGEEKWRF 158
PQQ_MDH cd10278
Large subunit of methanol dehydrogenase (moxF); Methanol dehydrogenase is a key enzyme in the ...
78-204 5.17e-06

Large subunit of methanol dehydrogenase (moxF); Methanol dehydrogenase is a key enzyme in the utilization of C1 compounds as a source of energy and carbon by bacteria. It catalyzes the oxidation of methanol to formaldehyde, transfering two electrons per methanol to cytochrome c(L) as the acceptor. Methanol dehydrogenase belongs to a family of dehydrogenases with pyrroloquinoline quinone (PQQ) as cofactor, which also includes dehydrogenases specific to other alcohols and membrane-bound glucose dehydrogenases. This alignment model for the large subunit contains an 8-bladed beta-propeller; the functional enzyme forms a heterotetramer composed of two large and two small subunits.


Pssm-ID: 199836 [Multi-domain]  Cd Length: 553  Bit Score: 49.25  E-value: 5.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724  78 WSFLTGDIG--RAYPVVTPQGVTIAASYDDTVYALD--PAGKLLWKTKLDGDIFATP----------ALRADGSVIVATA 143
Cdd:cd10278    31 WTFSTGVLRghEGAPLVVGDTMYVVTPFPNNVYALDlnDPGKILWKYKPKQDPSAVAvaccdvvnrgLAYADGKIFFNQL 110
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1901852724 144 GGTVHALDTQ-GRTLWTYRVGAP-----VFSSPAIAADGTIY------FGAQnNRMHAL-TPDGKLKW-AYTAGS 204
Cdd:cd10278   111 DGHLVALDAKtGKEVWKVKNGDPkvgetLTMAPLVVKDKVIVgisggeFGVR-GYVTAYdLKTGKLVWrAYSTGP 184
PQQ_3 pfam13570
PQQ-like domain;
154-190 6.94e-06

PQQ-like domain;


Pssm-ID: 463925 [Multi-domain]  Cd Length: 36  Bit Score: 42.96  E-value: 6.94e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1901852724 154 GRTLWTYRVGAPVFSSPAIaADGTIYFGAQNNRMHAL 190
Cdd:pfam13570   1 GEVLWRFETGGPIVSSPAV-AGGLVYVGTGDGTLYAL 36
PQQ COG1520
Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell ...
44-232 6.94e-06

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: 48.27  E-value: 6.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724  44 LRVISGVTVSpnGDLTFMGSDA-RLHRTDA-TGSEKWSfltgdigraYPVVTPQGVT-------------------IAAS 102
Cdd:COG1520   172 LRGTSSPVIV--GGAVLVGFANgKLVALDLaNGQPLWE---------QRVAQPRGRTelerlvdvdgtpvvdggvvYAVA 240
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724 103 YDDTVYALDPA-GKLLWKTKLDGdiFATPALrADGSVIVATAGGTVHALDTQ-GRTLWT-----YR-VGAPVFSSPAIA- 173
Cdd:COG1520   241 YQGRLAALDLRsGRVLWSRDLSS--YTGLAV-DGNNLYVTDDDGRVWALDRRnGAELWKqdallYRgLTAPVVLGDYVVv 317
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724 174 ADGTIYfgaqnnrMHALTP-DGKLKWAYTAGSLVFSSPAIGADGTVYFGSSDRRIYALNP 232
Cdd:COG1520   318 GDFEGY-------LHWLSRdDGSLVARLRVDGSGIRAAPVVVGDTLYVQTRDGTLAALRL 370
PQQ COG1520
Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell ...
209-320 9.95e-06

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: 47.89  E-value: 9.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724 209 SPAIgADGTVYFGSSDRRIYALNPD-GTPRWSLPTGLFVnASPIVTSAGLVVVGSYDGSVYAVNP-TGEIEWTYRAGAGI 286
Cdd:COG1520    52 APAV-AGDRVYAADADGRVAALDAAtGKELWRVDLGEPL-SGGVGADGGLVVVGTEDGEVIALDAdDGEELWRARLSSEV 129
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1901852724 287 AGSAAeLSDGSVIVPDLAGTVHAI-GKAGQSLWQI 320
Cdd:COG1520   130 LAAPA-VAGGRVVVRTGDGRVYALdAATGERLWSY 163
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
130-346 1.10e-05

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 47.32  E-value: 1.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724 130 PALRADGSV-IVATAGGTVHALDTQGRTLWTYRVGApvFSSP---AIAADGTIYF-GAQNNRMHALTP-DGKLK-WAYTA 202
Cdd:COG4257    22 VAVDPDGAVwFTDQGGGRIGRLDPATGEFTEYPLGG--GSGPhgiAVDPDGNLWFtDNGNNRIGRIDPkTGEITtFALPG 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724 203 GSLVFSSPAIGADGTVYF-GSSDRRIYALNPDgTPRWSLPTGLFVNASP---IVTSAGLVVVGSYDGS-VYAVNP-TGEI 276
Cdd:COG4257   100 GGSNPHGIAFDPDGNLWFtDQGGNRIGRLDPA-TGEVTEFPLPTGGAGPygiAVDPDGNLWVTDFGANaIGRIDPdTGTL 178
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1901852724 277 -EWTYRAGAGIAGSAAELSDGSVIVPDLAGtvHAIGK----AGQ-SLWQIKTGKKIDLGVSVSDQGSVYFTTEGGG 346
Cdd:COG4257   179 tEYALPTPGAGPRGLAVDPDGNLWVADTGS--GRIGRfdpkTGTvTEYPLPGGGARPYGVAVDGDGRVWFAESGAN 252
PQQ smart00564
beta-propeller repeat; Beta-propeller repeat occurring in enzymes with pyrrolo-quinoline ...
250-281 2.06e-05

beta-propeller repeat; Beta-propeller repeat occurring in enzymes with pyrrolo-quinoline quinone (PQQ) as cofactor, in Ire1p-like Ser/Thr kinases, and in prokaryotic dehydrogenases.


Pssm-ID: 128836 [Multi-domain]  Cd Length: 33  Bit Score: 41.37  E-value: 2.06e-05
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1901852724  250 PIVTSAGLVVVGSYDGSVYAVNP-TGEIEWTYR 281
Cdd:smart00564   1 PVVLSDGTVYVGSTDGTLYALDAkTGEILWTYK 33
PQQ_mGDH cd10280
Membrane-bound PQQ-dependent glucose dehydrogenase; This bacterial subfamily of enzymes ...
158-279 2.16e-05

Membrane-bound PQQ-dependent glucose dehydrogenase; This bacterial subfamily of enzymes belongs to the dehydrogenase family with pyrroloquinoline quinone (PQQ) as cofactor, and is the only subfamily that is bound to the membrane. Glucose dehydrogenase converts D-glucose to D-glucono-1,5-lactone in a reaction that is coupled with the respiratory chain in the periplasmic oxidation of sugars and alcohols in gram-negative bacteria. Ubiquinone functions as the electron acceptor. The alignment model contains an 8-bladed beta-propeller.


Pssm-ID: 199838 [Multi-domain]  Cd Length: 616  Bit Score: 47.19  E-value: 2.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724 158 WTYRVGAPVFSSPA--------IAADGTIYFGAQNNRMHALTPD-GKLKWAYTAGSLVFSSPAIGA-------------- 214
Cdd:cd10280    31 WTYHTGDLPGPDGNegtfeatpLKVGGTLYLCTPHNRVIALDAAtGKELWRFDPKAGADAAPGHQTcrgvsywedgaaaa 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724 215 --DGTVYFGSSDRRIYALNPD-GTPRWS---------------LPTGLFVNASPIVTSAGLVVVGS--YDGsVYAVNP-- 272
Cdd:cd10280   111 acARRIFFGTGDARLIALDARtGKPCPDfgdngvvdlreglgrVKPGFYSSTSPPTVYGDLVIVGSavADN-QAVDAPsg 189
                         170
                  ....*....|....*
gi 1901852724 273 --------TGEIEWT 279
Cdd:cd10280   190 virafdvrTGKLVWA 204
PQQ_3 pfam13570
PQQ-like domain;
194-230 2.44e-05

PQQ-like domain;


Pssm-ID: 463925 [Multi-domain]  Cd Length: 36  Bit Score: 41.42  E-value: 2.44e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1901852724 194 GKLKWAYTAGSLVFSSPAIgADGTVYFGSSDRRIYAL 230
Cdd:pfam13570   1 GEVLWRFETGGPIVSSPAV-AGGLVYVGTGDGTLYAL 36
PQQ_mGDH cd10280
Membrane-bound PQQ-dependent glucose dehydrogenase; This bacterial subfamily of enzymes ...
90-145 3.03e-05

Membrane-bound PQQ-dependent glucose dehydrogenase; This bacterial subfamily of enzymes belongs to the dehydrogenase family with pyrroloquinoline quinone (PQQ) as cofactor, and is the only subfamily that is bound to the membrane. Glucose dehydrogenase converts D-glucose to D-glucono-1,5-lactone in a reaction that is coupled with the respiratory chain in the periplasmic oxidation of sugars and alcohols in gram-negative bacteria. Ubiquinone functions as the electron acceptor. The alignment model contains an 8-bladed beta-propeller.


Pssm-ID: 199838 [Multi-domain]  Cd Length: 616  Bit Score: 46.80  E-value: 3.03e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724  90 PVVTPQGVT-IAASYDDTVYALDPA-GKLLWKTKLDGDIFATPAL-RADG-SVIVATAGG 145
Cdd:cd10280   540 PVVTAGGLVfIAATQDNYLRAFDKAtGKELWEARLPAGGQATPMTyEVDGkQYVVIAAGG 599
YvrE COG3386
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase ...
37-196 4.88e-05

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


Pssm-ID: 442613 [Multi-domain]  Cd Length: 266  Bit Score: 45.27  E-value: 4.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724  37 KVSVFKEL-RVISGVTVSPNGDLTFMGSDARLHRTD-ATGSEKWSFLTGDIGRAYP---VVTPQG---VTIAASYDDT-- 106
Cdd:COG3386    40 AVEVFAEPsGRPNGLAFDPDGRLLVADHGRGLVRFDpADGEVTVLADEYGKPLNRPndgVVDPDGrlyFTDMGEYLPTga 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724 107 VYALDPAGKLlwkTKLDGDIFAT--PALRADGS-VIVA-TAGGTVHALDTQG-RTLWTYRVGAPVFSSP------AIAAD 175
Cdd:COG3386   120 LYRVDPDGSL---RVLADGLTFPngIAFSPDGRtLYVAdTGAGRIYRFDLDAdGTLGNRRVFADLPDGPggpdglAVDAD 196
                         170       180
                  ....*....|....*....|..
gi 1901852724 176 GTIYFGA-QNNRMHALTPDGKL 196
Cdd:COG3386   197 GNLWVALwGGGGVVRFDPDGEL 218
YvrE COG3386
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase ...
169-277 5.02e-05

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


Pssm-ID: 442613 [Multi-domain]  Cd Length: 266  Bit Score: 45.27  E-value: 5.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724 169 SPAIAADGTIYF-GAQNNRMHALTPDGKLKWAYTAGSLVFSSPAIGADGTVYFGSSDRRIYALNP-DGTPRWSLPTGLFV 246
Cdd:COG3386    12 GPVWDPDGRLYWvDIPGGRIHRYDPDGGAVEVFAEPSGRPNGLAFDPDGRLLVADHGRGLVRFDPaDGEVTVLADEYGKP 91
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1901852724 247 NASP---IVTSAGLVVVGSYD-----GSVYAVNPTGEIE 277
Cdd:COG3386    92 LNRPndgVVDPDGRLYFTDMGeylptGALYRVDPDGSLR 130
PQQ_ADH_I cd10277
Ethanol dehydrogenase, a bacterial quinoprotein (PQQ-dependent type I alcohol dehydrogenase); ...
55-165 8.60e-05

Ethanol dehydrogenase, a bacterial quinoprotein (PQQ-dependent type I alcohol dehydrogenase); This bacterial family of homodimeric ethanol dehydrogenases utilize pyrroloquinoline quinone (PQQ) as a cofactor. It represents proteins whose expression may be induced by ethanol, and which are similar to quinoprotein methanol dehydrogenases, but have higher specificities for ethanol and other primary and secondary alcohols. Dehydrogenases with PQQ cofactors, such as ethanol, methanol, and membrane-bound glucose dehydrogenases, form an 8-bladed beta-propeller.


Pssm-ID: 199835 [Multi-domain]  Cd Length: 529  Bit Score: 45.37  E-value: 8.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724  55 NGDLTFMGSDARLHRTDA-TGSEKWSF---LTGDIGRAYPVVTpQGVtiaASYDDTVY---------ALDPA-GKLLWKT 120
Cdd:cd10277    60 DGVMYVTTSYNRVFAIDAkTGKELWKYkhrLPEDIRPCCDVVN-RGV---ALYGDKVYfgtldahlvALDAKtGKVVWKK 135
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1901852724 121 KLD----GDIFATPALRADGSVIVATAG------GTVHALDTQ-GRTLW-TYRVGAP 165
Cdd:cd10277   136 KVAdykaGYSMTLAPLVVKGKVIVGVSGgefgvrGFIAALDAEtGKEVWrTYTVPGP 192
NHL_PAL_like cd14958
Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5); PAL catalyzes the ...
44-339 9.85e-05

Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5); PAL catalyzes the N-dealkylation of peptidyl-alpha-hydroxyglycine, which results in an alpha-amidated peptide and glyoxylate. Amidation of the C-terminus is required for the activity of many peptide hormones and neuropeptides. The catalytic residues of PAL are located on several NHL-repeats. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.


Pssm-ID: 271328 [Multi-domain]  Cd Length: 300  Bit Score: 44.56  E-value: 9.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724  44 LRVISGVTVSPNGDLTFmgsdarLHRTDAtgseKWSFLTGDiGRAYpvvtpqgVTIAASYDDTVYALDPAGKLLwkTKLD 123
Cdd:cd14958    12 LGQVSGVAVDSLGNGVV------FHRGGR----VWDANSFD-ANVY-------VFKGPIEEDTILVFDPDGGFL--RSWG 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724 124 GDIFATP-ALR--ADGSV-IVATAGGTVHALDTQGR--TLWTY----RVGAPV--FSSP---AIAADGTIYF--GAQNNR 186
Cdd:cd14958    72 AGLFYMPhGLTidPDGNIwVTDVGLHQVFKFDPEGKllPLLTLgergEPGSDQthFCKPtdvAVAPDGDIFVadGYCNSR 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724 187 MHALTPDGKL--KW-AYTAGSLVFSSP---AIGADGTVYFGssDR---RIYALNPDGTPR--WSLPTGlfvnaspivtsa 255
Cdd:cd14958   152 IVKFSPDGKLlkSWgEPGSGPGQFNLPhsiALDEDGRVYVA--DRengRIQVFDADGKFLteWTNPEL------------ 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724 256 GLVVVGSYDGS--VYAVNptGEIEWTYRAGagiagsaaelSDGSVIVPDLAGTVHAIGKAGQSLWQIKTGKkidlGVSVS 333
Cdd:cd14958   218 GRPYALAIDPDglLYVVD--GPPRLNRSLP----------VRGFVIRIGKGLILGRFGPGGKAPGQFQNPH----DIAVD 281

                  ....*.
gi 1901852724 334 DQGSVY 339
Cdd:cd14958   282 SGGDIY 287
PQQ_3 pfam13570
PQQ-like domain;
114-150 1.15e-04

PQQ-like domain;


Pssm-ID: 463925 [Multi-domain]  Cd Length: 36  Bit Score: 39.49  E-value: 1.15e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1901852724 114 GKLLWKTKLDGDIFATPALrADGSVIVATAGGTVHAL 150
Cdd:pfam13570   1 GEVLWRFETGGPIVSSPAV-AGGLVYVGTGDGTLYAL 36
PQQ_ADH_I cd10277
Ethanol dehydrogenase, a bacterial quinoprotein (PQQ-dependent type I alcohol dehydrogenase); ...
158-279 1.20e-04

Ethanol dehydrogenase, a bacterial quinoprotein (PQQ-dependent type I alcohol dehydrogenase); This bacterial family of homodimeric ethanol dehydrogenases utilize pyrroloquinoline quinone (PQQ) as a cofactor. It represents proteins whose expression may be induced by ethanol, and which are similar to quinoprotein methanol dehydrogenases, but have higher specificities for ethanol and other primary and secondary alcohols. Dehydrogenases with PQQ cofactors, such as ethanol, methanol, and membrane-bound glucose dehydrogenases, form an 8-bladed beta-propeller.


Pssm-ID: 199835 [Multi-domain]  Cd Length: 529  Bit Score: 44.98  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724 158 WTYRVGAPV--FSSPAIAADGTIYFGAQNNRMHALTPD-GKLKWAY----TAGSLVFSSP----AIGADGTVYFGSSDRR 226
Cdd:cd10277    41 WSFSFGGKQrgQESQPIVNDGVMYVTTSYNRVFAIDAKtGKELWKYkhrlPEDIRPCCDVvnrgVALYGDKVYFGTLDAH 120
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1901852724 227 IYALNPD-GTPRWSLP-----TGLFVNASPIVTSaGLVVVGSYDGS------VYAVNP-TGEIEWT 279
Cdd:cd10277   121 LVALDAKtGKVVWKKKvadykAGYSMTLAPLVVK-GKVIVGVSGGEfgvrgfIAALDAeTGKEVWR 185
NHL_like_3 cd14956
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
41-271 5.32e-04

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


Pssm-ID: 271326 [Multi-domain]  Cd Length: 274  Bit Score: 42.27  E-value: 5.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724  41 FKELRvisGVTVSPNGDLTFmgSDARLHRT---DATGSEK---WSFLTGDIGRAYP---VVTPQG-VTIAASYDDTVYAL 110
Cdd:cd14956    12 FKDPR---GIAVDADDNVYV--ADARNGRIqvfDKDGTFLrrfGTTGDGPGQFGRPrglAVDKDGwLYVADYWGDRIQVF 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724 111 DPAGKLLWKTKLDGD---IFATP---ALRADGSVIVATAGGT-VHALDTQGRTL--WTYRVGAPV-FSSP---AIAADGT 177
Cdd:cd14956    87 TLTGELQTIGGSSGSgpgQFNAPrgvAVDADGNLYVADFGNQrIQKFDPDGSFLrqWGGTGIEPGsFNYPrgvAVDPDGT 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724 178 IYFG-AQNNRMHALTPDGKL--KWAYT-AGSLVFSSP---AIGADGTVYFGSSD-RRIYALNPDGTPRWSL---PTGLFV 246
Cdd:cd14956   167 LYVAdTYNDRIQVFDNDGAFlrKWGGRgTGPGQFNYPygiAIDPDGNVFVADFGnNRIQKFTADGTFLTSWgspGTGPGQ 246
                         250       260
                  ....*....|....*....|....*
gi 1901852724 247 NASPIvtsaGLVVVGsyDGSVYAVN 271
Cdd:cd14956   247 FKNPW----GVVVDA--DGTVYVAD 265
Luminal_IRE1 cd09769
The Luminal domain, a dimerization domain, of the Serine/Threonine protein kinase, ...
138-232 1.43e-03

The Luminal domain, a dimerization domain, of the Serine/Threonine protein kinase, Inositol-requiring protein 1; The Luminal domain is a dimerization domain present in Inositol-requiring protein 1 (IRE1), a serine/threonine protein kinase (STK) and a type I transmembrane protein that is localized in the endoplasmic reticulum (ER). IRE1, also called Endoplasmic reticulum (ER)-to-nucleus signaling protein (or ERN), is a kinase receptor that also contains an endoribonuclease domain in the cytoplasmic side. It plays roles in the signaling of the unfolded protein response (UPR), which is activated when protein misfolding is detected in the ER in order to decrease the synthesis of new proteins and increase the capacity of the ER to cope with the stress. IRE1 acts as an ER stress sensor and is the oldest and most conserved component of the UPR in eukaryotes. During ER stress, IRE1 dimerizes through its luminal domain and forms oligomers, allowing the kinase domain to undergo trans-autophosphorylation. This leads to a conformational change that stimulates its endoribonuclease activity and results in the cleavage of its mRNA substrate, HAC1 in yeast and Xbp1 in metazoans, promoting a splicing event that enables translation into a transcription factor which activates the UPR. Mammals contain two IRE1 proteins, IRE1alpha (or ERN1) and IRE1beta (or ERN2). IRE1alpha is expressed in all cells and tissues while IRE1beta is found only in intestinal epithelial cells.


Pssm-ID: 188875 [Multi-domain]  Cd Length: 295  Bit Score: 40.76  E-value: 1.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724 138 VIVATAGGTVHALD-TQGRTLWTYRVGAPVFSSPAIAA-------------DGTIYFGAQNNrmhaltpDGKLKWAYTAG 203
Cdd:cd09769     4 LLVSTVDGGLHAVDrKTGKILWSLKAEDPLVEVPHHSTlsidgptfiveprDGSLYVLNPGN-------EGLKKLPFTIP 76
                          90       100
                  ....*....|....*....|....*....
gi 1901852724 204 SLVFSSPAIGADGTVYFGSSDRRIYALNP 232
Cdd:cd09769    77 QLVQSSPCRSSDGILYTGSKQTTWYTVDP 105
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
49-196 1.78e-03

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 40.39  E-value: 1.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724  49 GVTVSPNGDLTF-MGSDARLHRTDaTGSEKWSFLTGDIGRAYP---VVTPQG-VTIAASYDDTVYALDPAGKLLWKTKLD 123
Cdd:COG4257   106 GIAFDPDGNLWFtDQGGNRIGRLD-PATGEVTEFPLPTGGAGPygiAVDPDGnLWVTDFGANAIGRIDPDTGTLTEYALP 184
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901852724 124 GDiFATP---ALRADGSV-IVATAGGTVHALDTQGRTLWTYRVGAPVFSSPAIAAD--GTIYFGAQ-NNRMHALTPDGKL 196
Cdd:COG4257   185 TP-GAGPrglAVDPDGNLwVADTGSGRIGRFDPKTGTVTEYPLPGGGARPYGVAVDgdGRVWFAESgANRIVRFDPDTEL 263
PQQ smart00564
beta-propeller repeat; Beta-propeller repeat occurring in enzymes with pyrrolo-quinoline ...
210-241 2.59e-03

beta-propeller repeat; Beta-propeller repeat occurring in enzymes with pyrrolo-quinoline quinone (PQQ) as cofactor, in Ire1p-like Ser/Thr kinases, and in prokaryotic dehydrogenases.


Pssm-ID: 128836 [Multi-domain]  Cd Length: 33  Bit Score: 35.59  E-value: 2.59e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1901852724  210 PAIGADGTVYFGSSDRRIYALNP-DGTPRWSLP 241
Cdd:smart00564   1 PVVLSDGTVYVGSTDGTLYALDAkTGEILWTYK 33
PQQ smart00564
beta-propeller repeat; Beta-propeller repeat occurring in enzymes with pyrrolo-quinoline ...
170-201 3.45e-03

beta-propeller repeat; Beta-propeller repeat occurring in enzymes with pyrrolo-quinoline quinone (PQQ) as cofactor, in Ire1p-like Ser/Thr kinases, and in prokaryotic dehydrogenases.


Pssm-ID: 128836 [Multi-domain]  Cd Length: 33  Bit Score: 35.20  E-value: 3.45e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1901852724  170 PAIAADGTIYFGAQNNRMHALTP-DGKLKWAYT 201
Cdd:smart00564   1 PVVLSDGTVYVGSTDGTLYALDAkTGEILWTYK 33
PQQ pfam01011
PQQ enzyme repeat; The family represent a single repeat of a beta propeller. This propeller ...
256-281 3.81e-03

PQQ enzyme repeat; The family represent a single repeat of a beta propeller. This propeller has been found in several enzymes which utilize pyrrolo-quinoline quinone as a prosthetic group.


Pssm-ID: 395799 [Multi-domain]  Cd Length: 36  Bit Score: 35.25  E-value: 3.81e-03
                          10        20
                  ....*....|....*....|....*..
gi 1901852724 256 GLVVVGSYDGSVYAVN-PTGEIEWTYR 281
Cdd:pfam01011   1 GTVYLGSDDGYLYALDaETGKVLWSFK 27
PQQ_3 pfam13570
PQQ-like domain;
234-270 6.83e-03

PQQ-like domain;


Pssm-ID: 463925 [Multi-domain]  Cd Length: 36  Bit Score: 34.49  E-value: 6.83e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1901852724 234 GTPRWSLPTGLFVNASPiVTSAGLVVVGSYDGSVYAV 270
Cdd:pfam13570   1 GEVLWRFETGGPIVSSP-AVAGGLVYVGTGDGTLYAL 36
PQQ smart00564
beta-propeller repeat; Beta-propeller repeat occurring in enzymes with pyrrolo-quinoline ...
90-121 7.66e-03

beta-propeller repeat; Beta-propeller repeat occurring in enzymes with pyrrolo-quinoline quinone (PQQ) as cofactor, in Ire1p-like Ser/Thr kinases, and in prokaryotic dehydrogenases.


Pssm-ID: 128836 [Multi-domain]  Cd Length: 33  Bit Score: 34.43  E-value: 7.66e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1901852724   90 PVVTPQGVTIAASYDDTVYALDPA-GKLLWKTK 121
Cdd:smart00564   1 PVVLSDGTVYVGSTDGTLYALDAKtGEILWTYK 33
 
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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