|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11138 |
PRK11138 |
outer membrane biogenesis protein BamB; Provisional |
1-393 |
0e+00 |
|
outer membrane biogenesis protein BamB; Provisional
Pssm-ID: 236857 [Multi-domain] Cd Length: 394 Bit Score: 748.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362902 1 MQLRKTLLVGLVSAALLSGCSLFNSEEDVVTMSPLPKVENQFTPSKAWSTSVGDGIGEYYSHLRPAYQDSTIYAADRFGI 80
Cdd:PRK11138 1 MQLRKTLLPGLLSVTLLSGCSSFNSEEDVVKMSPLPQVENQFTPTTVWSTSVGDGVGDYYSRLHPAVAYNKVYAADRAGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362902 81 VKAMDADSGNEKWKVNLSEKTGFFSSNLSALLSGGLTVAGDKVYVGSEKAVVYALNTADGAIAWQTKVAGEAISRPVISD 160
Cdd:PRK11138 81 VKALDADTGKEIWSVDLSEKDGWFSKNKSALLSGGVTVAGGKVYIGSEKGQVYALNAEDGEVAWQTKVAGEALSRPVVSD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362902 161 GMVLVHTSNGMLQALNEADGAVKWTVNLDMPSLSLRGESAPAVAFGAAIVGGDNGRVSAVLMQQGQLIWQQRISQPSGAT 240
Cdd:PRK11138 161 GLVLVHTSNGMLQALNESDGAVKWTVNLDVPSLTLRGESAPATAFGGAIVGGDNGRVSAVLMEQGQLIWQQRISQPTGAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362902 241 EIDRLNDVDTTPVIVDGVVYALGYNGNLTALDLRSGQIIWKRELGSVNDFIVDAGRIYLIDQNDRVVALSTEGGVTVWTQ 320
Cdd:PRK11138 241 EIDRLVDVDTTPVVVGGVVYALAYNGNLVALDLRSGQIVWKREYGSVNDFAVDGGRIYLVDQNDRVYALDTRGGVELWSQ 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 644362902 321 SDLLHRNLTPPVMYNGYLVTGDAEGYLHWVNTTDGRFVAQQEVDSSGFLSAPMVAGDKLVIQARGGKVYAFTR 393
Cdd:PRK11138 321 SDLLHRLLTAPVLYNGYLVVGDSEGYLHWINREDGRFVAQQKVDSSGFLSEPVVADDKLLIQARDGTVYAITR 393
|
|
| PQQ |
COG1520 |
Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell ... |
13-393 |
7.23e-176 |
|
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: 494.33 E-value: 7.23e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362902 13 SAALLSGCSLFNSEEDVVTMSPLPKVENQFTPSKAWSTSVGDGIGEYYSHLRPAYQDSTIYAADRFGIVKAMDADSGNEK 92
Cdd:COG1520 1 LLLLLLLLSGFSSEDDEPPPAPLPEFEPSVKVKQLWSASVGDGVGKGYSRLAPAVAGDRVYAADADGRVAALDAATGKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362902 93 WKVNLSEKtgffssnlsalLSGGLTVAGDKVYVGSEKAVVYALNTADGAIAWQTKVAGEAISRPVISDGMVLVHTSNGML 172
Cdd:COG1520 81 WRVDLGEP-----------LSGGVGADGGLVVVGTEDGEVIALDADDGEELWRARLSSEVLAAPAVAGGRVVVRTGDGRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362902 173 QALNEADGAVKWTVNLDMPSLSLRGESAPAVAFGAAIVGGDNGRVSAVLMQQGQLIWQQRISQPSGATEIDRLNDVDTTP 252
Cdd:COG1520 150 YALDAATGERLWSYQRPVPALTLRGTSSPVIVGGAVLVGFANGKLVALDLANGQPLWEQRVAQPRGRTELERLVDVDGTP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362902 253 VIVDGVVYALGYNGNLTALDLRSGQIIWKRELGSVNDFIVDAGRIYLIDQNDRVVALSTEGGVTVWTQSDLLHRNLTPPV 332
Cdd:COG1520 230 VVDGGVVYAVAYQGRLAALDLRSGRVLWSRDLSSYTGLAVDGNNLYVTDDDGRVWALDRRNGAELWKQDALLYRGLTAPV 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 644362902 333 MYNGYLVTGDAEGYLHWVNTTDGRFVAQQEVDSSGFLSAPMVAGDKLVIQARGGKVYAFTR 393
Cdd:COG1520 310 VLGDYVVVGDFEGYLHWLSRDDGSLVARLRVDGSGIRAAPVVVGDTLYVQTRDGTLAALRL 370
|
|
| assembly_YfgL |
TIGR03300 |
outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a ... |
5-392 |
1.67e-163 |
|
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: 463.25 E-value: 1.67e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362902 5 KTLLVGLVSAALLSGCSLFNSEEDVVTMSPLPKVENQFTPSKAWSTSVGDGIGEYYSHLRPAYQDSTIYAADRFGIVKAM 84
Cdd:TIGR03300 1 KRLALVLACAALLSGCSWFSSEDDEPQPAELPEFQPTVKVDQVWSASVGDGVGHYYLRLQPAVAGGKVYAADADGTVAAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362902 85 DADSGNEKWKVNLSEKtgffssnlsalLSGGLTVAGDKVYVGSEKAVVYALNTADGAIAWQTKVAGEAISRPVISDGMVL 164
Cdd:TIGR03300 81 DAETGKRLWRVDLDER-----------LSGGVGADGGLVFVGTEKGEVIALDAEDGKELWRAKLSSEVLSPPLVANGLVV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362902 165 VHTSNGMLQALNEADGAVKWTVNLDMPSLSLRGESAPAVAFGAAIVGGDNGRVSAVLMQQGQLIWQQRISQPSGATEIDR 244
Cdd:TIGR03300 150 VRTNDGRLTALDAATGERLWTYSRVTPPLTLRGSASPVIADGGVLVGFAGGKLVALDLQTGQPLWEQRVALPKGRTELER 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362902 245 LNDVDTTPVIVDGVVYALGYNGNLTALDLRSGQIIWKRELGSVNDFIVDAGRIYLIDQNDRVVALSTEGGVTVWTQSDLL 324
Cdd:TIGR03300 230 LVDVDGDPVVDGGQVYAVSYQGRVAALDLRSGRVLWKRDASSYQGPAVDDNRLYVTDADGVVVALDRRSGSELWKNDELK 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 644362902 325 HRNLTPPVMYNGYLVTGDAEGYLHWVNTTDGRFVAQQEVDSSGFLSAPMVAGDKLVIQARGGKVYAFT 392
Cdd:TIGR03300 310 YRQLTAPAVLGGYLVVGDFEGYLHWLDRDDGSFVARLKTDGSGIASPPVVVGDGLLVQTRDGDLYAFR 377
|
|
| BamB_YfgL |
cd10276 |
Beta-barrel assembly machinery (Bam) complex component B and related proteins; BamB (YflG) is ... |
32-393 |
7.75e-109 |
|
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: 323.51 E-value: 7.75e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362902 32 MSPLPKVENQFTPSKAWSTSVGDGiGEYYSHLRPAYQDSTIYAADRFGIVKAMDADSGNEKWKVNLSEKtgffssnlsAL 111
Cdd:cd10276 2 PTDLPEPTPEFDPEVLWSKSVGNG-GMAGIDLTPVVAGDMVYAADANGQVSAFNATTGKIIWETSLSGK---------GF 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362902 112 LSGGLTVAGDKVYVGSEKAVVYALNTADGAIAWQTKVA-GEAISRPVISDGMVLVHTSNGMLQALNEADGAVKWTVNLDM 190
Cdd:cd10276 72 LGGTPAVGNGKIFVGTESGYLYALDAKDGSELWRTEVSdSQLLSPPTYADGKIYVGTGDGRLYYCNAETGKVVWNRTSTA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362902 191 PSLSLRGESAPAVAFGAAIVGGDNGRVSAVLMQQGQLIWQQRISQPSGATEIDRLNDVDTTPVIVDGVVYALGYNGNLTA 270
Cdd:cd10276 152 PELSLRGGAAPVGAYDVVFVGDGNGTVVALNTGTGVDIWEFSVSEPRGRTELPRMIDSSVTYVVVGGYLYSTSYQGYLVA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362902 271 LDLRSGQIIWKRELGSVNDFIVDA-GRIYLIDQNDRVVALSTEGGVTVWTQSDLLHRNLTPPVMY-NGYLVTGD-AEGYL 347
Cdd:cd10276 232 LDFESGQFLWSRKASGGTSTSTDAnGRVYVGDGEGSLYCLDASTGDELWSQTVLLGRVLSSPAIYvGVYIYVTDnAEGYL 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 644362902 348 HWVNTTDGRFVAQQEVDSS-GFLSAPMVAGDKLVIQARGGKVYAFTR 393
Cdd:cd10276 312 YCLKDNDGLTVARVEVDYSqYILQGPAVSDGWLYYGTDDGYLYALTR 358
|
|
| PQQ_2 |
pfam13360 |
PQQ-like domain; This domain contains several repeats of the PQQ repeat. |
77-320 |
9.70e-63 |
|
PQQ-like domain; This domain contains several repeats of the PQQ repeat.
Pssm-ID: 433144 [Multi-domain] Cd Length: 233 Bit Score: 201.09 E-value: 9.70e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362902 77 RFGIVKAMDADSGNEKWKVNLSEKtgffssnlsalLSGGLTVAGDKVYVGSEKAVVYALNTADGAIAWQTKVAGEAISRP 156
Cdd:pfam13360 1 ADGVVTALDAATGAELWRVDLETG-----------LGGGVAVDGGRLFVATGGGQLVALDAATGKLLWRQTLSGEVLGAP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362902 157 VISDGMVLVHTSNGMLQALNEADGAVKWTVNLDMPSLSLRGESAPAVAFGAAIVGGDNGRVSAVLMQQGQLIWQQRISQP 236
Cdd:pfam13360 70 LVAGGRVFVVAGDGSLIALDAADGRRLWSYQRSGEPLALRSSGSPAVVGDTVVAGFSSGKLVALDPATGKVRWEAPLAAP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362902 237 SGATEIDRLNDVDTTPVIVDGVVYALGYNGNLTALDLRSGQIIWKRELGSVNDFIVDAGRIYLIDQNDRVVALSTEGGVT 316
Cdd:pfam13360 150 RGTNELERLVDITGTPVVAGGRVFASAYQGRLVAFDAATGRRLWTREISGPNGPILDGDLLYVVSDDGELYALDRATGAV 229
|
....
gi 644362902 317 VWTQ 320
Cdd:pfam13360 230 VWKT 233
|
|
| PQQ |
smart00564 |
beta-propeller repeat; Beta-propeller repeat occurring in enzymes with pyrrolo-quinoline ... |
159-187 |
8.02e-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: 33.66 E-value: 8.02e-03
10 20
....*....|....*....|....*....
gi 644362902 159 SDGMVLVHTSNGMLQALNEADGAVKWTVN 187
Cdd:smart00564 5 SDGTVYVGSTDGTLYALDAKTGEILWTYK 33
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11138 |
PRK11138 |
outer membrane biogenesis protein BamB; Provisional |
1-393 |
0e+00 |
|
outer membrane biogenesis protein BamB; Provisional
Pssm-ID: 236857 [Multi-domain] Cd Length: 394 Bit Score: 748.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362902 1 MQLRKTLLVGLVSAALLSGCSLFNSEEDVVTMSPLPKVENQFTPSKAWSTSVGDGIGEYYSHLRPAYQDSTIYAADRFGI 80
Cdd:PRK11138 1 MQLRKTLLPGLLSVTLLSGCSSFNSEEDVVKMSPLPQVENQFTPTTVWSTSVGDGVGDYYSRLHPAVAYNKVYAADRAGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362902 81 VKAMDADSGNEKWKVNLSEKTGFFSSNLSALLSGGLTVAGDKVYVGSEKAVVYALNTADGAIAWQTKVAGEAISRPVISD 160
Cdd:PRK11138 81 VKALDADTGKEIWSVDLSEKDGWFSKNKSALLSGGVTVAGGKVYIGSEKGQVYALNAEDGEVAWQTKVAGEALSRPVVSD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362902 161 GMVLVHTSNGMLQALNEADGAVKWTVNLDMPSLSLRGESAPAVAFGAAIVGGDNGRVSAVLMQQGQLIWQQRISQPSGAT 240
Cdd:PRK11138 161 GLVLVHTSNGMLQALNESDGAVKWTVNLDVPSLTLRGESAPATAFGGAIVGGDNGRVSAVLMEQGQLIWQQRISQPTGAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362902 241 EIDRLNDVDTTPVIVDGVVYALGYNGNLTALDLRSGQIIWKRELGSVNDFIVDAGRIYLIDQNDRVVALSTEGGVTVWTQ 320
Cdd:PRK11138 241 EIDRLVDVDTTPVVVGGVVYALAYNGNLVALDLRSGQIVWKREYGSVNDFAVDGGRIYLVDQNDRVYALDTRGGVELWSQ 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 644362902 321 SDLLHRNLTPPVMYNGYLVTGDAEGYLHWVNTTDGRFVAQQEVDSSGFLSAPMVAGDKLVIQARGGKVYAFTR 393
Cdd:PRK11138 321 SDLLHRLLTAPVLYNGYLVVGDSEGYLHWINREDGRFVAQQKVDSSGFLSEPVVADDKLLIQARDGTVYAITR 393
|
|
| PQQ |
COG1520 |
Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell ... |
13-393 |
7.23e-176 |
|
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: 494.33 E-value: 7.23e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362902 13 SAALLSGCSLFNSEEDVVTMSPLPKVENQFTPSKAWSTSVGDGIGEYYSHLRPAYQDSTIYAADRFGIVKAMDADSGNEK 92
Cdd:COG1520 1 LLLLLLLLSGFSSEDDEPPPAPLPEFEPSVKVKQLWSASVGDGVGKGYSRLAPAVAGDRVYAADADGRVAALDAATGKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362902 93 WKVNLSEKtgffssnlsalLSGGLTVAGDKVYVGSEKAVVYALNTADGAIAWQTKVAGEAISRPVISDGMVLVHTSNGML 172
Cdd:COG1520 81 WRVDLGEP-----------LSGGVGADGGLVVVGTEDGEVIALDADDGEELWRARLSSEVLAAPAVAGGRVVVRTGDGRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362902 173 QALNEADGAVKWTVNLDMPSLSLRGESAPAVAFGAAIVGGDNGRVSAVLMQQGQLIWQQRISQPSGATEIDRLNDVDTTP 252
Cdd:COG1520 150 YALDAATGERLWSYQRPVPALTLRGTSSPVIVGGAVLVGFANGKLVALDLANGQPLWEQRVAQPRGRTELERLVDVDGTP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362902 253 VIVDGVVYALGYNGNLTALDLRSGQIIWKRELGSVNDFIVDAGRIYLIDQNDRVVALSTEGGVTVWTQSDLLHRNLTPPV 332
Cdd:COG1520 230 VVDGGVVYAVAYQGRLAALDLRSGRVLWSRDLSSYTGLAVDGNNLYVTDDDGRVWALDRRNGAELWKQDALLYRGLTAPV 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 644362902 333 MYNGYLVTGDAEGYLHWVNTTDGRFVAQQEVDSSGFLSAPMVAGDKLVIQARGGKVYAFTR 393
Cdd:COG1520 310 VLGDYVVVGDFEGYLHWLSRDDGSLVARLRVDGSGIRAAPVVVGDTLYVQTRDGTLAALRL 370
|
|
| assembly_YfgL |
TIGR03300 |
outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a ... |
5-392 |
1.67e-163 |
|
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: 463.25 E-value: 1.67e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362902 5 KTLLVGLVSAALLSGCSLFNSEEDVVTMSPLPKVENQFTPSKAWSTSVGDGIGEYYSHLRPAYQDSTIYAADRFGIVKAM 84
Cdd:TIGR03300 1 KRLALVLACAALLSGCSWFSSEDDEPQPAELPEFQPTVKVDQVWSASVGDGVGHYYLRLQPAVAGGKVYAADADGTVAAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362902 85 DADSGNEKWKVNLSEKtgffssnlsalLSGGLTVAGDKVYVGSEKAVVYALNTADGAIAWQTKVAGEAISRPVISDGMVL 164
Cdd:TIGR03300 81 DAETGKRLWRVDLDER-----------LSGGVGADGGLVFVGTEKGEVIALDAEDGKELWRAKLSSEVLSPPLVANGLVV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362902 165 VHTSNGMLQALNEADGAVKWTVNLDMPSLSLRGESAPAVAFGAAIVGGDNGRVSAVLMQQGQLIWQQRISQPSGATEIDR 244
Cdd:TIGR03300 150 VRTNDGRLTALDAATGERLWTYSRVTPPLTLRGSASPVIADGGVLVGFAGGKLVALDLQTGQPLWEQRVALPKGRTELER 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362902 245 LNDVDTTPVIVDGVVYALGYNGNLTALDLRSGQIIWKRELGSVNDFIVDAGRIYLIDQNDRVVALSTEGGVTVWTQSDLL 324
Cdd:TIGR03300 230 LVDVDGDPVVDGGQVYAVSYQGRVAALDLRSGRVLWKRDASSYQGPAVDDNRLYVTDADGVVVALDRRSGSELWKNDELK 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 644362902 325 HRNLTPPVMYNGYLVTGDAEGYLHWVNTTDGRFVAQQEVDSSGFLSAPMVAGDKLVIQARGGKVYAFT 392
Cdd:TIGR03300 310 YRQLTAPAVLGGYLVVGDFEGYLHWLDRDDGSFVARLKTDGSGIASPPVVVGDGLLVQTRDGDLYAFR 377
|
|
| BamB_YfgL |
cd10276 |
Beta-barrel assembly machinery (Bam) complex component B and related proteins; BamB (YflG) is ... |
32-393 |
7.75e-109 |
|
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: 323.51 E-value: 7.75e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362902 32 MSPLPKVENQFTPSKAWSTSVGDGiGEYYSHLRPAYQDSTIYAADRFGIVKAMDADSGNEKWKVNLSEKtgffssnlsAL 111
Cdd:cd10276 2 PTDLPEPTPEFDPEVLWSKSVGNG-GMAGIDLTPVVAGDMVYAADANGQVSAFNATTGKIIWETSLSGK---------GF 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362902 112 LSGGLTVAGDKVYVGSEKAVVYALNTADGAIAWQTKVA-GEAISRPVISDGMVLVHTSNGMLQALNEADGAVKWTVNLDM 190
Cdd:cd10276 72 LGGTPAVGNGKIFVGTESGYLYALDAKDGSELWRTEVSdSQLLSPPTYADGKIYVGTGDGRLYYCNAETGKVVWNRTSTA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362902 191 PSLSLRGESAPAVAFGAAIVGGDNGRVSAVLMQQGQLIWQQRISQPSGATEIDRLNDVDTTPVIVDGVVYALGYNGNLTA 270
Cdd:cd10276 152 PELSLRGGAAPVGAYDVVFVGDGNGTVVALNTGTGVDIWEFSVSEPRGRTELPRMIDSSVTYVVVGGYLYSTSYQGYLVA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362902 271 LDLRSGQIIWKRELGSVNDFIVDA-GRIYLIDQNDRVVALSTEGGVTVWTQSDLLHRNLTPPVMY-NGYLVTGD-AEGYL 347
Cdd:cd10276 232 LDFESGQFLWSRKASGGTSTSTDAnGRVYVGDGEGSLYCLDASTGDELWSQTVLLGRVLSSPAIYvGVYIYVTDnAEGYL 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 644362902 348 HWVNTTDGRFVAQQEVDSS-GFLSAPMVAGDKLVIQARGGKVYAFTR 393
Cdd:cd10276 312 YCLKDNDGLTVARVEVDYSqYILQGPAVSDGWLYYGTDDGYLYALTR 358
|
|
| PQQ_DH_like |
cd00216 |
PQQ-dependent dehydrogenases and related proteins; This family is composed of dehydrogenases ... |
38-386 |
6.93e-101 |
|
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: 306.07 E-value: 6.93e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362902 38 VENQFTPSKAWSTSVGDGiGEYYSHLRPAYQDSTIYAADRFGIVKAMDADSGNEKWKVNLSEKTGFFSSnLSALLSGGLT 117
Cdd:cd00216 1 ADNVFQLTPAWSFSTGDG-GNRGSELTPIVVDGVMYATTSFSRVFALDADDGKEIWSYDPALKDGWFEA-CCDLVNRGVA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362902 118 VAGDKVYVGSEKAVVYALNTADGAIAWQTKVA-----GEAISRPVISDGMVLVHTSN------GMLQALNEADGAVKWTV 186
Cdd:cd00216 79 VWGGKVYIGVLDGRVYALNAETGKVAWKVKNAdvlggYTATSAPVVVDGLVIIGSSGdefgvrGYLTAYDVATGEEKWRF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362902 187 NLDMP--------------------------SLSLRGESAPAVAF--GAAIVGGDN------------------GRVSAV 220
Cdd:cd00216 159 YLVMPdpnllpgkdstvtdrntptgdehtwtSGGGTGWSSAAYDAelNLIYVGGGNptpwnwggnrtpgdnlytSSIVAV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362902 221 LMQQGQLIWQQRISQPSGATeidrlNDVDTTPVIVD--------GVVYALGYNGNLTALDLRSGQIIWKRELgsVNDFIV 292
Cdd:cd00216 239 NADTGEMKWQYQTTPHDAWD-----YDGDNTPVLADikvkgkkvKVLFAPAKNGNFYVLDRRNGELVSARPL--VPDSYD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362902 293 DAGRIYLIDQNDRVVALSTEGGVTVWTQSDLlHRNLTPPVMYNGYLV-TGDAEGYLHWVNTTDGRFVAQQEVDsSGFLSA 371
Cdd:cd00216 312 PDRELFYVPANGRIMALDPVTGVVVWEKSEL-HPLLGGPLSTAGNLVfVGTSDGYLKAYNADTGEKLWQQKVP-SGFQAE 389
|
410
....*....|....*....
gi 644362902 372 PMVA----GDKLVIQARGG 386
Cdd:cd00216 390 PVTYevdgEQYVLIQAGGG 408
|
|
| PQQ_2 |
pfam13360 |
PQQ-like domain; This domain contains several repeats of the PQQ repeat. |
77-320 |
9.70e-63 |
|
PQQ-like domain; This domain contains several repeats of the PQQ repeat.
Pssm-ID: 433144 [Multi-domain] Cd Length: 233 Bit Score: 201.09 E-value: 9.70e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362902 77 RFGIVKAMDADSGNEKWKVNLSEKtgffssnlsalLSGGLTVAGDKVYVGSEKAVVYALNTADGAIAWQTKVAGEAISRP 156
Cdd:pfam13360 1 ADGVVTALDAATGAELWRVDLETG-----------LGGGVAVDGGRLFVATGGGQLVALDAATGKLLWRQTLSGEVLGAP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362902 157 VISDGMVLVHTSNGMLQALNEADGAVKWTVNLDMPSLSLRGESAPAVAFGAAIVGGDNGRVSAVLMQQGQLIWQQRISQP 236
Cdd:pfam13360 70 LVAGGRVFVVAGDGSLIALDAADGRRLWSYQRSGEPLALRSSGSPAVVGDTVVAGFSSGKLVALDPATGKVRWEAPLAAP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362902 237 SGATEIDRLNDVDTTPVIVDGVVYALGYNGNLTALDLRSGQIIWKRELGSVNDFIVDAGRIYLIDQNDRVVALSTEGGVT 316
Cdd:pfam13360 150 RGTNELERLVDITGTPVVAGGRVFASAYQGRLVAFDAATGRRLWTREISGPNGPILDGDLLYVVSDDGELYALDRATGAV 229
|
....
gi 644362902 317 VWTQ 320
Cdd:pfam13360 230 VWKT 233
|
|
| PQQ_2 |
pfam13360 |
PQQ-like domain; This domain contains several repeats of the PQQ repeat. |
213-365 |
1.04e-14 |
|
PQQ-like domain; This domain contains several repeats of the PQQ repeat.
Pssm-ID: 433144 [Multi-domain] Cd Length: 233 Bit Score: 72.82 E-value: 1.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362902 213 DNGRVSAVLMQQGQLIWQQRISQPSGATeidrlndvdttPVIVDGVVYALGYNGNLTALDLRSGQIIWKRELGS--VNDF 290
Cdd:pfam13360 1 ADGVVTALDAATGAELWRVDLETGLGGG-----------VAVDGGRLFVATGGGQLVALDAATGKLLWRQTLSGevLGAP 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 644362902 291 IVDAGRIYLIDQNDRVVALSTEGGVTVWTQSD----LLHRNLTPPVMYNGYLVTGDAEGYLHWVNTTDGRFVAQQEVDS 365
Cdd:pfam13360 70 LVAGGRVFVVAGDGSLIALDAADGRRLWSYQRsgepLALRSSGSPAVVGDTVVAGFSSGKLVALDPATGKVRWEAPLAA 148
|
|
| PQQ_2 |
pfam13360 |
PQQ-like domain; This domain contains several repeats of the PQQ repeat. |
65-185 |
5.22e-12 |
|
PQQ-like domain; This domain contains several repeats of the PQQ repeat.
Pssm-ID: 433144 [Multi-domain] Cd Length: 233 Bit Score: 65.12 E-value: 5.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362902 65 PAYQDSTIYAADRFGIVKAMDADSGNEKWKVNLSEKTGFFSSNLSALLSGGLTVAGDKVYVGSEKAVVYALNTADGAIAW 144
Cdd:pfam13360 114 PAVVGDTVVAGFSSGKLVALDPATGKVRWEAPLAAPRGTNELERLVDITGTPVVAGGRVFASAYQGRLVAFDAATGRRLW 193
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 644362902 145 QTKVAGeaISRPVISDGMVLVHTSNGMLQALNEADGAVKWT 185
Cdd:pfam13360 194 TREISG--PNGPILDGDLLYVVSDDGELYALDRATGAVVWK 232
|
|
| PQQ_ADH_I |
cd10277 |
Ethanol dehydrogenase, a bacterial quinoprotein (PQQ-dependent type I alcohol dehydrogenase); ... |
33-185 |
1.48e-11 |
|
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: 65.78 E-value: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362902 33 SPLPKV--ENQFTPSKAWSTSVGDGIGEYYShlRPAYQDSTIYAADRFGIVKAMDADSGNEKWKVN--LSEKTGFFSSNL 108
Cdd:cd10277 24 SPLKQIntDNVKNLVPAWSFSFGGKQRGQES--QPIVNDGVMYVTTSYNRVFAIDAKTGKELWKYKhrLPEDIRPCCDVV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362902 109 SAllsgGLTVAGDKVYVGSEKAVVYALNTADGAIAWQTKVA----GEAI-SRPVISDGMVLVHTSN------GMLQALNE 177
Cdd:cd10277 102 NR----GVALYGDKVYFGTLDAHLVALDAKTGKVVWKKKVAdykaGYSMtLAPLVVKGKVIVGVSGgefgvrGFIAALDA 177
|
....*...
gi 644362902 178 ADGAVKWT 185
Cdd:cd10277 178 ETGKEVWR 185
|
|
| PQQ_2 |
pfam13360 |
PQQ-like domain; This domain contains several repeats of the PQQ repeat. |
265-391 |
1.22e-09 |
|
PQQ-like domain; This domain contains several repeats of the PQQ repeat.
Pssm-ID: 433144 [Multi-domain] Cd Length: 233 Bit Score: 58.18 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362902 265 NGNLTALDLRSGQIIWKREL--GSVNDFIVDAGRIYLIDQNDRVVALSTEGGVTVWTQsDLLHRNLTPPVMYNGYLVTGD 342
Cdd:pfam13360 2 DGVVTALDAATGAELWRVDLetGLGGGVAVDGGRLFVATGGGQLVALDAATGKLLWRQ-TLSGEVLGAPLVAGGRVFVVA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 644362902 343 AEGYLHWVNTTDGRFVAQQEVDSSGFL----SAPMVAGDKLVIQARGGKVYAF 391
Cdd:pfam13360 81 GDGSLIALDAADGRRLWSYQRSGEPLAlrssGSPAVVGDTVVAGFSSGKLVAL 133
|
|
| Gcd |
COG4993 |
Glucose dehydrogenase, PQQ-dependent [Carbohydrate transport and metabolism]; |
118-229 |
5.81e-08 |
|
Glucose dehydrogenase, PQQ-dependent [Carbohydrate transport and metabolism];
Pssm-ID: 444017 [Multi-domain] Cd Length: 515 Bit Score: 54.39 E-value: 5.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362902 118 VAGDKVYVGSEKAVVYALNTADGAIAWQT--KVAGEAISRPVIS------DGMVLVHTSNGMLQALNEADGAVKWTVNLD 189
Cdd:COG4993 53 VVDGVLYVCTPHNRVFALDAATGKELWRYdpKLPDDAACCDVVNrgvayyDGRIFLGTLDGRLVALDAKTGKVCWDVKVG 132
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 644362902 190 MPSLSLRGESAPAVAFGAAIVG---GDN---GRVSAVLMQQGQLIW 229
Cdd:COG4993 133 DPKKGYTITSAPLVVKDKVIVGgsgGEFgprGVVRAYDARTGKLVW 178
|
|
| PQQ_ADH_II |
cd10279 |
PQQ_like domain of the quinohemoprotein alcohol dehydrogenase (type II); This family of ... |
118-229 |
5.93e-08 |
|
PQQ_like domain of the quinohemoprotein alcohol dehydrogenase (type II); This family of monomeric and soluble type II alcohol dehydrogenases utilizes pyrroloquinoline quinone (PQQ) as a cofactor and is related to ethanol, methanol, and membrane-bound glucose dehydrogenases. The alignment model contains an 8-bladed beta-propeller.
Pssm-ID: 199837 [Multi-domain] Cd Length: 549 Bit Score: 54.57 E-value: 5.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362902 118 VAGDKVYVGSEKAVVYALNTADGAIAWQ----------TKVAGEAISRPV-ISDGMVLVHTSNGMLQALNEADGAVKWTV 186
Cdd:cd10279 49 VVDGVMYVSGPWSVVYALDARTGKLLWQydpevdresgRKACCDVVNRGVaVWDGKVFVGTLDGRLIALDAKTGKEVWSV 128
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 644362902 187 NLDMPSLSLRGESAPAVAFGAAIVG------GDNGRVSAVLMQQGQLIW 229
Cdd:cd10279 129 DTIDPRKPYTITGAPRVAKGKVVIGnggaefGVRGYVSAYDAETGKLVW 177
|
|
| Gcd |
COG4993 |
Glucose dehydrogenase, PQQ-dependent [Carbohydrate transport and metabolism]; |
250-391 |
1.18e-07 |
|
Glucose dehydrogenase, PQQ-dependent [Carbohydrate transport and metabolism];
Pssm-ID: 444017 [Multi-domain] Cd Length: 515 Bit Score: 53.62 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362902 250 TTPVIVDGVVYALGYNGNLTALDLRSGQIIWKRELGSvndfivdAGRIYLIDQNDRvvalstegGVTVWtqsdllhrnlt 329
Cdd:COG4993 49 ATPLVVDGVLYVCTPHNRVFALDAATGKELWRYDPKL-------PDDAACCDVVNR--------GVAYY----------- 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 644362902 330 ppvmyNGYLVTGDAEGYLHWVNTTDGRFVAQQEV----DSSGFLSAPMVAGDKLVIQARG------GKVYAF 391
Cdd:COG4993 103 -----DGRIFLGTLDGRLVALDAKTGKVCWDVKVgdpkKGYTITSAPLVVKDKVIVGGSGgefgprGVVRAY 169
|
|
| PQQ_ADH_I |
cd10277 |
Ethanol dehydrogenase, a bacterial quinoprotein (PQQ-dependent type I alcohol dehydrogenase); ... |
154-282 |
2.12e-06 |
|
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: 49.60 E-value: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362902 154 SRPVISDGMVLVHTSNGMLQALNEADGAVKWTVNLDMPslslrGESAPA---VAFGAAIVGGD------NGRVSAVLMQQ 224
Cdd:cd10277 54 SQPIVNDGVMYVTTSYNRVFAIDAKTGKELWKYKHRLP-----EDIRPCcdvVNRGVALYGDKvyfgtlDAHLVALDAKT 128
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 644362902 225 GQLIWQQRISQPsGATEIdrlndVDTTPVIVDGVVYA------LGYNGNLTALDLRSGQIIWKR 282
Cdd:cd10277 129 GKVVWKKKVADY-KAGYS-----MTLAPLVVKGKVIVgvsggeFGVRGFIAALDAETGKEVWRT 186
|
|
| PQQ_MDH |
cd10278 |
Large subunit of methanol dehydrogenase (moxF); Methanol dehydrogenase is a key enzyme in the ... |
65-150 |
1.10e-05 |
|
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: 47.32 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362902 65 PAYQDSTIYAADRFGIVKAMDADSGNEKWKVNLSE-KTGffSSNLSALLsggltVAGDKVYVGS---EKAV---VYALNT 137
Cdd:cd10278 98 LAYADGKIFFNQLDGHLVALDAKTGKEVWKVKNGDpKVG--ETLTMAPL-----VVKDKVIVGIsggEFGVrgyVTAYDL 170
|
90
....*....|...
gi 644362902 138 ADGAIAWQTKVAG 150
Cdd:cd10278 171 KTGKLVWRAYSTG 183
|
|
| PQQ_MDH |
cd10278 |
Large subunit of methanol dehydrogenase (moxF); Methanol dehydrogenase is a key enzyme in the ... |
118-281 |
2.47e-05 |
|
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: 46.17 E-value: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362902 118 VAGDKVYVGSE-KAVVYALN-TADGAIAWQTKVAGEAISRPVI-----------SDGMVLVHTSNGMLQALNEADGAVKW 184
Cdd:cd10278 47 VVGDTMYVVTPfPNNVYALDlNDPGKILWKYKPKQDPSAVAVAccdvvnrglayADGKIFFNQLDGHLVALDAKTGKEVW 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362902 185 TVNLDMPSlslRGES---APAVAFGAAIVGGdngrvsavlmqqgqliwqqrisqpSGATeidrlndvdttpvivdgvvya 261
Cdd:cd10278 127 KVKNGDPK---VGETltmAPLVVKDKVIVGI------------------------SGGE--------------------- 158
|
170 180
....*....|....*....|
gi 644362902 262 LGYNGNLTALDLRSGQIIWK 281
Cdd:cd10278 159 FGVRGYVTAYDLKTGKLVWR 178
|
|
| PQQ_ADH_I |
cd10277 |
Ethanol dehydrogenase, a bacterial quinoprotein (PQQ-dependent type I alcohol dehydrogenase); ... |
76-157 |
5.29e-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: 5.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362902 76 DRFGIVKAMDADSGNEKWKVNlsektgffssNLSALLSGGLTVAGDKVYVGSEKAVVYALNTADGAIAWQTKVAGEAISR 155
Cdd:cd10277 413 DHIGELQAIDPTTGKKVWEHK----------TPLPLWGGVLTTAGGLVFTGTPDGYFRAFDAKTGKELWEFQTGSGIIGP 482
|
..
gi 644362902 156 PV 157
Cdd:cd10277 483 PV 484
|
|
| PQQ_ADH_II |
cd10279 |
PQQ_like domain of the quinohemoprotein alcohol dehydrogenase (type II); This family of ... |
69-184 |
8.10e-05 |
|
PQQ_like domain of the quinohemoprotein alcohol dehydrogenase (type II); This family of monomeric and soluble type II alcohol dehydrogenases utilizes pyrroloquinoline quinone (PQQ) as a cofactor and is related to ethanol, methanol, and membrane-bound glucose dehydrogenases. The alignment model contains an 8-bladed beta-propeller.
Pssm-ID: 199837 [Multi-domain] Cd Length: 549 Bit Score: 44.56 E-value: 8.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362902 69 DSTIYAADRFGIVKAMDADSGNEKWKVNLSEKTGFFSSNLSALLSGGLTVAGDKVYVGSEKAVVYALNTADGAIAWQTKV 148
Cdd:cd10279 51 DGVMYVSGPWSVVYALDARTGKLLWQYDPEVDRESGRKACCDVVNRGVAVWDGKVFVGTLDGRLIALDAKTGKEVWSVDT 130
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 644362902 149 ----AGEAIS-RPVISDGMVLVHTSN------GMLQALNEADGAVKW 184
Cdd:cd10279 131 idprKPYTITgAPRVAKGKVVIGNGGaefgvrGYVSAYDAETGKLVW 177
|
|
| PQQ |
pfam01011 |
PQQ enzyme repeat; The family represent a single repeat of a beta propeller. This propeller ... |
257-289 |
1.38e-04 |
|
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: 38.71 E-value: 1.38e-04
10 20 30
....*....|....*....|....*....|...
gi 644362902 257 GVVYALGYNGNLTALDLRSGQIIWKRELGSVND 289
Cdd:pfam01011 1 GTVYLGSDDGYLYALDAETGKVLWSFKTGGAVL 33
|
|
| PQQ_ADH_I |
cd10277 |
Ethanol dehydrogenase, a bacterial quinoprotein (PQQ-dependent type I alcohol dehydrogenase); ... |
249-320 |
4.96e-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: 42.28 E-value: 4.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362902 249 DTTPVIVDGVVYALGYNGNLTALDLRSGQIIWKRE----------LGSVN-DFIVDAGRIYLIDQNDRVVALSTEGGVTV 317
Cdd:cd10277 53 ESQPIVNDGVMYVTTSYNRVFAIDAKTGKELWKYKhrlpedirpcCDVVNrGVALYGDKVYFGTLDAHLVALDAKTGKVV 132
|
...
gi 644362902 318 WTQ 320
Cdd:cd10277 133 WKK 135
|
|
| PQQ |
pfam01011 |
PQQ enzyme repeat; The family represent a single repeat of a beta propeller. This propeller ... |
161-195 |
6.84e-04 |
|
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: 36.79 E-value: 6.84e-04
10 20 30
....*....|....*....|....*....|....*
gi 644362902 161 GMVLVHTSNGMLQALNEADGAVKWTVNLDMPSLSL 195
Cdd:pfam01011 1 GTVYLGSDDGYLYALDAETGKVLWSFKTGGAVLSS 35
|
|
| PQQ_ADH_II |
cd10279 |
PQQ_like domain of the quinohemoprotein alcohol dehydrogenase (type II); This family of ... |
239-318 |
8.27e-04 |
|
PQQ_like domain of the quinohemoprotein alcohol dehydrogenase (type II); This family of monomeric and soluble type II alcohol dehydrogenases utilizes pyrroloquinoline quinone (PQQ) as a cofactor and is related to ethanol, methanol, and membrane-bound glucose dehydrogenases. The alignment model contains an 8-bladed beta-propeller.
Pssm-ID: 199837 [Multi-domain] Cd Length: 549 Bit Score: 41.48 E-value: 8.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362902 239 ATEIDRLNDVDTTPVIVDGVVYALGYNGNLTALDLRSGQIIWK------RELG------SVNDFI-VDAGRIYLIDQNDR 305
Cdd:cd10279 34 YFDLDTNRGQEATPLVVDGVMYVSGPWSVVYALDARTGKLLWQydpevdRESGrkaccdVVNRGVaVWDGKVFVGTLDGR 113
|
90
....*....|...
gi 644362902 306 VVALSTEGGVTVW 318
Cdd:cd10279 114 LIALDAKTGKEVW 126
|
|
| PQQ_3 |
pfam13570 |
PQQ-like domain; |
140-175 |
1.54e-03 |
|
PQQ-like domain;
Pssm-ID: 463925 [Multi-domain] Cd Length: 36 Bit Score: 36.03 E-value: 1.54e-03
10 20 30
....*....|....*....|....*....|....*.
gi 644362902 140 GAIAWQTKVAGEAISRPVISDGMVLVHTSNGMLQAL 175
Cdd:pfam13570 1 GEVLWRFETGGPIVSSPAVAGGLVYVGTGDGTLYAL 36
|
|
| PQQ |
pfam01011 |
PQQ enzyme repeat; The family represent a single repeat of a beta propeller. This propeller ... |
121-156 |
2.21e-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: 2.21e-03
10 20 30
....*....|....*....|....*....|....*.
gi 644362902 121 DKVYVGSEKAVVYALNTADGAIAWQTKVAGEAISRP 156
Cdd:pfam01011 1 GTVYLGSDDGYLYALDAETGKVLWSFKTGGAVLSSP 36
|
|
| Luminal_IRE1_like |
cd09213 |
The Luminal domain, a dimerization domain, of Inositol-requiring protein 1-like proteins; The ... |
60-276 |
2.63e-03 |
|
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: 39.40 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362902 60 YSHLRPAyQDSTIYAADRFGIVKAMDADSGnEKWK-VNLSEKTGFFSSNLSALLSGGLT---VAGDKVYVGSEKAVVYAL 135
Cdd:cd09213 85 PLVSDTN-EDDVVVVGSKRTSVFALDAKTG-KIIKtYRADGLPSTGGSDSDGNSTPGPDelqEEEELLYIGRTDYVLQAI 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362902 136 NTADGAIAWQTKVAG-EAISRPVISDGMVlvhTSNGMLQALNEAD---------------GAVKWTVNLDMPSLSLRGES 199
Cdd:cd09213 163 DPRSGKELWNVTYGEyEALTLDADELGTS---SSSSPLSASFRISenepvpavyllglqgGKSLWEHLFDSPIVSAFDYS 239
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 644362902 200 APAVAFGAAIVGGDNGRVSAVLMQQGQLIWQQRISQPSGATEIDRLNDVDTTPVIVDgvvyaLGYNGNLTALDLRSG 276
Cdd:cd09213 240 SKLTNFEGLIKPIFVFQVHEYASSNSVYIGAHENGQLFALSSPSKSEDKESAISNIL-----EGENTSPSALEGVSG 311
|
|
| PQQ |
smart00564 |
beta-propeller repeat; Beta-propeller repeat occurring in enzymes with pyrrolo-quinoline ... |
159-187 |
8.02e-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: 33.66 E-value: 8.02e-03
10 20
....*....|....*....|....*....
gi 644362902 159 SDGMVLVHTSNGMLQALNEADGAVKWTVN 187
Cdd:smart00564 5 SDGTVYVGSTDGTLYALDAKTGEILWTYK 33
|
|
| PQQ_MDH |
cd10278 |
Large subunit of methanol dehydrogenase (moxF); Methanol dehydrogenase is a key enzyme in the ... |
115-185 |
8.45e-03 |
|
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: 38.08 E-value: 8.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362902 115 GLTVAGDKVYVGSEKAVVYALNTADGAIAWQTKVA----GEAISR-PVISDGMVLVHTSN------GMLQALNEADGAVK 183
Cdd:cd10278 97 GLAYADGKIFFNQLDGHLVALDAKTGKEVWKVKNGdpkvGETLTMaPLVVKDKVIVGISGgefgvrGYVTAYDLKTGKLV 176
|
..
gi 644362902 184 WT 185
Cdd:cd10278 177 WR 178
|
|
| |
