|
Name |
Accession |
Description |
Interval |
E-value |
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
40-502 |
3.45e-156 |
|
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain [Signal transduction mechanisms];
Pssm-ID: 444025 [Multi-domain] Cd Length: 678 Bit Score: 460.40 E-value: 3.45e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 40 IASLLETGVSLILFGGSIFVVLVIKWSNDSILELHTVAEKEKRNAVHDALTGLPNRKYCFELIEDRI----QSGDPFSVI 115
Cdd:COG5001 207 RLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEERLRHLAYHDPLTGLPNRRLFLDRLEQALararRSGRRLALL 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 116 LFDVVNFKQVNDAMGHFCGDQLLIQIGQRLQEKLKGSDKIFRVGGDEFVI-LTSSACEETGKSLIEELDSALSNRFHLDE 194
Cdd:COG5001 287 FIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAVlLPDLDDPEDAEAVAERILAALAEPFELDG 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 195 FQVSSRVVFGVSTYPYDALSNDLLIKHADIAMYHAKRNG-NLFAFYNEDMNVGAKYQLEISSRIQCALEKEEFQLYYQPL 273
Cdd:COG5001 367 HELYVSASIGIALYPDDGADAEELLRNADLAMYRAKAAGrNRYRFFDPEMDERARERLELEADLRRALERGELELHYQPQ 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 274 IDAHTNLAVGFEAVIRWHDENGKTISPNDFIPIAERSNQVHNITMWVLNQVEKDLQTFIEKDIK-LPVHVNLSAKDLSSN 352
Cdd:COG5001 447 VDLATGRIVGAEALLRWQHPERGLVSPAEFIPLAEETGLIVPLGEWVLREACRQLAAWQDAGLPdLRVAVNLSARQLRDP 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 353 LLFNRLETLLK---VNPqfaDLISLEITETMAIDRVVELNPLIHQIKGLGIKISLDDFGTGYSSLSLLRDLPVDQIKIDR 429
Cdd:COG5001 527 DLVDRVRRALAetgLPP---SRLELEITESALLEDPEEALETLRALRALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDR 603
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 686144922 430 SFLCTASRTEGTRSIVENTIALAHGLGYSVVAEGVQDMDTLHFLRSRGCDIIQGYLFCPALPLNEVITWVNEH 502
Cdd:COG5001 604 SFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRELGCDYAQGYLFSRPLPAEELEALLRAR 676
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
255-494 |
5.15e-91 |
|
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues and is also known as domain of unknown function 2 (DUF2). The EAL domain has been shown to stimulate degradation of a second messenger, cyclic di-GMP, and is a good candidate for a diguanylate phosphodiesterase function. Together with the GGDEF domain, EAL might be involved in regulating cell surface adhesiveness in bacteria.
Pssm-ID: 238923 [Multi-domain] Cd Length: 240 Bit Score: 277.89 E-value: 5.15e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 255 SRIQCALEKEEFQLYYQPLIDAHTNLAVGFEAVIRWHDENGKTISPNDFIPIAERSNQVHNITMWVLNQVEKDLQTFIEK 334
Cdd:cd01948 1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 335 DIKLPVHVNLSAKDLSSNLLFNRLETLLKVNPQFADLISLEITETMAIDRVVELNPLIHQIKGLGIKISLDDFGTGYSSL 414
Cdd:cd01948 81 GPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 415 SLLRDLPVDQIKIDRSFLCTASRTEGTRSIVENTIALAHGLGYSVVAEGVQDMDTLHFLRSRGCDIIQGYLFCPALPLNE 494
Cdd:cd01948 161 SYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAEE 240
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
87-501 |
7.78e-91 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 294.37 E-value: 7.78e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 87 DALTGLPNRKYCFELIEDRIQSGDPFSVILFDVVNFKQVNDAMGHFCGDQLLIQIGQRLQEKLKGSDKIFRVGGDEFViL 166
Cdd:PRK11359 379 DPLTGLPNRNNLHNYLDDLVDKAVSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGTQFV-L 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 167 TSSACEETGKSLI-EELDSALSNRFHLDEFQVSSRVVFGVStypYDALSN-DLLIKHADIAM-YHAKRNGNLFAFYNEDM 243
Cdd:PRK11359 458 VSLENDVSNITQIaDELRNVVSKPIMIDDKPFPLTLSIGIS---YDVGKNrDYLLSTAHNAMdYIRKNGGNGWQFFSPAM 534
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 244 NVGAKYQLEISSRIQCALEKEEFQLYYQPLIDAHTNLAVGFEAVIRWHDENGKTISPNDFIPIAERSNQVHNITMWVLNQ 323
Cdd:PRK11359 535 NEMVKERLVLGAALKEAISNNQLKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIPLAEEIGEIENIGRWVIAE 614
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 324 VEKDLQTFIEKDIKLP-VHVNLSAKDLSSNLLFNRLETLLKvnpQFA---DLISLEITETMAIDRVVELNPLIHQIKGLG 399
Cdd:PRK11359 615 ACRQLAEWRSQNIHIPaLSVNLSALHFRSNQLPNQVSDAMQ---AWGidgHQLTVEITESMMMEHDTEIFKRIQILRDMG 691
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 400 IKISLDDFGTGYSSLSLLRDLPVDQIKIDRSFLCTASRTEGTRSIVENTIALAHGLGYSVVAEGVQDMDTLHFLRSRGCD 479
Cdd:PRK11359 692 VGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQFEMLRKIHCR 771
|
410 420
....*....|....*....|..
gi 686144922 480 IIQGYLFCPALPLNEVITWVNE 501
Cdd:PRK11359 772 VIQGYFFSRPLPAEEIPGWMSS 793
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
256-494 |
6.06e-77 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 241.74 E-value: 6.06e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 256 RIQCALEKEEFQLYYQPLIDAHTNLAVGFEAVIRWHDENGKTISPNDFIPIAERSNQVHNITMWVLNQVEKDLQTFIEKD 335
Cdd:smart00052 3 ELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAQG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 336 IK-LPVHVNLSAKDLSSNLLFNRLETLLKVNPQFADLISLEITETMAIDRVVELNPLIHQIKGLGIKISLDDFGTGYSSL 414
Cdd:smart00052 83 PPpLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYSSL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 415 SLLRDLPVDQIKIDRSFLCTASRTEGTRSIVENTIALAHGLGYSVVAEGVQDMDTLHFLRSRGCDIIQGYLFCPALPLNE 494
Cdd:smart00052 163 SYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPLDD 242
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
256-489 |
2.88e-70 |
|
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues. The EAL domain is a good candidate for a diguanylate phosphodiesterase function. The domain contains many conserved acidic residues that could participate in metal binding and might form the phosphodiesterase active site.
Pssm-ID: 425752 [Multi-domain] Cd Length: 235 Bit Score: 224.12 E-value: 2.88e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 256 RIQCALEKEEFQLYYQPLIDAHTNLAVGFEAVIRWHDENGKTISPNDFIPIAERSNQVHNITMWVLNQVEKDLQTfIEKD 335
Cdd:pfam00563 3 ALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQ-LQLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 336 IKLPVHVNLSAKDLSSNLLFNRLETLLKVNPQFADLISLEITETMAIDRVVELNPLIHQIKGLGIKISLDDFGTGYSSLS 415
Cdd:pfam00563 82 PDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSLS 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 686144922 416 LLRDLPVDQIKIDRSFLCTASRTEGTRSIVENTIALAHGLGYSVVAEGVQDMDTLHFLRSRGCDIIQGYLFCPA 489
Cdd:pfam00563 162 YLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
84-241 |
7.68e-35 |
|
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by many proteins carrying the domain. There is evidence that the domain has diguanylate cyclase activity. Several proteins carrying this domain also carry domains with functions relating to environmental sensing. These include PleD, a response regulator protein involved in the swarmer-to-stalked cell transition in Caulobacter crescentus, and FixL, a heme-containing oxygen sensor protein. [Regulatory functions, Small molecule interactions, Signal transduction, Other]
Pssm-ID: 272984 [Multi-domain] Cd Length: 165 Bit Score: 128.22 E-value: 7.68e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 84 AVHDALTGLPNRKYCFELIEDRIQS----GDPFSVILFDVVNFKQVNDAMGHFCGDQLLIQIGQRLQEKLKGSDKIFRVG 159
Cdd:TIGR00254 2 AVRDPLTGLYNRRYLEEMLDSELKRarrfQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 160 GDEFVILTSsaceetGKSLIEELDSALSNRFHLDEF--------QVSSRVVFGVSTYPYDALSNDLLIKHADIAMYHAKR 231
Cdd:TIGR00254 82 GEEFVVILP------GTPLEDALSKAERLRDAINSKpievagseTLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKK 155
|
170
....*....|
gi 686144922 232 NGNLFAFYNE 241
Cdd:TIGR00254 156 AGRNRVVVAD 165
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
40-502 |
3.45e-156 |
|
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain [Signal transduction mechanisms];
Pssm-ID: 444025 [Multi-domain] Cd Length: 678 Bit Score: 460.40 E-value: 3.45e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 40 IASLLETGVSLILFGGSIFVVLVIKWSNDSILELHTVAEKEKRNAVHDALTGLPNRKYCFELIEDRI----QSGDPFSVI 115
Cdd:COG5001 207 RLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEERLRHLAYHDPLTGLPNRRLFLDRLEQALararRSGRRLALL 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 116 LFDVVNFKQVNDAMGHFCGDQLLIQIGQRLQEKLKGSDKIFRVGGDEFVI-LTSSACEETGKSLIEELDSALSNRFHLDE 194
Cdd:COG5001 287 FIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAVlLPDLDDPEDAEAVAERILAALAEPFELDG 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 195 FQVSSRVVFGVSTYPYDALSNDLLIKHADIAMYHAKRNG-NLFAFYNEDMNVGAKYQLEISSRIQCALEKEEFQLYYQPL 273
Cdd:COG5001 367 HELYVSASIGIALYPDDGADAEELLRNADLAMYRAKAAGrNRYRFFDPEMDERARERLELEADLRRALERGELELHYQPQ 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 274 IDAHTNLAVGFEAVIRWHDENGKTISPNDFIPIAERSNQVHNITMWVLNQVEKDLQTFIEKDIK-LPVHVNLSAKDLSSN 352
Cdd:COG5001 447 VDLATGRIVGAEALLRWQHPERGLVSPAEFIPLAEETGLIVPLGEWVLREACRQLAAWQDAGLPdLRVAVNLSARQLRDP 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 353 LLFNRLETLLK---VNPqfaDLISLEITETMAIDRVVELNPLIHQIKGLGIKISLDDFGTGYSSLSLLRDLPVDQIKIDR 429
Cdd:COG5001 527 DLVDRVRRALAetgLPP---SRLELEITESALLEDPEEALETLRALRALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDR 603
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 686144922 430 SFLCTASRTEGTRSIVENTIALAHGLGYSVVAEGVQDMDTLHFLRSRGCDIIQGYLFCPALPLNEVITWVNEH 502
Cdd:COG5001 604 SFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRELGCDYAQGYLFSRPLPAEELEALLRAR 676
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
14-500 |
4.05e-101 |
|
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) [Signal transduction mechanisms];
Pssm-ID: 441802 [Multi-domain] Cd Length: 576 Bit Score: 315.57 E-value: 4.05e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 14 WTFLLLLISCFIFAYAAFLHAIMQKPIASLLETGVSLILFGGSIFVVLVIkwsNDSILELHTVAEKEKRNAVHDALTGLP 93
Cdd:COG2200 87 LLLLLLLLLLLLLLLLLALLLAALLALLLLLLLLLLLLLLSLLLLLVLVL---LRLALELLLALLLLALLALLDLLLLLL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 94 NRKYCFELIEDRIQ-----SGDPFSVILFDVVNFKQVNDAMGHFCGDQLLIQIGQRLQEKLKGSDKIFRVGGDEFVILTS 168
Cdd:COG2200 164 LRRLLLLLLLLLLLlllalALLALLLLLLLLLLLLLDNDGLGGAGLLLLLLLALLLLLLLARLLLALLGGGGGGFLLLLL 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 169 S-ACEETGKSLIEELDSALSNRFHLDEFQVSSRVVFGVSTYPYDALSNDLLIKHADIAMYHAKRNGNLFAFYNEDMNVGA 247
Cdd:COG2200 244 LlAAAAAAAAALRLLLLLLLEPLLLGGGLVVVASSGGGAAAPDDGADAALLLAAAAAAAAAAAGGGRGRVVFFAAAEARA 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 248 KYQLEISSRIQCALEKEEFQLYYQPLIDAHTNLAVGFEAVIRWHDENGKTISPNDFIPIAERSNQVHNITMWVLNQVEKD 327
Cdd:COG2200 324 RRRLALESELREALEEGELRLYYQPIVDLRTGRVVGYEALLRWRHPDGGLISPAEFIPAAERSGLIVELDRWVLERALRQ 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 328 LQTFIEKDIKLPVHVNLSAKDLSSNLLFNRLETLLKVNPQFADLISLEITETMAIDRVVELNPLIHQIKGLGIKISLDDF 407
Cdd:COG2200 404 LARWPERGLDLRLSVNLSARSLLDPDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRIALDDF 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 408 GTGYSSLSLLRDLPVDQIKIDRSFLCTASRTEGTRSIVENTIALAHGLGYSVVAEGVQDMDTLHFLRSRGCDIIQGYLFC 487
Cdd:COG2200 484 GTGYSSLSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFG 563
|
490
....*....|...
gi 686144922 488 PALPLNEVITWVN 500
Cdd:COG2200 564 RPLPLEELEALLR 576
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
255-494 |
5.15e-91 |
|
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues and is also known as domain of unknown function 2 (DUF2). The EAL domain has been shown to stimulate degradation of a second messenger, cyclic di-GMP, and is a good candidate for a diguanylate phosphodiesterase function. Together with the GGDEF domain, EAL might be involved in regulating cell surface adhesiveness in bacteria.
Pssm-ID: 238923 [Multi-domain] Cd Length: 240 Bit Score: 277.89 E-value: 5.15e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 255 SRIQCALEKEEFQLYYQPLIDAHTNLAVGFEAVIRWHDENGKTISPNDFIPIAERSNQVHNITMWVLNQVEKDLQTFIEK 334
Cdd:cd01948 1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 335 DIKLPVHVNLSAKDLSSNLLFNRLETLLKVNPQFADLISLEITETMAIDRVVELNPLIHQIKGLGIKISLDDFGTGYSSL 414
Cdd:cd01948 81 GPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 415 SLLRDLPVDQIKIDRSFLCTASRTEGTRSIVENTIALAHGLGYSVVAEGVQDMDTLHFLRSRGCDIIQGYLFCPALPLNE 494
Cdd:cd01948 161 SYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAEE 240
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
87-501 |
7.78e-91 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 294.37 E-value: 7.78e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 87 DALTGLPNRKYCFELIEDRIQSGDPFSVILFDVVNFKQVNDAMGHFCGDQLLIQIGQRLQEKLKGSDKIFRVGGDEFViL 166
Cdd:PRK11359 379 DPLTGLPNRNNLHNYLDDLVDKAVSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGTQFV-L 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 167 TSSACEETGKSLI-EELDSALSNRFHLDEFQVSSRVVFGVStypYDALSN-DLLIKHADIAM-YHAKRNGNLFAFYNEDM 243
Cdd:PRK11359 458 VSLENDVSNITQIaDELRNVVSKPIMIDDKPFPLTLSIGIS---YDVGKNrDYLLSTAHNAMdYIRKNGGNGWQFFSPAM 534
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 244 NVGAKYQLEISSRIQCALEKEEFQLYYQPLIDAHTNLAVGFEAVIRWHDENGKTISPNDFIPIAERSNQVHNITMWVLNQ 323
Cdd:PRK11359 535 NEMVKERLVLGAALKEAISNNQLKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIPLAEEIGEIENIGRWVIAE 614
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 324 VEKDLQTFIEKDIKLP-VHVNLSAKDLSSNLLFNRLETLLKvnpQFA---DLISLEITETMAIDRVVELNPLIHQIKGLG 399
Cdd:PRK11359 615 ACRQLAEWRSQNIHIPaLSVNLSALHFRSNQLPNQVSDAMQ---AWGidgHQLTVEITESMMMEHDTEIFKRIQILRDMG 691
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 400 IKISLDDFGTGYSSLSLLRDLPVDQIKIDRSFLCTASRTEGTRSIVENTIALAHGLGYSVVAEGVQDMDTLHFLRSRGCD 479
Cdd:PRK11359 692 VGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQFEMLRKIHCR 771
|
410 420
....*....|....*....|..
gi 686144922 480 IIQGYLFCPALPLNEVITWVNE 501
Cdd:PRK11359 772 VIQGYFFSRPLPAEEIPGWMSS 793
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
87-508 |
3.04e-79 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 260.77 E-value: 3.04e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 87 DALTGLPNRKYCFELIEDRIQSGDPFSV-ILF-DVVNFKQVNDAMGHFCGDQLLIQIGQRLQEKLKGSDKIFRVGGDEFV 164
Cdd:PRK10060 240 DSITGLPNRNAIQELIDHAINAADNNQVgIVYlDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQTLARLGGDEFL 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 165 ILTssacEETGKSLIEELDSALSNR----FHLDEFQVSSRVVFGVSTYPYDALSNDLLIKHADIAMYHAKRNG-NLFAFY 239
Cdd:PRK10060 320 VLA----SHTSQAALEAMASRILTRlrlpFRIGLIEVYTGCSIGIALAPEHGDDSESLIRSADTAMYTAKEGGrGQFCVF 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 240 NEDMN--VgAKYqLEISSRIQCALEKEEFQLYYQPLIDAhTNLAVGFEAVIRWHDENGKTISPNDFIPIAERSNQVHNIT 317
Cdd:PRK10060 396 SPEMNqrV-FEY-LWLDTNLRKALENDQLVIHYQPKITW-RGEVRSLEALVRWQSPERGLIPPLEFISYAEESGLIVPLG 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 318 MWVLNQVEKDLQTFIEKDIKLPVHVNLSAKDLSSNLLFNRLETLLKVNPQFADLISLEITETMAIDRVVELNPLIHQIKG 397
Cdd:PRK10060 473 RWVMLDVVRQVAKWRDKGINLRVAVNVSARQLADQTIFTALKQALQELNFEYCPIDVELTESCLIENEELALSVIQQFSQ 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 398 LGIKISLDDFGTGYSSLSLLRDLPVDQIKIDRSFLCTASRTEGTRSIVENTIALAHGLGYSVVAEGVQDMDTLHFLRSRG 477
Cdd:PRK10060 553 LGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNG 632
|
410 420 430
....*....|....*....|....*....|.
gi 686144922 478 CDIIQGYLFCPALPLNEVITWVNEHDEKQSR 508
Cdd:PRK10060 633 VNERQGFLFAKPMPAVAFERWYKRYLKRKLI 663
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
256-494 |
6.06e-77 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 241.74 E-value: 6.06e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 256 RIQCALEKEEFQLYYQPLIDAHTNLAVGFEAVIRWHDENGKTISPNDFIPIAERSNQVHNITMWVLNQVEKDLQTFIEKD 335
Cdd:smart00052 3 ELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAQG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 336 IK-LPVHVNLSAKDLSSNLLFNRLETLLKVNPQFADLISLEITETMAIDRVVELNPLIHQIKGLGIKISLDDFGTGYSSL 414
Cdd:smart00052 83 PPpLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYSSL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 415 SLLRDLPVDQIKIDRSFLCTASRTEGTRSIVENTIALAHGLGYSVVAEGVQDMDTLHFLRSRGCDIIQGYLFCPALPLNE 494
Cdd:smart00052 163 SYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPLDD 242
|
|
| YjcC |
COG4943 |
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ... |
253-502 |
7.84e-72 |
|
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal transduction mechanisms];
Pssm-ID: 443970 [Multi-domain] Cd Length: 528 Bit Score: 237.51 E-value: 7.84e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 253 ISSRIQCALEKEEFQLYYQPLIDAHTNLAVGFEAVIRWHDENGKTISPNDFIPIAERSNQVHNITMWVLNQVEKDLQTFI 332
Cdd:COG4943 272 PRRRLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWRDPDGSVISPDIFIPLAEQSGLISPLTRQVIEQVFRDLGDLL 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 333 EKDIKLPVHVNLSAKDLSSNLLFNRLETLLKVNPQFADLISLEITETMAIDrVVELNPLIHQIKGLGIKISLDDFGTGYS 412
Cdd:COG4943 352 AADPDFHISINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEITERGFID-PAKARAVIAALREAGHRIAIDDFGTGYS 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 413 SLSLLRDLPVDQIKIDRSFLCTASRTEGTRSIVENTIALAHGLGYSVVAEGVQDMDTLHFLRSRGCDIIQGYLFCPALPL 492
Cdd:COG4943 431 SLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQYGQGWLFAKPLPA 510
|
250
....*....|
gi 686144922 493 NEVITWVNEH 502
Cdd:COG4943 511 EEFIAWLAAQ 520
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
256-489 |
2.88e-70 |
|
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues. The EAL domain is a good candidate for a diguanylate phosphodiesterase function. The domain contains many conserved acidic residues that could participate in metal binding and might form the phosphodiesterase active site.
Pssm-ID: 425752 [Multi-domain] Cd Length: 235 Bit Score: 224.12 E-value: 2.88e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 256 RIQCALEKEEFQLYYQPLIDAHTNLAVGFEAVIRWHDENGKTISPNDFIPIAERSNQVHNITMWVLNQVEKDLQTfIEKD 335
Cdd:pfam00563 3 ALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQ-LQLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 336 IKLPVHVNLSAKDLSSNLLFNRLETLLKVNPQFADLISLEITETMAIDRVVELNPLIHQIKGLGIKISLDDFGTGYSSLS 415
Cdd:pfam00563 82 PDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSLS 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 686144922 416 LLRDLPVDQIKIDRSFLCTASRTEGTRSIVENTIALAHGLGYSVVAEGVQDMDTLHFLRSRGCDIIQGYLFCPA 489
Cdd:pfam00563 162 YLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
90-494 |
2.05e-55 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 196.70 E-value: 2.05e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 90 TGLPNRKYCFELIEDRIQSG---DPFSVILFDVVNFKQVNDAMGHFCGDQLLIQIGQRLQEKLKGSDKIFRVGGDEFVIL 166
Cdd:PRK11829 238 TELPNRSLFISLLEKEIASStrtDHFHLLVIGIETLQEVSGAMSEAQHQQLLLTIVQRIEQCIDDSDLLAQLSKTEFAVL 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 167 TSSACEET-GKSLIEELDSALSNRFHLDEFQVSSRVVFGVSTYPYDALSNDLLIKHADIAMYHAKRNG-NLFAFYNEDMN 244
Cdd:PRK11829 318 ARGTRRSFpAMQLARRIMSQVTQPLFFDEITLRPSASIGITRYQAQQDTAESMMRNASTAMMAAHHEGrNQIMVFEPHLI 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 245 VGAKYQLEISSRIQCALEKEEFQLYYQPLIDAHTNLAVGFEAVIRWHDENGKTISPNDFIPIAERSNQVHNITMWVLNQV 324
Cdd:PRK11829 398 EKTHKRLTQENDLLQAIENHDFTLFLQPQWDMKRQQVIGAEALLRWCQPDGSYVLPSGFVHFAEEEGMMVPLGNWVLEEA 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 325 EKDLQTFIEKDIKLPVHVNLSAKDLSSNLLFNRLETLLKVNPQFADLISLEITETMAIDRVVELNPLIHQIKGLGIKISL 404
Cdd:PRK11829 478 CRILADWKARGVSLPLSVNISGLQVQNKQFLPHLKTLISHYHIDPQQLLLEITETAQIQDLDEALRLLRELQGLGLLIAL 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 405 DDFGTGYSSLSLLR---DLPVDQIKIDRSFLCTASRTEGTRSIVEntiALAHGLGYSVVAEGVQDMDTLHFLRSRGCDII 481
Cdd:PRK11829 558 DDFGIGYSSLRYLNhlkSLPIHMIKLDKSFVKNLPEDDAIARIIS---CVSDVLKVRVMAEGVETEEQRQWLLEHGIQCG 634
|
410
....*....|...
gi 686144922 482 QGYLFCPALPLNE 494
Cdd:PRK11829 635 QGFLFSPPLPRAE 647
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
78-494 |
1.05e-54 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 194.55 E-value: 1.05e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 78 EKEKRNAVHDALTGLPNRKYCFELIEDRIQSGDPFSVIlfdVVNFKQVNDAMGHFCGDQ---LLIQIGQRLQEKLKGSDK 154
Cdd:PRK13561 225 EEQSRNATRFPVSDLPNKALLMALLEQVVARKQTTALM---IITCETLRDTAGVLKEAQreiLLLTLVEKLKSVLSPRMV 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 155 IFRVGGDEFVILTSSACE-ETGKSLIEELDSALSNRFHLDEFQVSSRVVFGVSTYpYDALSNDLLIKHADIAMYHAKRNG 233
Cdd:PRK13561 302 LAQISGYDFAIIANGVKEpWHAITLGQQVLTIINERLPIQRIQLRPSCSIGIAMF-YGDLTAEQLYSRAISAAFTARRKG 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 234 -NLFAFYNEDMNVGAKYQLEISSRIQCALEKEEFQLYYQPLIDAHTNLAVGFEAVIRWHDENGKTISPNDFIPIAERSNQ 312
Cdd:PRK13561 381 kNQIQFFDPQQMEAAQKRLTEESDILNALENHQFAIWLQPQVEMRSGKLVSAEALLRMQQPDGSWDLPEGLIDRIESCGL 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 313 VHNITMWVLNQVEKDLQTFIEKDIKLPVHVNLSAKDLSSNLLFNRLETLL---KVNPqfaDLISLEITETMAIDRVVELN 389
Cdd:PRK13561 461 MVTVGHWVLEESCRLLAAWQERGIMLPLSVNLSALQLMHPNMVADMLELLtryRIQP---GTLILEVTESRRIDDPHAAV 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 390 PLIHQIKGLGIKISLDDFGTGYSSLSLL---RDLPVDQIKIDRSFLCTASRTEgtrSIVENTIALAHGLGYSVVAEGVQD 466
Cdd:PRK13561 538 AILRPLRNAGVRVALDDFGMGYAGLRQLqhmKSLPIDVLKIDKMFVDGLPEDD---SMVAAIIMLAQSLNLQVIAEGVET 614
|
410 420
....*....|....*....|....*...
gi 686144922 467 MDTLHFLRSRGCDIIQGYLFCPALPLNE 494
Cdd:PRK13561 615 EAQRDWLLKAGVGIAQGFLFARALPIEI 642
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
54-496 |
3.10e-51 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 188.34 E-value: 3.10e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 54 GGSIFVVLVIKwsndSILELHTVAEKEKRNAVHDALTGLPNR----KYCFELIEDRIQSGDPFSVILFDVVNFKQVNDAM 129
Cdd:PRK09776 639 GENIGSVLVIQ----DVTESRKMLRQLSYSASHDALTHLANRasfeKQLRRLLQTVNSTHQRHALVFIDLDRFKAVNDSA 714
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 130 GHFCGDQLLIQIGQRLQEKLKGSDKIFRVGGDEFVILTSSaCEetgkslieeLDSALsnrfhldefQVSSRVVFGVSTYP 209
Cdd:PRK09776 715 GHAAGDALLRELASLMLSMLRSSDVLARLGGDEFGLLLPD-CN---------VESAR---------FIATRIISAINDYH 775
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 210 -------YD--------ALSNDL-----LIKHADIAMYHAKRNG----NLFAFYNEDMNvGAKYQLEISSRIQCALEKEE 265
Cdd:PRK09776 776 fpwegrvYRvgasagitLIDANNhqaseVMSQADIACYAAKNAGrgrvTVYEPQQAAAH-SEHRALSLAEQWRMIKENQL 854
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 266 FQLYYQpLIDAHTNLAVGF-EAVIRWHDENGKTISPNDFIPIAERSNQVHNITMWVLNQVekdLQTFIEKDIK--LPVHV 342
Cdd:PRK09776 855 MMLAHG-VASPRIPEARNHwLISLRLWDPEGEIIDEGAFRPAAEDPALMHALDRRVIHEF---FRQAAKAVASkgLSIAL 930
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 343 NLSAKDLSSNLLFNRLETLLKVNPQFADLISLEITETMAIDRVVELNPLIHQIKGLGIKISLDDFGTGYSSLSLLRDLPV 422
Cdd:PRK09776 931 PLSVAGLSSPTLLPFLLEQLENSPLPPRLLHLEITETALLNHAESASRLVQKLRLAGCRVVLSDFGRGLSSFNYLKAFMA 1010
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 686144922 423 DQIKIDRSFLCTASRTEGTRSIVENTIALAHGLGYSVVAEGVQDMDTLHFLRSRGCDIIQGYLFCPALPLNEVI 496
Cdd:PRK09776 1011 DYLKLDGELVANLHGNLMDEMLISIIQGHAQRLGMKTIAGPVELPLVLDTLSGIGVDLAYGYAIARPQPLDLLL 1084
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
86-233 |
8.33e-51 |
|
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as a domain of unknown function 1 (DUF1). This domain is widely present in bacteria, linked to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain shows homology to the adenylyl cyclase catalytic domain. This correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesion in bacteria.
Pssm-ID: 143635 [Multi-domain] Cd Length: 158 Bit Score: 170.82 E-value: 8.33e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 86 HDALTGLPNRKYCFELIEDRIQ----SGDPFSVILFDVVNFKQVNDAMGHFCGDQLLIQIGQRLQEKLKGSDKIFRVGGD 161
Cdd:cd01949 2 TDPLTGLPNRRAFEERLERLLArarrSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGD 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 686144922 162 EFVILTSSACEETGKSLIEELDSALSNRFHLDEFQVSSRVVFGVSTYPYDALSNDLLIKHADIAMYHAKRNG 233
Cdd:cd01949 82 EFAILLPGTDLEEAEALAERLREAIEEPFFIDGQEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSG 153
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
14-239 |
2.05e-49 |
|
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants [Signal transduction mechanisms];
Pssm-ID: 441801 [Multi-domain] Cd Length: 275 Bit Score: 170.93 E-value: 2.05e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 14 WTFLLLLISCFIFAYAAFLHAIMQKPIASLLETGVSLILFGGSIFVVLVIKWSNDSILELHTVAEKEKRNAVHDALTGLP 93
Cdd:COG2199 44 LLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLLLLLALEDITELRRLEERLRRLATHDPLTGLP 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 94 NRKYCFELIEDRIQ----SGDPFSVILFDVVNFKQVNDAMGHFCGDQLLIQIGQRLQEKLKGSDKIFRVGGDEFVILTSS 169
Cdd:COG2199 124 NRRAFEERLERELArarrEGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPG 203
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 686144922 170 ACEETGKSLIEELDSALSN-RFHLDEFQVSSRVVFGVSTYPYDALSNDLLIKHADIAMYHAKRNG-NLFAFY 239
Cdd:COG2199 204 TDLEEAEALAERLREALEQlPFELEGKELRVTVSIGVALYPEDGDSAEELLRRADLALYRAKRAGrNRVVVY 275
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
82-239 |
2.03e-40 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 143.16 E-value: 2.03e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 82 RNAVHDALTGLPNRKYCFELIEDRIQ----SGDPFSVILFDVVNFKQVNDAMGHFCGDQLLIQIGQRLQEKLKGSDKIFR 157
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQraqrQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 158 VGGDEFVILTSSACEETGKSLIEELDSALSNRFHLDEFQVSSRVVFGVSTYPYDALSNDLLIKHADIAMYHAKRNG-NLF 236
Cdd:smart00267 81 LGGDEFALLLPETSLEEAIALAERILQQLREPIIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGrNQV 160
|
...
gi 686144922 237 AFY 239
Cdd:smart00267 161 AVY 163
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
84-233 |
3.94e-40 |
|
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of non-homologous domains in a variety of bacteria. It has been shown to be homologous to the adenylyl cyclase catalytic domain and has diguanylate cyclase activity. This observation correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. In the WspR protein of Pseudomonas aeruginosa, the GGDEF domain acts as a diguanylate cyclase, PDB:3bre, when the whole molecule appears to form a tetramer consisting of two symmetrically-related dimers representing a biological unit. The active site is the GGD/EF motif, buried in the structure, and the cyclic dimeric guanosine monophosphate (c-di-GMP) bind to the inhibitory-motif RxxD on the surface. The enzyme thus catalyzes the cyclization of two guanosine triphosphate (GTP) molecules to one c-di-GMP molecule.
Pssm-ID: 425976 [Multi-domain] Cd Length: 160 Bit Score: 142.39 E-value: 3.94e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 84 AVHDALTGLPNRKYCFELIEDRIQ----SGDPFSVILFDVVNFKQVNDAMGHFCGDQLLIQIGQRLQEKLKGSDKIFRVG 159
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQralrEGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 686144922 160 GDEFVILTSSACEETGKSLIEELDSALSNR---FHLDEFQVSSRVVFGVSTYPYDALSNDLLIKHADIAMYHAKRNG 233
Cdd:pfam00990 81 GDEFAILLPETSLEGAQELAERIRRLLAKLkipHTVSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAG 157
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
84-241 |
7.68e-35 |
|
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by many proteins carrying the domain. There is evidence that the domain has diguanylate cyclase activity. Several proteins carrying this domain also carry domains with functions relating to environmental sensing. These include PleD, a response regulator protein involved in the swarmer-to-stalked cell transition in Caulobacter crescentus, and FixL, a heme-containing oxygen sensor protein. [Regulatory functions, Small molecule interactions, Signal transduction, Other]
Pssm-ID: 272984 [Multi-domain] Cd Length: 165 Bit Score: 128.22 E-value: 7.68e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 84 AVHDALTGLPNRKYCFELIEDRIQS----GDPFSVILFDVVNFKQVNDAMGHFCGDQLLIQIGQRLQEKLKGSDKIFRVG 159
Cdd:TIGR00254 2 AVRDPLTGLYNRRYLEEMLDSELKRarrfQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 160 GDEFVILTSsaceetGKSLIEELDSALSNRFHLDEF--------QVSSRVVFGVSTYPYDALSNDLLIKHADIAMYHAKR 231
Cdd:TIGR00254 82 GEEFVVILP------GTPLEDALSKAERLRDAINSKpievagseTLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKK 155
|
170
....*....|
gi 686144922 232 NGNLFAFYNE 241
Cdd:TIGR00254 156 AGRNRVVVAD 165
|
|
| PRK10551 |
PRK10551 |
cyclic di-GMP phosphodiesterase; |
245-501 |
1.77e-32 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 182541 [Multi-domain] Cd Length: 518 Bit Score: 130.11 E-value: 1.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 245 VGAKYQLEISSR----IQCALEKEEFQLYYQPLIDAHTNLAVGFEAVIRWHDENGKTISPNDFIPIAERSNQVHNITMWV 320
Cdd:PRK10551 252 LLCYYLLSLRMRpgkeILTGIKRGQFYVEYQPVVDTQTLRVTGLEALLRWRHPTAGEIPPDAFINYAEAQKLIVPLTQHL 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 321 LNQVEKD---LQTFIEKDIKLPVhvNLSAKDLSSNLLFNRLETLLKVNPQFADLISLEITE-TMAIDRvvELNPLIHQIK 396
Cdd:PRK10551 332 FELIARDaaeLQKVLPVGAKLGI--NISPAHLHSDSFKADVQRLLASLPADHFQIVLEITErDMVQEE--EATKLFAWLH 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 397 GLGIKISLDDFGTGYSSLSLLRDLPVDQIKIDRSFLCTASRTEGTRSIVENTIALAHGLGYSVVAEGVQDMDTLHFLRSR 476
Cdd:PRK10551 408 SQGIEIAIDDFGTGHSALIYLERFTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRER 487
|
250 260
....*....|....*....|....*
gi 686144922 477 GCDIIQGYLFCPALPLNEVITWVNE 501
Cdd:PRK10551 488 GVNFLQGYWISRPLPLEDFVRWLKE 512
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
84-233 |
1.09e-23 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 103.83 E-value: 1.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 84 AVHDALTGLPNRKYcFE-----LIEDRIQSGDPFSVILFDVVNFKQVNDAMGHFCGDQLLIQIGQRLQEKLKGSDKIFRV 158
Cdd:PRK09581 292 AVTDGLTGLHNRRY-FDmhlknLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARY 370
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 686144922 159 GGDEFVILTSSACEETGKSLIEELDSALSNR-FHL--DEFQVSSRVVFGVSTYPYDALSNDLLIKHADIAMYHAKRNG 233
Cdd:PRK09581 371 GGEEFVVVMPDTDIEDAIAVAERIRRKIAEEpFIIsdGKERLNVTVSIGVAELRPSGDTIEALIKRADKALYEAKNTG 448
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
87-242 |
5.34e-23 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 98.99 E-value: 5.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 87 DALTGLPNRKYCFELIE-DRIQSGD-PFSVILFDVVNFKQVNDAMGHFCGDQLLIQIGQRLQEKLKGSDKIFRVGGDEFV 164
Cdd:PRK09894 132 DVLTGLPGRRVLDESFDhQLRNREPqNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYGGEEFI 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 165 ILTSSACEETGKSLIEELDSALS-NRFHLDEFQVSSRVVFGVSTYPYDaLSNDLLIKHADIAMYHAKRNG-NLFAFYNED 242
Cdd:PRK09894 212 ICLKAATDEEACRAGERIRQLIAnHAITHSDGRINITATFGVSRAFPE-ETLDVVIGRADRAMYEGKQTGrNRVMFIDEQ 290
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
84-233 |
9.01e-16 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 80.06 E-value: 9.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 84 AVHDALTGLPNRKYCFE----LIEDRIQSGDPFSVILFDVVNFKQVNDAMGHFCGDQLLIQIGQRLQEKLKGSDKIFRVG 159
Cdd:PRK15426 398 AWHDPLTRLYNRGALFEkaraLAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRVG 477
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 686144922 160 GDEFVILTSSACEETGKSLIEELDSALSNRFHLDEFQVSSRVV--FGVS-TYPYDALSNDLLIKHADIAMYHAKRNG 233
Cdd:PRK15426 478 GEEFCVVLPGASLAEAAQVAERIRLRINEKEILVAKSTTIRISasLGVSsAEEDGDYDFEQLQSLADRRLYLAKQAG 554
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
82-230 |
8.65e-14 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 73.12 E-value: 8.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 82 RNAVHDALTGLPNR---KYCF-ELIEDriQSGDPFSVILF-DVVNFKQVNDAMGHFCGDQLLIQIGQRLQEKLKGSDKIF 156
Cdd:PRK09966 246 RTALHDPLTGLANRaafRSGInTLMNN--SDARKTSALLFlDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHKAY 323
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 686144922 157 RVGGDEF-VILTSSACEETGKSLIEELDSALSNRFHLDEFQVSSRVVFGVSTYPYDALSNDLLIKHADIAMYHAK 230
Cdd:PRK09966 324 RLGGDEFaMVLYDVQSESEVQQICSALTQIFNLPFDLHNGHQTTMTLSIGYAMTIEHASAEKLQELADHNMYQAK 398
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
76-233 |
1.53e-12 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 69.09 E-value: 1.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 76 VAEKEKRNAV---HDALTGLPNRKY-----CFELIEDRIQSGDPfSVILFDVVNFKQVNDAMGHFCGDQLLIQIGQRLQE 147
Cdd:PRK10245 194 LAEHKRRLQVmstRDGMTGVYNRRHwetllRNEFDNCRRHHRDA-TLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQI 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 148 KLKGSDKIFRVGGDEFVILTSSACEETGKSLIEELDSALSNRFHLDEFQVSSRVVFGVSTYPYDALSNDLLIKHADIAMY 227
Cdd:PRK10245 273 TLRGSDVIGRFGGDEFAVIMSGTPAESAITAMSRVHEGLNTLRLPNAPQVTLRISVGVAPLNPQMSHYREWLKSADLALY 352
|
....*.
gi 686144922 228 HAKRNG 233
Cdd:PRK10245 353 KAKNAG 358
|
|
| YuxH |
COG3434 |
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ... |
339-487 |
5.54e-09 |
|
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction mechanisms];
Pssm-ID: 442660 [Multi-domain] Cd Length: 407 Bit Score: 58.27 E-value: 5.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 339 PVHVNLSAkdlssNLLFNRLETLLKvnpqfADLISLEITETMAIDRvvELNPLIHQIKGLGIKISLDDFGTGYSSLSLLR 418
Cdd:COG3434 63 LAFINFTE-----ELLLSDLPELLP-----PERVVLEILEDVEPDE--ELLEALKELKEKGYRIALDDFVLDPEWDPLLP 130
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 686144922 419 DlpVDQIKIDrsFLctASRTEGTRSIVEntiaLAHGLGYSVVAEGVQDMDTLHFLRSRGCDIIQGYLFC 487
Cdd:COG3434 131 L--ADIIKID--VL--ALDLEELAELVA----RLKRYGIKLLAEKVETREEFELCKELGFDLFQGYFFS 189
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
83-493 |
1.72e-07 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 53.71 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 83 NAVHDALTGLPNRKYcFE-----LIEDRIQSGDPFSVILFDVVNFKQVNDAMGHFCGDQLLIQIG----QRLQEKlkgSD 153
Cdd:PRK11059 227 NAFQDAKTGLGNRLF-FDnqlatLLEDQEMVGAHGVVMLIRLPDFDLLQEEWGESQVEELLFELInllsTFVMRY---PG 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 154 KIF-RVGGDEFVIL----TSSACEETGKSLIEELDSALSNR-------FHLdefqvssrvvfGVSTYpYDALSNDLLIKH 221
Cdd:PRK11059 303 ALLaRYSRSDFAVLlphrSLKEADSLASQLLKAVDALPPPKmldrddfLHI-----------GICAY-RSGQSTEQVMEE 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 222 ADIAMYHA--KRNGNLFafynedmnVGAKYQLEISSR--------IQCALEKEEFQLYYQPLIDAHTNlAVGFEAVIRWH 291
Cdd:PRK11059 371 AEMALRSAqlQGGNGWF--------VYDKAQLPEKGRgsvrwrtlLEQTLVRGGPRLYQQPAVTRDGK-VHHRELFCRIR 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 292 DENGKTISPNDFIPIAERSNQVHNITMWVLNQVEKDLqtfiEKDIKLPVHVNLSAKDLSSNLLFNRL-ETLLKVNPQFAD 370
Cdd:PRK11059 442 DGQGELLSAELFMPMVQQLGLSEQYDRQVIERVLPLL----RYWPEENLSINLSVDSLLSRAFQRWLrDTLLQCPRSQRK 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 371 LISLEITETMAIDRVVELNPLIHQIKGLGIKISLDDFGTGYSSLSLLRDLPVDQIKIDRSfLCT--ASRTEG---TRSIV 445
Cdd:PRK11059 518 RLIFELAEADVCQHISRLRPVLRMLRGLGCRLAVDQAGLTVVSTSYIKELNVELIKLHPS-LVRniHKRTENqlfVRSLV 596
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 686144922 446 EntiALAhGLGYSVVAEGVQDMDTLHFLRSRGCDIIQGYLFCPALPLN 493
Cdd:PRK11059 597 G---ACA-GTETQVFATGVESREEWQTLQELGVSGGQGDFFAESQPLD 640
|
|
| Nucleotidyl_cyc_III |
cd07556 |
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
111-232 |
1.04e-05 |
|
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse group of nucleotidyl cyclases (NC's) containing prokaryotic and eukaryotic proteins. They can be divided into two major groups; the mononucleotidyl cyclases (MNC's) and the diguanylate cyclases (DGC's). The MNC's, which include the adenylate cyclases (AC's) and the guanylate cyclases (GC's), have a conserved cyclase homology domain (CHD), while the DGC's have a conserved GGDEF domain, named after a conserved motif within this subgroup. Their products, cyclic guanylyl and adenylyl nucleotides, are second messengers that play important roles in eukaryotic signal transduction and prokaryotic sensory pathways.
Pssm-ID: 143637 [Multi-domain] Cd Length: 133 Bit Score: 45.04 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686144922 111 PFSVILFDVVNFKQVNDAMGHFCGDQLLIQIGQRLQEKL-KGSDKIFRVGGDEFVILTS----SACEETGKSLIEELDSA 185
Cdd:cd07556 1 PVTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIrRSGDLKIKTIGDEFMVVSGldhpAAAVAFAEDMREAVSAL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 686144922 186 LSNRFHLDEFQV---SSRVVFGV--STYPYDALSNdlLIKHADIAMYHAKRN 232
Cdd:cd07556 81 NQSEGNPVRVRIgihTGPVVVGVigSRPQYDVWGA--LVNLASRMESQAKAG 130
|
|
| PleD |
COG3706 |
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ... |
153-230 |
5.22e-04 |
|
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate cyclase (GGDEF) domain [Signal transduction mechanisms, Transcription];
Pssm-ID: 442920 [Multi-domain] Cd Length: 179 Bit Score: 41.05 E-value: 5.22e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 686144922 153 DKIFRVGGDEFVILTSSACEETGKSLIEELDSALSNrfhLDEFQVSsrVVFGVstypydalSNDLLIKHADiAMYHAK 230
Cdd:COG3706 116 DLVARYGGEEFAILLPGTDLEGALAVAERIREAVAE---LPSLRVT--VSIGV--------AGDSLLKRAD-ALYQAR 179
|
|
| |
