|
Name |
Accession |
Description |
Interval |
E-value |
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
344-828 |
1.63e-69 |
|
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: 240.46 E-value: 1.63e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 344 DDRQEILHHSLTYIAMRESDEINEFRCEDFQRDSTVSPLLNLVRNAVADLDSMNTQMEKKLHQQARRLTESYRIDSRTGL 423
Cdd:COG2200 79 LLLLLALLLLLLLLLLLLLLLLLLLALLLAALLALLLLLLLLLLLLLLSLLLLLVLVLLRLALELLLALLLLALLALLDL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 424 PNRIVLKERLNTILFSEHLLTLKLTNFHQVNEKYGYQVGDQLLLDLSNHFVERLHLSVAKESQVKVELFSIGVGEWAIIF 503
Cdd:COG2200 159 LLLLLLRRLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLDNDGLGGAGLLLLLLLALLLLLLLARLLLALLGGGGGGF 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 504 NANVGCDKIEQRFVEFADDIEHINFEPYGLADIDYLSVSLCGGFASRCDFLTDNGDEILLKAIEARRYGVRNNTHITNAK 583
Cdd:COG2200 239 LLLLLLLAAAAAAAAALRLLLLLLLEPLLLGGGLVVVASSGGGAAAPDDGADAALLLAAAAAAAAAAAGGGRGRVVFFAA 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 584 DiqvsEEDRKEQLGWLSCVSRAILDQNIITYSQPIVASGTHEMIGQECLVRIMESDGTIVPPGKFLPIIADTHLYTRLSR 663
Cdd:COG2200 319 A----EARARRRLALESELREALEEGELRLYYQPIVDLRTGRVVGYEALLRWRHPDGGLISPAEFIPAAERSGLIVELDR 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 664 HMIKNTIGYMADKQS-----PFSINLSPQDLLSDKTLEVLETAISAMN-DPTRLGLEVLESEQIKDYGRMIEVCDHFRAL 737
Cdd:COG2200 395 WVLERALRQLARWPErgldlRLSVNLSARSLLDPDFLERLLELLAEYGlPPERLVLEITESALLEDLEAAIELLARLRAL 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 738 GARIIVDDFGSGYSNIDEIIKLEPQIIKLDGSLIRNIDKDQKQRNIASQLVRLCQVFNAQTVAEFVHNQQVCEIAEQMGV 817
Cdd:COG2200 475 GVRIALDDFGTGYSSLSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGC 554
|
490
....*....|.
gi 2282447070 818 DYLQGYYFGEP 828
Cdd:COG2200 555 DYAQGYLFGRP 565
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
602-828 |
1.43e-66 |
|
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: 221.42 E-value: 1.43e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 602 VSRAILDQNIITYSQPIVASGTHEMIGQECLVRIMESDGTIVPPGKFLPIIADTHLYTRLSRHMIKNTIGYMADKQS--- 678
Cdd:pfam00563 4 LRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQLgpd 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 679 -PFSINLSPQDLLSDKTLE-VLETAISAMNDPTRLGLEVLESEQIKDYGRMIEVCDHFRALGARIIVDDFGSGYSNIDEI 756
Cdd:pfam00563 84 iKLSINLSPASLADPGFLElLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSLSYL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2282447070 757 IKLEPQIIKLDGSLIRNIDKDQKQRNIASQLVRLCQVFNAQTVAEFVHNQQVCEIAEQMGVDYLQGYYFGEP 828
Cdd:pfam00563 164 LRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
602-828 |
7.76e-60 |
|
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: 203.16 E-value: 7.76e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 602 VSRAILDQNIITYSQPIVASGTHEMIGQECLVRIMESDGTIVPPGKFLPIIADTHLYTRLSRHMIKNTIGYMADKQS--- 678
Cdd:cd01948 3 LRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAggp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 679 --PFSINLSPQDLLSDKTLEVLETAISAMN-DPTRLGLEVLESEQIKDYGRMIEVCDHFRALGARIIVDDFGSGYSNIDE 755
Cdd:cd01948 83 dlRLSVNLSARQLRDPDFLDRLLELLAETGlPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSLSY 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2282447070 756 IIKLEPQIIKLDGSLIRNIDKDQKQRNIASQLVRLCQVFNAQTVAEFVHNQQVCEIAEQMGVDYLQGYYFGEP 828
Cdd:cd01948 163 LKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRP 235
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
614-832 |
4.14e-44 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 159.30 E-value: 4.14e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 614 YSQPIVASGTHEMIGQECLVRIMESDGTIVPPGKFLPIIADTHLYTRLSRHMIKNTIGYMADKQS------PFSINLSPQ 687
Cdd:smart00052 16 YYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAqgppplLISINLSAR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 688 DLLSDKTLE-VLETAISAMNDPTRLGLEVLESEQIKDYGRMIEVCDHFRALGARIIVDDFGSGYSNIDEIIKLEPQIIKL 766
Cdd:smart00052 96 QLISPDLVPrVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYSSLSYLKRLPVDLLKI 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2282447070 767 DGSLIRNIDKDQKQRNIASQLVRLCQVFNAQTVAEFVHNQQVCEIAEQMGVDYLQGYYFGEPKRLF 832
Cdd:smart00052 176 DKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPLD 241
|
|
| FIST |
COG3287 |
FIST domain protein MJ1623, contains FIST_N and FIST_C domains [Signal transduction mechanisms] ... |
1-361 |
1.25e-43 |
|
FIST domain protein MJ1623, contains FIST_N and FIST_C domains [Signal transduction mechanisms];
Pssm-ID: 442517 [Multi-domain] Cd Length: 382 Bit Score: 162.43 E-value: 1.25e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 1 MQTFTFLANTEELFKSQFDQ------REWCDSKQYLIQLFSAQSSDvARRIASVALNRLSNATLIGQSARHVICDNCLES 74
Cdd:COG3287 1 MKTFVGVGHSTAADPAEAGRaaeealAQLGAADPALVLVFASPDYD-LEALLAALRAAFPGAPIIGCSTAGEISPGGVLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 75 SCTLIIISEFNETRLTSAV-QPFTGNPNQDSQELASQL----DLSKDAKTVISLCDQVEGRDYPIYSAFEN-LPYTLPVA 148
Cdd:COG3287 80 GSVVLLAFSFDKFRVGVAVgDGLSDDSREAGRELARRLlaalGPDPDLRFALLLSDGLSGNEEELLEGLYSaLGPDVPIF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 149 GGLCHENEYGR--WVMHNEQTYQHACVAVALtNPRLKVWSDAYSEWNPIGMKLRVTHAVGNRLYALNDKPAIDVFKHYL- 225
Cdd:COG3287 160 GGSAGDDLRFEktYVFHNGEVLSDAAVVALL-GTSLPVGVGSSHGWKPTGPEMVVTKAEGRVVYEIDGEPAAEVYARYLg 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 226 ADGKDLPFSqLMSFPLYRELGRKKG-ISTPLRINDDGSIEFDSPWHVGEEAQFCYNHPSLTAEKVRHGAEMLAMH---QP 301
Cdd:COG3287 239 DDAEELPAS-FLLFPLGVRIGGGEYlVRSPLAVEEDGSLTFAGDIPEGSVLRLMEGNPDDLIEAAERAAEAALARlggKP 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2282447070 302 ESVIIYNCVSRLEFIDSKL--ELKPFEGI--VNACGAYCMGELYRNDDRQEILH-HSLTYIAMRE 361
Cdd:COG3287 318 EAALLFDCVGRRLVLGQRVeeELEAVSELlgAPVAGFYTYGEIGPFGGGGNQHHnQTLTGVAFGE 382
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
401-828 |
3.20e-33 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 136.74 E-value: 3.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 401 EKKLHQQarRLTESYRIDSRTGLPNRIVLKERLNTILFSEH-----LLTLKLTNFHQVNEKYGYQVGDQLLLDLSNHFve 475
Cdd:PRK10060 225 EERRAQE--RLRILANTDSITGLPNRNAIQELIDHAINAADnnqvgIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAI-- 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 476 rlhLSVAKESQVkveLFSIGvGEWAIIFNANVGCDKIE---QRFVEFADDIEHInfepyGLADIdYLSVSLcgGFAsrcd 552
Cdd:PRK10060 301 ---LSCLEEDQT---LARLG-GDEFLVLASHTSQAALEamaSRILTRLRLPFRI-----GLIEV-YTGCSI--GIA---- 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 553 FLTDNGDEilLKAIearrygVRN-NTHITNAKD-------IQVSEEDRK--EQLgWLSCVSRAILDQN--IITYsQPIVa 620
Cdd:PRK10060 362 LAPEHGDD--SESL------IRSaDTAMYTAKEggrgqfcVFSPEMNQRvfEYL-WLDTNLRKALENDqlVIHY-QPKI- 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 621 SGTHEMIGQECLVRIMESDGTIVPPGKFLPIIADTHLYTRLSRHMIKNTIGYMADKQSP-----FSINLSPQDLLSDKTL 695
Cdd:PRK10060 431 TWRGEVRSLEALVRWQSPERGLIPPLEFISYAEESGLIVPLGRWVMLDVVRQVAKWRDKginlrVAVNVSARQLADQTIF 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 696 EVLETAISAMN-DPTRLGLEVLESEQIKDYGRMIEVCDHFRALGARIIVDDFGSGYSNIDEIIKLEPQIIKLDGSLIRNI 774
Cdd:PRK10060 511 TALKQALQELNfEYCPIDVELTESCLIENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDI 590
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2282447070 775 DKDQKQRNIASQLVRLCQVFNAQTVAEFVHNQQVCEIAEQMGVDYLQGYYFGEP 828
Cdd:PRK10060 591 HKQPVSQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVNERQGFLFAKP 644
|
|
| FIST |
smart00897 |
FIST N domain; The FIST N domain is a novel sensory domain, which is present in signal ... |
30-215 |
5.18e-19 |
|
FIST N domain; The FIST N domain is a novel sensory domain, which is present in signal transduction proteins from Bacteria, Archaea and Eukarya. Chromosomal proximity of FIST-encoding genes to those coding for proteins involved in amino acid metabolism and transport suggest that FIST domains bind small ligands, such as amino acids.
Pssm-ID: 214894 Cd Length: 196 Bit Score: 85.83 E-value: 5.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 30 LIQLFSAQSSDVARRIASVALNRLSNAT-LIGQSARHVICDN---CLESSCtLIIISEFNETRLTSAVQP-FTGNPNQDS 104
Cdd:smart00897 3 LLVLFFSSPAYDAEALLAALRERFPGATpIVGCSTAGEITTGvvqEFEDEP-ALSVMLFELPLVSFDVFSlVDPLPDLVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 105 QELASQLDLS---KDAKTVISLCDQVEGRDYPIYSAF-ENLPYTLPVAGGLCHENE--YGRWVMHNEQTYQHAcVAVALT 178
Cdd:smart00897 82 GLLLAALLAAidpRNTFALLLLDDLSSSNEEELLEGLdEALPEGIPIGGGSAGDNLrfQETYVFTNGRVHSGA-VVVAFG 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 2282447070 179 nPRLKVWSDAYSEWNPIGMKLRVTHAVGNRLYALNDK 215
Cdd:smart00897 161 -GGLRFGTGVTQGWRPIGPPFVVTKAEGNVVYELDGE 196
|
|
| FIST_C |
pfam10442 |
FIST C domain; The FIST C domain is a novel sensory domain, which is present in signal ... |
217-342 |
1.19e-16 |
|
FIST C domain; The FIST C domain is a novel sensory domain, which is present in signal transduction proteins from Bacteria, Archaea and Eukarya. Chromosomal proximity of FIST-encoding genes to those coding for proteins involved in amino acid metabolism and transport suggest that FIST domains bind small ligands, such as amino acids.
Pssm-ID: 463094 Cd Length: 135 Bit Score: 77.35 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 217 AIDVFKHYL--ADGKDLPFSqLMSFPLyrelGRKKG-----ISTPLRIN-DDGSIEFDSPWHVGEEAQFCYNHPSLTAEK 288
Cdd:pfam10442 1 ALEVYKEYLggEEDEELPAS-ALEFPL----GVVVGggdylVRSPLGVDpEDGSLAFAGDVPEGSVVQLMLRDADDLIEA 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 289 VRHGAEMLAMHQPESVIIYNCVSRLEFIDSKL--ELKPFE----GIVNACGAYCMGELYR 342
Cdd:pfam10442 76 AERAAEAALANPPEGALLFSCAGRGLGLGERFdeELEAIRealgDGVPLAGFYTYGEIGP 135
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
417-484 |
1.55e-04 |
|
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: 43.09 E-value: 1.55e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2282447070 417 IDSRTGLPNRIVLKERLN---------TILFSehLLTLKLTNFHQVNEKYGYQVGDQLLldlsNHFVERLHLSVAKE 484
Cdd:TIGR00254 4 RDPLTGLYNRRYLEEMLDselkrarrfQRSFS--VLMIDIDNFKKINDTLGHDVGDEVL----REVARILQSSVRGS 74
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
344-828 |
1.63e-69 |
|
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: 240.46 E-value: 1.63e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 344 DDRQEILHHSLTYIAMRESDEINEFRCEDFQRDSTVSPLLNLVRNAVADLDSMNTQMEKKLHQQARRLTESYRIDSRTGL 423
Cdd:COG2200 79 LLLLLALLLLLLLLLLLLLLLLLLLALLLAALLALLLLLLLLLLLLLLSLLLLLVLVLLRLALELLLALLLLALLALLDL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 424 PNRIVLKERLNTILFSEHLLTLKLTNFHQVNEKYGYQVGDQLLLDLSNHFVERLHLSVAKESQVKVELFSIGVGEWAIIF 503
Cdd:COG2200 159 LLLLLLRRLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLDNDGLGGAGLLLLLLLALLLLLLLARLLLALLGGGGGGF 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 504 NANVGCDKIEQRFVEFADDIEHINFEPYGLADIDYLSVSLCGGFASRCDFLTDNGDEILLKAIEARRYGVRNNTHITNAK 583
Cdd:COG2200 239 LLLLLLLAAAAAAAAALRLLLLLLLEPLLLGGGLVVVASSGGGAAAPDDGADAALLLAAAAAAAAAAAGGGRGRVVFFAA 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 584 DiqvsEEDRKEQLGWLSCVSRAILDQNIITYSQPIVASGTHEMIGQECLVRIMESDGTIVPPGKFLPIIADTHLYTRLSR 663
Cdd:COG2200 319 A----EARARRRLALESELREALEEGELRLYYQPIVDLRTGRVVGYEALLRWRHPDGGLISPAEFIPAAERSGLIVELDR 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 664 HMIKNTIGYMADKQS-----PFSINLSPQDLLSDKTLEVLETAISAMN-DPTRLGLEVLESEQIKDYGRMIEVCDHFRAL 737
Cdd:COG2200 395 WVLERALRQLARWPErgldlRLSVNLSARSLLDPDFLERLLELLAEYGlPPERLVLEITESALLEDLEAAIELLARLRAL 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 738 GARIIVDDFGSGYSNIDEIIKLEPQIIKLDGSLIRNIDKDQKQRNIASQLVRLCQVFNAQTVAEFVHNQQVCEIAEQMGV 817
Cdd:COG2200 475 GVRIALDDFGTGYSSLSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGC 554
|
490
....*....|.
gi 2282447070 818 DYLQGYYFGEP 828
Cdd:COG2200 555 DYAQGYLFGRP 565
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
602-828 |
1.43e-66 |
|
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: 221.42 E-value: 1.43e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 602 VSRAILDQNIITYSQPIVASGTHEMIGQECLVRIMESDGTIVPPGKFLPIIADTHLYTRLSRHMIKNTIGYMADKQS--- 678
Cdd:pfam00563 4 LRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQLgpd 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 679 -PFSINLSPQDLLSDKTLE-VLETAISAMNDPTRLGLEVLESEQIKDYGRMIEVCDHFRALGARIIVDDFGSGYSNIDEI 756
Cdd:pfam00563 84 iKLSINLSPASLADPGFLElLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSLSYL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2282447070 757 IKLEPQIIKLDGSLIRNIDKDQKQRNIASQLVRLCQVFNAQTVAEFVHNQQVCEIAEQMGVDYLQGYYFGEP 828
Cdd:pfam00563 164 LRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
602-828 |
7.76e-60 |
|
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: 203.16 E-value: 7.76e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 602 VSRAILDQNIITYSQPIVASGTHEMIGQECLVRIMESDGTIVPPGKFLPIIADTHLYTRLSRHMIKNTIGYMADKQS--- 678
Cdd:cd01948 3 LRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAggp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 679 --PFSINLSPQDLLSDKTLEVLETAISAMN-DPTRLGLEVLESEQIKDYGRMIEVCDHFRALGARIIVDDFGSGYSNIDE 755
Cdd:cd01948 83 dlRLSVNLSARQLRDPDFLDRLLELLAETGlPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSLSY 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2282447070 756 IIKLEPQIIKLDGSLIRNIDKDQKQRNIASQLVRLCQVFNAQTVAEFVHNQQVCEIAEQMGVDYLQGYYFGEP 828
Cdd:cd01948 163 LKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRP 235
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
399-828 |
8.84e-50 |
|
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: 186.90 E-value: 8.84e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 399 QMEKKLHQQARRltesyriDSRTGLPNRIVLKERLNTILFSEH-------LLTLKLTNFHQVNEKYGYQVGDQLLLDLSn 471
Cdd:COG5001 242 RAEERLRHLAYH-------DPLTGLPNRRLFLDRLEQALARARrsgrrlaLLFIDLDRFKEINDTLGHAAGDELLREVA- 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 472 hfvERLHLSVAKESQVkvelFSIGvG-EWAIIFNANVGCDKIEQrfveFADDI-EHINfEPYGLADID-YLSVSLcgGFA 548
Cdd:COG5001 314 ---RRLRACLREGDTV----ARLG-GdEFAVLLPDLDDPEDAEA----VAERIlAALA-EPFELDGHElYVSASI--GIA 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 549 SRCDfltDNGD-EILLKA--I---EARRYGvRNNTHITNAkdiQVSEEDRkEQLGWLSCVSRAILDQNIITYSQPIVASG 622
Cdd:COG5001 379 LYPD---DGADaEELLRNadLamyRAKAAG-RNRYRFFDP---EMDERAR-ERLELEADLRRALERGELELHYQPQVDLA 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 623 THEMIGQECLVRIMESDGTIVPPGKFLPIIADTHLYTRLSRHMIKNTIGYMADKQS------PFSINLSPQDLLSDKTLE 696
Cdd:COG5001 451 TGRIVGAEALLRWQHPERGLVSPAEFIPLAEETGLIVPLGEWVLREACRQLAAWQDaglpdlRVAVNLSARQLRDPDLVD 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 697 VLETAISAMN-DPTRLGLEVLESEQIKDYGRMIEVCDHFRALGARIIVDDFGSGYSNIDEIIKLEPQIIKLDGSLIRNID 775
Cdd:COG5001 531 RVRRALAETGlPPSRLELEITESALLEDPEEALETLRALRALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLA 610
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2282447070 776 KDQKQRNIASQLVRLCQVFNAQTVAEFVHNQQVCEIAEQMGVDYLQGYYFGEP 828
Cdd:COG5001 611 EDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRELGCDYAQGYLFSRP 663
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
614-832 |
4.14e-44 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 159.30 E-value: 4.14e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 614 YSQPIVASGTHEMIGQECLVRIMESDGTIVPPGKFLPIIADTHLYTRLSRHMIKNTIGYMADKQS------PFSINLSPQ 687
Cdd:smart00052 16 YYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAqgppplLISINLSAR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 688 DLLSDKTLE-VLETAISAMNDPTRLGLEVLESEQIKDYGRMIEVCDHFRALGARIIVDDFGSGYSNIDEIIKLEPQIIKL 766
Cdd:smart00052 96 QLISPDLVPrVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYSSLSYLKRLPVDLLKI 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2282447070 767 DGSLIRNIDKDQKQRNIASQLVRLCQVFNAQTVAEFVHNQQVCEIAEQMGVDYLQGYYFGEPKRLF 832
Cdd:smart00052 176 DKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPLD 241
|
|
| FIST |
COG3287 |
FIST domain protein MJ1623, contains FIST_N and FIST_C domains [Signal transduction mechanisms] ... |
1-361 |
1.25e-43 |
|
FIST domain protein MJ1623, contains FIST_N and FIST_C domains [Signal transduction mechanisms];
Pssm-ID: 442517 [Multi-domain] Cd Length: 382 Bit Score: 162.43 E-value: 1.25e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 1 MQTFTFLANTEELFKSQFDQ------REWCDSKQYLIQLFSAQSSDvARRIASVALNRLSNATLIGQSARHVICDNCLES 74
Cdd:COG3287 1 MKTFVGVGHSTAADPAEAGRaaeealAQLGAADPALVLVFASPDYD-LEALLAALRAAFPGAPIIGCSTAGEISPGGVLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 75 SCTLIIISEFNETRLTSAV-QPFTGNPNQDSQELASQL----DLSKDAKTVISLCDQVEGRDYPIYSAFEN-LPYTLPVA 148
Cdd:COG3287 80 GSVVLLAFSFDKFRVGVAVgDGLSDDSREAGRELARRLlaalGPDPDLRFALLLSDGLSGNEEELLEGLYSaLGPDVPIF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 149 GGLCHENEYGR--WVMHNEQTYQHACVAVALtNPRLKVWSDAYSEWNPIGMKLRVTHAVGNRLYALNDKPAIDVFKHYL- 225
Cdd:COG3287 160 GGSAGDDLRFEktYVFHNGEVLSDAAVVALL-GTSLPVGVGSSHGWKPTGPEMVVTKAEGRVVYEIDGEPAAEVYARYLg 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 226 ADGKDLPFSqLMSFPLYRELGRKKG-ISTPLRINDDGSIEFDSPWHVGEEAQFCYNHPSLTAEKVRHGAEMLAMH---QP 301
Cdd:COG3287 239 DDAEELPAS-FLLFPLGVRIGGGEYlVRSPLAVEEDGSLTFAGDIPEGSVLRLMEGNPDDLIEAAERAAEAALARlggKP 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2282447070 302 ESVIIYNCVSRLEFIDSKL--ELKPFEGI--VNACGAYCMGELYRNDDRQEILH-HSLTYIAMRE 361
Cdd:COG3287 318 EAALLFDCVGRRLVLGQRVeeELEAVSELlgAPVAGFYTYGEIGPFGGGGNQHHnQTLTGVAFGE 382
|
|
| YjcC |
COG4943 |
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ... |
604-828 |
2.79e-38 |
|
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: 150.45 E-value: 2.79e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 604 RAILDQNIITYSQPIVASGTHEMIGQECLVRIMESDGTIVPPGKFLPIIADTHLYTRLSRHMIKNTIGYMAD---KQSPF 680
Cdd:COG4943 278 RAIKRREFYVHYQPIVDLKTGRCVGAEALVRWRDPDGSVISPDIFIPLAEQSGLISPLTRQVIEQVFRDLGDllaADPDF 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 681 --SINLSPQDLLSDKTLEVLETAISAMN-DPTRLGLEVLESEQIkDYGRMIEVCDHFRALGARIIVDDFGSGYSNIDEII 757
Cdd:COG4943 358 hiSINLSASDLLSPRFLDDLERLLARTGvAPQQIVLEITERGFI-DPAKARAVIAALREAGHRIAIDDFGTGYSSLSYLQ 436
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2282447070 758 KLEPQIIKLDGSLIRNIDKDQKQRNIASQLVRLCQVFNAQTVAEFVHNQQVCEIAEQMGVDYLQGYYFGEP 828
Cdd:COG4943 437 TLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQYGQGWLFAKP 507
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
401-828 |
3.20e-33 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 136.74 E-value: 3.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 401 EKKLHQQarRLTESYRIDSRTGLPNRIVLKERLNTILFSEH-----LLTLKLTNFHQVNEKYGYQVGDQLLLDLSNHFve 475
Cdd:PRK10060 225 EERRAQE--RLRILANTDSITGLPNRNAIQELIDHAINAADnnqvgIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAI-- 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 476 rlhLSVAKESQVkveLFSIGvGEWAIIFNANVGCDKIE---QRFVEFADDIEHInfepyGLADIdYLSVSLcgGFAsrcd 552
Cdd:PRK10060 301 ---LSCLEEDQT---LARLG-GDEFLVLASHTSQAALEamaSRILTRLRLPFRI-----GLIEV-YTGCSI--GIA---- 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 553 FLTDNGDEilLKAIearrygVRN-NTHITNAKD-------IQVSEEDRK--EQLgWLSCVSRAILDQN--IITYsQPIVa 620
Cdd:PRK10060 362 LAPEHGDD--SESL------IRSaDTAMYTAKEggrgqfcVFSPEMNQRvfEYL-WLDTNLRKALENDqlVIHY-QPKI- 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 621 SGTHEMIGQECLVRIMESDGTIVPPGKFLPIIADTHLYTRLSRHMIKNTIGYMADKQSP-----FSINLSPQDLLSDKTL 695
Cdd:PRK10060 431 TWRGEVRSLEALVRWQSPERGLIPPLEFISYAEESGLIVPLGRWVMLDVVRQVAKWRDKginlrVAVNVSARQLADQTIF 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 696 EVLETAISAMN-DPTRLGLEVLESEQIKDYGRMIEVCDHFRALGARIIVDDFGSGYSNIDEIIKLEPQIIKLDGSLIRNI 774
Cdd:PRK10060 511 TALKQALQELNfEYCPIDVELTESCLIENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDI 590
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2282447070 775 DKDQKQRNIASQLVRLCQVFNAQTVAEFVHNQQVCEIAEQMGVDYLQGYYFGEP 828
Cdd:PRK10060 591 HKQPVSQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVNERQGFLFAKP 644
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
334-828 |
1.11e-28 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 122.74 E-value: 1.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 334 AYCMGEL-----------YRNDDRQEILHHSLTYIAMRESDEINEfrcedfqrdstvspllnLVRNAvadldSMNTQMEK 402
Cdd:PRK11829 165 AWCINRLiihplramakeLEDIGDHGVLHHQLTLPAHHQDDELGV-----------------LVRNY-----NRNQQLLA 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 403 KLHQQARRLTESYridSRTGLPNRIVLKERLNTILFSE------HLLTLKLTNFHQVNEKYGYQVGDQLLLDLsnhfVER 476
Cdd:PRK11829 223 DAYADMGRISHRF---PVTELPNRSLFISLLEKEIASStrtdhfHLLVIGIETLQEVSGAMSEAQHQQLLLTI----VQR 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 477 LHLSVAKES---QVKVELFSIGVGEWAIIFNAnvgcdkieqrfVEFADDIEHINFEPYGLADIDYLSVSLCGgfASRCDF 553
Cdd:PRK11829 296 IEQCIDDSDllaQLSKTEFAVLARGTRRSFPA-----------MQLARRIMSQVTQPLFFDEITLRPSASIG--ITRYQA 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 554 LTDNGDEILLKAIEARrygvrNNTHITNAKDIQVSE----EDRKEQLGWLSCVSRAILDQNIITYSQPIVASGTHEMIGQ 629
Cdd:PRK11829 363 QQDTAESMMRNASTAM-----MAAHHEGRNQIMVFEphliEKTHKRLTQENDLLQAIENHDFTLFLQPQWDMKRQQVIGA 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 630 ECLVRIMESDGTIVPPGKFLPIIADTHLYTRLSRHMIKNTIGYMADKQS-----PFSINLSPQDLLSDKTLEVLETAISA 704
Cdd:PRK11829 438 EALLRWCQPDGSYVLPSGFVHFAEEEGMMVPLGNWVLEEACRILADWKArgvslPLSVNISGLQVQNKQFLPHLKTLISH 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 705 MN-DPTRLGLEVLESEQIKDYGRMIEVCDHFRALGARIIVDDFGSGYSNID---EIIKLEPQIIKLDGSLIRNIDKDQKQ 780
Cdd:PRK11829 518 YHiDPQQLLLEITETAQIQDLDEALRLLRELQGLGLLIALDDFGIGYSSLRylnHLKSLPIHMIKLDKSFVKNLPEDDAI 597
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2282447070 781 RNIASQlvrLCQVFNAQTVAEFVHNQQVCEIAEQMGVDYLQGYYFGEP 828
Cdd:PRK11829 598 ARIISC---VSDVLKVRVMAEGVETEEQRQWLLEHGIQCGQGFLFSPP 642
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
406-828 |
1.49e-27 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 119.49 E-value: 1.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 406 QQARRLTesyRIDSRTGLPNRIVLKERLNTILFSEHLLT---LKLTNFHQVNEKYGYQVGDQLLLDLSNHFVERLHlsvA 482
Cdd:PRK11359 370 QHIEQLI---QFDPLTGLPNRNNLHNYLDDLVDKAVSPVvylIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLK---P 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 483 KESQVKVElfsigvGEWAIIFNANVGCDKIEQrfveFADDIEHINFEPYGLADiDYLSVSLCGGFA----SRCDFLTDNG 558
Cdd:PRK11359 444 DQYLCRIE------GTQFVLVSLENDVSNITQ----IADELRNVVSKPIMIDD-KPFPLTLSIGISydvgKNRDYLLSTA 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 559 DeillKAIEARRYGVRNNTHITNAKDIQVSEEdrKEQLGwlSCVSRAILDQNIITYSQPIVASGTHEMIGQECLVRIMES 638
Cdd:PRK11359 513 H----NAMDYIRKNGGNGWQFFSPAMNEMVKE--RLVLG--AALKEAISNNQLKLVYQPQIFAETGELYGIEALARWHDP 584
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 639 DGTIVPPGKFLPIIADTHLYTRLSRHMIKNTIGYMADKQS------PFSINLSPQDLLSDKTLEVLETAISAMNDP-TRL 711
Cdd:PRK11359 585 LHGHVPPSRFIPLAEEIGEIENIGRWVIAEACRQLAEWRSqnihipALSVNLSALHFRSNQLPNQVSDAMQAWGIDgHQL 664
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 712 GLEVLESEQIKDYGRMIEVCDHFRALGARIIVDDFGSGYSNIDEIIKLEPQIIKLDGSLIRNIDKDQKQRNIASQLVRLC 791
Cdd:PRK11359 665 TVEITESMMMEHDTEIFKRIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIG 744
|
410 420 430
....*....|....*....|....*....|....*..
gi 2282447070 792 QVFNAQTVAEFVHNQQVCEIAEQMGVDYLQGYYFGEP 828
Cdd:PRK11359 745 QSLNLTVVAEGVETKEQFEMLRKIHCRVIQGYFFSRP 781
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
409-831 |
3.62e-24 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 109.38 E-value: 3.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 409 RRLTESYRIDSRTGLPNRIVLKERLNTILFSEH-------LLTLKLTNFHQVNEKYGYQVGDQLLLDLSnhfveRLHLSV 481
Cdd:PRK09776 659 RQLSYSASHDALTHLANRASFEKQLRRLLQTVNsthqrhaLVFIDLDRFKAVNDSAGHAAGDALLRELA-----SLMLSM 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 482 AKESQVkveLFSIGVGEWAIIFnanVGCDKIEQRFVEfADDIEHINFEPY-------------GLADIDyLSVSLCGGFA 548
Cdd:PRK09776 734 LRSSDV---LARLGGDEFGLLL---PDCNVESARFIA-TRIISAINDYHFpwegrvyrvgasaGITLID-ANNHQASEVM 805
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 549 SRCDFltdngdeillkAIEARRYGVRNNTHI--TNAKDIQVSEEDRKEQLGWlscvsRAILDQNII-TYSQPIVASGTHE 625
Cdd:PRK09776 806 SQADI-----------ACYAAKNAGRGRVTVyePQQAAAHSEHRALSLAEQW-----RMIKENQLMmLAHGVASPRIPEA 869
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 626 MIGQECLVRIMESDGTIVPPGKFLPIIADTHLYTRLSRHMIKNT-IGY---MADKQSPFSINLSPQDLLSDKTLEVLETA 701
Cdd:PRK09776 870 RNHWLISLRLWDPEGEIIDEGAFRPAAEDPALMHALDRRVIHEFfRQAakaVASKGLSIALPLSVAGLSSPTLLPFLLEQ 949
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 702 ISA-MNDPTRLGLEVLESEQIKDYGRMIEVCDHFRALGARIIVDDFGSGYSNIDEIIKLEPQIIKLDGSLIRNIDKDQKQ 780
Cdd:PRK09776 950 LENsPLPPRLLHLEITETALLNHAESASRLVQKLRLAGCRVVLSDFGRGLSSFNYLKAFMADYLKLDGELVANLHGNLMD 1029
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2282447070 781 RNIASQLVRLCQVFNAQTVAEFVHNQQVCEIAEQMGVDYLQGYYFGEPKRL 831
Cdd:PRK09776 1030 EMLISIIQGHAQRLGMKTIAGPVELPLVLDTLSGIGVDLAYGYAIARPQPL 1080
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
303-828 |
6.01e-21 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 98.25 E-value: 6.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 303 SVIIYNCVSRLEfidskleLKPFEGIVNacgaycmgELyrND-DRQEILHHSLTYIAMRESDEINEfrcedfqrdstvsp 381
Cdd:PRK13561 160 TVAISWCINRLI-------VHPLRNIAR--------EL--NDiPPQELVGHQLALPRLHQDDEIGM-------------- 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 382 llnLVRNAvadldSMNTQMEKKLHQQARRLTESYRIdsrTGLPNRIVLKERLNTILFSEHLLTLKLTNFHQVNEKYGYQV 461
Cdd:PRK13561 209 ---LVRSY-----NLNQQLLQRQYEEQSRNATRFPV---SDLPNKALLMALLEQVVARKQTTALMIITCETLRDTAGVLK 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 462 GDQ---LLLDLsnhfVERL------HLSVAKESQVKVELFSIGVGE-W-AIIFNANVgCDKIEQRFvefadDIEHINFEP 530
Cdd:PRK13561 278 EAQreiLLLTL----VEKLksvlspRMVLAQISGYDFAIIANGVKEpWhAITLGQQV-LTIINERL-----PIQRIQLRP 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 531 ygladidylSVSLcgGFASrcdFLTDNGDEILLK-----AIEARRYGV------------RNNTHITNAKDIQVSEEDRK 593
Cdd:PRK13561 348 ---------SCSI--GIAM---FYGDLTAEQLYSraisaAFTARRKGKnqiqffdpqqmeAAQKRLTEESDILNALENHQ 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 594 EQLgWLscvsraildqniitysQPIVASGTHEMIGQECLVRIMESDGTIVPPGKFLPIIADTHLYTRLSRHMIKNTIGYM 673
Cdd:PRK13561 414 FAI-WL----------------QPQVEMRSGKLVSAEALLRMQQPDGSWDLPEGLIDRIESCGLMVTVGHWVLEESCRLL 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 674 ADKQS-----PFSINLSPQDLLSDKTLEVLETAISAMN-DPTRLGLEVLESEQIKDYGRMIEVCDHFRALGARIIVDDFG 747
Cdd:PRK13561 477 AAWQErgimlPLSVNLSALQLMHPNMVADMLELLTRYRiQPGTLILEVTESRRIDDPHAAVAILRPLRNAGVRVALDDFG 556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 748 SGYSNIDEIIK---LEPQIIKLDGSLIRNIDKDQKQRNIASQLVRlcqVFNAQTVAEFVHNQQVCEIAEQMGVDYLQGYY 824
Cdd:PRK13561 557 MGYAGLRQLQHmksLPIDVLKIDKMFVDGLPEDDSMVAAIIMLAQ---SLNLQVIAEGVETEAQRDWLLKAGVGIAQGFL 633
|
....
gi 2282447070 825 FGEP 828
Cdd:PRK13561 634 FARA 637
|
|
| FIST |
smart00897 |
FIST N domain; The FIST N domain is a novel sensory domain, which is present in signal ... |
30-215 |
5.18e-19 |
|
FIST N domain; The FIST N domain is a novel sensory domain, which is present in signal transduction proteins from Bacteria, Archaea and Eukarya. Chromosomal proximity of FIST-encoding genes to those coding for proteins involved in amino acid metabolism and transport suggest that FIST domains bind small ligands, such as amino acids.
Pssm-ID: 214894 Cd Length: 196 Bit Score: 85.83 E-value: 5.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 30 LIQLFSAQSSDVARRIASVALNRLSNAT-LIGQSARHVICDN---CLESSCtLIIISEFNETRLTSAVQP-FTGNPNQDS 104
Cdd:smart00897 3 LLVLFFSSPAYDAEALLAALRERFPGATpIVGCSTAGEITTGvvqEFEDEP-ALSVMLFELPLVSFDVFSlVDPLPDLVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 105 QELASQLDLS---KDAKTVISLCDQVEGRDYPIYSAF-ENLPYTLPVAGGLCHENE--YGRWVMHNEQTYQHAcVAVALT 178
Cdd:smart00897 82 GLLLAALLAAidpRNTFALLLLDDLSSSNEEELLEGLdEALPEGIPIGGGSAGDNLrfQETYVFTNGRVHSGA-VVVAFG 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 2282447070 179 nPRLKVWSDAYSEWNPIGMKLRVTHAVGNRLYALNDK 215
Cdd:smart00897 161 -GGLRFGTGVTQGWRPIGPPFVVTKAEGNVVYELDGE 196
|
|
| FIST_C |
pfam10442 |
FIST C domain; The FIST C domain is a novel sensory domain, which is present in signal ... |
217-342 |
1.19e-16 |
|
FIST C domain; The FIST C domain is a novel sensory domain, which is present in signal transduction proteins from Bacteria, Archaea and Eukarya. Chromosomal proximity of FIST-encoding genes to those coding for proteins involved in amino acid metabolism and transport suggest that FIST domains bind small ligands, such as amino acids.
Pssm-ID: 463094 Cd Length: 135 Bit Score: 77.35 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 217 AIDVFKHYL--ADGKDLPFSqLMSFPLyrelGRKKG-----ISTPLRIN-DDGSIEFDSPWHVGEEAQFCYNHPSLTAEK 288
Cdd:pfam10442 1 ALEVYKEYLggEEDEELPAS-ALEFPL----GVVVGggdylVRSPLGVDpEDGSLAFAGDVPEGSVVQLMLRDADDLIEA 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 289 VRHGAEMLAMHQPESVIIYNCVSRLEFIDSKL--ELKPFE----GIVNACGAYCMGELYR 342
Cdd:pfam10442 76 AERAAEAALANPPEGALLFSCAGRGLGLGERFdeELEAIRealgDGVPLAGFYTYGEIGP 135
|
|
| FIST |
pfam08495 |
FIST N domain; The FIST N domain is a novel sensory domain, which is present in signal ... |
134-215 |
4.15e-16 |
|
FIST N domain; The FIST N domain is a novel sensory domain, which is present in signal transduction proteins from Bacteria, Archaea and Eukarya. Chromosomal proximity of FIST-encoding genes to those coding for proteins involved in amino acid metabolism and transport suggest that FIST domains bind small ligands, such as amino acids.
Pssm-ID: 462495 Cd Length: 126 Bit Score: 75.31 E-value: 4.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 134 IYSAFENLpyTLPVAGGLCHENEYGR--WVMHNEQTYQHACVAVALTNPRLKVWSDAYSEWNPIGMKLRVTHAVGNRLYA 211
Cdd:pfam08495 45 LDSALGYP--GVPVVGGLAGDGLRFErtWVLFNGEVYSDGAVAVALYGDALKVGVGVSQGWRPIGPPFVVTKADGNRVYE 122
|
....
gi 2282447070 212 LNDK 215
Cdd:pfam08495 123 LDGR 126
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
418-831 |
5.61e-14 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 75.67 E-value: 5.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 418 DSRTGLPNRIVLKERLNTIL-----FSEH--LLTLKLTNFHQVNEKYGYQVGDQLLLDLSN---HFVERLHLSvakesqv 487
Cdd:PRK11059 231 DAKTGLGNRLFFDNQLATLLedqemVGAHgvVMLIRLPDFDLLQEEWGESQVEELLFELINllsTFVMRYPGA------- 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 488 kveLFSigvgewaiifnanvgcdkieQRF-VEFADDIEHInfepyGLADIDylsvslcgGFASRcdfltdngdeiLLKAI 566
Cdd:PRK11059 304 ---LLA--------------------RYSrSDFAVLLPHR-----SLKEAD--------SLASQ-----------LLKAV 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 567 EARrygvrNNTHITNAKD---IQVS---EEDRKEQL-----------------GWL-------------SCVSRAILDQ- 609
Cdd:PRK11059 337 DAL-----PPPKMLDRDDflhIGICayrSGQSTEQVmeeaemalrsaqlqggnGWFvydkaqlpekgrgSVRWRTLLEQt 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 610 ----NIITYSQPIVASGTHEMiGQECLVRIMESDGTIVPPGKFLPIIADTHLYTRLSRHMIKNTIGYMADKQS-PFSINL 684
Cdd:PRK11059 412 lvrgGPRLYQQPAVTRDGKVH-HRELFCRIRDGQGELLSAELFMPMVQQLGLSEQYDRQVIERVLPLLRYWPEeNLSINL 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 685 SPQDLLSD------KTlEVLETAISamnDPTRLGLEVLESEQIKDYGRMIEVCDHFRALGARIIVDDFG-----SGYsni 753
Cdd:PRK11059 491 SVDSLLSRafqrwlRD-TLLQCPRS---QRKRLIFELAEADVCQHISRLRPVLRMLRGLGCRLAVDQAGltvvsTSY--- 563
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2282447070 754 deiIK-LEPQIIKLDGSLIRNIDKDQKQRNIASQLVRLCQVFNAQTVAEFVHNQQVCEIAEQMGVDYLQGYYFGEPKRL 831
Cdd:PRK11059 564 ---IKeLNVELIKLHPSLVRNIHKRTENQLFVRSLVGACAGTETQVFATGVESREEWQTLQELGVSGGQGDFFAESQPL 639
|
|
| YuxH |
COG3434 |
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ... |
682-828 |
1.17e-12 |
|
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction mechanisms];
Pssm-ID: 442660 [Multi-domain] Cd Length: 407 Bit Score: 70.60 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 682 INLSPQDLLSDkTLEVLetaisamnDPTRLGLEVLESEQIKDygRMIEVCDHFRALGARIIVDDF--GSGYSNIDEIIkl 759
Cdd:COG3434 66 INFTEELLLSD-LPELL--------PPERVVLEILEDVEPDE--ELLEALKELKEKGYRIALDDFvlDPEWDPLLPLA-- 132
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2282447070 760 epQIIKLDgslIRNIDKDQkqrniASQLVRLCQVFNAQTVAEFVHNQQVCEIAEQMGVDYLQGYYFGEP 828
Cdd:COG3434 133 --DIIKID---VLALDLEE-----LAELVARLKRYGIKLLAEKVETREEFELCKELGFDLFQGYFFSKP 191
|
|
| PRK10551 |
PRK10551 |
cyclic di-GMP phosphodiesterase; |
616-831 |
1.51e-11 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 182541 [Multi-domain] Cd Length: 518 Bit Score: 67.71 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 616 QPIVASGTHEMIGQECLVRIMESDGTIVPPGKFLPIIADTHLYTRLSRHMIKNTI--GYMADKQSP----FSINLSPQDL 689
Cdd:PRK10551 282 QPVVDTQTLRVTGLEALLRWRHPTAGEIPPDAFINYAEAQKLIVPLTQHLFELIArdAAELQKVLPvgakLGINISPAHL 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 690 LSDKTLEVLETAISAMN-DPTRLGLEVLESEQIKDYgRMIEVCDHFRALGARIIVDDFGSGYSnidEIIKLEP---QIIK 765
Cdd:PRK10551 362 HSDSFKADVQRLLASLPaDHFQIVLEITERDMVQEE-EATKLFAWLHSQGIEIAIDDFGTGHS---ALIYLERftlDYLK 437
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2282447070 766 LDGSLIRNIDKDQKQRNIASQLVRLCQVFNAQTVAEFVHNQQVCEIAEQMGVDYLQGYYFGEPKRL 831
Cdd:PRK10551 438 IDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRERGVNFLQGYWISRPLPL 503
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
346-568 |
3.67e-08 |
|
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: 55.75 E-value: 3.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 346 RQEILHHSLTYIAMRESDEINEFRCEDFQRDSTVSPLLNLVRNAVADLDSMNtQMEKKLHQQARRltesyriDSRTGLPN 425
Cdd:COG2199 53 LLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLLLLLALEDITELR-RLEERLRRLATH-------DPLTGLPN 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 426 RIVLKERLNTILFSEH-------LLTLKLTNFHQVNEKYGYQVGDQLLLdlsnHFVERLHLSVAKESQVkvelFSIGVGE 498
Cdd:COG2199 125 RRAFEERLERELARARregrplaLLLIDLDHFKRINDTYGHAAGDEVLK----EVARRLRASLRESDLV----ARLGGDE 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2282447070 499 WAIIFnanVGCDkiEQRFVEFADDI-EHINFEPYGLADIDyLSVSLCGGFASRCDFlTDNGDEILLKAIEA 568
Cdd:COG2199 197 FAVLL---PGTD--LEEAEALAERLrEALEQLPFELEGKE-LRVTVSIGVALYPED-GDSAEELLRRADLA 260
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
416-568 |
8.41e-08 |
|
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: 52.56 E-value: 8.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 416 RIDSRTGLPNRIVLKERLNTIL---------FSehLLTLKLTNFHQVNEKYGYQVGDQLLLdlsnHFVERLHLSVAKESQ 486
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLararrsgrpLA--LLLIDIDHFKQINDTYGHAAGDEVLK----EVAERLRSSLRESDL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 487 VkvelFSIGVGEWAIIFNanvGCDkiEQRFVEFADDI-EHINFEPYGLADIDYLSVSLcgGFASrCDFLTDNGDEILLKA 565
Cdd:cd01949 75 V----ARLGGDEFAILLP---GTD--LEEAEALAERLrEAIEEPFFIDGQEIRVTASI--GIAT-YPEDGEDAEELLRRA 142
|
...
gi 2282447070 566 IEA 568
Cdd:cd01949 143 DEA 145
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
417-466 |
8.58e-06 |
|
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: 46.48 E-value: 8.58e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2282447070 417 IDSRTGLPNRIVLKERLNT---ILFSEH----LLTLKLTNFHQVNEKYGYQVGDQLL 466
Cdd:pfam00990 3 HDPLTGLPNRRYFEEQLEQelqRALREGspvaVLLIDLDNFKRINDTYGHSVGDEVL 59
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
416-471 |
6.04e-05 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 44.16 E-value: 6.04e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2282447070 416 RIDSRTGLPNRIVLKERLNTILFSEH-------LLTLKLTNFHQVNEKYGYQVGDQLLLDLSN 471
Cdd:smart00267 4 FRDPLTGLPNRRYFEEELEQELQRAQrqgspfaLLLIDLDNFKDINDTYGHAVGDELLQEVAQ 66
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
417-484 |
1.55e-04 |
|
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: 43.09 E-value: 1.55e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2282447070 417 IDSRTGLPNRIVLKERLN---------TILFSehLLTLKLTNFHQVNEKYGYQVGDQLLldlsNHFVERLHLSVAKE 484
Cdd:TIGR00254 4 RDPLTGLYNRRYLEEMLDselkrarrfQRSFS--VLMIDIDNFKKINDTLGHDVGDEVL----REVARILQSSVRGS 74
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
392-475 |
5.28e-04 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 43.46 E-value: 5.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282447070 392 DLDSMNTQMEK-KLHQQAR--RLTESYRIDSRTGLPNRIVLKERLNTIL------FSEHLLTLKLTNFHQVNEKYGYQVG 462
Cdd:PRK09966 222 DFNSLLDEMEEwQLRLQAKnaQLLRTALHDPLTGLANRAAFRSGINTLMnnsdarKTSALLFLDGDNFKYINDTWGHATG 301
|
90
....*....|...
gi 2282447070 463 DQLLLDLSNHFVE 475
Cdd:PRK09966 302 DRVLIEIAKRLAE 314
|
|
| |
