|
Name |
Accession |
Description |
Interval |
E-value |
| ODP |
pfam19583 |
ODP family beta lactamase; The ODP (Oxygen-binding Di-iron Protein) domain is a distinct ... |
27-217 |
1.54e-79 |
|
ODP family beta lactamase; The ODP (Oxygen-binding Di-iron Protein) domain is a distinct member of the metallo-beta-lactamase superfamily recruited to various bacterial and archaeal signal transduction pathways, including chemotaxis, to function as oxygen and iron sensors (1). ODP was shown to act as a sensor for chemotactic responses to both iron and oxygen in the human pathogen Treponema denticola (Td). The ODP di-iron site binds oxygen at high affinity to reversibly form an unusually stable peroxo adduct.
Pssm-ID: 437415 Cd Length: 194 Bit Score: 248.55 E-value: 1.54e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 27 FQCHVYLILNGKGSILIDPGSKITFKYALEKIEQIIPFSYIKYFICQHQDPDITASLEIIRDLLirDDAVIVSHWRAIAL 106
Cdd:pfam19583 1 VQCNQYLIVDGGEAVLIDPGGRLTFPAVLAKVSKYIDPEKIKYIFASHQDPDICSSLPLWLDVI--PDAKIVISELWERF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 107 LKHYNLN-IPMICVEKENWKLNAG-GRELEFIFTPYCHFPGAFCTYDKKSKVLFSSDLFGGFT--DRFKLFAEDIN-YFD 181
Cdd:pfam19583 79 LPHYGLKkSRFIPIPDEGGRITLGsGRRLEFIPAHFLHSPGNFVTYDPVSKILFSGDIGAALFpgKDWSLFVEDFDaHIP 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 290753359 182 SIAAFHEPYMPSKEILVHSLKKIEQYDIDLIAPQHG 217
Cdd:pfam19583 159 YMEGFHRRYMPSNKALRLWVEMVRKLDIEMIAPQHG 194
|
|
| flavodiiron_proteins_MBL-fold |
cd07709 |
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ... |
9-235 |
1.04e-61 |
|
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold metallo-hydrolase domain; FDPs catalyze the reduction of oxygen and/or nitric oxide to water or nitrous oxide respectively. In addition to this N-terminal catalytic domain they contain a C-terminal flavin mononucleotide-binding flavodoxin-like domain. Although some FDPs are able to reduce NO or O2 with similar catalytic efficiencies others are selective for either NO or O2, such as Escherichia coli flavorubredoxin which is selective toward NO and G. intestinalis FDP which is selective toward O2. These enzymes belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. Some members of this subgroup are single domain.
Pssm-ID: 293795 [Multi-domain] Cd Length: 238 Bit Score: 203.49 E-value: 1.04e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 9 VEIAEDIFWVGHELPD-----------DPFQCHVYLILNGKGsILIDPGSKITFKYALEKIEQIIPFSYIKYFICQHQDP 77
Cdd:cd07709 1 VEIADDIYWVGVNDWDlrlfegeyptpRGTSYNSYLIKDEKT-ALIDTVKEPFFDEFLENLEEVIDPRKIDYIVVNHQEP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 78 DITASLEIIrdLLIRDDAVIVSHWRAIALLKHY--NLNIPMICVeKENWKLNAGGRELEFIFTPYCHFPGAFCTYDKKSK 155
Cdd:cd07709 80 DHSGSLPEL--LELAPNAKIVCSKKAARFLKHFypGIDERFVVV-KDGDTLDLGKHTLKFIPAPMLHWPDTMVTYDPEDK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 156 VLFSSDLFGGFTDRFKLFAEDI-NYFDSIAAFHEPYM-PSKEILVHSLKKIEQYDIDLIAPQHGSIIRRDlIKPIINKMK 233
Cdd:cd07709 157 ILFSGDAFGAHGASGELFDDEVeDYLEEARRYYANIMgPFSKQVRKALEKLEALDIKMIAPSHGPIWRKD-PGEIIDLYR 235
|
..
gi 290753359 234 NL 235
Cdd:cd07709 236 DW 237
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
340-570 |
3.17e-54 |
|
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: 185.18 E-value: 3.17e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 340 YLYVRNVLYIPIPEIESDKIIAVMKLYLKESIVIDNDILEILKEVINFLSIAFEREFIRRKLIEEREKFYEISIHDTLTG 419
Cdd:COG2199 42 LLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLLLLLALEDITELRRLEERLRRLATHDPLTG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 420 CYSRYYLKETIKRVLAIHDRGEiRNVGIVMLDIDDFKNINDTYGHDVGDEVLKVIADIIKNEVRVGDIPVRYGGEEFMIV 499
Cdd:COG2199 122 LPNRRAFEERLERELARARREG-RPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVL 200
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 290753359 500 AVVNDIKSVYMVAERIRTKLEEYKWDAPLDKERITASFGVV-LRKKGESFEDVIKRVDINLYKAKSAGKNTV 570
Cdd:COG2199 201 LPGTDLEEAEALAERLREALEQLPFELEGKELRVTVSIGVAlYPEDGDSAEELLRRADLALYRAKRAGRNRV 272
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
414-571 |
1.09e-52 |
|
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: 176.98 E-value: 1.09e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 414 HDTLTGCYSRYYLKETIKRVLAIHDRGEiRNVGIVMLDIDDFKNINDTYGHDVGDEVLKVIADIIKNEVRVGDIPVRYGG 493
Cdd:cd01949 2 TDPLTGLPNRRAFEERLERLLARARRSG-RPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 290753359 494 EEFMIVAVVNDIKSVYMVAERIRTKLEEYKWDAPLDKeRITASFGVVL-RKKGESFEDVIKRVDINLYKAKSAGKNTVI 571
Cdd:cd01949 81 DEFAILLPGTDLEEAEALAERLREAIEEPFFIDGQEI-RVTASIGIATyPEDGEDAEELLRRADEALYRAKRSGRNRVV 158
|
|
| NorV |
COG0426 |
Flavorubredoxin [Energy production and conversion]; |
8-235 |
1.33e-49 |
|
Flavorubredoxin [Energy production and conversion];
Pssm-ID: 440195 [Multi-domain] Cd Length: 390 Bit Score: 176.18 E-value: 1.33e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 8 PVEIAEDIFWVG---------HELPDDP--FQCHVYLILNGKGsILIDPGSKITFKYALEKIEQIIPFSYIKYFICQHQD 76
Cdd:COG0426 2 AVEIAHGVYWVGvldwdrrlfEGEYPTPrgTTYNSYLIVDEKT-ALIDTVGESFFEEFLENLSKVIDPKKIDYIIVNHQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 77 PDITASLEIIrdLLIRDDAVIVSHWRAIALLKHYnLNIP---MICVeKENWKLNAGGRELEFIFTPYCHFPGAFCTYDKK 153
Cdd:COG0426 81 PDHSGSLPEL--LELAPNAKIVCSKKAARFLPHF-YGIPdfrFIVV-KEGDTLDLGGHTLQFIPAPMLHWPDTMFTYDPE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 154 SKVLFSSDLFGGFTDRFKLFAEDIN---YFDSIAAFHEPYMPSKEILVHSLKKIEQYDIDLIAPQHGSIIRRDLIKpIIN 230
Cdd:COG0426 157 DKILFSGDAFGSHGASDELFDDEVDehlEEEARRYYANIMMPFSKQVLKALKKVRGLDIDMIAPSHGPIWRGNPKE-ILD 235
|
....*
gi 290753359 231 KMKNL 235
Cdd:COG0426 236 WYRKW 240
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
412-568 |
2.10e-46 |
|
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: 160.11 E-value: 2.10e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 412 SIHDTLTGCYSRYYLKETIKRVLAIHDRgEIRNVGIVMLDIDDFKNINDTYGHDVGDEVLKVIADIIKNEVRVGDIPVRY 491
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRALR-EGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 492 GGEEFMIVAVVNDIKSVYMVAERIRTKLEEYK--WDAPLDKERITASFGVVL-RKKGESFEDVIKRVDINLYKAKSAGKN 568
Cdd:pfam00990 80 GGDEFAILLPETSLEGAQELAERIRRLLAKLKipHTVSGLPLYVTISIGIAAyPNDGEDPEDLLKRADTALYQAKQAGRN 159
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
410-571 |
5.27e-45 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 165.46 E-value: 5.27e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 410 EISIHDTLTGCYSRYY----LKETIKRVLAihdRGeiRNVGIVMLDIDDFKNINDTYGHDVGDEVLKVIADIIKNEVRVG 485
Cdd:PRK09581 290 EMAVTDGLTGLHNRRYfdmhLKNLIERANE---RG--KPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGT 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 486 DIPVRYGGEEFMIVAVVNDIKSVYMVAERIRTKLEEYKWDAPLDKERI--TASFGVV-LRKKGESFEDVIKRVDINLYKA 562
Cdd:PRK09581 365 DLIARYGGEEFVVVMPDTDIEDAIAVAERIRRKIAEEPFIISDGKERLnvTVSIGVAeLRPSGDTIEALIKRADKALYEA 444
|
....*....
gi 290753359 563 KSAGKNTVI 571
Cdd:PRK09581 445 KNTGRNRVV 453
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
412-570 |
2.22e-43 |
|
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: 152.11 E-value: 2.22e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 412 SIHDTLTGCYSRYYLKETIKRVLAIHDRGEiRNVGIVMLDIDDFKNINDTYGHDVGDEVLKVIADIIKNEVRVGDIPVRY 491
Cdd:TIGR00254 2 AVRDPLTGLYNRRYLEEMLDSELKRARRFQ-RSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 492 GGEEFMIVAVVNDIKSVYMVAERIRTKLE-EYKWDAPLDKERITASFGVV-LRKKGESFEDVIKRVDINLYKAKSAGKNT 569
Cdd:TIGR00254 81 GGEEFVVILPGTPLEDALSKAERLRDAINsKPIEVAGSETLTVTVSIGVAcYPGHGLTLEELLKRADEALYQAKKAGRNR 160
|
.
gi 290753359 570 V 570
Cdd:TIGR00254 161 V 161
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
410-570 |
7.57e-42 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 148.16 E-value: 7.57e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 410 EISIHDTLTGCYSRYYLKETIKRVLAIHDRGEIRnVGIVMLDIDDFKNINDTYGHDVGDEVLKVIADIIKNEVRVGDIPV 489
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSP-FALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 490 RYGGEEFMIVAVVNDIKSVYMVAERIRTKLEEYkWDAPLDKERITASFGVVL-RKKGESFEDVIKRVDINLYKAKSAGKN 568
Cdd:smart00267 80 RLGGDEFALLLPETSLEEAIALAERILQQLREP-IIIHGIPLYLTISIGVAAyPNPGEDAEDLLKRADTALYQAKKAGRN 158
|
..
gi 290753359 569 TV 570
Cdd:smart00267 159 QV 160
|
|
| diguan_SiaD |
NF038266 |
biofilm regulation diguanylate cyclase SiaD; |
399-570 |
1.43e-38 |
|
biofilm regulation diguanylate cyclase SiaD;
Pssm-ID: 468439 [Multi-domain] Cd Length: 252 Bit Score: 142.04 E-value: 1.43e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 399 RKLIEEREKFYEISIHDTLTGCYSRYYLKETIKRVLAIHDRGEiRNVGIVMLDIDDFKNINDTYGHDVGDEVLKVIADII 478
Cdd:NF038266 81 RMMRDLNEALREASTRDPLTGLPNRRLLMERLREEVERARRSG-RPFTLAMLDVDHFKRINDRYGHEVGDRVLVEIARTL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 479 KNEVRVGDIPVRYGGEEFMIVAVVNDIKSVYMVAERIRTKLEEYKWDAPLDKERITASFGVV-LRKKGESFEDVIKRVDI 557
Cdd:NF038266 160 RAELREYDLCGRWGGEEFLLLLPETGLEEAQVVLERLREAVRALAVRVGDDVLSVTASAGLAeHRPPEEGLSATLSRADQ 239
|
170
....*....|...
gi 290753359 558 NLYKAKSAGKNTV 570
Cdd:NF038266 240 ALYQAKRAGRDRV 252
|
|
| dguan_cyc_DgcA |
NF041606 |
diguanylate cyclase DgcA; |
444-570 |
2.76e-28 |
|
diguanylate cyclase DgcA;
Pssm-ID: 469490 [Multi-domain] Cd Length: 340 Bit Score: 115.62 E-value: 2.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 444 NVGIVMLDIDDFKNINDTYGHDVGDEVLKVIADIIKNEVRVGDIPVRYGGEEFMIVAVVNDIKSVYMVAERIRTKLEEYk 523
Cdd:NF041606 209 PLSILMLDIDFFKQINDTYGHACGDLVLQMVASIIQSCTRTQDMAARYGGEEFVVMLSNTSSKTAKKIAERIRKSIENL- 287
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 290753359 524 wDAPLDKE--RITASFGVV-LRKKGESFEDVIKRVDINLYKAKSAGKNTV 570
Cdd:NF041606 288 -SILYDEQhiRVTISIGVAeYNFDVESAKSLVERADKALYESKQNGRNRV 336
|
|
| Lactamase_B |
smart00849 |
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ... |
30-216 |
2.13e-15 |
|
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins contain this domain. These proteins include thiolesterases, members of the glyoxalase II family, that catalyse the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid and a competence protein that is essential for natural transformation in Neisseria gonorrhoeae and could be a transporter involved in DNA uptake. Except for the competence protein these proteins bind two zinc ions per molecule as cofactor.
Pssm-ID: 214854 [Multi-domain] Cd Length: 177 Bit Score: 74.51 E-value: 2.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 30 HVYLILNGKGSILIDPGSKITFKYaLEKIEQIIPFSyIKYFICQHQDPDITASLEIIRDLLirdDAVIVSHWRAIALLKH 109
Cdd:smart00849 1 NSYLVRDDGGAILIDTGPGEAEDL-LAELKKLGPKK-IDAIILTHGHPDHIGGLPELLEAP---GAPVYAPEGTAELLKD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 110 YNLNIPMICVEKENW----------KLNAGGRELEFIFTPyCHFPGAFCTYDKKSKVLFSSDLFGGFTDRFKLFaediny 179
Cdd:smart00849 76 LLALLGELGAEAEPAppdrtlkdgdELDLGGGELEVIHTP-GHTPGSIVLYLPEGKILFTGDLLFAGGDGRTLV------ 148
|
170 180 190
....*....|....*....|....*....|....*..
gi 290753359 180 fdsiaafhEPYMPSKEILVHSLKKIEQYDIDLIAPQH 216
Cdd:smart00849 149 --------DGGDAAASDALESLLKLLKLLPKLVVPGH 177
|
|
| PRK11921 |
PRK11921 |
anaerobic nitric oxide reductase flavorubredoxin; |
9-231 |
2.60e-12 |
|
anaerobic nitric oxide reductase flavorubredoxin;
Pssm-ID: 237023 [Multi-domain] Cd Length: 394 Bit Score: 68.57 E-value: 2.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 9 VEIAEDIFWVGH---ELPD---DPFQCH------VYLILNGKgSILIDPGSKITFKYALEKIEQIIPFSYIKYFICQHQD 76
Cdd:PRK11921 1 FKINDNVTWVGKidwELRKfhgEEYSTHrgssynSYLIKDEK-TVLIDTVWQPFAKEFVENLKKEIDLDKIDYIVANHGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 77 PDITASL-EIIRdlLIRDDAVIVSHWRAIALLKHYNLNIPMICVeKENWKLNAGGRELEFIFTPYCHFPGAFCTYDKKSK 155
Cdd:PRK11921 80 IDHSGALpELMK--EIPDTPIYCTKNGAKSLKGHYHQDWNFVVV-KTGDRLEIGSNELIFIEAPMLHWPDSMFTYLTGDN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 156 VLFSSDLFG----------GFTDRFKLFAEDINYFDSIAAfhePYMPskeiLVhsLKKIEQY-----DIDLIAPQHGsII 220
Cdd:PRK11921 157 ILFSNDAFGqhyaselmynDLVDQGELYQEAIKYYANILT---PFSP----LV--IKKIEEIlslnlPVDMICPSHG-VI 226
|
250
....*....|.
gi 290753359 221 RRDLIKPIINK 231
Cdd:PRK11921 227 WRDNPLQIVEK 237
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ODP |
pfam19583 |
ODP family beta lactamase; The ODP (Oxygen-binding Di-iron Protein) domain is a distinct ... |
27-217 |
1.54e-79 |
|
ODP family beta lactamase; The ODP (Oxygen-binding Di-iron Protein) domain is a distinct member of the metallo-beta-lactamase superfamily recruited to various bacterial and archaeal signal transduction pathways, including chemotaxis, to function as oxygen and iron sensors (1). ODP was shown to act as a sensor for chemotactic responses to both iron and oxygen in the human pathogen Treponema denticola (Td). The ODP di-iron site binds oxygen at high affinity to reversibly form an unusually stable peroxo adduct.
Pssm-ID: 437415 Cd Length: 194 Bit Score: 248.55 E-value: 1.54e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 27 FQCHVYLILNGKGSILIDPGSKITFKYALEKIEQIIPFSYIKYFICQHQDPDITASLEIIRDLLirDDAVIVSHWRAIAL 106
Cdd:pfam19583 1 VQCNQYLIVDGGEAVLIDPGGRLTFPAVLAKVSKYIDPEKIKYIFASHQDPDICSSLPLWLDVI--PDAKIVISELWERF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 107 LKHYNLN-IPMICVEKENWKLNAG-GRELEFIFTPYCHFPGAFCTYDKKSKVLFSSDLFGGFT--DRFKLFAEDIN-YFD 181
Cdd:pfam19583 79 LPHYGLKkSRFIPIPDEGGRITLGsGRRLEFIPAHFLHSPGNFVTYDPVSKILFSGDIGAALFpgKDWSLFVEDFDaHIP 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 290753359 182 SIAAFHEPYMPSKEILVHSLKKIEQYDIDLIAPQHG 217
Cdd:pfam19583 159 YMEGFHRRYMPSNKALRLWVEMVRKLDIEMIAPQHG 194
|
|
| flavodiiron_proteins_MBL-fold |
cd07709 |
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ... |
9-235 |
1.04e-61 |
|
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold metallo-hydrolase domain; FDPs catalyze the reduction of oxygen and/or nitric oxide to water or nitrous oxide respectively. In addition to this N-terminal catalytic domain they contain a C-terminal flavin mononucleotide-binding flavodoxin-like domain. Although some FDPs are able to reduce NO or O2 with similar catalytic efficiencies others are selective for either NO or O2, such as Escherichia coli flavorubredoxin which is selective toward NO and G. intestinalis FDP which is selective toward O2. These enzymes belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. Some members of this subgroup are single domain.
Pssm-ID: 293795 [Multi-domain] Cd Length: 238 Bit Score: 203.49 E-value: 1.04e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 9 VEIAEDIFWVGHELPD-----------DPFQCHVYLILNGKGsILIDPGSKITFKYALEKIEQIIPFSYIKYFICQHQDP 77
Cdd:cd07709 1 VEIADDIYWVGVNDWDlrlfegeyptpRGTSYNSYLIKDEKT-ALIDTVKEPFFDEFLENLEEVIDPRKIDYIVVNHQEP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 78 DITASLEIIrdLLIRDDAVIVSHWRAIALLKHY--NLNIPMICVeKENWKLNAGGRELEFIFTPYCHFPGAFCTYDKKSK 155
Cdd:cd07709 80 DHSGSLPEL--LELAPNAKIVCSKKAARFLKHFypGIDERFVVV-KDGDTLDLGKHTLKFIPAPMLHWPDTMVTYDPEDK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 156 VLFSSDLFGGFTDRFKLFAEDI-NYFDSIAAFHEPYM-PSKEILVHSLKKIEQYDIDLIAPQHGSIIRRDlIKPIINKMK 233
Cdd:cd07709 157 ILFSGDAFGAHGASGELFDDEVeDYLEEARRYYANIMgPFSKQVRKALEKLEALDIKMIAPSHGPIWRKD-PGEIIDLYR 235
|
..
gi 290753359 234 NL 235
Cdd:cd07709 236 DW 237
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
340-570 |
3.17e-54 |
|
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: 185.18 E-value: 3.17e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 340 YLYVRNVLYIPIPEIESDKIIAVMKLYLKESIVIDNDILEILKEVINFLSIAFEREFIRRKLIEEREKFYEISIHDTLTG 419
Cdd:COG2199 42 LLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLLLLLALEDITELRRLEERLRRLATHDPLTG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 420 CYSRYYLKETIKRVLAIHDRGEiRNVGIVMLDIDDFKNINDTYGHDVGDEVLKVIADIIKNEVRVGDIPVRYGGEEFMIV 499
Cdd:COG2199 122 LPNRRAFEERLERELARARREG-RPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVL 200
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 290753359 500 AVVNDIKSVYMVAERIRTKLEEYKWDAPLDKERITASFGVV-LRKKGESFEDVIKRVDINLYKAKSAGKNTV 570
Cdd:COG2199 201 LPGTDLEEAEALAERLREALEQLPFELEGKELRVTVSIGVAlYPEDGDSAEELLRRADLALYRAKRAGRNRV 272
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
414-571 |
1.09e-52 |
|
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: 176.98 E-value: 1.09e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 414 HDTLTGCYSRYYLKETIKRVLAIHDRGEiRNVGIVMLDIDDFKNINDTYGHDVGDEVLKVIADIIKNEVRVGDIPVRYGG 493
Cdd:cd01949 2 TDPLTGLPNRRAFEERLERLLARARRSG-RPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 290753359 494 EEFMIVAVVNDIKSVYMVAERIRTKLEEYKWDAPLDKeRITASFGVVL-RKKGESFEDVIKRVDINLYKAKSAGKNTVI 571
Cdd:cd01949 81 DEFAILLPGTDLEEAEALAERLREAIEEPFFIDGQEI-RVTASIGIATyPEDGEDAEELLRRADEALYRAKRSGRNRVV 158
|
|
| NorV |
COG0426 |
Flavorubredoxin [Energy production and conversion]; |
8-235 |
1.33e-49 |
|
Flavorubredoxin [Energy production and conversion];
Pssm-ID: 440195 [Multi-domain] Cd Length: 390 Bit Score: 176.18 E-value: 1.33e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 8 PVEIAEDIFWVG---------HELPDDP--FQCHVYLILNGKGsILIDPGSKITFKYALEKIEQIIPFSYIKYFICQHQD 76
Cdd:COG0426 2 AVEIAHGVYWVGvldwdrrlfEGEYPTPrgTTYNSYLIVDEKT-ALIDTVGESFFEEFLENLSKVIDPKKIDYIIVNHQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 77 PDITASLEIIrdLLIRDDAVIVSHWRAIALLKHYnLNIP---MICVeKENWKLNAGGRELEFIFTPYCHFPGAFCTYDKK 153
Cdd:COG0426 81 PDHSGSLPEL--LELAPNAKIVCSKKAARFLPHF-YGIPdfrFIVV-KEGDTLDLGGHTLQFIPAPMLHWPDTMFTYDPE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 154 SKVLFSSDLFGGFTDRFKLFAEDIN---YFDSIAAFHEPYMPSKEILVHSLKKIEQYDIDLIAPQHGSIIRRDLIKpIIN 230
Cdd:COG0426 157 DKILFSGDAFGSHGASDELFDDEVDehlEEEARRYYANIMMPFSKQVLKALKKVRGLDIDMIAPSHGPIWRGNPKE-ILD 235
|
....*
gi 290753359 231 KMKNL 235
Cdd:COG0426 236 WYRKW 240
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
412-568 |
2.10e-46 |
|
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: 160.11 E-value: 2.10e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 412 SIHDTLTGCYSRYYLKETIKRVLAIHDRgEIRNVGIVMLDIDDFKNINDTYGHDVGDEVLKVIADIIKNEVRVGDIPVRY 491
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRALR-EGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 492 GGEEFMIVAVVNDIKSVYMVAERIRTKLEEYK--WDAPLDKERITASFGVVL-RKKGESFEDVIKRVDINLYKAKSAGKN 568
Cdd:pfam00990 80 GGDEFAILLPETSLEGAQELAERIRRLLAKLKipHTVSGLPLYVTISIGIAAyPNDGEDPEDLLKRADTALYQAKQAGRN 159
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
410-571 |
5.27e-45 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 165.46 E-value: 5.27e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 410 EISIHDTLTGCYSRYY----LKETIKRVLAihdRGeiRNVGIVMLDIDDFKNINDTYGHDVGDEVLKVIADIIKNEVRVG 485
Cdd:PRK09581 290 EMAVTDGLTGLHNRRYfdmhLKNLIERANE---RG--KPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGT 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 486 DIPVRYGGEEFMIVAVVNDIKSVYMVAERIRTKLEEYKWDAPLDKERI--TASFGVV-LRKKGESFEDVIKRVDINLYKA 562
Cdd:PRK09581 365 DLIARYGGEEFVVVMPDTDIEDAIAVAERIRRKIAEEPFIISDGKERLnvTVSIGVAeLRPSGDTIEALIKRADKALYEA 444
|
....*....
gi 290753359 563 KSAGKNTVI 571
Cdd:PRK09581 445 KNTGRNRVV 453
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
412-570 |
2.22e-43 |
|
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: 152.11 E-value: 2.22e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 412 SIHDTLTGCYSRYYLKETIKRVLAIHDRGEiRNVGIVMLDIDDFKNINDTYGHDVGDEVLKVIADIIKNEVRVGDIPVRY 491
Cdd:TIGR00254 2 AVRDPLTGLYNRRYLEEMLDSELKRARRFQ-RSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 492 GGEEFMIVAVVNDIKSVYMVAERIRTKLE-EYKWDAPLDKERITASFGVV-LRKKGESFEDVIKRVDINLYKAKSAGKNT 569
Cdd:TIGR00254 81 GGEEFVVILPGTPLEDALSKAERLRDAINsKPIEVAGSETLTVTVSIGVAcYPGHGLTLEELLKRADEALYQAKKAGRNR 160
|
.
gi 290753359 570 V 570
Cdd:TIGR00254 161 V 161
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
410-570 |
7.57e-42 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 148.16 E-value: 7.57e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 410 EISIHDTLTGCYSRYYLKETIKRVLAIHDRGEIRnVGIVMLDIDDFKNINDTYGHDVGDEVLKVIADIIKNEVRVGDIPV 489
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSP-FALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 490 RYGGEEFMIVAVVNDIKSVYMVAERIRTKLEEYkWDAPLDKERITASFGVVL-RKKGESFEDVIKRVDINLYKAKSAGKN 568
Cdd:smart00267 80 RLGGDEFALLLPETSLEEAIALAERILQQLREP-IIIHGIPLYLTISIGVAAyPNPGEDAEDLLKRADTALYQAKKAGRN 158
|
..
gi 290753359 569 TV 570
Cdd:smart00267 159 QV 160
|
|
| diguan_SiaD |
NF038266 |
biofilm regulation diguanylate cyclase SiaD; |
399-570 |
1.43e-38 |
|
biofilm regulation diguanylate cyclase SiaD;
Pssm-ID: 468439 [Multi-domain] Cd Length: 252 Bit Score: 142.04 E-value: 1.43e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 399 RKLIEEREKFYEISIHDTLTGCYSRYYLKETIKRVLAIHDRGEiRNVGIVMLDIDDFKNINDTYGHDVGDEVLKVIADII 478
Cdd:NF038266 81 RMMRDLNEALREASTRDPLTGLPNRRLLMERLREEVERARRSG-RPFTLAMLDVDHFKRINDRYGHEVGDRVLVEIARTL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 479 KNEVRVGDIPVRYGGEEFMIVAVVNDIKSVYMVAERIRTKLEEYKWDAPLDKERITASFGVV-LRKKGESFEDVIKRVDI 557
Cdd:NF038266 160 RAELREYDLCGRWGGEEFLLLLPETGLEEAQVVLERLREAVRALAVRVGDDVLSVTASAGLAeHRPPEEGLSATLSRADQ 239
|
170
....*....|...
gi 290753359 558 NLYKAKSAGKNTV 570
Cdd:NF038266 240 ALYQAKRAGRDRV 252
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
353-570 |
6.73e-38 |
|
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: 148.77 E-value: 6.73e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 353 EIESDKIIAVMKLYLKESIVIDNDILEILKEVINFLSIAFEREFIRRKLIEEREKFyeISIHDTLTGCYSRYYLKETIKR 432
Cdd:COG5001 194 LRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEERLRH--LAYHDPLTGLPNRRLFLDRLEQ 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 433 VLAIHDRGEiRNVGIVMLDIDDFKNINDTYGHDVGDEVLKVIADIIKNEVRVGDIPVRYGGEEFMIVAV-VNDIKSVYMV 511
Cdd:COG5001 272 ALARARRSG-RRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAVLLPdLDDPEDAEAV 350
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 290753359 512 AERIRTKLEE-YKWDaplDKE-RITASFGVVLR-KKGESFEDVIKRVDINLYKAKSAGKNTV 570
Cdd:COG5001 351 AERILAALAEpFELD---GHElYVSASIGIALYpDDGADAEELLRNADLAMYRAKAAGRNRY 409
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
415-571 |
1.61e-34 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 132.11 E-value: 1.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 415 DTLTGCYSRYYLKETIKRVLAihDRGEiRNVGIVMLDIDDFKNINDTYGHDVGDEVLKVIADIIKNEVRVGDIPVRYGGE 494
Cdd:PRK09894 132 DVLTGLPGRRVLDESFDHQLR--NREP-QNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYGGE 208
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 290753359 495 EFMIVAVVNDIKSVYMVAERIRTKLEEYKWDAPLDKERITASFGVVLRKKGESFEDVIKRVDINLYKAKSAGKNTVI 571
Cdd:PRK09894 209 EFIICLKAATDEEACRAGERIRQLIANHAITHSDGRINITATFGVSRAFPEETLDVVIGRADRAMYEGKQTGRNRVM 285
|
|
| dguan_cyc_DgcA |
NF041606 |
diguanylate cyclase DgcA; |
444-570 |
2.76e-28 |
|
diguanylate cyclase DgcA;
Pssm-ID: 469490 [Multi-domain] Cd Length: 340 Bit Score: 115.62 E-value: 2.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 444 NVGIVMLDIDDFKNINDTYGHDVGDEVLKVIADIIKNEVRVGDIPVRYGGEEFMIVAVVNDIKSVYMVAERIRTKLEEYk 523
Cdd:NF041606 209 PLSILMLDIDFFKQINDTYGHACGDLVLQMVASIIQSCTRTQDMAARYGGEEFVVMLSNTSSKTAKKIAERIRKSIENL- 287
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 290753359 524 wDAPLDKE--RITASFGVV-LRKKGESFEDVIKRVDINLYKAKSAGKNTV 570
Cdd:NF041606 288 -SILYDEQhiRVTISIGVAeYNFDVESAKSLVERADKALYESKQNGRNRV 336
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
414-574 |
1.31e-27 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 117.04 E-value: 1.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 414 HDTLTGCYSRYYLKETIKRVLAIHDRgEIRNVGIVMLDIDDFKNINDTYGHDVGDEVLKVIADIIKNEVRVGDIPVRYGG 493
Cdd:PRK15426 400 HDPLTRLYNRGALFEKARALAKRCQR-DQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRVGG 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 494 EEFMIVAVVNDIKSVYMVAERIRTKLEE----YKWDAPLdkeRITASFGVV-LRKKGE-SFEDVIKRVDINLYKAKSAGK 567
Cdd:PRK15426 479 EEFCVVLPGASLAEAAQVAERIRLRINEkeilVAKSTTI---RISASLGVSsAEEDGDyDFEQLQSLADRRLYLAKQAGR 555
|
....*..
gi 290753359 568 NTVICEE 574
Cdd:PRK15426 556 NRVCASD 562
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
400-568 |
1.13e-21 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 96.82 E-value: 1.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 400 KLIEEREKFYEISIHDTLTGCYSRYYLkETIKRVLAIHDRGEIRNVGIVMLDIDDFKNINDTYGHDVGDEVLKVIADIIK 479
Cdd:PRK10245 193 KLAEHKRRLQVMSTRDGMTGVYNRRHW-ETLLRNEFDNCRRHHRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQ 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 480 NEVRVGDIPVRYGGEEFMIVAVVNDIKSVYMVAERIRTKLEEYKWD-APLDKERItaSFGVV-LRKKGESFEDVIKRVDI 557
Cdd:PRK10245 272 ITLRGSDVIGRFGGDEFAVIMSGTPAESAITAMSRVHEGLNTLRLPnAPQVTLRI--SVGVApLNPQMSHYREWLKSADL 349
|
170
....*....|.
gi 290753359 558 NLYKAKSAGKN 568
Cdd:PRK10245 350 ALYKAKNAGRN 360
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
403-574 |
7.14e-19 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 90.51 E-value: 7.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 403 EER---EKFYEISIHDTLTGCYSRYYLKETIKRVLAIHDRGEirnVGIVMLDIDDFKNINDTYGHDVGDEVLKVIADIIK 479
Cdd:PRK10060 225 EERraqERLRILANTDSITGLPNRNAIQELIDHAINAADNNQ---VGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAIL 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 480 NEVRVGDIPVRYGGEEFMIVAVVNDIKSVYMVAERIRTKLEEykwdaPLdkeRI-------TASFGVVLR-KKGESFEDV 551
Cdd:PRK10060 302 SCLEEDQTLARLGGDEFLVLASHTSQAALEAMASRILTRLRL-----PF---RIglievytGCSIGIALApEHGDDSESL 373
|
170 180
....*....|....*....|....*
gi 290753359 552 IKRVDINLYKAKSAGKNT--VICEE 574
Cdd:PRK10060 374 IRSADTAMYTAKEGGRGQfcVFSPE 398
|
|
| GloB |
COG0491 |
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ... |
15-226 |
5.29e-17 |
|
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
Pssm-ID: 440257 [Multi-domain] Cd Length: 215 Bit Score: 80.12 E-value: 5.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 15 IFWVGHELPDDPFQCHVYLILNGKGSILIDPGSKITFKYAL-EKIEQIipFSYIKYFICQHQDPDITASLEIIRDLLird 93
Cdd:COG0491 1 VYVLPGGTPGAGLGVNSYLIVGGDGAVLIDTGLGPADAEALlAALAAL--GLDIKAVLLTHLHPDHVGGLAALAEAF--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 94 DAVIVSHWRAIALLKH----YNLNIPMICVE---KENWKLNAGGRELEFIFTPYcHFPGAFCTYDKKSKVLFSSD-LFGG 165
Cdd:COG0491 76 GAPVYAHAAEAEALEApaagALFGREPVPPDrtlEDGDTLELGGPGLEVIHTPG-HTPGHVSFYVPDEKVLFTGDaLFSG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 290753359 166 FTDRFKLFAEDInyfdsiaafhepympskEILVHSLKKIEQYDIDLIAPQHGSIIRRDLIK 226
Cdd:COG0491 155 GVGRPDLPDGDL-----------------AQWLASLERLLALPPDLVIPGHGPPTTAEAID 198
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
399-570 |
8.70e-17 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 84.34 E-value: 8.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 399 RKLieEREKFYEISiHDTLTGCYSRYYLKETIKRVL-AIHDRGEiRNVgIVMLDIDDFKNINDTYGHDVGDEVLKVIADI 477
Cdd:PRK09776 655 RKM--LRQLSYSAS-HDALTHLANRASFEKQLRRLLqTVNSTHQ-RHA-LVFIDLDRFKAVNDSAGHAAGDALLRELASL 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 478 IKNEVRVGDIPVRYGGEEFMIVAVVNDIKSVYMVAERIRTKLEEYK--WDAPLdkERITASFGV-VLRKKGESFEDVIKR 554
Cdd:PRK09776 730 MLSMLRSSDVLARLGGDEFGLLLPDCNVESARFIATRIISAINDYHfpWEGRV--YRVGASAGItLIDANNHQASEVMSQ 807
|
170
....*....|....*.
gi 290753359 555 VDINLYKAKSAGKNTV 570
Cdd:PRK09776 808 ADIACYAAKNAGRGRV 823
|
|
| Lactamase_B |
smart00849 |
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ... |
30-216 |
2.13e-15 |
|
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins contain this domain. These proteins include thiolesterases, members of the glyoxalase II family, that catalyse the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid and a competence protein that is essential for natural transformation in Neisseria gonorrhoeae and could be a transporter involved in DNA uptake. Except for the competence protein these proteins bind two zinc ions per molecule as cofactor.
Pssm-ID: 214854 [Multi-domain] Cd Length: 177 Bit Score: 74.51 E-value: 2.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 30 HVYLILNGKGSILIDPGSKITFKYaLEKIEQIIPFSyIKYFICQHQDPDITASLEIIRDLLirdDAVIVSHWRAIALLKH 109
Cdd:smart00849 1 NSYLVRDDGGAILIDTGPGEAEDL-LAELKKLGPKK-IDAIILTHGHPDHIGGLPELLEAP---GAPVYAPEGTAELLKD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 110 YNLNIPMICVEKENW----------KLNAGGRELEFIFTPyCHFPGAFCTYDKKSKVLFSSDLFGGFTDRFKLFaediny 179
Cdd:smart00849 76 LLALLGELGAEAEPAppdrtlkdgdELDLGGGELEVIHTP-GHTPGSIVLYLPEGKILFTGDLLFAGGDGRTLV------ 148
|
170 180 190
....*....|....*....|....*....|....*..
gi 290753359 180 fdsiaafhEPYMPSKEILVHSLKKIEQYDIDLIAPQH 216
Cdd:smart00849 149 --------DGGDAAASDALESLLKLLKLLPKLVVPGH 177
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
372-563 |
3.65e-13 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 71.58 E-value: 3.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 372 VIDNDILEILKEVINFLSIAFEREFIRRKLIEEREKFYEISIHDTLTGCYSRYYLKETIKRVLaiHDRGEIRNVGIVMLD 451
Cdd:PRK09966 208 VSEERIAEFHRFALDFNSLLDEMEEWQLRLQAKNAQLLRTALHDPLTGLANRAAFRSGINTLM--NNSDARKTSALLFLD 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 452 IDDFKNINDTYGHDVGDEVLKVIAdiiKNEVRVGDI---PVRYGGEEFMIvaVVNDIKSVYMVaERIRTKLEEyKWDAPL 528
Cdd:PRK09966 286 GDNFKYINDTWGHATGDRVLIEIA---KRLAEFGGLrhkAYRLGGDEFAM--VLYDVQSESEV-QQICSALTQ-IFNLPF 358
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 290753359 529 D-----KERITASFGVVLRKKGESFEDVIKRVDINLYKAK 563
Cdd:PRK09966 359 DlhnghQTTMTLSIGYAMTIEHASAEKLQELADHNMYQAK 398
|
|
| Nucleotidyl_cyc_III |
cd07556 |
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
444-563 |
7.84e-13 |
|
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: 65.84 E-value: 7.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 444 NVGIVMLDIDDFKNINDTYGHDVGDEVLKVIADIIKNEV-RVGDIPVRYGGEEFMIVAVVNDIKSVYMVAERIRTKLEEY 522
Cdd:cd07556 1 PVTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIrRSGDLKIKTIGDEFMVVSGLDHPAAAVAFAEDMREAVSAL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 290753359 523 KWDAPLDKE-RITASFGVV------LRKKGESFEDVIKRVDINLYKAK 563
Cdd:cd07556 81 NQSEGNPVRvRIGIHTGPVvvgvigSRPQYDVWGALVNLASRMESQAK 128
|
|
| PRK11921 |
PRK11921 |
anaerobic nitric oxide reductase flavorubredoxin; |
9-231 |
2.60e-12 |
|
anaerobic nitric oxide reductase flavorubredoxin;
Pssm-ID: 237023 [Multi-domain] Cd Length: 394 Bit Score: 68.57 E-value: 2.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 9 VEIAEDIFWVGH---ELPD---DPFQCH------VYLILNGKgSILIDPGSKITFKYALEKIEQIIPFSYIKYFICQHQD 76
Cdd:PRK11921 1 FKINDNVTWVGKidwELRKfhgEEYSTHrgssynSYLIKDEK-TVLIDTVWQPFAKEFVENLKKEIDLDKIDYIVANHGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 77 PDITASL-EIIRdlLIRDDAVIVSHWRAIALLKHYNLNIPMICVeKENWKLNAGGRELEFIFTPYCHFPGAFCTYDKKSK 155
Cdd:PRK11921 80 IDHSGALpELMK--EIPDTPIYCTKNGAKSLKGHYHQDWNFVVV-KTGDRLEIGSNELIFIEAPMLHWPDSMFTYLTGDN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 156 VLFSSDLFG----------GFTDRFKLFAEDINYFDSIAAfhePYMPskeiLVhsLKKIEQY-----DIDLIAPQHGsII 220
Cdd:PRK11921 157 ILFSNDAFGqhyaselmynDLVDQGELYQEAIKYYANILT---PFSP----LV--IKKIEEIlslnlPVDMICPSHG-VI 226
|
250
....*....|.
gi 290753359 221 RRDLIKPIINK 231
Cdd:PRK11921 227 WRDNPLQIVEK 237
|
|
| Lactamase_B |
pfam00753 |
Metallo-beta-lactamase superfamily; |
25-216 |
1.60e-11 |
|
Metallo-beta-lactamase superfamily;
Pssm-ID: 425851 [Multi-domain] Cd Length: 196 Bit Score: 63.54 E-value: 1.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 25 DPFQCHVYLILNGKGSILIDPGSKITFKY-ALEKIEQIIPFSyIKYFICQHQDPDITASLEIIRDLLirdDAVIVSH--- 100
Cdd:pfam00753 2 GPGQVNSYLIEGGGGAVLIDTGGSAEAALlLLLAALGLGPKD-IDAVILTHGHFDHIGGLGELAEAT---DVPVIVVaee 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 101 -------WRAIALLKHYNLNIPMICVEKENWKLN-----AGGRELEFIFTPYcHFPGAFCTYDKKSKVLFSSD-LFGGFT 167
Cdd:pfam00753 78 arelldeELGLAASRLGLPGPPVVPLPPDVVLEEgdgilGGGLGLLVTHGPG-HGPGHVVVYYGGGKVLFTGDlLFAGEI 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 290753359 168 DRFKLFAEDinyfdsiaaFHEPYMPSKEILVHSLKKIEQYDIDLIAPQH 216
Cdd:pfam00753 157 GRLDLPLGG---------LLVLHPSSAESSLESLLKLAKLKAAVIVPGH 196
|
|
| yflN-like_MBL-fold |
cd07721 |
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ... |
20-217 |
4.45e-11 |
|
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase domain; This subgroup includes the uncharacterized Bacillus subtilis yflN protein. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.
Pssm-ID: 293807 [Multi-domain] Cd Length: 202 Bit Score: 62.24 E-value: 4.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 20 HELPDDPFqCHVYLILNGKGSILIDPGSKITFKYALEKIEQI-IPFSYIKYFICQHQDPDITASLEIIRDLLirdDAVIV 98
Cdd:cd07721 3 YQLPLLPP-VNAYLIEDDDGLTLIDTGLPGSAKRILKALRELgLSPKDIRRILLTHGHIDHIGSLAALKEAP---GAPVY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 99 SHWRAIALL---------------KHYNLNIPMICVE-----KENWKLNAGGrELEFIFTPyCHFPGAFCTYDKKSKVLF 158
Cdd:cd07721 79 AHEREAPYLegekpypppvrlgllGLLSPLLPVKPVPvdrtlEDGDTLDLAG-GLRVIHTP-GHTPGHISLYLEEDGVLI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 290753359 159 SSDLF----GGFTDRFKLFAEDinyfdsiaafhepympsKEILVHSLKKIEQYDIDLIAPQHG 217
Cdd:cd07721 157 AGDALvtvgGELVPPPPPFTWD-----------------MEEALESLRKLAELDPEVLAPGHG 202
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
389-516 |
3.90e-10 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 62.86 E-value: 3.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 389 SIAFEREfirrkliEEREKFYEISIHDTLTGCYSRYYLKETIKRVLaihdrGEIRNVGIVMLDIDDFKNINDTYGHDVGD 468
Cdd:PRK11359 360 ALALEQE-------KSRQHIEQLIQFDPLTGLPNRNNLHNYLDDLV-----DKAVSPVVYLIGVDHFQDVIDSLGYAWAD 427
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 290753359 469 EVLKVIADIIKNEVRVGDIPVRYGGEEFMIVAVVNDIKSVYMVAERIR 516
Cdd:PRK11359 428 QALLEVVNRFREKLKPDQYLCRIEGTQFVLVSLENDVSNITQIADELR 475
|
|
| PleD |
COG3706 |
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ... |
486-563 |
3.16e-09 |
|
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: 56.46 E-value: 3.16e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 290753359 486 DIPVRYGGEEFMIVAVVNDIKSVYMVAERIRTKLEEykwdapLDKERITASFGVvlrkkgeSFEDVIKRVDiNLYKAK 563
Cdd:COG3706 116 DLVARYGGEEFAILLPGTDLEGALAVAERIREAVAE------LPSLRVTVSIGV-------AGDSLLKRAD-ALYQAR 179
|
|
| TTHA1429-like_MBL-fold |
cd07725 |
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ... |
31-221 |
2.76e-08 |
|
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized Thermus thermophilus TTHA1429 and related proteins. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.
Pssm-ID: 293811 [Multi-domain] Cd Length: 184 Bit Score: 53.84 E-value: 2.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 31 VYLILNGKGSILIDPGSKITF--KYALEKIEQI-IPFSYIKYFICQHQDPDITASLEIIRDLLIRDdaVIVSHWRAIall 107
Cdd:cd07725 17 VYLLRDGDETTLIDTGLATEEdaEALWEGLKELgLKPSDIDRVLLTHHHPDHIGLAGKLQEKSGAT--VYILDVTPV--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 108 khynlnipmicveKENWKLNAGGRELEFIFTPyCHFPGAFCTYDKKSKVLFSSDlfggftdrfkLFAEDINYFDSIAAFH 187
Cdd:cd07725 92 -------------KDGDKIDLGGLRLKVIETP-GHTPGHIVLYDEDRRELFVGD----------AVLPKITPNVSLWAVR 147
|
170 180 190
....*....|....*....|....*....|....
gi 290753359 188 EPyMPSKEILvHSLKKIEQYDIDLIAPQHGSIIR 221
Cdd:cd07725 148 VE-DPLGAYL-ESLDKLEKLDVDLAYPGHGGPIK 179
|
|
| PRK05452 |
PRK05452 |
anaerobic nitric oxide reductase flavorubredoxin; Provisional |
32-231 |
2.57e-07 |
|
anaerobic nitric oxide reductase flavorubredoxin; Provisional
Pssm-ID: 235475 [Multi-domain] Cd Length: 479 Bit Score: 53.22 E-value: 2.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 32 YLILNGKgSILIDpgsKITFKYALEKIEQI---IPFSYIKYFICQHQDPD----ITASLEIIRDLLI--RDDAV--IVSH 100
Cdd:PRK05452 38 YLIREEK-NVLID---TVDHKFSREFVQNLrneIDLADIDYIVINHAEEDhagaLTELMAQIPDTPIycTANAIdsINGH 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 101 wraiallKH---YNLNipmicVEKENWKLNAG-GRELEFIFTPYCHFPGAFCTYDKKSKVLFSSDLFGGF---------- 166
Cdd:PRK05452 114 -------HHhpeWNFN-----VVKTGDTLDIGnGKQLIFVETPMLHWPDSMMTYLTGDAVLFSNDAFGQHycdehlfnde 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 290753359 167 TDRFKLFAEDINYFDSIAAFHEPYMPSK--EILVHSLKkieqydIDLIAPQHGsIIRRDLIKPIINK 231
Cdd:PRK05452 182 VDQTELFEQCQRYYANILTPFSRLVTPKitEILGFNLP------VDMIATSHG-VVWRDNPTQIVEL 241
|
|
| metallo-hydrolase-like_MBL-fold |
cd16276 |
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ... |
37-220 |
2.80e-06 |
|
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily.Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.
Pssm-ID: 293834 [Multi-domain] Cd Length: 188 Bit Score: 47.96 E-value: 2.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 37 GKGSILIDPGSKITFKYaLEKIEQI--IPfsyIKYFICQHQDPDITASLEIIRDllirDDAVIVSHWRAIALLK---HYN 111
Cdd:cd16276 18 DKGVIVVDAPPSLGENL-LAAIRKVtdKP---VTHVVYSHNHADHIGGASIFKD----EGATIIAHEATAELLKrnpDPK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 112 LNIPMICVEKENwKLNAGGRELEFIFTPYCHFPGAFCTYDKKSKVLFSSDLFggftdrfklFAEDINYFDSIAAFHEPYM 191
Cdd:cd16276 90 RPVPTVTFDDEY-TLEVGGQTLELSYFGPNHGPGNIVIYLPKQKVLMAVDLI---------NPGWVPFFNFAGSEDIPGY 159
|
170 180
....*....|....*....|....*....
gi 290753359 192 pskeilVHSLKKIEQYDIDLIAPQHGSII 220
Cdd:cd16276 160 ------IEALDELLEYDFDTFVGGHGNRL 182
|
|
| metallo-hydrolase-like_MBL-fold |
cd06262 |
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ... |
22-216 |
4.72e-06 |
|
mainly hydrolytic enzymes and related proteins which carry out various biological functions; MBL-fold metallohydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases which can catalyze the hydrolysis of a wide range of beta-lactam antibiotics, hydroxyacylglutathione hydrolases (also called glyoxalase II) which hydrolyze S-d-lactoylglutathione to d-lactate in the second step of the glycoxlase system, AHL lactonases which catalyze the hydrolysis and opening of the homoserine lactone rings of acyl homoserine lactones (AHLs), persulfide dioxygenase which catalyze the oxidation of glutathione persulfide to glutathione and persulfite in the mitochondria, flavodiiron proteins which catalyze the reduction of oxygen and/or nitric oxide to water or nitrous oxide respectively, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J which has both 5'-3' exoribonucleolytic and endonucleolytic activity and ribonuclease Z which catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors, cyclic nucleotide phosphodiesterases which decompose cyclic adenosine and guanosine 3', 5'-monophosphate (cAMP and cGMP) respectively, insecticide hydrolases, and proteins required for natural transformation competence. The diversity of biological roles is reflected in variations in the active site metallo-chemistry, for example classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, human persulfide dioxygenase ETHE1 is a mono-iron binding member of the superfamily; Arabidopsis thaliana hydroxyacylglutathione hydrolases incorporates iron, manganese, and zinc in its dinuclear metal binding site, and flavodiiron proteins contains a diiron site.
Pssm-ID: 293792 [Multi-domain] Cd Length: 188 Bit Score: 47.28 E-value: 4.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 22 LPDDPFQCHVYLILNGKGS-ILIDPGSkitfkYALEKIEQIIPFSY--IKYFICQHQDPDITASLEIIRDlliRDDAVIV 98
Cdd:cd06262 3 LPVGPLQTNCYLVSDEEGEaILIDPGA-----GALEKILEAIEELGlkIKAILLTHGHFDHIGGLAELKE---APGAPVY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 99 SH------WRAIALLKHYNLNIPMICVE-----KENWKLNAGGRELEFIFTPyCHFPGAFCTYDKKSKVLFSSDLfggft 167
Cdd:cd06262 75 IHeadaelLEDPELNLAFFGGGPLPPPEpdillEDGDTIELGGLELEVIHTP-GHTPGSVCFYIEEEGVLFTGDT----- 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 290753359 168 drfkLFAEDINYFDsiaafhePYMPSKEILVHSLKKI--EQYDIDLIAPQH 216
Cdd:cd06262 149 ----LFAGSIGRTD-------LPGGDPEQLIESIKKLllLLPDDTVVYPGH 188
|
|
| metallo-hydrolase-like_MBL-fold |
cd16282 |
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ... |
33-225 |
8.95e-06 |
|
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily.Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.
Pssm-ID: 293840 [Multi-domain] Cd Length: 209 Bit Score: 46.79 E-value: 8.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 33 LILNGKGSILIDPGSkiTFKYA---LEKIEQII--PfsyIKYFICQHQDPDITASLEIIRDllirDDAVIVSHWRAIALL 107
Cdd:cd16282 19 FIVGDDGVVVIDTGA--SPRLAralLAAIRKVTdkP---VRYVVNTHYHGDHTLGNAAFAD----AGAPIIAHENTREEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 108 KHY--NLNIPMICVEKENWK----------------LNAGGRELEFIFTPYCHFPGAFCTYDKKSKVLFSSDL-FGGFTD 168
Cdd:cd16282 90 AARgeAYLELMRRLGGDAMAgtelvlpdrtfddgltLDLGGRTVELIHLGPAHTPGDLVVWLPEEGVLFAGDLvFNGRIP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 290753359 169 rfklFAEDINYFDSIAAfhepympskeilvhsLKKIEQYDIDLIAPQHGSIIRRDLI 225
Cdd:cd16282 170 ----FLPDGSLAGWIAA---------------LDRLLALDATVVVPGHGPVGDKADL 207
|
|
| GAF |
COG2203 |
GAF domain [Signal transduction mechanisms]; |
241-516 |
1.25e-05 |
|
GAF domain [Signal transduction mechanisms];
Pssm-ID: 441805 [Multi-domain] Cd Length: 712 Bit Score: 48.27 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 241 LLTQSSTELEKLRKLNKFLNAFLETMATYKDFTELIREFVIELRSAFDFDSIEFYT-DYKGTLLYFLA------------ 307
Cdd:COG2203 177 IARLLTQRARLELERLALLNEISQALRSALDLEELLQRILELAGELLGADRGAILLvDEDGGELELVAapglpeeelgrl 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 308 --ETPSIWEKIKQQE--YVKDILQ-IKMSEYYEKYPNYLYVRNVLYIPIpeIESDKIIAVMKLYLKESIVIDNDILEILK 382
Cdd:COG2203 257 plGEGLAGRALRTGEpvVVNDASTdPRFAPSLRELLLALGIRSLLCVPL--LVDGRLIGVLALYSKEPRAFTEEDLELLE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 383 EVINFLSIAFEREFIRRKLIEEREKFYEI-----SIHDTLTGCYSRYYLKETIKRVLAIHDRGEIRNVGIVMLDIDDFKN 457
Cdd:COG2203 335 ALADQAAIAIERARLYEALEAALAALLQElallrLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAADLSG 414
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 290753359 458 INDTYGHDVGDEVLKVIADIIKNEVRVGDIPVRYGGEEFMIVAVVNDIKSVYMVAERIR 516
Cdd:COG2203 415 LLALEGLLLLDLLLLLLLLRRILLLRVLRRLLLGDEEGLVLLLALAELELLEILELLVL 473
|
|
| ST1585-like_MBL-fold |
cd07726 |
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ... |
14-216 |
8.02e-05 |
|
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo hydrolase domain; This subgroup includes the uncharacterized Sulfolobus tokodaii ST1585 protein. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.
Pssm-ID: 293812 [Multi-domain] Cd Length: 215 Bit Score: 44.02 E-value: 8.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 14 DIFWVGHELPDDPFQCHVYLILNGKGSILIDPGSKITFKYALEKIEQI-IPFSYIKYFICQHqdpditasleIIRD---- 88
Cdd:cd07726 1 GIYLIDLGFLGFPGRIASYLLDGEGRPALIDTGPSSSVPRLLAALEALgIAPEDVDYIILTH----------IHLDhagg 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 89 --LLIRD--DAVIVSHWRAIallKH-------------------YNLNIPMICVEKEN-------WKLNAGGRELEFIFT 138
Cdd:cd07726 71 agLLAEAlpNAKVYVHPRGA---RHlidpsklwasaravygdeaDRLGGEILPVPEERvivledgETLDLGGRTLEVIDT 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 139 PyCHFPGAFCTYDKKSKVLFSSDLFGGftdrfklfaedinyfdSIAAFHEPYMPS-------KEILVHSLKKIEQYDIDL 211
Cdd:cd07726 148 P-GHAPHHLSFLDEESDGLFTGDAAGV----------------RYPELDVVGPPStpppdfdPEAWLESLDRLLSLKPER 210
|
....*
gi 290753359 212 IAPQH 216
Cdd:cd07726 211 IYLTH 215
|
|
| TTHA1623-like_MBL-fold |
cd16322 |
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ... |
26-165 |
8.72e-05 |
|
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized Thermus thermophilus TTHA1623 and related proteins. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. This family includes homologs present in a wide range of bacteria and archaea and some eukaryota. Members of the MBL-fold metallo-hydrolase superfamily exhibit a variety of active site metallo-chemistry, TTHA1623 exhibiting a uniquely shaped putative substrate-binding pocket with a glyoxalase II-type metal-coordination mode.
Pssm-ID: 293877 [Multi-domain] Cd Length: 204 Bit Score: 43.88 E-value: 8.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 26 PFQCHVYLI--LNGKGSILIDPGSKitfkyALEKIEQIIPFSY-IKYFICQHQDPDITASLEIIRDlliRDDAVIVSHWR 102
Cdd:cd16322 8 PLQENTYLVadEGGGEAVLVDPGDE-----SEKLLARFGTTGLtLLYILLTHAHFDHVGGVADLRR---HPGAPVYLHPD 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 290753359 103 AIALLKHYN-------LNI-PMICVE---KENWKLNAGGRELEFIFTPyCHFPGAFCTYDKKSKVLFSSDL-FGG 165
Cdd:cd16322 80 DLPLYEAADlgakafgLGIePLPPPDrllEDGQTLTLGGLEFKVLHTP-GHSPGHVCFYVEEEGLLFSGDLlFQG 153
|
|
| LACTB2-like_MBL-fold |
cd07722 |
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ... |
32-220 |
9.90e-04 |
|
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold metallo hydrolase domain; Includes functionally uncharacterized human lactamase beta 2. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.
Pssm-ID: 293808 [Multi-domain] Cd Length: 188 Bit Score: 40.59 E-value: 9.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 32 YLILNGKGSILIDPGS-KITFKYALEKIEQIIPFSYIKYFICQHQDPDITASLEIIRDLLiRDDAVIVSHWRAIALLKHY 110
Cdd:cd07722 21 YLVGTGKRRILIDTGEgRPSYIPLLKSVLDSEGNATISDILLTHWHHDHVGGLPDVLDLL-RGPSPRVYKFPRPEEDEDP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290753359 111 NLNIPMICVEKENWKLNAGGRELEFIFTPyCHFPGAFCTYDKKSKVLFSSD--LFGGFTDrfklfaedinyFDSIAAfhe 188
Cdd:cd07722 100 DEDGGDIHDLQDGQVFKVEGATLRVIHTP-GHTTDHVCFLLEEENALFTGDcvLGHGTAV-----------FEDLAA--- 164
|
170 180 190
....*....|....*....|....*....|..
gi 290753359 189 pYMpskeilvHSLKKIEQYDIDLIAPQHGSII 220
Cdd:cd07722 165 -YM-------ASLKKLLSLGPGRIYPGHGPVI 188
|
|
| |
