NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|966416724|ref|WP_058460009|]
View 

MBL fold metallo-hydrolase [Legionella bozemanae]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
TaR3-like_MBL-fold cd07715
MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold ...
 127-345 2.16e-85

MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold metallo-hydrolase domain; Myxococcus xanthus Tar3 may function as an ammonium regulator/effector protein involved in biosynthesis of the antibiotic TA. Some are members of this subgroup are annotated as ribonucleases. 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: 293801 [Multi-domain]  Cd Length: 212  Bit Score: 258.97  E-value: 2.16e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966416724 127 FWGMTGAFPAPGKDFVKYGGHTSCVTLNfVNERMIILDAGSGIIPLGNELIiKNQNPIEADIFISHEHWDHIHGLTFFKP 206
Cdd:cd07715    2 FWGVRGSIPVPGPDTVRYGGNTSCVEVR-AGGELLILDAGTGIRELGNELM-KEGPPGEAHLLLSHTHWDHIQGFPFFAP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966416724 207 LYHPGNLFNFYGPPQGVKSVHELLSGLMDGIYFPVKIDNLPSTISYHDLMADQNFKIDNIKIATIALQHPCATYGYKIQY 286
Cdd:cd07715   80 AYDPGNRIHIYGPHKDGGSLEEVLRRQMSPPYFPVPLEELLAAIEFHDLEPGEPFSIGGVTVTTIPLNHPGGALGYRIEE 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 966416724 287 NNKIISYITDNELYDKSYHLYnadfvHNLIQFTMDSDILIVDCAFTDEEYDSgRVCWGH 345
Cdd:cd07715  160 DGKSVVYATDTEHYPDDGESD-----EALLEFARGADLLIHDAQYTDEEYPS-KRGWGH 212
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
 18-102 1.51e-05

phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response regulators (PRRs); Two-component systems (TCSs) involving a sensor and a response regulator are used by bacteria to adapt to changing environments. Processes regulated by two-component systems in bacteria include sporulation, pathogenicity, virulence, chemotaxis, and membrane transport. Response regulators (RRs) share the common phosphoacceptor REC domain and different effector/output domains such as DNA, RNA, ligand-binding, protein-binding, or enzymatic domains. Response regulators regulate transcription, post-transcription or post-translation, or have functions such as methylesterases, adenylate or diguanylate cyclase, c-di-GMP-specific phosphodiesterases, histidine kinases, serine/threonine protein kinases, and protein phosphatases, depending on their output domains. The function of some output domains are still unknown. TCSs are found in all three domains of life - bacteria, archaea, and eukaryotes, however, the presence and abundance of particular RRs vary between the lineages. Archaea encode very few RRs with DNA-binding output domains; most are stand-alone REC domains. Among eukaryotes, TCSs are found primarily in protozoa, fungi, algae, and green plants. REC domains function as phosphorylation-mediated switches within RRs, but some also transfer phosphoryl groups in multistep phosphorelays.


:

Pssm-ID: 381085 [Multi-domain]  Cd Length: 99  Bit Score: 43.37  E-value: 1.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966416724  18 DPNIIGLITNELKTSGHITSSTDNVEDALMQVNKFKPDYVLIDQQIP-------TEKIKELCKsnKYKVIILS-LDPSNK 89
Cdd:cd00156    6 DPAIRELLKSLLEREGYEVDTAADGEEALELLREERPDLVLLDLMMPgmdglelLRKLRELPP--DIPVIVLTaKADEED 83

                         90
                 ....*....|...
gi 966416724  90 NINPYKLGAHGCI 102
Cdd:cd00156   84 AVRALELGADDYL 96
 
Name Accession Description Interval E-value
TaR3-like_MBL-fold cd07715
MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold ...
 127-345 2.16e-85

MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold metallo-hydrolase domain; Myxococcus xanthus Tar3 may function as an ammonium regulator/effector protein involved in biosynthesis of the antibiotic TA. Some are members of this subgroup are annotated as ribonucleases. 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: 293801 [Multi-domain]  Cd Length: 212  Bit Score: 258.97  E-value: 2.16e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966416724 127 FWGMTGAFPAPGKDFVKYGGHTSCVTLNfVNERMIILDAGSGIIPLGNELIiKNQNPIEADIFISHEHWDHIHGLTFFKP 206
Cdd:cd07715    2 FWGVRGSIPVPGPDTVRYGGNTSCVEVR-AGGELLILDAGTGIRELGNELM-KEGPPGEAHLLLSHTHWDHIQGFPFFAP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966416724 207 LYHPGNLFNFYGPPQGVKSVHELLSGLMDGIYFPVKIDNLPSTISYHDLMADQNFKIDNIKIATIALQHPCATYGYKIQY 286
Cdd:cd07715   80 AYDPGNRIHIYGPHKDGGSLEEVLRRQMSPPYFPVPLEELLAAIEFHDLEPGEPFSIGGVTVTTIPLNHPGGALGYRIEE 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 966416724 287 NNKIISYITDNELYDKSYHLYnadfvHNLIQFTMDSDILIVDCAFTDEEYDSgRVCWGH 345
Cdd:cd07715  160 DGKSVVYATDTEHYPDDGESD-----EALLEFARGADLLIHDAQYTDEEYPS-KRGWGH 212
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 125-365 2.74e-36

Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism];


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 133.48  E-value: 2.74e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966416724 125 IEFWGmTGA---FPAPGKD-------FVKYGGHTSCVTLNFVNERmIILDAGSGIIPLGNELIIkNQNPIEAdIFISHEH 194
Cdd:COG1235    3 VTFLG-SGSsggVPQIGCDcpvcastDPRYGRTRSSILVEADGTR-LLIDAGPDLREQLLRLGL-DPSKIDA-ILLTHEH 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966416724 195 WDHIHGLTFFKPLYHPGNLfNFYGPPqgvkSVHELLSGLMDGIYFPvkidnLPSTISYHDLMADQNFKIDNIKIATIALQ 274
Cdd:COG1235   79 ADHIAGLDDLRPRYGPNPI-PVYATP----GTLEALERRFPYLFAP-----YPGKLEFHEIEPGEPFEIGGLTVTPFPVP 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966416724 275 HPCA-TYGYKIQYNNKIISYITDNELYDksyhlynadfvHNLIQFTMDSDILIVDCAFTDEEydsgrvcWGHSCPRQISE 353
Cdd:COG1235  149 HDAGdPVGYRIEDGGKKLAYATDTGYIP-----------EEVLELLRGADLLILDATYDDPE-------PGHLSNEEALE 210

                        250
                 ....*....|..
gi 966416724 354 FAYLTNAKQLIL 365
Cdd:COG1235  211 LLARLGPKRLVL 222
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 183-365 3.03e-12

Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and is related to pfam00753.


Pssm-ID: 432732 [Multi-domain]  Cd Length: 196  Bit Score: 65.02  E-value: 3.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966416724  183 PIEAdIFISHEHWDHIHGLTFFKPLYHpgnlFNFYGPPqgvkSVHELLSGlmdgiYFPVKIDNLPSTISYHDLMADQNFK 262
Cdd:pfam12706  28 PIDA-VLLTHDHYDHLAGLLDLREGRP----RPLYAPL----GVLAHLRR-----NFPYLFLLEHYGVRVHEIDWGESFT 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966416724  263 ID--NIKIATIALQH---------PCATYGYKIQYNNKIISYITDNELYDKSyhlynadfvhnLIQFTMDSDILIVDCAF 331
Cdd:pfam12706  94 VGdgGLTVTATPARHgsprgldpnPGDTLGFRIEGPGKRVYYAGDTGYFPDE-----------IGERLGGADLLLLDGGA 162

                         170       180       190
                  ....*....|....*....|....*....|....
gi 966416724  332 TDEEYDSGrvcWGHSCPRQISEFAYLTNAKQLIL 365
Cdd:pfam12706 163 WRDDEMIH---MGHMTPEEAVEAAADLGARRKVL 193
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 124-365 1.42e-09

ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of endonuclease or exonuclease activity, and differs in different species. Member of this family are ribonuclease Z, a tRNA 3-prime endonuclease that processes tRNAs to prepare for addition of CCA. In species where all tRNA sequences already have the CCA tail, such as E. coli, the need for such an enzyme is unclear. Protein similar to the E. coli enzyme, matched by TIGRFAMs model TIGR02649, are designated ribonuclease BN. [Transcription, RNA processing]


Pssm-ID: 274246 [Multi-domain]  Cd Length: 299  Bit Score: 58.77  E-value: 1.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966416724  124 DIEFWGMTGAFPAPGKdfvkyggHTSCVTLNFVNERmIILDAGSG------IIPLGNELIIKnqnpieadIFISHEHWDH 197
Cdd:TIGR02651   1 EITFLGTGGGVPTKER-------NLPSIALKLNGEL-WLFDCGEGtqrqmlRSGISPMKIDR--------IFITHLHGDH 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966416724  198 IHGLtffkplyhPGNL--FNF---------YGPPqGVKsvhELLSGLMDGIYFpvkidNLPSTISYHDLMADQN-FKIDN 265
Cdd:TIGR02651  65 ILGL--------PGLLstMSFqgrkepltiYGPP-GIK---EFIETSLRVSYT-----YLNYPIKIHEIEEGGLvFEDDG 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966416724  266 IKIATIALQHPCATYGYKIQY---------------------------NNKIISYItDNELYDKSYHL----------YN 308
Cdd:TIGR02651 128 FKVEAFPLDHSIPSLGYRFEEkdrpgkfdrekakelgippgplygklkRGETVTLI-DGRIIDPEDVLgpprkgrkiaYT 206

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966416724  309 AD--FVHNLIQFTMDSDILIVDCAFTDEE----YDSgrvcwGHSCPRQISEFAYLTNAKQLIL 365
Cdd:TIGR02651 207 GDtrPCEEVIEFAKNADLLIHEATFLDEDkklaKEY-----GHSTAAQAAEIAKEANVKRLIL 264
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
 18-102 1.51e-05

phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response regulators (PRRs); Two-component systems (TCSs) involving a sensor and a response regulator are used by bacteria to adapt to changing environments. Processes regulated by two-component systems in bacteria include sporulation, pathogenicity, virulence, chemotaxis, and membrane transport. Response regulators (RRs) share the common phosphoacceptor REC domain and different effector/output domains such as DNA, RNA, ligand-binding, protein-binding, or enzymatic domains. Response regulators regulate transcription, post-transcription or post-translation, or have functions such as methylesterases, adenylate or diguanylate cyclase, c-di-GMP-specific phosphodiesterases, histidine kinases, serine/threonine protein kinases, and protein phosphatases, depending on their output domains. The function of some output domains are still unknown. TCSs are found in all three domains of life - bacteria, archaea, and eukaryotes, however, the presence and abundance of particular RRs vary between the lineages. Archaea encode very few RRs with DNA-binding output domains; most are stand-alone REC domains. Among eukaryotes, TCSs are found primarily in protozoa, fungi, algae, and green plants. REC domains function as phosphorylation-mediated switches within RRs, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381085 [Multi-domain]  Cd Length: 99  Bit Score: 43.37  E-value: 1.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966416724  18 DPNIIGLITNELKTSGHITSSTDNVEDALMQVNKFKPDYVLIDQQIP-------TEKIKELCKsnKYKVIILS-LDPSNK 89
Cdd:cd00156    6 DPAIRELLKSLLEREGYEVDTAADGEEALELLREERPDLVLLDLMMPgmdglelLRKLRELPP--DIPVIVLTaKADEED 83

                         90
                 ....*....|...
gi 966416724  90 NINPYKLGAHGCI 102
Cdd:cd00156   84 AVRALELGADDYL 96
PRK00055 PRK00055
ribonuclease Z; Reviewed
 123-365 2.95e-05

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 45.17  E-value: 2.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966416724 123 IDIEFWGMTGAFPAPGKdfvkyggHTSCVTLNFvNERMIILDAGSGIIplgNELIIKNQNP--IEAdIFISHEHWDHIHG 200
Cdd:PRK00055   2 MELTFLGTGSGVPTPTR-------NVSSILLRL-GGELFLFDCGEGTQ---RQLLKTGIKPrkIDK-IFITHLHGDHIFG 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966416724 201 LtffkplyhPGNL--FNF---------YGPPqGVKsvhELLSGLMDGIYF----------PVKID-------NLPSTISY 252
Cdd:PRK00055  70 L--------PGLLstRSLsgrtepltiYGPK-GIK---EFVETLLRASGSlgyriaekdkPGKLDaeklkalGVPPGPLF 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966416724 253 HDLMADQNFKIDNIKIATIAlqhpcatYGYKIQYNNKIISYITDNELYDksyhlynadfvhNLIQFTMDSDILIVDCAFT 332
Cdd:PRK00055 138 GKLKRGEDVTLEDGRIINPA-------DVLGPPRKGRKVAYCGDTRPCE------------ALVELAKGADLLVHEATFG 198

                        250       260       270
                 ....*....|....*....|....*....|...
gi 966416724 333 DEEYDSGRvCWGHSCPRQISEFAYLTNAKQLIL 365
Cdd:PRK00055 199 DEDEELAK-EYGHSTARQAAEIAKEAGVKRLIL 230
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
 12-102 1.40e-04

Response regulator receiver domain; This domain receives the signal from the sensor partner in bacterial two-component systems. It is usually found N-terminal to a DNA binding effector domain.


Pssm-ID: 395025 [Multi-domain]  Cd Length: 111  Bit Score: 40.98  E-value: 1.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966416724   12 IYLVHQDPNIIGLITNELKTSGHITSSTDNVEDALMQVNKFKPDYVLIDQQIP-------TEKIKELckSNKYKVIILSL 84
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPgmdglelLKRIRRR--DPTTPVIILTA 78

                          90       100
                  ....*....|....*....|
gi 966416724   85 --DPSNKnINPYKLGAHGCI 102
Cdd:pfam00072  79 hgDEDDA-VEALEAGADDFL 97
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
 5-83 2.18e-04

CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator Spo0F [Signal transduction mechanisms];


Pssm-ID: 440547 [Multi-domain]  Cd Length: 128  Bit Score: 40.99  E-value: 2.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966416724   5 TQQRPLPIYLVHQDPNIIGLITNELKTSGHITSSTDNVEDALMQVNKFKPDYVLIDQQIP-------TEKIKELCKSNKY 77
Cdd:COG0784    1 PPLGGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPgmdglelLRRIRALPRLPDI 80


                 ....*.
gi 966416724  78 KVIILS 83
Cdd:COG0784   81 PIIALT 86
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 157-268 7.50e-04

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: 40.23  E-value: 7.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966416724   157 NERMIILDAGSG-IIPLGNELIIKNQNPIEAdIFISHEHWDHIHGLTFFKPLYHPgnlfNFYGPPQGVKSVHELLSGLMD 235
Cdd:smart00849   8 DGGAILIDTGPGeAEDLLAELKKLGPKKIDA-IILTHGHPDHIGGLPELLEAPGA----PVYAPEGTAELLKDLLALLGE 82

                           90       100       110
                   ....*....|....*....|....*....|...
gi 966416724   236 GIYFPVKIDNlpstisYHDLMADQNFKIDNIKI 268
Cdd:smart00849  83 LGAEAEPAPP------DRTLKDGDELDLGGGEL 109
 
Name Accession Description Interval E-value
TaR3-like_MBL-fold cd07715
MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold ...
 127-345 2.16e-85

MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold metallo-hydrolase domain; Myxococcus xanthus Tar3 may function as an ammonium regulator/effector protein involved in biosynthesis of the antibiotic TA. Some are members of this subgroup are annotated as ribonucleases. 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: 293801 [Multi-domain]  Cd Length: 212  Bit Score: 258.97  E-value: 2.16e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966416724 127 FWGMTGAFPAPGKDFVKYGGHTSCVTLNfVNERMIILDAGSGIIPLGNELIiKNQNPIEADIFISHEHWDHIHGLTFFKP 206
Cdd:cd07715    2 FWGVRGSIPVPGPDTVRYGGNTSCVEVR-AGGELLILDAGTGIRELGNELM-KEGPPGEAHLLLSHTHWDHIQGFPFFAP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966416724 207 LYHPGNLFNFYGPPQGVKSVHELLSGLMDGIYFPVKIDNLPSTISYHDLMADQNFKIDNIKIATIALQHPCATYGYKIQY 286
Cdd:cd07715   80 AYDPGNRIHIYGPHKDGGSLEEVLRRQMSPPYFPVPLEELLAAIEFHDLEPGEPFSIGGVTVTTIPLNHPGGALGYRIEE 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 966416724 287 NNKIISYITDNELYDKSYHLYnadfvHNLIQFTMDSDILIVDCAFTDEEYDSgRVCWGH 345
Cdd:cd07715  160 DGKSVVYATDTEHYPDDGESD-----EALLEFARGADLLIHDAQYTDEEYPS-KRGWGH 212
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 125-365 2.74e-36

Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism];


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 133.48  E-value: 2.74e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966416724 125 IEFWGmTGA---FPAPGKD-------FVKYGGHTSCVTLNFVNERmIILDAGSGIIPLGNELIIkNQNPIEAdIFISHEH 194
Cdd:COG1235    3 VTFLG-SGSsggVPQIGCDcpvcastDPRYGRTRSSILVEADGTR-LLIDAGPDLREQLLRLGL-DPSKIDA-ILLTHEH 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966416724 195 WDHIHGLTFFKPLYHPGNLfNFYGPPqgvkSVHELLSGLMDGIYFPvkidnLPSTISYHDLMADQNFKIDNIKIATIALQ 274
Cdd:COG1235   79 ADHIAGLDDLRPRYGPNPI-PVYATP----GTLEALERRFPYLFAP-----YPGKLEFHEIEPGEPFEIGGLTVTPFPVP 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966416724 275 HPCA-TYGYKIQYNNKIISYITDNELYDksyhlynadfvHNLIQFTMDSDILIVDCAFTDEEydsgrvcWGHSCPRQISE 353
Cdd:COG1235  149 HDAGdPVGYRIEDGGKKLAYATDTGYIP-----------EEVLELLRGADLLILDATYDDPE-------PGHLSNEEALE 210

                        250
                 ....*....|..
gi 966416724 354 FAYLTNAKQLIL 365
Cdd:COG1235  211 LLARLGPKRLVL 222
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
123-365 6.47e-34

Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 126.85  E-value: 6.47e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966416724 123 IDIEFWGMTGAFPAPGkdfvkygGHTSCVTLNfVNERMIILDAGSGIIPLGNELIIKnQNPIEAdIFISHEHWDHIHGLT 202
Cdd:COG1234    1 MKLTFLGTGGAVPTPG-------RATSSYLLE-AGGERLLIDCGEGTQRQLLRAGLD-PRDIDA-IFITHLHGDHIAGLP 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966416724 203 FF----------KPLYhpgnlfnFYGPPQGVKSVHELLSGLMDGIYFPVKIdnlpstisyHDLMADQNFKIDNIKIATIA 272
Cdd:COG1234   71 GLlstrslagreKPLT-------IYGPPGTKEFLEALLKASGTDLDFPLEF---------HEIEPGEVFEIGGFTVTAFP 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966416724 273 LQHPCATYGYKIQYNNKIISYITDNELYDksyhlynadfvhNLIQFTMDSDILIVDCAFTDEEYDSGRVcWGHSCPRQIS 352
Cdd:COG1234  135 LDHPVPAYGYRFEEPGRSLVYSGDTRPCE------------ALVELAKGADLLIHEATFLDEEAELAKE-TGHSTAKEAA 201

                        250
                 ....*....|...
gi 966416724 353 EFAYLTNAKQLIL 365
Cdd:COG1234  202 ELAAEAGVKRLVL 214
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 145-329 1.13e-19

Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as tRNase Z or 3' tRNase) catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors. Two forms of RNase Z exist in eukaryotes, one long (ELAC2) and one short form (ELAC1), the former may have resulted from a duplication of the shorter enzyme. Only the short form exists in bacteria. It includes the C-terminus of human ELAC2 and Escherichia coli zinc phosphodiesterase (ZiPD, also known as ecoZ, tRNase Z, or RNase BN) is a 3' tRNA-processing endonuclease, encoded by the elaC gene. 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: 293830 [Multi-domain]  Cd Length: 180  Bit Score: 85.78  E-value: 1.13e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966416724 145 GGHTSCVTLNFVNERmIILDAGSGIIPLGNELIIKNQNPIeaDIFISHEHWDHIHGLT---FFKPLYHPGNLFNFYGPpq 221
Cdd:cd16272   14 TRNTSSYLLETGGTR-ILLDCGEGTVYRLLKAGVDPDKLD--AIFLSHFHLDHIGGLPtllFARRYGGRKKPLTIYGP-- 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966416724 222 gvKSVHELLSGLMDgiyFPVKIDNLPSTISYHDL-MADQNFKIDNIKIATIALQHPCATYGYKIQYNNKIISYITDNElY 300
Cdd:cd16272   89 --KGIKEFLEKLLN---FPVEILPLGFPLEIEELeEGGEVLELGDLKVEAFPVKHSVESLGYRIEAEGKSIVYSGDTG-P 162

                        170       180
                 ....*....|....*....|....*....
gi 966416724 301 DKsyhlynadfvhNLIQFTMDSDILIVDC 329
Cdd:cd16272  163 CE-----------NLVELAKGADLLIHEC 180
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 125-365 5.50e-18

Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as tRNase Z or 3' tRNase) catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors. Escherichia coli zinc phosphodiesterase (ZiPD, also known as ecoZ, tRNase Z, or RNase BN) is a 3' tRNA-processing endonuclease, encoded by the elaC gene. Two forms of RNase Z exist in eukaryotes, one long (ELAC2) and one short form (ELAC1), the former may have resulted from a duplication of the shorter enzyme; this subgroup includes the short form (ELAC1). Only the short form exists in bacteria. 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: 293803 [Multi-domain]  Cd Length: 247  Bit Score: 82.88  E-value: 5.50e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966416724 125 IEFWGMTGAFPAPGKdfvkygGHTSCVtLNFvNERMIILDAGSGI--------IPLGNeliiknqnpIEAdIFISHEHWD 196
Cdd:cd07717    1 LTFLGTGSAVPTPER------NLSSIA-LRL-EGELWLFDCGEGTqrqllragLSPSK---------IDR-IFITHLHGD 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966416724 197 HIHGLTFF----------KPLYhpgnlfnFYGPpqgvKSVHELLSGLMDGIYFpvkidNLPSTISYHDLMADQN--FKID 264
Cdd:cd07717   63 HILGLPGLlstmsllgrtEPLT-------IYGP----KGLKEFLETLLRLSAS-----RLPYPIEVHELEPDPGlvFEDD 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966416724 265 NIKIATIALQHPCATYGYKIQyNNKIISYITDNelydksyhlynaDFVHNLIQFTMDSDILIVDCAFTDEEYDSGRVcWG 344
Cdd:cd07717  127 GFTVTAFPLDHRVPCFGYRFE-EGRKIAYLGDT------------RPCEGLVELAKGADLLIHEATFLDDDAEKAKE-TG 192

                        250       260
                 ....*....|....*....|.
gi 966416724 345 HSCPRQISEFAYLTNAKQLIL 365
Cdd:cd07717  193 HSTAKQAAEIAKKAGVKKLVL 213
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 129-329 1.15e-12

uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as tRNase Z or 3' tRNase) catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors. Two forms of RNase Z exist in eukaryotes, one long (ELAC2) and one short form (ELAC1), the former may have resulted from a duplication of the shorter enzyme. Only the short form exists in bacteria. Members of this bacterial 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: 293802 [Multi-domain]  Cd Length: 175  Bit Score: 65.93  E-value: 1.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966416724 129 GMTGAFPAPGkdfvkygGHTSC--VTLNFVNermIILDAGSGIipLGNelIIKNQNPIEAD-IFISHEHWDHI---HGLT 202
Cdd:cd07716    6 GCSGSYPGPG-------GACSGylLEADGFR---ILLDCGSGV--LSR--LQRYIDPEDLDaVVLSHLHPDHCadlGVLQ 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966416724 203 F---FKPLYHPGNLFNFYGPPQGVKSVHELLSglmdgiyfpvkidnLPSTISYHDLMADQNFKIDNIKIATIALQHPCAT 279
Cdd:cd07716   72 YarrYHPRGARKPPLPLYGPAGPAERLAALYG--------------LEDVFDFHPIEPGEPLEIGPFTITFFRTVHPVPC 137

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 966416724 280 YGYKIQYNNKIISYITDNELYDksyhlynadfvhNLIQFTMDSDILIVDC 329
Cdd:cd07716  138 YAMRIEDGGKVLVYTGDTGYCD------------ELVEFARGADLLLCEA 175
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 183-365 3.03e-12

Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and is related to pfam00753.


Pssm-ID: 432732 [Multi-domain]  Cd Length: 196  Bit Score: 65.02  E-value: 3.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966416724  183 PIEAdIFISHEHWDHIHGLTFFKPLYHpgnlFNFYGPPqgvkSVHELLSGlmdgiYFPVKIDNLPSTISYHDLMADQNFK 262
Cdd:pfam12706  28 PIDA-VLLTHDHYDHLAGLLDLREGRP----RPLYAPL----GVLAHLRR-----NFPYLFLLEHYGVRVHEIDWGESFT 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966416724  263 ID--NIKIATIALQH---------PCATYGYKIQYNNKIISYITDNELYDKSyhlynadfvhnLIQFTMDSDILIVDCAF 331
Cdd:pfam12706  94 VGdgGLTVTATPARHgsprgldpnPGDTLGFRIEGPGKRVYYAGDTGYFPDE-----------IGERLGGADLLLLDGGA 162

                         170       180       190
                  ....*....|....*....|....*....|....
gi 966416724  332 TDEEYDSGrvcWGHSCPRQISEFAYLTNAKQLIL 365
Cdd:pfam12706 163 WRDDEMIH---MGHMTPEEAVEAAADLGARRKVL 193
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 188-329 5.60e-11

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; 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. Some members of this subgroup are named as octanoyltransferase (also known as lipoate-protein ligase B).


Pssm-ID: 293837 [Multi-domain]  Cd Length: 193  Bit Score: 61.34  E-value: 5.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966416724 188 IFISHEHWDHIHGLT----FFKPLYHPGNLfnfYGPPQGVKSVHEllsglMDGIYFPVKIDNLPSTISYHDLMADQNFKI 263
Cdd:cd16279   70 VLLTHAHADHIHGLDdlrpFNRLQQRPIPV---YASEETLDDLKR-----RFPYFFAATGGGGVPKLDLHIIEPDEPFTI 141

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966416724 264 DNIKIATIALQH-PCATYGYKIqyNNkiISYITD-NELYDKSYhlynaDFVHNLiqftmdsDILIVDC 329
Cdd:cd16279  142 GGLEITPLPVLHgKLPSLGFRF--GD--FAYLTDvSEIPEESL-----EKLRGL-------DVLILDA 193
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 124-365 1.42e-09

ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of endonuclease or exonuclease activity, and differs in different species. Member of this family are ribonuclease Z, a tRNA 3-prime endonuclease that processes tRNAs to prepare for addition of CCA. In species where all tRNA sequences already have the CCA tail, such as E. coli, the need for such an enzyme is unclear. Protein similar to the E. coli enzyme, matched by TIGRFAMs model TIGR02649, are designated ribonuclease BN. [Transcription, RNA processing]


Pssm-ID: 274246 [Multi-domain]  Cd Length: 299  Bit Score: 58.77  E-value: 1.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966416724  124 DIEFWGMTGAFPAPGKdfvkyggHTSCVTLNFVNERmIILDAGSG------IIPLGNELIIKnqnpieadIFISHEHWDH 197
Cdd:TIGR02651   1 EITFLGTGGGVPTKER-------NLPSIALKLNGEL-WLFDCGEGtqrqmlRSGISPMKIDR--------IFITHLHGDH 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966416724  198 IHGLtffkplyhPGNL--FNF---------YGPPqGVKsvhELLSGLMDGIYFpvkidNLPSTISYHDLMADQN-FKIDN 265
Cdd:TIGR02651  65 ILGL--------PGLLstMSFqgrkepltiYGPP-GIK---EFIETSLRVSYT-----YLNYPIKIHEIEEGGLvFEDDG 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966416724  266 IKIATIALQHPCATYGYKIQY---------------------------NNKIISYItDNELYDKSYHL----------YN 308
Cdd:TIGR02651 128 FKVEAFPLDHSIPSLGYRFEEkdrpgkfdrekakelgippgplygklkRGETVTLI-DGRIIDPEDVLgpprkgrkiaYT 206

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966416724  309 AD--FVHNLIQFTMDSDILIVDCAFTDEE----YDSgrvcwGHSCPRQISEFAYLTNAKQLIL 365
Cdd:TIGR02651 207 GDtrPCEEVIEFAKNADLLIHEATFLDEDkklaKEY-----GHSTAAQAAEIAKEANVKRLIL 264
PhnP-like_MBL-fold cd07736
phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase ...
 156-329 2.01e-08

phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase domain; Escherichia coli PhnP catalyzes the hydrolysis of 5-phospho-D-ribose-1,2-cyclic phosphate to D-ribose-1,5-bisphosphate, a step in the C-P lyase pathway. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily. 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: 293822 [Multi-domain]  Cd Length: 186  Bit Score: 53.78  E-value: 2.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966416724 156 VNERMIILDAGSgiIPLGNELiikNQNPIEAdIFISHEHWDHIHGLtfFKPLYHPGNLFNFYGPPQGVksvhellsGLMD 235
Cdd:cd07736   44 VDGERILLDAGL--TDLAERF---PPGSIDA-ILLTHFHMDHVQGL--FHLRWGVGDPIPVYGPPDPQ--------GCAD 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966416724 236 GIYFPVKIDNLPSTISYhdlmadQNFKIDNIKIATIALQHPCATYGYKIQYNNKIISYITDNE-LYDKSYhlynadfvhn 314
Cdd:cd07736  108 LFKHPGILDFQPLVAPF------QSFELGGLKITPLPLNHSKPTFGYLLESGGKRLAYLTDTLgLPEETL---------- 171

                        170
                 ....*....|....*..
gi 966416724 315 liQFTMDS--DILIVDC 329
Cdd:cd07736  172 --EFLKQQqpDVLVLDC 186
metallo-hydrolase-like_MBL-fold cd07741
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 182-365 2.37e-07

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) 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: 293827 [Multi-domain]  Cd Length: 212  Bit Score: 51.04  E-value: 2.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966416724 182 NPIEAD-IFISHEHWDH-------IHGLTF--FKPLYHpgnlfnFYGPpqgvKSVhelLSGlmDGIYFPVKIDNLPSTIS 251
Cdd:cd07741   50 DPTKLDaIILSHRHLDHsndanvlIEAMTEggFKKRGT------LLAP----EDA---LNG--EPVVLLYYHRRKLEEIE 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966416724 252 YhdLMADQNFKIDNIKIATIALQHPCA-TYGYKIQYNNKIISYITDNELYDKsyhlynadfvhnLIQFTMDSDILIVDCA 330
Cdd:cd07741  115 I--LEEGDEYELGGIKIEATRHKHSDPtTYGFIFRTSDKKIGYISDTRYFEE------------LIEYYSNCDVLIINVT 180

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 966416724 331 FTDeeydsGRVCWGHSCPRQISEFAYLTNAKQLIL 365
Cdd:cd07741  181 RPR-----PRKGVDHLSVEDVEKILKEIKPKLAIL 210
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 156-293 2.50e-07

Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold metallo-hydrolase domain; Arylsulfatase (also known as aryl-sulfate sulfohydrolase, EC 3.1.6.1). Pseudoalteromonas carrageenovora arylsulfatase AtsA may function as a glycosulfohydrolase involved with desulfation of sulfated polysaccharides, which catalyzes hydrolysis of the arylsulfate ester bond, producing the aryl compounds and inorganic sulfate. CD also includes some sequences annotated as ribonucleases. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily.


Pssm-ID: 293805 [Multi-domain]  Cd Length: 193  Bit Score: 50.59  E-value: 2.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966416724 156 VNERMIILDAGSGI--------IPLGNeliiknqnpIEAdIFISHEHWDHIHGL-TFFKPLYHPGNL--FNFYGPPqGVK 224
Cdd:cd07719   25 VGGRVYLVDAGSGVvrrlaqagLPLGD---------LDA-VFLTHLHSDHVADLpALLLTAWLAGRKtpLPVYGPP-GTR 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966416724 225 svhELLSGLM-----DGIYFPVKIDNLPSTISY----HDLMADQ-NFKIDNIKIATIALQHP--CATYGYKIQYNNKIIS 292
Cdd:cd07719   94 ---ALVDGLLaayalDIDYRARIGDEGRPDPGAlvevHEIAAGGvVYEDDGVKVTAFLVDHGpvPPALAYRFDTPGRSVV 170


                 .
gi 966416724 293 Y 293
Cdd:cd07719  171 F 171
class_II_PDE_MBL-fold cd07735
class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium ...
 145-349 3.99e-07

class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium discoideum PDE1 and PDE7, and related proteins; MBL-fold metallo-hydrolase domain; Cyclic nucleotide phosphodiesterases (PDEs) decompose the second messengers cyclic adenosine and guanosine 3',5'-monophosphate (cAMP and cGMP, respectively). Saccharomyces cerevisiae PDE1 and Dictyostelium discoideum PDE1 and PDE7, have dual cAMP/cGMP specificity. 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: 293821  Cd Length: 259  Bit Score: 51.06  E-value: 3.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966416724 145 GGHTSCVTLNFVNERMII-LDAGSGIiplgNELIIKNQNPIEA---------------DIFISHEHWDHIHGLTFFKPly 208
Cdd:cd07735   14 EGNTSSFLLDPAGSDGDIlLDAGTGV----GALSLEEMFNDILfpsqkaayelyqrirHYLITHAHLDHIAGLPLLSP-- 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966416724 209 hpgNLFNFYGPPqgvKSVH---ELLSGLMDGIY-------FPVKIDNLPSTISYHDLMADQNFKIDNIKIATIALQH--P 276
Cdd:cd07735   88 ---NDGGQRGSP---KTIYglpETIDALKKHIFnwviwpdFTSIPSGKYPYLRLEPIEPEYPIALTGLSVTAFPVSHgvP 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966416724 277 CATyGYKIQYNNKIISYITDNELYDKSYHLYNADFVHNLIQFTMDS-DILIVDCAFTDEEYDSGRvcWGHSCPR 349
Cdd:cd07735  162 VST-AFLIRDGGDSFLFFGDTGPDSVSKSPRLDALWRALAPLIPKKlKAIIIECSFPNSRPDALL--YGHLTPK 232
PDE1 COG5212
cAMP phosphodiesterase [Signal transduction mechanisms];
145-349 5.62e-07

cAMP phosphodiesterase [Signal transduction mechanisms];


Pssm-ID: 444071 [Multi-domain]  Cd Length: 300  Bit Score: 50.73  E-value: 5.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966416724 145 GGHTSCVTLNFVNERMIILDAGSGI--IPLGNELIIKNQNP------IEAdIFISHEHWDHIHGLTFFKPLYHPgnlFNF 216
Cdd:COG5212   26 GNLTTYLLRPLGSDDYVLLDAGTVVsgLELAEQKGAFKGRQgyvlehIKG-YLISHAHLDHIAGLPILSPDDSP---KTI 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966416724 217 YGPPQGVKSVHELlsglmdgiYFPVKI----DNLPS-----TISYHDLMADQNFKIDN--IKIATIALQHPCATYGYKIQ 285
Cdd:COG5212  102 YALPETIDALRNH--------YFNWVIwpdfTDIGSaphlpKYRYVPLKPGQTFPLGGtgLRVTAFPLSHSVPSSAFLIE 173

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966416724 286 YNNKIISYITD-----NELYDKSYHLYNAdfVHNLIQfTMDSDILIVDCAFTDEEYDSGRVcwGHSCPR 349
Cdd:COG5212  174 SGGGAFLYSGDtgpdeVEKSTNLDALWEA--LAPLVR-SKKLKAIIIEVSFPNEQPDALLF--GHLTPA 237
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 161-335 8.29e-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) 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: 293826 [Multi-domain]  Cd Length: 194  Bit Score: 46.10  E-value: 8.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966416724 161 IILDAGSGIIPLGNELIIkNQNPIEAdIFISHEHWDHIHGLTFF-----------KPLyhpgnlfNFYGPPqGVKsvhEL 229
Cdd:cd07740   28 FLIDCGASSLIALKRAGI-DPNAIDA-IFITHLHGDHFGGLPFFlldaqfvakrtRPL-------TIAGPP-GLR---ER 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966416724 230 LSGLMDgIYFPVKIDNLPS-TISYHDLMADQNFKIDNIKIATIALQHP--CATYGYKIQYNNKIISYITDNELYDksyhl 306
Cdd:cd07740   95 LRRAME-ALFPGSSKVPRRfDLEVIELEPGEPTTLGGVTVTAFPVVHPsgALPLALRLEAAGRVLAYSGDTEWTD----- 168

                        170       180
                 ....*....|....*....|....*....
gi 966416724 307 ynadfvhNLIQFTMDSDILIVDCAFTDEE 335
Cdd:cd07740  169 -------ALVPLARGADLFICECYFFEKK 190
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
 18-102 1.51e-05

phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response regulators (PRRs); Two-component systems (TCSs) involving a sensor and a response regulator are used by bacteria to adapt to changing environments. Processes regulated by two-component systems in bacteria include sporulation, pathogenicity, virulence, chemotaxis, and membrane transport. Response regulators (RRs) share the common phosphoacceptor REC domain and different effector/output domains such as DNA, RNA, ligand-binding, protein-binding, or enzymatic domains. Response regulators regulate transcription, post-transcription or post-translation, or have functions such as methylesterases, adenylate or diguanylate cyclase, c-di-GMP-specific phosphodiesterases, histidine kinases, serine/threonine protein kinases, and protein phosphatases, depending on their output domains. The function of some output domains are still unknown. TCSs are found in all three domains of life - bacteria, archaea, and eukaryotes, however, the presence and abundance of particular RRs vary between the lineages. Archaea encode very few RRs with DNA-binding output domains; most are stand-alone REC domains. Among eukaryotes, TCSs are found primarily in protozoa, fungi, algae, and green plants. REC domains function as phosphorylation-mediated switches within RRs, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381085 [Multi-domain]  Cd Length: 99  Bit Score: 43.37  E-value: 1.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966416724  18 DPNIIGLITNELKTSGHITSSTDNVEDALMQVNKFKPDYVLIDQQIP-------TEKIKELCKsnKYKVIILS-LDPSNK 89
Cdd:cd00156    6 DPAIRELLKSLLEREGYEVDTAADGEEALELLREERPDLVLLDLMMPgmdglelLRKLRELPP--DIPVIVLTaKADEED 83

                         90
                 ....*....|...
gi 966416724  90 NINPYKLGAHGCI 102
Cdd:cd00156   84 AVRALELGADDYL 96
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 161-296 2.70e-05

uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold metallo hydrolase domain; Includes the uncharacterized Bacillus subtilis YycJ 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: 293819 [Multi-domain]  Cd Length: 151  Bit Score: 43.79  E-value: 2.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966416724 161 IILDAGSGIIPLGNELIIKNQNP--IEAdIFISHEHWDHIHGLtffkplyhpGNLFNFYGPPqgVKSVHELLSGlmdgiy 238
Cdd:cd07733   21 LLIDAGLSGRKITGRLAEIGRDPedIDA-ILVTHEHADHIKGL---------GVLARKYNVP--IYATAGTLRA------ 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966416724 239 FPVKIDNLPSTiSYHDLMADQNFKIDNIKIATIALQH----PCatyGYKIQYNNKIISYITD 296
Cdd:cd07733   83 MERKVGLIDVD-QKQIFEPGETFSIGDFDVESFGVSHdaadPV---GYRFEEGGRRFGMLTD 140
PRK00055 PRK00055
ribonuclease Z; Reviewed
 123-365 2.95e-05

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 45.17  E-value: 2.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966416724 123 IDIEFWGMTGAFPAPGKdfvkyggHTSCVTLNFvNERMIILDAGSGIIplgNELIIKNQNP--IEAdIFISHEHWDHIHG 200
Cdd:PRK00055   2 MELTFLGTGSGVPTPTR-------NVSSILLRL-GGELFLFDCGEGTQ---RQLLKTGIKPrkIDK-IFITHLHGDHIFG 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966416724 201 LtffkplyhPGNL--FNF---------YGPPqGVKsvhELLSGLMDGIYF----------PVKID-------NLPSTISY 252
Cdd:PRK00055  70 L--------PGLLstRSLsgrtepltiYGPK-GIK---EFVETLLRASGSlgyriaekdkPGKLDaeklkalGVPPGPLF 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966416724 253 HDLMADQNFKIDNIKIATIAlqhpcatYGYKIQYNNKIISYITDNELYDksyhlynadfvhNLIQFTMDSDILIVDCAFT 332
Cdd:PRK00055 138 GKLKRGEDVTLEDGRIINPA-------DVLGPPRKGRKVAYCGDTRPCE------------ALVELAKGADLLVHEATFG 198

                        250       260       270
                 ....*....|....*....|....*....|...
gi 966416724 333 DEEYDSGRvCWGHSCPRQISEFAYLTNAKQLIL 365
Cdd:PRK00055 199 DEDEELAK-EYGHSTARQAAEIAKEAGVKRLIL 230
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 161-246 7.65e-05

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: 43.43  E-value: 7.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966416724 161 IILDAGSGIIPLGNELIIKNQNPIEAdIFISHEHWDHIHGLTFFKPLY------HPGNLFNFYGPpqgvksvHELLSGLM 234
Cdd:cd06262   23 ILIDPGAGALEKILEAIEELGLKIKA-ILLTHGHFDHIGGLAELKEAPgapvyiHEADAELLEDP-------ELNLAFFG 94

                         90
                 ....*....|..
gi 966416724 235 DGIYFPVKIDNL 246
Cdd:cd06262   95 GGPLPPPEPDIL 106
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
 12-102 1.40e-04

Response regulator receiver domain; This domain receives the signal from the sensor partner in bacterial two-component systems. It is usually found N-terminal to a DNA binding effector domain.


Pssm-ID: 395025 [Multi-domain]  Cd Length: 111  Bit Score: 40.98  E-value: 1.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966416724   12 IYLVHQDPNIIGLITNELKTSGHITSSTDNVEDALMQVNKFKPDYVLIDQQIP-------TEKIKELckSNKYKVIILSL 84
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPgmdglelLKRIRRR--DPTTPVIILTA 78

                          90       100
                  ....*....|....*....|
gi 966416724   85 --DPSNKnINPYKLGAHGCI 102
Cdd:pfam00072  79 hgDEDDA-VEALEAGADDFL 97
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
 5-83 2.18e-04

CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator Spo0F [Signal transduction mechanisms];


Pssm-ID: 440547 [Multi-domain]  Cd Length: 128  Bit Score: 40.99  E-value: 2.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966416724   5 TQQRPLPIYLVHQDPNIIGLITNELKTSGHITSSTDNVEDALMQVNKFKPDYVLIDQQIP-------TEKIKELCKSNKY 77
Cdd:COG0784    1 PPLGGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPgmdglelLRRIRALPRLPDI 80


                 ....*.
gi 966416724  78 KVIILS 83
Cdd:COG0784   81 PIIALT 86
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
 12-102 7.26e-04

DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, and a Fis-type DNA-binding domains [Signal transduction mechanisms];


Pssm-ID: 441806 [Multi-domain]  Cd Length: 418  Bit Score: 41.49  E-value: 7.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966416724  12 IYLVHQDPNIIGLITNELKTSGHITSSTDNVEDALMQVNKFKPDYVLIDQQIP-------TEKIKELCKSNkyKVIILSL 84
Cdd:COG2204    5 ILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPgmdglelLRELRALDPDL--PVILLTG 82

                         90
                 ....*....|....*....
gi 966416724  85 DPSNKN-INPYKLGAHGCI 102
Cdd:COG2204   83 YGDVETaVEAIKAGAFDYL 101
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 157-268 7.50e-04

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: 40.23  E-value: 7.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966416724   157 NERMIILDAGSG-IIPLGNELIIKNQNPIEAdIFISHEHWDHIHGLTFFKPLYHPgnlfNFYGPPQGVKSVHELLSGLMD 235
Cdd:smart00849   8 DGGAILIDTGPGeAEDLLAELKKLGPKKIDA-IILTHGHPDHIGGLPELLEAPGA----PVYAPEGTAELLKDLLALLGE 82

                           90       100       110
                   ....*....|....*....|....*....|...
gi 966416724   236 GIYFPVKIDNlpstisYHDLMADQNFKIDNIKI 268
Cdd:smart00849  83 LGAEAEPAPP------DRTLKDGDELDLGGGEL 109
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
 12-64 1.28e-03

phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family response regulators; Streptococcus agalactiae NsrR is a lantibiotic resistance-associated response regulator and is part of the nisin resistance operon. It is a member of the NsrRK two-component system (TCS) that is involved in the regulation of lantibiotic resistance genes such as a membrane-associated lipoprotein of LanI, and the nsr gene cluster which encodes for the resistance protein NSR and the ABC transporter NsrFP, both conferring resistance against nisin. This subfamily also includes Staphylococcus epidermidis GraR, part of the GraR/GraS TCS involved in resistance against cationic antimicrobial peptides, and Bacillus subtilis BceR, part of the BceS/BceR TCS involved in the regulation of bacitracin resistance. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381143 [Multi-domain]  Cd Length: 113  Bit Score: 38.42  E-value: 1.28e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 966416724  12 IYLVHQDPNIIGLITNELKTSGHITSSTDNVEDALMQVNKFKPDYVLIDQQIP 64
Cdd:cd18159    1 ILIVEDDETIASLLKKHLEKWGYEVVLIEDFEDVLEEFLQFKPDLVLLDINLP 53
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
156-211 1.29e-03

Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];


Pssm-ID: 440850  Cd Length: 273  Bit Score: 40.25  E-value: 1.29e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966416724 156 VNERMIILDAGSGiiplgnELIIKN-----QNPIEAD-IFISHEHWDHIHGLTFF------KPLY-HPG 211
Cdd:COG1237   29 TEGKRILFDTGQS------DVLLKNaeklgIDLSDIDaVVLSHGHYDHTGGLPALlelnpkAPVYaHPD 91
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
 12-83 2.05e-03

phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and similar domains; Thermotoga maritima contains a two-component signal transduction system (TCS) composed of the ThkA sensory histidine kinase (HK) and its cognate response regulator (RR) TrrA; the specific function of the system is unknown. TCSs couple environmental stimuli to adaptive responses. TrrA is a stand-alone RR containing only a REC domain with no output/effector domain. The REC domain itself functions as an effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381106 [Multi-domain]  Cd Length: 113  Bit Score: 37.59  E-value: 2.05e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966416724  12 IYLVHQDPNIIGLITNELKTSGHITSSTDNVEDALMQVNKFKPDYVLIDQQIP-------TEKIKElcKSNKYKVIILS 83
Cdd:cd17554    3 ILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLESEDPDLVILDIKMPgmdgletLRKIRE--KKPDLPVIICT 79
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
 13-83 2.15e-03

phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus subtilis PhoP (BsPhoP) is part of the PhoPR two-component system that participates in a signal transduction network that controls adaptation of the bacteria to phosphate deficiency by regulating (activating or repressing) genes of the Pho regulon upon phosphorylation by PhoR. When activated, PhoPR directs expression of phosphate scavenging enzymes, lowers synthesis of the phosphate-rich wall teichoic acid (WTA) and initiates synthesis of teichuronic acid, a non-phosphate containing replacement anionic polymer. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381164 [Multi-domain]  Cd Length: 116  Bit Score: 37.64  E-value: 2.15e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966416724  13 YLVHQDPNIIGLITNELKTSGHITSSTDNVEDALMQVNKFKPDYVLIDQQIPTEKIKELCK----SNKYK---VIILS 83
Cdd:cd19937    1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRilrsDPKTSsipIIMLT 78
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 188-258 9.50e-03

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. Some members of this subgroup are annotated as GumP protein.


Pssm-ID: 293816 [Multi-domain]  Cd Length: 250  Bit Score: 37.63  E-value: 9.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966416724 188 IFISHEHWDHIHGLTFFK--PLY-HPG--NLFNFYGPPQGVKSvhELL-SGLMDGIYFPVKIDNLPSTI----SYHDLMA 257
Cdd:cd07730   87 VILSHLHWDHIGGLSDFPnaRLIvGPGakEALRPPGYPSGFLP--ELLpSDFEGRLVRWEEDDFLWVPLgpfpRALDLFG 164


                 .
gi 966416724 258 D 258
Cdd:cd07730  165 D 165
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
 12-83 9.65e-03

phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The transcription factor PhoB is a component of the PhoR/PhoB two-component system, a key regulatory protein network that facilitates response to inorganic phosphate (Pi) starvation conditions by turning on the phosphate (pho) regulon whose products are involved in phosphorus uptake and metabolism. PhoB is a member of the OmpR family of DNA-binding response regulators that contains REC and winged helix-turn-helix (wHTH) DNA-binding output effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381133 [Multi-domain]  Cd Length: 118  Bit Score: 35.69  E-value: 9.65e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966416724  12 IYLVHQDPNIIGLITNELKTSGHITSSTDNVEDALMQVNKFKPDYVLIDQQIP----TEKIKELCKSNKYK---VIILS 83
Cdd:cd17618    3 ILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVEPRPDLILLDWMLPggsgIQFIRRLKRDEMTRdipIIMLT 81
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH