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Conserved domains on  [gi|501489457|ref|WP_012497922|]
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HD domain-containing protein [Rhodopseudomonas palustris]

Protein Classification

HD domain-containing protein( domain architecture ID 13402576)

HD domain-containing protein, likely a metal dependent phosphohydrolase; may contain response regulator PleD

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HDGYP COG2206
HD-GYP domain, c-di-GMP phosphodiesterase class II (or its inactivated variant) [Signal ...
180-360 1.83e-38

HD-GYP domain, c-di-GMP phosphodiesterase class II (or its inactivated variant) [Signal transduction mechanisms];


:

Pssm-ID: 441808 [Multi-domain]  Cd Length: 316  Bit Score: 139.72  E-value: 1.83e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501489457 180 ILKAIKRSSLREWLATVGRHHDESYRLCLFATGFAVAFAQYLGMREEDQRRLTRAALLYDVGKAYVDVSALDNLDNLKGD 259
Cdd:COG2206  121 ELDELLPDALLALLAALDAKDPYTYGHSVRVAVLALALARELGLSEEELEDLGLAALLHDIGKIGIPDEILNKPGKLTDE 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501489457 260 ALRKYREHPRLGYEALVAEGSFPrETLDVVLHHHELLDGSGYPDGLHGDQIADIVRITTIVDLFASLVAPRKNHTPMSPL 339
Cdd:COG2206  201 EFEIIKKHPEYGYEILKKLPGLS-EVAEIVLQHHERLDGSGYPRGLKGEEIPLLARILAVADVYDALTSDRPYRKALSPE 279
                        170       180
                 ....*....|....*....|..
gi 501489457 340 QAFITMENM-GGKIDQRLLQAF 360
Cdd:COG2206  280 EALEELRKGaGTQFDPELVEAF 301
PleD super family cl34659
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
15-159 3.98e-04

Two-component response regulator, PleD family, consists of two REC domains and a diguanylate cyclase (GGDEF) domain [Signal transduction mechanisms, Transcription];


The actual alignment was detected with superfamily member COG3706:

Pssm-ID: 442920 [Multi-domain]  Cd Length: 179  Bit Score: 40.66  E-value: 3.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501489457  15 RRRLLLASDRRDGSVDIAGILAS----VAEVETVPTA------HLPDApardlsgIVVDINLRSADSVQLVR--RKLLGG 82
Cdd:COG3706    1 PARILVVDDDPTNRKLLRRLLEAagyeVVEAADGEEAlellqeHRPDL-------ILLDLEMPDMDGLELCRrlRADPRT 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501489457  83 AYqpMPRLFVLADELHHGSMQAWALGATDTIARPFDPRDLLQRVRSA-----------FPDPSEDTATARAEALSDGVTA 151
Cdd:COG3706   74 AD--IPIIFLTALDDEEDRARALEAGADDYLTKPFDPEELLARVDLVaryggeefailLPGTDLEGALAVAERIREAVAE 151

                 ....*...
gi 501489457 152 AHKVLVKI 159
Cdd:COG3706  152 LPSLRVTV 159
 
Name Accession Description Interval E-value
HDGYP COG2206
HD-GYP domain, c-di-GMP phosphodiesterase class II (or its inactivated variant) [Signal ...
180-360 1.83e-38

HD-GYP domain, c-di-GMP phosphodiesterase class II (or its inactivated variant) [Signal transduction mechanisms];


Pssm-ID: 441808 [Multi-domain]  Cd Length: 316  Bit Score: 139.72  E-value: 1.83e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501489457 180 ILKAIKRSSLREWLATVGRHHDESYRLCLFATGFAVAFAQYLGMREEDQRRLTRAALLYDVGKAYVDVSALDNLDNLKGD 259
Cdd:COG2206  121 ELDELLPDALLALLAALDAKDPYTYGHSVRVAVLALALARELGLSEEELEDLGLAALLHDIGKIGIPDEILNKPGKLTDE 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501489457 260 ALRKYREHPRLGYEALVAEGSFPrETLDVVLHHHELLDGSGYPDGLHGDQIADIVRITTIVDLFASLVAPRKNHTPMSPL 339
Cdd:COG2206  201 EFEIIKKHPEYGYEILKKLPGLS-EVAEIVLQHHERLDGSGYPRGLKGEEIPLLARILAVADVYDALTSDRPYRKALSPE 279
                        170       180
                 ....*....|....*....|..
gi 501489457 340 QAFITMENM-GGKIDQRLLQAF 360
Cdd:COG2206  280 EALEELRKGaGTQFDPELVEAF 301
HD_5 pfam13487
HD domain; HD domains are metal dependent phosphohydrolases.
254-316 1.19e-12

HD domain; HD domains are metal dependent phosphohydrolases.


Pssm-ID: 433249 [Multi-domain]  Cd Length: 64  Bit Score: 62.23  E-value: 1.19e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501489457  254 DNLKGDALRKYREHPRLGYEALVAEGSFPRETLDVVLHHHELLDGSGYPDGLHGDQIADIVRI 316
Cdd:pfam13487   1 GTLTPEEREIINRHPEHTARLLSTLPRLPKEVAEIIAQHHERLDGSGYPRGLKGEEIPLGARI 63
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
207-333 4.15e-12

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 63.13  E-value: 4.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501489457 207 CLFATGFAVAFAQYLGMREEDQRRLTRAALLYDVGKAYVDVSALDNLDNLKGDalrkyreHPRLGYEALVA------EGS 280
Cdd:cd00077    7 SLRVAQLARRLAEELGLSEEDIELLRLAALLHDIGKPGTPDAITEEESELEKD-------HAIVGAEILREllleevIKL 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 501489457 281 FPRETLDVVLHHHELLDGSGYPDGLHGDQIADIVRITTIVDLFASLVAPRKNH 333
Cdd:cd00077   80 IDELILAVDASHHERLDGLGYPDGLKGEEITLEARIVKLADRLDALRRDSREK 132
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
15-159 3.98e-04

Two-component response regulator, PleD family, consists of two REC domains and a diguanylate cyclase (GGDEF) domain [Signal transduction mechanisms, Transcription];


Pssm-ID: 442920 [Multi-domain]  Cd Length: 179  Bit Score: 40.66  E-value: 3.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501489457  15 RRRLLLASDRRDGSVDIAGILAS----VAEVETVPTA------HLPDApardlsgIVVDINLRSADSVQLVR--RKLLGG 82
Cdd:COG3706    1 PARILVVDDDPTNRKLLRRLLEAagyeVVEAADGEEAlellqeHRPDL-------ILLDLEMPDMDGLELCRrlRADPRT 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501489457  83 AYqpMPRLFVLADELHHGSMQAWALGATDTIARPFDPRDLLQRVRSA-----------FPDPSEDTATARAEALSDGVTA 151
Cdd:COG3706   74 AD--IPIIFLTALDDEEDRARALEAGADDYLTKPFDPEELLARVDLVaryggeefailLPGTDLEGALAVAERIREAVAE 151

                 ....*...
gi 501489457 152 AHKVLVKI 159
Cdd:COG3706  152 LPSLRVTV 159
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
207-331 2.07e-03

Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic nucleotide phosphodiesterases (PDEc). This profile/HMM does not detect HD homologues in bacterial glycine aminoacyl-tRNA synthetases (beta subunit).


Pssm-ID: 214679 [Multi-domain]  Cd Length: 124  Bit Score: 37.66  E-value: 2.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501489457   207 CLFATGFAVAFAQYLGMREEDqrRLTRAALLYDVGKAYVDVSALDNLDNLkgdalrkyREHPRLGYEALVAEGsFPRETL 286
Cdd:smart00471   9 SLRVAQLAAALAEELGLLDIE--LLLLAALLHDIGKPGTPDSFLVKTSVL--------EDHHFIGAEILLEEE-EPRILE 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 501489457   287 DV----VLHHHELLDGSGypdglhGDQIADIVRITTIVDLFASLVAPRK 331
Cdd:smart00471  78 EIlrtaILSHHERPDGLR------GEPITLEARIVKVADRLDALRADRR 120
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
56-127 2.22e-03

phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator RpfG and similar proteins; Cyclic di-GMP phosphodiesterase response regulator RpfG, together with sensory/regulatory protein RpfC, constitute a two-component system implicated in sensing and responding to the diffusible signal factor (DSF) that is essential for cell-cell signaling. RpfC is a hybrid sensor/histidine kinase that phosphorylates and activates RpfG, which degrades cyclic di-GMP to GMP, leading to the activation of Clp, a global transcriptional regulator that regulates a large set of genes in the DSF pathway. RpfG contains a CheY-like receiver domain attached to a histidine-aspartic acid-glycine-tyrosine-proline (HD-GYP) cyclic di-GMP phosphodiesterase domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381103 [Multi-domain]  Cd Length: 118  Bit Score: 37.42  E-value: 2.22e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501489457  56 DLsgIVVDINLRSADSVQLVR--RKLLGGAYQPMprLFVLADELHHGSMQAWALGATDTIARPFDPRDLLQRVR 127
Cdd:cd17551   47 DL--ILLDYMMPGMDGLEFIRrlRALPGLEDVPI--VMITADTDREVRLRALEAGATDFLTKPFDPVELLARVR 116
PRK13856 PRK13856
two-component response regulator VirG; Provisional
60-129 2.93e-03

two-component response regulator VirG; Provisional


Pssm-ID: 172377 [Multi-domain]  Cd Length: 241  Bit Score: 38.64  E-value: 2.93e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501489457  60 IVVDINLRSADSVQLVRRKllgGAYQPMPRLFVLADELHHG-SMQAWALGATDTIARPFDPRDLLQRVRSA 129
Cdd:PRK13856  49 VVVDLNLGREDGLEIVRSL---ATKSDVPIIIISGDRLEEAdKVVALELGATDFIAKPFGTREFLARIRVA 116
 
Name Accession Description Interval E-value
HDGYP COG2206
HD-GYP domain, c-di-GMP phosphodiesterase class II (or its inactivated variant) [Signal ...
180-360 1.83e-38

HD-GYP domain, c-di-GMP phosphodiesterase class II (or its inactivated variant) [Signal transduction mechanisms];


Pssm-ID: 441808 [Multi-domain]  Cd Length: 316  Bit Score: 139.72  E-value: 1.83e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501489457 180 ILKAIKRSSLREWLATVGRHHDESYRLCLFATGFAVAFAQYLGMREEDQRRLTRAALLYDVGKAYVDVSALDNLDNLKGD 259
Cdd:COG2206  121 ELDELLPDALLALLAALDAKDPYTYGHSVRVAVLALALARELGLSEEELEDLGLAALLHDIGKIGIPDEILNKPGKLTDE 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501489457 260 ALRKYREHPRLGYEALVAEGSFPrETLDVVLHHHELLDGSGYPDGLHGDQIADIVRITTIVDLFASLVAPRKNHTPMSPL 339
Cdd:COG2206  201 EFEIIKKHPEYGYEILKKLPGLS-EVAEIVLQHHERLDGSGYPRGLKGEEIPLLARILAVADVYDALTSDRPYRKALSPE 279
                        170       180
                 ....*....|....*....|..
gi 501489457 340 QAFITMENM-GGKIDQRLLQAF 360
Cdd:COG2206  280 EALEELRKGaGTQFDPELVEAF 301
HD_5 pfam13487
HD domain; HD domains are metal dependent phosphohydrolases.
254-316 1.19e-12

HD domain; HD domains are metal dependent phosphohydrolases.


Pssm-ID: 433249 [Multi-domain]  Cd Length: 64  Bit Score: 62.23  E-value: 1.19e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501489457  254 DNLKGDALRKYREHPRLGYEALVAEGSFPRETLDVVLHHHELLDGSGYPDGLHGDQIADIVRI 316
Cdd:pfam13487   1 GTLTPEEREIINRHPEHTARLLSTLPRLPKEVAEIIAQHHERLDGSGYPRGLKGEEIPLGARI 63
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
207-333 4.15e-12

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 63.13  E-value: 4.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501489457 207 CLFATGFAVAFAQYLGMREEDQRRLTRAALLYDVGKAYVDVSALDNLDNLKGDalrkyreHPRLGYEALVA------EGS 280
Cdd:cd00077    7 SLRVAQLARRLAEELGLSEEDIELLRLAALLHDIGKPGTPDAITEEESELEKD-------HAIVGAEILREllleevIKL 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 501489457 281 FPRETLDVVLHHHELLDGSGYPDGLHGDQIADIVRITTIVDLFASLVAPRKNH 333
Cdd:cd00077   80 IDELILAVDASHHERLDGLGYPDGLKGEEITLEARIVKLADRLDALRRDSREK 132
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
15-159 3.98e-04

Two-component response regulator, PleD family, consists of two REC domains and a diguanylate cyclase (GGDEF) domain [Signal transduction mechanisms, Transcription];


Pssm-ID: 442920 [Multi-domain]  Cd Length: 179  Bit Score: 40.66  E-value: 3.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501489457  15 RRRLLLASDRRDGSVDIAGILAS----VAEVETVPTA------HLPDApardlsgIVVDINLRSADSVQLVR--RKLLGG 82
Cdd:COG3706    1 PARILVVDDDPTNRKLLRRLLEAagyeVVEAADGEEAlellqeHRPDL-------ILLDLEMPDMDGLELCRrlRADPRT 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501489457  83 AYqpMPRLFVLADELHHGSMQAWALGATDTIARPFDPRDLLQRVRSA-----------FPDPSEDTATARAEALSDGVTA 151
Cdd:COG3706   74 AD--IPIIFLTALDDEEDRARALEAGADDYLTKPFDPEELLARVDLVaryggeefailLPGTDLEGALAVAERIREAVAE 151

                 ....*...
gi 501489457 152 AHKVLVKI 159
Cdd:COG3706  152 LPSLRVTV 159
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
207-331 2.07e-03

Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic nucleotide phosphodiesterases (PDEc). This profile/HMM does not detect HD homologues in bacterial glycine aminoacyl-tRNA synthetases (beta subunit).


Pssm-ID: 214679 [Multi-domain]  Cd Length: 124  Bit Score: 37.66  E-value: 2.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501489457   207 CLFATGFAVAFAQYLGMREEDqrRLTRAALLYDVGKAYVDVSALDNLDNLkgdalrkyREHPRLGYEALVAEGsFPRETL 286
Cdd:smart00471   9 SLRVAQLAAALAEELGLLDIE--LLLLAALLHDIGKPGTPDSFLVKTSVL--------EDHHFIGAEILLEEE-EPRILE 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 501489457   287 DV----VLHHHELLDGSGypdglhGDQIADIVRITTIVDLFASLVAPRK 331
Cdd:smart00471  78 EIlrtaILSHHERPDGLR------GEPITLEARIVKVADRLDALRADRR 120
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
56-127 2.22e-03

phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator RpfG and similar proteins; Cyclic di-GMP phosphodiesterase response regulator RpfG, together with sensory/regulatory protein RpfC, constitute a two-component system implicated in sensing and responding to the diffusible signal factor (DSF) that is essential for cell-cell signaling. RpfC is a hybrid sensor/histidine kinase that phosphorylates and activates RpfG, which degrades cyclic di-GMP to GMP, leading to the activation of Clp, a global transcriptional regulator that regulates a large set of genes in the DSF pathway. RpfG contains a CheY-like receiver domain attached to a histidine-aspartic acid-glycine-tyrosine-proline (HD-GYP) cyclic di-GMP phosphodiesterase domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381103 [Multi-domain]  Cd Length: 118  Bit Score: 37.42  E-value: 2.22e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501489457  56 DLsgIVVDINLRSADSVQLVR--RKLLGGAYQPMprLFVLADELHHGSMQAWALGATDTIARPFDPRDLLQRVR 127
Cdd:cd17551   47 DL--ILLDYMMPGMDGLEFIRrlRALPGLEDVPI--VMITADTDREVRLRALEAGATDFLTKPFDPVELLARVR 116
PRK13856 PRK13856
two-component response regulator VirG; Provisional
60-129 2.93e-03

two-component response regulator VirG; Provisional


Pssm-ID: 172377 [Multi-domain]  Cd Length: 241  Bit Score: 38.64  E-value: 2.93e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501489457  60 IVVDINLRSADSVQLVRRKllgGAYQPMPRLFVLADELHHG-SMQAWALGATDTIARPFDPRDLLQRVRSA 129
Cdd:PRK13856  49 VVVDLNLGREDGLEIVRSL---ATKSDVPIIIISGDRLEEAdKVVALELGATDFIAKPFGTREFLARIRVA 116
HD pfam01966
HD domain; HD domains are metal dependent phosphohydrolases.
213-324 3.08e-03

HD domain; HD domains are metal dependent phosphohydrolases.


Pssm-ID: 460398 [Multi-domain]  Cd Length: 110  Bit Score: 36.83  E-value: 3.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501489457  213 FAVAFAQYLGmrEEDQRRLTRAALLYDVGKAYVdvsaldnldNLKGDALRKYREHPRLGYEALVAEGSFPRET--LDVVL 290
Cdd:pfam01966  11 LARELAEELG--ELDRELLLLAALLHDIGKGPF---------GDEKPEFEIFLGHAVVGAEILRELEKRLGLEdvLKLIL 79
                          90       100       110
                  ....*....|....*....|....*....|....
gi 501489457  291 HHHELLDGSGYPdglhgDQIADIVRITTIVDLFA 324
Cdd:pfam01966  80 EHHESWEGAGYP-----EEISLEARIVKLADRLD 108
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
60-130 3.14e-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: 37.25  E-value: 3.14e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501489457  60 IVVDINLRSADSVQLVRRKLLGGAYQPMPRLFVLADELHHGSMQAWALGATDTIARPFDPRDLLQRVRSAF 130
Cdd:cd19937   45 IILDLMLPGIDGLEVCRILRSDPKTSSIPIIMLTAKGEEFDKVLGLELGADDYITKPFSPRELLARVKAVL 115
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
60-200 3.73e-03

Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains [Signal transduction mechanisms];


Pssm-ID: 442663 [Multi-domain]  Cd Length: 224  Bit Score: 38.22  E-value: 3.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501489457  60 IVVDINLRSADSVQLVR--RKLLGGAYqpMPRLFVLADELHHGSMQAWALGATDTIARPFDPRDLLQRVRSAFPDPSEDT 137
Cdd:COG3437   54 ILLDVRMPGMDGFELLRllRADPSTRD--IPVIFLTALADPEDRERALEAGADDYLTKPFDPEELLARVRNALELRRLQR 131
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501489457 138 ATARAEALSDGVTAAHKV-LVKIFERLHGKP--LTFQDVMQAEGPILKAIKRSSLREWLATVGRHH 200
Cdd:COG3437  132 ELDDLVLYLKLAAPLHDIgKIGIPDAILLKPgkLTPEEWEITHAHIGAEILSGSLLPLLQLAAEIH 197
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
60-163 6.75e-03

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: 38.41  E-value: 6.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501489457  60 IVVDINLRSADSVQLVRRklLGGAYQPMPRLFVLADELHHGSMQAWALGATDTIARPFDPRDLLQRVRSAFPDPSEDTAT 139
Cdd:COG2204   50 VLLDLRMPGMDGLELLRE--LRALDPDLPVILLTGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRREN 127
                         90       100
                 ....*....|....*....|....
gi 501489457 140 ARAEALSdGVTAAHKVLVKIFERL 163
Cdd:COG2204  128 AEDSGLI-GRSPAMQEVRRLIEKV 150
 
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.
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