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Conserved domains on  [gi|2490891628|dbj|BDU70821|]
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hypothetical protein GETHOR_29220 [Geothrix oryzae]

Protein Classification

EAL domain-containing protein( domain architecture ID 10112612)

EAL domain-containing protein may act as a cyclic diguanylate phosphodiesterase

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
9-242 6.19e-36

EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues and is also known as domain of unknown function 2 (DUF2). The EAL domain has been shown to stimulate degradation of a second messenger, cyclic di-GMP, and is a good candidate for a diguanylate phosphodiesterase function. Together with the GGDEF domain, EAL might be involved in regulating cell surface adhesiveness in bacteria.


:

Pssm-ID: 238923 [Multi-domain]  Cd Length: 240  Bit Score: 128.43  E-value: 6.19e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891628   9 QLAIAQN-LQAFFQPILELRGDvlRLTAFEGFA--HGAD------DSFLGTPDLMGApgDGAMDRTLLDVACltRVLRAG 79
Cdd:cd01948     4 RRALERGeFELYYQPIVDLRTG--RIVGYEALLrwRHPEgglispAEFIPLAEETGL--IVELGRWVLEEAC--RQLARW 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891628  80 GELPDSTLLSLNVHTSTLaLLPEFPVFLSECAAEAGIPLTRLILELNVQSGSGQGTEHLDVLEDLRAHGVGVALDDVGVR 159
Cdd:cd01948    78 QAGGPDLRLSVNLSARQL-RDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891628 160 ETNLDQILEIRPDILKLSPLLTRGLLRDPRRQAILEALVDMTRKMGGRVLAKNLESVEDFRIARWMGVTLLQGYLFGVPG 239
Cdd:cd01948   157 YSSLSYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPL 236

                  ...
gi 2490891628 240 PIA 242
Cdd:cd01948   237 PAE 239
 
Name Accession Description Interval E-value
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
9-242 6.19e-36

EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues and is also known as domain of unknown function 2 (DUF2). The EAL domain has been shown to stimulate degradation of a second messenger, cyclic di-GMP, and is a good candidate for a diguanylate phosphodiesterase function. Together with the GGDEF domain, EAL might be involved in regulating cell surface adhesiveness in bacteria.


Pssm-ID: 238923 [Multi-domain]  Cd Length: 240  Bit Score: 128.43  E-value: 6.19e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891628   9 QLAIAQN-LQAFFQPILELRGDvlRLTAFEGFA--HGAD------DSFLGTPDLMGApgDGAMDRTLLDVACltRVLRAG 79
Cdd:cd01948     4 RRALERGeFELYYQPIVDLRTG--RIVGYEALLrwRHPEgglispAEFIPLAEETGL--IVELGRWVLEEAC--RQLARW 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891628  80 GELPDSTLLSLNVHTSTLaLLPEFPVFLSECAAEAGIPLTRLILELNVQSGSGQGTEHLDVLEDLRAHGVGVALDDVGVR 159
Cdd:cd01948    78 QAGGPDLRLSVNLSARQL-RDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891628 160 ETNLDQILEIRPDILKLSPLLTRGLLRDPRRQAILEALVDMTRKMGGRVLAKNLESVEDFRIARWMGVTLLQGYLFGVPG 239
Cdd:cd01948   157 YSSLSYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPL 236

                  ...
gi 2490891628 240 PIA 242
Cdd:cd01948   237 PAE 239
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
5-238 2.95e-34

EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues. The EAL domain is a good candidate for a diguanylate phosphodiesterase function. The domain contains many conserved acidic residues that could participate in metal binding and might form the phosphodiesterase active site.


Pssm-ID: 425752 [Multi-domain]  Cd Length: 235  Bit Score: 123.97  E-value: 2.95e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891628   5 QSAQQLAIAQNLQAFFQPILELRGDvlRLTAFEGFA---HGAD-----DSFLGTPDLMGApgDGAMDRTLLDVACltRVL 76
Cdd:pfam00563   2 RALRRALENGEFVLYYQPIVDLRTG--RVVGYEALLrwqHPDGglispARFLPLAEELGL--IAELDRWVLEQAL--ADL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891628  77 RAGGELPDsTLLSLNVHTSTLALlPEFPVFLSECAAEAGIPLTRLILELNVQSGSGQGTEHLDVLEDLRAHGVGVALDDV 156
Cdd:pfam00563  76 AQLQLGPD-IKLSINLSPASLAD-PGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDF 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891628 157 GVRETNLDQILEIRPDILKLSPLLTRGLLRDPRRQAILEALVDMTRKMGGRVLAKNLESVEDFRIARWMGVTLLQGYLFG 236
Cdd:pfam00563 154 GTGYSSLSYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFS 233

                  ..
gi 2490891628 237 VP 238
Cdd:pfam00563 234 KP 235
EAL COG2200
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ...
11-242 2.46e-30

EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) [Signal transduction mechanisms];


Pssm-ID: 441802 [Multi-domain]  Cd Length: 576  Bit Score: 119.12  E-value: 2.46e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891628  11 AIAQN-LQAFFQPILELRGDvlRLTAFEGFA--HGADDSFLGTPDLMGAPGD-GAMDRtlLDVACLTRVLRAGGELPDST 86
Cdd:COG2200   336 ALEEGeLRLYYQPIVDLRTG--RVVGYEALLrwRHPDGGLISPAEFIPAAERsGLIVE--LDRWVLERALRQLARWPERG 411
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891628  87 L---LSLNVHTSTLaLLPEFPVFLSECAAEAGIPLTRLILELNVQSGSGQGTEHLDVLEDLRAHGVGVALDDVGVRETNL 163
Cdd:COG2200   412 LdlrLSVNLSARSL-LDPDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRIALDDFGTGYSSL 490
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2490891628 164 DQILEIRPDILKLSPLLTRGLLRDPRRQAILEALVDMTRKMGGRVLAKNLESVEDFRIARWMGVTLLQGYLFGVPGPIA 242
Cdd:COG2200   491 SYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFGRPLPLE 569
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
9-243 1.97e-26

Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 103.45  E-value: 1.97e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891628    9 QLAIAQN-LQAFFQPILELRGdvLRLTAFEGFA--HGADDSFLGtPD----------LMGApgdgaMDRTLLDVAClTRV 75
Cdd:smart00052   5 RQALENGqFLLYYQPIVSLRT--GRLVGVEALIrwQHPEGGIIS-PDefiplaeetgLIVP-----LGRWVLEQAC-QQL 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891628   76 LRAGGELPDSTLLSLNVHTSTLALlPEFPVFLSECAAEAGIPLTRLILELnvqsgsgqgTEHL---------DVLEDLRA 146
Cdd:smart00052  76 AEWQAQGPPPLLISINLSARQLIS-PDLVPRVLELLEETGLPPQRLELEI---------TESVlldddesavATLQRLRE 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891628  147 HGVGVALDDVGVRETNLDQILEIRPDILKLSPLLTRGLLRDPRRQAILEALVDMTRKMGGRVLAKNLESVEDFRIARWMG 226
Cdd:smart00052 146 LGVRIALDDFGTGYSSLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLG 225
                          250
                   ....*....|....*..
gi 2490891628  227 VTLLQGYLFGVPGPIAL 243
Cdd:smart00052 226 CDYGQGYLFSRPLPLDD 242
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
101-240 4.68e-12

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 65.95  E-value: 4.68e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891628 101 PEFPVFLSECAAEAGIPLTRLILELNVQSGSGQGTEHLDVLEDLRAHGVGVALDDVGVRETNLDQILEIRPDILKLSPLL 180
Cdd:PRK11359  644 NQLPNQVSDAMQAWGIDGHQLTVEITESMMMEHDTEIFKRIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSF 723
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891628 181 TRGLLRDPRRQAILEALVDMTRKMGGRVLAKNLESVEDFRIARWMGVTLLQGYLFGVPGP 240
Cdd:PRK11359  724 VDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQFEMLRKIHCRVIQGYFFSRPLP 783
 
Name Accession Description Interval E-value
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
9-242 6.19e-36

EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues and is also known as domain of unknown function 2 (DUF2). The EAL domain has been shown to stimulate degradation of a second messenger, cyclic di-GMP, and is a good candidate for a diguanylate phosphodiesterase function. Together with the GGDEF domain, EAL might be involved in regulating cell surface adhesiveness in bacteria.


Pssm-ID: 238923 [Multi-domain]  Cd Length: 240  Bit Score: 128.43  E-value: 6.19e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891628   9 QLAIAQN-LQAFFQPILELRGDvlRLTAFEGFA--HGAD------DSFLGTPDLMGApgDGAMDRTLLDVACltRVLRAG 79
Cdd:cd01948     4 RRALERGeFELYYQPIVDLRTG--RIVGYEALLrwRHPEgglispAEFIPLAEETGL--IVELGRWVLEEAC--RQLARW 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891628  80 GELPDSTLLSLNVHTSTLaLLPEFPVFLSECAAEAGIPLTRLILELNVQSGSGQGTEHLDVLEDLRAHGVGVALDDVGVR 159
Cdd:cd01948    78 QAGGPDLRLSVNLSARQL-RDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891628 160 ETNLDQILEIRPDILKLSPLLTRGLLRDPRRQAILEALVDMTRKMGGRVLAKNLESVEDFRIARWMGVTLLQGYLFGVPG 239
Cdd:cd01948   157 YSSLSYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPL 236

                  ...
gi 2490891628 240 PIA 242
Cdd:cd01948   237 PAE 239
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
5-238 2.95e-34

EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues. The EAL domain is a good candidate for a diguanylate phosphodiesterase function. The domain contains many conserved acidic residues that could participate in metal binding and might form the phosphodiesterase active site.


Pssm-ID: 425752 [Multi-domain]  Cd Length: 235  Bit Score: 123.97  E-value: 2.95e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891628   5 QSAQQLAIAQNLQAFFQPILELRGDvlRLTAFEGFA---HGAD-----DSFLGTPDLMGApgDGAMDRTLLDVACltRVL 76
Cdd:pfam00563   2 RALRRALENGEFVLYYQPIVDLRTG--RVVGYEALLrwqHPDGglispARFLPLAEELGL--IAELDRWVLEQAL--ADL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891628  77 RAGGELPDsTLLSLNVHTSTLALlPEFPVFLSECAAEAGIPLTRLILELNVQSGSGQGTEHLDVLEDLRAHGVGVALDDV 156
Cdd:pfam00563  76 AQLQLGPD-IKLSINLSPASLAD-PGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDF 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891628 157 GVRETNLDQILEIRPDILKLSPLLTRGLLRDPRRQAILEALVDMTRKMGGRVLAKNLESVEDFRIARWMGVTLLQGYLFG 236
Cdd:pfam00563 154 GTGYSSLSYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFS 233

                  ..
gi 2490891628 237 VP 238
Cdd:pfam00563 234 KP 235
EAL COG2200
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ...
11-242 2.46e-30

EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) [Signal transduction mechanisms];


Pssm-ID: 441802 [Multi-domain]  Cd Length: 576  Bit Score: 119.12  E-value: 2.46e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891628  11 AIAQN-LQAFFQPILELRGDvlRLTAFEGFA--HGADDSFLGTPDLMGAPGD-GAMDRtlLDVACLTRVLRAGGELPDST 86
Cdd:COG2200   336 ALEEGeLRLYYQPIVDLRTG--RVVGYEALLrwRHPDGGLISPAEFIPAAERsGLIVE--LDRWVLERALRQLARWPERG 411
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891628  87 L---LSLNVHTSTLaLLPEFPVFLSECAAEAGIPLTRLILELNVQSGSGQGTEHLDVLEDLRAHGVGVALDDVGVRETNL 163
Cdd:COG2200   412 LdlrLSVNLSARSL-LDPDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRIALDDFGTGYSSL 490
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2490891628 164 DQILEIRPDILKLSPLLTRGLLRDPRRQAILEALVDMTRKMGGRVLAKNLESVEDFRIARWMGVTLLQGYLFGVPGPIA 242
Cdd:COG2200   491 SYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFGRPLPLE 569
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
9-243 1.97e-26

Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 103.45  E-value: 1.97e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891628    9 QLAIAQN-LQAFFQPILELRGdvLRLTAFEGFA--HGADDSFLGtPD----------LMGApgdgaMDRTLLDVAClTRV 75
Cdd:smart00052   5 RQALENGqFLLYYQPIVSLRT--GRLVGVEALIrwQHPEGGIIS-PDefiplaeetgLIVP-----LGRWVLEQAC-QQL 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891628   76 LRAGGELPDSTLLSLNVHTSTLALlPEFPVFLSECAAEAGIPLTRLILELnvqsgsgqgTEHL---------DVLEDLRA 146
Cdd:smart00052  76 AEWQAQGPPPLLISINLSARQLIS-PDLVPRVLELLEETGLPPQRLELEI---------TESVlldddesavATLQRLRE 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891628  147 HGVGVALDDVGVRETNLDQILEIRPDILKLSPLLTRGLLRDPRRQAILEALVDMTRKMGGRVLAKNLESVEDFRIARWMG 226
Cdd:smart00052 146 LGVRIALDDFGTGYSSLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLG 225
                          250
                   ....*....|....*..
gi 2490891628  227 VTLLQGYLFGVPGPIAL 243
Cdd:smart00052 226 CDYGQGYLFSRPLPLDD 242
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
72-242 3.40e-17

Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain [Signal transduction mechanisms];


Pssm-ID: 444025 [Multi-domain]  Cd Length: 678  Bit Score: 81.36  E-value: 3.40e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891628  72 LTRVLRAGGELPDSTL--LSLNVHTSTLALL-PEFPVFLSECAAEAGIPLTRLILELnvqsgsgqgTEH---------LD 139
Cdd:COG5001   494 LREACRQLAAWQDAGLpdLRVAVNLSARQLRdPDLVDRVRRALAETGLPPSRLELEI---------TESalledpeeaLE 564
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891628 140 VLEDLRAHGVGVALDDVGVRETNLDQILEIRPDILKLSPLLTRGLLRDPRRQAILEALVDMTRKMGGRVLAKNLESVEDF 219
Cdd:COG5001   565 TLRALRALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQL 644
                         170       180
                  ....*....|....*....|...
gi 2490891628 220 RIARWMGVTLLQGYLFGVPGPIA 242
Cdd:COG5001   645 EFLRELGCDYAQGYLFSRPLPAE 667
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
101-240 4.68e-12

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 65.95  E-value: 4.68e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891628 101 PEFPVFLSECAAEAGIPLTRLILELNVQSGSGQGTEHLDVLEDLRAHGVGVALDDVGVRETNLDQILEIRPDILKLSPLL 180
Cdd:PRK11359  644 NQLPNQVSDAMQAWGIDGHQLTVEITESMMMEHDTEIFKRIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSF 723
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891628 181 TRGLLRDPRRQAILEALVDMTRKMGGRVLAKNLESVEDFRIARWMGVTLLQGYLFGVPGP 240
Cdd:PRK11359  724 VDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQFEMLRKIHCRVIQGYFFSRPLP 783
PRK13561 PRK13561
putative diguanylate cyclase; Provisional
88-246 1.11e-08

putative diguanylate cyclase; Provisional


Pssm-ID: 184143 [Multi-domain]  Cd Length: 651  Bit Score: 55.49  E-value: 1.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891628  88 LSLNVHTSTLALL-PEFPVFLSECAAEAGIPLTRLILELNVQSGSGQGTEHLDVLEDLRAHGVGVALDDVGVRETNLDQI 166
Cdd:PRK13561  486 LPLSVNLSALQLMhPNMVADMLELLTRYRIQPGTLILEVTESRRIDDPHAAVAILRPLRNAGVRVALDDFGMGYAGLRQL 565
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891628 167 LEIRP---DILKLSPLLTRGLlrdPRRQAILEALVDMTRKMGGRVLAknlESVEDFRIARWM---GVTLLQGYLFGVPGP 240
Cdd:PRK13561  566 QHMKSlpiDVLKIDKMFVDGL---PEDDSMVAAIIMLAQSLNLQVIA---EGVETEAQRDWLlkaGVGIAQGFLFARALP 639

                  ....*.
gi 2490891628 241 IALWKE 246
Cdd:PRK13561  640 IEIFEE 645
YuxH COG3434
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ...
136-241 1.19e-08

c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction mechanisms];


Pssm-ID: 442660 [Multi-domain]  Cd Length: 407  Bit Score: 55.19  E-value: 1.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891628 136 EHLDVLEDLRAHGVGVALDDVgVRETNLDQILEIrPDILKLSplltrgLLRDPRRQaiLEALVDMTRKMGGRVLAKNLES 215
Cdd:COG3434    99 ELLEALKELKEKGYRIALDDF-VLDPEWDPLLPL-ADIIKID------VLALDLEE--LAELVARLKRYGIKLLAEKVET 168
                          90       100
                  ....*....|....*....|....*.
gi 2490891628 216 VEDFRIARWMGVTLLQGYLFGVPGPI 241
Cdd:COG3434   169 REEFELCKELGFDLFQGYFFSKPEIL 194
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
51-243 1.08e-06

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 49.67  E-value: 1.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891628   51 PDLMGApgdgamdrtlLDVACLTRVLRAGGELPDSTLLSLNVHTSTLALL-PEFPVFLSECAAEAGIPLTRLILELNVQS 129
Cdd:PRK09776   899 PALMHA----------LDRRVIHEFFRQAAKAVASKGLSIALPLSVAGLSsPTLLPFLLEQLENSPLPPRLLHLEITETA 968
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891628  130 GSGQGTEHLDVLEDLRAHGVGVALDDVGVRETNLDQILEIRPDILKLSPLLTRGLLRDPRRQAILEALVDMTRKMGGRVL 209
Cdd:PRK09776   969 LLNHAESASRLVQKLRLAGCRVVLSDFGRGLSSFNYLKAFMADYLKLDGELVANLHGNLMDEMLISIIQGHAQRLGMKTI 1048
                          170       180       190
                   ....*....|....*....|....*....|....
gi 2490891628  210 AKNLESVEDFRIARWMGVTLLQGYLFGVPGPIAL 243
Cdd:PRK09776  1049 AGPVELPLVLDTLSGIGVDLAYGYAIARPQPLDL 1082
PRK11829 PRK11829
biofilm formation regulator HmsP; Provisional
88-240 6.13e-04

biofilm formation regulator HmsP; Provisional


Pssm-ID: 183329 [Multi-domain]  Cd Length: 660  Bit Score: 41.08  E-value: 6.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891628  88 LSLNVHTSTLA---LLPEFPVFLSECAAEAgiplTRLILELNVQSGSGQGTEHLDVLEDLRAHGVGVALDDVGVRETNLD 164
Cdd:PRK11829  493 LSVNISGLQVQnkqFLPHLKTLISHYHIDP----QQLLLEITETAQIQDLDEALRLLRELQGLGLLIALDDFGIGYSSLR 568
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2490891628 165 QILEIRP---DILKLSPLLTRGLlrdPRRQAILEALVDMTRKMGGRVLAKNLESVEDFRIARWMGVTLLQGYLFGVPGP 240
Cdd:PRK11829  569 YLNHLKSlpiHMIKLDKSFVKNL---PEDDAIARIISCVSDVLKVRVMAEGVETEEQRQWLLEHGIQCGQGFLFSPPLP 644
 
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.
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