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Conserved domains on  [gi|2261231207|emb|CAH2572231|]
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putative protein AZC_3085 [Planktothrix rubescens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG5001 super family cl34859
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 6-86 3.07e-32

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


The actual alignment was detected with superfamily member COG5001:

Pssm-ID: 444025 [Multi-domain]  Cd Length: 678  Bit Score: 117.95  E-value: 3.07e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261231207   6 PIDTLKIDRSFVNRIGSNQGEIELIRTIITLAHGLGMDVVAEGIETKSQLNQLSLLGCEWGQGFLFSKSLNTTDATQYIA 85
Cdd:COG5001   595 PVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRELGCDYAQGYLFSRPLPAEELEALLR 674


                  .
gi 2261231207  86 D 86
Cdd:COG5001   675 A 675
 
Name Accession Description Interval E-value
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 6-86 3.07e-32

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: 117.95  E-value: 3.07e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261231207   6 PIDTLKIDRSFVNRIGSNQGEIELIRTIITLAHGLGMDVVAEGIETKSQLNQLSLLGCEWGQGFLFSKSLNTTDATQYIA 85
Cdd:COG5001   595 PVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRELGCDYAQGYLFSRPLPAEELEALLR 674


                  .
gi 2261231207  86 D 86
Cdd:COG5001   675 A 675
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 6-76 8.82e-31

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: 108.79  E-value: 8.82e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2261231207   6 PIDTLKIDRSFVNRIGSNQGEIELIRTIITLAHGLGMDVVAEGIETKSQLNQLSLLGCEWGQGFLFSKSLN 76
Cdd:cd01948   167 PVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLP 237
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
 3-76 1.04e-27

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


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 100.75  E-value: 1.04e-27
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2261231207    3 RLNPIDTLKIDRSFVNRIGSNQGEIELIRTIITLAHGLGMDVVAEGIETKSQLNQLSLLGCEWGQGFLFSKSLN 76
Cdd:smart00052 166 KRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLP 239
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 1-73 2.85e-23

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: 89.30  E-value: 2.85e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2261231207   1 MNRLN--PIDTLKIDRSFVNRIGSNQGEIELIRTIITLAHGLGMDVVAEGIETKSQLNQLSLLGCEWGQGFLFSK 73
Cdd:pfam00563 160 LSYLLrlPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSK 234
PRK13561 PRK13561
putative diguanylate cyclase; Provisional
 6-75 1.50e-15

putative diguanylate cyclase; Provisional


Pssm-ID: 184143 [Multi-domain]  Cd Length: 651  Bit Score: 70.51  E-value: 1.50e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261231207   6 PIDTLKIDRSFVNRIGSNQgeiELIRTIITLAHGLGMDVVAEGIETKSQLNQLSLLGCEWGQGFLFSKSL 75
Cdd:PRK13561  572 PIDVLKIDKMFVDGLPEDD---SMVAAIIMLAQSLNLQVIAEGVETEAQRDWLLKAGVGIAQGFLFARAL 638
 
Name Accession Description Interval E-value
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 6-86 3.07e-32

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: 117.95  E-value: 3.07e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261231207   6 PIDTLKIDRSFVNRIGSNQGEIELIRTIITLAHGLGMDVVAEGIETKSQLNQLSLLGCEWGQGFLFSKSLNTTDATQYIA 85
Cdd:COG5001   595 PVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRELGCDYAQGYLFSRPLPAEELEALLR 674


                  .
gi 2261231207  86 D 86
Cdd:COG5001   675 A 675
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 6-76 8.82e-31

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: 108.79  E-value: 8.82e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2261231207   6 PIDTLKIDRSFVNRIGSNQGEIELIRTIITLAHGLGMDVVAEGIETKSQLNQLSLLGCEWGQGFLFSKSLN 76
Cdd:cd01948   167 PVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLP 237
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
 3-76 1.04e-27

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


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 100.75  E-value: 1.04e-27
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2261231207    3 RLNPIDTLKIDRSFVNRIGSNQGEIELIRTIITLAHGLGMDVVAEGIETKSQLNQLSLLGCEWGQGFLFSKSLN 76
Cdd:smart00052 166 KRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLP 239
EAL COG2200
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ...
 6-85 2.93e-27

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: 103.71  E-value: 2.93e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261231207   6 PIDTLKIDRSFVNRIGSNQGEIELIRTIITLAHGLGMDVVAEGIETKSQLNQLSLLGCEWGQGFLFSKSLNTTDATQYIA 85
Cdd:COG2200   497 PPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFGRPLPLEELEALLR 576
YjcC COG4943
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ...
 6-86 2.35e-23

Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal transduction mechanisms];


Pssm-ID: 443970 [Multi-domain]  Cd Length: 528  Bit Score: 92.29  E-value: 2.35e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261231207   6 PIDTLKIDRSFVNRIGSNQGEIELIRTIITLAHGLGMDVVAEGIETKSQLNQLSLLGCEWGQGFLFSKSLNTTDATQYIA 85
Cdd:COG4943   439 PVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQYGQGWLFAKPLPAEEFIAWLA 518


                  .
gi 2261231207  86 D 86
Cdd:COG4943   519 A 519
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 1-73 2.85e-23

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: 89.30  E-value: 2.85e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2261231207   1 MNRLN--PIDTLKIDRSFVNRIGSNQGEIELIRTIITLAHGLGMDVVAEGIETKSQLNQLSLLGCEWGQGFLFSK 73
Cdd:pfam00563 160 LSYLLrlPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSK 234
PRK13561 PRK13561
putative diguanylate cyclase; Provisional
 6-75 1.50e-15

putative diguanylate cyclase; Provisional


Pssm-ID: 184143 [Multi-domain]  Cd Length: 651  Bit Score: 70.51  E-value: 1.50e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261231207   6 PIDTLKIDRSFVNRIGSNQgeiELIRTIITLAHGLGMDVVAEGIETKSQLNQLSLLGCEWGQGFLFSKSL 75
Cdd:PRK13561  572 PIDVLKIDKMFVDGLPEDD---SMVAAIIMLAQSLNLQVIAEGVETEAQRDWLLKAGVGIAQGFLFARAL 638
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 6-91 2.92e-15

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 69.41  E-value: 2.92e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261231207   6 PIDTLKIDRSFVNRIGSNQGEIELIRTIITLAHGLGMDVVAEGIETKSQLNQLSLLGCEWGQGFLFSKSLNTTDATQYIA 85
Cdd:PRK11359  713 PVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQFEMLRKIHCRVIQGYFFSRPLPAEEIPGWMS 792


                  ....*.
gi 2261231207  86 DFFPFK 91
Cdd:PRK11359  793 SVLPLK 798
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
6-73 6.20e-14

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 65.86  E-value: 6.20e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2261231207   6 PIDTLKIDRSFVNRIGSNQGEIELIRTIITLAHGLGMDVVAEGIETKSQLNQLSLLGCEWGQGFLFSK 73
Cdd:PRK10060  576 PIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVNERQGFLFAK 643
PRK10551 PRK10551
cyclic di-GMP phosphodiesterase;
8-92 3.15e-13

cyclic di-GMP phosphodiesterase;


Pssm-ID: 182541 [Multi-domain]  Cd Length: 518  Bit Score: 63.86  E-value: 3.15e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261231207   8 DTLKIDRSFVNRIGSNQGEIELIRTIITLAHGLGMDVVAEGIETKSQLNQLSLLGCEWGQGFLFSKSLNTTDATQYIADF 87
Cdd:PRK10551  434 DYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRERGVNFLQGYWISRPLPLEDFVRWLKEP 513


                  ....*
gi 2261231207  88 FPFKW 92
Cdd:PRK10551  514 YTPQW 518
PRK11829 PRK11829
biofilm formation regulator HmsP; Provisional
 6-88 2.01e-12

biofilm formation regulator HmsP; Provisional


Pssm-ID: 183329 [Multi-domain]  Cd Length: 660  Bit Score: 61.50  E-value: 2.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261231207   6 PIDTLKIDRSFVNRIGSNQGeieLIRTIITLAHGLGMDVVAEGIETKSQLNQLSLLGCEWGQGFLFSKSLNTTDatqYIA 85
Cdd:PRK11829  577 PIHMIKLDKSFVKNLPEDDA---IARIISCVSDVLKVRVMAEGVETEEQRQWLLEHGIQCGQGFLFSPPLPRAE---FEA 650


                  ...
gi 2261231207  86 DFF 88
Cdd:PRK11829  651 QYF 653
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
 5-68 4.59e-07

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 46.20  E-value: 4.59e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2261231207    5 NPIDTLKIDRSFVNRIGSNQGEIELIRTIITLAHGLGMDVVAEGIETKSQLNQLSLLGCEWGQG 68
Cdd:PRK09776  1008 FMADYLKLDGELVANLHGNLMDEMLISIIQGHAQRLGMKTIAGPVELPLVLDTLSGIGVDLAYG 1071
YuxH COG3434
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ...
 7-73 1.37e-05

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


Pssm-ID: 442660 [Multi-domain]  Cd Length: 407  Bit Score: 41.71  E-value: 1.37e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2261231207   7 IDTLKIDrsfVNRIGsnqgeIELIRTIITLAHGLGMDVVAEGIETKSQLNQLSLLGCEWGQGFLFSK 73
Cdd:COG3434   132 ADIIKID---VLALD-----LEELAELVARLKRYGIKLLAEKVETREEFELCKELGFDLFQGYFFSK 190
PRK11059 PRK11059
regulatory protein CsrD; Provisional
 6-74 7.79e-05

regulatory protein CsrD; Provisional


Pssm-ID: 236833 [Multi-domain]  Cd Length: 640  Bit Score: 39.85  E-value: 7.79e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2261231207   6 PIDTLKIDRSFVNRI---GSNQgeiELIRTIITLAHGLGMDVVAEGIETKSQLNQLSLLGCEWGQGFLFSKS 74
Cdd:PRK11059  568 NVELIKLHPSLVRNIhkrTENQ---LFVRSLVGACAGTETQVFATGVESREEWQTLQELGVSGGQGDFFAES 636
 
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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