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Conserved domains on  [gi|2679308885|ref|WP_333563109|]
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MULTISPECIES: HD domain-containing phosphohydrolase [unclassified Aeromonas]

Protein Classification

HD-GYP domain-containing protein( domain architecture ID 11454351)

HD-GYP domain-containing protein functions as a cyclic nucleotide phosphodiesterase, such as Borreliella burgdorferi cyclic di-GMP phosphodiesterase PdeB that catalyzes the hydrolysis of cyclic diguanylate (c-di-GMP) to GMP

CATH:  1.10.3210.10
Gene Ontology:  GO:0004112|GO:0046872
PubMed:  11008484|9868367

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 ...
 1-86 4.06e-36

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: 124.70  E-value: 4.06e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2679308885   1 MEFLRLAKEIACYHHEKWDGTGYPYGLHGDEIPLSARLMALADVYDALISKRCYKAAMSHQEVVPIILAGRGNHFDPDIT 80
Cdd:COG2206   219 LPGLSEVAEIVLQHHERLDGSGYPRGLKGEEIPLLARILAVADVYDALTSDRPYRKALSPEEALEELRKGAGTQFDPELV 298


                  ....*.
gi 2679308885  81 DAFARI 86
Cdd:COG2206   299 EAFIKV 304
 
Name Accession Description Interval E-value
HDGYP COG2206
HD-GYP domain, c-di-GMP phosphodiesterase class II (or its inactivated variant) [Signal ...
 1-86 4.06e-36

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: 124.70  E-value: 4.06e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2679308885   1 MEFLRLAKEIACYHHEKWDGTGYPYGLHGDEIPLSARLMALADVYDALISKRCYKAAMSHQEVVPIILAGRGNHFDPDIT 80
Cdd:COG2206   219 LPGLSEVAEIVLQHHERLDGSGYPRGLKGEEIPLLARILAVADVYDALTSDRPYRKALSPEEALEELRKGAGTQFDPELV 298


                  ....*.
gi 2679308885  81 DAFARI 86
Cdd:COG2206   299 EAFIKV 304
HD_5 pfam13487
HD domain; HD domains are metal dependent phosphohydrolases.
 1-39 1.91e-12

HD domain; HD domains are metal dependent phosphohydrolases.


Pssm-ID: 433249 [Multi-domain]  Cd Length: 64  Bit Score: 57.22  E-value: 1.91e-12
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2679308885   1 MEFLRLAKEIACYHHEKWDGTGYPYGLHGDEIPLSARLM 39
Cdd:pfam13487  26 PRLPKEVAEIIAQHHERLDGSGYPRGLKGEEIPLGARIL 64
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
 2-55 4.04e-08

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 48.10  E-value: 4.04e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2679308885   2 EFLRLAKEIACYHHEKWDGTGYPYGLHGDEIPLSARLMALADVYDALISKRCYK 55
Cdd:cd00077    79 LIDELILAVDASHHERLDGLGYPDGLKGEEITLEARIVKLADRLDALRRDSREK 132
 
Name Accession Description Interval E-value
HDGYP COG2206
HD-GYP domain, c-di-GMP phosphodiesterase class II (or its inactivated variant) [Signal ...
 1-86 4.06e-36

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: 124.70  E-value: 4.06e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2679308885   1 MEFLRLAKEIACYHHEKWDGTGYPYGLHGDEIPLSARLMALADVYDALISKRCYKAAMSHQEVVPIILAGRGNHFDPDIT 80
Cdd:COG2206   219 LPGLSEVAEIVLQHHERLDGSGYPRGLKGEEIPLLARILAVADVYDALTSDRPYRKALSPEEALEELRKGAGTQFDPELV 298


                  ....*.
gi 2679308885  81 DAFARI 86
Cdd:COG2206   299 EAFIKV 304
HD_5 pfam13487
HD domain; HD domains are metal dependent phosphohydrolases.
 1-39 1.91e-12

HD domain; HD domains are metal dependent phosphohydrolases.


Pssm-ID: 433249 [Multi-domain]  Cd Length: 64  Bit Score: 57.22  E-value: 1.91e-12
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2679308885   1 MEFLRLAKEIACYHHEKWDGTGYPYGLHGDEIPLSARLM 39
Cdd:pfam13487  26 PRLPKEVAEIIAQHHERLDGSGYPRGLKGEEIPLGARIL 64
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
 2-55 4.04e-08

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 48.10  E-value: 4.04e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2679308885   2 EFLRLAKEIACYHHEKWDGTGYPYGLHGDEIPLSARLMALADVYDALISKRCYK 55
Cdd:cd00077    79 LIDELILAVDASHHERLDGLGYPDGLKGEEITLEARIVKLADRLDALRRDSREK 132
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
 2-56 9.07e-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: 33.99  E-value: 9.07e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2679308885   2 EFLRLAKEIacyhHEKWDGTGypyglhgdeipLSARlmaladvyDALISKRCYKA 56
Cdd:COG3437   188 PLLQLAAEI----HERWDGSG-----------LSAR--------DALTSKKLEEA 219
 
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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