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Conserved domains on  [gi|427711950|ref|YP_007060574|]
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HD-GYP domain-containing protein [Synechococcus sp. PCC 6312]

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List of domain hits

Name Accession Description Interval E-value
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
443-522 1.87e-06

Metal dependent phosphohydrolases with conserved 'HD' motif


:

Pssm-ID: 238032  Cd Length: 145  Bit Score: 46.56  E-value: 1.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427711950 443 TPQERLAIESHVTHTYEFLRRIPWTSSLK----DVPIIAYGHHERLNGTGYPLGIAD--IPLQTQMLTIADIYDALTAAD 516
Cdd:cd00077   50 TEEESELEKDHAIVGAEILRELLLEEVIKlideLILAVDASHHERLDGLGYPDGLKGeeITLEARIVKLADRLDALRRDS 129

                 ....*.
gi 427711950 517 RPYKKS 522
Cdd:cd00077  130 REKRRR 135
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
255-320 6.30e-05

Metal dependent phosphohydrolases with conserved 'HD' motif


:

Pssm-ID: 238032  Cd Length: 145  Bit Score: 41.94  E-value: 6.30e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 427711950 255 TAGHSERVADLTLRLAAEVndqagigafvgvGFDQRQLQELRYAALLHDFGKVGVPEVILSKEKKL 320
Cdd:cd00077    3 RFEHSLRVAQLARRLAEEL------------GLSEEDIELLRLAALLHDIGKPGTPDAITEEESEL 56
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
60-224 5.36e-12

GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl cyclases, phytochromes, FhlA and NifA. Adenylyl and guanylyl cyclases catalyse ATP and GTP to the second messengers cAMP and cGMP, respectively, these products up-regulating catalytic activity by binding to the regulatory GAF domain(s). The opposite hydrolysis reaction is catalysed by phosphodiesterase. cGMP-dependent 3',5'-cyclic phosphodiesterase catalyses the conversion of guanosine 3',5'-cyclic phosphate to guanosine 5'-phosphate. Here too, cGMP regulates catalytic activity by GAF-domain binding. Phytochromes are regulatory photoreceptors in plants and bacteria which exist in two thermally-stable states that are reversibly inter-convertible by light: the Pr state absorbs maximally in the red region of the spectrum, while the Pfr state absorbs maximally in the far-red region. This domain is also found in FhlA (formate hydrogen lyase transcriptional activator) and NifA, a transcriptional activator which is required for activation of most Nif operons which are directly involved in nitrogen fixation. NifA interacts with sigma-54.


:

Pssm-ID: 250726  Cd Length: 146  Bit Score: 63.37  E-value: 5.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427711950   60 NLSDLLTLILTKSREITCSDAGSVFLVDRQAHPPNLWfktaQNDTHPELSLHEFFIPLNaESLVGYVALTGEILNIPDAY 139
Cdd:pfam01590   1 DLEELLQTILEELRELLGADRVAIYLADADGLLLYLV----AGDGLSDIPLAARGLPLG-GGVVGEVIAGGNPIVVPDVQ 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427711950  140 EIP--QAETYQFNRSFDDNLGYRTRSVLVIPMqNAEGEIIGVLQLLNRKIRadikitpdnatdvtvPYSHWEEAILRSLA 217
Cdd:pfam01590  76 DDPrfRDLTALASDLPHFLRGLGIRSCLAVPL-KGGGELIGVLVLHSTSPR---------------AFTEEELELLQALA 139

                  ....*..
gi 427711950  218 SQAAVSI 224
Cdd:pfam01590 140 DQVAIAL 146
 
Name Accession Description Interval E-value
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
443-522 1.87e-06

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032  Cd Length: 145  Bit Score: 46.56  E-value: 1.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427711950 443 TPQERLAIESHVTHTYEFLRRIPWTSSLK----DVPIIAYGHHERLNGTGYPLGIAD--IPLQTQMLTIADIYDALTAAD 516
Cdd:cd00077   50 TEEESELEKDHAIVGAEILRELLLEEVIKlideLILAVDASHHERLDGLGYPDGLKGeeITLEARIVKLADRLDALRRDS 129

                 ....*.
gi 427711950 517 RPYKKS 522
Cdd:cd00077  130 REKRRR 135
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
255-320 6.30e-05

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032  Cd Length: 145  Bit Score: 41.94  E-value: 6.30e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 427711950 255 TAGHSERVADLTLRLAAEVndqagigafvgvGFDQRQLQELRYAALLHDFGKVGVPEVILSKEKKL 320
Cdd:cd00077    3 RFEHSLRVAQLARRLAEEL------------GLSEEDIELLRLAALLHDIGKPGTPDAITEEESEL 56
HD_5 pfam13487
HD domain; HD domains are metal dependent phosphohydrolases.
440-503 1.03e-15

HD domain; HD domains are metal dependent phosphohydrolases.


Pssm-ID: 257811  Cd Length: 63  Bit Score: 72.21  E-value: 1.03e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 427711950  440 GNLTPQERLAIESHVTHTYEFLRRIPWtssLKDVPIIAYGHHERLNGTGYPLGIA--DIPLQTQML 503
Cdd:pfam13487   1 GTLTPEERAIINEHPEQTARLLEKIPR---LPPVAEIIGHHHERLDGSGYPRGLKgdEIPLGARIL 63
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
60-224 5.36e-12

GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl cyclases, phytochromes, FhlA and NifA. Adenylyl and guanylyl cyclases catalyse ATP and GTP to the second messengers cAMP and cGMP, respectively, these products up-regulating catalytic activity by binding to the regulatory GAF domain(s). The opposite hydrolysis reaction is catalysed by phosphodiesterase. cGMP-dependent 3',5'-cyclic phosphodiesterase catalyses the conversion of guanosine 3',5'-cyclic phosphate to guanosine 5'-phosphate. Here too, cGMP regulates catalytic activity by GAF-domain binding. Phytochromes are regulatory photoreceptors in plants and bacteria which exist in two thermally-stable states that are reversibly inter-convertible by light: the Pr state absorbs maximally in the red region of the spectrum, while the Pfr state absorbs maximally in the far-red region. This domain is also found in FhlA (formate hydrogen lyase transcriptional activator) and NifA, a transcriptional activator which is required for activation of most Nif operons which are directly involved in nitrogen fixation. NifA interacts with sigma-54.


Pssm-ID: 250726  Cd Length: 146  Bit Score: 63.37  E-value: 5.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427711950   60 NLSDLLTLILTKSREITCSDAGSVFLVDRQAHPPNLWfktaQNDTHPELSLHEFFIPLNaESLVGYVALTGEILNIPDAY 139
Cdd:pfam01590   1 DLEELLQTILEELRELLGADRVAIYLADADGLLLYLV----AGDGLSDIPLAARGLPLG-GGVVGEVIAGGNPIVVPDVQ 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427711950  140 EIP--QAETYQFNRSFDDNLGYRTRSVLVIPMqNAEGEIIGVLQLLNRKIRadikitpdnatdvtvPYSHWEEAILRSLA 217
Cdd:pfam01590  76 DDPrfRDLTALASDLPHFLRGLGIRSCLAVPL-KGGGELIGVLVLHSTSPR---------------AFTEEELELLQALA 139

                  ....*..
gi 427711950  218 SQAAVSI 224
Cdd:pfam01590 140 DQVAIAL 146
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
60-234 1.75e-11

Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these domains in PDE6B result in autosomal recessive inheritance of retinitis pigmentosa.


Pssm-ID: 214500  Cd Length: 149  Bit Score: 62.01  E-value: 1.75e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427711950    60 NLSDLLTLILTKSREITCSDAGSVFLVDRQAHPpNLWFKTAQNDTHPELSLHeffIPLnAESLVGYVALTGEILNIPDAY 139
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDENDRG-ELVLVAADGLTLPTLGIR---FPL-DEGLAGRVAETGRPLNIPDVE 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427711950   140 EipqaETYQFNRSFDDNLGyrTRSVLVIPMqNAEGEIIGVLQLLNRKIRAdikitpdnatdvtvPYSHWEEAILRSLASQ 219
Cdd:smart00065  76 A----DPLFAEDLLGRYQG--VRSFLAVPL-VADGELVGVLALHNKKSPR--------------PFTEEDEELLQALANQ 134
                          170
                   ....*....|....*
gi 427711950   220 AAVSIERNHLLESIE 234
Cdd:smart00065 135 LAIALANAQLYEELR 149
FhlA COG2203
FOG: GAF domain [Signal transduction mechanisms]
48-235 2.93e-08

FOG: GAF domain [Signal transduction mechanisms]


Pssm-ID: 225113  Cd Length: 175  Bit Score: 52.29  E-value: 2.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427711950  48 LLAVGTALSATENLSDLLTLILTKSREITCSDAGSVFLVDRQAHPPNLWFKTAQNDTHPELSLHEFFIPLNAESLVGYVA 127
Cdd:COG2203    6 LNELAAKIAQDLDLEEILQAALELLAELLGADRGLIYLLDEDGLLDGALVAEAAEAGLEQLIDELFGLVILPACLIGIAL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427711950 128 LTGEILNIPDAYEIPQAETyqfnrSFDDNLGYRTRSVLVIPMQnAEGEIIGVLQLLNRKIRAdikitpdnatdvtvPYSH 207
Cdd:COG2203   86 REGRPVVVEDILQDPRFRD-----NPLVLLEPPIRSYLGVPLI-AQGELLGLLCVHDSEPRR--------------QWSE 145
                        170       180
                 ....*....|....*....|....*...
gi 427711950 208 WEEAILRSLASQAAVSIERNHLLESIEK 235
Cdd:COG2203  146 EELELLEELAEQVAIAIERARLYEELQE 173
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic ...
255-333 1.29e-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  Cd Length: 124  Bit Score: 37.66  E-value: 1.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427711950   255 TAGHSERVADLTLRLAAEVNDQagigafvgvgfdqrQLQELRYAALLHDFGKVGVPEVILSKEKKLY---PLQLEIIRQR 331
Cdd:smart00471   5 VFEHSLRVAQLAAALAEELGLL--------------DIELLLLAALLHDIGKPGTPDSFLVKTSVLEdhhFIGAEILLEE 70

                   ..
gi 427711950   332 FH 333
Cdd:smart00471  71 EE 72
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic ...
437-521 3.85e-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  Cd Length: 124  Bit Score: 36.51  E-value: 3.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427711950   437 VRRGNLTPQERLAIESHVTHTYEFLRRIPWTSSLKDVPIIAYG-HHERLNGtgypLGIADIPLQTQMLTIADIYDALTaA 515
Cdd:smart00471  43 PGTPDSFLVKTSVLEDHHFIGAEILLEEEEPRILEEILRTAILsHHERPDG----LRGEPITLEARIVKVADRLDALR-A 117

                   ....*.
gi 427711950   516 DRPYKK 521
Cdd:smart00471 118 DRRYRR 123
COG2206 COG2206
c-di-GMP phosphodiesterase class II (HD-GYP domain) [Signal transduction mechanisms]
218-551 1.48e-28

c-di-GMP phosphodiesterase class II (HD-GYP domain) [Signal transduction mechanisms]


Pssm-ID: 225116 [Multi-domain]  Cd Length: 344  Bit Score: 115.66  E-value: 1.48e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427711950 218 SQAAVSIERNHLLESIEKLFEGFVTASVQA-----IEARDKITAGHSERVADLTLRLAAEVndqagigafvgvGFDQRQL 292
Cdd:COG2206  107 ILIAKLDATLAVRIELSKVAREIVKKALVAlargdIKAKDDYTYGHSVRVAELAEAIAKKL------------GLSEEKI 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427711950 293 QELRYAALLHDFGKVGVPEVILSKEKKLyplqleiirqrfhfvrrtlelecnqakldylqanphhdpdagtcdhcqqlrq 372
Cdd:COG2206  175 EELALAGLLHDIGKIGIPDSILNKPGKL---------------------------------------------------- 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427711950 373 fdlqlqaqlqnldrywqvveianepkvlaeeplgilqeltswhykdinghlqplvtiaeleqllvrrgnlTPQERLAIES 452
Cdd:COG2206  203 ----------------------------------------------------------------------TEEEFEIIKK 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427711950 453 HVTHTYEFLRRIPWTSSlkDVPIIAYGHHERLNGTGYPLGIA--DIPLQTQMLTIADIYDALTaADRPYKKSLPVPIALK 530
Cdd:COG2206  213 HPIYGYDILKDLPEFLE--SVRAVALRHHERWDGTGYPRGLKgeEIPLEARIIAVADVYDALT-SDRPYKKAKSPEEALE 289
                        330       340
                 ....*....|....*....|.
gi 427711950 531 ILHQEAeSNQINRDLVLLFEQ 551
Cdd:COG2206  290 ELRKNS-GGKFDPKVVDAFLK 309
 
Name Accession Description Interval E-value
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
443-522 1.87e-06

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032  Cd Length: 145  Bit Score: 46.56  E-value: 1.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427711950 443 TPQERLAIESHVTHTYEFLRRIPWTSSLK----DVPIIAYGHHERLNGTGYPLGIAD--IPLQTQMLTIADIYDALTAAD 516
Cdd:cd00077   50 TEEESELEKDHAIVGAEILRELLLEEVIKlideLILAVDASHHERLDGLGYPDGLKGeeITLEARIVKLADRLDALRRDS 129

                 ....*.
gi 427711950 517 RPYKKS 522
Cdd:cd00077  130 REKRRR 135
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
255-320 6.30e-05

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032  Cd Length: 145  Bit Score: 41.94  E-value: 6.30e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 427711950 255 TAGHSERVADLTLRLAAEVndqagigafvgvGFDQRQLQELRYAALLHDFGKVGVPEVILSKEKKL 320
Cdd:cd00077    3 RFEHSLRVAQLARRLAEEL------------GLSEEDIELLRLAALLHDIGKPGTPDAITEEESEL 56
HD_5 pfam13487
HD domain; HD domains are metal dependent phosphohydrolases.
440-503 1.03e-15

HD domain; HD domains are metal dependent phosphohydrolases.


Pssm-ID: 257811  Cd Length: 63  Bit Score: 72.21  E-value: 1.03e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 427711950  440 GNLTPQERLAIESHVTHTYEFLRRIPWtssLKDVPIIAYGHHERLNGTGYPLGIA--DIPLQTQML 503
Cdd:pfam13487   1 GTLTPEERAIINEHPEQTARLLEKIPR---LPPVAEIIGHHHERLDGSGYPRGLKgdEIPLGARIL 63
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
60-224 5.36e-12

GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl cyclases, phytochromes, FhlA and NifA. Adenylyl and guanylyl cyclases catalyse ATP and GTP to the second messengers cAMP and cGMP, respectively, these products up-regulating catalytic activity by binding to the regulatory GAF domain(s). The opposite hydrolysis reaction is catalysed by phosphodiesterase. cGMP-dependent 3',5'-cyclic phosphodiesterase catalyses the conversion of guanosine 3',5'-cyclic phosphate to guanosine 5'-phosphate. Here too, cGMP regulates catalytic activity by GAF-domain binding. Phytochromes are regulatory photoreceptors in plants and bacteria which exist in two thermally-stable states that are reversibly inter-convertible by light: the Pr state absorbs maximally in the red region of the spectrum, while the Pfr state absorbs maximally in the far-red region. This domain is also found in FhlA (formate hydrogen lyase transcriptional activator) and NifA, a transcriptional activator which is required for activation of most Nif operons which are directly involved in nitrogen fixation. NifA interacts with sigma-54.


Pssm-ID: 250726  Cd Length: 146  Bit Score: 63.37  E-value: 5.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427711950   60 NLSDLLTLILTKSREITCSDAGSVFLVDRQAHPPNLWfktaQNDTHPELSLHEFFIPLNaESLVGYVALTGEILNIPDAY 139
Cdd:pfam01590   1 DLEELLQTILEELRELLGADRVAIYLADADGLLLYLV----AGDGLSDIPLAARGLPLG-GGVVGEVIAGGNPIVVPDVQ 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427711950  140 EIP--QAETYQFNRSFDDNLGYRTRSVLVIPMqNAEGEIIGVLQLLNRKIRadikitpdnatdvtvPYSHWEEAILRSLA 217
Cdd:pfam01590  76 DDPrfRDLTALASDLPHFLRGLGIRSCLAVPL-KGGGELIGVLVLHSTSPR---------------AFTEEELELLQALA 139

                  ....*..
gi 427711950  218 SQAAVSI 224
Cdd:pfam01590 140 DQVAIAL 146
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
60-234 1.75e-11

Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these domains in PDE6B result in autosomal recessive inheritance of retinitis pigmentosa.


Pssm-ID: 214500  Cd Length: 149  Bit Score: 62.01  E-value: 1.75e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427711950    60 NLSDLLTLILTKSREITCSDAGSVFLVDRQAHPpNLWFKTAQNDTHPELSLHeffIPLnAESLVGYVALTGEILNIPDAY 139
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDENDRG-ELVLVAADGLTLPTLGIR---FPL-DEGLAGRVAETGRPLNIPDVE 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427711950   140 EipqaETYQFNRSFDDNLGyrTRSVLVIPMqNAEGEIIGVLQLLNRKIRAdikitpdnatdvtvPYSHWEEAILRSLASQ 219
Cdd:smart00065  76 A----DPLFAEDLLGRYQG--VRSFLAVPL-VADGELVGVLALHNKKSPR--------------PFTEEDEELLQALANQ 134
                          170
                   ....*....|....*
gi 427711950   220 AAVSIERNHLLESIE 234
Cdd:smart00065 135 LAIALANAQLYEELR 149
FhlA COG2203
FOG: GAF domain [Signal transduction mechanisms]
48-235 2.93e-08

FOG: GAF domain [Signal transduction mechanisms]


Pssm-ID: 225113  Cd Length: 175  Bit Score: 52.29  E-value: 2.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427711950  48 LLAVGTALSATENLSDLLTLILTKSREITCSDAGSVFLVDRQAHPPNLWFKTAQNDTHPELSLHEFFIPLNAESLVGYVA 127
Cdd:COG2203    6 LNELAAKIAQDLDLEEILQAALELLAELLGADRGLIYLLDEDGLLDGALVAEAAEAGLEQLIDELFGLVILPACLIGIAL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427711950 128 LTGEILNIPDAYEIPQAETyqfnrSFDDNLGYRTRSVLVIPMQnAEGEIIGVLQLLNRKIRAdikitpdnatdvtvPYSH 207
Cdd:COG2203   86 REGRPVVVEDILQDPRFRD-----NPLVLLEPPIRSYLGVPLI-AQGELLGLLCVHDSEPRR--------------QWSE 145
                        170       180
                 ....*....|....*....|....*...
gi 427711950 208 WEEAILRSLASQAAVSIERNHLLESIEK 235
Cdd:COG2203  146 EELELLEELAEQVAIAIERARLYEELQE 173
GAF_2 pfam13185
GAF domain;
58-225 2.41e-06

GAF domain;


Pssm-ID: 257553  Cd Length: 150  Bit Score: 46.43  E-value: 2.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427711950   58 TENLSDLLTLILTKSREITCSDAGSVFLVDRQAHPPNLWF----KTAQNDTHPELSLHEFFIPLNAESLVGYVALTGEIL 133
Cdd:pfam13185   1 ALSLEELLEAILEALLELTGSEAGFIGLLDEDGTLLLLAAsggtEELLRELAALSGELGGPPAAGAVGLGEGALRTGKPV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427711950  134 NIPDAYEIPQAETYQFNRsfddnlGYRTRSVLVIPMQNaEGEIIGVLQLLNRKIRAdikitpdnatdvtvpYSHWEEAIL 213
Cdd:pfam13185  81 IINDVASDPSGAGGLPAG------HEGLRSFLSVPLIS-GGRVIGVLALGSKEPGA---------------FDEEDLELL 138
                         170
                  ....*....|..
gi 427711950  214 RSLASQAAVSIE 225
Cdd:pfam13185 139 ELLAEQIAIAIE 150
GAF_3 pfam13492
GAF domain;
60-226 6.46e-06

GAF domain;


Pssm-ID: 257816  Cd Length: 129  Bit Score: 44.74  E-value: 6.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427711950   60 NLSDLLTLILTKSREITCSDAGSVFLVDRQAHPPNLwfkTAQNDTHPELSlheFFIPlNAESLVGYVALTGEILNIPDay 139
Cdd:pfam13492   1 DPDELLERALELLAELLGADRAALYLLDEDGLELRL---VAGSGGEPRLS---ESLP-EDSPLAQRALEKGEPVSVPA-- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427711950  140 eipqaetyqfnrsFDDNLGYRTRSVLVIPMQnAEGEIIGVLQLLNRKIRAdikITPDnatdvtvpyshwEEAILRSLASQ 219
Cdd:pfam13492  72 -------------GDNRDLLPSESLLAVPLR-AGGEVIGVLVLESTPEEA---FTPE------------DLELLELLASQ 122

                  ....*..
gi 427711950  220 AAVSIER 226
Cdd:pfam13492 123 IAIALEN 129
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic ...
255-333 1.29e-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  Cd Length: 124  Bit Score: 37.66  E-value: 1.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427711950   255 TAGHSERVADLTLRLAAEVNDQagigafvgvgfdqrQLQELRYAALLHDFGKVGVPEVILSKEKKLY---PLQLEIIRQR 331
Cdd:smart00471   5 VFEHSLRVAQLAAALAEELGLL--------------DIELLLLAALLHDIGKPGTPDSFLVKTSVLEdhhFIGAEILLEE 70

                   ..
gi 427711950   332 FH 333
Cdd:smart00471  71 EE 72
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic ...
437-521 3.85e-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  Cd Length: 124  Bit Score: 36.51  E-value: 3.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427711950   437 VRRGNLTPQERLAIESHVTHTYEFLRRIPWTSSLKDVPIIAYG-HHERLNGtgypLGIADIPLQTQMLTIADIYDALTaA 515
Cdd:smart00471  43 PGTPDSFLVKTSVLEDHHFIGAEILLEEEEPRILEEILRTAILsHHERPDG----LRGEPITLEARIVKVADRLDALR-A 117

                   ....*.
gi 427711950   516 DRPYKK 521
Cdd:smart00471 118 DRRYRR 123
COG2206 COG2206
c-di-GMP phosphodiesterase class II (HD-GYP domain) [Signal transduction mechanisms]
218-551 1.48e-28

c-di-GMP phosphodiesterase class II (HD-GYP domain) [Signal transduction mechanisms]


Pssm-ID: 225116 [Multi-domain]  Cd Length: 344  Bit Score: 115.66  E-value: 1.48e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427711950 218 SQAAVSIERNHLLESIEKLFEGFVTASVQA-----IEARDKITAGHSERVADLTLRLAAEVndqagigafvgvGFDQRQL 292
Cdd:COG2206  107 ILIAKLDATLAVRIELSKVAREIVKKALVAlargdIKAKDDYTYGHSVRVAELAEAIAKKL------------GLSEEKI 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427711950 293 QELRYAALLHDFGKVGVPEVILSKEKKLyplqleiirqrfhfvrrtlelecnqakldylqanphhdpdagtcdhcqqlrq 372
Cdd:COG2206  175 EELALAGLLHDIGKIGIPDSILNKPGKL---------------------------------------------------- 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427711950 373 fdlqlqaqlqnldrywqvveianepkvlaeeplgilqeltswhykdinghlqplvtiaeleqllvrrgnlTPQERLAIES 452
Cdd:COG2206  203 ----------------------------------------------------------------------TEEEFEIIKK 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427711950 453 HVTHTYEFLRRIPWTSSlkDVPIIAYGHHERLNGTGYPLGIA--DIPLQTQMLTIADIYDALTaADRPYKKSLPVPIALK 530
Cdd:COG2206  213 HPIYGYDILKDLPEFLE--SVRAVALRHHERWDGTGYPRGLKgeEIPLEARIIAVADVYDALT-SDRPYKKAKSPEEALE 289
                        330       340
                 ....*....|....*....|.
gi 427711950 531 ILHQEAeSNQINRDLVLLFEQ 551
Cdd:COG2206  290 ELRKNS-GGKFDPKVVDAFLK 309
COG3437 COG3437
Response regulator containing a CheY-like receiver domain and an HD-GYP domain [Transcription ...
429-538 1.69e-18

Response regulator containing a CheY-like receiver domain and an HD-GYP domain [Transcription / Signal transduction mechanisms]


Pssm-ID: 225971 [Multi-domain]  Cd Length: 360  Bit Score: 85.87  E-value: 1.69e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427711950 429 IAELEQLLVRRGNLTPQERLAIESHVTHTYEFLRRIpwTSSLKDVPIIAYGHHERLNGTGYPLGIA--DIPLQTQMLTIA 506
Cdd:COG3437  226 VAIPDSILLKPGKLTSEEFEIMKGHPILGAEILKSS--ERLMQVAAEIARHHHERWDGSGYPDGLKgdEIPLSARIVAIA 303
                         90       100       110
                 ....*....|....*....|....*....|..
gi 427711950 507 DIYDALTaADRPYKKSLPVPIALKILHQEAES 538
Cdd:COG3437  304 DVFDALV-SGRPYKEAMSTEEALEIIRAQSGR 334
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.11
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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