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Conserved domains on  [gi|332994267|gb|AEF04322|]
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metal-dependent phosphohydrolase domain-containing protein [Alteromonas naphthalenivorans]

Protein Classification

HD-GYP domain-containing protein( domain architecture ID 12112208)

HD-GYP domain-containing protein may be a phosphodiesterase; also contains a DUF3391 domain

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 ...
 116-333 8.58e-63

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: 204.44  E-value: 8.58e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332994267 116 FLSALNRGAVNDLKLVKELAQSLIDSIFdnkdaLSCLTLIKNNNAYLLEHSINCSILMGMFTQFLGYDRGTIDQASLGAL 195
Cdd:COG2206  103 LFEELRLGLLEELKKLVEELDELLPDAL-----LALLAALDAKDPYTYGHSVRVAVLALALARELGLSEEELEDLGLAAL 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332994267 196 LMDVGMSSIPMDVHNSVQDLSAADWELMKTHVDIGVELVEQCGDISDlVLSIIAQHHERIDGSGYPKALKEMEISEFARI 275
Cdd:COG2206  178 LHDIGKIGIPDEILNKPGKLTDEEFEIIKKHPEYGYEILKKLPGLSE-VAEIVLQHHERLDGSGYPRGLKGEEIPLLARI 256

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 332994267 276 AGIIDTYDAMVSNRPHKESISPTQALKRLTEDN--RLDQTLVNQFVTCMGVHPVGSIVRL 333
Cdd:COG2206  257 LAVADVYDALTSDRPYRKALSPEEALEELRKGAgtQFDPELVEAFIKVLGIYPPVVEIDL 316
DUF3391 pfam11871
Domain of unknown function (DUF3391); This functionally uncharacterized, N-terminal domain is ...
 2-129 3.26e-13

Domain of unknown function (DUF3391); This functionally uncharacterized, N-terminal domain is found in a number of bacterial proteins, including Cyclic di-GMP phosphodiesterase PA4108. It is often found associated with the HD domain pfam13328.


:

Pssm-ID: 432148  Cd Length: 136  Bit Score: 66.30  E-value: 3.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332994267    2 LKAVPIDDLKPGMYINQV-LKQTGSLRMRSKGLVKHQTVINTLKSRGIQVVQVDFDKSPNHEPA---TDSAPNPTSETIV 77
Cdd:pfam11871   1 LKKIPVDQLRPGMFVVKLdGSWLDHPFLRNRFLIKSEEDIEKLRALGIKEVWIDTERSDVPPLPgldVPAAEAAAAAEAA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 332994267   78 QAPTKVREEPSPATTSL--TRNAMKEANGLYFDAVNIQNGFLSALNRGAVNDLK 129
Cdd:pfam11871  81 EEPAALTEEKQERPERLeaRREELARAEKLYEEAKALVRSLFSDARLGKAIDVE 134
 
Name Accession Description Interval E-value
HDGYP COG2206
HD-GYP domain, c-di-GMP phosphodiesterase class II (or its inactivated variant) [Signal ...
 116-333 8.58e-63

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: 204.44  E-value: 8.58e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332994267 116 FLSALNRGAVNDLKLVKELAQSLIDSIFdnkdaLSCLTLIKNNNAYLLEHSINCSILMGMFTQFLGYDRGTIDQASLGAL 195
Cdd:COG2206  103 LFEELRLGLLEELKKLVEELDELLPDAL-----LALLAALDAKDPYTYGHSVRVAVLALALARELGLSEEELEDLGLAAL 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332994267 196 LMDVGMSSIPMDVHNSVQDLSAADWELMKTHVDIGVELVEQCGDISDlVLSIIAQHHERIDGSGYPKALKEMEISEFARI 275
Cdd:COG2206  178 LHDIGKIGIPDEILNKPGKLTDEEFEIIKKHPEYGYEILKKLPGLSE-VAEIVLQHHERLDGSGYPRGLKGEEIPLLARI 256

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 332994267 276 AGIIDTYDAMVSNRPHKESISPTQALKRLTEDN--RLDQTLVNQFVTCMGVHPVGSIVRL 333
Cdd:COG2206  257 LAVADVYDALTSDRPYRKALSPEEALEELRKGAgtQFDPELVEAFIKVLGIYPPVVEIDL 316
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
 161-292 8.66e-16

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 73.91  E-value: 8.66e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332994267 161 YLLEHSINCSILMGMFTQFLGYDRGTIDQASLGALLMDVGMSSIPMDVHNsvqdlsaADWELMKTHVDIGVELVEQ---- 236
Cdd:cd00077    2 HRFEHSLRVAQLARRLAEELGLSEEDIELLRLAALLHDIGKPGTPDAITE-------EESELEKDHAIVGAEILREllle 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 332994267 237 --CGDISDLVLSIIAQHHERIDGSGYPKALKEMEISEFARIAGIIDTYDAMVSNRPHK 292
Cdd:cd00077   75 evIKLIDELILAVDASHHERLDGLGYPDGLKGEEITLEARIVKLADRLDALRRDSREK 132
HD_5 pfam13487
HD domain; HD domains are metal dependent phosphohydrolases.
 213-275 1.33e-14

HD domain; HD domains are metal dependent phosphohydrolases.


Pssm-ID: 433249 [Multi-domain]  Cd Length: 64  Bit Score: 68.01  E-value: 1.33e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 332994267  213 QDLSAADWELMKTHVDIGVELVEQCGDISDLVLSIIAQHHERIDGSGYPKALKEMEISEFARI 275
Cdd:pfam13487   1 GTLTPEEREIINRHPEHTARLLSTLPRLPKEVAEIIAQHHERLDGSGYPRGLKGEEIPLGARI 63
DUF3391 pfam11871
Domain of unknown function (DUF3391); This functionally uncharacterized, N-terminal domain is ...
 2-129 3.26e-13

Domain of unknown function (DUF3391); This functionally uncharacterized, N-terminal domain is found in a number of bacterial proteins, including Cyclic di-GMP phosphodiesterase PA4108. It is often found associated with the HD domain pfam13328.


Pssm-ID: 432148  Cd Length: 136  Bit Score: 66.30  E-value: 3.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332994267    2 LKAVPIDDLKPGMYINQV-LKQTGSLRMRSKGLVKHQTVINTLKSRGIQVVQVDFDKSPNHEPA---TDSAPNPTSETIV 77
Cdd:pfam11871   1 LKKIPVDQLRPGMFVVKLdGSWLDHPFLRNRFLIKSEEDIEKLRALGIKEVWIDTERSDVPPLPgldVPAAEAAAAAEAA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 332994267   78 QAPTKVREEPSPATTSL--TRNAMKEANGLYFDAVNIQNGFLSALNRGAVNDLK 129
Cdd:pfam11871  81 EEPAALTEEKQERPERLeaRREELARAEKLYEEAKALVRSLFSDARLGKAIDVE 134
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
 161-293 2.50e-09

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: 54.99  E-value: 2.50e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332994267   161 YLLEHSINCSILMGMFTQFLGYDRgtIDQASLGALLMDVGMssiPMDVHNSVQDLSAadwelMKTHVDIGVELVEQCGDI 240
Cdd:smart00471   4 HVFEHSLRVAQLAAALAEELGLLD--IELLLLAALLHDIGK---PGTPDSFLVKTSV-----LEDHHFIGAEILLEEEEP 73

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 332994267   241 SDLVL---SIIAQHHERIDGsgypkaLKEMEISEFARIAGIIDTYDAMVSNRPHKE 293
Cdd:smart00471  74 RILEEilrTAILSHHERPDG------LRGEPITLEARIVKVADRLDALRADRRYRR 123
PRK12705 PRK12705
hypothetical protein; Provisional
 163-257 3.36e-04

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 42.77  E-value: 3.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332994267 163 LEHSINCSILMGMFTQFLGYDRgtiDQASLGALLMDVGMSsipmdvhnsvqdlsaADWELMKTHVDIGVELVEQCGDiSD 242
Cdd:PRK12705 325 LSHSLEVAHLAGIIAAEIGLDP---ALAKRAGLLHDIGKS---------------IDRESDGNHVEIGAELARKFNE-PD 385

                         90
                 ....*....|....*
gi 332994267 243 LVLSIIAQHHERIDG 257
Cdd:PRK12705 386 EVINAIASHHNKVNP 400
HDIG TIGR00277
HDIG domain; This domain is found in a few known nucleotidyltransferes and in a large number ...
 162-253 1.65e-03

HDIG domain; This domain is found in a few known nucleotidyltransferes and in a large number of uncharacterized proteins. It contains four widely separated His residues, the second of which is part of an invariant dipeptide His-Asp in a region matched approximately by the motif HDIG. This model may annotate homologous domains in which one or more of the His residues is conserved but misaligned, and some probable false-positive hits.


Pssm-ID: 272994 [Multi-domain]  Cd Length: 80  Bit Score: 36.93  E-value: 1.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332994267  162 LLEHSINCSILMGMFTQFLGYDRgtiDQASLGALLMDVGmssiPMDVHNSVqdlsaadweLMKTHVDIGVELVEQCGdIS 241
Cdd:TIGR00277   5 VLQHSLEVAKLAEALARELGLDV---ELARRGALLHDIG----KPITREGV---------IFESHVVVGAEIARKYG-EP 67

                          90
                  ....*....|..
gi 332994267  242 DLVLSIIAQHHE 253
Cdd:TIGR00277  68 LEVIDIIAEHHG 79
 
Name Accession Description Interval E-value
HDGYP COG2206
HD-GYP domain, c-di-GMP phosphodiesterase class II (or its inactivated variant) [Signal ...
 116-333 8.58e-63

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: 204.44  E-value: 8.58e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332994267 116 FLSALNRGAVNDLKLVKELAQSLIDSIFdnkdaLSCLTLIKNNNAYLLEHSINCSILMGMFTQFLGYDRGTIDQASLGAL 195
Cdd:COG2206  103 LFEELRLGLLEELKKLVEELDELLPDAL-----LALLAALDAKDPYTYGHSVRVAVLALALARELGLSEEELEDLGLAAL 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332994267 196 LMDVGMSSIPMDVHNSVQDLSAADWELMKTHVDIGVELVEQCGDISDlVLSIIAQHHERIDGSGYPKALKEMEISEFARI 275
Cdd:COG2206  178 LHDIGKIGIPDEILNKPGKLTDEEFEIIKKHPEYGYEILKKLPGLSE-VAEIVLQHHERLDGSGYPRGLKGEEIPLLARI 256

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 332994267 276 AGIIDTYDAMVSNRPHKESISPTQALKRLTEDN--RLDQTLVNQFVTCMGVHPVGSIVRL 333
Cdd:COG2206  257 LAVADVYDALTSDRPYRKALSPEEALEELRKGAgtQFDPELVEAFIKVLGIYPPVVEIDL 316
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
 161-292 8.66e-16

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 73.91  E-value: 8.66e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332994267 161 YLLEHSINCSILMGMFTQFLGYDRGTIDQASLGALLMDVGMSSIPMDVHNsvqdlsaADWELMKTHVDIGVELVEQ---- 236
Cdd:cd00077    2 HRFEHSLRVAQLARRLAEELGLSEEDIELLRLAALLHDIGKPGTPDAITE-------EESELEKDHAIVGAEILREllle 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 332994267 237 --CGDISDLVLSIIAQHHERIDGSGYPKALKEMEISEFARIAGIIDTYDAMVSNRPHK 292
Cdd:cd00077   75 evIKLIDELILAVDASHHERLDGLGYPDGLKGEEITLEARIVKLADRLDALRRDSREK 132
HD_5 pfam13487
HD domain; HD domains are metal dependent phosphohydrolases.
 213-275 1.33e-14

HD domain; HD domains are metal dependent phosphohydrolases.


Pssm-ID: 433249 [Multi-domain]  Cd Length: 64  Bit Score: 68.01  E-value: 1.33e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 332994267  213 QDLSAADWELMKTHVDIGVELVEQCGDISDLVLSIIAQHHERIDGSGYPKALKEMEISEFARI 275
Cdd:pfam13487   1 GTLTPEEREIINRHPEHTARLLSTLPRLPKEVAEIIAQHHERLDGSGYPRGLKGEEIPLGARI 63
DUF3391 pfam11871
Domain of unknown function (DUF3391); This functionally uncharacterized, N-terminal domain is ...
 2-129 3.26e-13

Domain of unknown function (DUF3391); This functionally uncharacterized, N-terminal domain is found in a number of bacterial proteins, including Cyclic di-GMP phosphodiesterase PA4108. It is often found associated with the HD domain pfam13328.


Pssm-ID: 432148  Cd Length: 136  Bit Score: 66.30  E-value: 3.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332994267    2 LKAVPIDDLKPGMYINQV-LKQTGSLRMRSKGLVKHQTVINTLKSRGIQVVQVDFDKSPNHEPA---TDSAPNPTSETIV 77
Cdd:pfam11871   1 LKKIPVDQLRPGMFVVKLdGSWLDHPFLRNRFLIKSEEDIEKLRALGIKEVWIDTERSDVPPLPgldVPAAEAAAAAEAA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 332994267   78 QAPTKVREEPSPATTSL--TRNAMKEANGLYFDAVNIQNGFLSALNRGAVNDLK 129
Cdd:pfam11871  81 EEPAALTEEKQERPERLeaRREELARAEKLYEEAKALVRSLFSDARLGKAIDVE 134
HD pfam01966
HD domain; HD domains are metal dependent phosphohydrolases.
 162-285 9.03e-12

HD domain; HD domains are metal dependent phosphohydrolases.


Pssm-ID: 460398 [Multi-domain]  Cd Length: 110  Bit Score: 61.48  E-value: 9.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332994267  162 LLEHSINCSILMGMFTQFLGYDRgtIDQASLGALLMDVGMSSIPMDvhnsvqdlsAADWELMKTHVDIGVELVEQCG--D 239
Cdd:pfam01966   1 RLEHSLRVALLARELAEELGELD--RELLLLAALLHDIGKGPFGDE---------KPEFEIFLGHAVVGAEILRELEkrL 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 332994267  240 ISDLVLSIIAQHHERIDGSGYPkalkeMEISEFARIAGIIDTYDAM 285
Cdd:pfam01966  70 GLEDVLKLILEHHESWEGAGYP-----EEISLEARIVKLADRLDAL 110
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
 161-293 2.50e-09

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: 54.99  E-value: 2.50e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332994267   161 YLLEHSINCSILMGMFTQFLGYDRgtIDQASLGALLMDVGMssiPMDVHNSVQDLSAadwelMKTHVDIGVELVEQCGDI 240
Cdd:smart00471   4 HVFEHSLRVAQLAAALAEELGLLD--IELLLLAALLHDIGK---PGTPDSFLVKTSV-----LEDHHFIGAEILLEEEEP 73

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 332994267   241 SDLVL---SIIAQHHERIDGsgypkaLKEMEISEFARIAGIIDTYDAMVSNRPHKE 293
Cdd:smart00471  74 RILEEilrTAILSHHERPDG------LRGEPITLEARIVKVADRLDALRADRRYRR 123
RnaY COG1418
HD superfamily phosphodieaserase, includes HD domain of RNase Y [Translation, ribosomal ...
 160-256 5.85e-05

HD superfamily phosphodieaserase, includes HD domain of RNase Y [Translation, ribosomal structure and biogenesis, General function prediction only];


Pssm-ID: 441028 [Multi-domain]  Cd Length: 191  Bit Score: 43.73  E-value: 5.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332994267 160 AYLLEHSINCSILMGMFTQFLGYDRgtiDQASLGALLMDVGmssipmdvhnsvqdlSAADWELMKTHVDIGVELVEQCG- 238
Cdd:COG1418   17 QHDLQHSLRVAKLAGLIAAEEGADV---EVAKRAALLHDIG---------------KAKDHEVEGSHAEIGAELARKYLe 78

                         90       100
                 ....*....|....*....|....
gi 332994267 239 ------DISDLVLSIIAQHHERID 256
Cdd:COG1418   79 slgfpeEEIEAVVHAIEAHSFSGG 102
HDOD COG1639
HD-like signal output (HDOD) domain, no enzymatic activity [Signal transduction mechanisms];
128-253 1.78e-04

HD-like signal output (HDOD) domain, no enzymatic activity [Signal transduction mechanisms];


Pssm-ID: 441246 [Multi-domain]  Cd Length: 244  Bit Score: 42.65  E-value: 1.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332994267 128 LKLVKELAQSL-IDSIFDNKDALSCLTLiknnnAYLLEHSINCSILMGMFTQFLGYDRGtiDQASLGALLMDVG------ 200
Cdd:COG1639   75 LDTVRNLALALaLRQLFSAKLPAYGLDL-----RRFWRHSLAVAAAARALARRLGLLDP--EEAFLAGLLHDIGklvlls 147

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 332994267 201 -----MSSIPMDVHNSVQDLSAADWELM-KTHVDIGVELVEQCGdISDLVLSIIAQHHE 253
Cdd:COG1639  148 lfpeeYAELLALAEADGLSLAEAEREVLgTDHAELGAALARKWG-LPEELVEAIRYHHD 205
PRK12705 PRK12705
hypothetical protein; Provisional
 163-257 3.36e-04

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 42.77  E-value: 3.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332994267 163 LEHSINCSILMGMFTQFLGYDRgtiDQASLGALLMDVGMSsipmdvhnsvqdlsaADWELMKTHVDIGVELVEQCGDiSD 242
Cdd:PRK12705 325 LSHSLEVAHLAGIIAAEIGLDP---ALAKRAGLLHDIGKS---------------IDRESDGNHVEIGAELARKFNE-PD 385

                         90
                 ....*....|....*
gi 332994267 243 LVLSIIAQHHERIDG 257
Cdd:PRK12705 386 EVINAIASHHNKVNP 400
PRK12704 PRK12704
phosphodiesterase; Provisional
 162-306 4.18e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.46  E-value: 4.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332994267 162 LLEHSINCSILMGMFTQFLGYDrgtIDQASLGALLMDVGmssipmdvhnsvqdlSAADWELMKTHVDIGVELVEQCGDiS 241
Cdd:PRK12704 336 VLQHSIEVAHLAGLMAAELGLD---VKLAKRAGLLHDIG---------------KALDHEVEGSHVEIGAELAKKYKE-S 396

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332994267 242 DLVLSIIAQHHEridgsgypkalkEMEISEFarIAGIIDTYDAMVSNRP--HKESIsptQA-LKRLTE 306
Cdd:PRK12704 397 PVVINAIAAHHG------------DEEPTSI--EAVLVAAADAISAARPgaRRETL---ENyIKRLEK 447
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
 192-259 6.36e-04

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: 40.92  E-value: 6.36e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332994267 192 LGALLMDVGMSSIPMDVHNSVQDLSAADWELMKTHVDIGVELVEQCGdisdlVLSIIAQHHERIDGSG 259
Cdd:COG3437  142 LAAPLHDIGKIGIPDAILLKPGKLTPEEWEITHAHIGAEILSGSLLP-----LLQLAAEIHERWDGSG 204
HDIG TIGR00277
HDIG domain; This domain is found in a few known nucleotidyltransferes and in a large number ...
 162-253 1.65e-03

HDIG domain; This domain is found in a few known nucleotidyltransferes and in a large number of uncharacterized proteins. It contains four widely separated His residues, the second of which is part of an invariant dipeptide His-Asp in a region matched approximately by the motif HDIG. This model may annotate homologous domains in which one or more of the His residues is conserved but misaligned, and some probable false-positive hits.


Pssm-ID: 272994 [Multi-domain]  Cd Length: 80  Bit Score: 36.93  E-value: 1.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332994267  162 LLEHSINCSILMGMFTQFLGYDRgtiDQASLGALLMDVGmssiPMDVHNSVqdlsaadweLMKTHVDIGVELVEQCGdIS 241
Cdd:TIGR00277   5 VLQHSLEVAKLAEALARELGLDV---ELARRGALLHDIG----KPITREGV---------IFESHVVVGAEIARKYG-EP 67

                          90
                  ....*....|..
gi 332994267  242 DLVLSIIAQHHE 253
Cdd:TIGR00277  68 LEVIDIIAEHHG 79
 
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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