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Conserved domains on  [gi|1491308094|gb|RLI71860|]
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MAG: hypothetical protein DRP02_03635, partial [Candidatus Gerdarchaeota archaeon]

Protein Classification

HD domain-containing protein( domain architecture ID 11437595)

HD domain-containing protein may function as a metal dependent phosphohydrolase; similar to Bacillus subtilis protein YwfO and protein YdhJ

CATH:  3.30.70.1370
Gene Ontology:  GO:0046872|GO:0042578
PubMed:  9868367
SCOP:  4000705

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YdhJ COG1078
HD superfamily phosphohydrolase [General function prediction only];
6-274 1.35e-115

HD superfamily phosphohydrolase [General function prediction only];


:

Pssm-ID: 440696 [Multi-domain]  Cd Length: 340  Bit Score: 335.23  E-value: 1.35e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308094   6 FIKDPIYGYIFLNNIDAKLIDTPYFQRLRRIKQLSGSEYVYPGANHTRFEHSLGVSFLAEKMASSLRhDEDSEIISEDIA 85
Cdd:COG1078     3 IIRDPVHGYIEVDELELDLIDTPEFQRLRRIKQLGLAYLVYPGAEHTRFEHSLGVMHLARRALDRLR-RKGVEIDEEERE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308094  86 LIRTAALLHDIGHGPFSHTFEALLsRINKHHEDLSRWLVVETEIKDILSDYNVSPSKVCGLIHGNNTVKnknYLNQIISS 165
Cdd:COG1078    82 LVRAAALLHDIGHGPFSHAFEEVL-LTGVDHEEITLRIIEENEINGILEKHGIDPELVADIIKGEYPNK---FLRQLISS 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308094 166 ACDVDKMDFIVRDSYHTGAEYGRVDVMRIIYTMGILKGNLAVNYSALSAFEAFLIARVESFRTIYFHKVSRASQLLIIRA 245
Cdd:COG1078   158 QLDADRMDYLLRDSYYTGVSYGNIDLERLIRMLRVVDDELVVEEKGIYAVESFLIARYLMYWQVYFHKTSRAAEVMLRRA 237

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1491308094 246 M---ELAEEELGLLQFTTPEEYLELDDYTVWS 274
Cdd:COG1078   238 LeraKELYDEGELENPLDLEDFLRLDDYDLLS 269
 
Name Accession Description Interval E-value
YdhJ COG1078
HD superfamily phosphohydrolase [General function prediction only];
6-274 1.35e-115

HD superfamily phosphohydrolase [General function prediction only];


Pssm-ID: 440696 [Multi-domain]  Cd Length: 340  Bit Score: 335.23  E-value: 1.35e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308094   6 FIKDPIYGYIFLNNIDAKLIDTPYFQRLRRIKQLSGSEYVYPGANHTRFEHSLGVSFLAEKMASSLRhDEDSEIISEDIA 85
Cdd:COG1078     3 IIRDPVHGYIEVDELELDLIDTPEFQRLRRIKQLGLAYLVYPGAEHTRFEHSLGVMHLARRALDRLR-RKGVEIDEEERE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308094  86 LIRTAALLHDIGHGPFSHTFEALLsRINKHHEDLSRWLVVETEIKDILSDYNVSPSKVCGLIHGNNTVKnknYLNQIISS 165
Cdd:COG1078    82 LVRAAALLHDIGHGPFSHAFEEVL-LTGVDHEEITLRIIEENEINGILEKHGIDPELVADIIKGEYPNK---FLRQLISS 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308094 166 ACDVDKMDFIVRDSYHTGAEYGRVDVMRIIYTMGILKGNLAVNYSALSAFEAFLIARVESFRTIYFHKVSRASQLLIIRA 245
Cdd:COG1078   158 QLDADRMDYLLRDSYYTGVSYGNIDLERLIRMLRVVDDELVVEEKGIYAVESFLIARYLMYWQVYFHKTSRAAEVMLRRA 237

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1491308094 246 M---ELAEEELGLLQFTTPEEYLELDDYTVWS 274
Cdd:COG1078   238 LeraKELYDEGELENPLDLEDFLRLDDYDLLS 269
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
 49-183 6.76e-16

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: 72.33  E-value: 6.76e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308094   49 ANHTRFEHSLGVSFLAEKMASSLRhdedseiiSEDIALIRTAALLHDIGHGPFSHTFEALLSRINKHHEdLSRWLVVETE 128
Cdd:smart00471   1 SDYHVFEHSLRVAQLAAALAEELG--------LLDIELLLLAALLHDIGKPGTPDSFLVKTSVLEDHHF-IGAEILLEEE 71

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1491308094  129 IKDILSDYNvspSKVCGLIHGNNTVKNKNYLNQIISSACDVDKMDFIVRDSYHTG 183
Cdd:smart00471  72 EPRILEEIL---RTAILSHHERPDGLRGEPITLEARIVKVADRLDALRADRRYRR 123
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
 51-195 3.17e-14

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 68.13  E-value: 3.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308094  51 HTRFEHSLGVSFLAEKMASSLRHDEdseiisEDIALIRTAALLHDIGHGPFSHTFEALLSRINKHHE----DLSRWLVVE 126
Cdd:cd00077     1 EHRFEHSLRVAQLARRLAEELGLSE------EDIELLRLAALLHDIGKPGTPDAITEEESELEKDHAivgaEILRELLLE 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1491308094 127 TEIKDILSDYNVSPSKVCGLIHGNNTVKNKNYLNQIISSAC--DVDKMDFIVRDSYHTGAEYGRVDVMRII 195
Cdd:cd00077    75 EVIKLIDELILAVDASHHERLDGLGYPDGLKGEEITLEARIvkLADRLDALRRDSREKRRRIAEEDLEELL 145
HD pfam01966
HD domain; HD domains are metal dependent phosphohydrolases.
 53-173 2.24e-12

HD domain; HD domains are metal dependent phosphohydrolases.


Pssm-ID: 460398 [Multi-domain]  Cd Length: 110  Bit Score: 62.25  E-value: 2.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308094  53 RFEHSLGVSFLAEKMASSLRhdedseiiSEDIALIRTAALLHDIGHGPFSHtfEALLSRINKHHEDLSRWLVVETEIKDI 132
Cdd:pfam01966   1 RLEHSLRVALLARELAEELG--------ELDRELLLLAALLHDIGKGPFGD--EKPEFEIFLGHAVVGAEILRELEKRLG 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1491308094 133 LSDynvspskVCGLIHGNNTVKN-KNYLNQIISSACDVDKMD 173
Cdd:pfam01966  71 LED-------VLKLILEHHESWEgAGYPEEISLEARIVKLAD 105
PRK01096 PRK01096
deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional
 23-133 3.94e-08

deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional


Pssm-ID: 234897 [Multi-domain]  Cd Length: 440  Bit Score: 53.77  E-value: 3.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308094  23 KLIDTPYFQRLRRIKQlsgseyVYPGAN----HTRFEHSLGVSFLAEKM----ASSLRHDEDSEIIS-EDI-ALIRTAAL 92
Cdd:PRK01096   34 RIIFSGSFRRLQRKTQ------VHPLAKndhiHTRLTHSLEVSCVGRSLgmrvGETLKEEKLPDWISpADIgAIVQSACL 107

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1491308094  93 LHDIGHGPFSHTFE-ALLSRINKH-HEDLSRWLvVETEIKDIL 133
Cdd:PRK01096  108 AHDIGNPPFGHFGEdAIREWFQDAaGRGFLDDL-SPQERADFL 149
HDIG TIGR00277
HDIG domain; This domain is found in a few known nucleotidyltransferes and in a large number ...
 54-97 9.10e-06

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: 43.09  E-value: 9.10e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1491308094  54 FEHSLGVSFLAEKMASSLRhdedseiisEDIALIRTAALLHDIG 97
Cdd:TIGR00277   6 LQHSLEVAKLAEALARELG---------LDVELARRGALLHDIG 40
 
Name Accession Description Interval E-value
YdhJ COG1078
HD superfamily phosphohydrolase [General function prediction only];
6-274 1.35e-115

HD superfamily phosphohydrolase [General function prediction only];


Pssm-ID: 440696 [Multi-domain]  Cd Length: 340  Bit Score: 335.23  E-value: 1.35e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308094   6 FIKDPIYGYIFLNNIDAKLIDTPYFQRLRRIKQLSGSEYVYPGANHTRFEHSLGVSFLAEKMASSLRhDEDSEIISEDIA 85
Cdd:COG1078     3 IIRDPVHGYIEVDELELDLIDTPEFQRLRRIKQLGLAYLVYPGAEHTRFEHSLGVMHLARRALDRLR-RKGVEIDEEERE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308094  86 LIRTAALLHDIGHGPFSHTFEALLsRINKHHEDLSRWLVVETEIKDILSDYNVSPSKVCGLIHGNNTVKnknYLNQIISS 165
Cdd:COG1078    82 LVRAAALLHDIGHGPFSHAFEEVL-LTGVDHEEITLRIIEENEINGILEKHGIDPELVADIIKGEYPNK---FLRQLISS 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308094 166 ACDVDKMDFIVRDSYHTGAEYGRVDVMRIIYTMGILKGNLAVNYSALSAFEAFLIARVESFRTIYFHKVSRASQLLIIRA 245
Cdd:COG1078   158 QLDADRMDYLLRDSYYTGVSYGNIDLERLIRMLRVVDDELVVEEKGIYAVESFLIARYLMYWQVYFHKTSRAAEVMLRRA 237

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1491308094 246 M---ELAEEELGLLQFTTPEEYLELDDYTVWS 274
Cdd:COG1078   238 LeraKELYDEGELENPLDLEDFLRLDDYDLLS 269
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
 49-183 6.76e-16

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: 72.33  E-value: 6.76e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308094   49 ANHTRFEHSLGVSFLAEKMASSLRhdedseiiSEDIALIRTAALLHDIGHGPFSHTFEALLSRINKHHEdLSRWLVVETE 128
Cdd:smart00471   1 SDYHVFEHSLRVAQLAAALAEELG--------LLDIELLLLAALLHDIGKPGTPDSFLVKTSVLEDHHF-IGAEILLEEE 71

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1491308094  129 IKDILSDYNvspSKVCGLIHGNNTVKNKNYLNQIISSACDVDKMDFIVRDSYHTG 183
Cdd:smart00471  72 EPRILEEIL---RTAILSHHERPDGLRGEPITLEARIVKVADRLDALRADRRYRR 123
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
 51-195 3.17e-14

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 68.13  E-value: 3.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308094  51 HTRFEHSLGVSFLAEKMASSLRHDEdseiisEDIALIRTAALLHDIGHGPFSHTFEALLSRINKHHE----DLSRWLVVE 126
Cdd:cd00077     1 EHRFEHSLRVAQLARRLAEELGLSE------EDIELLRLAALLHDIGKPGTPDAITEEESELEKDHAivgaEILRELLLE 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1491308094 127 TEIKDILSDYNVSPSKVCGLIHGNNTVKNKNYLNQIISSAC--DVDKMDFIVRDSYHTGAEYGRVDVMRII 195
Cdd:cd00077    75 EVIKLIDELILAVDASHHERLDGLGYPDGLKGEEITLEARIvkLADRLDALRRDSREKRRRIAEEDLEELL 145
HD pfam01966
HD domain; HD domains are metal dependent phosphohydrolases.
 53-173 2.24e-12

HD domain; HD domains are metal dependent phosphohydrolases.


Pssm-ID: 460398 [Multi-domain]  Cd Length: 110  Bit Score: 62.25  E-value: 2.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308094  53 RFEHSLGVSFLAEKMASSLRhdedseiiSEDIALIRTAALLHDIGHGPFSHtfEALLSRINKHHEDLSRWLVVETEIKDI 132
Cdd:pfam01966   1 RLEHSLRVALLARELAEELG--------ELDRELLLLAALLHDIGKGPFGD--EKPEFEIFLGHAVVGAEILRELEKRLG 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1491308094 133 LSDynvspskVCGLIHGNNTVKN-KNYLNQIISSACDVDKMD 173
Cdd:pfam01966  71 LED-------VLKLILEHHESWEgAGYPEEISLEARIVKLAD 105
PRK01096 PRK01096
deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional
 23-133 3.94e-08

deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional


Pssm-ID: 234897 [Multi-domain]  Cd Length: 440  Bit Score: 53.77  E-value: 3.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308094  23 KLIDTPYFQRLRRIKQlsgseyVYPGAN----HTRFEHSLGVSFLAEKM----ASSLRHDEDSEIIS-EDI-ALIRTAAL 92
Cdd:PRK01096   34 RIIFSGSFRRLQRKTQ------VHPLAKndhiHTRLTHSLEVSCVGRSLgmrvGETLKEEKLPDWISpADIgAIVQSACL 107

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1491308094  93 LHDIGHGPFSHTFE-ALLSRINKH-HEDLSRWLvVETEIKDIL 133
Cdd:PRK01096  108 AHDIGNPPFGHFGEdAIREWFQDAaGRGFLDDL-SPQERADFL 149
PRK01286 PRK01286
deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional
 52-116 9.62e-07

deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional


Pssm-ID: 234934 [Multi-domain]  Cd Length: 336  Bit Score: 49.01  E-value: 9.62e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1491308094  52 TRFEHSLGVSFLAEKMASSLRHDEDseiisediaLIRTAALLHDIGHGPFSHTFEALLSRINKHH 116
Cdd:PRK01286   62 TRLTHTLEVAQIARTIARALRLNED---------LTEAIALGHDLGHTPFGHAGEDALNELMKEY 117
HD_assoc_2 pfam19276
HD associated region; This entry represents a region that forms part of a larger HD domain. ...
 189-270 2.28e-06

HD associated region; This entry represents a region that forms part of a larger HD domain.According to the original paper describing the HD domain this family represents cluster 1.


Pssm-ID: 466023  Cd Length: 222  Bit Score: 47.49  E-value: 2.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308094 189 VDVMRIIYTMGILKGNLAVNYSALSAFEAFLIARVESFRTIYFHKVSRASQLLIIRAMELAEEELGllqfTTPEEYLELD 268
Cdd:pfam19276   1 IDHERLIRELTFVDGELVLDEGGVQAAESLLVARALMNPTVYQHHVARIAKAMLRRALERLIEEGD----LDAEELRRMD 76


                  ..
gi 1491308094 269 DY 270
Cdd:pfam19276  77 DA 78
COG4341 COG4341
Predicted HD phosphohydrolase [General function prediction only];
52-123 5.13e-06

Predicted HD phosphohydrolase [General function prediction only];


Pssm-ID: 443482  Cd Length: 182  Bit Score: 45.66  E-value: 5.13e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1491308094  52 TRFEHSLGVSFLAEkmasslRHDEDSEIIsedialirTAALLHDIGHgpFSHTFEALLSRINKHHEDLS-RWL 123
Cdd:COG4341    24 TQLEHALQTATLAE------RDGADEELV--------VAALLHDIGH--LLHDLGEDLDGGDDNHEEIAaAIL 80
HDIG TIGR00277
HDIG domain; This domain is found in a few known nucleotidyltransferes and in a large number ...
 54-97 9.10e-06

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: 43.09  E-value: 9.10e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1491308094  54 FEHSLGVSFLAEKMASSLRhdedseiisEDIALIRTAALLHDIG 97
Cdd:TIGR00277   6 LQHSLEVAKLAEALARELG---------LDVELARRGALLHDIG 40
YqeK COG1713
Diadenosine tetraphosphatase YqeK or a related HD superfamily phosphohydrolase [Signal ...
 53-129 1.45e-05

Diadenosine tetraphosphatase YqeK or a related HD superfamily phosphohydrolase [Signal transduction mechanisms, General function prediction only];


Pssm-ID: 441319 [Multi-domain]  Cd Length: 184  Bit Score: 44.73  E-value: 1.45e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1491308094  53 RFEHSLGVSFLAEKMASslRHDEDSEIisedialIRTAALLHDIGHGpFSHtfEALLSRINKHHEDLSRWLVVETEI 129
Cdd:COG1713    18 RYEHTLGVAETAVELAE--RYGVDVEK-------AELAGLLHDYAKE-LPP--EELLELAKEYGLDLDELEEYNPEL 82
HDGYP COG2206
HD-GYP domain, c-di-GMP phosphodiesterase class II (or its inactivated variant) [Signal ...
 54-97 5.74e-05

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: 43.81  E-value: 5.74e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1491308094  54 FEHSLGVSFLAEKMASSLRHDEdseiisEDIALIRTAALLHDIG 97
Cdd:COG2206   145 YGHSVRVAVLALALARELGLSE------EELEDLGLAALLHDIG 182
PRK05318 PRK05318
deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional
 22-103 6.34e-05

deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional


Pssm-ID: 235403 [Multi-domain]  Cd Length: 432  Bit Score: 43.71  E-value: 6.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308094  22 AKLIDTPYFQRLRRIKQLSGseyvyPGAN---HTRFEHSLGVSFLAEKMASSLRHDEDSEIIS--EDIALIRTAALLHDI 96
Cdd:PRK05318   30 ARILHSAAFRRLQAKTQVLG-----VGENdfyRTRLTHSLEVAQIGTGIVAQLKKEKQPELKPllPSDSLIESLCLAHDI 104


                  ....*..
gi 1491308094  97 GHGPFSH 103
Cdd:PRK05318  105 GHPPFGH 111
RnaY COG1418
HD superfamily phosphodieaserase, includes HD domain of RNase Y [Translation, ribosomal ...
 30-148 6.52e-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: 42.58  E-value: 6.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308094  30 FQRLRR-IKQLSGSEyvypGANhtRFEHSLGVSFLAEKMASSLrhdedseiiSEDIALIRTAALLHDIGHGPFSHtfeal 108
Cdd:COG1418     1 LPELIKlVKYLRTSY----GQH--DLQHSLRVAKLAGLIAAEE---------GADVEVAKRAALLHDIGKAKDHE----- 60

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1491308094 109 lsrINKHHEDLSrwlvvETEIKDILSDYNVSPSKVCGLIH 148
Cdd:COG1418    61 ---VEGSHAEIG-----AELARKYLESLGFPEEEIEAVVH 92
HDOD COG1639
HD-like signal output (HDOD) domain, no enzymatic activity [Signal transduction mechanisms];
30-118 3.42e-04

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


Pssm-ID: 441246 [Multi-domain]  Cd Length: 244  Bit Score: 41.10  E-value: 3.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308094  30 FQRLRRI------KQLSGSEYVYPGANHTRF-EHSLGVSFLAEKMASSLRHDEDSEIisedialiRTAALLHDIGHGPFS 102
Cdd:COG1639    75 LDTVRNLalalalRQLFSAKLPAYGLDLRRFwRHSLAVAAAARALARRLGLLDPEEA--------FLAGLLHDIGKLVLL 146

                          90
                  ....*....|....*.
gi 1491308094 103 HTFEALLSRINKHHED 118
Cdd:COG1639   147 SLFPEEYAELLALAEA 162
PRK12704 PRK12704
phosphodiesterase; Provisional
 56-97 9.28e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.15  E-value: 9.28e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1491308094  56 HSLGVSFLAEKMASSLrhdedseiiSEDIALIRTAALLHDIG 97
Cdd:PRK12704  339 HSIEVAHLAGLMAAEL---------GLDVKLAKRAGLLHDIG 371
HDOD pfam08668
HDOD domain;
48-97 3.31e-03

HDOD domain;


Pssm-ID: 430141 [Multi-domain]  Cd Length: 196  Bit Score: 37.59  E-value: 3.31e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1491308094  48 GANHTRF-EHSLGVSFLAEKMASSLRHDEdseiisEDIALirTAALLHDIG 97
Cdd:pfam08668  89 GFDLKGFwEHSLACALAARLLARRLGLDD------PEEAF--LAGLLHDIG 131
Phn-HD TIGR03276
phosphonate degradation operons associated HDIG domain protein; This small clade of proteins ...
 31-123 4.75e-03

phosphonate degradation operons associated HDIG domain protein; This small clade of proteins are found adjacent to other genes implicated in the catabolism of phosphonates. They are members of the TIGR00277 domain family and contain a series of five invariant histidines (the domain in general has only four).


Pssm-ID: 132319  Cd Length: 179  Bit Score: 36.96  E-value: 4.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308094  31 QRLRRIKQLSGSEYvYPGANHTRFEHSLGVSFLAEKMasslrhdedseiiSEDIALIrTAALLHDIGHGPFSHTFEALLS 110
Cdd:TIGR03276   5 DEIFALFDEHGARQ-YGGEAVSQLEHALQCAQLAEAA-------------GADDELI-VAAFLHDIGHLLADEGATPMGR 69

                          90
                  ....*....|....
gi 1491308094 111 RINKHHEDLS-RWL 123
Cdd:TIGR03276  70 GGDDHHEELAaDYL 83
 
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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