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Conserved domains on  [gi|1198450888|gb|OUN38491|]
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metal-dependent phosphohydrolase [Massilimicrobiota sp. An80]

Protein Classification

deoxyguanosinetriphosphate triphosphohydrolase family protein( domain architecture ID 11415476)

deoxyguanosinetriphosphate triphosphohydrolase family protein similar to deoxyguanosinetriphosphate (dGTP) triphosphohydrolase, which catalyzes the hydrolysis of dGTP to form deoxyguanosine and triphosphate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Dgt COG0232
dGTP triphosphohydrolase [Nucleotide transport and metabolism];
46-381 2.09e-95

dGTP triphosphohydrolase [Nucleotide transport and metabolism];


:

Pssm-ID: 440002 [Multi-domain]  Cd Length: 345  Bit Score: 288.98  E-value: 2.09e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450888  46 DIRWPFEEDIDRVLYSKSYSRYVDKTQALSFFSNVHITKRSLHVQWVSRIARQIGRGLNLNLDLIEAIALGHDLGHAPYG 125
Cdd:COG0232     2 DIRSPFQRDRDRIIHSAAFRRLQDKTQVFPLPEGDHYRTRLTHSLEVAQIARSIARALGLNEDLVEAAALAHDLGHPPFG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450888 126 HVGEKAINDCLEErgFGYFTHNANSVRNLLFIERNGI--GYNVSLQVLDGILCHNGEiLSPIYKPDSHKTIEQFWEEYEK 203
Cdd:COG0232    82 HAGEDALNELFRD--LGGFEGNAQSLRILTRLEKRYAfgGLNLTYATLDGILKYPGP-SLAAPKPKPKGFYQSEKDVFDW 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450888 204 CWHEKDYSFKILPMTLEGCVVRISDVISYVGKDIEDAIKVGIISIDDLP--------LEVVQVLGKDNKAIINRLIGDLV 275
Cdd:COG0232   159 VREELGLLALGRPRTLEAQIVELADDIAYSVHDLEDAIRAGLLSLEDLPelleylgpLDERRRLGELRSRLIGRLVTDVI 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450888 276 IHS----YHKPYLEFSKEVFHALEILFTFISTHIHHHPTILKENEKLTRMVKELYDILYDDFIyRHYPQKGICAHVSKMT 351
Cdd:COG0232   239 EASrenlFDGPLIAFSPEVAAALKELKKFLFERVYRHPEVLRLELKGRRIIRELFDAFLEDPL-ELLPEEFRERYEAADD 317

                         330       340       350
                  ....*....|....*....|....*....|
gi 1198450888 352 ETYRqspgELIVSDYLSGMTDSYALRFYEE 381
Cdd:COG0232   318 EYGR----LRVVADYIAGMTDRYALRLYRR 343
 
Name Accession Description Interval E-value
Dgt COG0232
dGTP triphosphohydrolase [Nucleotide transport and metabolism];
46-381 2.09e-95

dGTP triphosphohydrolase [Nucleotide transport and metabolism];


Pssm-ID: 440002 [Multi-domain]  Cd Length: 345  Bit Score: 288.98  E-value: 2.09e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450888  46 DIRWPFEEDIDRVLYSKSYSRYVDKTQALSFFSNVHITKRSLHVQWVSRIARQIGRGLNLNLDLIEAIALGHDLGHAPYG 125
Cdd:COG0232     2 DIRSPFQRDRDRIIHSAAFRRLQDKTQVFPLPEGDHYRTRLTHSLEVAQIARSIARALGLNEDLVEAAALAHDLGHPPFG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450888 126 HVGEKAINDCLEErgFGYFTHNANSVRNLLFIERNGI--GYNVSLQVLDGILCHNGEiLSPIYKPDSHKTIEQFWEEYEK 203
Cdd:COG0232    82 HAGEDALNELFRD--LGGFEGNAQSLRILTRLEKRYAfgGLNLTYATLDGILKYPGP-SLAAPKPKPKGFYQSEKDVFDW 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450888 204 CWHEKDYSFKILPMTLEGCVVRISDVISYVGKDIEDAIKVGIISIDDLP--------LEVVQVLGKDNKAIINRLIGDLV 275
Cdd:COG0232   159 VREELGLLALGRPRTLEAQIVELADDIAYSVHDLEDAIRAGLLSLEDLPelleylgpLDERRRLGELRSRLIGRLVTDVI 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450888 276 IHS----YHKPYLEFSKEVFHALEILFTFISTHIHHHPTILKENEKLTRMVKELYDILYDDFIyRHYPQKGICAHVSKMT 351
Cdd:COG0232   239 EASrenlFDGPLIAFSPEVAAALKELKKFLFERVYRHPEVLRLELKGRRIIRELFDAFLEDPL-ELLPEEFRERYEAADD 317

                         330       340       350
                  ....*....|....*....|....*....|
gi 1198450888 352 ETYRqspgELIVSDYLSGMTDSYALRFYEE 381
Cdd:COG0232   318 EYGR----LRVVADYIAGMTDRYALRLYRR 343
PRK01286 PRK01286
deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional
 46-386 1.81e-82

deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional


Pssm-ID: 234934 [Multi-domain]  Cd Length: 336  Bit Score: 255.48  E-value: 1.81e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450888  46 DIRWPFEEDIDRVLYSKSYSRYVDKTQAlsFFSNV--HITKRSLHVQWVSRIARQIGRGLNLNLDLIEAIALGHDLGHAP 123
Cdd:PRK01286   24 PIRTEFQRDRDRIIHSKAFRRLKHKTQV--FINPEgdHYRTRLTHTLEVAQIARTIARALRLNEDLTEAIALGHDLGHTP 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450888 124 YGHVGEKAINDCLeeRGFGYFTHNANSVRNLLFIERNGIGYNVSLQVLDGILCHNGEILSPIYKpdshktieqfweeyek 203
Cdd:PRK01286  102 FGHAGEDALNELM--KEYGGFEHNEQSLRVVDKLEKRYDGLNLTWEVREGILKHSGPRNAPLGT---------------- 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450888 204 cwhekdysfkilPMTLEGCVVRISDVISYVGKDIEDAIKVGIISIDDLPLEVVQVLGKDNKAIINRLIGDLVIHSY---- 279
Cdd:PRK01286  164 ------------AATLEGQIVRLADEIAYNNHDIDDGIRAGLITLEDLPEDVRRLLGETHRRRINTLVVDLIKNTQrnla 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450888 280 ----HKPYLEFSKEVFHALEILFTFISTHIHHHPTILKENEKLTRMVKELYDILYDdfiyrhypqkgicaHVSKMTETYR 355
Cdd:PRK01286  232 egaaAPPLVSFSEEVAEAMKELRRFLFENVYRHPKVKREREKAKRIVQDLFEYYME--------------DPELLPPEYQ 297

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1198450888 356 QSPGEL----IVSDYLSGMTDSYALRFYEERFLPR 386
Cdd:PRK01286  298 NIAEEEglerAVADYIAGMTDRYALREYRRLFVPK 332
dGTP_triPase TIGR01353
deoxyguanosinetriphosphate triphosphohydrolase, putative; dGTP triphosphohydrolase (dgt) ...
 47-383 6.53e-52

deoxyguanosinetriphosphate triphosphohydrolase, putative; dGTP triphosphohydrolase (dgt) releases inorganic triphosphate, an unusual activity reaction product, from GTP. Its activity has been called limited to the Enterobacteriaceae, although homologous sequences are detected elsewhere. This finding casts doubt on whether the activity is shared in other species. In several of these other species, the homologous gene is found in an apparent operon with dnaG, the DNA primase gene. The enzyme from E. coli was shown to bind coopertatively to single stranded DNA. The biological role of dgt is unknown. [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]


Pssm-ID: 273571 [Multi-domain]  Cd Length: 381  Bit Score: 177.56  E-value: 6.53e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450888  47 IRWPFEEDIDRVLYSKSYSRYVDKTQALSFFSNVHITKR---SLHVQWVSR-IARQIGRGLNLNL-------DLIEAIAL 115
Cdd:TIGR01353   1 ERTPFERDYDRIIHSSAFRRLQDKTQVFPLAENDFVRTRlthSLEVAQVGRsIANLIGLRYDLELeelgpfeRLAETACL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450888 116 GHDLGHAPYGHVGEKAINDCLEERGFGyFTHNANSVRNLLFIE---RNGIGYNVSLQVLDGILCHNGEILSPIYKP-DSH 191
Cdd:TIGR01353  81 AHDIGNPPFGHAGERALNDWMREYGPG-FEGNAQTFRILTTLEkrrRAKGGLNLTWRTLAGILKYPRPSSEDAFKGgYLN 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450888 192 KTIEQFWEEYEKCWHEKDYSFKILPMTLEGCVVRISDVISYVGKDIEDAIKVGIISIDDL--------------PLEVVQ 257
Cdd:TIGR01353 160 KKKGIYDSELAVFDRVAELLGLTWYRSPLAQLMEAADDIAYTVHDLEDAIKLGLLTFDDLqhllliqagfeelgSEMTDL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450888 258 VLGKDNKAI---INRLIGDLV----------------IHSYHKPYLEFSKEVFHALEILFTFISTHIHHHPTILKENEKL 318
Cdd:TIGR01353 240 SISAENEQIrslRGKLITDLIesvakaefsshlvailIGTFHHTLVEFSPRLAELLEALKKFLRKRVYRHPDVERIEYQG 319

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1198450888 319 TRMVKELYDILYDDFIYRHYPQkgicAHVSKMTETYRQSPGELIVSDYLSGMTDSYALRFYEERF 383
Cdd:TIGR01353 320 EQIITGLFDAFMPDLPPRLLPP----ELRSKLRKAEDNYYKARVVCDYIAGMTDRYALEEYRRLF 380
HD_assoc pfam13286
Phosphohydrolase-associated domain; This domain is found on bacterial and archaeal ...
 284-381 9.19e-12

Phosphohydrolase-associated domain; This domain is found on bacterial and archaeal metal-dependent phosphohydrolases.


Pssm-ID: 433087 [Multi-domain]  Cd Length: 91  Bit Score: 60.62  E-value: 9.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450888 284 LEFSKEVFHALEILFTFISTHIHHHPTILKENEKLTRMVKELYDILYDDFiyRHYPqkgicAHVSKMTETYRQSPGELIV 363
Cdd:pfam13286   1 VAFSPEMAAELAELKRFLFEYVYRHPRVQREEEKARRIIRELFEALMADP--ELLP-----PEFRARWEAAGDDARARVV 73

                          90
                  ....*....|....*...
gi 1198450888 364 SDYLSGMTDSYALRFYEE 381
Cdd:pfam13286  74 CDYIAGMTDRYALRLHRR 91
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
 88-132 7.18e-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 [Multi-domain]  Cd Length: 124  Bit Score: 36.51  E-value: 7.18e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1198450888   88 HVQWVSRIARQIGRGLNL-NLDLIEAIALGHDLGHAPYGHVGEKAI 132
Cdd:smart00471   8 HSLRVAQLAAALAEELGLlDIELLLLAALLHDIGKPGTPDSFLVKT 53
 
Name Accession Description Interval E-value
Dgt COG0232
dGTP triphosphohydrolase [Nucleotide transport and metabolism];
46-381 2.09e-95

dGTP triphosphohydrolase [Nucleotide transport and metabolism];


Pssm-ID: 440002 [Multi-domain]  Cd Length: 345  Bit Score: 288.98  E-value: 2.09e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450888  46 DIRWPFEEDIDRVLYSKSYSRYVDKTQALSFFSNVHITKRSLHVQWVSRIARQIGRGLNLNLDLIEAIALGHDLGHAPYG 125
Cdd:COG0232     2 DIRSPFQRDRDRIIHSAAFRRLQDKTQVFPLPEGDHYRTRLTHSLEVAQIARSIARALGLNEDLVEAAALAHDLGHPPFG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450888 126 HVGEKAINDCLEErgFGYFTHNANSVRNLLFIERNGI--GYNVSLQVLDGILCHNGEiLSPIYKPDSHKTIEQFWEEYEK 203
Cdd:COG0232    82 HAGEDALNELFRD--LGGFEGNAQSLRILTRLEKRYAfgGLNLTYATLDGILKYPGP-SLAAPKPKPKGFYQSEKDVFDW 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450888 204 CWHEKDYSFKILPMTLEGCVVRISDVISYVGKDIEDAIKVGIISIDDLP--------LEVVQVLGKDNKAIINRLIGDLV 275
Cdd:COG0232   159 VREELGLLALGRPRTLEAQIVELADDIAYSVHDLEDAIRAGLLSLEDLPelleylgpLDERRRLGELRSRLIGRLVTDVI 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450888 276 IHS----YHKPYLEFSKEVFHALEILFTFISTHIHHHPTILKENEKLTRMVKELYDILYDDFIyRHYPQKGICAHVSKMT 351
Cdd:COG0232   239 EASrenlFDGPLIAFSPEVAAALKELKKFLFERVYRHPEVLRLELKGRRIIRELFDAFLEDPL-ELLPEEFRERYEAADD 317

                         330       340       350
                  ....*....|....*....|....*....|
gi 1198450888 352 ETYRqspgELIVSDYLSGMTDSYALRFYEE 381
Cdd:COG0232   318 EYGR----LRVVADYIAGMTDRYALRLYRR 343
PRK01286 PRK01286
deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional
 46-386 1.81e-82

deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional


Pssm-ID: 234934 [Multi-domain]  Cd Length: 336  Bit Score: 255.48  E-value: 1.81e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450888  46 DIRWPFEEDIDRVLYSKSYSRYVDKTQAlsFFSNV--HITKRSLHVQWVSRIARQIGRGLNLNLDLIEAIALGHDLGHAP 123
Cdd:PRK01286   24 PIRTEFQRDRDRIIHSKAFRRLKHKTQV--FINPEgdHYRTRLTHTLEVAQIARTIARALRLNEDLTEAIALGHDLGHTP 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450888 124 YGHVGEKAINDCLeeRGFGYFTHNANSVRNLLFIERNGIGYNVSLQVLDGILCHNGEILSPIYKpdshktieqfweeyek 203
Cdd:PRK01286  102 FGHAGEDALNELM--KEYGGFEHNEQSLRVVDKLEKRYDGLNLTWEVREGILKHSGPRNAPLGT---------------- 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450888 204 cwhekdysfkilPMTLEGCVVRISDVISYVGKDIEDAIKVGIISIDDLPLEVVQVLGKDNKAIINRLIGDLVIHSY---- 279
Cdd:PRK01286  164 ------------AATLEGQIVRLADEIAYNNHDIDDGIRAGLITLEDLPEDVRRLLGETHRRRINTLVVDLIKNTQrnla 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450888 280 ----HKPYLEFSKEVFHALEILFTFISTHIHHHPTILKENEKLTRMVKELYDILYDdfiyrhypqkgicaHVSKMTETYR 355
Cdd:PRK01286  232 egaaAPPLVSFSEEVAEAMKELRRFLFENVYRHPKVKREREKAKRIVQDLFEYYME--------------DPELLPPEYQ 297

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1198450888 356 QSPGEL----IVSDYLSGMTDSYALRFYEERFLPR 386
Cdd:PRK01286  298 NIAEEEglerAVADYIAGMTDRYALREYRRLFVPK 332
dGTP_triPase TIGR01353
deoxyguanosinetriphosphate triphosphohydrolase, putative; dGTP triphosphohydrolase (dgt) ...
 47-383 6.53e-52

deoxyguanosinetriphosphate triphosphohydrolase, putative; dGTP triphosphohydrolase (dgt) releases inorganic triphosphate, an unusual activity reaction product, from GTP. Its activity has been called limited to the Enterobacteriaceae, although homologous sequences are detected elsewhere. This finding casts doubt on whether the activity is shared in other species. In several of these other species, the homologous gene is found in an apparent operon with dnaG, the DNA primase gene. The enzyme from E. coli was shown to bind coopertatively to single stranded DNA. The biological role of dgt is unknown. [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]


Pssm-ID: 273571 [Multi-domain]  Cd Length: 381  Bit Score: 177.56  E-value: 6.53e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450888  47 IRWPFEEDIDRVLYSKSYSRYVDKTQALSFFSNVHITKR---SLHVQWVSR-IARQIGRGLNLNL-------DLIEAIAL 115
Cdd:TIGR01353   1 ERTPFERDYDRIIHSSAFRRLQDKTQVFPLAENDFVRTRlthSLEVAQVGRsIANLIGLRYDLELeelgpfeRLAETACL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450888 116 GHDLGHAPYGHVGEKAINDCLEERGFGyFTHNANSVRNLLFIE---RNGIGYNVSLQVLDGILCHNGEILSPIYKP-DSH 191
Cdd:TIGR01353  81 AHDIGNPPFGHAGERALNDWMREYGPG-FEGNAQTFRILTTLEkrrRAKGGLNLTWRTLAGILKYPRPSSEDAFKGgYLN 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450888 192 KTIEQFWEEYEKCWHEKDYSFKILPMTLEGCVVRISDVISYVGKDIEDAIKVGIISIDDL--------------PLEVVQ 257
Cdd:TIGR01353 160 KKKGIYDSELAVFDRVAELLGLTWYRSPLAQLMEAADDIAYTVHDLEDAIKLGLLTFDDLqhllliqagfeelgSEMTDL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450888 258 VLGKDNKAI---INRLIGDLV----------------IHSYHKPYLEFSKEVFHALEILFTFISTHIHHHPTILKENEKL 318
Cdd:TIGR01353 240 SISAENEQIrslRGKLITDLIesvakaefsshlvailIGTFHHTLVEFSPRLAELLEALKKFLRKRVYRHPDVERIEYQG 319

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1198450888 319 TRMVKELYDILYDDFIYRHYPQkgicAHVSKMTETYRQSPGELIVSDYLSGMTDSYALRFYEERF 383
Cdd:TIGR01353 320 EQIITGLFDAFMPDLPPRLLPP----ELRSKLRKAEDNYYKARVVCDYIAGMTDRYALEEYRRLF 380
PRK05318 PRK05318
deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional
 46-383 2.99e-25

deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional


Pssm-ID: 235403 [Multi-domain]  Cd Length: 432  Bit Score: 106.50  E-value: 2.99e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450888  46 DIRWPFEEDIDRVLYSKSYSRYVDKTQAL----SFFSNVHITkRSLHV-QWVSRIARQIGRGLNLNL-------DLIEAI 113
Cdd:PRK05318   20 DHRSPYQRDRARILHSAAFRRLQAKTQVLgvgeNDFYRTRLT-HSLEVaQIGTGIVAQLKKEKQPELkpllpsdSLIESL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450888 114 ALGHDLGHAPYGHVGEKAINDCLeeRGFGYFTHNANSVRNLLFIER--NGIGYNVSLQVLDGIL----CHNgeILSPIYK 187
Cdd:PRK05318   99 CLAHDIGHPPFGHGGEVALNYMM--RDHGGFEGNGQTFRILTKLEPytEHFGMNLTRRTLLGILkypaLYS--ELVAQYP 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450888 188 PDSHKTIEQF--------------------W-------------EEYEKCWHEKDYSFKILPMTLEGCVVRISDVISYVG 234
Cdd:PRK05318  175 PPDVANHRQLkasdwkppkgifdddqdifdWvleplsendralfQSLRPEPDSPKEHLKTRYKSLDCSIMELADDIAYGV 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450888 235 KDIEDAIKVGIISIDDLPLEVVQVLGKDNKA--------IINRL-----------IGDLV---IHS--------YHKPYL 284
Cdd:PRK05318  255 HDLEDAIVLGLVTRSQWQEDVAPQLAQCGDPwleeeietIGEKLfsgehhlrkdaIGTLVnyfITSirikeneeFEEPLL 334

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450888 285 ----EFSKEVFHALEILFTFISTHIHHHPTILKENEKLTRMVKELYDILYDDfiyrhyPQKGICAHVSkmtETYRQSPGE 360
Cdd:PRK05318  335 rynaALEPEFAAALEVLKQFVYKYVIRKPEVQRLEYKGQQIVMELFEALSSD------PERLLPRNTQ---ERWRKAEDE 405

                         410       420
                  ....*....|....*....|....*..
gi 1198450888 361 L----IVSDYLSGMTDSYALRFYEERF 383
Cdd:PRK05318  406 EnsmrVICDYISGMTDEYAYRLYQQLF 432
PRK03007 PRK03007
deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional
 44-158 1.08e-18

deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional


Pssm-ID: 235098 [Multi-domain]  Cd Length: 428  Bit Score: 87.31  E-value: 1.08e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450888  44 EFDIRWPFEEDIDRVLYSKSYSRYVDKTQALSffSNVHITKRS--LHVQWVSRIARQIGRGLNLNLDLIEAIALGHDLGH 121
Cdd:PRK03007   30 EGQHRTDFARDRARVLHSAALRRLADKTQVVG--PREGDTPRTrlTHSLEVAQIGRGIAAGLGCDPDLVDLAGLAHDIGH 107

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1198450888 122 APYGHVGEKAINDCLEErgFGYFTHNANSVRNLLFIE 158
Cdd:PRK03007  108 PPYGHNGERALDEVAAD--CGGFEGNAQTLRILTRLE 142
PRK01096 PRK01096
deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional
 46-381 1.52e-14

deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional


Pssm-ID: 234897 [Multi-domain]  Cd Length: 440  Bit Score: 74.57  E-value: 1.52e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450888  46 DIRWPFEEDIDRVLYSKSYSRYVDKTQALSFFSNVHITKRSLHVQWVSRIARQIGRGLNLNL---------------DLI 110
Cdd:PRK01096   23 LGRSPFHKDYDRIIFSGSFRRLQRKTQVHPLAKNDHIHTRLTHSLEVSCVGRSLGMRVGETLkeeklpdwispadigAIV 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450888 111 EAIALGHDLGHAPYGHVGEKAI---------NDCL------EERGFGYFTHNANSVRNLLFIE----RNG---------- 161
Cdd:PRK01096  103 QSACLAHDIGNPPFGHFGEDAIrewfqdaagRGFLddlspqERADFLNFEGNAQGFRVLTKLEyhqdDGGmrltyatlgt 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450888 162 -IGYNVSLQVLDGIL-------CHNGEilSPIYKPDSHKTIEQFWEEYEKCWHekdysfkilPMT--LEGcvvriSDVIS 231
Cdd:PRK01096  183 yIKYPWSSRHANKQQikkkkfgCYQSE--LPLFEQIAEALGLPQLGEQRWCRH---------PLTylLEA-----ADDIC 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450888 232 YVGKDIEDAIKVGIISIDDL----------PLEVVQVLGKDNK---------AIINRLI--------------------G 272
Cdd:PRK01096  247 YALIDLEDGLEMGLLNYQEVealfleligdKEKYRQLGPQDSRrqklarlrgKAIGRLVnavaeafvenydailagtlpG 326

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450888 273 DLVIHSyhkpylefSKEVFHALEILFTFISTHIHHHPTILkeneKLTRMVKELYDILYDDFIYRHYPQKG---------- 342
Cdd:PRK01096  327 DLIEHC--------DPDAKRCVQQAKDLAREKIFQHKRKV----ELEIGAYTILEILLDAFVPAALYYDSgttpsfkdkr 394

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 1198450888 343 ----ICAHVSKMTETYRQSpgELIVSDYLSGMTDSYALRFYEE 381
Cdd:PRK01096  395 lldlLGDNAPDPTMKLYLR--LLRVLDFISGMTDSYAKELAQE 435
HD_assoc pfam13286
Phosphohydrolase-associated domain; This domain is found on bacterial and archaeal ...
 284-381 9.19e-12

Phosphohydrolase-associated domain; This domain is found on bacterial and archaeal metal-dependent phosphohydrolases.


Pssm-ID: 433087 [Multi-domain]  Cd Length: 91  Bit Score: 60.62  E-value: 9.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450888 284 LEFSKEVFHALEILFTFISTHIHHHPTILKENEKLTRMVKELYDILYDDFiyRHYPqkgicAHVSKMTETYRQSPGELIV 363
Cdd:pfam13286   1 VAFSPEMAAELAELKRFLFEYVYRHPRVQREEEKARRIIRELFEALMADP--ELLP-----PEFRARWEAAGDDARARVV 73

                          90
                  ....*....|....*...
gi 1198450888 364 SDYLSGMTDSYALRFYEE 381
Cdd:pfam13286  74 CDYIAGMTDRYALRLHRR 91
dgt PRK04926
deoxyguanosinetriphosphate triphosphohydrolase; Provisional
 51-381 4.21e-11

deoxyguanosinetriphosphate triphosphohydrolase; Provisional


Pssm-ID: 235320 [Multi-domain]  Cd Length: 503  Bit Score: 64.18  E-value: 4.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450888  51 FEEDIDRVLYSKSYSRYVDKTQALSFFSNVHITKR---SLHVQWVSR-IARQI-------GRGLNLNLD--------LIE 111
Cdd:PRK04926   32 FESDRGRIINSAAIRRLQQKTQVFPLERNAAVRSRlthSLEVQQVGRyIAKEIlsrlkeqKLLEAYGLDeltgpfesIVE 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450888 112 AIALGHDLGHAPYGHVGEKAINDCLEERGFGYFTHNANSV-RNLLFIERNGIGyNVSLQVLDGI----LCH---N----- 178
Cdd:PRK04926  112 MACLMHDIGNPPFGHFGEAAINDWFRQRLDPDAESQPLTDdRCSVAALRLRDG-EEPLNELRRKirqdLCHfegNaqgir 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450888 179 ---------------GEIL---SPIY----KPDSH----KTIEQFWEE---YEKCWHEKDYSfkilpmtlEGC------V 223
Cdd:PRK04926  191 lvhtllrlnltyaqvACILkytRPAWwrgpTPASHhylmKKPGYYLSEeayVARLRKELNLA--------PYSrfpltyI 262

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450888 224 VRISDVISYVGKDIEDAIKVGIISIDDLPLEVVQVLGKDNKAIINR------------------------------LIGD 273
Cdd:PRK04926  263 MEAADDISYCIADLEDAVEKRIFSVEQLYHHLHEAWGEHEKGDLFSlvvenaweksranslsrssedqffmylrvnTLNK 342

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450888 274 LVIHSYHKpYLEFSKEVFHA----------------LEILFTFISTHIHHHPtilkENEKLT----RMVKELYDIL---- 329
Cdd:PRK04926  343 LVPYAAQR-FIDNLPAIFAGtfnqalledaspasrlLKTFKNVARKHVFSHP----EVEQLElqgyRVISGLLDIYspll 417

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450888 330 ---YDDF-----------------IYRHYPQKGICAHVSKMTETYRQSPGE----------LIVsDYLSGMTDSYAlrfY 379
Cdd:PRK04926  418 alpLEDFtelvekerhkrypietrLFHKLSTRHRLAYVEAVSKLPSDSPEFplweyyyrarLIQ-DYISGMTDLYA---W 493


                  ..
gi 1198450888 380 EE 381
Cdd:PRK04926  494 DE 495
RnaY COG1418
HD superfamily phosphodieaserase, includes HD domain of RNase Y [Translation, ribosomal ...
 88-234 2.77e-03

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: 38.73  E-value: 2.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450888  88 HVQWVSRIARQIGRGLNLNLDLIEAIALGHDLGHAPYGHVGEKAindclEERGfgyfthnANSVRNLLfiERNGIGYNVS 167
Cdd:COG1418    22 HSLRVAKLAGLIAAEEGADVEVAKRAALLHDIGKAKDHEVEGSH-----AEIG-------AELARKYL--ESLGFPEEEI 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1198450888 168 LQVLDGILCHNgeilspiykpdshktieqfweeyekcwhekdYSFKILPMTLEGCVVRISDVISYVG 234
Cdd:COG1418    88 EAVVHAIEAHS-------------------------------FSGGIEPESLEAKIVQDADRLDALG 123
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
 88-132 7.18e-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 [Multi-domain]  Cd Length: 124  Bit Score: 36.51  E-value: 7.18e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1198450888   88 HVQWVSRIARQIGRGLNL-NLDLIEAIALGHDLGHAPYGHVGEKAI 132
Cdd:smart00471   8 HSLRVAQLAAALAEELGLlDIELLLLAALLHDIGKPGTPDSFLVKT 53
HD pfam01966
HD domain; HD domains are metal dependent phosphohydrolases.
 88-126 8.49e-03

HD domain; HD domains are metal dependent phosphohydrolases.


Pssm-ID: 460398 [Multi-domain]  Cd Length: 110  Bit Score: 35.67  E-value: 8.49e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1198450888  88 HVQWVSRIARQIGRGLN-LNLDLIEAIALGHDLGHAPYGH 126
Cdd:pfam01966   4 HSLRVALLARELAEELGeLDRELLLLAALLHDIGKGPFGD 43
 
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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