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Conserved domains on  [gi|1877322974|dbj|BBQ81239|]
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deoxyguanosinetriphosphate triphosphohydrolase-like protein 2 (plasmid) [Raoultella ornithinolytica]

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];
38-409 3.90e-112

dGTP triphosphohydrolase [Nucleotide transport and metabolism];


:

Pssm-ID: 440002 [Multi-domain]  Cd Length: 345  Bit Score: 332.50  E-value: 3.90e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877322974  38 RNEFERDYARILYSSSFRRLQGKMQLF---EVDpqkFNRNRLTHSLEVAQIARSIASELELeHHVVAELAALAHDIGNPP 114
Cdd:COG0232     4 RSPFQRDRDRIIHSAAFRRLQDKTQVFplpEGD---HYRTRLTHSLEVAQIARSIARALGL-NEDLVEAAALAHDLGHPP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877322974 115 FGHSGEKQLNKIAKDFGGYEGNAQALRILRSLEIKHPYcPGLNLTHRAILSVVKYP---FKNENGNKKFLYDNDYKYFTD 191
Cdd:COG0232    80 FGHAGEDALNELFRDLGGFEGNAQSLRILTRLEKRYAF-GGLNLTYATLDGILKYPgpsLAAPKPKPKGFYQSEKDVFDW 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877322974 192 LVNKYELDLQPGEKTIDAQIMDLSDEIAYAAHDLEDALSRSMVSIEDIVyefgrsdykdsigslnEIIEKSKATASKAfr 271
Cdd:COG0232   159 VREELGLLALGRPRTLEAQIVELADDIAYSVHDLEDAIRAGLLSLEDLP----------------ELLEYLGPLDERR-- 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877322974 272 lnsseefaiiFRKELTSNIVNVLVNDITVTQGENSFRQ--LGFG-TKENLSSGLKDIVFKVIMRKRDIKSYEHKGNMIIT 348
Cdd:COG0232   221 ----------RLGELRSRLIGRLVTDVIEASRENLFDGplIAFSpEVAAALKELKKFLFERVYRHPEVLRLELKGRRIIR 290

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1877322974 349 DLFNFYNSDnniefispqLYRTLPEEKINNEINPLYQKDKERAIVDYISGMMDTFAIREWE 409
Cdd:COG0232   291 ELFDAFLED---------PLELLPEEFRERYEAADDEYGRLRVVADYIAGMTDRYALRLYR 342
 
Name Accession Description Interval E-value
Dgt COG0232
dGTP triphosphohydrolase [Nucleotide transport and metabolism];
38-409 3.90e-112

dGTP triphosphohydrolase [Nucleotide transport and metabolism];


Pssm-ID: 440002 [Multi-domain]  Cd Length: 345  Bit Score: 332.50  E-value: 3.90e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877322974  38 RNEFERDYARILYSSSFRRLQGKMQLF---EVDpqkFNRNRLTHSLEVAQIARSIASELELeHHVVAELAALAHDIGNPP 114
Cdd:COG0232     4 RSPFQRDRDRIIHSAAFRRLQDKTQVFplpEGD---HYRTRLTHSLEVAQIARSIARALGL-NEDLVEAAALAHDLGHPP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877322974 115 FGHSGEKQLNKIAKDFGGYEGNAQALRILRSLEIKHPYcPGLNLTHRAILSVVKYP---FKNENGNKKFLYDNDYKYFTD 191
Cdd:COG0232    80 FGHAGEDALNELFRDLGGFEGNAQSLRILTRLEKRYAF-GGLNLTYATLDGILKYPgpsLAAPKPKPKGFYQSEKDVFDW 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877322974 192 LVNKYELDLQPGEKTIDAQIMDLSDEIAYAAHDLEDALSRSMVSIEDIVyefgrsdykdsigslnEIIEKSKATASKAfr 271
Cdd:COG0232   159 VREELGLLALGRPRTLEAQIVELADDIAYSVHDLEDAIRAGLLSLEDLP----------------ELLEYLGPLDERR-- 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877322974 272 lnsseefaiiFRKELTSNIVNVLVNDITVTQGENSFRQ--LGFG-TKENLSSGLKDIVFKVIMRKRDIKSYEHKGNMIIT 348
Cdd:COG0232   221 ----------RLGELRSRLIGRLVTDVIEASRENLFDGplIAFSpEVAAALKELKKFLFERVYRHPEVLRLELKGRRIIR 290

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1877322974 349 DLFNFYNSDnniefispqLYRTLPEEKINNEINPLYQKDKERAIVDYISGMMDTFAIREWE 409
Cdd:COG0232   291 ELFDAFLED---------PLELLPEEFRERYEAADDEYGRLRVVADYIAGMTDRYALRLYR 342
dGTP_triPase TIGR01353
deoxyguanosinetriphosphate triphosphohydrolase, putative; dGTP triphosphohydrolase (dgt) ...
 38-410 1.18e-105

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: 317.00  E-value: 1.18e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877322974  38 RNEFERDYARILYSSSFRRLQGKMQLFEVDPQKFNRNRLTHSLEVAQIARSIASELEL----------EHHVVAELAALA 107
Cdd:TIGR01353   2 RTPFERDYDRIIHSSAFRRLQDKTQVFPLAENDFVRTRLTHSLEVAQVGRSIANLIGLrydleleelgPFERLAETACLA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877322974 108 HDIGNPPFGHSGEKQLNKIAKDFG-GYEGNAQALRILRSLEIKHPYCPGLNLTHRAILSVVKYP--------FKNENGNK 178
Cdd:TIGR01353  82 HDIGNPPFGHAGERALNDWMREYGpGFEGNAQTFRILTTLEKRRRAKGGLNLTWRTLAGILKYPrpssedafKGGYLNKK 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877322974 179 KFLYDNDYKYFTdlvNKYELDLQPGEKTIDAQIMDLSDEIAYAAHDLEDALSRSMVSIEDIVYEFGRSDYKDSIGSLNEI 258
Cdd:TIGR01353 162 KGIYDSELAVFD---RVAELLGLTWYRSPLAQLMEAADDIAYTVHDLEDAIKLGLLTFDDLQHLLLIQAGFEELGSEMTD 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877322974 259 IEKSKATASKAFRLNSSEEFAI--IFRKELTSNIVNVLVNDItvtqgenSFRQLGFGTKEN-LSSGLKDIVFKVIMRKRD 335
Cdd:TIGR01353 239 LSISAENEQIRSLRGKLITDLIesVAKAEFSSHLVAILIGTF-------HHTLVEFSPRLAeLLEALKKFLRKRVYRHPD 311

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1877322974 336 IKSYEHKGNMIITDLFNFYNSDNNIEFISPQLYRTLPEEKINNEinplyqkdKERAIVDYISGMMDTFAIREWET 410
Cdd:TIGR01353 312 VERIEYQGEQIITGLFDAFMPDLPPRLLPPELRSKLRKAEDNYY--------KARVVCDYIAGMTDRYALEEYRR 378
antiphage_dGTPase NF041026
anti-phage deoxyguanosine triphosphatase; Proteins of this family are distant homologues of ...
 27-410 1.88e-88

anti-phage deoxyguanosine triphosphatase; Proteins of this family are distant homologues of human antiviral protein SAMHD1. It has been shown that proteins of this family protected bacteria from phage infection by degrading dGTP into phosphate-free deoxyguanosine. The anti-phage dGTPase may also be involved in other biological processes.


Pssm-ID: 468955 [Multi-domain]  Cd Length: 426  Bit Score: 274.39  E-value: 1.88e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877322974  27 EHSPSSADtrQRNEFERDYARILYSSSFRRLQGKMQLFEVDPQKFNRNRLTHSLEVAQIARSIASELELEHHVVA----- 101
Cdd:NF041026    8 EEKKRRND--HRSPFQRDRARIIHSAAFRRLQAKTQVLGLGESDFYRTRLTHSLEVAQIGTGIVAQLKAKQPEPLrallp 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877322974 102 -----ELAALAHDIGNPPFGHSGEKQLNKIAKDFGGYEGNAQALRILRSLEikhPYCP--GLNLTHRAILSVVKYP---- 170
Cdd:NF041026   86 ddsliEAICLAHDIGHPPFGHGGEVALNYMMRDHGGFEGNGQTLRILTKLE---PYTEhhGMNLTRRTLLGVLKYPalys 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877322974 171 --FKNENGNK---------------KFLYD---------------NDYKYFTDLVNKyeLDLQPGE---KTIDAQIMDLS 215
Cdd:NF041026  163 qvQAPQLPPKvsnfrqlkasdwkppKGYYDcdqdvvdwvlaplseNDRALFTSLDEK--PGKQHGKtrfKSLDCSIMELA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877322974 216 DEIAYAAHDLEDALSRSMVSIEDIVYEFGRSDYKDSIGSLNEIIEK-SKataskafRLNSSEEFAiifRKELTSNIVNVL 294
Cdd:NF041026  241 DDIAYGVHDLEDAIVLGLVTREQWQEAVAPKLAALGDPWLSDNLDElSD-------KLFSGEHYE---RKDAIGALVNYF 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877322974 295 VNDITVTQgENSFRQ--LGFGTK-----ENLSSGLKDIVFKVIMRKRDIKSYEHKGNMIITDLFNFYNSDnniefisPQl 367
Cdd:NF041026  311 ITSIEIKE-VDAFEEplLRYNAVlppevAALLEVLKQFVYQYVIRSPEVQQLEYKGQQIVMELFEALASD-------PE- 381

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 1877322974 368 yRTLPE---EKINN-EINPLYQKdkeRAIVDYISGMMDTFAIREWET 410
Cdd:NF041026  382 -RLLPEntrERWQEaEEDGENGK---RVICDYIAGMTDEYALRLYQR 424
PRK05318 PRK05318
deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional
 37-406 3.90e-79

deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional


Pssm-ID: 235403 [Multi-domain]  Cd Length: 432  Bit Score: 250.56  E-value: 3.90e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877322974  37 QRNEFERDYARILYSSSFRRLQGKMQLFEVDPQKFNRNRLTHSLEVAQIARSIASELELEHHvvAELAA----------- 105
Cdd:PRK05318   21 HRSPYQRDRARILHSAAFRRLQAKTQVLGVGENDFYRTRLTHSLEVAQIGTGIVAQLKKEKQ--PELKPllpsdsliesl 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877322974 106 -LAHDIGNPPFGHSGEKQLNKIAKDFGGYEGNAQALRILRSLEikhPYCP--GLNLTHRAILSVVKYP------------ 170
Cdd:PRK05318   99 cLAHDIGHPPFGHGGEVALNYMMRDHGGFEGNGQTFRILTKLE---PYTEhfGMNLTRRTLLGILKYPalyselvaqypp 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877322974 171 --------FKNENGNK-KFLYD---------------NDYKYFTDLVNKYELDLQPGE---KTIDAQIMDLSDEIAYAAH 223
Cdd:PRK05318  176 pdvanhrqLKASDWKPpKGIFDddqdifdwvleplseNDRALFQSLRPEPDSPKEHLKtryKSLDCSIMELADDIAYGVH 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877322974 224 DLEDALSRSMVSIEDivyeFGRSDYKDSIGSLNEIIEKSKATASKafRLNSSEEFAiifRKELTSNIVNVLVNDITVTQG 303
Cdd:PRK05318  256 DLEDAIVLGLVTRSQ----WQEDVAPQLAQCGDPWLEEEIETIGE--KLFSGEHHL---RKDAIGTLVNYFITSIRIKEN 326

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877322974 304 EN------SFR-QLGFGTKENLSSgLKDIVFKVIMRKRDIKSYEHKGNMIITDLFNFYNSDnniefisPQlyRTLPEEKI 376
Cdd:PRK05318  327 EEfeepllRYNaALEPEFAAALEV-LKQFVYKYVIRKPEVQRLEYKGQQIVMELFEALSSD-------PE--RLLPRNTQ 396

                         410       420       430
                  ....*....|....*....|....*....|
gi 1877322974 377 NNEINPLYQKDKERAIVDYISGMMDTFAIR 406
Cdd:PRK05318  397 ERWRKAEDEENSMRVICDYISGMTDEYAYR 426
HD_assoc pfam13286
Phosphohydrolase-associated domain; This domain is found on bacterial and archaeal ...
 322-409 7.69e-14

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


Pssm-ID: 433087 [Multi-domain]  Cd Length: 91  Bit Score: 66.78  E-value: 7.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877322974 322 LKDIVFKVIMRKRDIKSYEHKGNMIITDLFNFYNSDnnIEFISPQLYRTLPEEKinneinplyQKDKERAIVDYISGMMD 401
Cdd:pfam13286  14 LKRFLFEYVYRHPRVQREEEKARRIIRELFEALMAD--PELLPPEFRARWEAAG---------DDARARVVCDYIAGMTD 82


                  ....*...
gi 1877322974 402 TFAIREWE 409
Cdd:pfam13286  83 RYALRLHR 90
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
 71-134 1.56e-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: 55.38  E-value: 1.56e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1877322974   71 FNRNRLTHSLEVAQIARSIASELELEHHVVAELAALAHDIGNPPFGHSGEKQLNKIAK-DFGGYE 134
Cdd:smart00471   1 SDYHVFEHSLRVAQLAAALAEELGLLDIELLLLAALLHDIGKPGTPDSFLVKTSVLEDhHFIGAE 65
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
 73-231 2.30e-09

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 55.81  E-value: 2.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877322974  73 RNRLTHSLEVAQIARSIASELELEHH--VVAELAALAHDIGNPPFGHSGEKQLNKIAKDfggyeGNAQALRILRSLEIKH 150
Cdd:cd00077     1 EHRFEHSLRVAQLARRLAEELGLSEEdiELLRLAALLHDIGKPGTPDAITEEESELEKD-----HAIVGAEILRELLLEE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877322974 151 pycpGLNLTHRAILSVVKYPFKNENGnkkflydndykyftdlvNKYELDLQPGEKTIDAQIMDLSDEIAYAAHDLEDALS 230
Cdd:cd00077    76 ----VIKLIDELILAVDASHHERLDG-----------------LGYPDGLKGEEITLEARIVKLADRLDALRRDSREKRR 134


                  .
gi 1877322974 231 R 231
Cdd:cd00077   135 R 135
 
Name Accession Description Interval E-value
Dgt COG0232
dGTP triphosphohydrolase [Nucleotide transport and metabolism];
38-409 3.90e-112

dGTP triphosphohydrolase [Nucleotide transport and metabolism];


Pssm-ID: 440002 [Multi-domain]  Cd Length: 345  Bit Score: 332.50  E-value: 3.90e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877322974  38 RNEFERDYARILYSSSFRRLQGKMQLF---EVDpqkFNRNRLTHSLEVAQIARSIASELELeHHVVAELAALAHDIGNPP 114
Cdd:COG0232     4 RSPFQRDRDRIIHSAAFRRLQDKTQVFplpEGD---HYRTRLTHSLEVAQIARSIARALGL-NEDLVEAAALAHDLGHPP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877322974 115 FGHSGEKQLNKIAKDFGGYEGNAQALRILRSLEIKHPYcPGLNLTHRAILSVVKYP---FKNENGNKKFLYDNDYKYFTD 191
Cdd:COG0232    80 FGHAGEDALNELFRDLGGFEGNAQSLRILTRLEKRYAF-GGLNLTYATLDGILKYPgpsLAAPKPKPKGFYQSEKDVFDW 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877322974 192 LVNKYELDLQPGEKTIDAQIMDLSDEIAYAAHDLEDALSRSMVSIEDIVyefgrsdykdsigslnEIIEKSKATASKAfr 271
Cdd:COG0232   159 VREELGLLALGRPRTLEAQIVELADDIAYSVHDLEDAIRAGLLSLEDLP----------------ELLEYLGPLDERR-- 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877322974 272 lnsseefaiiFRKELTSNIVNVLVNDITVTQGENSFRQ--LGFG-TKENLSSGLKDIVFKVIMRKRDIKSYEHKGNMIIT 348
Cdd:COG0232   221 ----------RLGELRSRLIGRLVTDVIEASRENLFDGplIAFSpEVAAALKELKKFLFERVYRHPEVLRLELKGRRIIR 290

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1877322974 349 DLFNFYNSDnniefispqLYRTLPEEKINNEINPLYQKDKERAIVDYISGMMDTFAIREWE 409
Cdd:COG0232   291 ELFDAFLED---------PLELLPEEFRERYEAADDEYGRLRVVADYIAGMTDRYALRLYR 342
dGTP_triPase TIGR01353
deoxyguanosinetriphosphate triphosphohydrolase, putative; dGTP triphosphohydrolase (dgt) ...
 38-410 1.18e-105

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: 317.00  E-value: 1.18e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877322974  38 RNEFERDYARILYSSSFRRLQGKMQLFEVDPQKFNRNRLTHSLEVAQIARSIASELEL----------EHHVVAELAALA 107
Cdd:TIGR01353   2 RTPFERDYDRIIHSSAFRRLQDKTQVFPLAENDFVRTRLTHSLEVAQVGRSIANLIGLrydleleelgPFERLAETACLA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877322974 108 HDIGNPPFGHSGEKQLNKIAKDFG-GYEGNAQALRILRSLEIKHPYCPGLNLTHRAILSVVKYP--------FKNENGNK 178
Cdd:TIGR01353  82 HDIGNPPFGHAGERALNDWMREYGpGFEGNAQTFRILTTLEKRRRAKGGLNLTWRTLAGILKYPrpssedafKGGYLNKK 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877322974 179 KFLYDNDYKYFTdlvNKYELDLQPGEKTIDAQIMDLSDEIAYAAHDLEDALSRSMVSIEDIVYEFGRSDYKDSIGSLNEI 258
Cdd:TIGR01353 162 KGIYDSELAVFD---RVAELLGLTWYRSPLAQLMEAADDIAYTVHDLEDAIKLGLLTFDDLQHLLLIQAGFEELGSEMTD 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877322974 259 IEKSKATASKAFRLNSSEEFAI--IFRKELTSNIVNVLVNDItvtqgenSFRQLGFGTKEN-LSSGLKDIVFKVIMRKRD 335
Cdd:TIGR01353 239 LSISAENEQIRSLRGKLITDLIesVAKAEFSSHLVAILIGTF-------HHTLVEFSPRLAeLLEALKKFLRKRVYRHPD 311

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1877322974 336 IKSYEHKGNMIITDLFNFYNSDNNIEFISPQLYRTLPEEKINNEinplyqkdKERAIVDYISGMMDTFAIREWET 410
Cdd:TIGR01353 312 VERIEYQGEQIITGLFDAFMPDLPPRLLPPELRSKLRKAEDNYY--------KARVVCDYIAGMTDRYALEEYRR 378
antiphage_dGTPase NF041026
anti-phage deoxyguanosine triphosphatase; Proteins of this family are distant homologues of ...
 27-410 1.88e-88

anti-phage deoxyguanosine triphosphatase; Proteins of this family are distant homologues of human antiviral protein SAMHD1. It has been shown that proteins of this family protected bacteria from phage infection by degrading dGTP into phosphate-free deoxyguanosine. The anti-phage dGTPase may also be involved in other biological processes.


Pssm-ID: 468955 [Multi-domain]  Cd Length: 426  Bit Score: 274.39  E-value: 1.88e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877322974  27 EHSPSSADtrQRNEFERDYARILYSSSFRRLQGKMQLFEVDPQKFNRNRLTHSLEVAQIARSIASELELEHHVVA----- 101
Cdd:NF041026    8 EEKKRRND--HRSPFQRDRARIIHSAAFRRLQAKTQVLGLGESDFYRTRLTHSLEVAQIGTGIVAQLKAKQPEPLrallp 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877322974 102 -----ELAALAHDIGNPPFGHSGEKQLNKIAKDFGGYEGNAQALRILRSLEikhPYCP--GLNLTHRAILSVVKYP---- 170
Cdd:NF041026   86 ddsliEAICLAHDIGHPPFGHGGEVALNYMMRDHGGFEGNGQTLRILTKLE---PYTEhhGMNLTRRTLLGVLKYPalys 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877322974 171 --FKNENGNK---------------KFLYD---------------NDYKYFTDLVNKyeLDLQPGE---KTIDAQIMDLS 215
Cdd:NF041026  163 qvQAPQLPPKvsnfrqlkasdwkppKGYYDcdqdvvdwvlaplseNDRALFTSLDEK--PGKQHGKtrfKSLDCSIMELA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877322974 216 DEIAYAAHDLEDALSRSMVSIEDIVYEFGRSDYKDSIGSLNEIIEK-SKataskafRLNSSEEFAiifRKELTSNIVNVL 294
Cdd:NF041026  241 DDIAYGVHDLEDAIVLGLVTREQWQEAVAPKLAALGDPWLSDNLDElSD-------KLFSGEHYE---RKDAIGALVNYF 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877322974 295 VNDITVTQgENSFRQ--LGFGTK-----ENLSSGLKDIVFKVIMRKRDIKSYEHKGNMIITDLFNFYNSDnniefisPQl 367
Cdd:NF041026  311 ITSIEIKE-VDAFEEplLRYNAVlppevAALLEVLKQFVYQYVIRSPEVQQLEYKGQQIVMELFEALASD-------PE- 381

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 1877322974 368 yRTLPE---EKINN-EINPLYQKdkeRAIVDYISGMMDTFAIREWET 410
Cdd:NF041026  382 -RLLPEntrERWQEaEEDGENGK---RVICDYIAGMTDEYALRLYQR 424
PRK05318 PRK05318
deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional
 37-406 3.90e-79

deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional


Pssm-ID: 235403 [Multi-domain]  Cd Length: 432  Bit Score: 250.56  E-value: 3.90e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877322974  37 QRNEFERDYARILYSSSFRRLQGKMQLFEVDPQKFNRNRLTHSLEVAQIARSIASELELEHHvvAELAA----------- 105
Cdd:PRK05318   21 HRSPYQRDRARILHSAAFRRLQAKTQVLGVGENDFYRTRLTHSLEVAQIGTGIVAQLKKEKQ--PELKPllpsdsliesl 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877322974 106 -LAHDIGNPPFGHSGEKQLNKIAKDFGGYEGNAQALRILRSLEikhPYCP--GLNLTHRAILSVVKYP------------ 170
Cdd:PRK05318   99 cLAHDIGHPPFGHGGEVALNYMMRDHGGFEGNGQTFRILTKLE---PYTEhfGMNLTRRTLLGILKYPalyselvaqypp 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877322974 171 --------FKNENGNK-KFLYD---------------NDYKYFTDLVNKYELDLQPGE---KTIDAQIMDLSDEIAYAAH 223
Cdd:PRK05318  176 pdvanhrqLKASDWKPpKGIFDddqdifdwvleplseNDRALFQSLRPEPDSPKEHLKtryKSLDCSIMELADDIAYGVH 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877322974 224 DLEDALSRSMVSIEDivyeFGRSDYKDSIGSLNEIIEKSKATASKafRLNSSEEFAiifRKELTSNIVNVLVNDITVTQG 303
Cdd:PRK05318  256 DLEDAIVLGLVTRSQ----WQEDVAPQLAQCGDPWLEEEIETIGE--KLFSGEHHL---RKDAIGTLVNYFITSIRIKEN 326

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877322974 304 EN------SFR-QLGFGTKENLSSgLKDIVFKVIMRKRDIKSYEHKGNMIITDLFNFYNSDnniefisPQlyRTLPEEKI 376
Cdd:PRK05318  327 EEfeepllRYNaALEPEFAAALEV-LKQFVYKYVIRKPEVQRLEYKGQQIVMELFEALSSD-------PE--RLLPRNTQ 396

                         410       420       430
                  ....*....|....*....|....*....|
gi 1877322974 377 NNEINPLYQKDKERAIVDYISGMMDTFAIR 406
Cdd:PRK05318  397 ERWRKAEDEENSMRVICDYISGMTDEYAYR 426
PRK03007 PRK03007
deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional
 29-229 6.24e-67

deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional


Pssm-ID: 235098 [Multi-domain]  Cd Length: 428  Bit Score: 219.05  E-value: 6.24e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877322974  29 SPSSADTRQRNEFERDYARILYSSSFRRLQGKMQLfeVDPQK--FNRNRLTHSLEVAQIARSIASELELEHHVVaELAAL 106
Cdd:PRK03007   25 AGLPTEGQHRTDFARDRARVLHSAALRRLADKTQV--VGPREgdTPRTRLTHSLEVAQIGRGIAAGLGCDPDLV-DLAGL 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877322974 107 AHDIGNPPFGHSGEKQLNKIAKDFGGYEGNAQALRILRSLEIK----HPYCPGLNLThRAIL-SVVKYPFKNENG----N 177
Cdd:PRK03007  102 AHDIGHPPYGHNGERALDEVAADCGGFEGNAQTLRILTRLEPKvldpDGRSAGLNLT-RASLdAACKYPWTRGEAdgspR 180

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1877322974 178 KKF-LYDNDYKYFtDLVNKyelDLQPGEKTIDAQIMDLSDEIAYAAHDLEDAL 229
Cdd:PRK03007  181 RKFgFYDDDREVF-AWVRQ---GAPAGRPCLEAQVMDWADDVAYSVHDVEDGV 229
PRK01286 PRK01286
deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional
 20-409 1.34e-64

deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional


Pssm-ID: 234934 [Multi-domain]  Cd Length: 336  Bit Score: 210.03  E-value: 1.34e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877322974  20 SKLSSGREHSPSSADTRqrNEFERDYARILYSSSFRRLQGKMQLFeVDPQK-FNRNRLTHSLEVAQIARSIASELELEHH 98
Cdd:PRK01286   10 SANSRGRLRPEEPCPIR--TEFQRDRDRIIHSKAFRRLKHKTQVF-INPEGdHYRTRLTHTLEVAQIARTIARALRLNED 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877322974  99 VVaELAALAHDIGNPPFGHSGEKQLNKIAKDFGGYEGNAQALRILRSLEikHPYcPGLNLTHRAILSVVKYpfknengnk 178
Cdd:PRK01286   87 LT-EAIALGHDLGHTPFGHAGEDALNELMKEYGGFEHNEQSLRVVDKLE--KRY-DGLNLTWEVREGILKH--------- 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877322974 179 kflydndykyftdlvNKYELDLQPGEKTIDAQIMDLSDEIAYAAHDLEDALsRS-MVSIEDIvyefgRSDYKDSIGslne 257
Cdd:PRK01286  154 ---------------SGPRNAPLGTAATLEGQIVRLADEIAYNNHDIDDGI-RAgLITLEDL-----PEDVRRLLG---- 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877322974 258 iiekskataskafrlnsseefaiifrkELTSNIVNVLVNDITVTQGENSFRQLGFGTKENLSS-------GLKDIVFKVI 330
Cdd:PRK01286  209 ---------------------------ETHRRRINTLVVDLIKNTQRNLAEGAAAPPLVSFSEevaeamkELRRFLFENV 261

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1877322974 331 MRKRDIKSYEHKGNMIITDLFNFYNSDnniefispqlYRTLPEEkinnEINPLYQKDKERAIVDYISGMMDTFAIREWE 409
Cdd:PRK01286  262 YRHPKVKREREKAKRIVQDLFEYYMED----------PELLPPE----YQNIAEEEGLERAVADYIAGMTDRYALREYR 326
PRK01096 PRK01096
deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional
 26-404 5.05e-51

deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional


Pssm-ID: 234897 [Multi-domain]  Cd Length: 440  Bit Score: 177.42  E-value: 5.05e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877322974  26 REHSPSSADTRQRNEFERDYARILYSSSFRRLQGKMQLFEVDPQKFNRNRLTHSLEVAQIARSI---ASELELEHH---- 98
Cdd:PRK01096   13 GKKGKTSKDELGRSPFHKDYDRIIFSGSFRRLQRKTQVHPLAKNDHIHTRLTHSLEVSCVGRSLgmrVGETLKEEKlpdw 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877322974  99 -------VVAELAALAHDIGNPPFGHSGE-------------KQLNKIAK----DFGGYEGNAQALRILRSLEiKHPYCP 154
Cdd:PRK01096   93 ispadigAIVQSACLAHDIGNPPFGHFGEdairewfqdaagrGFLDDLSPqeraDFLNFEGNAQGFRVLTKLE-YHQDDG 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877322974 155 GLNLTHRAILSVVKYPFKNENGNKKFLYDNDYKYF---TDLVNK--YELDLQPGEKTIDAQ-----IMDLSDEIAYAAHD 224
Cdd:PRK01096  172 GMRLTYATLGTYIKYPWSSRHANKQQIKKKKFGCYqseLPLFEQiaEALGLPQLGEQRWCRhpltyLLEAADDICYALID 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877322974 225 LEDALSRSMVS---IEDIVYEF-GRSDYKDSIGSLNEIIEK-----SKA------TASKAFRLNSSEefaiIFRKELTSN 289
Cdd:PRK01096  252 LEDGLEMGLLNyqeVEALFLELiGDKEKYRQLGPQDSRRQKlarlrGKAigrlvnAVAEAFVENYDA----ILAGTLPGD 327

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877322974 290 IVNVlvnditvtqgensfrqlgfgTKENLSSGLKdiVFKVIMRKrdiKSYEHKG---------NMIITDLFNF------Y 354
Cdd:PRK01096  328 LIEH--------------------CDPDAKRCVQ--QAKDLARE---KIFQHKRkveleigayTILEILLDAFvpaalyY 382

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 1877322974 355 NSDNNIEFISpQLYRTLPEEKINNEINPLYQkdKERAIVDYISGMMDTFA 404
Cdd:PRK01096  383 DSGTTPSFKD-KRLLDLLGDNAPDPTMKLYL--RLLRVLDFISGMTDSYA 429
dgt PRK04926
deoxyguanosinetriphosphate triphosphohydrolase; Provisional
 20-413 1.22e-46

deoxyguanosinetriphosphate triphosphohydrolase; Provisional


Pssm-ID: 235320 [Multi-domain]  Cd Length: 503  Bit Score: 167.03  E-value: 1.22e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877322974  20 SKLSSGREHSPSSADTRQRN---EFERDYARILYSSSFRRLQGKMQLFEVDPQKFNRNRLTHSLEVAQIARSIASEL--- 93
Cdd:PRK04926    8 KKINWQRRYRSPQGVKTEHEilrIFESDRGRIINSAAIRRLQQKTQVFPLERNAAVRSRLTHSLEVQQVGRYIAKEIlsr 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877322974  94 -------------ELEHHVVA--ELAALAHDIGNPPFGHSGEKQLN---------------------------------- 124
Cdd:PRK04926   88 lkeqklleaygldELTGPFESivEMACLMHDIGNPPFGHFGEAAINdwfrqrldpdaesqpltddrcsvaalrlrdgeep 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877322974 125 ------KIAKDFGGYEGNAQALRILRSLEikhpycpGLNLTHRAILSVVKY----------PFKNENGNKKFLYdndykY 188
Cdd:PRK04926  168 lnelrrKIRQDLCHFEGNAQGIRLVHTLL-------RLNLTYAQVACILKYtrpawwrgptPASHHYLMKKPGY-----Y 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877322974 189 FT--DLVNKY--ELDLQPGEKTIDAQIMDLSDEIAYAAHDLEDALSRSMVSIEDiVYEFGRSDY-KDSIGSLNE--IIEK 261
Cdd:PRK04926  236 LSeeAYVARLrkELNLAPYSRFPLTYIMEAADDISYCIADLEDAVEKRIFSVEQ-LYHHLHEAWgEHEKGDLFSlvVENA 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877322974 262 SKATASKAFRLNSSEEFAIIFRkeltSNIVNVLVNDITVTQGEN-------SFRQL---GFGTKENLSSGLKDIVFKVIM 331
Cdd:PRK04926  315 WEKSRANSLSRSSEDQFFMYLR----VNTLNKLVPYAAQRFIDNlpaifagTFNQAlleDASPASRLLKTFKNVARKHVF 390

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877322974 332 RKRDIKSYEHKGNMIITDLFNFY---------------NSDNNIEF-ISPQLYRTLPE----------EKINNeiNPLYQ 385
Cdd:PRK04926  391 SHPEVEQLELQGYRVISGLLDIYspllalpledftelvEKERHKRYpIETRLFHKLSTrhrlayveavSKLPS--DSPEF 468

                         490       500       510
                  ....*....|....*....|....*....|...
gi 1877322974 386 KDKE-----RAIVDYISGMMDTFAireWETHCR 413
Cdd:PRK04926  469 PLWEyyyraRLIQDYISGMTDLYA---WDEYRR 498
HD_assoc pfam13286
Phosphohydrolase-associated domain; This domain is found on bacterial and archaeal ...
 322-409 7.69e-14

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


Pssm-ID: 433087 [Multi-domain]  Cd Length: 91  Bit Score: 66.78  E-value: 7.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877322974 322 LKDIVFKVIMRKRDIKSYEHKGNMIITDLFNFYNSDnnIEFISPQLYRTLPEEKinneinplyQKDKERAIVDYISGMMD 401
Cdd:pfam13286  14 LKRFLFEYVYRHPRVQREEEKARRIIRELFEALMAD--PELLPPEFRARWEAAG---------DDARARVVCDYIAGMTD 82


                  ....*...
gi 1877322974 402 TFAIREWE 409
Cdd:pfam13286  83 RYALRLHR 90
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
 71-134 1.56e-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: 55.38  E-value: 1.56e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1877322974   71 FNRNRLTHSLEVAQIARSIASELELEHHVVAELAALAHDIGNPPFGHSGEKQLNKIAK-DFGGYE 134
Cdd:smart00471   1 SDYHVFEHSLRVAQLAAALAEELGLLDIELLLLAALLHDIGKPGTPDSFLVKTSVLEDhHFIGAE 65
HD pfam01966
HD domain; HD domains are metal dependent phosphohydrolases.
 75-117 2.15e-09

HD domain; HD domains are metal dependent phosphohydrolases.


Pssm-ID: 460398 [Multi-domain]  Cd Length: 110  Bit Score: 54.93  E-value: 2.15e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1877322974  75 RLTHSLEVAQIARSIASELELEHHVVAELAALAHDIGNPPFGH 117
Cdd:pfam01966   1 RLEHSLRVALLARELAEELGELDRELLLLAALLHDIGKGPFGD 43
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
 73-231 2.30e-09

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 55.81  E-value: 2.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877322974  73 RNRLTHSLEVAQIARSIASELELEHH--VVAELAALAHDIGNPPFGHSGEKQLNKIAKDfggyeGNAQALRILRSLEIKH 150
Cdd:cd00077     1 EHRFEHSLRVAQLARRLAEELGLSEEdiELLRLAALLHDIGKPGTPDAITEEESELEKD-----HAIVGAEILRELLLEE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877322974 151 pycpGLNLTHRAILSVVKYPFKNENGnkkflydndykyftdlvNKYELDLQPGEKTIDAQIMDLSDEIAYAAHDLEDALS 230
Cdd:cd00077    76 ----VIKLIDELILAVDASHHERLDG-----------------LGYPDGLKGEEITLEARIVKLADRLDALRRDSREKRR 134


                  .
gi 1877322974 231 R 231
Cdd:cd00077   135 R 135
RnaY COG1418
HD superfamily phosphodieaserase, includes HD domain of RNase Y [Translation, ribosomal ...
 74-117 1.46e-06

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: 48.36  E-value: 1.46e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1877322974  74 NRLTHSLEVAQIARSIASELELEHHVVaELAALAHDIGNPPFGH 117
Cdd:COG1418    18 HDLQHSLRVAKLAGLIAAEEGADVEVA-KRAALLHDIGKAKDHE 60
HDOD COG1639
HD-like signal output (HDOD) domain, no enzymatic activity [Signal transduction mechanisms];
47-129 9.65e-05

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


Pssm-ID: 441246 [Multi-domain]  Cd Length: 244  Bit Score: 43.42  E-value: 9.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877322974  47 RILYSSSFRR-LQGKMQLFEVDPQKFNRnrltHSLEVAQIARSIASELELEHHVVAELAALAHDIGNPPFGHSGEKQLNK 125
Cdd:COG1639    80 NLALALALRQlFSAKLPAYGLDLRRFWR----HSLAVAAAARALARRLGLLDPEEAFLAGLLHDIGKLVLLSLFPEEYAE 155


                  ....
gi 1877322974 126 IAKD 129
Cdd:COG1639   156 LLAL 159
HDIG TIGR00277
HDIG domain; This domain is found in a few known nucleotidyltransferes and in a large number ...
 74-113 2.10e-04

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: 39.63  E-value: 2.10e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1877322974  74 NRLTHSLEVAQIARSIASELElEHHVVAELAALAHDIGNP 113
Cdd:TIGR00277   4 NVLQHSLEVAKLAEALARELG-LDVELARRGALLHDIGKP 42
PRK12704 PRK12704
phosphodiesterase; Provisional
 74-111 1.52e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.53  E-value: 1.52e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1877322974  74 NRLTHSLEVAQIARSIASELELEhHVVAELAALAHDIG 111
Cdd:PRK12704  335 NVLQHSIEVAHLAGLMAAELGLD-VKLAKRAGLLHDIG 371
HDOD pfam08668
HDOD domain;
48-111 1.63e-03

HDOD domain;


Pssm-ID: 430141 [Multi-domain]  Cd Length: 196  Bit Score: 39.52  E-value: 1.63e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1877322974  48 ILYSSSFRRLqgkmqLFEVDPQKFNRNRL-THSLEVAQIARSIASELELEHHVVAELAALAHDIG 111
Cdd:pfam08668  72 LALGISVKRI-----FRGTPPLGFDLKGFwEHSLACALAARLLARRLGLDDPEEAFLAGLLHDIG 131
PRK12705 PRK12705
hypothetical protein; Provisional
 71-111 6.22e-03

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 38.54  E-value: 6.22e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1877322974  71 FNRNRLTHSLEVAQIARSIASELELEhHVVAELAALAHDIG 111
Cdd:PRK12705  320 YGQNVLSHSLEVAHLAGIIAAEIGLD-PALAKRAGLLHDIG 359
 
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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