NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1582931838|gb|TBH11285|]
View 

deoxyguanosinetriphosphate triphosphohydrolase [Rhizobium leguminosarum]

Protein Classification

deoxyguanosinetriphosphate triphosphohydrolase family protein( domain architecture ID 11479518)

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PRK01286 PRK01286
deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional
 13-405 0e+00

deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional


:

Pssm-ID: 234934 [Multi-domain]  Cd Length: 336  Bit Score: 517.03  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582931838  13 SERAVYAADPWTTRGRLYQEDGSPTRSDFQRDRDRIVHTTAFRRLKHKTQVFIAQDGDHYRTRLTHTIEVAQIARALARA 92
Cdd:PRK01286    1 ATLAPYAALSANSRGRLRPEEPCPIRTEFQRDRDRIIHSKAFRRLKHKTQVFINPEGDHYRTRLTHTLEVAQIARTIARA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582931838  93 LKLDEDLAEGVALVHDFGHTPFGHTGEDALHEVLLPYGGFDHNAQSLRIVTKLERRYaefDGINLTWESLEGLVKHNGPL 172
Cdd:PRK01286   81 LRLNEDLTEAIALGHDLGHTPFGHAGEDALNELMKEYGGFEHNEQSLRVVDKLEKRY---DGLNLTWEVREGILKHSGPR 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582931838 173 LTADGvgtrgpvpqpildycelhdlelaTYASLEAQVAAIADDIAYNTHDIDDGLRSGYLTFDMLEEipflaglmaevra 252
Cdd:PRK01286  158 NAPLG-----------------------TAATLEGQIVRLADEIAYNNHDIDDGIRAGLITLEDLPE------------- 201

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582931838 253 ryphlEPSRFTHEIMRRQITRMVEDVIGVAQQRLSLLRpesaadiraADRVIATFSEGMAETDRQIKAMLFKRIYRNPDI 332
Cdd:PRK01286  202 -----DVRRLLGETHRRRINTLVVDLIKNTQRNLAEGA---------AAPPLVSFSEEVAEAMKELRRFLFENVYRHPKV 267

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1582931838 333 MRIRAGAAQIVTDLFAAYMANPKEMQSHYWvdhiAGLSDAPKARHVGDYLAGMTDTYAISAHRRLFDHTPDLR 405
Cdd:PRK01286  268 KREREKAKRIVQDLFEYYMEDPELLPPEYQ----NIAEEEGLERAVADYIAGMTDRYALREYRRLFVPKPWLY 336
 
Name Accession Description Interval E-value
PRK01286 PRK01286
deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional
 13-405 0e+00

deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional


Pssm-ID: 234934 [Multi-domain]  Cd Length: 336  Bit Score: 517.03  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582931838  13 SERAVYAADPWTTRGRLYQEDGSPTRSDFQRDRDRIVHTTAFRRLKHKTQVFIAQDGDHYRTRLTHTIEVAQIARALARA 92
Cdd:PRK01286    1 ATLAPYAALSANSRGRLRPEEPCPIRTEFQRDRDRIIHSKAFRRLKHKTQVFINPEGDHYRTRLTHTLEVAQIARTIARA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582931838  93 LKLDEDLAEGVALVHDFGHTPFGHTGEDALHEVLLPYGGFDHNAQSLRIVTKLERRYaefDGINLTWESLEGLVKHNGPL 172
Cdd:PRK01286   81 LRLNEDLTEAIALGHDLGHTPFGHAGEDALNELMKEYGGFEHNEQSLRVVDKLEKRY---DGLNLTWEVREGILKHSGPR 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582931838 173 LTADGvgtrgpvpqpildycelhdlelaTYASLEAQVAAIADDIAYNTHDIDDGLRSGYLTFDMLEEipflaglmaevra 252
Cdd:PRK01286  158 NAPLG-----------------------TAATLEGQIVRLADEIAYNNHDIDDGIRAGLITLEDLPE------------- 201

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582931838 253 ryphlEPSRFTHEIMRRQITRMVEDVIGVAQQRLSLLRpesaadiraADRVIATFSEGMAETDRQIKAMLFKRIYRNPDI 332
Cdd:PRK01286  202 -----DVRRLLGETHRRRINTLVVDLIKNTQRNLAEGA---------AAPPLVSFSEEVAEAMKELRRFLFENVYRHPKV 267

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1582931838 333 MRIRAGAAQIVTDLFAAYMANPKEMQSHYWvdhiAGLSDAPKARHVGDYLAGMTDTYAISAHRRLFDHTPDLR 405
Cdd:PRK01286  268 KREREKAKRIVQDLFEYYMEDPELLPPEYQ----NIAEEEGLERAVADYIAGMTDRYALREYRRLFVPKPWLY 336
Dgt COG0232
dGTP triphosphohydrolase [Nucleotide transport and metabolism];
35-398 7.47e-152

dGTP triphosphohydrolase [Nucleotide transport and metabolism];


Pssm-ID: 440002 [Multi-domain]  Cd Length: 345  Bit Score: 433.04  E-value: 7.47e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582931838  35 SPTRSDFQRDRDRIVHTTAFRRLKHKTQVFIAQDGDHYRTRLTHTIEVAQIARALARALKLDEDLAEGVALVHDFGHTPF 114
Cdd:COG0232     1 DDIRSPFQRDRDRIIHSAAFRRLQDKTQVFPLPEGDHYRTRLTHSLEVAQIARSIARALGLNEDLVEAAALAHDLGHPPF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582931838 115 GHTGEDALHEVLLPYGGFDHNAQSLRIVTKLERRYAeFDGINLTWESLEGLVKHNGPLLTADGVGTRGPVP--QPILDYC 192
Cdd:COG0232    81 GHAGEDALNELFRDLGGFEGNAQSLRILTRLEKRYA-FGGLNLTYATLDGILKYPGPSLAAPKPKPKGFYQseKDVFDWV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582931838 193 --ELHDLELATYASLEAQVAAIADDIAYNTHDIDDGLRSGYLTFDMLEEIPFLAGLMAEVRARyphlepsrftHEIMRRQ 270
Cdd:COG0232   160 reELGLLALGRPRTLEAQIVELADDIAYSVHDLEDAIRAGLLSLEDLPELLEYLGPLDERRRL----------GELRSRL 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582931838 271 ITRMVEDVIGVAQQRLsllrpesaadiraADRVIATFSEGMAETDRQIKAMLFKRIYRNPDIMRIRAGAAQIVTDLFAAY 350
Cdd:COG0232   230 IGRLVTDVIEASRENL-------------FDGPLIAFSPEVAAALKELKKFLFERVYRHPEVLRLELKGRRIIRELFDAF 296

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1582931838 351 MANPKE-MQSHYWVDHIAGLSDAPKARHVGDYLAGMTDTYAISAHRRLF 398
Cdd:COG0232   297 LEDPLElLPEEFRERYEAADDEYGRLRVVADYIAGMTDRYALRLYRRLF 345
dGTP_triPase TIGR01353
deoxyguanosinetriphosphate triphosphohydrolase, putative; dGTP triphosphohydrolase (dgt) ...
 37-398 4.71e-108

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: 322.78  E-value: 4.71e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582931838  37 TRSDFQRDRDRIVHTTAFRRLKHKTQVFIAQDGDHYRTRLTHTIEVAQIARALARALKL-----------DEDLAEGVAL 105
Cdd:TIGR01353   1 ERTPFERDYDRIIHSSAFRRLQDKTQVFPLAENDFVRTRLTHSLEVAQVGRSIANLIGLrydleleelgpFERLAETACL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582931838 106 VHDFGHTPFGHTGEDALHEVLLPYG-GFDHNAQSLRIVTKLERRYAEFDGINLTWESLEGLVKHNGPLLTADGVGtRGPV 184
Cdd:TIGR01353  81 AHDIGNPPFGHAGERALNDWMREYGpGFEGNAQTFRILTTLEKRRRAKGGLNLTWRTLAGILKYPRPSSEDAFKG-GYLN 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582931838 185 PQPILDYCEL-------HDLELATYASLEAQVAAIADDIAYNTHDIDDGLRSGYLTFDMLEEIPFLAGLMAEVRARYPHL 257
Cdd:TIGR01353 160 KKKGIYDSELavfdrvaELLGLTWYRSPLAQLMEAADDIAYTVHDLEDAIKLGLLTFDDLQHLLLIQAGFEELGSEMTDL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582931838 258 EPSRfTHEIMRRQITRMVEDVIGVAQQRLsLLRPESAADIRAADRVIATFSEGMAETDRQIKAMLFKRIYRNPDIMRIRA 337
Cdd:TIGR01353 240 SISA-ENEQIRSLRGKLITDLIESVAKAE-FSSHLVAILIGTFHHTLVEFSPRLAELLEALKKFLRKRVYRHPDVERIEY 317

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1582931838 338 GAAQIVTDLFAAYMANPKEMqsHYWVDHIAGLSDAP----KARHVGDYLAGMTDTYAISAHRRLF 398
Cdd:TIGR01353 318 QGEQIITGLFDAFMPDLPPR--LLPPELRSKLRKAEdnyyKARVVCDYIAGMTDRYALEEYRRLF 380
antiphage_dGTPase NF041026
anti-phage deoxyguanosine triphosphatase; Proteins of this family are distant homologues of ...
 23-398 5.60e-73

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: 234.32  E-value: 5.60e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582931838  23 WTTRgRLYQEDGSP--TRSDFQRDRDRIVHTTAFRRLKHKTQVFIAQDGDHYRTRLTHTIEVAQIARALARALKL----- 95
Cdd:NF041026    1 WQER-RRGEEKKRRndHRSPFQRDRARIIHSAAFRRLQAKTQVLGLGESDFYRTRLTHSLEVAQIGTGIVAQLKAkqpep 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582931838  96 ------DEDLAEGVALVHDFGHTPFGHTGEDALHEVLLPYGGFDHNAQSLRIVTKLErRYAEFDGINLTWESLEGLVKHn 169
Cdd:NF041026   80 lrallpDDSLIEAICLAHDIGHPPFGHGGEVALNYMMRDHGGFEGNGQTLRILTKLE-PYTEHHGMNLTRRTLLGVLKY- 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582931838 170 gPLLTADGVGTRGPVP----------------------QPILD-------------YCELHDLELAT-----YASLEAQV 209
Cdd:NF041026  158 -PALYSQVQAPQLPPKvsnfrqlkasdwkppkgyydcdQDVVDwvlaplsendralFTSLDEKPGKQhgktrFKSLDCSI 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582931838 210 AAIADDIAYNTHDIDDGLRSGYLTFDMLEEI---PFLAGLMAEVRARYPHLEPSRFTHEIMRR--QITRMVEDVIgvaqq 284
Cdd:NF041026  237 MELADDIAYGVHDLEDAIVLGLVTREQWQEAvapKLAALGDPWLSDNLDELSDKLFSGEHYERkdAIGALVNYFI----- 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582931838 285 rlsllrpeSAADIRAADRVI-------ATFSEGMAETDRQIKAMLFKRIYRNPDIMRIRAGAAQIVTDLFAAYMANPK-- 355
Cdd:NF041026  312 --------TSIEIKEVDAFEepllrynAVLPPEVAALLEVLKQFVYQYVIRSPEVQQLEYKGQQIVMELFEALASDPErl 383

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 1582931838 356 ---EMQSHYwvdHIAGLSDAPKARHVGDYLAGMTDTYAISAHRRLF 398
Cdd:NF041026  384 lpeNTRERW---QEAEEDGENGKRVICDYIAGMTDEYALRLYQRLF 426
HD_assoc pfam13286
Phosphohydrolase-associated domain; This domain is found on bacterial and archaeal ...
 305-396 1.03e-28

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


Pssm-ID: 433087 [Multi-domain]  Cd Length: 91  Bit Score: 107.61  E-value: 1.03e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582931838 305 ATFSEGMAETDRQIKAMLFKRIYRNPDIMRIRAGAAQIVTDLFAAYMANPKEMQSHYWVDHIAGlSDAPKARHVGDYLAG 384
Cdd:pfam13286   1 VAFSPEMAAELAELKRFLFEYVYRHPRVQREEEKARRIIRELFEALMADPELLPPEFRARWEAA-GDDARARVVCDYIAG 79

                          90
                  ....*....|..
gi 1582931838 385 MTDTYAISAHRR 396
Cdd:pfam13286  80 MTDRYALRLHRR 91
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
 73-146 3.37e-06

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: 46.14  E-value: 3.37e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1582931838   73 RTRLTHTIEVAQIARALARALKLDEDLAEGVA-LVHDFGHTPFGHTGEDALHEVllpyggFDHNAQSLRIVTKLE 146
Cdd:smart00471   3 YHVFEHSLRVAQLAAALAEELGLLDIELLLLAaLLHDIGKPGTPDSFLVKTSVL------EDHHFIGAEILLEEE 71
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
 73-148 1.10e-05

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 45.02  E-value: 1.10e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1582931838  73 RTRLTHTIEVAQIARALARALKLDEDLAEGV---ALVHDFGHTPFGHTGEDALHEVllpygGFDHNAQSLRIVTKLERR 148
Cdd:cd00077     1 EHRFEHSLRVAQLARRLAEELGLSEEDIELLrlaALLHDIGKPGTPDAITEEESEL-----EKDHAIVGAEILRELLLE 74
 
Name Accession Description Interval E-value
PRK01286 PRK01286
deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional
 13-405 0e+00

deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional


Pssm-ID: 234934 [Multi-domain]  Cd Length: 336  Bit Score: 517.03  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582931838  13 SERAVYAADPWTTRGRLYQEDGSPTRSDFQRDRDRIVHTTAFRRLKHKTQVFIAQDGDHYRTRLTHTIEVAQIARALARA 92
Cdd:PRK01286    1 ATLAPYAALSANSRGRLRPEEPCPIRTEFQRDRDRIIHSKAFRRLKHKTQVFINPEGDHYRTRLTHTLEVAQIARTIARA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582931838  93 LKLDEDLAEGVALVHDFGHTPFGHTGEDALHEVLLPYGGFDHNAQSLRIVTKLERRYaefDGINLTWESLEGLVKHNGPL 172
Cdd:PRK01286   81 LRLNEDLTEAIALGHDLGHTPFGHAGEDALNELMKEYGGFEHNEQSLRVVDKLEKRY---DGLNLTWEVREGILKHSGPR 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582931838 173 LTADGvgtrgpvpqpildycelhdlelaTYASLEAQVAAIADDIAYNTHDIDDGLRSGYLTFDMLEEipflaglmaevra 252
Cdd:PRK01286  158 NAPLG-----------------------TAATLEGQIVRLADEIAYNNHDIDDGIRAGLITLEDLPE------------- 201

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582931838 253 ryphlEPSRFTHEIMRRQITRMVEDVIGVAQQRLSLLRpesaadiraADRVIATFSEGMAETDRQIKAMLFKRIYRNPDI 332
Cdd:PRK01286  202 -----DVRRLLGETHRRRINTLVVDLIKNTQRNLAEGA---------AAPPLVSFSEEVAEAMKELRRFLFENVYRHPKV 267

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1582931838 333 MRIRAGAAQIVTDLFAAYMANPKEMQSHYWvdhiAGLSDAPKARHVGDYLAGMTDTYAISAHRRLFDHTPDLR 405
Cdd:PRK01286  268 KREREKAKRIVQDLFEYYMEDPELLPPEYQ----NIAEEEGLERAVADYIAGMTDRYALREYRRLFVPKPWLY 336
Dgt COG0232
dGTP triphosphohydrolase [Nucleotide transport and metabolism];
35-398 7.47e-152

dGTP triphosphohydrolase [Nucleotide transport and metabolism];


Pssm-ID: 440002 [Multi-domain]  Cd Length: 345  Bit Score: 433.04  E-value: 7.47e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582931838  35 SPTRSDFQRDRDRIVHTTAFRRLKHKTQVFIAQDGDHYRTRLTHTIEVAQIARALARALKLDEDLAEGVALVHDFGHTPF 114
Cdd:COG0232     1 DDIRSPFQRDRDRIIHSAAFRRLQDKTQVFPLPEGDHYRTRLTHSLEVAQIARSIARALGLNEDLVEAAALAHDLGHPPF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582931838 115 GHTGEDALHEVLLPYGGFDHNAQSLRIVTKLERRYAeFDGINLTWESLEGLVKHNGPLLTADGVGTRGPVP--QPILDYC 192
Cdd:COG0232    81 GHAGEDALNELFRDLGGFEGNAQSLRILTRLEKRYA-FGGLNLTYATLDGILKYPGPSLAAPKPKPKGFYQseKDVFDWV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582931838 193 --ELHDLELATYASLEAQVAAIADDIAYNTHDIDDGLRSGYLTFDMLEEIPFLAGLMAEVRARyphlepsrftHEIMRRQ 270
Cdd:COG0232   160 reELGLLALGRPRTLEAQIVELADDIAYSVHDLEDAIRAGLLSLEDLPELLEYLGPLDERRRL----------GELRSRL 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582931838 271 ITRMVEDVIGVAQQRLsllrpesaadiraADRVIATFSEGMAETDRQIKAMLFKRIYRNPDIMRIRAGAAQIVTDLFAAY 350
Cdd:COG0232   230 IGRLVTDVIEASRENL-------------FDGPLIAFSPEVAAALKELKKFLFERVYRHPEVLRLELKGRRIIRELFDAF 296

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1582931838 351 MANPKE-MQSHYWVDHIAGLSDAPKARHVGDYLAGMTDTYAISAHRRLF 398
Cdd:COG0232   297 LEDPLElLPEEFRERYEAADDEYGRLRVVADYIAGMTDRYALRLYRRLF 345
dGTP_triPase TIGR01353
deoxyguanosinetriphosphate triphosphohydrolase, putative; dGTP triphosphohydrolase (dgt) ...
 37-398 4.71e-108

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: 322.78  E-value: 4.71e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582931838  37 TRSDFQRDRDRIVHTTAFRRLKHKTQVFIAQDGDHYRTRLTHTIEVAQIARALARALKL-----------DEDLAEGVAL 105
Cdd:TIGR01353   1 ERTPFERDYDRIIHSSAFRRLQDKTQVFPLAENDFVRTRLTHSLEVAQVGRSIANLIGLrydleleelgpFERLAETACL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582931838 106 VHDFGHTPFGHTGEDALHEVLLPYG-GFDHNAQSLRIVTKLERRYAEFDGINLTWESLEGLVKHNGPLLTADGVGtRGPV 184
Cdd:TIGR01353  81 AHDIGNPPFGHAGERALNDWMREYGpGFEGNAQTFRILTTLEKRRRAKGGLNLTWRTLAGILKYPRPSSEDAFKG-GYLN 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582931838 185 PQPILDYCEL-------HDLELATYASLEAQVAAIADDIAYNTHDIDDGLRSGYLTFDMLEEIPFLAGLMAEVRARYPHL 257
Cdd:TIGR01353 160 KKKGIYDSELavfdrvaELLGLTWYRSPLAQLMEAADDIAYTVHDLEDAIKLGLLTFDDLQHLLLIQAGFEELGSEMTDL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582931838 258 EPSRfTHEIMRRQITRMVEDVIGVAQQRLsLLRPESAADIRAADRVIATFSEGMAETDRQIKAMLFKRIYRNPDIMRIRA 337
Cdd:TIGR01353 240 SISA-ENEQIRSLRGKLITDLIESVAKAE-FSSHLVAILIGTFHHTLVEFSPRLAELLEALKKFLRKRVYRHPDVERIEY 317

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1582931838 338 GAAQIVTDLFAAYMANPKEMqsHYWVDHIAGLSDAP----KARHVGDYLAGMTDTYAISAHRRLF 398
Cdd:TIGR01353 318 QGEQIITGLFDAFMPDLPPR--LLPPELRSKLRKAEdnyyKARVVCDYIAGMTDRYALEEYRRLF 380
antiphage_dGTPase NF041026
anti-phage deoxyguanosine triphosphatase; Proteins of this family are distant homologues of ...
 23-398 5.60e-73

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: 234.32  E-value: 5.60e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582931838  23 WTTRgRLYQEDGSP--TRSDFQRDRDRIVHTTAFRRLKHKTQVFIAQDGDHYRTRLTHTIEVAQIARALARALKL----- 95
Cdd:NF041026    1 WQER-RRGEEKKRRndHRSPFQRDRARIIHSAAFRRLQAKTQVLGLGESDFYRTRLTHSLEVAQIGTGIVAQLKAkqpep 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582931838  96 ------DEDLAEGVALVHDFGHTPFGHTGEDALHEVLLPYGGFDHNAQSLRIVTKLErRYAEFDGINLTWESLEGLVKHn 169
Cdd:NF041026   80 lrallpDDSLIEAICLAHDIGHPPFGHGGEVALNYMMRDHGGFEGNGQTLRILTKLE-PYTEHHGMNLTRRTLLGVLKY- 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582931838 170 gPLLTADGVGTRGPVP----------------------QPILD-------------YCELHDLELAT-----YASLEAQV 209
Cdd:NF041026  158 -PALYSQVQAPQLPPKvsnfrqlkasdwkppkgyydcdQDVVDwvlaplsendralFTSLDEKPGKQhgktrFKSLDCSI 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582931838 210 AAIADDIAYNTHDIDDGLRSGYLTFDMLEEI---PFLAGLMAEVRARYPHLEPSRFTHEIMRR--QITRMVEDVIgvaqq 284
Cdd:NF041026  237 MELADDIAYGVHDLEDAIVLGLVTREQWQEAvapKLAALGDPWLSDNLDELSDKLFSGEHYERkdAIGALVNYFI----- 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582931838 285 rlsllrpeSAADIRAADRVI-------ATFSEGMAETDRQIKAMLFKRIYRNPDIMRIRAGAAQIVTDLFAAYMANPK-- 355
Cdd:NF041026  312 --------TSIEIKEVDAFEepllrynAVLPPEVAALLEVLKQFVYQYVIRSPEVQQLEYKGQQIVMELFEALASDPErl 383

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 1582931838 356 ---EMQSHYwvdHIAGLSDAPKARHVGDYLAGMTDTYAISAHRRLF 398
Cdd:NF041026  384 lpeNTRERW---QEAEEDGENGKRVICDYIAGMTDEYALRLYQRLF 426
PRK05318 PRK05318
deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional
 21-398 7.60e-61

deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional


Pssm-ID: 235403 [Multi-domain]  Cd Length: 432  Bit Score: 202.80  E-value: 7.60e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582931838  21 DPWTTRgRLYQEDGSP--TRSDFQRDRDRIVHTTAFRRLKHKTQVFIAQDGDHYRTRLTHTIEVAQIARALARALKL--- 95
Cdd:PRK05318    4 SVWQER-RLGEDKQRRndHRSPYQRDRARILHSAAFRRLQAKTQVLGVGENDFYRTRLTHSLEVAQIGTGIVAQLKKekq 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582931838  96 --------DEDLAEGVALVHDFGHTPFGHTGEDALHEVLLPYGGFDHNAQSLRIVTKLErRYAEFDGINLTWESLEGLVK 167
Cdd:PRK05318   83 pelkpllpSDSLIESLCLAHDIGHPPFGHGGEVALNYMMRDHGGFEGNGQTFRILTKLE-PYTEHFGMNLTRRTLLGILK 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582931838 168 HNGPLLTADGVGTRGPVP--------------------QPILDY-----CElHDLEL----------------ATYASLE 206
Cdd:PRK05318  162 YPALYSELVAQYPPPDVAnhrqlkasdwkppkgifdddQDIFDWvleplSE-NDRALfqslrpepdspkehlkTRYKSLD 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582931838 207 AQVAAIADDIAYNTHDIDDGLRSGYLTFDMLEE--IPFLAGLMAE-VRARYPHLEPSRFTHEIMRRQ--ITRMVEDVIGV 281
Cdd:PRK05318  241 CSIMELADDIAYGVHDLEDAIVLGLVTRSQWQEdvAPQLAQCGDPwLEEEIETIGEKLFSGEHHLRKdaIGTLVNYFITS 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582931838 282 AQQRL------SLLRPEsaadiraadrviATFSEGMAETDRQIKAMLFKRIYRNPDIMRIRAGAAQIVTDLFAAYMANP- 354
Cdd:PRK05318  321 IRIKEneefeePLLRYN------------AALEPEFAAALEVLKQFVYKYVIRKPEVQRLEYKGQQIVMELFEALSSDPe 388

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 1582931838 355 ----KEMQSHYwvdhIAGLSDAPKARHVGDYLAGMTDTYAISAHRRLF 398
Cdd:PRK05318  389 rllpRNTQERW----RKAEDEENSMRVICDYISGMTDEYAYRLYQQLF 432
PRK03007 PRK03007
deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional
 9-400 4.82e-58

deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional


Pssm-ID: 235098 [Multi-domain]  Cd Length: 428  Bit Score: 195.55  E-value: 4.82e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582931838   9 GFGSSERAVYAADPWTTRGRLYQEDGsptRSDFQRDRDRIVHTTAFRRLKHKTQVFIAQDGDHYRTRLTHTIEVAQIARA 88
Cdd:PRK03007    8 PYDDFDRERRVPEPPKSAGLPTEGQH---RTDFARDRARVLHSAALRRLADKTQVVGPREGDTPRTRLTHSLEVAQIGRG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582931838  89 LARALKLDEDLAEGVALVHDFGHTPFGHTGEDALHEVLLPYGGFDHNAQSLRIVTKLE-RRYAEFD---GINLTWESLEG 164
Cdd:PRK03007   85 IAAGLGCDPDLVDLAGLAHDIGHPPYGHNGERALDEVAADCGGFEGNAQTLRILTRLEpKVLDPDGrsaGLNLTRASLDA 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582931838 165 LVKHNGPLLTADGVGTR--GPVPQ--PILDYceLHDLELATYASLEAQVAAIADDIAYNTHDIDDGLRSGYLTFDMLEEI 240
Cdd:PRK03007  165 ACKYPWTRGEADGSPRRkfGFYDDdrEVFAW--VRQGAPAGRPCLEAQVMDWADDVAYSVHDVEDGVVSGRIDLRVLADP 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582931838 241 PFLAGLMAEVRARYPHLEPSRFTHEIMRrqiTRMVEDVIGVAQQRLSLlrPESAADIRAADRVIATFSEGMAETDRQ--- 317
Cdd:PRK03007  243 VELAALAELGAAWFSGVDADELLAAADR---LSELPVVAAVGKFDGSL--RSSAALKNLTSELVGRFASAAITATRAaag 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582931838 318 -----------------------IKAMLFKRIYRNPDIMRIRAGAAQIVTDLFAAYMAN-PKEMQSHYWVDHIAGLSDAP 373
Cdd:PRK03007  318 pgpltrydadlvvpelvraevalLKTLALQFVMSDPRHLARQARQRERIHRVADALWAGaPGALDPQFRAAFNEAADDAA 397

                         410       420
                  ....*....|....*....|....*..
gi 1582931838 374 KARHVGDYLAGMTDTYAISAHRRLFDH 400
Cdd:PRK03007  398 RLRVVVDQIASLTESRLERLHARLCGR 424
PRK01096 PRK01096
deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional
 25-398 3.36e-43

deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional


Pssm-ID: 234897 [Multi-domain]  Cd Length: 440  Bit Score: 156.23  E-value: 3.36e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582931838  25 TRGRLYQEDGSPT----RSDFQRDRDRIVHTTAFRRLKHKTQVFIAQDGDHYRTRLTHTIEVAQIARALAR----ALKlD 96
Cdd:PRK01096    8 SRERLGKKGKTSKdelgRSPFHKDYDRIIFSGSFRRLQRKTQVHPLAKNDHIHTRLTHSLEVSCVGRSLGMrvgeTLK-E 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582931838  97 EDLAEGV------------ALVHDFGHTPFGHTGEDALHEVLLPYGG-----------------FDHNAQSLRIVTKLEr 147
Cdd:PRK01096   87 EKLPDWIspadigaivqsaCLAHDIGNPPFGHFGEDAIREWFQDAAGrgflddlspqeradflnFEGNAQGFRVLTKLE- 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582931838 148 rYAEFD-GINLTWESLEGLVKHNGPLLTADGVGTRG----------PVPQPILDYCELHDLELATYAS------LEAqva 210
Cdd:PRK01096  166 -YHQDDgGMRLTYATLGTYIKYPWSSRHANKQQIKKkkfgcyqselPLFEQIAEALGLPQLGEQRWCRhpltylLEA--- 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582931838 211 aiADDIAYNTHDIDDGLRSGYLTFDMLEEIpfLAGLMAEvRARYPHLEP--SRFTH--EIMRRQITRMVEDVIGV-AQQR 285
Cdd:PRK01096  242 --ADDICYALIDLEDGLEMGLLNYQEVEAL--FLELIGD-KEKYRQLGPqdSRRQKlaRLRGKAIGRLVNAVAEAfVENY 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582931838 286 LSLLRPESAADIraadrvIATFSEGMAETDRQIKAMLFKRIYRNPDIMRIRAGAAQIVTDLF-----AAYMANPKEMQSH 360
Cdd:PRK01096  317 DAILAGTLPGDL------IEHCDPDAKRCVQQAKDLAREKIFQHKRKVELEIGAYTILEILLdafvpAALYYDSGTTPSF 390

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 1582931838 361 YWVDHIAGLSD-APKA--------RHVGDYLAGMTDTYAISAHRRLF 398
Cdd:PRK01096  391 KDKRLLDLLGDnAPDPtmklylrlLRVLDFISGMTDSYAKELAQELT 437
HD_assoc pfam13286
Phosphohydrolase-associated domain; This domain is found on bacterial and archaeal ...
 305-396 1.03e-28

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


Pssm-ID: 433087 [Multi-domain]  Cd Length: 91  Bit Score: 107.61  E-value: 1.03e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582931838 305 ATFSEGMAETDRQIKAMLFKRIYRNPDIMRIRAGAAQIVTDLFAAYMANPKEMQSHYWVDHIAGlSDAPKARHVGDYLAG 384
Cdd:pfam13286   1 VAFSPEMAAELAELKRFLFEYVYRHPRVQREEEKARRIIRELFEALMADPELLPPEFRARWEAA-GDDARARVVCDYIAG 79

                          90
                  ....*....|..
gi 1582931838 385 MTDTYAISAHRR 396
Cdd:pfam13286  80 MTDRYALRLHRR 91
dgt PRK04926
deoxyguanosinetriphosphate triphosphohydrolase; Provisional
 41-237 1.00e-20

deoxyguanosinetriphosphate triphosphohydrolase; Provisional


Pssm-ID: 235320 [Multi-domain]  Cd Length: 503  Bit Score: 93.84  E-value: 1.00e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582931838  41 FQRDRDRIVHTTAFRRLKHKTQVFIAQDGDHYRTRLTHTIEVAQIARALAR-------------ALKLD------EDLAE 101
Cdd:PRK04926   32 FESDRGRIINSAAIRRLQQKTQVFPLERNAAVRSRLTHSLEVQQVGRYIAKeilsrlkeqklleAYGLDeltgpfESIVE 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582931838 102 GVALVHDFGHTPFGHTGEDA----LHEVLLPYGG------------------------------------FDHNAQSLRI 141
Cdd:PRK04926  112 MACLMHDIGNPPFGHFGEAAindwFRQRLDPDAEsqpltddrcsvaalrlrdgeeplnelrrkirqdlchFEGNAQGIRL 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582931838 142 VTKLERryaefdgINLTWESLEGLVKHNGPlltadgVGTRGPVPQPiLDY---------------CELHD-LELATYAS- 204
Cdd:PRK04926  192 VHTLLR-------LNLTYAQVACILKYTRP------AWWRGPTPAS-HHYlmkkpgyylseeayvARLRKeLNLAPYSRf 257

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1582931838 205 -----LEAqvaaiADDIAYNTHDIDDGLRSGYLTFDML 237
Cdd:PRK04926  258 pltyiMEA-----ADDISYCIADLEDAVEKRIFSVEQL 290
HD pfam01966
HD domain; HD domains are metal dependent phosphohydrolases.
 75-157 1.07e-06

HD domain; HD domains are metal dependent phosphohydrolases.


Pssm-ID: 460398 [Multi-domain]  Cd Length: 110  Bit Score: 46.84  E-value: 1.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582931838  75 RLTHTIEVAQIARALARALK-LDEDLAEGVALVHDFGHTPFGHTGEDALHEVllpyggfDHNAQSLRIVTKLERRYAEFD 153
Cdd:pfam01966   1 RLEHSLRVALLARELAEELGeLDRELLLLAALLHDIGKGPFGDEKPEFEIFL-------GHAVVGAEILRELEKRLGLED 73


                  ....
gi 1582931838 154 GINL 157
Cdd:pfam01966  74 VLKL 77
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
 73-146 3.37e-06

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: 46.14  E-value: 3.37e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1582931838   73 RTRLTHTIEVAQIARALARALKLDEDLAEGVA-LVHDFGHTPFGHTGEDALHEVllpyggFDHNAQSLRIVTKLE 146
Cdd:smart00471   3 YHVFEHSLRVAQLAAALAEELGLLDIELLLLAaLLHDIGKPGTPDSFLVKTSVL------EDHHFIGAEILLEEE 71
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
 73-148 1.10e-05

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 45.02  E-value: 1.10e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1582931838  73 RTRLTHTIEVAQIARALARALKLDEDLAEGV---ALVHDFGHTPFGHTGEDALHEVllpygGFDHNAQSLRIVTKLERR 148
Cdd:cd00077     1 EHRFEHSLRVAQLARRLAEELGLSEEDIELLrlaALLHDIGKPGTPDAITEEESEL-----EKDHAIVGAEILRELLLE 74
RnaY COG1418
HD superfamily phosphodieaserase, includes HD domain of RNase Y [Translation, ribosomal ...
 68-121 1.42e-04

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: 1.42e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1582931838  68 DGDHyrtRLTHTIEVAQIARALARALKLDEDLAEGVALVHDFGHTPFGHTGEDA 121
Cdd:COG1418    15 YGQH---DLQHSLRVAKLAGLIAAEEGADVEVAKRAALLHDIGKAKDHEVEGSH 65
HDIG TIGR00277
HDIG domain; This domain is found in a few known nucleotidyltransferes and in a large number ...
 76-126 2.62e-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: 39.24  E-value: 2.62e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1582931838  76 LTHTIEVAQIARALARALKLDEDLAEGVALVHDFG--HTPFGHTGEDalHEVL 126
Cdd:TIGR00277   6 LQHSLEVAKLAEALARELGLDVELARRGALLHDIGkpITREGVIFES--HVVV 56
PRK12704 PRK12704
phosphodiesterase; Provisional
 71-110 6.59e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.69  E-value: 6.59e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1582931838  71 HYRTR-----LTHTIEVAQIARALARALKLDEDLAEGVALVHDFG 110
Cdd:PRK12704  327 KYRTSygqnvLQHSIEVAHLAGLMAAELGLDVKLAKRAGLLHDIG 371
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH