NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1092788282|ref|WP_070709477|]
View 

MULTISPECIES: deoxyguanosinetriphosphate triphosphohydrolase [Micrococcus]

Protein Classification

deoxyguanosinetriphosphate triphosphohydrolase family protein( domain architecture ID 11479872)

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
PRK03007 PRK03007
deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional
 1-411 0e+00

deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional


:

Pssm-ID: 235098 [Multi-domain]  Cd Length: 428  Bit Score: 600.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092788282   1 MQTPGYTPWDRERWLPEPPKSS-------YRSDFERDRARVLHSAGLRRLGAKTQVVAPDADDFARTRLTHSLEVAQVGR 73
Cdd:PRK03007    4 MPQDPYDDFDRERRVPEPPKSAglptegqHRTDFARDRARVLHSAALRRLADKTQVVGPREGDTPRTRLTHSLEVAQIGR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092788282  74 ELGRSLGCDPDLVDTACLSHDLGHPPFGHNGEKALDALSEDVGGFEGNAQTLRLLARLEQKKLFADGSSAGLNLTRAALD 153
Cdd:PRK03007   84 GIAAGLGCDPDLVDLAGLAHDIGHPPYGHNGERALDEVAADCGGFEGNAQTLRILTRLEPKVLDPDGRSAGLNLTRASLD 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092788282 154 AACKYPWTREDaplrPDGTRSRKFGVYEDDLPVFRWFRAGVPGTRTSMEAQVMDLADDISYSVHDVEDGVVNAVFQLKWL 233
Cdd:PRK03007  164 AACKYPWTRGE----ADGSPRRKFGFYDDDREVFAWVRQGAPAGRPCLEAQVMDWADDVAYSVHDVEDGVVSGRIDLRVL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092788282 234 AIPEHRERVVETTRQWYlPHTDPAEVDAALARLEATDVW--VSEMDGSRRALAAMKDMTSQLIGRFCSAAFDATRQVFGN 311
Cdd:PRK03007  240 ADPVELAALAELGAAWF-SGVDADELLAAADRLSELPVVaaVGKFDGSLRSSAALKNLTSELVGRFASAAITATRAAAGP 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092788282 312 EPLTRHGADVVVPEETETEIAVMKGIAAAYVMTAEQRQPLYARQREVLAELVALLDATGDRYLEPMFAFDWAQAPDDAAR 391
Cdd:PRK03007  319 GPLTRYDADLVVPELVRAEVALLKTLALQFVMSDPRHLARQARQRERIHRVADALWAGAPGALDPQFRAAFNEAADDAAR 398

                         410       420
                  ....*....|....*....|
gi 1092788282 392 RRVVIDQIASLTDSTAVEWH 411
Cdd:PRK03007  399 LRVVVDQIASLTESRLERLH 418
 
Name Accession Description Interval E-value
PRK03007 PRK03007
deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional
 1-411 0e+00

deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional


Pssm-ID: 235098 [Multi-domain]  Cd Length: 428  Bit Score: 600.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092788282   1 MQTPGYTPWDRERWLPEPPKSS-------YRSDFERDRARVLHSAGLRRLGAKTQVVAPDADDFARTRLTHSLEVAQVGR 73
Cdd:PRK03007    4 MPQDPYDDFDRERRVPEPPKSAglptegqHRTDFARDRARVLHSAALRRLADKTQVVGPREGDTPRTRLTHSLEVAQIGR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092788282  74 ELGRSLGCDPDLVDTACLSHDLGHPPFGHNGEKALDALSEDVGGFEGNAQTLRLLARLEQKKLFADGSSAGLNLTRAALD 153
Cdd:PRK03007   84 GIAAGLGCDPDLVDLAGLAHDIGHPPYGHNGERALDEVAADCGGFEGNAQTLRILTRLEPKVLDPDGRSAGLNLTRASLD 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092788282 154 AACKYPWTREDaplrPDGTRSRKFGVYEDDLPVFRWFRAGVPGTRTSMEAQVMDLADDISYSVHDVEDGVVNAVFQLKWL 233
Cdd:PRK03007  164 AACKYPWTRGE----ADGSPRRKFGFYDDDREVFAWVRQGAPAGRPCLEAQVMDWADDVAYSVHDVEDGVVSGRIDLRVL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092788282 234 AIPEHRERVVETTRQWYlPHTDPAEVDAALARLEATDVW--VSEMDGSRRALAAMKDMTSQLIGRFCSAAFDATRQVFGN 311
Cdd:PRK03007  240 ADPVELAALAELGAAWF-SGVDADELLAAADRLSELPVVaaVGKFDGSLRSSAALKNLTSELVGRFASAAITATRAAAGP 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092788282 312 EPLTRHGADVVVPEETETEIAVMKGIAAAYVMTAEQRQPLYARQREVLAELVALLDATGDRYLEPMFAFDWAQAPDDAAR 391
Cdd:PRK03007  319 GPLTRYDADLVVPELVRAEVALLKTLALQFVMSDPRHLARQARQRERIHRVADALWAGAPGALDPQFRAAFNEAADDAAR 398

                         410       420
                  ....*....|....*....|
gi 1092788282 392 RRVVIDQIASLTDSTAVEWH 411
Cdd:PRK03007  399 LRVVVDQIASLTESRLERLH 418
Dgt COG0232
dGTP triphosphohydrolase [Nucleotide transport and metabolism];
21-414 2.90e-141

dGTP triphosphohydrolase [Nucleotide transport and metabolism];


Pssm-ID: 440002 [Multi-domain]  Cd Length: 345  Bit Score: 406.85  E-value: 2.90e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092788282  21 SSYRSDFERDRARVLHSAGLRRLGAKTQVVAPDADDFARTRLTHSLEVAQVGRELGRSLGCDPDLVDTACLSHDLGHPPF 100
Cdd:COG0232     1 DDIRSPFQRDRDRIIHSAAFRRLQDKTQVFPLPEGDHYRTRLTHSLEVAQIARSIARALGLNEDLVEAAALAHDLGHPPF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092788282 101 GHNGEKALDALSEDVGGFEGNAQTLRLLARLEQKKLFadgssAGLNLTRAALDAACKYPWTREDAPlrpdgtRSRKFGVY 180
Cdd:COG0232    81 GHAGEDALNELFRDLGGFEGNAQSLRILTRLEKRYAF-----GGLNLTYATLDGILKYPGPSLAAP------KPKPKGFY 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092788282 181 EDDLPVFRWFRAGV----PGTRTSMEAQVMDLADDISYSVHDVEDGVVNAVFqlkwlaipehrervvettrqwylphtDP 256
Cdd:COG0232   150 QSEKDVFDWVREELgllaLGRPRTLEAQIVELADDIAYSVHDLEDAIRAGLL--------------------------SL 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092788282 257 AEVDAALARleatdvwvsemDGSRRALAAMKDMTSQLIGRFCSAAFDATRQVFGNEPLtrhgadVVVPEETETEIAVMKG 336
Cdd:COG0232   204 EDLPELLEY-----------LGPLDERRRLGELRSRLIGRLVTDVIEASRENLFDGPL------IAFSPEVAAALKELKK 266

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1092788282 337 IAAAYVMTAEQRQPLYARQREVLAELVALLDATGDRYLEPMFAFDWAQAPDDAARRRVVIDQIASLTDSTAVEWHHTL 414
Cdd:COG0232   267 FLFERVYRHPEVLRLELKGRRIIRELFDAFLEDPLELLPEEFRERYEAADDEYGRLRVVADYIAGMTDRYALRLYRRL 344
antiphage_dGTPase NF041026
anti-phage deoxyguanosine triphosphatase; Proteins of this family are distant homologues of ...
 9-414 1.44e-90

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: 280.55  E-value: 1.44e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092788282   9 WDRERWLPEPPKSS-YRSDFERDRARVLHSAGLRRLGAKTQVVAPDADDFARTRLTHSLEVAQVGR-----------ELG 76
Cdd:NF041026    1 WQERRRGEEKKRRNdHRSPFQRDRARIIHSAAFRRLQAKTQVLGLGESDFYRTRLTHSLEVAQIGTgivaqlkakqpEPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092788282  77 RSLGCDPDLVDTACLSHDLGHPPFGHNGEKALDALSEDVGGFEGNAQTLRLLARLEQKKlfadgSSAGLNLTRAALDAAC 156
Cdd:NF041026   81 RALLPDDSLIEAICLAHDIGHPPFGHGGEVALNYMMRDHGGFEGNGQTLRILTKLEPYT-----EHHGMNLTRRTLLGVL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092788282 157 KYP--WTREDAPLRPDGTRSRKF----------GVYEDDLPVFRW---------------FRAGVPGT--RT---SMEAQ 204
Cdd:NF041026  156 KYPalYSQVQAPQLPPKVSNFRQlkasdwkppkGYYDCDQDVVDWvlaplsendralftsLDEKPGKQhgKTrfkSLDCS 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092788282 205 VMDLADDISYSVHDVEDGVVnavfqLKWLaipehrervveTTRQWYlPHTDPAEVDAALARLEATDVWVSEM----DGSR 280
Cdd:NF041026  236 IMELADDIAYGVHDLEDAIV-----LGLV-----------TREQWQ-EAVAPKLAALGDPWLSDNLDELSDKlfsgEHYE 298

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092788282 281 RalaamKDMTSQLIGRFCSAAFDATRQVFgNEPLTRHGAdvVVPEETETEIAVMKGIAAAYVMTAEQRQPLYARQREVLA 360
Cdd:NF041026  299 R-----KDAIGALVNYFITSIEIKEVDAF-EEPLLRYNA--VLPPEVAALLEVLKQFVYQYVIRSPEVQQLEYKGQQIVM 370

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1092788282 361 ELVALLDATGDRYLEPMFAFDWAQAPDD-AARRRVVIDQIASLTDSTAVEWHHTL 414
Cdd:NF041026  371 ELFEALASDPERLLPENTRERWQEAEEDgENGKRVICDYIAGMTDEYALRLYQRL 425
dGTP_triPase TIGR01353
deoxyguanosinetriphosphate triphosphohydrolase, putative; dGTP triphosphohydrolase (dgt) ...
 23-414 6.29e-84

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: 261.92  E-value: 6.29e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092788282  23 YRSDFERDRARVLHSAGLRRLGAKTQVVAPDADDFARTRLTHSLEVAQVGRELGRSLG-----------CDPDLVDTACL 91
Cdd:TIGR01353   1 ERTPFERDYDRIIHSSAFRRLQDKTQVFPLAENDFVRTRLTHSLEVAQVGRSIANLIGlrydleleelgPFERLAETACL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092788282  92 SHDLGHPPFGHNGEKALDALSEDVG-GFEGNAQTLRLLARLEQKKlfadGSSAGLNLTRAALDAACKYPWTREDAPlRPD 170
Cdd:TIGR01353  81 AHDIGNPPFGHAGERALNDWMREYGpGFEGNAQTFRILTTLEKRR----RAKGGLNLTWRTLAGILKYPRPSSEDA-FKG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092788282 171 GTRSRKFGVYEDDLPVFRWFRAGVPGTRT-SMEAQVMDLADDISYSVHDVEDGvvnavFQLKWLaipeHRERVVEttrqw 249
Cdd:TIGR01353 156 GYLNKKKGIYDSELAVFDRVAELLGLTWYrSPLAQLMEAADDIAYTVHDLEDA-----IKLGLL----TFDDLQH----- 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092788282 250 yLPHTDP--AEVDAALARLEATDvwvsemdgsrrALAAMKDMTSQLIGRFCSAAfdATRQVFGNEPL----TRHGADVVV 323
Cdd:TIGR01353 222 -LLLIQAgfEELGSEMTDLSISA-----------ENEQIRSLRGKLITDLIESV--AKAEFSSHLVAiligTFHHTLVEF 287

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092788282 324 PEETETEIAVMKGIAAAYVMTAEQRQPLYARQREVLAELV-ALLDATGDRYLEPMFAFDWAQAPDDAARRRVVIDQIASL 402
Cdd:TIGR01353 288 SPRLAELLEALKKFLRKRVYRHPDVERIEYQGEQIITGLFdAFMPDLPPRLLPPELRSKLRKAEDNYYKARVVCDYIAGM 367

                         410
                  ....*....|..
gi 1092788282 403 TDSTAVEWHHTL 414
Cdd:TIGR01353 368 TDRYALEEYRRL 379
HD_assoc pfam13286
Phosphohydrolase-associated domain; This domain is found on bacterial and archaeal ...
 321-412 6.54e-24

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


Pssm-ID: 433087 [Multi-domain]  Cd Length: 91  Bit Score: 94.90  E-value: 6.54e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092788282 321 VVVPEETETEIAVMKGIAAAYVMTAEQRQPLYARQREVLAELVALLDATGDRyLEPMFAFDWAQAPDDaARRRVVIDQIA 400
Cdd:pfam13286   1 VAFSPEMAAELAELKRFLFEYVYRHPRVQREEEKARRIIRELFEALMADPEL-LPPEFRARWEAAGDD-ARARVVCDYIA 78

                          90
                  ....*....|..
gi 1092788282 401 SLTDSTAVEWHH 412
Cdd:pfam13286  79 GMTDRYALRLHR 90
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
 57-111 1.53e-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: 55.77  E-value: 1.53e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1092788282   57 FARTRLTHSLEVAQVGRELGRSLGC-DPDLVDTACLSHDLGHPPFGHNGEKALDAL 111
Cdd:smart00471   1 SDYHVFEHSLRVAQLAAALAEELGLlDIELLLLAALLHDIGKPGTPDSFLVKTSVL 56
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
 59-102 3.78e-06

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 46.56  E-value: 3.78e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1092788282  59 RTRLTHSLEVAQVGRELGRSLG---CDPDLVDTACLSHDLGHPPFGH 102
Cdd:cd00077     1 EHRFEHSLRVAQLARRLAEELGlseEDIELLRLAALLHDIGKPGTPD 47
 
Name Accession Description Interval E-value
PRK03007 PRK03007
deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional
 1-411 0e+00

deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional


Pssm-ID: 235098 [Multi-domain]  Cd Length: 428  Bit Score: 600.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092788282   1 MQTPGYTPWDRERWLPEPPKSS-------YRSDFERDRARVLHSAGLRRLGAKTQVVAPDADDFARTRLTHSLEVAQVGR 73
Cdd:PRK03007    4 MPQDPYDDFDRERRVPEPPKSAglptegqHRTDFARDRARVLHSAALRRLADKTQVVGPREGDTPRTRLTHSLEVAQIGR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092788282  74 ELGRSLGCDPDLVDTACLSHDLGHPPFGHNGEKALDALSEDVGGFEGNAQTLRLLARLEQKKLFADGSSAGLNLTRAALD 153
Cdd:PRK03007   84 GIAAGLGCDPDLVDLAGLAHDIGHPPYGHNGERALDEVAADCGGFEGNAQTLRILTRLEPKVLDPDGRSAGLNLTRASLD 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092788282 154 AACKYPWTREDaplrPDGTRSRKFGVYEDDLPVFRWFRAGVPGTRTSMEAQVMDLADDISYSVHDVEDGVVNAVFQLKWL 233
Cdd:PRK03007  164 AACKYPWTRGE----ADGSPRRKFGFYDDDREVFAWVRQGAPAGRPCLEAQVMDWADDVAYSVHDVEDGVVSGRIDLRVL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092788282 234 AIPEHRERVVETTRQWYlPHTDPAEVDAALARLEATDVW--VSEMDGSRRALAAMKDMTSQLIGRFCSAAFDATRQVFGN 311
Cdd:PRK03007  240 ADPVELAALAELGAAWF-SGVDADELLAAADRLSELPVVaaVGKFDGSLRSSAALKNLTSELVGRFASAAITATRAAAGP 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092788282 312 EPLTRHGADVVVPEETETEIAVMKGIAAAYVMTAEQRQPLYARQREVLAELVALLDATGDRYLEPMFAFDWAQAPDDAAR 391
Cdd:PRK03007  319 GPLTRYDADLVVPELVRAEVALLKTLALQFVMSDPRHLARQARQRERIHRVADALWAGAPGALDPQFRAAFNEAADDAAR 398

                         410       420
                  ....*....|....*....|
gi 1092788282 392 RRVVIDQIASLTDSTAVEWH 411
Cdd:PRK03007  399 LRVVVDQIASLTESRLERLH 418
Dgt COG0232
dGTP triphosphohydrolase [Nucleotide transport and metabolism];
21-414 2.90e-141

dGTP triphosphohydrolase [Nucleotide transport and metabolism];


Pssm-ID: 440002 [Multi-domain]  Cd Length: 345  Bit Score: 406.85  E-value: 2.90e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092788282  21 SSYRSDFERDRARVLHSAGLRRLGAKTQVVAPDADDFARTRLTHSLEVAQVGRELGRSLGCDPDLVDTACLSHDLGHPPF 100
Cdd:COG0232     1 DDIRSPFQRDRDRIIHSAAFRRLQDKTQVFPLPEGDHYRTRLTHSLEVAQIARSIARALGLNEDLVEAAALAHDLGHPPF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092788282 101 GHNGEKALDALSEDVGGFEGNAQTLRLLARLEQKKLFadgssAGLNLTRAALDAACKYPWTREDAPlrpdgtRSRKFGVY 180
Cdd:COG0232    81 GHAGEDALNELFRDLGGFEGNAQSLRILTRLEKRYAF-----GGLNLTYATLDGILKYPGPSLAAP------KPKPKGFY 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092788282 181 EDDLPVFRWFRAGV----PGTRTSMEAQVMDLADDISYSVHDVEDGVVNAVFqlkwlaipehrervvettrqwylphtDP 256
Cdd:COG0232   150 QSEKDVFDWVREELgllaLGRPRTLEAQIVELADDIAYSVHDLEDAIRAGLL--------------------------SL 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092788282 257 AEVDAALARleatdvwvsemDGSRRALAAMKDMTSQLIGRFCSAAFDATRQVFGNEPLtrhgadVVVPEETETEIAVMKG 336
Cdd:COG0232   204 EDLPELLEY-----------LGPLDERRRLGELRSRLIGRLVTDVIEASRENLFDGPL------IAFSPEVAAALKELKK 266

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1092788282 337 IAAAYVMTAEQRQPLYARQREVLAELVALLDATGDRYLEPMFAFDWAQAPDDAARRRVVIDQIASLTDSTAVEWHHTL 414
Cdd:COG0232   267 FLFERVYRHPEVLRLELKGRRIIRELFDAFLEDPLELLPEEFRERYEAADDEYGRLRVVADYIAGMTDRYALRLYRRL 344
antiphage_dGTPase NF041026
anti-phage deoxyguanosine triphosphatase; Proteins of this family are distant homologues of ...
 9-414 1.44e-90

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: 280.55  E-value: 1.44e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092788282   9 WDRERWLPEPPKSS-YRSDFERDRARVLHSAGLRRLGAKTQVVAPDADDFARTRLTHSLEVAQVGR-----------ELG 76
Cdd:NF041026    1 WQERRRGEEKKRRNdHRSPFQRDRARIIHSAAFRRLQAKTQVLGLGESDFYRTRLTHSLEVAQIGTgivaqlkakqpEPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092788282  77 RSLGCDPDLVDTACLSHDLGHPPFGHNGEKALDALSEDVGGFEGNAQTLRLLARLEQKKlfadgSSAGLNLTRAALDAAC 156
Cdd:NF041026   81 RALLPDDSLIEAICLAHDIGHPPFGHGGEVALNYMMRDHGGFEGNGQTLRILTKLEPYT-----EHHGMNLTRRTLLGVL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092788282 157 KYP--WTREDAPLRPDGTRSRKF----------GVYEDDLPVFRW---------------FRAGVPGT--RT---SMEAQ 204
Cdd:NF041026  156 KYPalYSQVQAPQLPPKVSNFRQlkasdwkppkGYYDCDQDVVDWvlaplsendralftsLDEKPGKQhgKTrfkSLDCS 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092788282 205 VMDLADDISYSVHDVEDGVVnavfqLKWLaipehrervveTTRQWYlPHTDPAEVDAALARLEATDVWVSEM----DGSR 280
Cdd:NF041026  236 IMELADDIAYGVHDLEDAIV-----LGLV-----------TREQWQ-EAVAPKLAALGDPWLSDNLDELSDKlfsgEHYE 298

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092788282 281 RalaamKDMTSQLIGRFCSAAFDATRQVFgNEPLTRHGAdvVVPEETETEIAVMKGIAAAYVMTAEQRQPLYARQREVLA 360
Cdd:NF041026  299 R-----KDAIGALVNYFITSIEIKEVDAF-EEPLLRYNA--VLPPEVAALLEVLKQFVYQYVIRSPEVQQLEYKGQQIVM 370

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1092788282 361 ELVALLDATGDRYLEPMFAFDWAQAPDD-AARRRVVIDQIASLTDSTAVEWHHTL 414
Cdd:NF041026  371 ELFEALASDPERLLPENTRERWQEAEEDgENGKRVICDYIAGMTDEYALRLYQRL 425
dGTP_triPase TIGR01353
deoxyguanosinetriphosphate triphosphohydrolase, putative; dGTP triphosphohydrolase (dgt) ...
 23-414 6.29e-84

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: 261.92  E-value: 6.29e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092788282  23 YRSDFERDRARVLHSAGLRRLGAKTQVVAPDADDFARTRLTHSLEVAQVGRELGRSLG-----------CDPDLVDTACL 91
Cdd:TIGR01353   1 ERTPFERDYDRIIHSSAFRRLQDKTQVFPLAENDFVRTRLTHSLEVAQVGRSIANLIGlrydleleelgPFERLAETACL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092788282  92 SHDLGHPPFGHNGEKALDALSEDVG-GFEGNAQTLRLLARLEQKKlfadGSSAGLNLTRAALDAACKYPWTREDAPlRPD 170
Cdd:TIGR01353  81 AHDIGNPPFGHAGERALNDWMREYGpGFEGNAQTFRILTTLEKRR----RAKGGLNLTWRTLAGILKYPRPSSEDA-FKG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092788282 171 GTRSRKFGVYEDDLPVFRWFRAGVPGTRT-SMEAQVMDLADDISYSVHDVEDGvvnavFQLKWLaipeHRERVVEttrqw 249
Cdd:TIGR01353 156 GYLNKKKGIYDSELAVFDRVAELLGLTWYrSPLAQLMEAADDIAYTVHDLEDA-----IKLGLL----TFDDLQH----- 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092788282 250 yLPHTDP--AEVDAALARLEATDvwvsemdgsrrALAAMKDMTSQLIGRFCSAAfdATRQVFGNEPL----TRHGADVVV 323
Cdd:TIGR01353 222 -LLLIQAgfEELGSEMTDLSISA-----------ENEQIRSLRGKLITDLIESV--AKAEFSSHLVAiligTFHHTLVEF 287

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092788282 324 PEETETEIAVMKGIAAAYVMTAEQRQPLYARQREVLAELV-ALLDATGDRYLEPMFAFDWAQAPDDAARRRVVIDQIASL 402
Cdd:TIGR01353 288 SPRLAELLEALKKFLRKRVYRHPDVERIEYQGEQIITGLFdAFMPDLPPRLLPPELRSKLRKAEDNYYKARVVCDYIAGM 367

                         410
                  ....*....|..
gi 1092788282 403 TDSTAVEWHHTL 414
Cdd:TIGR01353 368 TDRYALEEYRRL 379
PRK05318 PRK05318
deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional
 7-414 6.45e-76

deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional


Pssm-ID: 235403 [Multi-domain]  Cd Length: 432  Bit Score: 242.86  E-value: 6.45e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092788282   7 TPWdRERWLPEPPKSS--YRSDFERDRARVLHSAGLRRLGAKTQVVAPDADDFARTRLTHSLEVAQVGR----------- 73
Cdd:PRK05318    4 SVW-QERRLGEDKQRRndHRSPYQRDRARILHSAAFRRLQAKTQVLGVGENDFYRTRLTHSLEVAQIGTgivaqlkkekq 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092788282  74 -ELgRSLGCDPDLVDTACLSHDLGHPPFGHNGEKALDALSEDVGGFEGNAQTLRLLARLEQKKLFadgssAGLNLTRAAL 152
Cdd:PRK05318   83 pEL-KPLLPSDSLIESLCLAHDIGHPPFGHGGEVALNYMMRDHGGFEGNGQTFRILTKLEPYTEH-----FGMNLTRRTL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092788282 153 DAACKYPWTREDA---PLRPDGTRSRKF---------GVYEDDLPVFRW------------FRAGVPGT-------RT-- 199
Cdd:PRK05318  157 LGILKYPALYSELvaqYPPPDVANHRQLkasdwkppkGIFDDDQDIFDWvleplsendralFQSLRPEPdspkehlKTry 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092788282 200 -SMEAQVMDLADDISYSVHDVEDGVVnavfqlkwlaipehrERVVeTTRQWYlphtdpAEVDAALArlEATDVWVSEMDG 278
Cdd:PRK05318  237 kSLDCSIMELADDIAYGVHDLEDAIV---------------LGLV-TRSQWQ------EDVAPQLA--QCGDPWLEEEIE 292

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092788282 279 S------RRALAAMKDMTSQLIGRFCSAAFDATRQVFgNEPLTRHGAdvVVPEETETEIAVMKGIAAAYVMTAEQRQPL- 351
Cdd:PRK05318  293 TigeklfSGEHHLRKDAIGTLVNYFITSIRIKENEEF-EEPLLRYNA--ALEPEFAAALEVLKQFVYKYVIRKPEVQRLe 369

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092788282 352 YARQREVLaELVALLDATGDRYLEPMFAFDWAQAPDDAARRRVVIDQIASLTDSTAVEWHHTL 414
Cdd:PRK05318  370 YKGQQIVM-ELFEALSSDPERLLPRNTQERWRKAEDEENSMRVICDYISGMTDEYAYRLYQQL 431
PRK01286 PRK01286
deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional
 11-248 1.18e-56

deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional


Pssm-ID: 234934 [Multi-domain]  Cd Length: 336  Bit Score: 189.61  E-value: 1.18e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092788282  11 RERWLPEPPkSSYRSDFERDRARVLHSAGLRRLGAKTQV-VAPDADDFaRTRLTHSLEVAQVGRELGRSLGCDPDLVDTA 89
Cdd:PRK01286   14 RGRLRPEEP-CPIRTEFQRDRDRIIHSKAFRRLKHKTQVfINPEGDHY-RTRLTHTLEVAQIARTIARALRLNEDLTEAI 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092788282  90 CLSHDLGHPPFGHNGEKALDALSEDVGGFEGNAQTLRLLARLEQKKlfadgssAGLNLTRAALDAACKYpwtredaplrp 169
Cdd:PRK01286   92 ALGHDLGHTPFGHAGEDALNELMKEYGGFEHNEQSLRVVDKLEKRY-------DGLNLTWEVREGILKH----------- 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092788282 170 dgtrsrkfgvyeddlpvfRWFRAGVPGTRTSMEAQVMDLADDISYSVHDVEDGVVNAVFQLKwlAIPEHRERVV-ETTRQ 248
Cdd:PRK01286  154 ------------------SGPRNAPLGTAATLEGQIVRLADEIAYNNHDIDDGIRAGLITLE--DLPEDVRRLLgETHRR 213
PRK01096 PRK01096
deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional
 16-223 1.45e-56

deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional


Pssm-ID: 234897 [Multi-domain]  Cd Length: 440  Bit Score: 192.44  E-value: 1.45e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092788282  16 PEPPKSSYRSDFERDRARVLHSAGLRRLGAKTQVVAPDADDFARTRLTHSLEVAQVGRELGRSLG-----------CDP- 83
Cdd:PRK01096   17 KTSKDELGRSPFHKDYDRIIFSGSFRRLQRKTQVHPLAKNDHIHTRLTHSLEVSCVGRSLGMRVGetlkeeklpdwISPa 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092788282  84 ---DLVDTACLSHDLGHPPFGHNGEKA-------------LDALS----EDVGGFEGNAQTLRLLARLEQkkLFADGssa 143
Cdd:PRK01096   97 digAIVQSACLAHDIGNPPFGHFGEDAirewfqdaagrgfLDDLSpqerADFLNFEGNAQGFRVLTKLEY--HQDDG--- 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092788282 144 GLNLTRAALDAACKYPWTREDAPlrPDGTRSRKFGVYEDDLPVFR--WFRAGVPGTRTS----------MEAqvmdlADD 211
Cdd:PRK01096  172 GMRLTYATLGTYIKYPWSSRHAN--KQQIKKKKFGCYQSELPLFEqiAEALGLPQLGEQrwcrhpltylLEA-----ADD 244

                         250
                  ....*....|..
gi 1092788282 212 ISYSVHDVEDGV 223
Cdd:PRK01096  245 ICYALIDLEDGL 256
dgt PRK04926
deoxyguanosinetriphosphate triphosphohydrolase; Provisional
 27-278 4.78e-34

deoxyguanosinetriphosphate triphosphohydrolase; Provisional


Pssm-ID: 235320 [Multi-domain]  Cd Length: 503  Bit Score: 132.74  E-value: 4.78e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092788282  27 FERDRARVLHSAGLRRLGAKTQVVAPDADDFARTRLTHSLEVAQVGRELGR-------------SLGCDP------DLVD 87
Cdd:PRK04926   32 FESDRGRIINSAAIRRLQQKTQVFPLERNAAVRSRLTHSLEVQQVGRYIAKeilsrlkeqklleAYGLDEltgpfeSIVE 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092788282  88 TACLSHDLGHPPFGHNGEKA--------LDA--------------------------------LSEDVGGFEGNAQTLRL 127
Cdd:PRK04926  112 MACLMHDIGNPPFGHFGEAAindwfrqrLDPdaesqpltddrcsvaalrlrdgeeplnelrrkIRQDLCHFEGNAQGIRL 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092788282 128 LARLeqkklfadgssAGLNLTRAALDAACKYP----WTREDAPlrPDGTRSRKFGVYEDDLPVFRWFRAGV---PGTRTS 200
Cdd:PRK04926  192 VHTL-----------LRLNLTYAQVACILKYTrpawWRGPTPA--SHHYLMKKPGYYLSEEAYVARLRKELnlaPYSRFP 258

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092788282 201 MeAQVMDLADDISYSVHDVEDGVVNAVFQLkwlaipehrERVVETTRQWYLPHTDP----AEVDAALARLEATDVWVSEM 276
Cdd:PRK04926  259 L-TYIMEAADDISYCIADLEDAVEKRIFSV---------EQLYHHLHEAWGEHEKGdlfsLVVENAWEKSRANSLSRSSE 328


                  ..
gi 1092788282 277 DG 278
Cdd:PRK04926  329 DQ 330
HD_assoc pfam13286
Phosphohydrolase-associated domain; This domain is found on bacterial and archaeal ...
 321-412 6.54e-24

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


Pssm-ID: 433087 [Multi-domain]  Cd Length: 91  Bit Score: 94.90  E-value: 6.54e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092788282 321 VVVPEETETEIAVMKGIAAAYVMTAEQRQPLYARQREVLAELVALLDATGDRyLEPMFAFDWAQAPDDaARRRVVIDQIA 400
Cdd:pfam13286   1 VAFSPEMAAELAELKRFLFEYVYRHPRVQREEEKARRIIRELFEALMADPEL-LPPEFRARWEAAGDD-ARARVVCDYIA 78

                          90
                  ....*....|..
gi 1092788282 401 SLTDSTAVEWHH 412
Cdd:pfam13286  79 GMTDRYALRLHR 90
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
 57-111 1.53e-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: 55.77  E-value: 1.53e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1092788282   57 FARTRLTHSLEVAQVGRELGRSLGC-DPDLVDTACLSHDLGHPPFGHNGEKALDAL 111
Cdd:smart00471   1 SDYHVFEHSLRVAQLAAALAEELGLlDIELLLLAALLHDIGKPGTPDSFLVKTSVL 56
HD pfam01966
HD domain; HD domains are metal dependent phosphohydrolases.
 61-103 5.01e-09

HD domain; HD domains are metal dependent phosphohydrolases.


Pssm-ID: 460398 [Multi-domain]  Cd Length: 110  Bit Score: 53.78  E-value: 5.01e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1092788282  61 RLTHSLEVAQVGRELGRSLG-CDPDLVDTACLSHDLGHPPFGHN 103
Cdd:pfam01966   1 RLEHSLRVALLARELAEELGeLDRELLLLAALLHDIGKGPFGDE 44
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
 59-102 3.78e-06

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 46.56  E-value: 3.78e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1092788282  59 RTRLTHSLEVAQVGRELGRSLG---CDPDLVDTACLSHDLGHPPFGH 102
Cdd:cd00077     1 EHRFEHSLRVAQLARRLAEELGlseEDIELLRLAALLHDIGKPGTPD 47
HDIG TIGR00277
HDIG domain; This domain is found in a few known nucleotidyltransferes and in a large number ...
 62-98 1.25e-05

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


Pssm-ID: 272994 [Multi-domain]  Cd Length: 80  Bit Score: 43.09  E-value: 1.25e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1092788282  62 LTHSLEVAQVGRELGRSLGCDPDLVDTACLSHDLGHP 98
Cdd:TIGR00277   6 LQHSLEVAKLAEALARELGLDVELARRGALLHDIGKP 42
RnaY COG1418
HD superfamily phosphodieaserase, includes HD domain of RNase Y [Translation, ribosomal ...
 61-102 1.46e-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: 1.46e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1092788282  61 RLTHSLEVAQVGRELGRSLGCDPDLVDTACLSHDLGHPPFGH 102
Cdd:COG1418    19 DLQHSLRVAKLAGLIAAEEGADVEVAKRAALLHDIGKAKDHE 60
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 4-425 1.58e-03

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 41.01  E-value: 1.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092788282    4 PGYtPWDRERWLPEPPKSSYRSDFERDRARVLHSAGLRRLGAKTQVVAPDADDFARTRLTHSLEVAQVGRELGRSLGCDP 83
Cdd:COG3321    864 PTY-PFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAAAL 942

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092788282   84 DLVDTACLSHDLGHPPFGHNGEKALDALSEDVGGFEGNAQTLRLLARLEQKKLFADGSSAGLnltRAALDAACKYPWTRE 163
Cdd:COG3321    943 LALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALAL---LAAAALLLAAAAAAA 1019

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092788282  164 DAPLRPDGTRSRkfGVYEDDLPVFRWFRAGVPGTRTSMEAQVMDLADDISYSVHDVEDGVVNAVFQLKWLAIPEHRERVV 243
Cdd:COG3321   1020 ALLALAALLAAA--AAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALAL 1097

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092788282  244 ETTRQWYLPHTDPAEVDAALARLEATDVWVSEMDGSRRALAAMKDMTSQLIGRFCSAAFDATRQVFGNEPLTRHGADVVV 323
Cdd:COG3321   1098 ALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLAL 1177

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092788282  324 PEETETEIAVMKGIAAAYVMTAEQRQPLyARQREVLAELVALLDATGDRYLEPMFAFDWAQAPDDAARRRVVIDQIASLT 403
Cdd:COG3321   1178 ALALAAALAAALAGLAALLLAALLAALL-AALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALL 1256

                          410       420
                   ....*....|....*....|..
gi 1092788282  404 DSTAVEWHHTLVQGAEFRRVWL 425
Cdd:COG3321   1257 AALAALALLAAAAGLAALAAAA 1278
 
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