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Conserved domains on  [gi|41944318|gb|AAH66037.1|]
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Selenophosphate synthetase 1 [Mus musculus]

Protein classification: selenophosphate synthetase catalyzes the conversion of selenium to selenophosphate in the synthesis of Secys-tRNA.

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SelD cd02195
Selenophosphate synthetase (SelD) catalyzes the conversion of selenium to selenophosphate ...
20-357 1.93e-118

Selenophosphate synthetase (SelD) catalyzes the conversion of selenium to selenophosphate which is required by a number of bacterial, archaeal and eukaryotic organisms for synthesis of Secys-tRNA, the precursor of selenocysteine in selenoenzymes. The N-terminal domain of SelD is related to the ATP-binding domains of hydrogen expression/formation protein HypE, the AIR synthases, and FGAM synthase and is thought to bind ATP.


:

Pssm-ID: 100031 [Multi-domain]  Cd Length: 287  Bit Score: 348.36  E-value: 1.93e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318  20 LTRFTELKGTGCKVPQDVLQKLLESLQENHfqedeqfLGAVMPRLGIGMDTCVIPLRhGGLSLVQTTDYIYPIVDDPYMM 99
Cdd:cd02195   1 LTSFMKCAGCGAKVGPGVLSQLLAGLPLPT-------DPNLLVGLGTGDDAAVYRLP-GGLALVQTTDFFPPIVDDPYLF 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318 100 GRIACANVLSDLYAMGVTeCDNMLMLLGVSNKMtDRERDKVIPLIIQGFKDAAEEAGTSVTGGQTVLNPWIVLGGVATTV 179
Cdd:cd02195  73 GRIAAANALSDIYAMGAK-PLSALAIVTLPRKL-PALQEEVLREILAGGKDKLREAGAVLVGGHTIEGPEPKYGLSVTGL 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318 180 CQPNEFIMPDNAVPGDVLVLTKPLGTQVAVAVHQWLDIPEKWnkikllvtqedvelaYQEAMMNMARLNRTAAGLMHTFN 259
Cdd:cd02195 151 VHPNKILRNSGAKPGDVLILTKPLGTGILFAAEMAGLARGED---------------IDAALESMARLNRAAAELLRKYG 215
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318 260 AHAATDITGFGILGHAQNLAKQQRNEVSFVIHNLPVLakmaavskacgnmfglmhgtcpETSGGLLICLPREQAARFCAE 339
Cdd:cd02195 216 AHACTDVTGFGLLGHLLEMARASGVSAEIDLDKLPLL----------------------QTSGGLLAAVPPEDAAALLAL 273
                       330
                ....*....|....*...
gi 41944318 340 IKSpkygEGHQAWIIGIV 357
Cdd:cd02195 274 LKA----GGPPAAIIGEV 287
selD TIGR00476
selenium donor protein; In prokaryotes, the incorporation of selenocysteine as the 21st amino ...
19-333 2.87e-120

selenium donor protein; In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3-prime or 5-prime non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation. This model describes SelD, known as selenophosphate synthetase, selenium donor protein, and selenide,water dikinase. SelD provides reduced selenium for the selenium transferase SelA. This protein itself contains selenocysteine in many species; any sequence scoring well but not aligning to the beginning of the model is likely to have a selenocysteine residue incorrectly interpreted as a stop codon upstream of the given sequence. The SelD protein also provides selenophosphate for the enzyme tRNA 2-selenouridine synthase, which catalyzes a tRNA base modification. It also contributes to selenium incorporation by selenium-dependent molybdenum hydroxylases (SDMH), in genomes with the marker TIGR03309. All genomes with SelD should make selenocysteine, selenouridine, SDMH, or some combination.


:

Pssm-ID: 273100 [Multi-domain]  Cd Length: 301  Bit Score: 353.72  E-value: 2.87e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318    19 RLTRFTELKGTGCKVPQDVLQKLLESLQENHFQEdeqflgaVMPRLGIGMDTCVIPLRhGGLSLVQTTDYIYPIVDDPYM 98
Cdd:TIGR00476   1 RLTEYSHGGGCGCKIGPGVLDKILASLPAAPDPN-------LLVGNDTGDDAAVYKLN-DGLALVSTTDFFTPIVDDPYD 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318    99 MGRIACANVLSDLYAMGVTEcDNMLMLLGVSNKMtdrERDKVIPLIIQGFKDAAEEAGTSVTGGQTVLNPWIVLGGVATT 178
Cdd:TIGR00476  73 FGRIAATNALSDIYAMGGTP-LTALAILGWPRNK---LPPEVLREILAGGADVCAEAGAPLAGGHSIDDPEPKYGLAVTG 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318   179 VCQPNEFIMPDNAVPGDVLVLTKPLGTQVAVAVHQWLDIPEKwnkikllvtqedvelAYQEAMMNMARLNRTAAGLMHTF 258
Cdd:TIGR00476 149 LVHPDKLKRNDGAQPGDVLILTKPLGVGVLTAALKKGGLAEE---------------AYAAAIASMTTLNKQAAELAALA 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318   259 NAHAATDITGFGILGHAQNLAKQQRNEVSFVIHNLPVLAKMAAVSKACGNMFGLMHGTC-------------PETSGGLL 325
Cdd:TIGR00476 214 GVHAMTDVTGFGLLGHLLEMCRGSGVSAEIDFDAVPLLAEQGCVPGGTGRNFASYGEKVpepageqrdllcdPQTSGGLL 293

                  ....*...
gi 41944318   326 ICLPREQA 333
Cdd:TIGR00476 294 IAVAPEAA 301
 
Name Accession Description Interval E-value
SelD cd02195
Selenophosphate synthetase (SelD) catalyzes the conversion of selenium to selenophosphate ...
20-357 1.93e-118

Selenophosphate synthetase (SelD) catalyzes the conversion of selenium to selenophosphate which is required by a number of bacterial, archaeal and eukaryotic organisms for synthesis of Secys-tRNA, the precursor of selenocysteine in selenoenzymes. The N-terminal domain of SelD is related to the ATP-binding domains of hydrogen expression/formation protein HypE, the AIR synthases, and FGAM synthase and is thought to bind ATP.


Pssm-ID: 100031 [Multi-domain]  Cd Length: 287  Bit Score: 348.36  E-value: 1.93e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318  20 LTRFTELKGTGCKVPQDVLQKLLESLQENHfqedeqfLGAVMPRLGIGMDTCVIPLRhGGLSLVQTTDYIYPIVDDPYMM 99
Cdd:cd02195   1 LTSFMKCAGCGAKVGPGVLSQLLAGLPLPT-------DPNLLVGLGTGDDAAVYRLP-GGLALVQTTDFFPPIVDDPYLF 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318 100 GRIACANVLSDLYAMGVTeCDNMLMLLGVSNKMtDRERDKVIPLIIQGFKDAAEEAGTSVTGGQTVLNPWIVLGGVATTV 179
Cdd:cd02195  73 GRIAAANALSDIYAMGAK-PLSALAIVTLPRKL-PALQEEVLREILAGGKDKLREAGAVLVGGHTIEGPEPKYGLSVTGL 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318 180 CQPNEFIMPDNAVPGDVLVLTKPLGTQVAVAVHQWLDIPEKWnkikllvtqedvelaYQEAMMNMARLNRTAAGLMHTFN 259
Cdd:cd02195 151 VHPNKILRNSGAKPGDVLILTKPLGTGILFAAEMAGLARGED---------------IDAALESMARLNRAAAELLRKYG 215
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318 260 AHAATDITGFGILGHAQNLAKQQRNEVSFVIHNLPVLakmaavskacgnmfglmhgtcpETSGGLLICLPREQAARFCAE 339
Cdd:cd02195 216 AHACTDVTGFGLLGHLLEMARASGVSAEIDLDKLPLL----------------------QTSGGLLAAVPPEDAAALLAL 273
                       330
                ....*....|....*...
gi 41944318 340 IKSpkygEGHQAWIIGIV 357
Cdd:cd02195 274 LKA----GGPPAAIIGEV 287
AIRS_C pfam02769
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression ...
193-368 6.81e-17

AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression/formation protein HypE, AIR synthases EC:6.3.3.1, FGAM synthase EC:6.3.5.3 and selenide, water dikinase EC:2.7.9.3. The function of the C-terminal domain of AIR synthase is unclear, but the cleft formed between N and C domains is postulated as a sulphate binding site.


Pssm-ID: 251518  Cd Length: 150  Bit Score: 76.62  E-value: 6.81e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318   193 PGDVLVLTKPLGTQVAVAvhqwldipekWNKIKLLVTQEDVELAYQEAMMNMARLNRTAAGLmhtFNAHAATDITGFGIL 272
Cdd:pfam02769   2 PGDVLILLGSSGLHGSGL----------SLVRKGLEEDGAVPLGDPLLEPTLIYVVLLLAAL---GLVKAAHDITGGGLA 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318   273 GHAQNLAKQQRNEVSFVIHNLPVlakmaavskACGNMFGL-MHGTcpETSGGLLICLPREQAARFCAEIKSpkygEGHQA 351
Cdd:pfam02769  69 GALAEMAPASGVGAEIDLDKVPI---------FEELVLPLeMLFS--ENQGRGLVVVVPEEAEAVLAILEE----EGLPA 133
                         170
                  ....*....|....*..
gi 41944318   352 WIIGIVEKGNRTARIID 368
Cdd:pfam02769 134 AVIGEVTAGGGLTLVVK 150
selD TIGR00476
selenium donor protein; In prokaryotes, the incorporation of selenocysteine as the 21st amino ...
19-333 2.87e-120

selenium donor protein; In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3-prime or 5-prime non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation. This model describes SelD, known as selenophosphate synthetase, selenium donor protein, and selenide,water dikinase. SelD provides reduced selenium for the selenium transferase SelA. This protein itself contains selenocysteine in many species; any sequence scoring well but not aligning to the beginning of the model is likely to have a selenocysteine residue incorrectly interpreted as a stop codon upstream of the given sequence. The SelD protein also provides selenophosphate for the enzyme tRNA 2-selenouridine synthase, which catalyzes a tRNA base modification. It also contributes to selenium incorporation by selenium-dependent molybdenum hydroxylases (SDMH), in genomes with the marker TIGR03309. All genomes with SelD should make selenocysteine, selenouridine, SDMH, or some combination.


Pssm-ID: 273100 [Multi-domain]  Cd Length: 301  Bit Score: 353.72  E-value: 2.87e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318    19 RLTRFTELKGTGCKVPQDVLQKLLESLQENHFQEdeqflgaVMPRLGIGMDTCVIPLRhGGLSLVQTTDYIYPIVDDPYM 98
Cdd:TIGR00476   1 RLTEYSHGGGCGCKIGPGVLDKILASLPAAPDPN-------LLVGNDTGDDAAVYKLN-DGLALVSTTDFFTPIVDDPYD 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318    99 MGRIACANVLSDLYAMGVTEcDNMLMLLGVSNKMtdrERDKVIPLIIQGFKDAAEEAGTSVTGGQTVLNPWIVLGGVATT 178
Cdd:TIGR00476  73 FGRIAATNALSDIYAMGGTP-LTALAILGWPRNK---LPPEVLREILAGGADVCAEAGAPLAGGHSIDDPEPKYGLAVTG 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318   179 VCQPNEFIMPDNAVPGDVLVLTKPLGTQVAVAVHQWLDIPEKwnkikllvtqedvelAYQEAMMNMARLNRTAAGLMHTF 258
Cdd:TIGR00476 149 LVHPDKLKRNDGAQPGDVLILTKPLGVGVLTAALKKGGLAEE---------------AYAAAIASMTTLNKQAAELAALA 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318   259 NAHAATDITGFGILGHAQNLAKQQRNEVSFVIHNLPVLAKMAAVSKACGNMFGLMHGTC-------------PETSGGLL 325
Cdd:TIGR00476 214 GVHAMTDVTGFGLLGHLLEMCRGSGVSAEIDFDAVPLLAEQGCVPGGTGRNFASYGEKVpepageqrdllcdPQTSGGLL 293

                  ....*...
gi 41944318   326 ICLPREQA 333
Cdd:TIGR00476 294 IAVAPEAA 301
PRK14105 PRK14105
selenophosphate synthetase; Provisional
13-375 2.14e-68

selenophosphate synthetase; Provisional


Pssm-ID: 237611 [Multi-domain]  Cd Length: 345  Bit Score: 221.57  E-value: 2.14e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318   13 ELDKSFRLTRFTELKGTGCKVPQDVLQKLLESLqenhfqEDEQFLGAVMprLGIGMDTCVIplRHGGLSLVQTTDYIYPI 92
Cdd:PRK14105   1 KMEEKIKLTEMVKLHGUACKLPSTELENLVKGI------ILEEDLKHTK--VGLGDDAAVI--IKNGLAIVKTVDVFTPI 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318   93 VDDPYMMGRIACANVLSDLYAMGVTECDNMLMLLGVSNKMTDrerdKVIPLIIQGFKDAAEEAGTSVTGGQTVLNPWIVL 172
Cdd:PRK14105  71 VDDPYIQGKIAACNSTSDVYAMGLSEIIGVLVILGIPPELPI----EVAKEMLQGFQDFCRENDTTIIGGHTILNPWPLI 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318  173 GGVATTVCQPNEFIMPDNAVPGDVLVLTKPLGTQVAVAVhqwLDIPEKWNKIkLLVTQEDVELAYQEAMMNMARLNRTAA 252
Cdd:PRK14105 147 GGAVTGVGKEEDILTKAGAKEGDVLILTKPLGTQSAMAL---SRVPEEFEDL-IDITKEEKEYIINKAIELMTTSNRYAL 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318  253 GLMHTFN-------AHAATDITGFGILGHAQNLAKQQRneVSFVIHNLPVLAKMAAVSKACGnmFGLMHGTCPETSGGLL 325
Cdd:PRK14105 223 LALREAEeevgekiANAMTDVTGFGILGHSQEMAEQSN--VEIEISTLPVIKGTPELSSLFG--HALLDGYGAETAGGLL 298
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 41944318  326 ICLPREQAARFCAEIKSpkygEGHQAWIIG-IVEKGNRTARIIDKPRIIEV 375
Cdd:PRK14105 299 ISVKPEYKDKLIDKLEK----NNVYAFEVGkVVKNGVGKAKLSENVKILEI 345
SelD COG0709
Selenophosphate synthase [Amino acid transport and metabolism];
19-367 4.14e-46

Selenophosphate synthase [Amino acid transport and metabolism];


Pssm-ID: 223781 [Multi-domain]  Cd Length: 346  Bit Score: 162.92  E-value: 4.14e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318  19 RLTRFTELKGTGCKVPQDVLQKLLESLQENHFqeDEQFLGAVmprlGIGMDTCVipLRHG-GLSLVQTTDYIYPIVDDPY 97
Cdd:COG0709   7 RLTQYSHGAGCGCKISPKVLEQILHGTPAKPD--FAKLLVGN----ETGDDAAV--YDLGnGHSIISTTDFFMPIVDDPF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318  98 MMGRIACANVLSDLYAMGvtecDNMLMLLGVSNKMTDRERDKVIPLIIQGFKDAAEEAGTSVTGGQTVLNPWIVLGGVAT 177
Cdd:COG0709  79 DFGRIAATNAISDVFAMG----GKPIMAIAILGFPNDLLDKEIAQEVIEGGRDACREAGIALAGGHSIDAPEPIFGLAVT 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318 178 TVCQPNEFIMPDNAVPGDVLVLTKPLGTQVAVAVhqwldipEKWNKIKllvtqedvELAYQEAMMNMARLNRTAAGLMHT 257
Cdd:COG0709 155 GIVPTGKVKRNSTAKAGCKLILTKPLGIGILTTA-------EKKGLLK--------EEHKGLALENMCTLNKIGAQFAPD 219
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318 258 FNAHAATDITGFGILGHAQNLAkqQRNEVSFVIHNLPV--------LAKMAAVSKACGNMFG----LMHGTCPE------ 319
Cdd:COG0709 220 FGVAAMTDVTGFGLLGHLKEMA--EGAGVDARLFDSPIpfldgvefYIENGIIPGGTARNFGsygiFAGKDLPEeqklll 297
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|...
gi 41944318 320 ----TSGGLLICLPREQAARfCAEIKSPkygEGHQAWIIG-IVEKGNRTARII 367
Cdd:COG0709 298 cdpqTSGGLLIAVVPEGKGE-GLEIAPE---LGIQLIIIGeLVAKQRALIEVL 346
 
Name Accession Description Interval E-value
SelD cd02195
Selenophosphate synthetase (SelD) catalyzes the conversion of selenium to selenophosphate ...
20-357 1.93e-118

Selenophosphate synthetase (SelD) catalyzes the conversion of selenium to selenophosphate which is required by a number of bacterial, archaeal and eukaryotic organisms for synthesis of Secys-tRNA, the precursor of selenocysteine in selenoenzymes. The N-terminal domain of SelD is related to the ATP-binding domains of hydrogen expression/formation protein HypE, the AIR synthases, and FGAM synthase and is thought to bind ATP.


Pssm-ID: 100031 [Multi-domain]  Cd Length: 287  Bit Score: 348.36  E-value: 1.93e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318  20 LTRFTELKGTGCKVPQDVLQKLLESLQENHfqedeqfLGAVMPRLGIGMDTCVIPLRhGGLSLVQTTDYIYPIVDDPYMM 99
Cdd:cd02195   1 LTSFMKCAGCGAKVGPGVLSQLLAGLPLPT-------DPNLLVGLGTGDDAAVYRLP-GGLALVQTTDFFPPIVDDPYLF 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318 100 GRIACANVLSDLYAMGVTeCDNMLMLLGVSNKMtDRERDKVIPLIIQGFKDAAEEAGTSVTGGQTVLNPWIVLGGVATTV 179
Cdd:cd02195  73 GRIAAANALSDIYAMGAK-PLSALAIVTLPRKL-PALQEEVLREILAGGKDKLREAGAVLVGGHTIEGPEPKYGLSVTGL 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318 180 CQPNEFIMPDNAVPGDVLVLTKPLGTQVAVAVHQWLDIPEKWnkikllvtqedvelaYQEAMMNMARLNRTAAGLMHTFN 259
Cdd:cd02195 151 VHPNKILRNSGAKPGDVLILTKPLGTGILFAAEMAGLARGED---------------IDAALESMARLNRAAAELLRKYG 215
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318 260 AHAATDITGFGILGHAQNLAKQQRNEVSFVIHNLPVLakmaavskacgnmfglmhgtcpETSGGLLICLPREQAARFCAE 339
Cdd:cd02195 216 AHACTDVTGFGLLGHLLEMARASGVSAEIDLDKLPLL----------------------QTSGGLLAAVPPEDAAALLAL 273
                       330
                ....*....|....*...
gi 41944318 340 IKSpkygEGHQAWIIGIV 357
Cdd:cd02195 274 LKA----GGPPAAIIGEV 287
AIRS_C pfam02769
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression ...
193-368 6.81e-17

AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression/formation protein HypE, AIR synthases EC:6.3.3.1, FGAM synthase EC:6.3.5.3 and selenide, water dikinase EC:2.7.9.3. The function of the C-terminal domain of AIR synthase is unclear, but the cleft formed between N and C domains is postulated as a sulphate binding site.


Pssm-ID: 251518  Cd Length: 150  Bit Score: 76.62  E-value: 6.81e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318   193 PGDVLVLTKPLGTQVAVAvhqwldipekWNKIKLLVTQEDVELAYQEAMMNMARLNRTAAGLmhtFNAHAATDITGFGIL 272
Cdd:pfam02769   2 PGDVLILLGSSGLHGSGL----------SLVRKGLEEDGAVPLGDPLLEPTLIYVVLLLAAL---GLVKAAHDITGGGLA 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318   273 GHAQNLAKQQRNEVSFVIHNLPVlakmaavskACGNMFGL-MHGTcpETSGGLLICLPREQAARFCAEIKSpkygEGHQA 351
Cdd:pfam02769  69 GALAEMAPASGVGAEIDLDKVPI---------FEELVLPLeMLFS--ENQGRGLVVVVPEEAEAVLAILEE----EGLPA 133
                         170
                  ....*....|....*..
gi 41944318   352 WIIGIVEKGNRTARIID 368
Cdd:pfam02769 134 AVIGEVTAGGGLTLVVK 150
PurM-like1 cd06061
AIR synthase (PurM) related protein, subgroup 1 of unknown function. The family of PurM ...
32-355 8.48e-17

AIR synthase (PurM) related protein, subgroup 1 of unknown function. The family of PurM related proteins includes Hydrogen expression/formation protein HypE, AIR synthases, FGAM synthase and Selenophosphate synthetase (SelD). They all contain two conserved domains and seem to dimerize. The N-terminal domain forms the dimer interface and is a putative ATP binding domain.


Pssm-ID: 100037 [Multi-domain]  Cd Length: 298  Bit Score: 78.79  E-value: 8.48e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318  32 KVPQDVLQKLLesLQENHFQEDEqflgaVMPRLGIGMDTCVIplRHGGLSLVQTTDyiyPIVDDPYMMGRIACANVLSDL 111
Cdd:cd06061   4 KLPPEFLKRLI--LKNLGADRDE-----VLVGPGGGEDAAVV--DFGGKVLVVSTD---PITGAGKDAGWLAVHIAANDI 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318 112 YAMGVtECDNMLMLLGVSNKMTDRERDKviplIIQGFKDAAEEAGTSVTGGQT----VLNPWIVlGGVATTVCQPNEFIM 187
Cdd:cd06061  72 ATSGA-RPRWLLVTLLLPPGTDEEELKA----IMREINEAAKELGVSIVGGHTevtpGVTRPII-SVTAIGKGEKDKLVT 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318 188 PDNAVPGDVLVLTKPLGTQVAvavhqWLDIPEKWNKIKLLVTQEDVELAYQ-EAMMNMARlnrtAAGLMHTFNAHAATDI 266
Cdd:cd06061 146 PSGAKPGDDIVMTKGAGIEGT-----AILANDFEEELKKRLSEEELREAAKlFYKISVVK----EALIAAEAGVTAMHDA 216
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318 267 TGFGILGHAQNLAKQQRNEVSFVIHNLPVLAKMAAVSKAcgnmFGLMhgtcP---ETSGGLLICLPREQAARFCAEIKSp 343
Cdd:cd06061 217 TEGGILGALWEVAEASGVGLRIEKDKIPIRQETKEICEA----LGID----PlrlISSGTLLITVPPEKGDELVDALEE- 287
                       330
                ....*....|..
gi 41944318 344 kygEGHQAWIIG 355
Cdd:cd06061 288 ---AGIPASVIG 296
ThiL cd02194
ThiL (Thiamine-monophosphate kinase) plays a dual role in de novo biosynthesis and in salvage ...
63-358 1.15e-14

ThiL (Thiamine-monophosphate kinase) plays a dual role in de novo biosynthesis and in salvage of exogenous thiamine. Thiamine salvage occurs in two steps, with thiamine kinase catalyzing the formation of thiamine phosphate, and ThiL catalyzing the conversion of this intermediate to thiamine pyrophosphate. The N-terminal domain of ThiL binds ATP and is related to the ATP-binding domains of hydrogen expression/formation protein HypE, the AIR synthases, FGAM synthase and selenophosphate synthetase (SelD).


Pssm-ID: 100030 [Multi-domain]  Cd Length: 291  Bit Score: 72.59  E-value: 1.15e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318  63 RLGIGMDTCVIplRHGGLSLVQTTDYI-----YPIVDDPYMMG-RIACANvLSDLYAMGVTECDnMLMLLGVSNKMTDRE 136
Cdd:cd02194  20 LLGIGDDAAVL--KPPGGRLVVTTDTLvegvhFPPDTTPEDIGwKALAVN-LSDLAAMGARPLG-FLLSLGLPPDTDEEW 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318 137 RDKviplIIQGFKDAAEEAGTSVTGGQTVLNPWIVLGGVATTVCQPNEFIMPDNAVPGDVLVLTKPLGtQVAVAVHQWLD 216
Cdd:cd02194  96 LEE----FYRGLAEAADRYGVPLVGGDTTSGSELVISVTALGEVEKGKPLRRSGAKPGDLLYVTGTLG-DAAAGLALLLG 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318 217 ipekwnkiKLLVTQEDVELAYQEAMMNMARLNrtAAGLMHTFNAHAATDITGfGILGHAQNLAKqqRNEVSFVIHN--LP 294
Cdd:cd02194 171 --------GLKLPEELYEELIERHLRPEPRLE--LGRALAEGLATAMIDISD-GLLADLGHIAE--ASGVGAVIDLdkLP 237
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41944318 295 VLAKM-AAVSKACGNMFGLmhgtcpetSGG----LLICLPREQAARFCAEIKSPkygeghqAWIIGIVE 358
Cdd:cd02194 238 LSPALrAAELGEDALELAL--------SGGedyeLLFTVPPENAEAAAAKLGVP-------VTVIGRVT 291
AIRS pfam00586
AIR synthase related protein, N-terminal domain; This family includes Hydrogen expression ...
67-164 2.37e-13

AIR synthase related protein, N-terminal domain; This family includes Hydrogen expression/formation protein HypE, AIR synthases EC:6.3.3.1, FGAM synthase EC:6.3.5.3 and selenide, water dikinase EC:2.7.9.3. The N-terminal domain of AIR synthase forms the dimer interface of the protein, and is suggested as a putative ATP binding domain.


Pssm-ID: 249981  Cd Length: 94  Bit Score: 65.21  E-value: 2.37e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318    67 GMDTCVIPLRHGGLsLVQTTDYIYPIVD---DPYMMGRIACANVLSDLYAMGVTECdNMLMLLGVSNkmtdrERDKVIPL 143
Cdd:pfam00586   1 GDDAAVIRLGEGPA-LVVTTDGVVTHVHfaaDPYTGGATAVAGNLSDLAAMGAKPL-ALLDGLALGE-----LDPEWLEE 73
                          90       100
                  ....*....|....*....|.
gi 41944318   144 IIQGFKDAAEEAGTSVTGGQT 164
Cdd:pfam00586  74 IVAGIAEACNEAGVPLVGGDT 94
PurM-like cd00396
AIR (aminoimidazole ribonucleotide) synthase related protein. This family includes Hydrogen ...
81-356 4.21e-12

AIR (aminoimidazole ribonucleotide) synthase related protein. This family includes Hydrogen expression/formation protein HypE, AIR synthases, FGAM (formylglycinamidine ribonucleotide) synthase and Selenophosphate synthetase (SelD). The N-terminal domain of AIR synthase forms the dimer interface of the protein, and is suggested as a putative ATP binding domain.


Pssm-ID: 100027 [Multi-domain]  Cd Length: 222  Bit Score: 63.95  E-value: 4.21e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318  81 SLVQTTDYIYPIVD-DPYMMGRIACANVLSDLYAMGVtECDNMLMLLGVSNkmtDRERDKVIPLIIQGfKDAAEEAGTSV 159
Cdd:cd00396   1 SLAMSTDGINPPLAiNPWAGGRLAVGGAVNDIAAMGA-RPIALLASLSLSN---GLEVDILEDVVDGV-AEACNQLGVPI 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318 160 TGGQT-----VLNPWIVLGGVATTVCQPNEFIMPDNAVPGDVLVLTKplgtqvavavhqwldipekwnkikllvtqedve 234
Cdd:cd00396  76 VGGHTsvspgTMGHKLSLAVFAIGVVEKDRVIDSSGARPGDVLILTG--------------------------------- 122
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318 235 layqeammnmarlNRTAAGLMHTFNAHAATDITGFGILGHAQNLAKQQRNEVSFVIHNLPVlakMAAVSKACGNmFGLMH 314
Cdd:cd00396 123 -------------VDAVLELVAAGDVHAMHDITDGGLLGTLPELAQASGVGAEIDLEAIPL---DEVVRWLCVE-HIEEA 185
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 41944318 315 gTCPETSGGLLICLPREQAARFCAEIkspkYGEGHQAWIIGI 356
Cdd:cd00396 186 -LLFNSSGGLLIAVPAEEADAVLLLL----NGNGIDAAVIGR 222
HypE cd02197
HypE (Hydrogenase expression/formation protein). HypE is involved in Ni-Fe hydrogenase ...
144-357 2.84e-04

HypE (Hydrogenase expression/formation protein). HypE is involved in Ni-Fe hydrogenase biosynthesis. HypE dehydrates its own carbamoyl moiety in an ATP-dependent process to yield the enzyme thiocyanate. The N-terminal domain of HypE is related to the ATP-binding domains of the AIR synthases, selenophosphate synthetase (SelD), and FGAM synthase and is thought to bind ATP.


Pssm-ID: 100033 [Multi-domain]  Cd Length: 293  Bit Score: 40.90  E-value: 2.84e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318 144 IIQGFKDAAEEAGTSVTGGQT-VlnpwiVLGGVA------TT---VCQPNEFIMPDNAVPGDVLVLTKPLGTQVAVavhq 213
Cdd:cd02197  98 IVKSMAEAAREAGVKIVTGDTkV-----VPKGKAdgifinTTgigVIPRGVIISPSNIRPGDKIIVSGTIGDHGAA---- 168
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318 214 wldipekwnkikLLVTQEDVELAyQEAMMNMARLNRTAAGLMHTFNA-HAATDITGFGILGHAQNLAKQQRneVSFVIH- 291
Cdd:cd02197 169 ------------ILAAREGLGFE-TDIESDCAPLNGLVEALLEAGPGiHAMRDPTRGGLAAVLNEIARASG--VGIEIEe 233
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41944318 292 -NLPVLAkmaAVSKACgNMFGL--MHGTCpEtsGGLLICLPREQAARFCAEIKSPKYGEghQAWIIGIV 357
Cdd:cd02197 234 eAIPVRE---EVRGAC-EMLGLdpLYLAN-E--GKFVAIVPPEDAEEVLEALRSHPLGK--EAAIIGEV 293
PurM-like3 cd02192
AIR synthase (PurM) related protein, subgroup 3 of unknown function. The family of PurM ...
48-200 4.21e-04

AIR synthase (PurM) related protein, subgroup 3 of unknown function. The family of PurM related proteins includes Hydrogen expression/formation protein HypE, AIR synthases, FGAM synthase and Selenophosphate synthetase (SelD). They all contain two conserved domains and seem to dimerize. The N-terminal domain forms the dimer interface and is a putative ATP binding domain.


Pssm-ID: 100028 [Multi-domain]  Cd Length: 283  Bit Score: 40.27  E-value: 4.21e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318  48 NHFQEDEQFLGAVMPRLGigMDTCVIPlrHGGLSLVQTTDYIYP-IVD-DPYMMGriACA---NVlSDLYAMGVTEcdnm 122
Cdd:cd02192  18 AILPDAPFDSLGVAADLG--DDAAAIP--DGDGYLLLAADGIWPsLVEaDPWWAG--YCSvlvNV-SDIAAMGGRP---- 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318 123 lmlLGVSNKMTDRERDKVIPlIIQGFKDAAEEAGTSVTGGQTVLN-PWIVLG----GVATTVCqpnefIMPDNAVPGDVL 197
Cdd:cd02192  87 ---LAMVDALWSPSAEAAAQ-VLEGMRDAAEKFGVPIVGGHTHPDsPYNALSvailGRARKDL-----LISFGAKPGDRL 157

                ...
gi 41944318 198 VLT 200
Cdd:cd02192 158 ILA 160
selD TIGR00476
selenium donor protein; In prokaryotes, the incorporation of selenocysteine as the 21st amino ...
19-333 2.87e-120

selenium donor protein; In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3-prime or 5-prime non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation. This model describes SelD, known as selenophosphate synthetase, selenium donor protein, and selenide,water dikinase. SelD provides reduced selenium for the selenium transferase SelA. This protein itself contains selenocysteine in many species; any sequence scoring well but not aligning to the beginning of the model is likely to have a selenocysteine residue incorrectly interpreted as a stop codon upstream of the given sequence. The SelD protein also provides selenophosphate for the enzyme tRNA 2-selenouridine synthase, which catalyzes a tRNA base modification. It also contributes to selenium incorporation by selenium-dependent molybdenum hydroxylases (SDMH), in genomes with the marker TIGR03309. All genomes with SelD should make selenocysteine, selenouridine, SDMH, or some combination.


Pssm-ID: 273100 [Multi-domain]  Cd Length: 301  Bit Score: 353.72  E-value: 2.87e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318    19 RLTRFTELKGTGCKVPQDVLQKLLESLQENHFQEdeqflgaVMPRLGIGMDTCVIPLRhGGLSLVQTTDYIYPIVDDPYM 98
Cdd:TIGR00476   1 RLTEYSHGGGCGCKIGPGVLDKILASLPAAPDPN-------LLVGNDTGDDAAVYKLN-DGLALVSTTDFFTPIVDDPYD 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318    99 MGRIACANVLSDLYAMGVTEcDNMLMLLGVSNKMtdrERDKVIPLIIQGFKDAAEEAGTSVTGGQTVLNPWIVLGGVATT 178
Cdd:TIGR00476  73 FGRIAATNALSDIYAMGGTP-LTALAILGWPRNK---LPPEVLREILAGGADVCAEAGAPLAGGHSIDDPEPKYGLAVTG 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318   179 VCQPNEFIMPDNAVPGDVLVLTKPLGTQVAVAVHQWLDIPEKwnkikllvtqedvelAYQEAMMNMARLNRTAAGLMHTF 258
Cdd:TIGR00476 149 LVHPDKLKRNDGAQPGDVLILTKPLGVGVLTAALKKGGLAEE---------------AYAAAIASMTTLNKQAAELAALA 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318   259 NAHAATDITGFGILGHAQNLAKQQRNEVSFVIHNLPVLAKMAAVSKACGNMFGLMHGTC-------------PETSGGLL 325
Cdd:TIGR00476 214 GVHAMTDVTGFGLLGHLLEMCRGSGVSAEIDFDAVPLLAEQGCVPGGTGRNFASYGEKVpepageqrdllcdPQTSGGLL 293

                  ....*...
gi 41944318   326 ICLPREQA 333
Cdd:TIGR00476 294 IAVAPEAA 301
PRK14105 PRK14105
selenophosphate synthetase; Provisional
13-375 2.14e-68

selenophosphate synthetase; Provisional


Pssm-ID: 237611 [Multi-domain]  Cd Length: 345  Bit Score: 221.57  E-value: 2.14e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318   13 ELDKSFRLTRFTELKGTGCKVPQDVLQKLLESLqenhfqEDEQFLGAVMprLGIGMDTCVIplRHGGLSLVQTTDYIYPI 92
Cdd:PRK14105   1 KMEEKIKLTEMVKLHGUACKLPSTELENLVKGI------ILEEDLKHTK--VGLGDDAAVI--IKNGLAIVKTVDVFTPI 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318   93 VDDPYMMGRIACANVLSDLYAMGVTECDNMLMLLGVSNKMTDrerdKVIPLIIQGFKDAAEEAGTSVTGGQTVLNPWIVL 172
Cdd:PRK14105  71 VDDPYIQGKIAACNSTSDVYAMGLSEIIGVLVILGIPPELPI----EVAKEMLQGFQDFCRENDTTIIGGHTILNPWPLI 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318  173 GGVATTVCQPNEFIMPDNAVPGDVLVLTKPLGTQVAVAVhqwLDIPEKWNKIkLLVTQEDVELAYQEAMMNMARLNRTAA 252
Cdd:PRK14105 147 GGAVTGVGKEEDILTKAGAKEGDVLILTKPLGTQSAMAL---SRVPEEFEDL-IDITKEEKEYIINKAIELMTTSNRYAL 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318  253 GLMHTFN-------AHAATDITGFGILGHAQNLAKQQRneVSFVIHNLPVLAKMAAVSKACGnmFGLMHGTCPETSGGLL 325
Cdd:PRK14105 223 LALREAEeevgekiANAMTDVTGFGILGHSQEMAEQSN--VEIEISTLPVIKGTPELSSLFG--HALLDGYGAETAGGLL 298
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 41944318  326 ICLPREQAARFCAEIKSpkygEGHQAWIIG-IVEKGNRTARIIDKPRIIEV 375
Cdd:PRK14105 299 ISVKPEYKDKLIDKLEK----NNVYAFEVGkVVKNGVGKAKLSENVKILEI 345
SelD COG0709
Selenophosphate synthase [Amino acid transport and metabolism];
19-367 4.14e-46

Selenophosphate synthase [Amino acid transport and metabolism];


Pssm-ID: 223781 [Multi-domain]  Cd Length: 346  Bit Score: 162.92  E-value: 4.14e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318  19 RLTRFTELKGTGCKVPQDVLQKLLESLQENHFqeDEQFLGAVmprlGIGMDTCVipLRHG-GLSLVQTTDYIYPIVDDPY 97
Cdd:COG0709   7 RLTQYSHGAGCGCKISPKVLEQILHGTPAKPD--FAKLLVGN----ETGDDAAV--YDLGnGHSIISTTDFFMPIVDDPF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318  98 MMGRIACANVLSDLYAMGvtecDNMLMLLGVSNKMTDRERDKVIPLIIQGFKDAAEEAGTSVTGGQTVLNPWIVLGGVAT 177
Cdd:COG0709  79 DFGRIAATNAISDVFAMG----GKPIMAIAILGFPNDLLDKEIAQEVIEGGRDACREAGIALAGGHSIDAPEPIFGLAVT 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318 178 TVCQPNEFIMPDNAVPGDVLVLTKPLGTQVAVAVhqwldipEKWNKIKllvtqedvELAYQEAMMNMARLNRTAAGLMHT 257
Cdd:COG0709 155 GIVPTGKVKRNSTAKAGCKLILTKPLGIGILTTA-------EKKGLLK--------EEHKGLALENMCTLNKIGAQFAPD 219
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318 258 FNAHAATDITGFGILGHAQNLAkqQRNEVSFVIHNLPV--------LAKMAAVSKACGNMFG----LMHGTCPE------ 319
Cdd:COG0709 220 FGVAAMTDVTGFGLLGHLKEMA--EGAGVDARLFDSPIpfldgvefYIENGIIPGGTARNFGsygiFAGKDLPEeqklll 297
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|...
gi 41944318 320 ----TSGGLLICLPREQAARfCAEIKSPkygEGHQAWIIG-IVEKGNRTARII 367
Cdd:COG0709 298 cdpqTSGGLLIAVVPEGKGE-GLEIAPE---LGIQLIIIGeLVAKQRALIEVL 346
PRK00943 PRK00943
selenophosphate synthetase; Provisional
19-366 8.65e-36

selenophosphate synthetase; Provisional


Pssm-ID: 234870 [Multi-domain]  Cd Length: 347  Bit Score: 134.59  E-value: 8.65e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318   19 RLTRFTELKGTGCKVPQDVLQKLLESLQEnhfqedeqflGAVMPRLGIGMDT----CVIPLrHGGLSLVQTTDYIYPIVD 94
Cdd:PRK00943   7 RLTQYSHGAGCGCKISPKVLETILASEQA----------KFVDPNLLVGNETrddaAVYDL-NDGTGIISTTDFFMPIVD 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318   95 DPYMMGRIACANVLSDLYAMGVTEcdnmLM---LLGVSNKMTDRErdkVIPLIIQGFKDAAEEAGTSVTGGQTVLNPWIV 171
Cdd:PRK00943  76 DPFDFGRIAATNAISDIYAMGGKP----IMaiaILGWPINKLPPE---VAREVLEGGRAACRQAGIPLAGGHSIDAPEPI 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318  172 LGGVATTVCQPNEFIMPDNAVPGDVLVLTKPLGTQVavavhqwLDIPEKWNKIKllvtQEDvelaYQEAMMNMARLNRTA 251
Cdd:PRK00943 149 FGLAVTGVVPPERVKRNATAQAGDKLFLTKPLGIGI-------LTTAEKKSKLK----PEH----YGLAIEAMCQLNRPG 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318  252 AGLMHTFNAHAATDITGFGILGHAQNLAkqQRNEVSFVIH--NLPVLAKMAA-VSKAC------------GNMFGLMHGT 316
Cdd:PRK00943 214 ADFAKLPGVHAMTDVTGFGLLGHLLEMC--QGAGLTARVDyaAVPLLPGVEEyIAQGCvpggtgrnfasyGHLIGELPDE 291
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 41944318  317 C------PETSGGLLICLPREQAARFCAEIKSpkygEGHQAWIIG-IVEKGNRTARI 366
Cdd:PRK00943 292 QrallcdPQTSGGLLVAVAPEAEAEVLAIAAE----HGIELAAIGeLVEARGGRARV 344
thiL TIGR01379
thiamine-phosphate kinase; This model describes thiamine-monophosphate kinase, an enzyme that ...
64-267 2.26e-14

thiamine-phosphate kinase; This model describes thiamine-monophosphate kinase, an enzyme that converts thiamine monophosphate into thiamine pyrophosphate (TPP, coenzyme B1), an enzyme cofactor. Thiamine monophosphate may be derived from de novo synthesis or from unphosphorylated thiamine, known as vitamin B1. Proteins scoring between the trusted and noise cutoff for this model include short forms from the Thermoplasmas (which lack the N-terminal region) and a highly derived form from Campylobacter jejuni. Eukaryotes lack this enzyme, and add pyrophosphate from ATP to unphosphorylated thiamine in a single step. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]


Pssm-ID: 273589 [Multi-domain]  Cd Length: 317  Bit Score: 71.98  E-value: 2.26e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318    64 LGIGMDTCVIPLRHGGLsLVQTTDYI-----YPIVDDPYMMGRIACANVLSDLYAMGVTEcDNMLMLLGVSNKMTDRERD 138
Cdd:TIGR01379  21 LGIGDDAALVSAPEGRD-LVLTTDTLvegvhFPPDTTPEDLGWKAVAVNLSDLAAMGATP-KWFLLSLGLPSDLDEAWLE 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318   139 KviplIIQGFKDAAEEAGTSVTGGQTVLNPWIVLGGVATTVCQPNEFIMPDNAVPGDVLVLTKPLGtQVAVAVHQWLDIP 218
Cdd:TIGR01379  99 A----FYDGLFEAAKQYGVPLVGGDTVSSPELVVTVTAIGEAPKGRALLRSGAKPGDLVFVTGTLG-DSAAGLALLLKGK 173
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 41944318   219 EKWNkikllvtqEDVELAYQEAMMN-MARLnrtAAGLMHTFNAHAATDIT 267
Cdd:TIGR01379 174 KEPD--------EEDDEALLQRHLRpEPRV---EEGLALAGYANAAIDVS 212
HypE COG0309
Hydrogenase maturation factor [Posttranslational modification, protein turnover, chaperones];
27-374 4.06e-14

Hydrogenase maturation factor [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 223386 [Multi-domain]  Cd Length: 339  Bit Score: 71.53  E-value: 4.06e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318  27 KGTGCKVPQDVLQKLLESLQENHfqedeqflgAVMPRLGIGMDTCVIPLrhGGLSLVQTTD--YIYPIVDDPYMMGRIAC 104
Cdd:COG0309   7 HGAGGKLMQELINKVILPNFGRR---------DVNVGLANGEDAAIIDL--GDGVLAFTTDpfVIDPLFFPGGDIGKLAV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318 105 ANVLSDLYAMGVTEC-DNMLMLLGVSNKMTDRERdkviplIIQGFKDAAEEAGTSVTGGQT-----VLNPWIVlGGVATT 178
Cdd:COG0309  76 HGTANDVAVSGAKPRyLSVGLILPEGLPIEDLER------ILKSIDEEAEEAGVSIVTGDTkvvpgGKDPIVI-NTTGIG 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318 179 VCQPNEFIMPDNAVPGDVLVLTKPLGTQVA--VAVHQWL--------DIPEKWNKIKLLVTQEDVELAyqeammnmarln 248
Cdd:COG0309 149 IIDKEILVSPSGARPGDAVIVTGTIGIHGAsiLAHRFGEeletelgsDCAPLAKLVKALLSVVGEALA------------ 216
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318 249 rTAAGLMHtfnahaatDITGFGILGHAQNLAKQQRneVSFVIH--NLPVLakmAAVSKACgNMFGLMhgtcPET---SGG 323
Cdd:COG0309 217 -AAVTAMH--------DATRGGLAGALNEMAEASG--VGISIEeeKIPVR---EEVRGVC-ELLGLD----PLElanEGK 277
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 41944318 324 LLICLPREQAARFCAEIKSPKYGEghqAWIIGIVEKGNRTARIIDK---PRIIE 374
Cdd:COG0309 278 LVIAVPPEHAEEVLEALRSHGLKD---AAIIGEVVEEKGGVGLETAgggKRILE 328
fusion_not_SelD TIGR04369
oxidoreductase/SelD-related fusion protein; Some selenium donor proteins (selenide,water ...
30-274 2.84e-13

oxidoreductase/SelD-related fusion protein; Some selenium donor proteins (selenide,water dikase, product of the selD gene, model TIGR00476) are fusion proteins with an N-terminal extension described by model TIGR03169. Members of this family have a C-terminal region similar to yet outside the scope of the SelD model, fused to an N-terminal region similar to but outside the scope of TIGR03169.


Pssm-ID: 275162 [Multi-domain]  Cd Length: 702  Bit Score: 70.06  E-value: 2.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318    30 GC--KVPQDVLQKLLESLQENHFQEDEQflgavmprlgigmDTCVIPLRHGGLSLVQTTDYIYPIVDDPYMMGRI----A 103
Cdd:TIGR04369 357 GCaaKLPAAPLNAALKQAGLEGLGPSPE-------------DAALIGSSNGGDLLLQSVDGFPALVSDPWLNGRLtalhA 423
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318   104 CanvlSDLYAMG--VTECDNMLMLLGVSNKmtdrERDKVIPLIIQGFKDAAEEAGTSVTGGQTV-----LNPWIVLG-GV 175
Cdd:TIGR04369 424 C----SDLWACGarVISAQAVVTLPKVSSA----LQQELLVQTLAGIKSVLEPQGAELIGGHTLesrsePPEPISLGiQI 495
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318   176 ATTV---CQPNEFIMPDNAV-PGDVLVLTKPLGTQV--AVAVH-----QWLDipekwNKIKLLVT--QEDVELAYQEAMM 242
Cdd:TIGR04369 496 SLSVngqLAPGRKPWPKGGLqPGDELLLSRPLGTGVlfAAAMAgaaepEWLD-----AALEQMQQsqHPLVELLAKHQNE 570
                         250       260       270
                  ....*....|....*....|....*....|..
gi 41944318   243 NMarlnrtaaglmhtFNAHAATDITGFGILGH 274
Cdd:TIGR04369 571 DS-------------FGIHACTDITGFGLLGH 589
ThiL COG0611
Thiamine monophosphate kinase [Coenzyme transport and metabolism];
57-374 4.15e-11

Thiamine monophosphate kinase [Coenzyme transport and metabolism];


Pssm-ID: 223684 [Multi-domain]  Cd Length: 317  Bit Score: 62.33  E-value: 4.15e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318  57 LGAVMPRLGIGMDTCVIPLRHGGlSLVQTTD-----YIYPIVDDPYMMGRIACANVLSDLYAMGVTEcDNMLMLLGVSNK 131
Cdd:COG0611  16 RQREDVVLGIGDDAALVDAPEGQ-RLVVTTDmlvegTHFPPDMTPEDLGWKALAVNLSDLAAMGARP-KAFLLSLGLPPD 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318 132 MTDRERDKviplIIQGFKDAAEEAGTSVTGGQTVLNPWiVLGGVATTVCQPNEFIMPDNAVPGDVLVLTKPLGtQVAVAV 211
Cdd:COG0611  94 LDEEWLEA----LADGIFEAAKKYGVKLIGGDTNRGPL-SISVTAIGVLPKGRALLRSGAKPGDLVAVTGTLG-RSAAGL 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318 212 HQWLDIPEkwnkikllvtqEDVELAYQEAMMN-MARLnrtAAGLMHTFNAHAATDITGfGILGHAQNLAkqQRNEVSFVI 290
Cdd:COG0611 168 ELLLNVLG-----------PEDEEELIERHLRpTPRV---ELGLALAKLASAAMDISD-GLAADLGHIA--RASGVGIVI 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318 291 HN--LPVLAKMAAVSKACGNmfglmhgtcPET---SGG----LLICLPREQAARFCAEIKSpkygegHQAWIIGIVEKGN 361
Cdd:COG0611 231 DEdlLPLSDAVLEALDELGD---------PLEwalSGGedyeLVFTVPEENREALLDALRS------LGVTIIGRVTEGE 295
                       330
                ....*....|...
gi 41944318 362 RTARIIDKPRIIE 374
Cdd:COG0611 296 GVVVLVDGKELTL 308
PRK05731 PRK05731
thiamine monophosphate kinase; Provisional
62-360 4.66e-09

thiamine monophosphate kinase; Provisional


Pssm-ID: 235583 [Multi-domain]  Cd Length: 318  Bit Score: 55.99  E-value: 4.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318   62 PRLGIGMDTCVIPLRHGGlSLVQTTD------YIYPIVDDPYMMGRIACANVLSDLYAMGVTEcdnMLMLLGVSnkmtdr 135
Cdd:PRK05731  20 RELGIGDDAALLGPPPGQ-RLVVSTDmlvegvHFRPDWSSPEDLGYKALAVNLSDLAAMGARP---AAFLLALA------ 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318  136 erdkvIPL---------IIQGFKDAAEEAGTSVTGGQTVLNPWIVLGGVATTVCQPNEFIMPDNAVPGDVLVLTKPLGtQ 206
Cdd:PRK05731  90 -----LPKdldeawleaLADGLFELADRYGAELIGGDTTRGPDLSISVTAIGDVPGGRALRRSGAKPGDLVAVTGTLG-D 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318  207 VAVAVHQWLdipekwNKIKLlvtQEDVELAYQEAMMN-MARLN--RTAAGLmhtfnAHAATDIT-G-FGILGHaqnLAKq 281
Cdd:PRK05731 164 SAAGLALLL------NGLRV---PDADAAALISRHLRpQPRVGlgQALAGL-----ASAAIDISdGlAADLGH---IAE- 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318  282 qRNEVSFVIhNLPVLAKMAAVSKACGnmfglmhGTCPET---SGG----LLICLPREQAARFCAEIKSpkygEGHQAWII 354
Cdd:PRK05731 226 -ASGVGADI-DLDALPISPALREAAE-------GEDALRwalSGGedyeLLFTFPPENRGALLAAAGH----LGVGVTII 292

                 ....*.
gi 41944318  355 GIVEKG 360
Cdd:PRK05731 293 GRVTEG 298
COG2144 COG2144
Selenophosphate synthetase-related protein [General function prediction only];
64-199 2.38e-06

Selenophosphate synthetase-related protein [General function prediction only];


Pssm-ID: 225055 [Multi-domain]  Cd Length: 324  Bit Score: 47.41  E-value: 2.38e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318  64 LGIGMDTCVIPLrhGGLSLVQTTDYIYP--IVDDPYMMGRIACANVLSDLYAMGvTECDNMLMLLGVSNKMTDRErdkvi 141
Cdd:COG2144  40 LDFGDDAAVIRV--GDGKLLIAADGIWGklIDADPWWAGYCSVLVNVNDVAAMG-GEPVGAVDAISAKSEDQARE----- 111
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 41944318 142 plIIQGFKDAAEEAGTSVTGGQTVLN-PWIVLGGVATTVCQPNEFIMPDNAVPGDVLVL 199
Cdd:COG2144 112 --ILEGLRKGARKFGVPIVGGHTHPDtPYCVLDVVIGGLIAEEPIITSGTAKPGDLLIF 168
PurM COG0150
Phosphoribosylaminoimidazole (AIR) synthetase [Nucleotide transport and metabolism]; linked to ...
144-367 1.51e-04

Phosphoribosylaminoimidazole (AIR) synthetase [Nucleotide transport and metabolism]; linked to 3D-structure


Pssm-ID: 223228 [Multi-domain]  Cd Length: 345  Bit Score: 41.81  E-value: 1.51e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318 144 IIQGFKDAAEEAGTSVTGGQTVLNPWIVLGG---VATT---VCQPNEFIMPDNAVPGDVLVLTKPLGtqvavaVH----- 212
Cdd:COG0150 119 IVKGIAEGCKQAGCALVGGETAEMPGMYRGGdydLAGFavgVVEKDEIIDGSKVKEGDVIIGLASSG------LHsngys 192
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318 213 --QWLDIPEKWNKIKLLVTQEDVELAyqEAMMNMARL-NRTAAGLMHTFNAHAATDITGFGILGhaqNLAKQQRNEVSFV 289
Cdd:COG0150 193 lvRKIIEESGLDYDDELPEELGKTLG--EELLEPTRIyVKPVLALIKEGDVKGMAHITGGGFVE---NLPRVLPEGLGAV 267
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41944318 290 IHNLPV--------LAKMAAVSKAcgNMFGL--MhGTcpetsgGLLICLPREQAARFCAEIKspkyGEGHQAWIIGIVEK 359
Cdd:COG0150 268 IDKPSWppppifkwLQKAGNVERE--EMYRTfnM-GV------GMVLIVPEEDAEKALALLK----EQGETAYVIGRVEA 334

                ....*...
gi 41944318 360 GNRTARII 367
Cdd:COG0150 335 GEGEVVGV 342
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.14
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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