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Conserved domains on  [gi|1859508745|ref|WP_175187722|]
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phosphoribosylformylglycinamidine cyclo-ligase [Prosthecochloris ethylica]

Protein Classification

phosphoribosylformylglycinamidine cyclo-ligase( domain architecture ID 11414961)

phosphoribosylformylglycinamidine cyclo-ligase catalyzes the conversion of formylglycinamide ribonucleotide (FGAM) and ATP to AIR, ADP, and Pi, in the fifth step in de novo purine biosynthesis

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PurM COG0150
Phosphoribosylaminoimidazole (AIR) synthetase [Nucleotide transport and metabolism]; ...
1-329 0e+00

Phosphoribosylaminoimidazole (AIR) synthetase [Nucleotide transport and metabolism]; Phosphoribosylaminoimidazole (AIR) synthetase is part of the Pathway/BioSystem: Purine biosynthesis


:

Pssm-ID: 439920 [Multi-domain]  Cd Length: 343  Bit Score: 518.44  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508745   1 MDYKSAGVDIGAGEEFVKLIKPQVRQTFTSRVMTDIGAFGGFFRPDFGAYQDPVLVSSIDGVGTKLKVAAEVGRYDTIGS 80
Cdd:COG0150     5 LTYKDAGVDIDAGNAAVERIKPAVKRTFRPGVLGGLGGFGGLFDLPAKGYKEPVLVSGTDGVGTKLKIAQALDKHDTIGI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508745  81 CLVNHCVNDILVCGARPMFFLDYYACGQLRPAMAADVVKGMVTACRENGCALIGGETAEMPGVYAKDDFDLAGTIVGMVD 160
Cdd:COG0150    85 DLVAMCVNDILVQGAEPLFFLDYIATGKLDPEVAAAVVKGIAEGCRQAGCALIGGETAEMPGMYAPGEYDLAGFAVGVVE 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508745 161 RPMIINGSRISDGDVLIGLPSTGLHTNGYSLARKVFEGR---MGHTFEGMERSVGEELLQVHRSYLPVIEDILSSEDLHG 237
Cdd:COG0150   165 KDKIIDGSRVKAGDVLIGLASSGLHSNGYSLVRKILEVAgldLDDPVPELGRTLGEALLEPTRIYVKPVLALLKAVDVHG 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508745 238 MSHVTGGGLVGNTMRIVPSGLELDVDWNAWPEPVIFDVIRREGGVPEDDMKRTFNLGIGLVLIVAAASVDTMMAGLKAKQ 317
Cdd:COG0150   245 MAHITGGGLPENLPRVLPEGLGAVIDRGSWPVPPIFDWLQELGNVSEEEMYRTFNMGIGMVLVVPPEDADAALALLKAAG 324
                         330
                  ....*....|..
gi 1859508745 318 ENAYIIGSVKAG 329
Cdd:COG0150   325 ETAYVIGEVVAG 336
 
Name Accession Description Interval E-value
PurM COG0150
Phosphoribosylaminoimidazole (AIR) synthetase [Nucleotide transport and metabolism]; ...
1-329 0e+00

Phosphoribosylaminoimidazole (AIR) synthetase [Nucleotide transport and metabolism]; Phosphoribosylaminoimidazole (AIR) synthetase is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 439920 [Multi-domain]  Cd Length: 343  Bit Score: 518.44  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508745   1 MDYKSAGVDIGAGEEFVKLIKPQVRQTFTSRVMTDIGAFGGFFRPDFGAYQDPVLVSSIDGVGTKLKVAAEVGRYDTIGS 80
Cdd:COG0150     5 LTYKDAGVDIDAGNAAVERIKPAVKRTFRPGVLGGLGGFGGLFDLPAKGYKEPVLVSGTDGVGTKLKIAQALDKHDTIGI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508745  81 CLVNHCVNDILVCGARPMFFLDYYACGQLRPAMAADVVKGMVTACRENGCALIGGETAEMPGVYAKDDFDLAGTIVGMVD 160
Cdd:COG0150    85 DLVAMCVNDILVQGAEPLFFLDYIATGKLDPEVAAAVVKGIAEGCRQAGCALIGGETAEMPGMYAPGEYDLAGFAVGVVE 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508745 161 RPMIINGSRISDGDVLIGLPSTGLHTNGYSLARKVFEGR---MGHTFEGMERSVGEELLQVHRSYLPVIEDILSSEDLHG 237
Cdd:COG0150   165 KDKIIDGSRVKAGDVLIGLASSGLHSNGYSLVRKILEVAgldLDDPVPELGRTLGEALLEPTRIYVKPVLALLKAVDVHG 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508745 238 MSHVTGGGLVGNTMRIVPSGLELDVDWNAWPEPVIFDVIRREGGVPEDDMKRTFNLGIGLVLIVAAASVDTMMAGLKAKQ 317
Cdd:COG0150   245 MAHITGGGLPENLPRVLPEGLGAVIDRGSWPVPPIFDWLQELGNVSEEEMYRTFNMGIGMVLVVPPEDADAALALLKAAG 324
                         330
                  ....*....|..
gi 1859508745 318 ENAYIIGSVKAG 329
Cdd:COG0150   325 ETAYVIGEVVAG 336
PurM cd02196
PurM (Aminoimidazole Ribonucleotide [AIR] synthetase), one of eleven enzymes required for ...
34-327 2.21e-157

PurM (Aminoimidazole Ribonucleotide [AIR] synthetase), one of eleven enzymes required for purine biosynthesis, catalyzes the conversion of formylglycinamide ribonucleotide (FGAM) and ATP to AIR, ADP, and Pi, the fifth step in de novo purine biosynthesis. The N-terminal domain of PurM is related to the ATP-binding domains of hydrogen expression/formation protein HypE, the AIR synthases, selenophosphate synthetase (SelD), and FGAM synthase and is thought to bind ATP.


Pssm-ID: 100032 [Multi-domain]  Cd Length: 297  Bit Score: 441.91  E-value: 2.21e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508745  34 TDIGAFGGFFRPDFGAYQDPVLVSSIDGVGTKLKVAAEVGRYDTIGSCLVNHCVNDILVCGARPMFFLDYYACGQLRPAM 113
Cdd:cd02196     1 GGIGGFAGLFDLGLGGYKDPVLVSGTDGVGTKLKLAQEMGKHDTIGIDLVAMCVNDILCQGAEPLFFLDYIATGKLDPEV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508745 114 AADVVKGMVTACRENGCALIGGETAEMPGVYAKDDFDLAGTIVGMVDRPMIINGSRISDGDVLIGLPSTGLHTNGYSLAR 193
Cdd:cd02196    81 AAEIVKGIAEGCRQAGCALLGGETAEMPGVYAEGEYDLAGFAVGVVEKDKIIDGSKIKPGDVLIGLPSSGLHSNGYSLVR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508745 194 KVFEGRMG---HTFEGMERSVGEELLQVHRSYLPVIEDILSSEDLHGMSHVTGGGLVGNTMRIVPSGLELDVDWNAWPEP 270
Cdd:cd02196   161 KILFEEGLdydDPEPGLGKTLGEELLTPTRIYVKPILPLLEKVLVKGMAHITGGGLPENLPRVLPEGLGAVIDLGSWEIP 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1859508745 271 VIFDVIRREGGVPEDDMKRTFNLGIGLVLIVAAASVDTMMAGLKAKQENAYIIGSVK 327
Cdd:cd02196   241 PIFKWIQKAGNVSEEEMYRTFNMGIGMVLIVSEEDADEVLEILEKLGEKAYVIGEVV 297
purM TIGR00878
phosphoribosylaminoimidazole synthetase; Alternate name: phosphoribosylformylglycinamidine ...
1-329 1.42e-131

phosphoribosylaminoimidazole synthetase; Alternate name: phosphoribosylformylglycinamidine cyclo-ligase; AIRS; AIR synthase This enzyme is found as a homodimeric monofunctional protein in prokaryotes and as part of a larger, multifunctional protein, sometimes with two copies of this enzyme in tandem, in eukaryotes. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 273316 [Multi-domain]  Cd Length: 332  Bit Score: 377.83  E-value: 1.42e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508745   1 MDYKSAGVDIGAGEEFVKLIKPQVRQTFTSRVMTDIGAFGGFFrpDFG-AYQDPVLVSSIDGVGTKLKVAAEVGRYDTIG 79
Cdd:TIGR00878   1 VTYADAGVDIDAGNEAVKRIKSLVKKTRRPEVMGGLGGFAGLF--DLGdKYKEPVLVSGTDGVGTKLLVAEAMNKHDTIG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508745  80 SCLVNHCVNDILVCGARPMFFLDYYACGQLRPAMAADVVKGMVTACRENGCALIGGETAEMPGVYAKDDFDLAGTIVGMV 159
Cdd:TIGR00878  79 IDLVAMNVNDLLVQGAEPLFFLDYLAVGKLDPEVASQIVKGIAEGCKQAGCALVGGETAEMPGMYRGGHYDLAGTAVGVV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508745 160 DRPMIINGSRISDGDVLIGLPSTGLHTNGYSLARKVFE--GRMGH--TFEGMERSVGEELLQVHRSYLPVIEDILSSEDL 235
Cdd:TIGR00878 159 EKDEIITGEKVKPGDVLIGLGSSGIHSNGLSLVRKVLEdiAGLDYedTPEEFGKTLGEELLEPTRIYVKPILELIKSVIV 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508745 236 HGMSHVTGGGLVGNTMRIVPSGLELDVDWNAWPEPVIFDVIRREGGVPEDDMKRTFNLGIGLVLIVAAASVDTMMAGLKA 315
Cdd:TIGR00878 239 HGLAHITGGGLLENIPRRLPDGLKAVIDMSSWPQPPIFKWIQEAGNVEEEEMYRTFNMGVGFVVIVPEEEVDKALALLNA 318
                         330
                  ....*....|....
gi 1859508745 316 KQENAYIIGSVKAG 329
Cdd:TIGR00878 319 YGEKAWVIGEVKKG 332
PLN02557 PLN02557
phosphoribosylformylglycinamidine cyclo-ligase
1-329 6.87e-102

phosphoribosylformylglycinamidine cyclo-ligase


Pssm-ID: 178172 [Multi-domain]  Cd Length: 379  Bit Score: 304.42  E-value: 6.87e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508745   1 MDYKSAGVDIGAGEEFVKLIKpqvrqtftsRVMTDIGAFGGFFrpDFGayqDPVLVSSIDGVGTKLKVAAEVGRYDTIGS 80
Cdd:PLN02557   59 LTYKDAGVDIDAGSELVRRIA---------KMAPGIGGFGGLF--PFG---DSYLVAGTDGVGTKLKLAFETGIHDTIGI 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508745  81 CLVNHCVNDILVCGARPMFFLDYYACGQLRPAMAADVVKGMVTACRENGCALIGGETAEMPGVYAKDDFDLAGTIVGMVD 160
Cdd:PLN02557  125 DLVAMSVNDIVTSGAKPLFFLDYFATSHLDVDLAEKVIKGIVDGCQQSDCALLGGETAEMPGFYAEGEYDLSGFAVGSVK 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508745 161 RPMIINGSRISDGDVLIGLPSTGLHTNGYSLARKVFEgRMGHTFE----GMERSVGEELLQVHRSYLPVIEDILSSEDLH 236
Cdd:PLN02557  205 KDAVIDGKNIVAGDVLIGLPSSGVHSNGFSLVRRVLA-KSGLSLKdqlpGASVTIGEALMAPTVIYVKQVLDIISKGGVK 283
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508745 237 GMSHVTGGGLVGNTMRIVPSGLELDVDWNAWPEPVIFDVIRREGGVPEDDMKRTFNLGIGLVLIVAAASVDTMmagLKAK 316
Cdd:PLN02557  284 GIAHITGGGFTDNIPRVFPKGLGAKIRTGSWEVPPLFKWLQEAGNIEDAEMRRTFNMGIGMVLVVSPEAADRI---LEEG 360
                         330
                  ....*....|...
gi 1859508745 317 QENAYIIGSVKAG 329
Cdd:PLN02557  361 AYPAYRIGEVING 373
AIRS pfam00586
AIR synthase related protein, N-terminal domain; This family includes Hydrogen expression ...
55-159 3.66e-20

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: 459859 [Multi-domain]  Cd Length: 104  Bit Score: 83.65  E-value: 3.66e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508745  55 LVSSIDGVGTKLKVAAevgrYDTIGSCLVNHCVNDILVCGARPMFFLDYYACGQ--LRPAMAADVVKGMVTACRENGCAL 132
Cdd:pfam00586   5 VAVTTDGHGTPSLVDP----YHFPGAKAVAGNLSDIAAMGARPLAFLDSLALPGgpEVEWVLEEIVEGIAEACREAGVPL 80
                          90       100
                  ....*....|....*....|....*..
gi 1859508745 133 IGGETAEMPGVyakDDFDLAGTIVGMV 159
Cdd:pfam00586  81 VGGDTSFDPEG---GKPTISVTAVGIV 104
 
Name Accession Description Interval E-value
PurM COG0150
Phosphoribosylaminoimidazole (AIR) synthetase [Nucleotide transport and metabolism]; ...
1-329 0e+00

Phosphoribosylaminoimidazole (AIR) synthetase [Nucleotide transport and metabolism]; Phosphoribosylaminoimidazole (AIR) synthetase is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 439920 [Multi-domain]  Cd Length: 343  Bit Score: 518.44  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508745   1 MDYKSAGVDIGAGEEFVKLIKPQVRQTFTSRVMTDIGAFGGFFRPDFGAYQDPVLVSSIDGVGTKLKVAAEVGRYDTIGS 80
Cdd:COG0150     5 LTYKDAGVDIDAGNAAVERIKPAVKRTFRPGVLGGLGGFGGLFDLPAKGYKEPVLVSGTDGVGTKLKIAQALDKHDTIGI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508745  81 CLVNHCVNDILVCGARPMFFLDYYACGQLRPAMAADVVKGMVTACRENGCALIGGETAEMPGVYAKDDFDLAGTIVGMVD 160
Cdd:COG0150    85 DLVAMCVNDILVQGAEPLFFLDYIATGKLDPEVAAAVVKGIAEGCRQAGCALIGGETAEMPGMYAPGEYDLAGFAVGVVE 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508745 161 RPMIINGSRISDGDVLIGLPSTGLHTNGYSLARKVFEGR---MGHTFEGMERSVGEELLQVHRSYLPVIEDILSSEDLHG 237
Cdd:COG0150   165 KDKIIDGSRVKAGDVLIGLASSGLHSNGYSLVRKILEVAgldLDDPVPELGRTLGEALLEPTRIYVKPVLALLKAVDVHG 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508745 238 MSHVTGGGLVGNTMRIVPSGLELDVDWNAWPEPVIFDVIRREGGVPEDDMKRTFNLGIGLVLIVAAASVDTMMAGLKAKQ 317
Cdd:COG0150   245 MAHITGGGLPENLPRVLPEGLGAVIDRGSWPVPPIFDWLQELGNVSEEEMYRTFNMGIGMVLVVPPEDADAALALLKAAG 324
                         330
                  ....*....|..
gi 1859508745 318 ENAYIIGSVKAG 329
Cdd:COG0150   325 ETAYVIGEVVAG 336
PurM cd02196
PurM (Aminoimidazole Ribonucleotide [AIR] synthetase), one of eleven enzymes required for ...
34-327 2.21e-157

PurM (Aminoimidazole Ribonucleotide [AIR] synthetase), one of eleven enzymes required for purine biosynthesis, catalyzes the conversion of formylglycinamide ribonucleotide (FGAM) and ATP to AIR, ADP, and Pi, the fifth step in de novo purine biosynthesis. The N-terminal domain of PurM is related to the ATP-binding domains of hydrogen expression/formation protein HypE, the AIR synthases, selenophosphate synthetase (SelD), and FGAM synthase and is thought to bind ATP.


Pssm-ID: 100032 [Multi-domain]  Cd Length: 297  Bit Score: 441.91  E-value: 2.21e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508745  34 TDIGAFGGFFRPDFGAYQDPVLVSSIDGVGTKLKVAAEVGRYDTIGSCLVNHCVNDILVCGARPMFFLDYYACGQLRPAM 113
Cdd:cd02196     1 GGIGGFAGLFDLGLGGYKDPVLVSGTDGVGTKLKLAQEMGKHDTIGIDLVAMCVNDILCQGAEPLFFLDYIATGKLDPEV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508745 114 AADVVKGMVTACRENGCALIGGETAEMPGVYAKDDFDLAGTIVGMVDRPMIINGSRISDGDVLIGLPSTGLHTNGYSLAR 193
Cdd:cd02196    81 AAEIVKGIAEGCRQAGCALLGGETAEMPGVYAEGEYDLAGFAVGVVEKDKIIDGSKIKPGDVLIGLPSSGLHSNGYSLVR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508745 194 KVFEGRMG---HTFEGMERSVGEELLQVHRSYLPVIEDILSSEDLHGMSHVTGGGLVGNTMRIVPSGLELDVDWNAWPEP 270
Cdd:cd02196   161 KILFEEGLdydDPEPGLGKTLGEELLTPTRIYVKPILPLLEKVLVKGMAHITGGGLPENLPRVLPEGLGAVIDLGSWEIP 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1859508745 271 VIFDVIRREGGVPEDDMKRTFNLGIGLVLIVAAASVDTMMAGLKAKQENAYIIGSVK 327
Cdd:cd02196   241 PIFKWIQKAGNVSEEEMYRTFNMGIGMVLIVSEEDADEVLEILEKLGEKAYVIGEVV 297
purM TIGR00878
phosphoribosylaminoimidazole synthetase; Alternate name: phosphoribosylformylglycinamidine ...
1-329 1.42e-131

phosphoribosylaminoimidazole synthetase; Alternate name: phosphoribosylformylglycinamidine cyclo-ligase; AIRS; AIR synthase This enzyme is found as a homodimeric monofunctional protein in prokaryotes and as part of a larger, multifunctional protein, sometimes with two copies of this enzyme in tandem, in eukaryotes. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 273316 [Multi-domain]  Cd Length: 332  Bit Score: 377.83  E-value: 1.42e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508745   1 MDYKSAGVDIGAGEEFVKLIKPQVRQTFTSRVMTDIGAFGGFFrpDFG-AYQDPVLVSSIDGVGTKLKVAAEVGRYDTIG 79
Cdd:TIGR00878   1 VTYADAGVDIDAGNEAVKRIKSLVKKTRRPEVMGGLGGFAGLF--DLGdKYKEPVLVSGTDGVGTKLLVAEAMNKHDTIG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508745  80 SCLVNHCVNDILVCGARPMFFLDYYACGQLRPAMAADVVKGMVTACRENGCALIGGETAEMPGVYAKDDFDLAGTIVGMV 159
Cdd:TIGR00878  79 IDLVAMNVNDLLVQGAEPLFFLDYLAVGKLDPEVASQIVKGIAEGCKQAGCALVGGETAEMPGMYRGGHYDLAGTAVGVV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508745 160 DRPMIINGSRISDGDVLIGLPSTGLHTNGYSLARKVFE--GRMGH--TFEGMERSVGEELLQVHRSYLPVIEDILSSEDL 235
Cdd:TIGR00878 159 EKDEIITGEKVKPGDVLIGLGSSGIHSNGLSLVRKVLEdiAGLDYedTPEEFGKTLGEELLEPTRIYVKPILELIKSVIV 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508745 236 HGMSHVTGGGLVGNTMRIVPSGLELDVDWNAWPEPVIFDVIRREGGVPEDDMKRTFNLGIGLVLIVAAASVDTMMAGLKA 315
Cdd:TIGR00878 239 HGLAHITGGGLLENIPRRLPDGLKAVIDMSSWPQPPIFKWIQEAGNVEEEEMYRTFNMGVGFVVIVPEEEVDKALALLNA 318
                         330
                  ....*....|....
gi 1859508745 316 KQENAYIIGSVKAG 329
Cdd:TIGR00878 319 YGEKAWVIGEVKKG 332
PLN02557 PLN02557
phosphoribosylformylglycinamidine cyclo-ligase
1-329 6.87e-102

phosphoribosylformylglycinamidine cyclo-ligase


Pssm-ID: 178172 [Multi-domain]  Cd Length: 379  Bit Score: 304.42  E-value: 6.87e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508745   1 MDYKSAGVDIGAGEEFVKLIKpqvrqtftsRVMTDIGAFGGFFrpDFGayqDPVLVSSIDGVGTKLKVAAEVGRYDTIGS 80
Cdd:PLN02557   59 LTYKDAGVDIDAGSELVRRIA---------KMAPGIGGFGGLF--PFG---DSYLVAGTDGVGTKLKLAFETGIHDTIGI 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508745  81 CLVNHCVNDILVCGARPMFFLDYYACGQLRPAMAADVVKGMVTACRENGCALIGGETAEMPGVYAKDDFDLAGTIVGMVD 160
Cdd:PLN02557  125 DLVAMSVNDIVTSGAKPLFFLDYFATSHLDVDLAEKVIKGIVDGCQQSDCALLGGETAEMPGFYAEGEYDLSGFAVGSVK 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508745 161 RPMIINGSRISDGDVLIGLPSTGLHTNGYSLARKVFEgRMGHTFE----GMERSVGEELLQVHRSYLPVIEDILSSEDLH 236
Cdd:PLN02557  205 KDAVIDGKNIVAGDVLIGLPSSGVHSNGFSLVRRVLA-KSGLSLKdqlpGASVTIGEALMAPTVIYVKQVLDIISKGGVK 283
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508745 237 GMSHVTGGGLVGNTMRIVPSGLELDVDWNAWPEPVIFDVIRREGGVPEDDMKRTFNLGIGLVLIVAAASVDTMmagLKAK 316
Cdd:PLN02557  284 GIAHITGGGFTDNIPRVFPKGLGAKIRTGSWEVPPLFKWLQEAGNIEDAEMRRTFNMGIGMVLVVSPEAADRI---LEEG 360
                         330
                  ....*....|...
gi 1859508745 317 QENAYIIGSVKAG 329
Cdd:PLN02557  361 AYPAYRIGEVING 373
PurM-like cd00396
AIR (aminoimidazole ribonucleotide) synthase related protein. This family includes Hydrogen ...
54-325 1.55e-30

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: 115.19  E-value: 1.55e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508745  54 VLVSSIDGVGTKLKVaaevgRYDTIGSCLVNHCVNDILVCGARPMFFLDYYACGQLR-PAMAADVVKGMVTACRENGCAL 132
Cdd:cd00396     1 SLAMSTDGINPPLAI-----NPWAGGRLAVGGAVNDIAAMGARPIALLASLSLSNGLeVDILEDVVDGVAEACNQLGVPI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508745 133 IGGETAEMPGvYAKDDFDLAGTIVGMVDRPMIINGSRISDGDVLIGLpstglhtngyslarkvfeGRMghtfegmersvg 212
Cdd:cd00396    76 VGGHTSVSPG-TMGHKLSLAVFAIGVVEKDRVIDSSGARPGDVLILT------------------GVD------------ 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508745 213 eellqvhrsylpVIEDILSSEDLHGMSHVTGGGLVGNTMRIVP-SGLELDVDWNAWPEPVIFDVIRREGGvpedDMKRTF 291
Cdd:cd00396   125 ------------AVLELVAAGDVHAMHDITDGGLLGTLPELAQaSGVGAEIDLEAIPLDEVVRWLCVEHI----EEALLF 188
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1859508745 292 NLGIGLVLIVAAASVDTMMAGLKAKQENAYIIGS 325
Cdd:cd00396   189 NSSGGLLIAVPAEEADAVLLLLNGNGIDAAVIGR 222
AIRS pfam00586
AIR synthase related protein, N-terminal domain; This family includes Hydrogen expression ...
55-159 3.66e-20

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: 459859 [Multi-domain]  Cd Length: 104  Bit Score: 83.65  E-value: 3.66e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508745  55 LVSSIDGVGTKLKVAAevgrYDTIGSCLVNHCVNDILVCGARPMFFLDYYACGQ--LRPAMAADVVKGMVTACRENGCAL 132
Cdd:pfam00586   5 VAVTTDGHGTPSLVDP----YHFPGAKAVAGNLSDIAAMGARPLAFLDSLALPGgpEVEWVLEEIVEGIAEACREAGVPL 80
                          90       100
                  ....*....|....*....|....*..
gi 1859508745 133 IGGETAEMPGVyakDDFDLAGTIVGMV 159
Cdd:pfam00586  81 VGGDTSFDPEG---GKPTISVTAVGIV 104
AIRS_C pfam02769
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression ...
173-329 1.31e-19

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: 460684 [Multi-domain]  Cd Length: 152  Bit Score: 83.93  E-value: 1.31e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508745 173 GDVLIGLPSTGLHTNGYSLARKVFEGRmghtfEGMERSVGEELLQVHRSYLpVIEDILSSEDLHGMSHVTGGGLVGNTMR 252
Cdd:pfam02769   3 GDVLILLGSSGLHGAGLSLSRKGLEDS-----GLAAVQLGDPLLEPTLIYV-KLLLAALGGLVKAMHDITGGGLAGALAE 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1859508745 253 IVP-SGLELDVDWNAWPepvifdvIRREGGVPEdDMKRTFNLGIGLVlIVAAASVDTMMAGLKAKQENAYIIGSVKAG 329
Cdd:pfam02769  77 MAPaSGVGAEIDLDKVP-------IFEELMLPL-EMLLSENQGRGLV-VVAPEEAEAVLAILEKEGLEAAVIGEVTAG 145
HypE COG0309
Carbamoyl dehydratase HypE (hydrogenase maturation factor) [Posttranslational modification, ...
78-329 5.23e-11

Carbamoyl dehydratase HypE (hydrogenase maturation factor) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440078 [Multi-domain]  Cd Length: 328  Bit Score: 62.78  E-value: 5.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508745  78 IGSCLVNHCVNDILVCGARPMFFLdyyaCGQLRP-----AMAADVVKGMVTACRENGCALIGGETaempGVYAKDDFD-- 150
Cdd:COG0309    62 IGKLAVHGTVNDLAVSGAKPLYLS----VSLILEegfplEDLERIVESMAEAAREAGVSIVTGDT----KVVERGGVDgp 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508745 151 -LAGTIVGMVDRPMIINGSRISDGDVLI-----GLPSTGLhtngysLARkvfegRMGHTFEGmersvgeELLQVHRSYLP 224
Cdd:COG0309   134 fINTTGIGVVPKGRLISPSGARPGDKIIvtggiGDHGTAI------LAA-----REGLELEG-------ELLSDAAPLND 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508745 225 VIEDIL--SSEDLHGMSHVTGGGLVG--NTMRIVpSGLELDVDWNAWPepvifdvirreggVPED-----DMkrtfnLGI 295
Cdd:COG0309   196 LVSVLLeaAPGGVHAMRDPTRGGLAGalNEIAEA-SGVGIEIDEDAIP-------------VRPEvrgicEL-----LGL 256
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1859508745 296 --------G-LVLIVAAASVDTMMAGLKAKQENAYIIGSVKAG 329
Cdd:COG0309   257 dplylaneGkLVAVVPPEDAEAVLEALRAHGIDAAIIGEVTEG 299
PurM-like1 cd06061
AIR synthase (PurM) related protein, subgroup 1 of unknown function. The family of PurM ...
76-248 3.66e-07

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: 50.67  E-value: 3.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508745  76 DTIGSCLVNHCVNDILVCGARPMFFLDYYAcgqLRPAMAAD----VVKGMVTACRENGCALIGGETaempGVYAKDDFDL 151
Cdd:cd06061    57 KDAGWLAVHIAANDIATSGARPRWLLVTLL---LPPGTDEEelkaIMREINEAAKELGVSIVGGHT----EVTPGVTRPI 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508745 152 AG-TIVGMVDRPMIINGSRISDGDVLI-----GLPSTGLhtngysLARkVFEGRMghtfegMERSVGEELLQVHR--SYL 223
Cdd:cd06061   130 ISvTAIGKGEKDKLVTPSGAKPGDDIVmtkgaGIEGTAI------LAN-DFEEEL------KKRLSEEELREAAKlfYKI 196
                         170       180
                  ....*....|....*....|....*..
gi 1859508745 224 PVIED--ILSSEDLHGMSHVTGGGLVG 248
Cdd:cd06061   197 SVVKEalIAAEAGVTAMHDATEGGILG 223
SelD cd02195
Selenophosphate synthetase (SelD) catalyzes the conversion of selenium to selenophosphate ...
83-326 1.13e-06

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: 49.44  E-value: 1.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508745  83 VNHCVNDILVCGARPMFFLDY----YACGQLRPAMAADVVKGMVTACRENGCALIGGETAEMPGVyakddfDLAGTIVGM 158
Cdd:cd02195    77 AANALSDIYAMGAKPLSALAIvtlpRKLPALQEEVLREILAGGKDKLREAGAVLVGGHTIEGPEP------KYGLSVTGL 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508745 159 VDRPMIINGSRISDGDVLI-----GlpsTGLHTNGY---SLARKVFEGRMGHtfegMERSVGEellqvhrsylpvIEDIL 230
Cdd:cd02195   151 VHPNKILRNSGAKPGDVLIltkplG---TGILFAAEmagLARGEDIDAALES----MARLNRA------------AAELL 211
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508745 231 SSEDLHGMSHVTGGGLVGNTMRIV-PSGLELDVDWNAWPepvifdVIRREGgvpeddmkrtfnlgiGLVLIVAAASVDTM 309
Cdd:cd02195   212 RKYGAHACTDVTGFGLLGHLLEMArASGVSAEIDLDKLP------LLQTSG---------------GLLAAVPPEDAAAL 270
                         250
                  ....*....|....*..
gi 1859508745 310 MAGLKAKQENAYIIGSV 326
Cdd:cd02195   271 LALLKAGGPPAAIIGEV 287
HypE cd02197
HypE (Hydrogenase expression/formation protein). HypE is involved in Ni-Fe hydrogenase ...
78-326 3.54e-06

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: 47.83  E-value: 3.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508745  78 IGSCLVNHCVNDILVCGARPMffldYYACG----------QLRpamaaDVVKGMVTACRENGCALIGGETAEMP-----G 142
Cdd:cd02197    58 IGKLAVCGTVNDLAMMGAKPL----YLSLGfileegfpleDLE-----RIVKSMAEAAREAGVKIVTGDTKVVPkgkadG 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508745 143 VYakddfdLAGTIVGMVDRPMIINGSRISDGDVLIGLPSTGLHtnGYSlarkVFEGRMGHTFEGmersvgeELLQVHRSY 222
Cdd:cd02197   129 IF------INTTGIGVIPRGVIISPSNIRPGDKIIVSGTIGDH--GAA----ILAAREGLGFET-------DIESDCAPL 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508745 223 LPVIEDILSS-EDLHGMSHVTGGGLvGNTMrivpsgleldvdwNAWPEPVIFDVIRREGGVPEDDMKRTFN--LGI---- 295
Cdd:cd02197   190 NGLVEALLEAgPGIHAMRDPTRGGL-AAVL-------------NEIARASGVGIEIEEEAIPVREEVRGACemLGLdply 255
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1859508745 296 ----G-LVLIVAAASVDTMMAGLKA--KQENAYIIGSV 326
Cdd:cd02197   256 laneGkFVAIVPPEDAEEVLEALRShpLGKEAAIIGEV 293
SelD COG0709
Selenophosphate synthase [Amino acid transport and metabolism];
84-329 3.67e-05

Selenophosphate synthase [Amino acid transport and metabolism];


Pssm-ID: 440473 [Multi-domain]  Cd Length: 346  Bit Score: 45.07  E-value: 3.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508745  84 NHCVNDILVCGARPMFFLdyyA-----CGQLRPAMAADVVKGMVTACRENGCALIGGETAEmpgvyakDD---FDLAGTi 155
Cdd:COG0709    84 ANALSDVYAMGGRPLTAL---AivgfpIDKLPEEVLAEILAGGADKCREAGAPLAGGHSID-------DPepkYGLAVT- 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508745 156 vGMVDRPMII--NGSRisDGDVLI-------GLPSTG-----LHTNGYSLARKVfegrmghtfegMERS--VGEELLQVH 219
Cdd:COG0709   153 -GLVHPDKVLrnAGAR--PGDVLIltkplgtGILTTAikaglADGEDIAAAIAS-----------MTTLnkAAAELARLY 218
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508745 220 rsylpviedilsseDLHGMSHVTGGGLVGNTMRIV-PSGLELDVDWNAWPepvIFDVIR---REGGVP----------ED 285
Cdd:COG0709   219 --------------GVHACTDVTGFGLLGHLLEMArGSGVSAEIDLDAVP---LLPGALelaEQGIVPggtyrnrasyGA 281
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1859508745 286 DMKRTFNL--------------GiGLVLIVAAASVDTMMAGLKAKQENAYIIGSVKAG 329
Cdd:COG0709   282 KVEFAEGLdeaqrdllfdpqtsG-GLLIAVPPEAAEELLAALRAAGYAAAIIGEVTAG 338
ThiL cd02194
ThiL (Thiamine-monophosphate kinase) plays a dual role in de novo biosynthesis and in salvage ...
87-185 9.70e-04

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: 40.23  E-value: 9.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508745  87 VN--DILVCGARPMFFLDYYAC-GQLRPAMAADVVKGMVTACRENGCALIGGETAEMPGVYakddfdLAGTIVGMVDRPM 163
Cdd:cd02194    66 VNlsDLAAMGARPLGFLLSLGLpPDTDEEWLEEFYRGLAEAADRYGVPLVGGDTTSGSELV------ISVTALGEVEKGK 139
                          90       100
                  ....*....|....*....|....*....
gi 1859508745 164 II--NGSRIsdGDVL-----IGLPSTGLH 185
Cdd:cd02194   140 PLrrSGAKP--GDLLyvtgtLGDAAAGLA 166
hypE TIGR02124
hydrogenase expression/formation protein HypE; This family contains HypE (or HupE), a protein ...
78-253 1.34e-03

hydrogenase expression/formation protein HypE; This family contains HypE (or HupE), a protein required for expression of catalytically active hydrogenase in many systems. It appears to be an accessory protein involved in maturation rather than a regulatory protein involved in expression. HypE shows considerable homology to the thiamine-monophosphate kinase ThiL (TIGR01379) and other enzymes.


Pssm-ID: 273984 [Multi-domain]  Cd Length: 320  Bit Score: 39.93  E-value: 1.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508745  78 IGSCLVNHCVNDILVCGARPMffldYYACG-----QLRPAMAADVVKGMVTACRENGCALIGGETAEMPGVYAKDDFdLA 152
Cdd:TIGR02124  53 IGKLAVCGTVNDVAVSGAKPL----YLSCGfileeGFPIEDLERIVKSMAEAARKAGVKIVTGDTKVVEKGKADGIF-IN 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508745 153 GTIVGMVDRPMIINGSRISDGDVLIGLPSTGLHtnGYSLARKvfegRMGHTFEGmersvgeELLQVHRSYLPVIEDILSS 232
Cdd:TIGR02124 128 TTGIGVIPSGIPISAHNLQPGDKIIVSGTIGDH--GAAILAV----REGLGFET-------NLESDCAPLNGLVETLLNA 194
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1859508745 233 -EDLHGMSHVTGGGL----------VGNTMRI 253
Cdd:TIGR02124 195 gPAVHAMRDATRGGLaavlnewaqaSGVGIVI 226
PRK05731 PRK05731
thiamine monophosphate kinase; Provisional
87-197 2.13e-03

thiamine monophosphate kinase; Provisional


Pssm-ID: 235583 [Multi-domain]  Cd Length: 318  Bit Score: 39.43  E-value: 2.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508745  87 VN--DILVCGARPMFFLDYYAC-GQLRPAMAADVVKGMVTACRENGCALIGGETAEMPgvyakdDFDLAGTIVGMVDRPM 163
Cdd:PRK05731   69 VNlsDLAAMGARPAAFLLALALpKDLDEAWLEALADGLFELADRYGAELIGGDTTRGP------DLSISVTAIGDVPGGR 142
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1859508745 164 IINGSRISDGDVL-----IGLPSTGLH--TNGYSLARKVFE 197
Cdd:PRK05731  143 ALRRSGAKPGDLVavtgtLGDSAAGLAllLNGLRVPDADAA 183
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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