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Conserved domains on  [gi|1125431597|gb|OLD60613|]
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hypothetical protein AUF60_00350 [Gemmatimonadetes bacterium 13_1_20CM_69_28]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TIGR00284 super family cl36615
dihydropteroate synthase-related protein; This protein has been found so far only in the ...
12-444 1.66e-50

dihydropteroate synthase-related protein; This protein has been found so far only in the Archaea, and in particular in those archaea that lack a bacterial-type dihydropteroate synthase. The central region of this protein shows considerable homology to the amino-terminal half of dihydropteroate synthases, while the carboxyl-terminal region shows homology to the small, uncharacterized protein slr0651 of Synechocystis PCC6803. [Unknown function, General]


The actual alignment was detected with superfamily member TIGR00284:

Pssm-ID: 272997 [Multi-domain]  Cd Length: 499  Bit Score: 179.34  E-value: 1.66e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431597  12 RVLFVTGRLAEPGLRRTLAEMAPAFayDVAVMKITVAALMTTPWIAR-------FLAVPAGTDLVLIPGLCEGDTAAIAD 84
Cdd:TIGR00284   2 KVLLITGRLAKGLIEGILKESDQEA--EVIVLNVHVAGMLSTKTIAKilksrrdLLERARSVDILLIPGLVRGDAKVVEE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431597  85 RAGVRVEKGPKDLRQIP-------------------EYFGRAAAARDYGAYGIE--------------------IVAEVN 125
Cdd:TIGR00284  80 VTGRPVFKGTVEAVDIPdiieilrsgiklsteepadEVVLEIKKLEEYTSKIEEreadfrigslkiplkppplrVVAEIP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431597 126 NAPrlAREALRREADHYRASGADVIDIGCTPGREFPG-LADTVRELVDAGMR-VSVDSLDAGEIRTAVVAGAELVLSVNR 203
Cdd:TIGR00284 160 PTV--AEDGIEGLAARMERDGADMVALGTGSFDDDPDvVKEKVKTALDALDSpVIADTPTLDELYEALKAGASGVIMPDV 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431597 204 SNLD-VARDFAGTPTRVVVIP-DFGEGLETLEPSIAALESWGVSYLI-DPVIEPIGFGFFASLERFAEVRRRYPAAqLFM 280
Cdd:TIGR00284 238 ENAVeLASEKKLPEDAFVVVPgNQPTNYEELAKAVKKLRTSGYSKVAaDPSLSPPLLGLLESIIRFRRASRLLNVP-LVF 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431597 281 GIGNITELTAADTTGVNALLIAICEELGVRAVLTTEVIPWARGVVREVDIARRLMHHAVTRQTLPKGVDDRLVTLKDPtv 360
Cdd:TIGR00284 317 GAANVTELVDADSHGVNALLAAIALEAGASILYVVEDSYKSYRSTAEAAEAAKMASAARKLNSLPKDIGTRLFVVKDK-- 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431597 361 RGYPEA--------ELRELQARVTDPNY-RIFADRD----VITVFN----DEIFVRGTDIHEIFAQL----GVEEATHAF 419
Cdd:TIGR00284 395 RRPPEPveppgeriNVDYIEPSMDRTGYaKIQVDHErgviMLTFYPaggePVVTIEGKKPTSILRALirrfPVSSLEHAG 474
                         490       500
                  ....*....|....*....|....*
gi 1125431597 420 YLGRELMKARLALTLGKNYRQEGAL 444
Cdd:TIGR00284 475 YIGYELAKAEIALALGKTYVQDSPL 499
 
Name Accession Description Interval E-value
TIGR00284 TIGR00284
dihydropteroate synthase-related protein; This protein has been found so far only in the ...
12-444 1.66e-50

dihydropteroate synthase-related protein; This protein has been found so far only in the Archaea, and in particular in those archaea that lack a bacterial-type dihydropteroate synthase. The central region of this protein shows considerable homology to the amino-terminal half of dihydropteroate synthases, while the carboxyl-terminal region shows homology to the small, uncharacterized protein slr0651 of Synechocystis PCC6803. [Unknown function, General]


Pssm-ID: 272997 [Multi-domain]  Cd Length: 499  Bit Score: 179.34  E-value: 1.66e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431597  12 RVLFVTGRLAEPGLRRTLAEMAPAFayDVAVMKITVAALMTTPWIAR-------FLAVPAGTDLVLIPGLCEGDTAAIAD 84
Cdd:TIGR00284   2 KVLLITGRLAKGLIEGILKESDQEA--EVIVLNVHVAGMLSTKTIAKilksrrdLLERARSVDILLIPGLVRGDAKVVEE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431597  85 RAGVRVEKGPKDLRQIP-------------------EYFGRAAAARDYGAYGIE--------------------IVAEVN 125
Cdd:TIGR00284  80 VTGRPVFKGTVEAVDIPdiieilrsgiklsteepadEVVLEIKKLEEYTSKIEEreadfrigslkiplkppplrVVAEIP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431597 126 NAPrlAREALRREADHYRASGADVIDIGCTPGREFPG-LADTVRELVDAGMR-VSVDSLDAGEIRTAVVAGAELVLSVNR 203
Cdd:TIGR00284 160 PTV--AEDGIEGLAARMERDGADMVALGTGSFDDDPDvVKEKVKTALDALDSpVIADTPTLDELYEALKAGASGVIMPDV 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431597 204 SNLD-VARDFAGTPTRVVVIP-DFGEGLETLEPSIAALESWGVSYLI-DPVIEPIGFGFFASLERFAEVRRRYPAAqLFM 280
Cdd:TIGR00284 238 ENAVeLASEKKLPEDAFVVVPgNQPTNYEELAKAVKKLRTSGYSKVAaDPSLSPPLLGLLESIIRFRRASRLLNVP-LVF 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431597 281 GIGNITELTAADTTGVNALLIAICEELGVRAVLTTEVIPWARGVVREVDIARRLMHHAVTRQTLPKGVDDRLVTLKDPtv 360
Cdd:TIGR00284 317 GAANVTELVDADSHGVNALLAAIALEAGASILYVVEDSYKSYRSTAEAAEAAKMASAARKLNSLPKDIGTRLFVVKDK-- 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431597 361 RGYPEA--------ELRELQARVTDPNY-RIFADRD----VITVFN----DEIFVRGTDIHEIFAQL----GVEEATHAF 419
Cdd:TIGR00284 395 RRPPEPveppgeriNVDYIEPSMDRTGYaKIQVDHErgviMLTFYPaggePVVTIEGKKPTSILRALirrfPVSSLEHAG 474
                         490       500
                  ....*....|....*....|....*
gi 1125431597 420 YLGRELMKARLALTLGKNYRQEGAL 444
Cdd:TIGR00284 475 YIGYELAKAEIALALGKTYVQDSPL 499
DUF6513 pfam20123
Family of unknown function (DUF6513); This presumed domain is functionally uncharacterized. ...
13-95 2.92e-21

Family of unknown function (DUF6513); This presumed domain is functionally uncharacterized. This domain family is found in bacteria and archaea, and is typically between 75 and 86 amino acids in length.


Pssm-ID: 437955  Cd Length: 86  Bit Score: 87.73  E-value: 2.92e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431597  13 VLFVTGRLAEPGLRRTLAEMAPA-FAYDVAVMKITVAALMTTPWIARFLAVPAGTDLVLIPGLCEGDTAAIADRAGVRVE 91
Cdd:pfam20123   3 ILFLTGKLAEKSLHKILAEMQPApFEYTVAQLGLSVAALMTAEMIARRLADTRGADRILVPGRCRGDLEALSEKYGVPVE 82

                  ....
gi 1125431597  92 KGPK 95
Cdd:pfam20123  83 RGPE 86
Pterin_binding cd00423
Pterin binding enzymes. This family includes dihydropteroate synthase (DHPS) and ...
120-319 1.18e-14

Pterin binding enzymes. This family includes dihydropteroate synthase (DHPS) and cobalamin-dependent methyltransferases such as methyltetrahydrofolate, corrinoid iron-sulfur protein methyltransferase (MeTr) and methionine synthase (MetH). DHPS, a functional homodimer, catalyzes the condensation of p-aminobenzoic acid (pABA) in the de novo biosynthesis of folate, which is an essential cofactor in both nucleic acid and protein biosynthesis. Prokaryotes (and some lower eukaryotes) must synthesize folate de novo, while higher eukaryotes are able to utilize dietary folate and therefore lack DHPS. Sulfonamide drugs, which are substrate analogs of pABA, target DHPS. Cobalamin-dependent methyltransferases catalyze the transfer of a methyl group via a methyl- cob(III)amide intermediate. These include MeTr, a functional heterodimer, and the folate binding domain of MetH.


Pssm-ID: 238242 [Multi-domain]  Cd Length: 258  Bit Score: 73.85  E-value: 1.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431597 120 IVAEVNNAP--------RLAREALRREADHYRASGADVIDIG---CTPGREFPGLAD-------TVRELVDAGM-RVSVD 180
Cdd:cd00423     3 IMGILNVTPdsfsdggkFLSLDKALEHARRMVEEGADIIDIGgesTRPGAEPVSVEEelervipVLRALAGEPDvPISVD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431597 181 SLDAGEIRTAVVAGAELVLSVN--RSNLDVARDFAGTPTRVVVIP----------------DFGEGLETLEPSIAALESW 242
Cdd:cd00423    83 TFNAEVAEAALKAGADIINDVSggRGDPEMAPLAAEYGAPVVLMHmdgtpqtmqnnpyyadVVDEVVEFLEERVEAATEA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431597 243 GVSY---LIDPVIEPI-----GFGFFASLERFaevrRRYPAAQLFMGIGNITELTAADTTGVNALL------IAICEELG 308
Cdd:cd00423   163 GIPPediILDPGIGFGkteehNLELLRRLDAF----RELPGLPLLLGVSRKSFLGDLLSVGPKDRLagtaafLAAAILNG 238
                         250
                  ....*....|.
gi 1125431597 309 VRAVLTTEVIP 319
Cdd:cd00423   239 ADIVRVHDVKE 249
 
Name Accession Description Interval E-value
TIGR00284 TIGR00284
dihydropteroate synthase-related protein; This protein has been found so far only in the ...
12-444 1.66e-50

dihydropteroate synthase-related protein; This protein has been found so far only in the Archaea, and in particular in those archaea that lack a bacterial-type dihydropteroate synthase. The central region of this protein shows considerable homology to the amino-terminal half of dihydropteroate synthases, while the carboxyl-terminal region shows homology to the small, uncharacterized protein slr0651 of Synechocystis PCC6803. [Unknown function, General]


Pssm-ID: 272997 [Multi-domain]  Cd Length: 499  Bit Score: 179.34  E-value: 1.66e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431597  12 RVLFVTGRLAEPGLRRTLAEMAPAFayDVAVMKITVAALMTTPWIAR-------FLAVPAGTDLVLIPGLCEGDTAAIAD 84
Cdd:TIGR00284   2 KVLLITGRLAKGLIEGILKESDQEA--EVIVLNVHVAGMLSTKTIAKilksrrdLLERARSVDILLIPGLVRGDAKVVEE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431597  85 RAGVRVEKGPKDLRQIP-------------------EYFGRAAAARDYGAYGIE--------------------IVAEVN 125
Cdd:TIGR00284  80 VTGRPVFKGTVEAVDIPdiieilrsgiklsteepadEVVLEIKKLEEYTSKIEEreadfrigslkiplkppplrVVAEIP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431597 126 NAPrlAREALRREADHYRASGADVIDIGCTPGREFPG-LADTVRELVDAGMR-VSVDSLDAGEIRTAVVAGAELVLSVNR 203
Cdd:TIGR00284 160 PTV--AEDGIEGLAARMERDGADMVALGTGSFDDDPDvVKEKVKTALDALDSpVIADTPTLDELYEALKAGASGVIMPDV 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431597 204 SNLD-VARDFAGTPTRVVVIP-DFGEGLETLEPSIAALESWGVSYLI-DPVIEPIGFGFFASLERFAEVRRRYPAAqLFM 280
Cdd:TIGR00284 238 ENAVeLASEKKLPEDAFVVVPgNQPTNYEELAKAVKKLRTSGYSKVAaDPSLSPPLLGLLESIIRFRRASRLLNVP-LVF 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431597 281 GIGNITELTAADTTGVNALLIAICEELGVRAVLTTEVIPWARGVVREVDIARRLMHHAVTRQTLPKGVDDRLVTLKDPtv 360
Cdd:TIGR00284 317 GAANVTELVDADSHGVNALLAAIALEAGASILYVVEDSYKSYRSTAEAAEAAKMASAARKLNSLPKDIGTRLFVVKDK-- 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431597 361 RGYPEA--------ELRELQARVTDPNY-RIFADRD----VITVFN----DEIFVRGTDIHEIFAQL----GVEEATHAF 419
Cdd:TIGR00284 395 RRPPEPveppgeriNVDYIEPSMDRTGYaKIQVDHErgviMLTFYPaggePVVTIEGKKPTSILRALirrfPVSSLEHAG 474
                         490       500
                  ....*....|....*....|....*
gi 1125431597 420 YLGRELMKARLALTLGKNYRQEGAL 444
Cdd:TIGR00284 475 YIGYELAKAEIALALGKTYVQDSPL 499
DUF6513 pfam20123
Family of unknown function (DUF6513); This presumed domain is functionally uncharacterized. ...
13-95 2.92e-21

Family of unknown function (DUF6513); This presumed domain is functionally uncharacterized. This domain family is found in bacteria and archaea, and is typically between 75 and 86 amino acids in length.


Pssm-ID: 437955  Cd Length: 86  Bit Score: 87.73  E-value: 2.92e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431597  13 VLFVTGRLAEPGLRRTLAEMAPA-FAYDVAVMKITVAALMTTPWIARFLAVPAGTDLVLIPGLCEGDTAAIADRAGVRVE 91
Cdd:pfam20123   3 ILFLTGKLAEKSLHKILAEMQPApFEYTVAQLGLSVAALMTAEMIARRLADTRGADRILVPGRCRGDLEALSEKYGVPVE 82

                  ....
gi 1125431597  92 KGPK 95
Cdd:pfam20123  83 RGPE 86
Pterin_binding cd00423
Pterin binding enzymes. This family includes dihydropteroate synthase (DHPS) and ...
120-319 1.18e-14

Pterin binding enzymes. This family includes dihydropteroate synthase (DHPS) and cobalamin-dependent methyltransferases such as methyltetrahydrofolate, corrinoid iron-sulfur protein methyltransferase (MeTr) and methionine synthase (MetH). DHPS, a functional homodimer, catalyzes the condensation of p-aminobenzoic acid (pABA) in the de novo biosynthesis of folate, which is an essential cofactor in both nucleic acid and protein biosynthesis. Prokaryotes (and some lower eukaryotes) must synthesize folate de novo, while higher eukaryotes are able to utilize dietary folate and therefore lack DHPS. Sulfonamide drugs, which are substrate analogs of pABA, target DHPS. Cobalamin-dependent methyltransferases catalyze the transfer of a methyl group via a methyl- cob(III)amide intermediate. These include MeTr, a functional heterodimer, and the folate binding domain of MetH.


Pssm-ID: 238242 [Multi-domain]  Cd Length: 258  Bit Score: 73.85  E-value: 1.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431597 120 IVAEVNNAP--------RLAREALRREADHYRASGADVIDIG---CTPGREFPGLAD-------TVRELVDAGM-RVSVD 180
Cdd:cd00423     3 IMGILNVTPdsfsdggkFLSLDKALEHARRMVEEGADIIDIGgesTRPGAEPVSVEEelervipVLRALAGEPDvPISVD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431597 181 SLDAGEIRTAVVAGAELVLSVN--RSNLDVARDFAGTPTRVVVIP----------------DFGEGLETLEPSIAALESW 242
Cdd:cd00423    83 TFNAEVAEAALKAGADIINDVSggRGDPEMAPLAAEYGAPVVLMHmdgtpqtmqnnpyyadVVDEVVEFLEERVEAATEA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431597 243 GVSY---LIDPVIEPI-----GFGFFASLERFaevrRRYPAAQLFMGIGNITELTAADTTGVNALL------IAICEELG 308
Cdd:cd00423   163 GIPPediILDPGIGFGkteehNLELLRRLDAF----RELPGLPLLLGVSRKSFLGDLLSVGPKDRLagtaafLAAAILNG 238
                         250
                  ....*....|.
gi 1125431597 309 VRAVLTTEVIP 319
Cdd:cd00423   239 ADIVRVHDVKE 249
Pterin_bind pfam00809
Pterin binding enzyme; This family includes a variety of pterin binding enzymes that all adopt ...
144-312 1.04e-04

Pterin binding enzyme; This family includes a variety of pterin binding enzymes that all adopt a TIM barrel fold. The family includes dihydropteroate synthase EC:2.5.1.15 as well as a group methyltransferase enzymes including methyltetrahydrofolate, corrinoid iron-sulfur protein methyltransferase (MeTr) that catalyzes a key step in the Wood-Ljungdahl pathway of carbon dioxide fixation. It transfers the N5-methyl group from methyltetrahydrofolate (CH3-H4folate) to a cob(I)amide centre in another protein, the corrinoid iron-sulfur protein. MeTr is a member of a family of proteins that includes methionine synthase and methanogenic enzymes that activate the methyl group of methyltetra-hydromethano(or -sarcino)pterin.


Pssm-ID: 395651 [Multi-domain]  Cd Length: 243  Bit Score: 43.81  E-value: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431597 144 ASGADVIDIGCTPGREFPGLADTVRELV-----------DAGMRVSVDSLDAGEIRTAVVAGAELVLSVNRSNLD----- 207
Cdd:pfam00809  32 EEGADIIDIGGESTRPGAERVDGEEEMErvlpvlaalrdEADVPISVDTTKAEVAEAALKAGADIINDISGGDGDpemae 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431597 208 VARD---------FAGTPTRVVVIPDFGEGLET-----LEPSIAALESWGV---SYLIDPviepiGFGF-------FASL 263
Cdd:pfam00809 112 LAAEygaavvvmhMDGTPKTMQENEQQYEDVVEeverfLRARVAAAEEAGVppeDIILDP-----GIGFgkteehnLELL 186
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1125431597 264 ERFAEVRRRYPaAQLFMG------IGNITELTAADTTGVNALLIAICEELGVRAV 312
Cdd:pfam00809 187 RTLDELRVILG-VPVLLGvsrksfIGRGLPLGGEERDAGTAAFLALAIAAGADIV 240
DUF4346 pfam14251
Domain of unknown function (DUF4346); This family of proteins is found in bacteria, archaea ...
417-440 2.55e-04

Domain of unknown function (DUF4346); This family of proteins is found in bacteria, archaea and eukaryotes. Proteins in this family are typically between 127 and 502 amino acids in length. There are two conserved sequence motifs: LDP and DHA. Many members of this family have been annotated as dihydropteroate synthases, however no experimental evidence can be found for this and Swiss:Q57571 has been shown not to possess dihydropteroate synthase activity.


Pssm-ID: 405014  Cd Length: 118  Bit Score: 40.63  E-value: 2.55e-04
                          10        20
                  ....*....|....*....|....
gi 1125431597 417 HAFYLGRELMKARLALTLGKNYRQ 440
Cdd:pfam14251  94 HAAYLGREFQRAEAALISGQEYIQ 117
DHPS cd00739
DHPS subgroup of Pterin binding enzymes. DHPS (dihydropteroate synthase), a functional ...
144-317 1.50e-03

DHPS subgroup of Pterin binding enzymes. DHPS (dihydropteroate synthase), a functional homodimer, catalyzes the condensation of p-aminobenzoic acid (pABA) in the de novo biosynthesis of folate, which is an essential cofactor in both nucleic acid and protein biosynthesis. Prokaryotes (and some lower eukaryotes) must synthesize folate de novo, while higher eukaryotes are able to utilize dietary folate and therefore lack DHPS. Sulfonamide drugs, which are substrate analogs of pABA, target DHPS.


Pssm-ID: 238380  Cd Length: 257  Bit Score: 40.28  E-value: 1.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431597 144 ASGADVIDIG----------CTPGREFPGLADTVRELVDAGM-RVSVDSLDAGEIRTAVVAGAELVLSVNRSNLD----- 207
Cdd:cd00739    35 AEGADIIDIGgestrpgadpVSVEEELERVIPVLEALRGELDvLISVDTFRAEVARAALEAGADIINDVSGGSDDpamle 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431597 208 VARDF---------AGTPTRVVVIPD----FGEGLETLEPSIAALESWGV---SYLIDPviepiGFGFFASLE------- 264
Cdd:cd00739   115 VAAEYgaplvlmhmRGTPKTMQENPYyedvVDEVLSFLEARLEAAESAGVarnRIILDP-----GIGFGKTPEhnlellr 189
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431597 265 RFAEVRRR-YPaaqLFMG------IGNITELTAADTTGVNALLIAICEELGVRAVLTTEV 317
Cdd:cd00739   190 RLDELKQLgLP---VLVGasrksfIGALLGREPKDRDWGTLALSALAAANGADIVRVHDV 246
 
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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