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Conserved domains on  [gi|114619479|ref|XP_001165532|]
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elongator complex protein 3 isoform X1 [Pan troglodytes]

Protein Classification

elongator complex protein 3( domain architecture ID 1003394)

elongator complex protein 3 is the catalytic histone acetyltransferase subunit of the RNA polymerase II elongator complex, which is a component of the RNA polymerase II holoenzyme and is involved in transcriptional elongation

EC:  2.3.1.-
Gene Ontology:  GO:0046872|GO:0016407|GO:0006357

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ELP3 super family cl36845
radical SAM enzyme/protein acetyltransferase, ELP3 family; This family includes elongator ...
36-546 0e+00

radical SAM enzyme/protein acetyltransferase, ELP3 family; This family includes elongator complex protein 3 (ELP3) from eukaryotes and related proteins from other lineages. ELP3 is a component of the RNA polymerase II holoenzyme. It has an N-terminal radical SAM domain and C-terminal GNAT acetyltransferase domain. Members of this family are found in eukaryotes, archaea, and a few bacteria (e.g. Atopobium sp). The activity discovered first was an acetyltransferase modification at the N-termini of all four core histones, shown in vitro in eukaryotes. More recently, the radical SAM domain was shown to play a role in zygotic paternal genome demethylation. Family TIGR01212, widespread in prokaryotes, lacks the GNAT acetyltransferase domain but shares extensive sequence similarity with this family (TIGR01211). [Transcription, DNA-dependent RNA polymerase]


The actual alignment was detected with superfamily member TIGR01211:

Pssm-ID: 273503 [Multi-domain]  Cd Length: 522  Bit Score: 758.13  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114619479   36 IDLNKVKTKTAAKYGLSAQPRLVDIIAAVPPQYRKVLIPKLKAKPIRTASGIAVVAVMCKPHRCPHISftgniCVYCPGG 115
Cdd:TIGR01211  15 EDLEDLKLEVSRKYGLSKVPSNSEILNSAPDEEKKKLEPILRKKPVRTISGVAVVAVMTSPHRCPHGK-----CLYCPGG 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114619479  116 PDSdfEYSTQSYTGYEPTSMRAIRARYDPFLQTRHRIEQLKQLGHSVDKVEFIVMGGTFMALPEEYRDYFIRNLHDALSG 195
Cdd:TIGR01211  90 PDS--ENSPQSYTGYEPAAMRGRQNDYDPYEQVTARLEQLEQIGHPVDKVELIIMGGTFPARDLDYQEWFIKRCLNAMNG 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114619479  196 HTS-----NNIYEAVKYSERSLTKCIGITIETRPDYCMKRHLSDMLTYGCTRLEIGVQSVYEDVARDTNRGHTVKAVCES 270
Cdd:TIGR01211 168 FDQelkgnSTLEEAIRINETSKHRCVGLTIETRPDYCREEHIDRMLKLGATRVELGVQTIYNDILERTKRGHTVRDVVEA 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114619479  271 FHLAKDSGFKVVAHMMPDLPNVGLERDIEQFTEFFENPAFRPDGLKLYPTLVIRGTGLYELWKSGRYKSYSPSDLVELVA 350
Cdd:TIGR01211 248 TRLLRDAGLKVVYHIMPGLPGSSFERDLEMFREIFEDPRFKPDMLKIYPTLVTRGTELYELWKRGEYKPYTTEEAVELIV 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114619479  351 RILALVPPWTRVYRVQRDIPMPLVSSGVEHGNLRELALARMKDLGIQCRDVRTREVGIQEIHHKVRPY-QVELVRRDYVA 429
Cdd:TIGR01211 328 EIKRMMPKWVRIQRIQRDIPAPLIVAGVKKSNLRELVYRRMKEHGITCRCIRCREVGHQMVKPVQPEEeNVELIVEEYAA 407
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114619479  430 NGGWETFLSYEDPDQDILIGLLRLRKCSEETFRfELGGGVSIVRELHVYGSVVPVSSRDPTKFQHQGFGMLLMeEAERIA 509
Cdd:TIGR01211 408 SGGTEFFLSYEDPKNDILIGFLRLRFPSEPAHR-KEVDATALVRELHVYGSEVPIGERGDDEWQHRGYGRRLL-EEAERI 485
                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 114619479  510 REEHGSGKIAVISGVGTRNYYRKIGYRLQGPYMVKML 546
Cdd:TIGR01211 486 AAEEGSEKILVISGIGVREYYRKLGYELDGPYMSKRL 522
 
Name Accession Description Interval E-value
ELP3 TIGR01211
radical SAM enzyme/protein acetyltransferase, ELP3 family; This family includes elongator ...
36-546 0e+00

radical SAM enzyme/protein acetyltransferase, ELP3 family; This family includes elongator complex protein 3 (ELP3) from eukaryotes and related proteins from other lineages. ELP3 is a component of the RNA polymerase II holoenzyme. It has an N-terminal radical SAM domain and C-terminal GNAT acetyltransferase domain. Members of this family are found in eukaryotes, archaea, and a few bacteria (e.g. Atopobium sp). The activity discovered first was an acetyltransferase modification at the N-termini of all four core histones, shown in vitro in eukaryotes. More recently, the radical SAM domain was shown to play a role in zygotic paternal genome demethylation. Family TIGR01212, widespread in prokaryotes, lacks the GNAT acetyltransferase domain but shares extensive sequence similarity with this family (TIGR01211). [Transcription, DNA-dependent RNA polymerase]


Pssm-ID: 273503 [Multi-domain]  Cd Length: 522  Bit Score: 758.13  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114619479   36 IDLNKVKTKTAAKYGLSAQPRLVDIIAAVPPQYRKVLIPKLKAKPIRTASGIAVVAVMCKPHRCPHISftgniCVYCPGG 115
Cdd:TIGR01211  15 EDLEDLKLEVSRKYGLSKVPSNSEILNSAPDEEKKKLEPILRKKPVRTISGVAVVAVMTSPHRCPHGK-----CLYCPGG 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114619479  116 PDSdfEYSTQSYTGYEPTSMRAIRARYDPFLQTRHRIEQLKQLGHSVDKVEFIVMGGTFMALPEEYRDYFIRNLHDALSG 195
Cdd:TIGR01211  90 PDS--ENSPQSYTGYEPAAMRGRQNDYDPYEQVTARLEQLEQIGHPVDKVELIIMGGTFPARDLDYQEWFIKRCLNAMNG 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114619479  196 HTS-----NNIYEAVKYSERSLTKCIGITIETRPDYCMKRHLSDMLTYGCTRLEIGVQSVYEDVARDTNRGHTVKAVCES 270
Cdd:TIGR01211 168 FDQelkgnSTLEEAIRINETSKHRCVGLTIETRPDYCREEHIDRMLKLGATRVELGVQTIYNDILERTKRGHTVRDVVEA 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114619479  271 FHLAKDSGFKVVAHMMPDLPNVGLERDIEQFTEFFENPAFRPDGLKLYPTLVIRGTGLYELWKSGRYKSYSPSDLVELVA 350
Cdd:TIGR01211 248 TRLLRDAGLKVVYHIMPGLPGSSFERDLEMFREIFEDPRFKPDMLKIYPTLVTRGTELYELWKRGEYKPYTTEEAVELIV 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114619479  351 RILALVPPWTRVYRVQRDIPMPLVSSGVEHGNLRELALARMKDLGIQCRDVRTREVGIQEIHHKVRPY-QVELVRRDYVA 429
Cdd:TIGR01211 328 EIKRMMPKWVRIQRIQRDIPAPLIVAGVKKSNLRELVYRRMKEHGITCRCIRCREVGHQMVKPVQPEEeNVELIVEEYAA 407
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114619479  430 NGGWETFLSYEDPDQDILIGLLRLRKCSEETFRfELGGGVSIVRELHVYGSVVPVSSRDPTKFQHQGFGMLLMeEAERIA 509
Cdd:TIGR01211 408 SGGTEFFLSYEDPKNDILIGFLRLRFPSEPAHR-KEVDATALVRELHVYGSEVPIGERGDDEWQHRGYGRRLL-EEAERI 485
                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 114619479  510 REEHGSGKIAVISGVGTRNYYRKIGYRLQGPYMVKML 546
Cdd:TIGR01211 486 AAEEGSEKILVISGIGVREYYRKLGYELDGPYMSKRL 522
ELP3 COG1243
Histone acetyltransferase, component of the RNA polymerase elongator complex [Transcription, ...
34-546 0e+00

Histone acetyltransferase, component of the RNA polymerase elongator complex [Transcription, Chromatin structure and dynamics];


Pssm-ID: 224164 [Multi-domain]  Cd Length: 515  Bit Score: 743.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114619479  34 KDIDLNKVKTKTAAKYGLSAQPRLVDIIAAVPPQYRkvLIPKLKAKPIRTASGIAVVAVMCKPHRCPHisftgNICVYCP 113
Cdd:COG1243   14 KKKELEDLKLEVSRKYGLSKVPRNSDILNAAPPEER--LREILRRKPVRTISGVAVVAVMTSPHGCPH-----GRCVFCP 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114619479 114 GGPDsdfEYSTQSYTGYEPTSMRAIRARYDPFLQTRHRIEQLKQLGHSVDKVEFIVMGGTFMALPEEYRDYFIRNLHDAL 193
Cdd:COG1243   87 GGPD---KDSPQSYTGEEPAALRAIKNRYDPYEQVRARLKQLETIGHTSDKVELIIMGGTFTALSLEYQEWFLKVALKAM 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114619479 194 SGHtSNNIYEAVKYSERSLTKCIGITIETRPDYCMKRHLSDMLTYGCTRLEIGVQSVYEDVARDTNRGHTVKAVCESFHL 273
Cdd:COG1243  164 NDF-GYDLEEAQRKNETAELRCVGITIETRPDYIDEEHLDQMLKYGVTRVELGVQSIYDDVLERTKRGHTVEDVVEATRL 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114619479 274 AKDSGFKVVAHMMPDLPNVGLERDIEQFTEFFENPAFRPDGLKLYPTLVIRGTGLYELWKSGRYKSYSPSDLVELVARIL 353
Cdd:COG1243  243 LKDAGFKVGYHIMPGLPGSDFERDLESFREIFEDPRFRPDMLKIYPTLVIEGTELYEMWKRGLYKPYTTEEAVELIVEIY 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114619479 354 ALVPPWTRVYRVQRDIPMPLVSSGVEHGNLRELALARMKDLGIQCRDVRTREVGIQEIHHKVRPY--QVELVRRDYVANG 431
Cdd:COG1243  323 RLEPKWVRVIRIQRDIPAELIVDGVKKSNLRELVENRMREEGIKCRCIRCREVGIVVVKNVVIPPveQILLKREEYEASG 402
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114619479 432 GWETFLSYEDPDQDILIGLLRLRKCSEETFRFELGGGVSIVRELHVYGSVVPVSSRdPTKFQHQGFGMLLMEEAERIARE 511
Cdd:COG1243  403 GTEIFLSYEDPKNDILIGFLRLREPSEGAHREEIDDKTAIVRELHVYGSEVPIGKR-EDEWQHRGYGRELLEEAERIARE 481
                        490       500       510
                 ....*....|....*....|....*....|....*
gi 114619479 512 EHgSGKIAVISGVGTRNYYRKIGYRLQGPYMVKML 546
Cdd:COG1243  482 EG-AKKILVISGIGVREYYRKLGYELDGPYMSKRL 515
Radical_SAM_C pfam16199
Radical_SAM C-terminal domain; This domain is found as a C-terminal extension to a subset of ...
312-390 6.25e-27

Radical_SAM C-terminal domain; This domain is found as a C-terminal extension to a subset of Radical_SAM domains. It is found in archaeal, bacterial, fungal, plant and human proteins.


Pssm-ID: 435209 [Multi-domain]  Cd Length: 83  Bit Score: 104.01  E-value: 6.25e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114619479  312 PDGLKLYPTLVIRGTGLYELWKSGRYKSYSPSDLVELVARILALVPPWTRVYRVQRDIPMPLVSSGVEHG-NLRELALAR 390
Cdd:pfam16199   1 PDGVKIHPLLVLKGTPLAELYERGEYKPLSLEEYVELVADFLELLPPDIVIHRLGGDAPKELLVAPPWHLpKLRVLNLIE 80
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
89-349 5.02e-24

Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, coproporphyrinogen III oxidase, biotin synthase and MiaB families, and includes a representative in the eukaryotic elongator subunit, Elp-3. Some members of the family are methyltransferases.


Pssm-ID: 214792 [Multi-domain]  Cd Length: 216  Bit Score: 100.17  E-value: 5.02e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114619479    89 VVAVMCKPHRCPHIsftgniCVYCpggpdsdfeystqsytgYEPTSMRAIRARYdpfLQTRHR-IEQLKQLGHSVDKVEF 167
Cdd:smart00729   1 PLALYIITRGCPRR------CTFC-----------------SFPSLRGKLRSRY---LEALVReIELLAEKGEKEGLVGT 54
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114619479   168 IVM-GGTFMALPEEYRDYFIRNLHDALSghtsnniyeavkysersLTKCIGITIETRPDYCMKRHLSDMLTYGCTRLEIG 246
Cdd:smart00729  55 VFIgGGTPTLLSPEQLEELLEAIREILG-----------------LAKDVEITIETRPDTLTEELLEALKEAGVNRVSLG 117
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114619479   247 VQSVYEDVARDTNRGHTVKAVCESFHLAKDSGF-KVVAHMMPDLPNVGLErDIEQFTEFFEnpAFRPDGLKLYPTLVIRG 325
Cdd:smart00729 118 VQSGDDEVLKAINRGHTVEDVLEAVELLREAGPiKVSTDLIVGLPGETEE-DFEETLKLLK--ELGPDRVSIFPLSPRPG 194
                          250       260
                   ....*....|....*....|....
gi 114619479   326 TGLYELWKsgRYKSYSPSDLVELV 349
Cdd:smart00729 195 TPLAKMYK--RLKPPTKEERAELL 216
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
96-340 3.82e-14

Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S cluster and S-adenosylmethionine (SAM) in close proximity. They are characterized by a conserved CxxxCxxC motif, which coordinates the conserved iron-sulfur cluster. Mechanistically, they share the transfer of a single electron from the iron-sulfur cluster to SAM, which leads to its reductive cleavage to methionine and a 5'-deoxyadenosyl radical, which, in turn, abstracts a hydrogen from the appropriately positioned carbon atom. Depending on the enzyme, SAM is consumed during this process or it is restored and reused. Radical SAM enzymes catalyze steps in metabolism, DNA repair, the biosynthesis of vitamins and coenzymes, and the biosynthesis of many antibiotics. Examples are biotin synthase (BioB), lipoyl synthase (LipA), pyruvate formate-lyase (PFL), coproporphyrinogen oxidase (HemN), lysine 2,3-aminomutase (LAM), anaerobic ribonucleotide reductase (ARR), and MoaA, an enzyme of the biosynthesis of molybdopterin.


Pssm-ID: 100105 [Multi-domain]  Cd Length: 204  Bit Score: 71.21  E-value: 3.82e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114619479  96 PHRCPHIsftgniCVYCPGGPDSDFEystqsytgyeptsmrairaryDPFLQTRHRIEQLKQLGHSVDKVEFIVMGGTFM 175
Cdd:cd01335    4 TRGCNLN------CGFCSNPASKGRG---------------------PESPPEIEEILDIVLEAKERGVEVVILTGGEPL 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114619479 176 ALPeeYRDYFIRNLHDALSGHTsnniyeavkysersltkcigITIETRPDYCMKRHLSDMLTYGCTRLEIGVQSVYEDVA 255
Cdd:cd01335   57 LYP--ELAELLRRLKKELPGFE--------------------ISIETNGTLLTEELLKELKELGLDGVGVSLDSGDEEVA 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114619479 256 RDTN-RGHTVKAVCESFHLAKDSGFKVVAHMMPDLPNVGLERDIEQFteFFENPAFRPDGLKLYPTLVIRGTGLYELWKS 334
Cdd:cd01335  115 DKIRgSGESFKERLEALKELREAGLGLSTTLLVGLGDEDEEDDLEEL--ELLAEFRSPDRVSLFRLLPEEGTPLELAAPV 192

                 ....*.
gi 114619479 335 GRYKSY 340
Cdd:cd01335  193 VPAEKL 198
PRK08207 PRK08207
coproporphyrinogen III oxidase; Provisional
109-352 2.15e-08

coproporphyrinogen III oxidase; Provisional


Pssm-ID: 236187 [Multi-domain]  Cd Length: 488  Bit Score: 56.43  E-value: 2.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114619479 109 CVYCpggpdsdfeystqSYTGYEptsMRAIRARYDPFLQTRHR-IEQ----LKQLGHSVDKVEFivMGGTFMALPEEYRD 183
Cdd:PRK08207 177 CLYC-------------SFPSYP---IKGYKGLVEPYLEALHYeIEEigkyLKEKGLKITTIYF--GGGTPTSLTAEELE 238
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114619479 184 YFIRNLHDALSGhtSNNIYEavkysersltkcigITIET-RPDYCMKRHLSDMLTYGCTRLEIGVQSVYEDVARDTNRGH 262
Cdd:PRK08207 239 RLLEEIYENFPD--VKNVKE--------------FTVEAgRPDTITEEKLEVLKKYGVDRISINPQTMNDETLKAIGRHH 302
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114619479 263 TVKAVCESFHLAKDSGFKVVaHMmpD----LPNVGLE------RDIEQfteffenpaFRPDGLKLYpTLVI-RGTGLYEL 331
Cdd:PRK08207 303 TVEDIIEKFHLAREMGFDNI-NM--DliigLPGEGLEevkhtlEEIEK---------LNPESLTVH-TLAIkRASRLTEN 369
                        250       260
                 ....*....|....*....|.
gi 114619479 332 WKsgRYKSYSPSDLVELVARI 352
Cdd:PRK08207 370 KE--KYKVADREEIEKMMEEA 388
 
Name Accession Description Interval E-value
ELP3 TIGR01211
radical SAM enzyme/protein acetyltransferase, ELP3 family; This family includes elongator ...
36-546 0e+00

radical SAM enzyme/protein acetyltransferase, ELP3 family; This family includes elongator complex protein 3 (ELP3) from eukaryotes and related proteins from other lineages. ELP3 is a component of the RNA polymerase II holoenzyme. It has an N-terminal radical SAM domain and C-terminal GNAT acetyltransferase domain. Members of this family are found in eukaryotes, archaea, and a few bacteria (e.g. Atopobium sp). The activity discovered first was an acetyltransferase modification at the N-termini of all four core histones, shown in vitro in eukaryotes. More recently, the radical SAM domain was shown to play a role in zygotic paternal genome demethylation. Family TIGR01212, widespread in prokaryotes, lacks the GNAT acetyltransferase domain but shares extensive sequence similarity with this family (TIGR01211). [Transcription, DNA-dependent RNA polymerase]


Pssm-ID: 273503 [Multi-domain]  Cd Length: 522  Bit Score: 758.13  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114619479   36 IDLNKVKTKTAAKYGLSAQPRLVDIIAAVPPQYRKVLIPKLKAKPIRTASGIAVVAVMCKPHRCPHISftgniCVYCPGG 115
Cdd:TIGR01211  15 EDLEDLKLEVSRKYGLSKVPSNSEILNSAPDEEKKKLEPILRKKPVRTISGVAVVAVMTSPHRCPHGK-----CLYCPGG 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114619479  116 PDSdfEYSTQSYTGYEPTSMRAIRARYDPFLQTRHRIEQLKQLGHSVDKVEFIVMGGTFMALPEEYRDYFIRNLHDALSG 195
Cdd:TIGR01211  90 PDS--ENSPQSYTGYEPAAMRGRQNDYDPYEQVTARLEQLEQIGHPVDKVELIIMGGTFPARDLDYQEWFIKRCLNAMNG 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114619479  196 HTS-----NNIYEAVKYSERSLTKCIGITIETRPDYCMKRHLSDMLTYGCTRLEIGVQSVYEDVARDTNRGHTVKAVCES 270
Cdd:TIGR01211 168 FDQelkgnSTLEEAIRINETSKHRCVGLTIETRPDYCREEHIDRMLKLGATRVELGVQTIYNDILERTKRGHTVRDVVEA 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114619479  271 FHLAKDSGFKVVAHMMPDLPNVGLERDIEQFTEFFENPAFRPDGLKLYPTLVIRGTGLYELWKSGRYKSYSPSDLVELVA 350
Cdd:TIGR01211 248 TRLLRDAGLKVVYHIMPGLPGSSFERDLEMFREIFEDPRFKPDMLKIYPTLVTRGTELYELWKRGEYKPYTTEEAVELIV 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114619479  351 RILALVPPWTRVYRVQRDIPMPLVSSGVEHGNLRELALARMKDLGIQCRDVRTREVGIQEIHHKVRPY-QVELVRRDYVA 429
Cdd:TIGR01211 328 EIKRMMPKWVRIQRIQRDIPAPLIVAGVKKSNLRELVYRRMKEHGITCRCIRCREVGHQMVKPVQPEEeNVELIVEEYAA 407
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114619479  430 NGGWETFLSYEDPDQDILIGLLRLRKCSEETFRfELGGGVSIVRELHVYGSVVPVSSRDPTKFQHQGFGMLLMeEAERIA 509
Cdd:TIGR01211 408 SGGTEFFLSYEDPKNDILIGFLRLRFPSEPAHR-KEVDATALVRELHVYGSEVPIGERGDDEWQHRGYGRRLL-EEAERI 485
                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 114619479  510 REEHGSGKIAVISGVGTRNYYRKIGYRLQGPYMVKML 546
Cdd:TIGR01211 486 AAEEGSEKILVISGIGVREYYRKLGYELDGPYMSKRL 522
ELP3 COG1243
Histone acetyltransferase, component of the RNA polymerase elongator complex [Transcription, ...
34-546 0e+00

Histone acetyltransferase, component of the RNA polymerase elongator complex [Transcription, Chromatin structure and dynamics];


Pssm-ID: 224164 [Multi-domain]  Cd Length: 515  Bit Score: 743.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114619479  34 KDIDLNKVKTKTAAKYGLSAQPRLVDIIAAVPPQYRkvLIPKLKAKPIRTASGIAVVAVMCKPHRCPHisftgNICVYCP 113
Cdd:COG1243   14 KKKELEDLKLEVSRKYGLSKVPRNSDILNAAPPEER--LREILRRKPVRTISGVAVVAVMTSPHGCPH-----GRCVFCP 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114619479 114 GGPDsdfEYSTQSYTGYEPTSMRAIRARYDPFLQTRHRIEQLKQLGHSVDKVEFIVMGGTFMALPEEYRDYFIRNLHDAL 193
Cdd:COG1243   87 GGPD---KDSPQSYTGEEPAALRAIKNRYDPYEQVRARLKQLETIGHTSDKVELIIMGGTFTALSLEYQEWFLKVALKAM 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114619479 194 SGHtSNNIYEAVKYSERSLTKCIGITIETRPDYCMKRHLSDMLTYGCTRLEIGVQSVYEDVARDTNRGHTVKAVCESFHL 273
Cdd:COG1243  164 NDF-GYDLEEAQRKNETAELRCVGITIETRPDYIDEEHLDQMLKYGVTRVELGVQSIYDDVLERTKRGHTVEDVVEATRL 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114619479 274 AKDSGFKVVAHMMPDLPNVGLERDIEQFTEFFENPAFRPDGLKLYPTLVIRGTGLYELWKSGRYKSYSPSDLVELVARIL 353
Cdd:COG1243  243 LKDAGFKVGYHIMPGLPGSDFERDLESFREIFEDPRFRPDMLKIYPTLVIEGTELYEMWKRGLYKPYTTEEAVELIVEIY 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114619479 354 ALVPPWTRVYRVQRDIPMPLVSSGVEHGNLRELALARMKDLGIQCRDVRTREVGIQEIHHKVRPY--QVELVRRDYVANG 431
Cdd:COG1243  323 RLEPKWVRVIRIQRDIPAELIVDGVKKSNLRELVENRMREEGIKCRCIRCREVGIVVVKNVVIPPveQILLKREEYEASG 402
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114619479 432 GWETFLSYEDPDQDILIGLLRLRKCSEETFRFELGGGVSIVRELHVYGSVVPVSSRdPTKFQHQGFGMLLMEEAERIARE 511
Cdd:COG1243  403 GTEIFLSYEDPKNDILIGFLRLREPSEGAHREEIDDKTAIVRELHVYGSEVPIGKR-EDEWQHRGYGRELLEEAERIARE 481
                        490       500       510
                 ....*....|....*....|....*....|....*
gi 114619479 512 EHgSGKIAVISGVGTRNYYRKIGYRLQGPYMVKML 546
Cdd:COG1243  482 EG-AKKILVISGIGVREYYRKLGYELDGPYMSKRL 515
Radical_SAM_C pfam16199
Radical_SAM C-terminal domain; This domain is found as a C-terminal extension to a subset of ...
312-390 6.25e-27

Radical_SAM C-terminal domain; This domain is found as a C-terminal extension to a subset of Radical_SAM domains. It is found in archaeal, bacterial, fungal, plant and human proteins.


Pssm-ID: 435209 [Multi-domain]  Cd Length: 83  Bit Score: 104.01  E-value: 6.25e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114619479  312 PDGLKLYPTLVIRGTGLYELWKSGRYKSYSPSDLVELVARILALVPPWTRVYRVQRDIPMPLVSSGVEHG-NLRELALAR 390
Cdd:pfam16199   1 PDGVKIHPLLVLKGTPLAELYERGEYKPLSLEEYVELVADFLELLPPDIVIHRLGGDAPKELLVAPPWHLpKLRVLNLIE 80
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
89-349 5.02e-24

Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, coproporphyrinogen III oxidase, biotin synthase and MiaB families, and includes a representative in the eukaryotic elongator subunit, Elp-3. Some members of the family are methyltransferases.


Pssm-ID: 214792 [Multi-domain]  Cd Length: 216  Bit Score: 100.17  E-value: 5.02e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114619479    89 VVAVMCKPHRCPHIsftgniCVYCpggpdsdfeystqsytgYEPTSMRAIRARYdpfLQTRHR-IEQLKQLGHSVDKVEF 167
Cdd:smart00729   1 PLALYIITRGCPRR------CTFC-----------------SFPSLRGKLRSRY---LEALVReIELLAEKGEKEGLVGT 54
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114619479   168 IVM-GGTFMALPEEYRDYFIRNLHDALSghtsnniyeavkysersLTKCIGITIETRPDYCMKRHLSDMLTYGCTRLEIG 246
Cdd:smart00729  55 VFIgGGTPTLLSPEQLEELLEAIREILG-----------------LAKDVEITIETRPDTLTEELLEALKEAGVNRVSLG 117
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114619479   247 VQSVYEDVARDTNRGHTVKAVCESFHLAKDSGF-KVVAHMMPDLPNVGLErDIEQFTEFFEnpAFRPDGLKLYPTLVIRG 325
Cdd:smart00729 118 VQSGDDEVLKAINRGHTVEDVLEAVELLREAGPiKVSTDLIVGLPGETEE-DFEETLKLLK--ELGPDRVSIFPLSPRPG 194
                          250       260
                   ....*....|....*....|....
gi 114619479   326 TGLYELWKsgRYKSYSPSDLVELV 349
Cdd:smart00729 195 TPLAKMYK--RLKPPTKEERAELL 216
YhcC COG1242
Radical SAM superfamily enzyme [General function prediction only];
216-373 1.90e-20

Radical SAM superfamily enzyme [General function prediction only];


Pssm-ID: 224163 [Multi-domain]  Cd Length: 312  Bit Score: 92.00  E-value: 1.90e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114619479 216 IGITIETRPDyCMKRHLSDMLTYGCTR----LEIGVQSVYEDVARDTNRGHTVKAVCESFHLAKDSGFKVVAHMMPDLPN 291
Cdd:COG1242  116 VGLSIGTRPD-CLPDDVLDLLAEYNKRyevwVELGLQTAHDKTLKRINRGHDFACYVDAVKRLRKRGIKVCTHLINGLPG 194
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114619479 292 VGLERDIEQFTEFFENPAfrpDGLKLYPTLVIRGTGLYELWKSGRYKSYSPSDLVELVARILALVPPWTRVYRVQRDIPM 371
Cdd:COG1242  195 ETRDEMLETAKIVAELGV---DGIKLHPLHVVKGTPMEKMYEKGRLKFLSLEEYVELVCDQLEHLPPEVVIHRITGDAPR 271

                 ..
gi 114619479 372 PL 373
Cdd:COG1242  272 DT 273
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
96-340 3.82e-14

Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S cluster and S-adenosylmethionine (SAM) in close proximity. They are characterized by a conserved CxxxCxxC motif, which coordinates the conserved iron-sulfur cluster. Mechanistically, they share the transfer of a single electron from the iron-sulfur cluster to SAM, which leads to its reductive cleavage to methionine and a 5'-deoxyadenosyl radical, which, in turn, abstracts a hydrogen from the appropriately positioned carbon atom. Depending on the enzyme, SAM is consumed during this process or it is restored and reused. Radical SAM enzymes catalyze steps in metabolism, DNA repair, the biosynthesis of vitamins and coenzymes, and the biosynthesis of many antibiotics. Examples are biotin synthase (BioB), lipoyl synthase (LipA), pyruvate formate-lyase (PFL), coproporphyrinogen oxidase (HemN), lysine 2,3-aminomutase (LAM), anaerobic ribonucleotide reductase (ARR), and MoaA, an enzyme of the biosynthesis of molybdopterin.


Pssm-ID: 100105 [Multi-domain]  Cd Length: 204  Bit Score: 71.21  E-value: 3.82e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114619479  96 PHRCPHIsftgniCVYCPGGPDSDFEystqsytgyeptsmrairaryDPFLQTRHRIEQLKQLGHSVDKVEFIVMGGTFM 175
Cdd:cd01335    4 TRGCNLN------CGFCSNPASKGRG---------------------PESPPEIEEILDIVLEAKERGVEVVILTGGEPL 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114619479 176 ALPeeYRDYFIRNLHDALSGHTsnniyeavkysersltkcigITIETRPDYCMKRHLSDMLTYGCTRLEIGVQSVYEDVA 255
Cdd:cd01335   57 LYP--ELAELLRRLKKELPGFE--------------------ISIETNGTLLTEELLKELKELGLDGVGVSLDSGDEEVA 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114619479 256 RDTN-RGHTVKAVCESFHLAKDSGFKVVAHMMPDLPNVGLERDIEQFteFFENPAFRPDGLKLYPTLVIRGTGLYELWKS 334
Cdd:cd01335  115 DKIRgSGESFKERLEALKELREAGLGLSTTLLVGLGDEDEEDDLEEL--ELLAEFRSPDRVSLFRLLPEEGTPLELAAPV 192

                 ....*.
gi 114619479 335 GRYKSY 340
Cdd:cd01335  193 VPAEKL 198
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
136-301 2.46e-13

Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual methylations, isomerisation, sulphur insertion, ring formation, anaerobic oxidation and protein radical formation.


Pssm-ID: 427681 [Multi-domain]  Cd Length: 159  Bit Score: 67.94  E-value: 2.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114619479  136 RAIRARYDPFLQTRHRIEQLKQLGHSVDKVEFIVMGGTFMALPEEYRDYFIRNLHDALSGhtsnniyeavkysersltkc 215
Cdd:pfam04055  15 PSIRARGKGRELSPEEILEEAKELKRLGVEVVILGGGEPLLLPDLVELLERLLKLELAEG-------------------- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114619479  216 IGITIETRPDYCMKRHLSDMLTYGCTRLEIGVQSVYEDVARDTNRGHTVKAVCESFHLAKDSGFKVVAHMMPDLPNVGLE 295
Cdd:pfam04055  75 IRITLETNGTLLDEELLELLKEAGLDRVSIGLESGDDEVLKLINRGHTFEEVLEALELLREAGIPVVTDNIVGLPGETDE 154

                  ....*.
gi 114619479  296 rDIEQF 301
Cdd:pfam04055 155 -DLEET 159
HemN COG0635
Coproporphyrinogen III oxidase or related Fe-S oxidoreductase [Coenzyme transport and ...
101-348 3.36e-09

Coproporphyrinogen III oxidase or related Fe-S oxidoreductase [Coenzyme transport and metabolism];


Pssm-ID: 223708 [Multi-domain]  Cd Length: 416  Bit Score: 58.82  E-value: 3.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114619479 101 HISFTGNICVYCpggpdsDF-------EYSTQSYTGYEPTSMRAIRARYDPflqtRHRIEQLkqlghsvdkveFIVmGGT 173
Cdd:COG0635   40 HIPFCVSKCPYC------DFnshvtkrGQPVDEYLDALLEEIELVAALLGG----QREVKTI-----------YFG-GGT 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114619479 174 FMALPEEYRDYFIRNLHDALsghtsnniyeavkyseRSLTKCIGITIETRPDYCMKRHLSDMLTYGCTRLEIGVQSVYED 253
Cdd:COG0635   98 PSLLSPEQLERLLKALRELF----------------NDLDPDAEITIEANPGTVEAEKFKALKEAGVNRISLGVQSFNDE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114619479 254 VARDTNRGHTVKAVCESFHLAKDSGFK-VVAHMMPDLPN---VGLERDIEQFTEffenpaFRPDGLKLYPTLVIRGTGLY 329
Cdd:COG0635  162 VLKALGRIHDEEEAKEAVELARKAGFTsINIDLIYGLPGqtlESLKEDLEQALE------LGPDHLSLYSLAIEPGTKFA 235
                        250
                 ....*....|....*....
gi 114619479 330 ELWKSGRyksYSPSDLVEL 348
Cdd:COG0635  236 QRKIKGK---ALPDEDEKA 251
PRK08207 PRK08207
coproporphyrinogen III oxidase; Provisional
109-352 2.15e-08

coproporphyrinogen III oxidase; Provisional


Pssm-ID: 236187 [Multi-domain]  Cd Length: 488  Bit Score: 56.43  E-value: 2.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114619479 109 CVYCpggpdsdfeystqSYTGYEptsMRAIRARYDPFLQTRHR-IEQ----LKQLGHSVDKVEFivMGGTFMALPEEYRD 183
Cdd:PRK08207 177 CLYC-------------SFPSYP---IKGYKGLVEPYLEALHYeIEEigkyLKEKGLKITTIYF--GGGTPTSLTAEELE 238
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114619479 184 YFIRNLHDALSGhtSNNIYEavkysersltkcigITIET-RPDYCMKRHLSDMLTYGCTRLEIGVQSVYEDVARDTNRGH 262
Cdd:PRK08207 239 RLLEEIYENFPD--VKNVKE--------------FTVEAgRPDTITEEKLEVLKKYGVDRISINPQTMNDETLKAIGRHH 302
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114619479 263 TVKAVCESFHLAKDSGFKVVaHMmpD----LPNVGLE------RDIEQfteffenpaFRPDGLKLYpTLVI-RGTGLYEL 331
Cdd:PRK08207 303 TVEDIIEKFHLAREMGFDNI-NM--DliigLPGEGLEevkhtlEEIEK---------LNPESLTVH-TLAIkRASRLTEN 369
                        250       260
                 ....*....|....*....|.
gi 114619479 332 WKsgRYKSYSPSDLVELVARI 352
Cdd:PRK08207 370 KE--KYKVADREEIEKMMEEA 388
PRK08208 PRK08208
coproporphyrinogen III oxidase family protein;
152-340 8.87e-05

coproporphyrinogen III oxidase family protein;


Pssm-ID: 181292 [Multi-domain]  Cd Length: 430  Bit Score: 45.00  E-value: 8.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114619479 152 IEQLKQLGHSVDKVEF---IVMGGTFMALPEEYRDYFIRNLHDALSGHTSNniyeavkysersltkcIGITIETRPDYCM 228
Cdd:PRK08208  77 IRQAEQVAEALAPARFasfAVGGGTPTLLNAAELEKLFDSVERVLGVDLGN----------------IPKSVETSPATTT 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114619479 229 KRHLSDMLTYGCTRLEIGVQSVYEDVARDTNRGHTVKAVCESFHLAKDSGFkvvahmmPDLpNVGLERDIE-QFTEFFEN 307
Cdd:PRK08208 141 AEKLALLAARGVNRLSIGVQSFHDSELHALHRPQKRADVHQALEWIRAAGF-------PIL-NIDLIYGIPgQTHASWME 212
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 114619479 308 P-----AFRPDGLKLYPTLVIRGTGLYEL---WKSGRYKSY 340
Cdd:PRK08208 213 SldqalVYRPEELFLYPLYVRPLTGLGRRaraWDDQRLSLY 253
COG1244 COG1244
Uncharacterized Fe-S cluster-containing protein. MiaB family [General function prediction only] ...
155-338 5.41e-04

Uncharacterized Fe-S cluster-containing protein. MiaB family [General function prediction only];


Pssm-ID: 224165 [Multi-domain]  Cd Length: 358  Bit Score: 42.39  E-value: 5.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114619479 155 LKQLGHSVDKVEF--------IVMGGTF---MALPEEYRDYFIRNLHDalsghtSNNIYEAVkysersltkcigitIETR 223
Cdd:COG1244   85 INQFDEAYSKYEGkfdefvvkIFTSGSFldpEEVPREARRYILERISE------NDNVKEVV--------------VESR 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114619479 224 PDYCMKRHLSDMLTYGC---TRLEIGVQSVYEDVARDT-NRGHTVKAVCESFHLAKDSGFKVVAHMMPDLPNVGLERDIE 299
Cdd:COG1244  145 PEFIREERLEEITEILEgkiVEVAIGLETANDKIREDSiNKGFTFEDFVRAAEIIRNYGAKVKTYLLLKPPFLSEKEAIE 224
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 114619479 300 QFTEFFENPAFRPDGLKLYPTLVIRGTgLYE-LWKSGRYK 338
Cdd:COG1244  225 DVISSIVAAKPGTDTISINPTNVQKGT-LVEkLWRRGLYR 263
PRK05904 PRK05904
coproporphyrinogen III oxidase; Provisional
219-307 5.84e-03

coproporphyrinogen III oxidase; Provisional


Pssm-ID: 235641 [Multi-domain]  Cd Length: 353  Bit Score: 39.02  E-value: 5.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114619479 219 TIETRPDYCMKRHLSDMLTYGCTRLEIGVQSVYEDVARDTNRGHTVKAVCESFHLAKDSG-FKVVAHMMPDLPNVGLErD 297
Cdd:PRK05904  93 TIECNPELITQSQINLLKKNKVNRISLGVQSMNNNILKQLNRTHTIQDSKEAINLLHKNGiYNISCDFLYCLPILKLK-D 171
                         90
                 ....*....|
gi 114619479 298 IEQFTEFFEN 307
Cdd:PRK05904 172 LDEVFNFILK 181
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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