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Conserved domains on  [gi|68989265|ref|NP_001014344|]
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elongator complex protein 3 [Danio rerio]

Protein Classification

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 ...
37-547 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: 776.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265    37 INLNKVKTKTSAKYGLSAQPRLVDIIAAVPPHYRRALVPKLKAKPIRTASGIAVVAVMCKPHRCPHISftgniCVYCPGG 116
Cdd:TIGR01211  15 EDLEDLKLEVSRKYGLSKVPSNSEILNSAPDEEKKKLEPILRKKPVRTISGVAVVAVMTSPHRCPHGK-----CLYCPGG 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265   117 PDSdfEYSTQSYTGYEPTSMRAIRARYDPYLQTRHRVEQLKQLGHSVDKVEFIVMGGTFMALPEEYRDYFIRNLHDALSG 196
Cdd:TIGR01211  90 PDS--ENSPQSYTGYEPAAMRGRQNDYDPYEQVTARLEQLEQIGHPVDKVELIIMGGTFPARDLDYQEWFIKRCLNAMNG 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265   197 HTS-----NNVTEAVRYSERSNTKCVGITIETRPDYCLKRHLSDMLGYGCTRLEIGVQSVYEDVARDTNRGHTVRAVCES 271
Cdd:TIGR01211 168 FDQelkgnSTLEEAIRINETSKHRCVGLTIETRPDYCREEHIDRMLKLGATRVELGVQTIYNDILERTKRGHTVRDVVEA 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265   272 FHLAKDAGFKVVAHMMPDLPNVGMERDVEQFIEFFENPAFRPDGLKLYPTLVIRGTGLYELWKTGRYKSYSPSALVDLVA 351
Cdd:TIGR01211 248 TRLLRDAGLKVVYHIMPGLPGSSFERDLEMFREIFEDPRFKPDMLKIYPTLVTRGTELYELWKRGEYKPYTTEEAVELIV 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265   352 RILALVPPWTRVYRVQRDIPMPLVSSGVEHGNLRELALARMKDMGTECRDVRTREVGIQEIHHKVRPY-QVELIRRDYVA 430
Cdd:TIGR01211 328 EIKRMMPKWVRIQRIQRDIPAPLIVAGVKKSNLRELVYRRMKEHGITCRCIRCREVGHQMVKPVQPEEeNVELIVEEYAA 407
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265   431 NGGWETFLSYEDPEQDILIGLLRLRRCSPQSFRPELKgGVSIVRELHVYGSVVPVSSRDPSKFQHQGFGMMLMEEAERIA 510
Cdd:TIGR01211 408 SGGTEFFLSYEDPKNDILIGFLRLRFPSEPAHRKEVD-ATALVRELHVYGSEVPIGERGDDEWQHRGYGRRLLEEAERIA 486
                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 68989265   511 RDEhGSSKLAVISGVGTRNYYRKMGYELEGPYMVKNL 547
Cdd:TIGR01211 487 AEE-GSEKILVISGIGVREYYRKLGYELDGPYMSKRL 522
 
Name Accession Description Interval E-value
ELP3 TIGR01211
radical SAM enzyme/protein acetyltransferase, ELP3 family; This family includes elongator ...
37-547 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: 776.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265    37 INLNKVKTKTSAKYGLSAQPRLVDIIAAVPPHYRRALVPKLKAKPIRTASGIAVVAVMCKPHRCPHISftgniCVYCPGG 116
Cdd:TIGR01211  15 EDLEDLKLEVSRKYGLSKVPSNSEILNSAPDEEKKKLEPILRKKPVRTISGVAVVAVMTSPHRCPHGK-----CLYCPGG 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265   117 PDSdfEYSTQSYTGYEPTSMRAIRARYDPYLQTRHRVEQLKQLGHSVDKVEFIVMGGTFMALPEEYRDYFIRNLHDALSG 196
Cdd:TIGR01211  90 PDS--ENSPQSYTGYEPAAMRGRQNDYDPYEQVTARLEQLEQIGHPVDKVELIIMGGTFPARDLDYQEWFIKRCLNAMNG 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265   197 HTS-----NNVTEAVRYSERSNTKCVGITIETRPDYCLKRHLSDMLGYGCTRLEIGVQSVYEDVARDTNRGHTVRAVCES 271
Cdd:TIGR01211 168 FDQelkgnSTLEEAIRINETSKHRCVGLTIETRPDYCREEHIDRMLKLGATRVELGVQTIYNDILERTKRGHTVRDVVEA 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265   272 FHLAKDAGFKVVAHMMPDLPNVGMERDVEQFIEFFENPAFRPDGLKLYPTLVIRGTGLYELWKTGRYKSYSPSALVDLVA 351
Cdd:TIGR01211 248 TRLLRDAGLKVVYHIMPGLPGSSFERDLEMFREIFEDPRFKPDMLKIYPTLVTRGTELYELWKRGEYKPYTTEEAVELIV 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265   352 RILALVPPWTRVYRVQRDIPMPLVSSGVEHGNLRELALARMKDMGTECRDVRTREVGIQEIHHKVRPY-QVELIRRDYVA 430
Cdd:TIGR01211 328 EIKRMMPKWVRIQRIQRDIPAPLIVAGVKKSNLRELVYRRMKEHGITCRCIRCREVGHQMVKPVQPEEeNVELIVEEYAA 407
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265   431 NGGWETFLSYEDPEQDILIGLLRLRRCSPQSFRPELKgGVSIVRELHVYGSVVPVSSRDPSKFQHQGFGMMLMEEAERIA 510
Cdd:TIGR01211 408 SGGTEFFLSYEDPKNDILIGFLRLRFPSEPAHRKEVD-ATALVRELHVYGSEVPIGERGDDEWQHRGYGRRLLEEAERIA 486
                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 68989265   511 RDEhGSSKLAVISGVGTRNYYRKMGYELEGPYMVKNL 547
Cdd:TIGR01211 487 AEE-GSEKILVISGIGVREYYRKLGYELDGPYMSKRL 522
ELP3 COG1243
Histone acetyltransferase, component of the RNA polymerase elongator complex [Transcription, ...
20-547 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: 768.06  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265  20 IADVIKQLVEAheEGKDINLNKVKTKTSAKYGLSAQPRLVDIIAAVPPHYRraLVPKLKAKPIRTASGIAVVAVMCKPHR 99
Cdd:COG1243   1 CEEIVEELLSG--EIKKKELEDLKLEVSRKYGLSKVPRNSDILNAAPPEER--LREILRRKPVRTISGVAVVAVMTSPHG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265 100 CPHisftgNICVYCPGGPDsdfEYSTQSYTGYEPTSMRAIRARYDPYLQTRHRVEQLKQLGHSVDKVEFIVMGGTFMALP 179
Cdd:COG1243  77 CPH-----GRCVFCPGGPD---KDSPQSYTGEEPAALRAIKNRYDPYEQVRARLKQLETIGHTSDKVELIIMGGTFTALS 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265 180 EEYRDYFIRNLHDALSGHtSNNVTEAVRYSERSNTKCVGITIETRPDYCLKRHLSDMLGYGCTRLEIGVQSVYEDVARDT 259
Cdd:COG1243 149 LEYQEWFLKVALKAMNDF-GYDLEEAQRKNETAELRCVGITIETRPDYIDEEHLDQMLKYGVTRVELGVQSIYDDVLERT 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265 260 NRGHTVRAVCESFHLAKDAGFKVVAHMMPDLPNVGMERDVEQFIEFFENPAFRPDGLKLYPTLVIRGTGLYELWKTGRYK 339
Cdd:COG1243 228 KRGHTVEDVVEATRLLKDAGFKVGYHIMPGLPGSDFERDLESFREIFEDPRFRPDMLKIYPTLVIEGTELYEMWKRGLYK 307
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265 340 SYSPSALVDLVARILALVPPWTRVYRVQRDIPMPLVSSGVEHGNLRELALARMKDMGTECRDVRTREVGIQEIHHKVRPY 419
Cdd:COG1243 308 PYTTEEAVELIVEIYRLEPKWVRVIRIQRDIPAELIVDGVKKSNLRELVENRMREEGIKCRCIRCREVGIVVVKNVVIPP 387
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265 420 --QVELIRRDYVANGGWETFLSYEDPEQDILIGLLRLRRCSPQSFRPELKGGVSIVRELHVYGSVVPVSSRdPSKFQHQG 497
Cdd:COG1243 388 veQILLKREEYEASGGTEIFLSYEDPKNDILIGFLRLREPSEGAHREEIDDKTAIVRELHVYGSEVPIGKR-EDEWQHRG 466
                       490       500       510       520       530
                ....*....|....*....|....*....|....*....|....*....|
gi 68989265 498 FGMMLMEEAERIARDEHgSSKLAVISGVGTRNYYRKMGYELEGPYMVKNL 547
Cdd:COG1243 467 YGRELLEEAERIAREEG-AKKILVISGIGVREYYRKLGYELDGPYMSKRL 515
Radical_SAM_C pfam16199
Radical_SAM C-terminal domain; This domain is found as a C-terminal extension to a subset of ...
313-391 2.54e-26

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: 406581 [Multi-domain]  Cd Length: 83  Bit Score: 102.09  E-value: 2.54e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265   313 PDGLKLYPTLVIRGTGLYELWKTGRYKSYSPSALVDLVARILALVPPWTRVYRVQRDIPMPLVSSGVEHG-NLRELALAR 391
Cdd:pfam16199   1 PDGVKIHPLLVLKGTPLAELYERGEYKPLSLEEYVELVADFLELLPPDIVIHRLGGDAPKELLVAPPWHLpKLRVLNLIE 80
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
90-350 3.23e-25

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: 103.64  E-value: 3.23e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265     90 VVAVMCKPHRCPHIsftgniCVYCPGGPDSdfeystqsytgyeptsmraiRARYDPYLQTRHR-VEQLKQLGHSVDKVEF 168
Cdd:smart00729   1 PLALYIITRGCPRR------CTFCSFPSLR--------------------GKLRSRYLEALVReIELLAEKGEKEGLVGT 54
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265    169 IVM-GGTFMALPEEYRDYFIRNLHDALSGHtsnnvteavrysersntKCVGITIETRPDYCLKRHLSDMLGYGCTRLEIG 247
Cdd:smart00729  55 VFIgGGTPTLLSPEQLEELLEAIREILGLA-----------------KDVEITIETRPDTLTEELLEALKEAGVNRVSLG 117
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265    248 VQSVYEDVARDTNRGHTVRAVCESFHLAKDAGF-KVVAHMMPDLPNVGMErDVEQFIEFFEnpAFRPDGLKLYPTLVIRG 326
Cdd:smart00729 118 VQSGDDEVLKAINRGHTVEDVLEAVELLREAGPiKVSTDLIVGLPGETEE-DFEETLKLLK--ELGPDRVSIFPLSPRPG 194
                          250       260
                   ....*....|....*....|....
gi 68989265    327 TGLYELWKtgRYKSYSPSALVDLV 350
Cdd:smart00729 195 TPLAKMYK--RLKPPTKEERAELL 216
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
97-334 1.37e-13

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: 69.67  E-value: 1.37e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265  97 PHRCPHIsftgniCVYCPGGPDSDFEystqsytgyeptsmrairaryDPYLQTRHRVEQLKQLGHSVDKVEFIVMGGTFM 176
Cdd:cd01335   4 TRGCNLN------CGFCSNPASKGRG---------------------PESPPEIEEILDIVLEAKERGVEVVILTGGEPL 56
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265 177 ALPeeYRDYFIRNLHDALSGHTsnnvteavrysersntkcvgITIETRPDYCLKRHLSDMLGYGCTRLEIGVQSVYEDVA 256
Cdd:cd01335  57 LYP--ELAELLRRLKKELPGFE--------------------ISIETNGTLLTEELLKELKELGLDGVGVSLDSGDEEVA 114
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 68989265 257 RDTN-RGHTVRAVCESFHLAKDAGFKVVAHMMPDLPNVGMERDVEQFieFFENPAFRPDGLKLYPTLVIRGTGLYELWK 334
Cdd:cd01335 115 DKIRgSGESFKERLEALKELREAGLGLSTTLLVGLGDEDEEDDLEEL--ELLAEFRSPDRVSLFRLLPEEGTPLELAAP 191
PRK08207 PRK08207
coproporphyrinogen III oxidase; Provisional
110-339 3.38e-08

coproporphyrinogen III oxidase; Provisional


Pssm-ID: 236187 [Multi-domain]  Cd Length: 488  Bit Score: 56.04  E-value: 3.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265  110 CVYCpggpdsdfeystqSYTGYEptsMRAIRARYDPYLQTRHR-----VEQLKQLGHSVDKVEFivMGGTFMALPEEYRD 184
Cdd:PRK08207 177 CLYC-------------SFPSYP---IKGYKGLVEPYLEALHYeieeiGKYLKEKGLKITTIYF--GGGTPTSLTAEELE 238
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265  185 YFIRNLHDALSGhtSNNVTEavrysersntkcvgITIET-RPDYCLKRHLSDMLGYGCTRLEIGVQSVYEDVARDTNRGH 263
Cdd:PRK08207 239 RLLEEIYENFPD--VKNVKE--------------FTVEAgRPDTITEEKLEVLKKYGVDRISINPQTMNDETLKAIGRHH 302
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265  264 TVRAVCESFHLAKDAGFKVVaHMmpD----LPNVGMErDVEQFIEFFEnpAFRPDGLKLYpTLVI-RGTGLYELWKtgRY 338
Cdd:PRK08207 303 TVEDIIEKFHLAREMGFDNI-NM--DliigLPGEGLE-EVKHTLEEIE--KLNPESLTVH-TLAIkRASRLTENKE--KY 373

                 .
gi 68989265  339 K 339
Cdd:PRK08207 374 K 374
 
Name Accession Description Interval E-value
ELP3 TIGR01211
radical SAM enzyme/protein acetyltransferase, ELP3 family; This family includes elongator ...
37-547 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: 776.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265    37 INLNKVKTKTSAKYGLSAQPRLVDIIAAVPPHYRRALVPKLKAKPIRTASGIAVVAVMCKPHRCPHISftgniCVYCPGG 116
Cdd:TIGR01211  15 EDLEDLKLEVSRKYGLSKVPSNSEILNSAPDEEKKKLEPILRKKPVRTISGVAVVAVMTSPHRCPHGK-----CLYCPGG 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265   117 PDSdfEYSTQSYTGYEPTSMRAIRARYDPYLQTRHRVEQLKQLGHSVDKVEFIVMGGTFMALPEEYRDYFIRNLHDALSG 196
Cdd:TIGR01211  90 PDS--ENSPQSYTGYEPAAMRGRQNDYDPYEQVTARLEQLEQIGHPVDKVELIIMGGTFPARDLDYQEWFIKRCLNAMNG 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265   197 HTS-----NNVTEAVRYSERSNTKCVGITIETRPDYCLKRHLSDMLGYGCTRLEIGVQSVYEDVARDTNRGHTVRAVCES 271
Cdd:TIGR01211 168 FDQelkgnSTLEEAIRINETSKHRCVGLTIETRPDYCREEHIDRMLKLGATRVELGVQTIYNDILERTKRGHTVRDVVEA 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265   272 FHLAKDAGFKVVAHMMPDLPNVGMERDVEQFIEFFENPAFRPDGLKLYPTLVIRGTGLYELWKTGRYKSYSPSALVDLVA 351
Cdd:TIGR01211 248 TRLLRDAGLKVVYHIMPGLPGSSFERDLEMFREIFEDPRFKPDMLKIYPTLVTRGTELYELWKRGEYKPYTTEEAVELIV 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265   352 RILALVPPWTRVYRVQRDIPMPLVSSGVEHGNLRELALARMKDMGTECRDVRTREVGIQEIHHKVRPY-QVELIRRDYVA 430
Cdd:TIGR01211 328 EIKRMMPKWVRIQRIQRDIPAPLIVAGVKKSNLRELVYRRMKEHGITCRCIRCREVGHQMVKPVQPEEeNVELIVEEYAA 407
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265   431 NGGWETFLSYEDPEQDILIGLLRLRRCSPQSFRPELKgGVSIVRELHVYGSVVPVSSRDPSKFQHQGFGMMLMEEAERIA 510
Cdd:TIGR01211 408 SGGTEFFLSYEDPKNDILIGFLRLRFPSEPAHRKEVD-ATALVRELHVYGSEVPIGERGDDEWQHRGYGRRLLEEAERIA 486
                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 68989265   511 RDEhGSSKLAVISGVGTRNYYRKMGYELEGPYMVKNL 547
Cdd:TIGR01211 487 AEE-GSEKILVISGIGVREYYRKLGYELDGPYMSKRL 522
ELP3 COG1243
Histone acetyltransferase, component of the RNA polymerase elongator complex [Transcription, ...
20-547 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: 768.06  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265  20 IADVIKQLVEAheEGKDINLNKVKTKTSAKYGLSAQPRLVDIIAAVPPHYRraLVPKLKAKPIRTASGIAVVAVMCKPHR 99
Cdd:COG1243   1 CEEIVEELLSG--EIKKKELEDLKLEVSRKYGLSKVPRNSDILNAAPPEER--LREILRRKPVRTISGVAVVAVMTSPHG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265 100 CPHisftgNICVYCPGGPDsdfEYSTQSYTGYEPTSMRAIRARYDPYLQTRHRVEQLKQLGHSVDKVEFIVMGGTFMALP 179
Cdd:COG1243  77 CPH-----GRCVFCPGGPD---KDSPQSYTGEEPAALRAIKNRYDPYEQVRARLKQLETIGHTSDKVELIIMGGTFTALS 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265 180 EEYRDYFIRNLHDALSGHtSNNVTEAVRYSERSNTKCVGITIETRPDYCLKRHLSDMLGYGCTRLEIGVQSVYEDVARDT 259
Cdd:COG1243 149 LEYQEWFLKVALKAMNDF-GYDLEEAQRKNETAELRCVGITIETRPDYIDEEHLDQMLKYGVTRVELGVQSIYDDVLERT 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265 260 NRGHTVRAVCESFHLAKDAGFKVVAHMMPDLPNVGMERDVEQFIEFFENPAFRPDGLKLYPTLVIRGTGLYELWKTGRYK 339
Cdd:COG1243 228 KRGHTVEDVVEATRLLKDAGFKVGYHIMPGLPGSDFERDLESFREIFEDPRFRPDMLKIYPTLVIEGTELYEMWKRGLYK 307
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265 340 SYSPSALVDLVARILALVPPWTRVYRVQRDIPMPLVSSGVEHGNLRELALARMKDMGTECRDVRTREVGIQEIHHKVRPY 419
Cdd:COG1243 308 PYTTEEAVELIVEIYRLEPKWVRVIRIQRDIPAELIVDGVKKSNLRELVENRMREEGIKCRCIRCREVGIVVVKNVVIPP 387
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265 420 --QVELIRRDYVANGGWETFLSYEDPEQDILIGLLRLRRCSPQSFRPELKGGVSIVRELHVYGSVVPVSSRdPSKFQHQG 497
Cdd:COG1243 388 veQILLKREEYEASGGTEIFLSYEDPKNDILIGFLRLREPSEGAHREEIDDKTAIVRELHVYGSEVPIGKR-EDEWQHRG 466
                       490       500       510       520       530
                ....*....|....*....|....*....|....*....|....*....|
gi 68989265 498 FGMMLMEEAERIARDEHgSSKLAVISGVGTRNYYRKMGYELEGPYMVKNL 547
Cdd:COG1243 467 YGRELLEEAERIAREEG-AKKILVISGIGVREYYRKLGYELDGPYMSKRL 515
Radical_SAM_C pfam16199
Radical_SAM C-terminal domain; This domain is found as a C-terminal extension to a subset of ...
313-391 2.54e-26

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: 406581 [Multi-domain]  Cd Length: 83  Bit Score: 102.09  E-value: 2.54e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265   313 PDGLKLYPTLVIRGTGLYELWKTGRYKSYSPSALVDLVARILALVPPWTRVYRVQRDIPMPLVSSGVEHG-NLRELALAR 391
Cdd:pfam16199   1 PDGVKIHPLLVLKGTPLAELYERGEYKPLSLEEYVELVADFLELLPPDIVIHRLGGDAPKELLVAPPWHLpKLRVLNLIE 80
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
90-350 3.23e-25

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: 103.64  E-value: 3.23e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265     90 VVAVMCKPHRCPHIsftgniCVYCPGGPDSdfeystqsytgyeptsmraiRARYDPYLQTRHR-VEQLKQLGHSVDKVEF 168
Cdd:smart00729   1 PLALYIITRGCPRR------CTFCSFPSLR--------------------GKLRSRYLEALVReIELLAEKGEKEGLVGT 54
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265    169 IVM-GGTFMALPEEYRDYFIRNLHDALSGHtsnnvteavrysersntKCVGITIETRPDYCLKRHLSDMLGYGCTRLEIG 247
Cdd:smart00729  55 VFIgGGTPTLLSPEQLEELLEAIREILGLA-----------------KDVEITIETRPDTLTEELLEALKEAGVNRVSLG 117
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265    248 VQSVYEDVARDTNRGHTVRAVCESFHLAKDAGF-KVVAHMMPDLPNVGMErDVEQFIEFFEnpAFRPDGLKLYPTLVIRG 326
Cdd:smart00729 118 VQSGDDEVLKAINRGHTVEDVLEAVELLREAGPiKVSTDLIVGLPGETEE-DFEETLKLLK--ELGPDRVSIFPLSPRPG 194
                          250       260
                   ....*....|....*....|....
gi 68989265    327 TGLYELWKtgRYKSYSPSALVDLV 350
Cdd:smart00729 195 TPLAKMYK--RLKPPTKEERAELL 216
YhcC COG1242
Radical SAM superfamily enzyme [General function prediction only];
217-374 1.11e-20

Radical SAM superfamily enzyme [General function prediction only];


Pssm-ID: 224163 [Multi-domain]  Cd Length: 312  Bit Score: 92.77  E-value: 1.11e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265 217 VGITIETRPDyCLKRHLSDMLGYGCTR----LEIGVQSVYEDVARDTNRGHTVRAVCESFHLAKDAGFKVVAHMMPDLPN 292
Cdd:COG1242 116 VGLSIGTRPD-CLPDDVLDLLAEYNKRyevwVELGLQTAHDKTLKRINRGHDFACYVDAVKRLRKRGIKVCTHLINGLPG 194
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265 293 VGMERDVEQFIEFFENPAfrpDGLKLYPTLVIRGTGLYELWKTGRYKSYSPSALVDLVARILALVPPWTRVYRVQRDIPM 372
Cdd:COG1242 195 ETRDEMLETAKIVAELGV---DGIKLHPLHVVKGTPMEKMYEKGRLKFLSLEEYVELVCDQLEHLPPEVVIHRITGDAPR 271

                ..
gi 68989265 373 PL 374
Cdd:COG1242 272 DT 273
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
137-302 1.08e-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: 397943 [Multi-domain]  Cd Length: 159  Bit Score: 68.70  E-value: 1.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265   137 RAIRARYDPYLQTRHRVEQLKQLGHSVDKVEFIVMGGTFMALPEEYRDYFIRNLHDALSGHTsnnvteavrysersntkc 216
Cdd:pfam04055  15 PSIRARGKPRELSPEEILEEAKELKRLGVEVVILGGGEPLLLPDLVELLERLLKLEEAEGIR------------------ 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265   217 vgITIETRPDYCLKRHLSDMLGYGCTRLEIGVQSVYEDVARDTNRGHTVRAVCESFHLAKDAGFKVVAHMMPDLPNVGME 296
Cdd:pfam04055  77 --ITLETNGTLLDEELLELLKEAGLDRVSIGLESGDDEVLKLINRGHTFEEVLEAIELLREAGIPVVTDNIVGLPGETDE 154

                  ....*.
gi 68989265   297 rDVEQF 302
Cdd:pfam04055 155 -DLEEL 159
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
97-334 1.37e-13

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: 69.67  E-value: 1.37e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265  97 PHRCPHIsftgniCVYCPGGPDSDFEystqsytgyeptsmrairaryDPYLQTRHRVEQLKQLGHSVDKVEFIVMGGTFM 176
Cdd:cd01335   4 TRGCNLN------CGFCSNPASKGRG---------------------PESPPEIEEILDIVLEAKERGVEVVILTGGEPL 56
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265 177 ALPeeYRDYFIRNLHDALSGHTsnnvteavrysersntkcvgITIETRPDYCLKRHLSDMLGYGCTRLEIGVQSVYEDVA 256
Cdd:cd01335  57 LYP--ELAELLRRLKKELPGFE--------------------ISIETNGTLLTEELLKELKELGLDGVGVSLDSGDEEVA 114
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 68989265 257 RDTN-RGHTVRAVCESFHLAKDAGFKVVAHMMPDLPNVGMERDVEQFieFFENPAFRPDGLKLYPTLVIRGTGLYELWK 334
Cdd:cd01335 115 DKIRgSGESFKERLEALKELREAGLGLSTTLLVGLGDEDEEDDLEEL--ELLAEFRSPDRVSLFRLLPEEGTPLELAAP 191
HemN COG0635
Coproporphyrinogen III oxidase or related Fe-S oxidoreductase [Coenzyme transport and ...
102-338 2.34e-09

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


Pssm-ID: 223708 [Multi-domain]  Cd Length: 416  Bit Score: 59.59  E-value: 2.34e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265 102 HISFTGNICVYCpggpdsDF-------EYSTQSYTGYEPTSMRAIRARYDPylqtRHRVEQLkqlghsvdkveFIVmGGT 174
Cdd:COG0635  40 HIPFCVSKCPYC------DFnshvtkrGQPVDEYLDALLEEIELVAALLGG----QREVKTI-----------YFG-GGT 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265 175 FMALPEEYRDYFIRNLHDALSGHTsnNVTEavrysersntkcvgITIETRPDYCLKRHLSDMLGYGCTRLEIGVQSVYED 254
Cdd:COG0635  98 PSLLSPEQLERLLKALRELFNDLD--PDAE--------------ITIEANPGTVEAEKFKALKEAGVNRISLGVQSFNDE 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265 255 VARDTNRGHTVRAVCESFHLAKDAGFK-VVAHMMPDLPN---VGMERDVEQFIEffenpaFRPDGLKLYPTLVIRGTGLY 330
Cdd:COG0635 162 VLKALGRIHDEEEAKEAVELARKAGFTsINIDLIYGLPGqtlESLKEDLEQALE------LGPDHLSLYSLAIEPGTKFA 235

                ....*...
gi 68989265 331 ELWKTGRY 338
Cdd:COG0635 236 QRKIKGKA 243
PRK08207 PRK08207
coproporphyrinogen III oxidase; Provisional
110-339 3.38e-08

coproporphyrinogen III oxidase; Provisional


Pssm-ID: 236187 [Multi-domain]  Cd Length: 488  Bit Score: 56.04  E-value: 3.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265  110 CVYCpggpdsdfeystqSYTGYEptsMRAIRARYDPYLQTRHR-----VEQLKQLGHSVDKVEFivMGGTFMALPEEYRD 184
Cdd:PRK08207 177 CLYC-------------SFPSYP---IKGYKGLVEPYLEALHYeieeiGKYLKEKGLKITTIYF--GGGTPTSLTAEELE 238
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265  185 YFIRNLHDALSGhtSNNVTEavrysersntkcvgITIET-RPDYCLKRHLSDMLGYGCTRLEIGVQSVYEDVARDTNRGH 263
Cdd:PRK08207 239 RLLEEIYENFPD--VKNVKE--------------FTVEAgRPDTITEEKLEVLKKYGVDRISINPQTMNDETLKAIGRHH 302
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265  264 TVRAVCESFHLAKDAGFKVVaHMmpD----LPNVGMErDVEQFIEFFEnpAFRPDGLKLYpTLVI-RGTGLYELWKtgRY 338
Cdd:PRK08207 303 TVEDIIEKFHLAREMGFDNI-NM--DliigLPGEGLE-EVKHTLEEIE--KLNPESLTVH-TLAIkRASRLTENKE--KY 373

                 .
gi 68989265  339 K 339
Cdd:PRK08207 374 K 374
PRK08446 PRK08446
coproporphyrinogen III oxidase family protein;
102-281 4.49e-07

coproporphyrinogen III oxidase family protein;


Pssm-ID: 181428 [Multi-domain]  Cd Length: 350  Bit Score: 51.88  E-value: 4.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265  102 HISFTGNICVYCpggpdsdfeySTQSYT---GYEPTSMRAIrarydpYLQTRHrveQLKQLGHSVDKVEFIvMGGTFMAL 178
Cdd:PRK08446   6 HIPFCESKCGYC----------AFNSYEnkhDLKKEYMQAL------CLDLKF---ELEQFTDEKIESVFI-GGGTPSTV 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265  179 -PEEYRDYFIRnlhdaLSGHTSNNvTEavrysersntkcvgITIETRPDYCLKRHLSDMLGYGCTRLEIGVQSVYEDVAR 257
Cdd:PRK08446  66 sAKFYEPIFEI-----ISPYLSKD-CE--------------ITTEANPNSATKAWLKGMKNLGVNRISFGVQSFNEDKLK 125
                        170       180
                 ....*....|....*....|....
gi 68989265  258 DTNRGHTVRAVCESFHLAKDAGFK 281
Cdd:PRK08446 126 FLGRIHSQKQIIKAIENAKKAGFE 149
PRK05799 PRK05799
oxygen-independent coproporphyrinogen III oxidase;
102-339 5.74e-07

oxygen-independent coproporphyrinogen III oxidase;


Pssm-ID: 180263 [Multi-domain]  Cd Length: 374  Bit Score: 51.91  E-value: 5.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265  102 HISFTGNICVYCpggpdsDFeystQSYTGYEPTSMRAIRArydpylqtrhrveQLKQLGHSVDKVEFIVM---GGTFMAL 178
Cdd:PRK05799   9 HIPFCKQKCLYC------DF----PSYSGKEDLMMEYIKA-------------LSKEIRNSTKNKKIKSIfigGGTPTYL 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265  179 PEEYrdyfIRNLHDALSghtsnnvteavRYSERSNtkcVGITIETRPDYCLKRHLSDMLGYGCTRLEIGVQSVYEDVARD 258
Cdd:PRK05799  66 SLEA----LEILKETIK-----------KLNKKED---LEFTVEGNPGTFTEEKLKILKSMGVNRLSIGLQAWQNSLLKY 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265  259 TNRGHTVRAVCESFHLAKDAGFK-VVAHMMPDLPNvgmeRDVEQFIEFFENPA-FRPDGLKLYPTLVIRGTGLYELWKTG 336
Cdd:PRK05799 128 LGRIHTFEEFLENYKLARKLGFNnINVDLMFGLPN----QTLEDWKETLEKVVeLNPEHISCYSLIIEEGTPFYNLYENG 203

                 ...
gi 68989265  337 RYK 339
Cdd:PRK05799 204 KLK 206
PRK08599 PRK08599
oxygen-independent coproporphyrinogen III oxidase;
102-305 5.58e-06

oxygen-independent coproporphyrinogen III oxidase;


Pssm-ID: 236309 [Multi-domain]  Cd Length: 377  Bit Score: 48.71  E-value: 5.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265  102 HISFTGNICVYCpggpdsDFE---YSTQ---SYTGYEPTSMRAIRARYDPYLQTrhrveqlkqlghsvdkveFIVMGGTF 175
Cdd:PRK08599   7 HIPFCEHICYYC------DFNkvfIKNQpvdEYLDALIKEMNTYAIRPFDKLKT------------------IYIGGGTP 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265  176 MALPEEYRDYFIRNLHDALsghTSNNVTEavrysersntkcvgITIETRPDYCLKRHLSDMLGYGCTRLEIGVQSVYEDV 255
Cdd:PRK08599  63 TALSAEQLERLLTAIHRNL---PLSGLEE--------------FTFEANPGDLTKEKLQVLKDSGVNRISLGVQTFNDEL 125
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 68989265  256 ARDTNRGHTVRAVCESFHLAKDAGFKVVA-HMMPDLPNVGME---RDVEQFIEF 305
Cdd:PRK08599 126 LKKIGRTHNEEDVYEAIANAKKAGFDNISiDLIYALPGQTIEdfkESLAKALAL 179
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
405-541 4.99e-05

Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.


Pssm-ID: 404548 [Multi-domain]  Cd Length: 128  Bit Score: 43.03  E-value: 4.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265   405 REVGIQEIHHKVRPYQVelirRDYVANGGWETFLSYEDpeqDILIGLLRLRRCSpqsfrpelkggvsivrelHVYGSVVp 484
Cdd:pfam13673   6 SEEGIETFLEFISPEAL----RERIDEGEYFFFVAFEG---GKIVGVIALRNGG------------------HISLLFV- 59
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 68989265   485 vssrDPsKFQHQGFGMMLMEEAERIARDEHGS-SKLAVISGVGTRNYYRKMGYELEGP 541
Cdd:pfam13673  60 ----DP-EYQGQGIGKALLEAAEKYAEKDGIKlSEVTVNASPYAVPFYEKLGFVATGP 112
PRK08208 PRK08208
coproporphyrinogen III oxidase family protein;
219-398 1.01e-04

coproporphyrinogen III oxidase family protein;


Pssm-ID: 181292 [Multi-domain]  Cd Length: 430  Bit Score: 44.61  E-value: 1.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265  219 ITIETRPDYCLKRHLSDMLGYGCTRLEIGVQSVYEDVARDTNRGHTVRAVCESFHLAKDAGFkvvahmmPDLpNV----G 294
Cdd:PRK08208 130 KSVETSPATTTAEKLALLAARGVNRLSIGVQSFHDSELHALHRPQKRADVHQALEWIRAAGF-------PIL-NIdliyG 201
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265  295 MER-DVEQFIEFFENP-AFRPDGLKLYPTLVIRGTGLYElwktgRYKSYSPSALvdlvarilalvppwtRVYRVQRDIpm 372
Cdd:PRK08208 202 IPGqTHASWMESLDQAlVYRPEELFLYPLYVRPLTGLGR-----RARAWDDQRL---------------SLYRLARDL-- 259
                        170       180
                 ....*....|....*....|....*.
gi 68989265  373 pLVSSGVEHGNLRELALARMKDMGTE 398
Cdd:PRK08208 260 -LLEAGYTQTSMRMFRRNDAPDKGAP 284
COG1244 COG1244
Uncharacterized Fe-S cluster-containing protein. MiaB family [General function prediction only] ...
156-339 6.27e-04

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


Pssm-ID: 224165 [Multi-domain]  Cd Length: 358  Bit Score: 42.00  E-value: 6.27e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265 156 LKQLGHSVDKVEF--------IVMGGTF---MALPEEYRDYFIRNLHDalsghtSNNVTEAVrysersntkcvgitIETR 224
Cdd:COG1244  85 INQFDEAYSKYEGkfdefvvkIFTSGSFldpEEVPREARRYILERISE------NDNVKEVV--------------VESR 144
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265 225 PDYCLKRHLSDMLGYGC---TRLEIGVQSVYEDVARDT-NRGHTVRAVCESFHLAKDAGFKVVAHMMPDLPNVGMERDVE 300
Cdd:COG1244 145 PEFIREERLEEITEILEgkiVEVAIGLETANDKIREDSiNKGFTFEDFVRAAEIIRNYGAKVKTYLLLKPPFLSEKEAIE 224
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 68989265 301 QFIEFFENPAFRPDGLKLYPTLVIRGTgLYE-LWKTGRYK 339
Cdd:COG1244 225 DVISSIVAAKPGTDTISINPTNVQKGT-LVEkLWRRGLYR 263
PRK05904 PRK05904
coproporphyrinogen III oxidase; Provisional
220-308 2.06e-03

coproporphyrinogen III oxidase; Provisional


Pssm-ID: 235641 [Multi-domain]  Cd Length: 353  Bit Score: 40.56  E-value: 2.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265  220 TIETRPDYCLKRHLSDMLGYGCTRLEIGVQSVYEDVARDTNRGHTVRAVCESFHLAKDAG-FKVVAHMMPDLPNVGMErD 298
Cdd:PRK05904  93 TIECNPELITQSQINLLKKNKVNRISLGVQSMNNNILKQLNRTHTIQDSKEAINLLHKNGiYNISCDFLYCLPILKLK-D 171
                         90
                 ....*....|
gi 68989265  299 VEQFIEFFEN 308
Cdd:PRK05904 172 LDEVFNFILK 181
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
465-548 3.36e-03

Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal structure and biogenesis];


Pssm-ID: 223532  Cd Length: 177  Bit Score: 38.82  E-value: 3.36e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265 465 ELKGGVSIVRELHVYGSVVpvssrDPSkFQHQGFGMMLMEEAERIARDEHGSSKLAVI---SGVGTRNYYRKMGYELEGp 541
Cdd:COG0456  81 VVDGRPSADHEGHIYNLAV-----DPE-YRGRGIGRALLDEALERLRERGLADKIVLEvreSNEAAIGLYRKLGFEVVK- 153

                ....*..
gi 68989265 542 yMVKNLY 548
Cdd:COG0456 154 -IRKNYY 159
PRK06294 PRK06294
coproporphyrinogen III oxidase; Provisional
219-304 4.46e-03

coproporphyrinogen III oxidase; Provisional


Pssm-ID: 180518 [Multi-domain]  Cd Length: 370  Bit Score: 39.36  E-value: 4.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989265  219 ITIETRPDYCLKRHLSDMLGYGCTRLEIGVQSVYEDVARDTNRGHTVRAVCESFHLAKDAGFK-VVAHMMPDLPnvgmER 297
Cdd:PRK06294  92 ITLEANPENLSESYIRALALTGINRISIGVQTFDDPLLKLLGRTHSSSKAIDAVQECSEHGFSnLSIDLIYGLP----TQ 167

                 ....*..
gi 68989265  298 DVEQFIE 304
Cdd:PRK06294 168 SLSDFIV 174
YgiQ COG1032
Radical SAM superfamily enzyme YgiQ, UPF0313 family [General function prediction only];
240-307 6.18e-03

Radical SAM superfamily enzyme YgiQ, UPF0313 family [General function prediction only];


Pssm-ID: 223963 [Multi-domain]  Cd Length: 490  Bit Score: 39.15  E-value: 6.18e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 68989265 240 GCTRLEIGVQSVYEDVARDTNRGHTVRAVC-ESFHLAKDAGFKVVAHMMPDLPNVGMErDVEQFIEFFE 307
Cdd:COG1032 310 GLRRVYIGIESGSEELLKKINKGITTEEVLeEAVKIAKEHGLRVKLYFIVGLPGETEE-DVKETIELAK 377
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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