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Conserved domains on  [gi|293353904|ref|XP_002728336|]
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elongator complex protein 3 isoform X2 [Rattus norvegicus]

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 ...
37-546 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: 780.85  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904   37 DLNKLKTKTASKYGLSSQPRLVDIIAAVPPHYRKILIPKLKAKPIRTASGIAVVAVMCKPHRCPHISftgniCVYCPGGP 116
Cdd:TIGR01211  16 DLEDLKLEVSRKYGLSKVPSNSEILNSAPDEEKKKLEPILRKKPVRTISGVAVVAVMTSPHRCPHGK-----CLYCPGGP 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904  117 DSdfEYSTQSYTGYEPTSMRAIRARYDPYLQTRHRIEQLKQLGHSVDKVEFIVMGGTFMALPEEYRDYFIRNLHDALSGH 196
Cdd:TIGR01211  91 DS--ENSPQSYTGYEPAAMRGRQNDYDPYEQVTARLEQLEQIGHPVDKVELIIMGGTFPARDLDYQEWFIKRCLNAMNGF 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904  197 TS-----NNIYEAIKYSERSLTKCIGITIETRPDYCMKRHLSDMLTYGCTRLEIGVQSVYEDVARDTNRGHTVKAVCESF 271
Cdd:TIGR01211 169 DQelkgnSTLEEAIRINETSKHRCVGLTIETRPDYCREEHIDRMLKLGATRVELGVQTIYNDILERTKRGHTVRDVVEAT 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904  272 HLAKDSGFKVVAHMMPDLPNVGLERDIEQFIEFFENPAFRPDGLKLYPTLVIRGTGLYELWKSGRYRSYSPSDLIELVAR 351
Cdd:TIGR01211 249 RLLRDAGLKVVYHIMPGLPGSSFERDLEMFREIFEDPRFKPDMLKIYPTLVTRGTELYELWKRGEYKPYTTEEAVELIVE 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904  352 ILALVPPWTRVYRVQRDIPMPLVSSGVDHGNLRELAFARMKDLGIQCRDVRTREVGIQEIHHRVRPY-QVELVRRDYVAN 430
Cdd:TIGR01211 329 IKRMMPKWVRIQRIQRDIPAPLIVAGVKKSNLRELVYRRMKEHGITCRCIRCREVGHQMVKPVQPEEeNVELIVEEYAAS 408
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904  431 GGWETFLSYEDPDQDILIGLLRLRKCSEETFRfELGGGVSIVRELHVYGSVVPVSSRDPTKFQHQGFGMLLMEEAERIAL 510
Cdd:TIGR01211 409 GGTEFFLSYEDPKNDILIGFLRLRFPSEPAHR-KEVDATALVRELHVYGSEVPIGERGDDEWQHRGYGRRLLEEAERIAA 487
                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 293353904  511 EEhGSGKIAVISGVGTRNYYRKMGYRLQGPYMVKML 546
Cdd:TIGR01211 488 EE-GSEKILVISGIGVREYYRKLGYELDGPYMSKRL 522
 
Name Accession Description Interval E-value
ELP3 TIGR01211
radical SAM enzyme/protein acetyltransferase, ELP3 family; This family includes elongator ...
37-546 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: 780.85  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904   37 DLNKLKTKTASKYGLSSQPRLVDIIAAVPPHYRKILIPKLKAKPIRTASGIAVVAVMCKPHRCPHISftgniCVYCPGGP 116
Cdd:TIGR01211  16 DLEDLKLEVSRKYGLSKVPSNSEILNSAPDEEKKKLEPILRKKPVRTISGVAVVAVMTSPHRCPHGK-----CLYCPGGP 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904  117 DSdfEYSTQSYTGYEPTSMRAIRARYDPYLQTRHRIEQLKQLGHSVDKVEFIVMGGTFMALPEEYRDYFIRNLHDALSGH 196
Cdd:TIGR01211  91 DS--ENSPQSYTGYEPAAMRGRQNDYDPYEQVTARLEQLEQIGHPVDKVELIIMGGTFPARDLDYQEWFIKRCLNAMNGF 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904  197 TS-----NNIYEAIKYSERSLTKCIGITIETRPDYCMKRHLSDMLTYGCTRLEIGVQSVYEDVARDTNRGHTVKAVCESF 271
Cdd:TIGR01211 169 DQelkgnSTLEEAIRINETSKHRCVGLTIETRPDYCREEHIDRMLKLGATRVELGVQTIYNDILERTKRGHTVRDVVEAT 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904  272 HLAKDSGFKVVAHMMPDLPNVGLERDIEQFIEFFENPAFRPDGLKLYPTLVIRGTGLYELWKSGRYRSYSPSDLIELVAR 351
Cdd:TIGR01211 249 RLLRDAGLKVVYHIMPGLPGSSFERDLEMFREIFEDPRFKPDMLKIYPTLVTRGTELYELWKRGEYKPYTTEEAVELIVE 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904  352 ILALVPPWTRVYRVQRDIPMPLVSSGVDHGNLRELAFARMKDLGIQCRDVRTREVGIQEIHHRVRPY-QVELVRRDYVAN 430
Cdd:TIGR01211 329 IKRMMPKWVRIQRIQRDIPAPLIVAGVKKSNLRELVYRRMKEHGITCRCIRCREVGHQMVKPVQPEEeNVELIVEEYAAS 408
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904  431 GGWETFLSYEDPDQDILIGLLRLRKCSEETFRfELGGGVSIVRELHVYGSVVPVSSRDPTKFQHQGFGMLLMEEAERIAL 510
Cdd:TIGR01211 409 GGTEFFLSYEDPKNDILIGFLRLRFPSEPAHR-KEVDATALVRELHVYGSEVPIGERGDDEWQHRGYGRRLLEEAERIAA 487
                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 293353904  511 EEhGSGKIAVISGVGTRNYYRKMGYRLQGPYMVKML 546
Cdd:TIGR01211 488 EE-GSEKILVISGIGVREYYRKLGYELDGPYMSKRL 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: 768.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904  34 KDVDLNKLKTKTASKYGLSSQPRLVDIIAAVPPHYRkiLIPKLKAKPIRTASGIAVVAVMCKPHRCPHisftgNICVYCP 113
Cdd:COG1243   14 KKKELEDLKLEVSRKYGLSKVPRNSDILNAAPPEER--LREILRRKPVRTISGVAVVAVMTSPHGCPH-----GRCVFCP 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904 114 GGPDsdfEYSTQSYTGYEPTSMRAIRARYDPYLQTRHRIEQLKQLGHSVDKVEFIVMGGTFMALPEEYRDYFIRNLHDAL 193
Cdd:COG1243   87 GGPD---KDSPQSYTGEEPAALRAIKNRYDPYEQVRARLKQLETIGHTSDKVELIIMGGTFTALSLEYQEWFLKVALKAM 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904 194 SGHtSNNIYEAIKYSERSLTKCIGITIETRPDYCMKRHLSDMLTYGCTRLEIGVQSVYEDVARDTNRGHTVKAVCESFHL 273
Cdd:COG1243  164 NDF-GYDLEEAQRKNETAELRCVGITIETRPDYIDEEHLDQMLKYGVTRVELGVQSIYDDVLERTKRGHTVEDVVEATRL 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904 274 AKDSGFKVVAHMMPDLPNVGLERDIEQFIEFFENPAFRPDGLKLYPTLVIRGTGLYELWKSGRYRSYSPSDLIELVARIL 353
Cdd:COG1243  243 LKDAGFKVGYHIMPGLPGSDFERDLESFREIFEDPRFRPDMLKIYPTLVIEGTELYEMWKRGLYKPYTTEEAVELIVEIY 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904 354 ALVPPWTRVYRVQRDIPMPLVSSGVDHGNLRELAFARMKDLGIQCRDVRTREVGIQEIHHRVRPY--QVELVRRDYVANG 431
Cdd:COG1243  323 RLEPKWVRVIRIQRDIPAELIVDGVKKSNLRELVENRMREEGIKCRCIRCREVGIVVVKNVVIPPveQILLKREEYEASG 402
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904 432 GWETFLSYEDPDQDILIGLLRLRKCSEETFRFELGGGVSIVRELHVYGSVVPVSSRdPTKFQHQGFGMLLMEEAERIALE 511
Cdd:COG1243  403 GTEIFLSYEDPKNDILIGFLRLREPSEGAHREEIDDKTAIVRELHVYGSEVPIGKR-EDEWQHRGYGRELLEEAERIARE 481
                        490       500       510
                 ....*....|....*....|....*....|....*
gi 293353904 512 EHgSGKIAVISGVGTRNYYRKMGYRLQGPYMVKML 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 4.36e-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: 101.32  E-value: 4.36e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904  312 PDGLKLYPTLVIRGTGLYELWKSGRYRSYSPSDLIELVARILALVPPWTRVYRVQRDIPMPLVSSGVDHG-NLRELAFAR 390
Cdd:pfam16199   1 PDGVKIHPLLVLKGTPLAELYERGEYKPLSLEEYVELVADFLELLPPDIVIHRLGGDAPKELLVAPPWHLpKLRVLNLIE 80
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
89-352 2.35e-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: 104.02  E-value: 2.35e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904    89 VVAVMCKPHRCPHIsftgniCVYCPGGPDSdfeystqsytgyeptsmraiRARYDPYLQTRHR-IEQLKQLGHSVDKVEF 167
Cdd:smart00729   1 PLALYIITRGCPRR------CTFCSFPSLR--------------------GKLRSRYLEALVReIELLAEKGEKEGLVGT 54
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904   168 IVM-GGTFMALPEEYRDYFIRNLHDALSghtsnniyeaikysersLTKCIGITIETRPDYCMKRHLSDMLTYGCTRLEIG 246
Cdd:smart00729  55 VFIgGGTPTLLSPEQLEELLEAIREILG-----------------LAKDVEITIETRPDTLTEELLEALKEAGVNRVSLG 117
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904   247 VQSVYEDVARDTNRGHTVKAVCESFHLAKDSGF-KVVAHMMPDLPNVGLErDIEQFIEFFEnpAFRPDGLKLYPTLVIRG 325
Cdd:smart00729 118 VQSGDDEVLKAINRGHTVEDVLEAVELLREAGPiKVSTDLIVGLPGETEE-DFEETLKLLK--ELGPDRVSIFPLSPRPG 194
                          250       260
                   ....*....|....*....|....*..
gi 293353904   326 TGLYELWKsgryrSYSPSDLIELVARI 352
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 6.55e-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: 70.83  E-value: 6.55e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904  96 PHRCPHIsftgniCVYCPGGPDSDFEystqsytgyeptsmrairaryDPYLQTRHRIEQLKQLGHSVDKVEFIVMGGTFM 175
Cdd:cd01335    4 TRGCNLN------CGFCSNPASKGRG---------------------PESPPEIEEILDIVLEAKERGVEVVILTGGEPL 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904 176 ALPeeYRDYFIRNLHDALSGHTsnniyeaikysersltkcigITIETRPDYCMKRHLSDMLTYGCTRLEIGVQSVYEDVA 255
Cdd:cd01335   57 LYP--ELAELLRRLKKELPGFE--------------------ISIETNGTLLTEELLKELKELGLDGVGVSLDSGDEEVA 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904 256 RDTN-RGHTVKAVCESFHLAKDSGFKVVAHMMPDLPNVGLERDIEQFieFFENPAFRPDGLKLYPTLVIRGTGLYELWKS 334
Cdd:cd01335  115 DKIRgSGESFKERLEALKELREAGLGLSTTLLVGLGDEDEEDDLEEL--ELLAEFRSPDRVSLFRLLPEEGTPLELAAPV 192

                 ....*.
gi 293353904 335 GRYRSY 340
Cdd:cd01335  193 VPAEKL 198
PRK05799 PRK05799
oxygen-independent coproporphyrinogen III oxidase;
101-336 8.90e-10

oxygen-independent coproporphyrinogen III oxidase;


Pssm-ID: 180263 [Multi-domain]  Cd Length: 374  Bit Score: 60.38  E-value: 8.90e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904 101 HISFTGNICVYCpggpdsDFeystQSYTGYEPTSMRAIRArydpylqtrhrieQLKQLGHSVDKVEFIVM---GGTFMAL 177
Cdd:PRK05799   9 HIPFCKQKCLYC------DF----PSYSGKEDLMMEYIKA-------------LSKEIRNSTKNKKIKSIfigGGTPTYL 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904 178 PEEYrdyfirnlhdalsghtSNNIYEAIKYSerSLTKCIGITIETRPDYCMKRHLSDMLTYGCTRLEIGVQSVYEDVARD 257
Cdd:PRK05799  66 SLEA----------------LEILKETIKKL--NKKEDLEFTVEGNPGTFTEEKLKILKSMGVNRLSIGLQAWQNSLLKY 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904 258 TNRGHTVKAVCESFHLAKDSGFK-VVAHMMPDLPNvgleRDIEQFIEFFENPA-FRPDGLKLYPTLVIRGTGLYELWKSG 335
Cdd:PRK05799 128 LGRIHTFEEFLENYKLARKLGFNnINVDLMFGLPN----QTLEDWKETLEKVVeLNPEHISCYSLIIEEGTPFYNLYENG 203

                 .
gi 293353904 336 R 336
Cdd:PRK05799 204 K 204
 
Name Accession Description Interval E-value
ELP3 TIGR01211
radical SAM enzyme/protein acetyltransferase, ELP3 family; This family includes elongator ...
37-546 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: 780.85  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904   37 DLNKLKTKTASKYGLSSQPRLVDIIAAVPPHYRKILIPKLKAKPIRTASGIAVVAVMCKPHRCPHISftgniCVYCPGGP 116
Cdd:TIGR01211  16 DLEDLKLEVSRKYGLSKVPSNSEILNSAPDEEKKKLEPILRKKPVRTISGVAVVAVMTSPHRCPHGK-----CLYCPGGP 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904  117 DSdfEYSTQSYTGYEPTSMRAIRARYDPYLQTRHRIEQLKQLGHSVDKVEFIVMGGTFMALPEEYRDYFIRNLHDALSGH 196
Cdd:TIGR01211  91 DS--ENSPQSYTGYEPAAMRGRQNDYDPYEQVTARLEQLEQIGHPVDKVELIIMGGTFPARDLDYQEWFIKRCLNAMNGF 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904  197 TS-----NNIYEAIKYSERSLTKCIGITIETRPDYCMKRHLSDMLTYGCTRLEIGVQSVYEDVARDTNRGHTVKAVCESF 271
Cdd:TIGR01211 169 DQelkgnSTLEEAIRINETSKHRCVGLTIETRPDYCREEHIDRMLKLGATRVELGVQTIYNDILERTKRGHTVRDVVEAT 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904  272 HLAKDSGFKVVAHMMPDLPNVGLERDIEQFIEFFENPAFRPDGLKLYPTLVIRGTGLYELWKSGRYRSYSPSDLIELVAR 351
Cdd:TIGR01211 249 RLLRDAGLKVVYHIMPGLPGSSFERDLEMFREIFEDPRFKPDMLKIYPTLVTRGTELYELWKRGEYKPYTTEEAVELIVE 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904  352 ILALVPPWTRVYRVQRDIPMPLVSSGVDHGNLRELAFARMKDLGIQCRDVRTREVGIQEIHHRVRPY-QVELVRRDYVAN 430
Cdd:TIGR01211 329 IKRMMPKWVRIQRIQRDIPAPLIVAGVKKSNLRELVYRRMKEHGITCRCIRCREVGHQMVKPVQPEEeNVELIVEEYAAS 408
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904  431 GGWETFLSYEDPDQDILIGLLRLRKCSEETFRfELGGGVSIVRELHVYGSVVPVSSRDPTKFQHQGFGMLLMEEAERIAL 510
Cdd:TIGR01211 409 GGTEFFLSYEDPKNDILIGFLRLRFPSEPAHR-KEVDATALVRELHVYGSEVPIGERGDDEWQHRGYGRRLLEEAERIAA 487
                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 293353904  511 EEhGSGKIAVISGVGTRNYYRKMGYRLQGPYMVKML 546
Cdd:TIGR01211 488 EE-GSEKILVISGIGVREYYRKLGYELDGPYMSKRL 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: 768.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904  34 KDVDLNKLKTKTASKYGLSSQPRLVDIIAAVPPHYRkiLIPKLKAKPIRTASGIAVVAVMCKPHRCPHisftgNICVYCP 113
Cdd:COG1243   14 KKKELEDLKLEVSRKYGLSKVPRNSDILNAAPPEER--LREILRRKPVRTISGVAVVAVMTSPHGCPH-----GRCVFCP 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904 114 GGPDsdfEYSTQSYTGYEPTSMRAIRARYDPYLQTRHRIEQLKQLGHSVDKVEFIVMGGTFMALPEEYRDYFIRNLHDAL 193
Cdd:COG1243   87 GGPD---KDSPQSYTGEEPAALRAIKNRYDPYEQVRARLKQLETIGHTSDKVELIIMGGTFTALSLEYQEWFLKVALKAM 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904 194 SGHtSNNIYEAIKYSERSLTKCIGITIETRPDYCMKRHLSDMLTYGCTRLEIGVQSVYEDVARDTNRGHTVKAVCESFHL 273
Cdd:COG1243  164 NDF-GYDLEEAQRKNETAELRCVGITIETRPDYIDEEHLDQMLKYGVTRVELGVQSIYDDVLERTKRGHTVEDVVEATRL 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904 274 AKDSGFKVVAHMMPDLPNVGLERDIEQFIEFFENPAFRPDGLKLYPTLVIRGTGLYELWKSGRYRSYSPSDLIELVARIL 353
Cdd:COG1243  243 LKDAGFKVGYHIMPGLPGSDFERDLESFREIFEDPRFRPDMLKIYPTLVIEGTELYEMWKRGLYKPYTTEEAVELIVEIY 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904 354 ALVPPWTRVYRVQRDIPMPLVSSGVDHGNLRELAFARMKDLGIQCRDVRTREVGIQEIHHRVRPY--QVELVRRDYVANG 431
Cdd:COG1243  323 RLEPKWVRVIRIQRDIPAELIVDGVKKSNLRELVENRMREEGIKCRCIRCREVGIVVVKNVVIPPveQILLKREEYEASG 402
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904 432 GWETFLSYEDPDQDILIGLLRLRKCSEETFRFELGGGVSIVRELHVYGSVVPVSSRdPTKFQHQGFGMLLMEEAERIALE 511
Cdd:COG1243  403 GTEIFLSYEDPKNDILIGFLRLREPSEGAHREEIDDKTAIVRELHVYGSEVPIGKR-EDEWQHRGYGRELLEEAERIARE 481
                        490       500       510
                 ....*....|....*....|....*....|....*
gi 293353904 512 EHgSGKIAVISGVGTRNYYRKMGYRLQGPYMVKML 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 4.36e-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: 101.32  E-value: 4.36e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904  312 PDGLKLYPTLVIRGTGLYELWKSGRYRSYSPSDLIELVARILALVPPWTRVYRVQRDIPMPLVSSGVDHG-NLRELAFAR 390
Cdd:pfam16199   1 PDGVKIHPLLVLKGTPLAELYERGEYKPLSLEEYVELVADFLELLPPDIVIHRLGGDAPKELLVAPPWHLpKLRVLNLIE 80
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
89-352 2.35e-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: 104.02  E-value: 2.35e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904    89 VVAVMCKPHRCPHIsftgniCVYCPGGPDSdfeystqsytgyeptsmraiRARYDPYLQTRHR-IEQLKQLGHSVDKVEF 167
Cdd:smart00729   1 PLALYIITRGCPRR------CTFCSFPSLR--------------------GKLRSRYLEALVReIELLAEKGEKEGLVGT 54
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904   168 IVM-GGTFMALPEEYRDYFIRNLHDALSghtsnniyeaikysersLTKCIGITIETRPDYCMKRHLSDMLTYGCTRLEIG 246
Cdd:smart00729  55 VFIgGGTPTLLSPEQLEELLEAIREILG-----------------LAKDVEITIETRPDTLTEELLEALKEAGVNRVSLG 117
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904   247 VQSVYEDVARDTNRGHTVKAVCESFHLAKDSGF-KVVAHMMPDLPNVGLErDIEQFIEFFEnpAFRPDGLKLYPTLVIRG 325
Cdd:smart00729 118 VQSGDDEVLKAINRGHTVEDVLEAVELLREAGPiKVSTDLIVGLPGETEE-DFEETLKLLK--ELGPDRVSIFPLSPRPG 194
                          250       260
                   ....*....|....*....|....*..
gi 293353904   326 TGLYELWKsgryrSYSPSDLIELVARI 352
Cdd:smart00729 195 TPLAKMYK-----RLKPPTKEERAELL 216
YhcC COG1242
Radical SAM superfamily enzyme [General function prediction only];
216-373 2.49e-20

Radical SAM superfamily enzyme [General function prediction only];


Pssm-ID: 224163 [Multi-domain]  Cd Length: 312  Bit Score: 91.62  E-value: 2.49e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904 216 IGITIETRPDyCMKRHLSDMLTYGCTR----LEIGVQSVYEDVARDTNRGHTVKAVCESFHLAKDSGFKVVAHMMPDLPN 291
Cdd:COG1242  116 VGLSIGTRPD-CLPDDVLDLLAEYNKRyevwVELGLQTAHDKTLKRINRGHDFACYVDAVKRLRKRGIKVCTHLINGLPG 194
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904 292 VGLERDIEQFIEFFENPAfrpDGLKLYPTLVIRGTGLYELWKSGRYRSYSPSDLIELVARILALVPPWTRVYRVQRDIPM 371
Cdd:COG1242  195 ETRDEMLETAKIVAELGV---DGIKLHPLHVVKGTPMEKMYEKGRLKFLSLEEYVELVCDQLEHLPPEVVIHRITGDAPR 271

                 ..
gi 293353904 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 6.55e-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: 70.83  E-value: 6.55e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904  96 PHRCPHIsftgniCVYCPGGPDSDFEystqsytgyeptsmrairaryDPYLQTRHRIEQLKQLGHSVDKVEFIVMGGTFM 175
Cdd:cd01335    4 TRGCNLN------CGFCSNPASKGRG---------------------PESPPEIEEILDIVLEAKERGVEVVILTGGEPL 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904 176 ALPeeYRDYFIRNLHDALSGHTsnniyeaikysersltkcigITIETRPDYCMKRHLSDMLTYGCTRLEIGVQSVYEDVA 255
Cdd:cd01335   57 LYP--ELAELLRRLKKELPGFE--------------------ISIETNGTLLTEELLKELKELGLDGVGVSLDSGDEEVA 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904 256 RDTN-RGHTVKAVCESFHLAKDSGFKVVAHMMPDLPNVGLERDIEQFieFFENPAFRPDGLKLYPTLVIRGTGLYELWKS 334
Cdd:cd01335  115 DKIRgSGESFKERLEALKELREAGLGLSTTLLVGLGDEDEEDDLEEL--ELLAEFRSPDRVSLFRLLPEEGTPLELAAPV 192

                 ....*.
gi 293353904 335 GRYRSY 340
Cdd:cd01335  193 VPAEKL 198
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
136-301 9.03e-14

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: 69.09  E-value: 9.03e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904  136 RAIRARYDPYLQTRHRIEQLKQLGHSVDKVEFIVMGGTFMALPEEYRDYFIRNLHDALSGhtsnniyeaikysersltkc 215
Cdd:pfam04055  15 PSIRARGKPRELSPEEILEEAKELKRLGVEVVILGGGEPLLLPDLVELLERLLKLEEAEG-------------------- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904  216 IGITIETRPDYCMKRHLSDMLTYGCTRLEIGVQSVYEDVARDTNRGHTVKAVCESFHLAKDSGFKVVAHMMPDLPNVGLE 295
Cdd:pfam04055  75 IRITLETNGTLLDEELLELLKEAGLDRVSIGLESGDDEVLKLINRGHTFEEVLEAIELLREAGIPVVTDNIVGLPGETDE 154

                  ....*.
gi 293353904  296 rDIEQF 301
Cdd:pfam04055 155 -DLEEL 159
HemN COG0635
Coproporphyrinogen III oxidase or related Fe-S oxidoreductase [Coenzyme transport and ...
101-348 3.62e-10

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


Pssm-ID: 223708 [Multi-domain]  Cd Length: 416  Bit Score: 61.90  E-value: 3.62e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904 101 HISFTGNICVYCpggpdsDFeYSTQsYTGYEPtsmrairarYDPYLQTRHR-IEQLKQLG---HSVDKVEFIvmGGTFMA 176
Cdd:COG0635   40 HIPFCVSKCPYC------DF-NSHV-TKRGQP---------VDEYLDALLEeIELVAALLggqREVKTIYFG--GGTPSL 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904 177 LPEEyrdyfirNLHDalsghtsnnIYEAIKYSERSLTKCIGITIETRPDYCMKRHLSDMLTYGCTRLEIGVQSVYEDVAR 256
Cdd:COG0635  101 LSPE-------QLER---------LLKALRELFNDLDPDAEITIEANPGTVEAEKFKALKEAGVNRISLGVQSFNDEVLK 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904 257 DTNRGHTVKAVCESFHLAKDSGFK-VVAHMMPDLPN---VGLERDIEQFIEffenpaFRPDGLKLYPTLVIRGTGLYELW 332
Cdd:COG0635  165 ALGRIHDEEEAKEAVELARKAGFTsINIDLIYGLPGqtlESLKEDLEQALE------LGPDHLSLYSLAIEPGTKFAQRK 238
                        250
                 ....*....|....*.
gi 293353904 333 KSGRyrsYSPSDLIEL 348
Cdd:COG0635  239 IKGK---ALPDEDEKA 251
PRK05799 PRK05799
oxygen-independent coproporphyrinogen III oxidase;
101-336 8.90e-10

oxygen-independent coproporphyrinogen III oxidase;


Pssm-ID: 180263 [Multi-domain]  Cd Length: 374  Bit Score: 60.38  E-value: 8.90e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904 101 HISFTGNICVYCpggpdsDFeystQSYTGYEPTSMRAIRArydpylqtrhrieQLKQLGHSVDKVEFIVM---GGTFMAL 177
Cdd:PRK05799   9 HIPFCKQKCLYC------DF----PSYSGKEDLMMEYIKA-------------LSKEIRNSTKNKKIKSIfigGGTPTYL 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904 178 PEEYrdyfirnlhdalsghtSNNIYEAIKYSerSLTKCIGITIETRPDYCMKRHLSDMLTYGCTRLEIGVQSVYEDVARD 257
Cdd:PRK05799  66 SLEA----------------LEILKETIKKL--NKKEDLEFTVEGNPGTFTEEKLKILKSMGVNRLSIGLQAWQNSLLKY 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904 258 TNRGHTVKAVCESFHLAKDSGFK-VVAHMMPDLPNvgleRDIEQFIEFFENPA-FRPDGLKLYPTLVIRGTGLYELWKSG 335
Cdd:PRK05799 128 LGRIHTFEEFLENYKLARKLGFNnINVDLMFGLPN----QTLEDWKETLEKVVeLNPEHISCYSLIIEEGTPFYNLYENG 203

                 .
gi 293353904 336 R 336
Cdd:PRK05799 204 K 204
PRK08207 PRK08207
coproporphyrinogen III oxidase; Provisional
109-352 9.33e-09

coproporphyrinogen III oxidase; Provisional


Pssm-ID: 236187 [Multi-domain]  Cd Length: 488  Bit Score: 57.58  E-value: 9.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904 109 CVYCpggpdsdfeystqSYTGYEptsMRAIRARYDPYLQTRHR-IEQ----LKQLGHSVDKVEFivMGGTFMALPEEYRD 183
Cdd:PRK08207 177 CLYC-------------SFPSYP---IKGYKGLVEPYLEALHYeIEEigkyLKEKGLKITTIYF--GGGTPTSLTAEELE 238
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904 184 YfirnlhdalsghtsnnIYEAIKYSERSLTKCIGITIET-RPDYCMKRHLSDMLTYGCTRLEIGVQSVYEDVARDTNRGH 262
Cdd:PRK08207 239 R----------------LLEEIYENFPDVKNVKEFTVEAgRPDTITEEKLEVLKKYGVDRISINPQTMNDETLKAIGRHH 302
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904 263 TVKAVCESFHLAKDSGFKVVaHMmpD----LPNVGLErDIEQFIEFFEnpAFRPDGLKLYpTLVI-RGTGLYELWKsgRY 337
Cdd:PRK08207 303 TVEDIIEKFHLAREMGFDNI-NM--DliigLPGEGLE-EVKHTLEEIE--KLNPESLTVH-TLAIkRASRLTENKE--KY 373
                        250
                 ....*....|....*
gi 293353904 338 RSYSPSDLIELVARI 352
Cdd:PRK08207 374 KVADREEIEKMMEEA 388
PRK08446 PRK08446
coproporphyrinogen III oxidase family protein;
101-280 1.13e-07

coproporphyrinogen III oxidase family protein;


Pssm-ID: 181428 [Multi-domain]  Cd Length: 350  Bit Score: 53.81  E-value: 1.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904 101 HISFTGNICVYCpggpdsdfeySTQSYT---GYEPTSMRAIrarydpYLQTRHRIEQLKqlghsVDKVE--FIvMGGTFM 175
Cdd:PRK08446   6 HIPFCESKCGYC----------AFNSYEnkhDLKKEYMQAL------CLDLKFELEQFT-----DEKIEsvFI-GGGTPS 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904 176 AL-PEEYRDYFIRnlhdaLSGHTSNNiyeaikySErsltkcigITIETRPDYCMKRHLSDMLTYGCTRLEIGVQSVYEDV 254
Cdd:PRK08446  64 TVsAKFYEPIFEI-----ISPYLSKD-------CE--------ITTEANPNSATKAWLKGMKNLGVNRISFGVQSFNEDK 123
                        170       180
                 ....*....|....*....|....*.
gi 293353904 255 ARDTNRGHTVKAVCESFHLAKDSGFK 280
Cdd:PRK08446 124 LKFLGRIHSQKQIIKAIENAKKAGFE 149
PRK08599 PRK08599
oxygen-independent coproporphyrinogen III oxidase;
101-303 1.15e-05

oxygen-independent coproporphyrinogen III oxidase;


Pssm-ID: 236309 [Multi-domain]  Cd Length: 377  Bit Score: 47.55  E-value: 1.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904 101 HISFTGNICVYCpggpdsDFE---YSTQ---SYTGYEPTSMRAIRARYDPYLQTrhrieqlkqlghsvdkveFIVMGGTF 174
Cdd:PRK08599   7 HIPFCEHICYYC------DFNkvfIKNQpvdEYLDALIKEMNTYAIRPFDKLKT------------------IYIGGGTP 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904 175 MALPEEYRDYFIRNLHDALsghtsnniyeaikyserSLTKCIGITIETRPDYCMKRHLSDMLTYGCTRLEIGVQSVYEDV 254
Cdd:PRK08599  63 TALSAEQLERLLTAIHRNL-----------------PLSGLEEFTFEANPGDLTKEKLQVLKDSGVNRISLGVQTFNDEL 125
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 293353904 255 ARDTNRGHTVKAVCESFHLAKDSGFKVVA-HMMPDLPNvgleRDIEQFIE 303
Cdd:PRK08599 126 LKKIGRTHNEEDVYEAIANAKKAGFDNISiDLIYALPG----QTIEDFKE 171
COG1244 COG1244
Uncharacterized Fe-S cluster-containing protein. MiaB family [General function prediction only] ...
155-338 1.42e-05

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


Pssm-ID: 224165 [Multi-domain]  Cd Length: 358  Bit Score: 47.39  E-value: 1.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904 155 LKQLGHSVDKVEF--------IVMGGTF---MALPEEYRDYFIRNLHDalsghtSNNIYEaikysersltkcigITIETR 223
Cdd:COG1244   85 INQFDEAYSKYEGkfdefvvkIFTSGSFldpEEVPREARRYILERISE------NDNVKE--------------VVVESR 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904 224 PDYCMKRHLSDMLTYGC---TRLEIGVQSVYEDVARDT-NRGHTVKAVCESFHLAKDSGFKVVAHMMPDLPNVGLERDIE 299
Cdd:COG1244  145 PEFIREERLEEITEILEgkiVEVAIGLETANDKIREDSiNKGFTFEDFVRAAEIIRNYGAKVKTYLLLKPPFLSEKEAIE 224
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 293353904 300 QFIEFFENPAFRPDGLKLYPTLVIRGTgLYE-LWKSGRYR 338
Cdd:COG1244  225 DVISSIVAAKPGTDTISINPTNVQKGT-LVEkLWRRGLYR 263
PRK08208 PRK08208
coproporphyrinogen III oxidase family protein;
101-340 6.24e-05

coproporphyrinogen III oxidase family protein;


Pssm-ID: 181292 [Multi-domain]  Cd Length: 430  Bit Score: 45.38  E-value: 6.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904 101 HISFTGNICVYCpggpdsdfeySTQSYTGyeptsmrAIRARYDPYLQTRhrIEQLKQLGHSVDKVEF---IVMGGTFMAL 177
Cdd:PRK08208  45 HIPFCEMRCGFC----------NLFTRTG-------ADAEFIDSYLDAL--IRQAEQVAEALAPARFasfAVGGGTPTLL 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904 178 PEEYRDYFIRNLHDALSGHTSNniyeaikysersltkcIGITIETRPDYCMKRHLSDMLTYGCTRLEIGVQSVYEDVARD 257
Cdd:PRK08208 106 NAAELEKLFDSVERVLGVDLGN----------------IPKSVETSPATTTAEKLALLAARGVNRLSIGVQSFHDSELHA 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904 258 TNRGHTVKAVCESFHLAKDSGFkvvahmmPDLpNVGLERDIE-QFIEFFENP-----AFRPDGLKLYPTLVIRGTGLYEL 331
Cdd:PRK08208 170 LHRPQKRADVHQALEWIRAAGF-------PIL-NIDLIYGIPgQTHASWMESldqalVYRPEELFLYPLYVRPLTGLGRR 241
                        250
                 ....*....|..
gi 293353904 332 ---WKSGRYRSY 340
Cdd:PRK08208 242 araWDDQRLSLY 253
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
404-540 8.30e-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: 42.26  E-value: 8.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904  404 REVGIQEIHHRVRPYQVelvrRDYVANGGWETFLSYEDpdqDILIGLLRLRKCSeetfrfelgggvsivrelHVYGSVVp 483
Cdd:pfam13673   6 SEEGIETFLEFISPEAL----RERIDEGEYFFFVAFEG---GKIVGVIALRNGG------------------HISLLFV- 59
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 293353904  484 vssrDPtKFQHQGFGMLLMEEAERIALEEHGS-GKIAVISGVGTRNYYRKMGYRLQGP 540
Cdd:pfam13673  60 ----DP-EYQGQGIGKALLEAAEKYAEKDGIKlSEVTVNASPYAVPFYEKLGFVATGP 112
PRK05904 PRK05904
coproporphyrinogen III oxidase; Provisional
219-307 1.53e-03

coproporphyrinogen III oxidase; Provisional


Pssm-ID: 235641 [Multi-domain]  Cd Length: 353  Bit Score: 40.95  E-value: 1.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904 219 TIETRPDYCMKRHLSDMLTYGCTRLEIGVQSVYEDVARDTNRGHTVKAVCESFHLAKDSG-FKVVAHMMPDLPNVGLErD 297
Cdd:PRK05904  93 TIECNPELITQSQINLLKKNKVNRISLGVQSMNNNILKQLNRTHTIQDSKEAINLLHKNGiYNISCDFLYCLPILKLK-D 171
                         90
                 ....*....|
gi 293353904 298 IEQFIEFFEN 307
Cdd:PRK05904 172 LDEVFNFILK 181
PRK06294 PRK06294
coproporphyrinogen III oxidase; Provisional
218-303 4.04e-03

coproporphyrinogen III oxidase; Provisional


Pssm-ID: 180518 [Multi-domain]  Cd Length: 370  Bit Score: 39.74  E-value: 4.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293353904 218 ITIETRPDYCMKRHLSDMLTYGCTRLEIGVQSVYEDVARDTNRGHTVKAVCESFHLAKDSGFK-VVAHMMPDLPnvglER 296
Cdd:PRK06294  92 ITLEANPENLSESYIRALALTGINRISIGVQTFDDPLLKLLGRTHSSSKAIDAVQECSEHGFSnLSIDLIYGLP----TQ 167

                 ....*..
gi 293353904 297 DIEQFIE 303
Cdd:PRK06294 168 SLSDFIV 174
 
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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