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Conserved domains on  [gi|359465533|ref|NP_001240741|]
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elongator complex protein 3 isoform 1 [Mus musculus]

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 ...
56-565 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: 751.19  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533   56 DLNKMKTKTAAKYGLASQPRLVDIIAAVPPHYRKILIPKLKAKPVRTASGIAVVAVMCKPHRCPHISftgniCIYCPGGP 135
Cdd:TIGR01211  16 DLEDLKLEVSRKYGLSKVPSNSEILNSAPDEEKKKLEPILRKKPVRTISGVAVVAVMTSPHRCPHGK-----CLYCPGGP 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533  136 DSdfEYSTQSYTGYEPTSMRAIRARYDPFLQTRHRIEQLKQLGHSVDKVEFIVMGGTFMALPEEYRDYFIRSLHDALSGH 215
Cdd:TIGR01211  91 DS--ENSPQSYTGYEPAAMRGRQNDYDPYEQVTARLEQLEQIGHPVDKVELIIMGGTFPARDLDYQEWFIKRCLNAMNGF 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533  216 TS-----NNIHEAIKYSERSFTKCVGITIETRPDYCMKRHLSDMLTYGCTRLEIGVQSVYEDVARDTNRGHTVKAACESF 290
Cdd:TIGR01211 169 DQelkgnSTLEEAIRINETSKHRCVGLTIETRPDYCREEHIDRMLKLGATRVELGVQTIYNDILERTKRGHTVRDVVEAT 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533  291 HLAKDSGFKVVTHMMPDLPNVGLERDIEQFIEFFENPAFRPDGLKLYPTLVIRGTGLYELWKSGRYRSYSPSDLIELVAR 370
Cdd:TIGR01211 249 RLLRDAGLKVVYHIMPGLPGSSFERDLEMFREIFEDPRFKPDMLKIYPTLVTRGTELYELWKRGEYKPYTTEEAVELIVE 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533  371 ILALVPPWTRVYRVQRDIPMPLVSSGVEHGNLRELAFARMKDLGIQCRDVRTREVGIQEIHHRVRPY-QVELVRRDYVAN 449
Cdd:TIGR01211 329 IKRMMPKWVRIQRIQRDIPAPLIVAGVKKSNLRELVYRRMKEHGITCRCIRCREVGHQMVKPVQPEEeNVELIVEEYAAS 408
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533  450 GGWETFLSYEDPDQDILIGLLRLRKCSEETFRfELGGGVSIVRELHVYGSVVPVSSRDPTKFQHQGFGMLLMeEAERIAR 529
Cdd:TIGR01211 409 GGTEFFLSYEDPKNDILIGFLRLRFPSEPAHR-KEVDATALVRELHVYGSEVPIGERGDDEWQHRGYGRRLL-EEAERIA 486
                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 359465533  530 EEHGSGKMAVISGVGTRNYYRKIGYRLQGPYMVKML 565
Cdd:TIGR01211 487 AEEGSEKILVISGIGVREYYRKLGYELDGPYMSKRL 522
 
Name Accession Description Interval E-value
ELP3 TIGR01211
radical SAM enzyme/protein acetyltransferase, ELP3 family; This family includes elongator ...
56-565 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: 751.19  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533   56 DLNKMKTKTAAKYGLASQPRLVDIIAAVPPHYRKILIPKLKAKPVRTASGIAVVAVMCKPHRCPHISftgniCIYCPGGP 135
Cdd:TIGR01211  16 DLEDLKLEVSRKYGLSKVPSNSEILNSAPDEEKKKLEPILRKKPVRTISGVAVVAVMTSPHRCPHGK-----CLYCPGGP 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533  136 DSdfEYSTQSYTGYEPTSMRAIRARYDPFLQTRHRIEQLKQLGHSVDKVEFIVMGGTFMALPEEYRDYFIRSLHDALSGH 215
Cdd:TIGR01211  91 DS--ENSPQSYTGYEPAAMRGRQNDYDPYEQVTARLEQLEQIGHPVDKVELIIMGGTFPARDLDYQEWFIKRCLNAMNGF 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533  216 TS-----NNIHEAIKYSERSFTKCVGITIETRPDYCMKRHLSDMLTYGCTRLEIGVQSVYEDVARDTNRGHTVKAACESF 290
Cdd:TIGR01211 169 DQelkgnSTLEEAIRINETSKHRCVGLTIETRPDYCREEHIDRMLKLGATRVELGVQTIYNDILERTKRGHTVRDVVEAT 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533  291 HLAKDSGFKVVTHMMPDLPNVGLERDIEQFIEFFENPAFRPDGLKLYPTLVIRGTGLYELWKSGRYRSYSPSDLIELVAR 370
Cdd:TIGR01211 249 RLLRDAGLKVVYHIMPGLPGSSFERDLEMFREIFEDPRFKPDMLKIYPTLVTRGTELYELWKRGEYKPYTTEEAVELIVE 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533  371 ILALVPPWTRVYRVQRDIPMPLVSSGVEHGNLRELAFARMKDLGIQCRDVRTREVGIQEIHHRVRPY-QVELVRRDYVAN 449
Cdd:TIGR01211 329 IKRMMPKWVRIQRIQRDIPAPLIVAGVKKSNLRELVYRRMKEHGITCRCIRCREVGHQMVKPVQPEEeNVELIVEEYAAS 408
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533  450 GGWETFLSYEDPDQDILIGLLRLRKCSEETFRfELGGGVSIVRELHVYGSVVPVSSRDPTKFQHQGFGMLLMeEAERIAR 529
Cdd:TIGR01211 409 GGTEFFLSYEDPKNDILIGFLRLRFPSEPAHR-KEVDATALVRELHVYGSEVPIGERGDDEWQHRGYGRRLL-EEAERIA 486
                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 359465533  530 EEHGSGKMAVISGVGTRNYYRKIGYRLQGPYMVKML 565
Cdd:TIGR01211 487 AEEGSEKILVISGIGVREYYRKLGYELDGPYMSKRL 522
ELP3 COG1243
Histone acetyltransferase, component of the RNA polymerase elongator complex [Transcription, ...
53-565 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: 738.40  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533  53 KDVDLNKMKTKTAAKYGLASQPRLVDIIAAVPPHYRkiLIPKLKAKPVRTASGIAVVAVMCKPHRCPHisftgNICIYCP 132
Cdd:COG1243   14 KKKELEDLKLEVSRKYGLSKVPRNSDILNAAPPEER--LREILRRKPVRTISGVAVVAVMTSPHGCPH-----GRCVFCP 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533 133 GGPDsdfEYSTQSYTGYEPTSMRAIRARYDPFLQTRHRIEQLKQLGHSVDKVEFIVMGGTFMALPEEYRDYFIRSLHDAL 212
Cdd:COG1243   87 GGPD---KDSPQSYTGEEPAALRAIKNRYDPYEQVRARLKQLETIGHTSDKVELIIMGGTFTALSLEYQEWFLKVALKAM 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533 213 SGHtSNNIHEAIKYSERSFTKCVGITIETRPDYCMKRHLSDMLTYGCTRLEIGVQSVYEDVARDTNRGHTVKAACESFHL 292
Cdd:COG1243  164 NDF-GYDLEEAQRKNETAELRCVGITIETRPDYIDEEHLDQMLKYGVTRVELGVQSIYDDVLERTKRGHTVEDVVEATRL 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533 293 AKDSGFKVVTHMMPDLPNVGLERDIEQFIEFFENPAFRPDGLKLYPTLVIRGTGLYELWKSGRYRSYSPSDLIELVARIL 372
Cdd:COG1243  243 LKDAGFKVGYHIMPGLPGSDFERDLESFREIFEDPRFRPDMLKIYPTLVIEGTELYEMWKRGLYKPYTTEEAVELIVEIY 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533 373 ALVPPWTRVYRVQRDIPMPLVSSGVEHGNLRELAFARMKDLGIQCRDVRTREVGIQEIHHRVRPY--QVELVRRDYVANG 450
Cdd:COG1243  323 RLEPKWVRVIRIQRDIPAELIVDGVKKSNLRELVENRMREEGIKCRCIRCREVGIVVVKNVVIPPveQILLKREEYEASG 402
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533 451 GWETFLSYEDPDQDILIGLLRLRKCSEETFRFELGGGVSIVRELHVYGSVVPVSSRdPTKFQHQGFGMLLMEEAERIARE 530
Cdd:COG1243  403 GTEIFLSYEDPKNDILIGFLRLREPSEGAHREEIDDKTAIVRELHVYGSEVPIGKR-EDEWQHRGYGRELLEEAERIARE 481
                        490       500       510
                 ....*....|....*....|....*....|....*
gi 359465533 531 EHgSGKMAVISGVGTRNYYRKIGYRLQGPYMVKML 565
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 ...
331-409 1.01e-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: 103.24  E-value: 1.01e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533  331 PDGLKLYPTLVIRGTGLYELWKSGRYRSYSPSDLIELVARILALVPPWTRVYRVQRDIPMPLVSSGVEHG-NLRELAFAR 409
Cdd:pfam16199   1 PDGVKIHPLLVLKGTPLAELYERGEYKPLSLEEYVELVADFLELLPPDIVIHRLGGDAPKELLVAPPWHLpKLRVLNLIE 80
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
108-371 2.69e-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: 2.69e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533   108 VVAVMCKPHRCPHIsftgniCIYCpggpdsdfeystqsytgYEPTSMRAIRARYdpfLQTRHR-IEQLKQLGHSVDKVEF 186
Cdd:smart00729   1 PLALYIITRGCPRR------CTFC-----------------SFPSLRGKLRSRY---LEALVReIELLAEKGEKEGLVGT 54
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533   187 IVM-GGTFMALPEEYRDYFIRSLHDALSghtsnniheaikysersFTKCVGITIETRPDYCMKRHLSDMLTYGCTRLEIG 265
Cdd:smart00729  55 VFIgGGTPTLLSPEQLEELLEAIREILG-----------------LAKDVEITIETRPDTLTEELLEALKEAGVNRVSLG 117
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533   266 VQSVYEDVARDTNRGHTVKAACESFHLAKDSGF-KVVTHMMPDLPNVGLErDIEQFIEFFEnpAFRPDGLKLYPTLVIRG 344
Cdd:smart00729 118 VQSGDDEVLKAINRGHTVEDVLEAVELLREAGPiKVSTDLIVGLPGETEE-DFEETLKLLK--ELGPDRVSIFPLSPRPG 194
                          250       260
                   ....*....|....*....|....*..
gi 359465533   345 TGLYELWKsgryrSYSPSDLIELVARI 371
Cdd:smart00729 195 TPLAKMYK-----RLKPPTKEERAELL 216
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
115-359 1.66e-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: 72.37  E-value: 1.66e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533 115 PHRCPHIsftgniCIYCPGGPDSDFEystqsytgyeptsmrairaryDPFLQTRHRIEQLKQLGHSVDKVEFIVMGGTFM 194
Cdd:cd01335    4 TRGCNLN------CGFCSNPASKGRG---------------------PESPPEIEEILDIVLEAKERGVEVVILTGGEPL 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533 195 ALPeeYRDYFIRSLHDALSGHTsnniheaikysersftkcvgITIETRPDYCMKRHLSDMLTYGCTRLEIGVQSVYEDVA 274
Cdd:cd01335   57 LYP--ELAELLRRLKKELPGFE--------------------ISIETNGTLLTEELLKELKELGLDGVGVSLDSGDEEVA 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533 275 RDTN-RGHTVKAACESFHLAKDSGFKVVTHMMPDLPNVGLERDIEQFieFFENPAFRPDGLKLYPTLVIRGTGLYELWKS 353
Cdd:cd01335  115 DKIRgSGESFKERLEALKELREAGLGLSTTLLVGLGDEDEEDDLEEL--ELLAEFRSPDRVSLFRLLPEEGTPLELAAPV 192

                 ....*.
gi 359465533 354 GRYRSY 359
Cdd:cd01335  193 VPAEKL 198
PRK05799 PRK05799
oxygen-independent coproporphyrinogen III oxidase;
120-355 6.88e-09

oxygen-independent coproporphyrinogen III oxidase;


Pssm-ID: 180263 [Multi-domain]  Cd Length: 374  Bit Score: 57.69  E-value: 6.88e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533 120 HISFTGNICIYCpggpdsDFeystQSYTGYEPTSMRAIRArydpflqtrhrieQLKQLGHSVDKVEFIVM---GGTFMAL 196
Cdd:PRK05799   9 HIPFCKQKCLYC------DF----PSYSGKEDLMMEYIKA-------------LSKEIRNSTKNKKIKSIfigGGTPTYL 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533 197 PEEYrdyfirslhdalsghtSNNIHEAIKYSerSFTKCVGITIETRPDYCMKRHLSDMLTYGCTRLEIGVQSVYEDVARD 276
Cdd:PRK05799  66 SLEA----------------LEILKETIKKL--NKKEDLEFTVEGNPGTFTEEKLKILKSMGVNRLSIGLQAWQNSLLKY 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533 277 TNRGHTVKAACESFHLAKDSGFKVVT-HMMPDLPNvgleRDIEQFIEFFENPA-FRPDGLKLYPTLVIRGTGLYELWKSG 354
Cdd:PRK05799 128 LGRIHTFEEFLENYKLARKLGFNNINvDLMFGLPN----QTLEDWKETLEKVVeLNPEHISCYSLIIEEGTPFYNLYENG 203

                 .
gi 359465533 355 R 355
Cdd:PRK05799 204 K 204
 
Name Accession Description Interval E-value
ELP3 TIGR01211
radical SAM enzyme/protein acetyltransferase, ELP3 family; This family includes elongator ...
56-565 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: 751.19  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533   56 DLNKMKTKTAAKYGLASQPRLVDIIAAVPPHYRKILIPKLKAKPVRTASGIAVVAVMCKPHRCPHISftgniCIYCPGGP 135
Cdd:TIGR01211  16 DLEDLKLEVSRKYGLSKVPSNSEILNSAPDEEKKKLEPILRKKPVRTISGVAVVAVMTSPHRCPHGK-----CLYCPGGP 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533  136 DSdfEYSTQSYTGYEPTSMRAIRARYDPFLQTRHRIEQLKQLGHSVDKVEFIVMGGTFMALPEEYRDYFIRSLHDALSGH 215
Cdd:TIGR01211  91 DS--ENSPQSYTGYEPAAMRGRQNDYDPYEQVTARLEQLEQIGHPVDKVELIIMGGTFPARDLDYQEWFIKRCLNAMNGF 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533  216 TS-----NNIHEAIKYSERSFTKCVGITIETRPDYCMKRHLSDMLTYGCTRLEIGVQSVYEDVARDTNRGHTVKAACESF 290
Cdd:TIGR01211 169 DQelkgnSTLEEAIRINETSKHRCVGLTIETRPDYCREEHIDRMLKLGATRVELGVQTIYNDILERTKRGHTVRDVVEAT 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533  291 HLAKDSGFKVVTHMMPDLPNVGLERDIEQFIEFFENPAFRPDGLKLYPTLVIRGTGLYELWKSGRYRSYSPSDLIELVAR 370
Cdd:TIGR01211 249 RLLRDAGLKVVYHIMPGLPGSSFERDLEMFREIFEDPRFKPDMLKIYPTLVTRGTELYELWKRGEYKPYTTEEAVELIVE 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533  371 ILALVPPWTRVYRVQRDIPMPLVSSGVEHGNLRELAFARMKDLGIQCRDVRTREVGIQEIHHRVRPY-QVELVRRDYVAN 449
Cdd:TIGR01211 329 IKRMMPKWVRIQRIQRDIPAPLIVAGVKKSNLRELVYRRMKEHGITCRCIRCREVGHQMVKPVQPEEeNVELIVEEYAAS 408
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533  450 GGWETFLSYEDPDQDILIGLLRLRKCSEETFRfELGGGVSIVRELHVYGSVVPVSSRDPTKFQHQGFGMLLMeEAERIAR 529
Cdd:TIGR01211 409 GGTEFFLSYEDPKNDILIGFLRLRFPSEPAHR-KEVDATALVRELHVYGSEVPIGERGDDEWQHRGYGRRLL-EEAERIA 486
                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 359465533  530 EEHGSGKMAVISGVGTRNYYRKIGYRLQGPYMVKML 565
Cdd:TIGR01211 487 AEEGSEKILVISGIGVREYYRKLGYELDGPYMSKRL 522
ELP3 COG1243
Histone acetyltransferase, component of the RNA polymerase elongator complex [Transcription, ...
53-565 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: 738.40  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533  53 KDVDLNKMKTKTAAKYGLASQPRLVDIIAAVPPHYRkiLIPKLKAKPVRTASGIAVVAVMCKPHRCPHisftgNICIYCP 132
Cdd:COG1243   14 KKKELEDLKLEVSRKYGLSKVPRNSDILNAAPPEER--LREILRRKPVRTISGVAVVAVMTSPHGCPH-----GRCVFCP 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533 133 GGPDsdfEYSTQSYTGYEPTSMRAIRARYDPFLQTRHRIEQLKQLGHSVDKVEFIVMGGTFMALPEEYRDYFIRSLHDAL 212
Cdd:COG1243   87 GGPD---KDSPQSYTGEEPAALRAIKNRYDPYEQVRARLKQLETIGHTSDKVELIIMGGTFTALSLEYQEWFLKVALKAM 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533 213 SGHtSNNIHEAIKYSERSFTKCVGITIETRPDYCMKRHLSDMLTYGCTRLEIGVQSVYEDVARDTNRGHTVKAACESFHL 292
Cdd:COG1243  164 NDF-GYDLEEAQRKNETAELRCVGITIETRPDYIDEEHLDQMLKYGVTRVELGVQSIYDDVLERTKRGHTVEDVVEATRL 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533 293 AKDSGFKVVTHMMPDLPNVGLERDIEQFIEFFENPAFRPDGLKLYPTLVIRGTGLYELWKSGRYRSYSPSDLIELVARIL 372
Cdd:COG1243  243 LKDAGFKVGYHIMPGLPGSDFERDLESFREIFEDPRFRPDMLKIYPTLVIEGTELYEMWKRGLYKPYTTEEAVELIVEIY 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533 373 ALVPPWTRVYRVQRDIPMPLVSSGVEHGNLRELAFARMKDLGIQCRDVRTREVGIQEIHHRVRPY--QVELVRRDYVANG 450
Cdd:COG1243  323 RLEPKWVRVIRIQRDIPAELIVDGVKKSNLRELVENRMREEGIKCRCIRCREVGIVVVKNVVIPPveQILLKREEYEASG 402
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533 451 GWETFLSYEDPDQDILIGLLRLRKCSEETFRFELGGGVSIVRELHVYGSVVPVSSRdPTKFQHQGFGMLLMEEAERIARE 530
Cdd:COG1243  403 GTEIFLSYEDPKNDILIGFLRLREPSEGAHREEIDDKTAIVRELHVYGSEVPIGKR-EDEWQHRGYGRELLEEAERIARE 481
                        490       500       510
                 ....*....|....*....|....*....|....*
gi 359465533 531 EHgSGKMAVISGVGTRNYYRKIGYRLQGPYMVKML 565
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 ...
331-409 1.01e-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: 103.24  E-value: 1.01e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533  331 PDGLKLYPTLVIRGTGLYELWKSGRYRSYSPSDLIELVARILALVPPWTRVYRVQRDIPMPLVSSGVEHG-NLRELAFAR 409
Cdd:pfam16199   1 PDGVKIHPLLVLKGTPLAELYERGEYKPLSLEEYVELVADFLELLPPDIVIHRLGGDAPKELLVAPPWHLpKLRVLNLIE 80
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
108-371 2.69e-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: 2.69e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533   108 VVAVMCKPHRCPHIsftgniCIYCpggpdsdfeystqsytgYEPTSMRAIRARYdpfLQTRHR-IEQLKQLGHSVDKVEF 186
Cdd:smart00729   1 PLALYIITRGCPRR------CTFC-----------------SFPSLRGKLRSRY---LEALVReIELLAEKGEKEGLVGT 54
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533   187 IVM-GGTFMALPEEYRDYFIRSLHDALSghtsnniheaikysersFTKCVGITIETRPDYCMKRHLSDMLTYGCTRLEIG 265
Cdd:smart00729  55 VFIgGGTPTLLSPEQLEELLEAIREILG-----------------LAKDVEITIETRPDTLTEELLEALKEAGVNRVSLG 117
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533   266 VQSVYEDVARDTNRGHTVKAACESFHLAKDSGF-KVVTHMMPDLPNVGLErDIEQFIEFFEnpAFRPDGLKLYPTLVIRG 344
Cdd:smart00729 118 VQSGDDEVLKAINRGHTVEDVLEAVELLREAGPiKVSTDLIVGLPGETEE-DFEETLKLLK--ELGPDRVSIFPLSPRPG 194
                          250       260
                   ....*....|....*....|....*..
gi 359465533   345 TGLYELWKsgryrSYSPSDLIELVARI 371
Cdd:smart00729 195 TPLAKMYK-----RLKPPTKEERAELL 216
YhcC COG1242
Radical SAM superfamily enzyme [General function prediction only];
235-392 7.21e-21

Radical SAM superfamily enzyme [General function prediction only];


Pssm-ID: 224163 [Multi-domain]  Cd Length: 312  Bit Score: 93.54  E-value: 7.21e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533 235 VGITIETRPDyCMKRHLSDMLTYGCTR----LEIGVQSVYEDVARDTNRGHTVKAACESFHLAKDSGFKVVTHMMPDLPN 310
Cdd:COG1242  116 VGLSIGTRPD-CLPDDVLDLLAEYNKRyevwVELGLQTAHDKTLKRINRGHDFACYVDAVKRLRKRGIKVCTHLINGLPG 194
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533 311 VGLERDIEQFIEFFENPAfrpDGLKLYPTLVIRGTGLYELWKSGRYRSYSPSDLIELVARILALVPPWTRVYRVQRDIPM 390
Cdd:COG1242  195 ETRDEMLETAKIVAELGV---DGIKLHPLHVVKGTPMEKMYEKGRLKFLSLEEYVELVCDQLEHLPPEVVIHRITGDAPR 271

                 ..
gi 359465533 391 PL 392
Cdd:COG1242  272 DT 273
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
115-359 1.66e-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: 72.37  E-value: 1.66e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533 115 PHRCPHIsftgniCIYCPGGPDSDFEystqsytgyeptsmrairaryDPFLQTRHRIEQLKQLGHSVDKVEFIVMGGTFM 194
Cdd:cd01335    4 TRGCNLN------CGFCSNPASKGRG---------------------PESPPEIEEILDIVLEAKERGVEVVILTGGEPL 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533 195 ALPeeYRDYFIRSLHDALSGHTsnniheaikysersftkcvgITIETRPDYCMKRHLSDMLTYGCTRLEIGVQSVYEDVA 274
Cdd:cd01335   57 LYP--ELAELLRRLKKELPGFE--------------------ISIETNGTLLTEELLKELKELGLDGVGVSLDSGDEEVA 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533 275 RDTN-RGHTVKAACESFHLAKDSGFKVVTHMMPDLPNVGLERDIEQFieFFENPAFRPDGLKLYPTLVIRGTGLYELWKS 353
Cdd:cd01335  115 DKIRgSGESFKERLEALKELREAGLGLSTTLLVGLGDEDEEDDLEEL--ELLAEFRSPDRVSLFRLLPEEGTPLELAAPV 192

                 ....*.
gi 359465533 354 GRYRSY 359
Cdd:cd01335  193 VPAEKL 198
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
155-320 1.87e-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: 68.32  E-value: 1.87e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533  155 RAIRARYDPFLQTRHRIEQLKQLGHSVDKVEFIVMGGTFMALPEEYRDYFIRSLHDALSGHTsnniheaikysersftkc 234
Cdd:pfam04055  15 PSIRARGKPRELSPEEILEEAKELKRLGVEVVILGGGEPLLLPDLVELLERLLKLEEAEGIR------------------ 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533  235 vgITIETRPDYCMKRHLSDMLTYGCTRLEIGVQSVYEDVARDTNRGHTVKAACESFHLAKDSGFKVVTHMMPDLPNVGLE 314
Cdd:pfam04055  77 --ITLETNGTLLDEELLELLKEAGLDRVSIGLESGDDEVLKLINRGHTFEEVLEAIELLREAGIPVVTDNIVGLPGETDE 154

                  ....*.
gi 359465533  315 rDIEQF 320
Cdd:pfam04055 155 -DLEEL 159
HemN COG0635
Coproporphyrinogen III oxidase or related Fe-S oxidoreductase [Coenzyme transport and ...
120-367 3.51e-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: 3.51e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533 120 HISFTGNICIYCpggpdsDF-------EYSTQSYTGYEPTSMRAIRARYDPflqtRHRIEQLkqlghsvdkveFIVmGGT 192
Cdd:COG0635   40 HIPFCVSKCPYC------DFnshvtkrGQPVDEYLDALLEEIELVAALLGG----QREVKTI-----------YFG-GGT 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533 193 FMALPEEYRDYFIRSLHDALsghtsnniheaikyseRSFTKCVGITIETRPDYCMKRHLSDMLTYGCTRLEIGVQSVYED 272
Cdd:COG0635   98 PSLLSPEQLERLLKALRELF----------------NDLDPDAEITIEANPGTVEAEKFKALKEAGVNRISLGVQSFNDE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533 273 VARDTNRGHTVKAACESFHLAKDSGFK-VVTHMMPDLPN---VGLERDIEQFIEffenpaFRPDGLKLYPTLVIRGTGLY 348
Cdd:COG0635  162 VLKALGRIHDEEEAKEAVELARKAGFTsINIDLIYGLPGqtlESLKEDLEQALE------LGPDHLSLYSLAIEPGTKFA 235
                        250
                 ....*....|....*....
gi 359465533 349 ELWKSGRyrsYSPSDLIEL 367
Cdd:COG0635  236 QRKIKGK---ALPDEDEKA 251
PRK05799 PRK05799
oxygen-independent coproporphyrinogen III oxidase;
120-355 6.88e-09

oxygen-independent coproporphyrinogen III oxidase;


Pssm-ID: 180263 [Multi-domain]  Cd Length: 374  Bit Score: 57.69  E-value: 6.88e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533 120 HISFTGNICIYCpggpdsDFeystQSYTGYEPTSMRAIRArydpflqtrhrieQLKQLGHSVDKVEFIVM---GGTFMAL 196
Cdd:PRK05799   9 HIPFCKQKCLYC------DF----PSYSGKEDLMMEYIKA-------------LSKEIRNSTKNKKIKSIfigGGTPTYL 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533 197 PEEYrdyfirslhdalsghtSNNIHEAIKYSerSFTKCVGITIETRPDYCMKRHLSDMLTYGCTRLEIGVQSVYEDVARD 276
Cdd:PRK05799  66 SLEA----------------LEILKETIKKL--NKKEDLEFTVEGNPGTFTEEKLKILKSMGVNRLSIGLQAWQNSLLKY 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533 277 TNRGHTVKAACESFHLAKDSGFKVVT-HMMPDLPNvgleRDIEQFIEFFENPA-FRPDGLKLYPTLVIRGTGLYELWKSG 354
Cdd:PRK05799 128 LGRIHTFEEFLENYKLARKLGFNNINvDLMFGLPN----QTLEDWKETLEKVVeLNPEHISCYSLIIEEGTPFYNLYENG 203

                 .
gi 359465533 355 R 355
Cdd:PRK05799 204 K 204
PRK08207 PRK08207
coproporphyrinogen III oxidase; Provisional
128-371 2.60e-08

coproporphyrinogen III oxidase; Provisional


Pssm-ID: 236187 [Multi-domain]  Cd Length: 488  Bit Score: 56.43  E-value: 2.60e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533 128 CIYCpggpdsdfeystqSYTGYEptsMRAIRARYDPFLQTRHR-IEQ----LKQLGHSVDKVEFivMGGTFMALPEEYRD 202
Cdd:PRK08207 177 CLYC-------------SFPSYP---IKGYKGLVEPYLEALHYeIEEigkyLKEKGLKITTIYF--GGGTPTSLTAEELE 238
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533 203 YFIRSLHDALSGhtSNNIHEaikysersftkcvgITIET-RPDYCMKRHLSDMLTYGCTRLEIGVQSVYEDVARDTNRGH 281
Cdd:PRK08207 239 RLLEEIYENFPD--VKNVKE--------------FTVEAgRPDTITEEKLEVLKKYGVDRISINPQTMNDETLKAIGRHH 302
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533 282 TVKAACESFHLAKDSGFKVVtHMmpD----LPNVGLErDIEQFIEFFEnpAFRPDGLKLYpTLVI-RGTGLYELWKsgRY 356
Cdd:PRK08207 303 TVEDIIEKFHLAREMGFDNI-NM--DliigLPGEGLE-EVKHTLEEIE--KLNPESLTVH-TLAIkRASRLTENKE--KY 373
                        250
                 ....*....|....*
gi 359465533 357 RSYSPSDLIELVARI 371
Cdd:PRK08207 374 KVADREEIEKMMEEA 388
PRK08446 PRK08446
coproporphyrinogen III oxidase family protein;
120-299 7.05e-08

coproporphyrinogen III oxidase family protein;


Pssm-ID: 181428 [Multi-domain]  Cd Length: 350  Bit Score: 54.58  E-value: 7.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533 120 HISFTGNICIYCpggpdsdfeySTQSYT---GYEPTSMRAIRarydpfLQTRHRIEQLKqlghsVDKVE--FIvMGGTFM 194
Cdd:PRK08446   6 HIPFCESKCGYC----------AFNSYEnkhDLKKEYMQALC------LDLKFELEQFT-----DEKIEsvFI-GGGTPS 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533 195 AL-PEEYRDYFIRslhdaLSGHTSNNIHeaikysersftkcvgITIETRPDYCMKRHLSDMLTYGCTRLEIGVQSVYEDV 273
Cdd:PRK08446  64 TVsAKFYEPIFEI-----ISPYLSKDCE---------------ITTEANPNSATKAWLKGMKNLGVNRISFGVQSFNEDK 123
                        170       180
                 ....*....|....*....|....*.
gi 359465533 274 ARDTNRGHTVKAACESFHLAKDSGFK 299
Cdd:PRK08446 124 LKFLGRIHSQKQIIKAIENAKKAGFE 149
PRK08599 PRK08599
oxygen-independent coproporphyrinogen III oxidase;
120-322 1.88e-05

oxygen-independent coproporphyrinogen III oxidase;


Pssm-ID: 236309 [Multi-domain]  Cd Length: 377  Bit Score: 47.17  E-value: 1.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533 120 HISFTGNICIYCpggpdsDFE---YSTQ---SYTGYEPTSMRAIRARYDPFLQTrhrieqlkqlghsvdkveFIVMGGTF 193
Cdd:PRK08599   7 HIPFCEHICYYC------DFNkvfIKNQpvdEYLDALIKEMNTYAIRPFDKLKT------------------IYIGGGTP 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533 194 MALPEEYRDYFIRSLHDALSghtsnniheaikysersFTKCVGITIETRPDYCMKRHLSDMLTYGCTRLEIGVQSVYEDV 273
Cdd:PRK08599  63 TALSAEQLERLLTAIHRNLP-----------------LSGLEEFTFEANPGDLTKEKLQVLKDSGVNRISLGVQTFNDEL 125
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 359465533 274 ARDTNRGHTVKAACESFHLAKDSGFKVVT-HMMPDLPNvgleRDIEQFIE 322
Cdd:PRK08599 126 LKKIGRTHNEEDVYEAIANAKKAGFDNISiDLIYALPG----QTIEDFKE 171
COG1244 COG1244
Uncharacterized Fe-S cluster-containing protein. MiaB family [General function prediction only] ...
174-357 3.99e-05

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


Pssm-ID: 224165 [Multi-domain]  Cd Length: 358  Bit Score: 45.85  E-value: 3.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533 174 LKQLGHSVDKVEF--------IVMGGTF---MALPEEYRDYFIRSLHDalsghtSNNIHEaikysersftkcvgITIETR 242
Cdd:COG1244   85 INQFDEAYSKYEGkfdefvvkIFTSGSFldpEEVPREARRYILERISE------NDNVKE--------------VVVESR 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533 243 PDYCMKRHLSDMLTYGC---TRLEIGVQSVYEDVARDT-NRGHTVKAACESFHLAKDSGFKVVTHMMPDLPNVGLERDIE 318
Cdd:COG1244  145 PEFIREERLEEITEILEgkiVEVAIGLETANDKIREDSiNKGFTFEDFVRAAEIIRNYGAKVKTYLLLKPPFLSEKEAIE 224
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 359465533 319 QFIEFFENPAFRPDGLKLYPTLVIRGTgLYE-LWKSGRYR 357
Cdd:COG1244  225 DVISSIVAAKPGTDTISINPTNVQKGT-LVEkLWRRGLYR 263
PRK08208 PRK08208
coproporphyrinogen III oxidase family protein;
171-359 1.45e-04

coproporphyrinogen III oxidase family protein;


Pssm-ID: 181292 [Multi-domain]  Cd Length: 430  Bit Score: 44.23  E-value: 1.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533 171 IEQLKQLGHSVDKVEF---IVMGGTFMALPEEYRDYFIRSLHDALSGHTSNniheaikysersftkcVGITIETRPDYCM 247
Cdd:PRK08208  77 IRQAEQVAEALAPARFasfAVGGGTPTLLNAAELEKLFDSVERVLGVDLGN----------------IPKSVETSPATTT 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533 248 KRHLSDMLTYGCTRLEIGVQSVYEDVARDTNRGHTVKAACESFHLAKDSGFkvvthmmPDLpNVGLERDIE-QFIEFFEN 326
Cdd:PRK08208 141 AEKLALLAARGVNRLSIGVQSFHDSELHALHRPQKRADVHQALEWIRAAGF-------PIL-NIDLIYGIPgQTHASWME 212
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 359465533 327 P-----AFRPDGLKLYPTLVIRGTGLYEL---WKSGRYRSY 359
Cdd:PRK08208 213 SldqalVYRPEELFLYPLYVRPLTGLGRRaraWDDQRLSLY 253
PRK06294 PRK06294
coproporphyrinogen III oxidase; Provisional
237-322 1.12e-03

coproporphyrinogen III oxidase; Provisional


Pssm-ID: 180518 [Multi-domain]  Cd Length: 370  Bit Score: 41.28  E-value: 1.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533 237 ITIETRPDYCMKRHLSDMLTYGCTRLEIGVQSVYEDVARDTNRGHTVKAACESFHLAKDSGFKVVT-HMMPDLPnvglER 315
Cdd:PRK06294  92 ITLEANPENLSESYIRALALTGINRISIGVQTFDDPLLKLLGRTHSSSKAIDAVQECSEHGFSNLSiDLIYGLP----TQ 167

                 ....*..
gi 359465533 316 DIEQFIE 322
Cdd:PRK06294 168 SLSDFIV 174
PRK05904 PRK05904
coproporphyrinogen III oxidase; Provisional
238-326 3.51e-03

coproporphyrinogen III oxidase; Provisional


Pssm-ID: 235641 [Multi-domain]  Cd Length: 353  Bit Score: 39.79  E-value: 3.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465533 238 TIETRPDYCMKRHLSDMLTYGCTRLEIGVQSVYEDVARDTNRGHTVKAACESFHLAKDSGFKVVT-HMMPDLPNVGLErD 316
Cdd:PRK05904  93 TIECNPELITQSQINLLKKNKVNRISLGVQSMNNNILKQLNRTHTIQDSKEAINLLHKNGIYNIScDFLYCLPILKLK-D 171
                         90
                 ....*....|
gi 359465533 317 IEQFIEFFEN 326
Cdd:PRK05904 172 LDEVFNFILK 181
 
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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