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Conserved domains on  [gi|33469023|ref|NP_083087|]
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Protein Classification

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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: 750.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469023    37 DLNKMKTKTAAKYGLASQPRLVDIIAAVPPHYRKILIPKLKAKPVRTASGIAVVAVMCKPHRCPHISftgniCIYCPGGP 116
Cdd:TIGR01211  16 DLEDLKLEVSRKYGLSKVPSNSEILNSAPDEEKKKLEPILRKKPVRTISGVAVVAVMTSPHRCPHGK-----CLYCPGGP 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469023   117 DSdfEYSTQSYTGYEPTSMRAIRARYDPFLQTRHRIEQLKQLGHSVDKVEFIVMGGTFMALPEEYRDYFIRSLHDALSGH 196
Cdd:TIGR01211  91 DS--ENSPQSYTGYEPAAMRGRQNDYDPYEQVTARLEQLEQIGHPVDKVELIIMGGTFPARDLDYQEWFIKRCLNAMNGF 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469023   197 TS-----NNIHEAIKYSERSFTKCVGITIETRPDYCMKRHLSDMLTYGCTRLEIGVQSVYEDVARDTNRGHTVKAACESF 271
Cdd:TIGR01211 169 DQelkgnSTLEEAIRINETSKHRCVGLTIETRPDYCREEHIDRMLKLGATRVELGVQTIYNDILERTKRGHTVRDVVEAT 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469023   272 HLAKDSGFKVVTHMMPDLPNVGLERDIEQFIEFFENPAFRPDGLKLYPTLVIRGTGLYELWKSGRYRSYSPSDLIELVAR 351
Cdd:TIGR01211 249 RLLRDAGLKVVYHIMPGLPGSSFERDLEMFREIFEDPRFKPDMLKIYPTLVTRGTELYELWKRGEYKPYTTEEAVELIVE 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469023   352 ILALVPPWTRVYRVQRDIPMPLVSSGVEHGNLRELAFARMKDLGIQCRDVRTREVGIQEIHHRVRPY-QVELVRRDYVAN 430
Cdd:TIGR01211 329 IKRMMPKWVRIQRIQRDIPAPLIVAGVKKSNLRELVYRRMKEHGITCRCIRCREVGHQMVKPVQPEEeNVELIVEEYAAS 408
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469023   431 GGWETFLSYEDPDQDILIGLLRLRKCSEETFRfELGGGVSIVRELHVYGSVVPVSSRDPTKFQHQGFGMLLMeEAERIAR 510
Cdd:TIGR01211 409 GGTEFFLSYEDPKNDILIGFLRLRFPSEPAHR-KEVDATALVRELHVYGSEVPIGERGDDEWQHRGYGRRLL-EEAERIA 486
                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 33469023   511 EEHGSGKMAVISGVGTRNYYRKIGYRLQGPYMVKML 546
Cdd:TIGR01211 487 AEEGSEKILVISGIGVREYYRKLGYELDGPYMSKRL 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: 750.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469023    37 DLNKMKTKTAAKYGLASQPRLVDIIAAVPPHYRKILIPKLKAKPVRTASGIAVVAVMCKPHRCPHISftgniCIYCPGGP 116
Cdd:TIGR01211  16 DLEDLKLEVSRKYGLSKVPSNSEILNSAPDEEKKKLEPILRKKPVRTISGVAVVAVMTSPHRCPHGK-----CLYCPGGP 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469023   117 DSdfEYSTQSYTGYEPTSMRAIRARYDPFLQTRHRIEQLKQLGHSVDKVEFIVMGGTFMALPEEYRDYFIRSLHDALSGH 196
Cdd:TIGR01211  91 DS--ENSPQSYTGYEPAAMRGRQNDYDPYEQVTARLEQLEQIGHPVDKVELIIMGGTFPARDLDYQEWFIKRCLNAMNGF 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469023   197 TS-----NNIHEAIKYSERSFTKCVGITIETRPDYCMKRHLSDMLTYGCTRLEIGVQSVYEDVARDTNRGHTVKAACESF 271
Cdd:TIGR01211 169 DQelkgnSTLEEAIRINETSKHRCVGLTIETRPDYCREEHIDRMLKLGATRVELGVQTIYNDILERTKRGHTVRDVVEAT 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469023   272 HLAKDSGFKVVTHMMPDLPNVGLERDIEQFIEFFENPAFRPDGLKLYPTLVIRGTGLYELWKSGRYRSYSPSDLIELVAR 351
Cdd:TIGR01211 249 RLLRDAGLKVVYHIMPGLPGSSFERDLEMFREIFEDPRFKPDMLKIYPTLVTRGTELYELWKRGEYKPYTTEEAVELIVE 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469023   352 ILALVPPWTRVYRVQRDIPMPLVSSGVEHGNLRELAFARMKDLGIQCRDVRTREVGIQEIHHRVRPY-QVELVRRDYVAN 430
Cdd:TIGR01211 329 IKRMMPKWVRIQRIQRDIPAPLIVAGVKKSNLRELVYRRMKEHGITCRCIRCREVGHQMVKPVQPEEeNVELIVEEYAAS 408
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469023   431 GGWETFLSYEDPDQDILIGLLRLRKCSEETFRfELGGGVSIVRELHVYGSVVPVSSRDPTKFQHQGFGMLLMeEAERIAR 510
Cdd:TIGR01211 409 GGTEFFLSYEDPKNDILIGFLRLRFPSEPAHR-KEVDATALVRELHVYGSEVPIGERGDDEWQHRGYGRRLL-EEAERIA 486
                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 33469023   511 EEHGSGKMAVISGVGTRNYYRKIGYRLQGPYMVKML 546
Cdd:TIGR01211 487 AEEGSEKILVISGIGVREYYRKLGYELDGPYMSKRL 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: 737.63  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469023  34 KDVDLNKMKTKTAAKYGLASQPRLVDIIAAVPPHYRkiLIPKLKAKPVRTASGIAVVAVMCKPHRCPHisftgNICIYCP 113
Cdd:COG1243  14 KKKELEDLKLEVSRKYGLSKVPRNSDILNAAPPEER--LREILRRKPVRTISGVAVVAVMTSPHGCPH-----GRCVFCP 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469023 114 GGPDsdfEYSTQSYTGYEPTSMRAIRARYDPFLQTRHRIEQLKQLGHSVDKVEFIVMGGTFMALPEEYRDYFIRSLHDAL 193
Cdd:COG1243  87 GGPD---KDSPQSYTGEEPAALRAIKNRYDPYEQVRARLKQLETIGHTSDKVELIIMGGTFTALSLEYQEWFLKVALKAM 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469023 194 SGHtSNNIHEAIKYSERSFTKCVGITIETRPDYCMKRHLSDMLTYGCTRLEIGVQSVYEDVARDTNRGHTVKAACESFHL 273
Cdd:COG1243 164 NDF-GYDLEEAQRKNETAELRCVGITIETRPDYIDEEHLDQMLKYGVTRVELGVQSIYDDVLERTKRGHTVEDVVEATRL 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469023 274 AKDSGFKVVTHMMPDLPNVGLERDIEQFIEFFENPAFRPDGLKLYPTLVIRGTGLYELWKSGRYRSYSPSDLIELVARIL 353
Cdd:COG1243 243 LKDAGFKVGYHIMPGLPGSDFERDLESFREIFEDPRFRPDMLKIYPTLVIEGTELYEMWKRGLYKPYTTEEAVELIVEIY 322
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469023 354 ALVPPWTRVYRVQRDIPMPLVSSGVEHGNLRELAFARMKDLGIQCRDVRTREVGIQEIHHRVRPY--QVELVRRDYVANG 431
Cdd:COG1243 323 RLEPKWVRVIRIQRDIPAELIVDGVKKSNLRELVENRMREEGIKCRCIRCREVGIVVVKNVVIPPveQILLKREEYEASG 402
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469023 432 GWETFLSYEDPDQDILIGLLRLRKCSEETFRFELGGGVSIVRELHVYGSVVPVSSRdPTKFQHQGFGMLLMEEAERIARE 511
Cdd:COG1243 403 GTEIFLSYEDPKNDILIGFLRLREPSEGAHREEIDDKTAIVRELHVYGSEVPIGKR-EDEWQHRGYGRELLEEAERIARE 481
                       490       500       510
                ....*....|....*....|....*....|....*
gi 33469023 512 EHgSGKMAVISGVGTRNYYRKIGYRLQGPYMVKML 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 1.47e-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: 102.86  E-value: 1.47e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469023   312 PDGLKLYPTLVIRGTGLYELWKSGRYRSYSPSDLIELVARILALVPPWTRVYRVQRDIPMPLVSSGVEHG-NLRELAFAR 390
Cdd:pfam16199   1 PDGVKIHPLLVLKGTPLAELYERGEYKPLSLEEYVELVADFLELLPPDIVIHRLGGDAPKELLVAPPWHLpKLRVLNLIE 80
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
89-352 4.10e-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: 103.25  E-value: 4.10e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469023     89 VVAVMCKPHRCPHIsftgniCIYCpggpdsdfeystqsytgYEPTSMRAIRARYdpfLQTRHR-IEQLKQLGHSVDKVEF 167
Cdd:smart00729   1 PLALYIITRGCPRR------CTFC-----------------SFPSLRGKLRSRY---LEALVReIELLAEKGEKEGLVGT 54
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469023    168 IVM-GGTFMALPEEYRDYFIRSLHDALSghtsnniheaikysersFTKCVGITIETRPDYCMKRHLSDMLTYGCTRLEIG 246
Cdd:smart00729  55 VFIgGGTPTLLSPEQLEELLEAIREILG-----------------LAKDVEITIETRPDTLTEELLEALKEAGVNRVSLG 117
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469023    247 VQSVYEDVARDTNRGHTVKAACESFHLAKDSGF-KVVTHMMPDLPNVGLErDIEQFIEFFEnpAFRPDGLKLYPTLVIRG 325
Cdd:smart00729 118 VQSGDDEVLKAINRGHTVEDVLEAVELLREAGPiKVSTDLIVGLPGETEE-DFEETLKLLK--ELGPDRVSIFPLSPRPG 194
                          250       260
                   ....*....|....*....|....*..
gi 33469023    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 2.73e-14

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


Pssm-ID: 100105 [Multi-domain]  Cd Length: 204  Bit Score: 71.60  E-value: 2.73e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469023  96 PHRCPHIsftgniCIYCPGGPDSDFEystqsytgyeptsmrairaryDPFLQTRHRIEQLKQLGHSVDKVEFIVMGGTFM 175
Cdd:cd01335   4 TRGCNLN------CGFCSNPASKGRG---------------------PESPPEIEEILDIVLEAKERGVEVVILTGGEPL 56
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469023 176 ALPeeYRDYFIRSLHDALSGHTsnniheaikysersftkcvgITIETRPDYCMKRHLSDMLTYGCTRLEIGVQSVYEDVA 255
Cdd:cd01335  57 LYP--ELAELLRRLKKELPGFE--------------------ISIETNGTLLTEELLKELKELGLDGVGVSLDSGDEEVA 114
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469023 256 RDTN-RGHTVKAACESFHLAKDSGFKVVTHMMPDLPNVGLERDIEQFieFFENPAFRPDGLKLYPTLVIRGTGLYELWKS 334
Cdd:cd01335 115 DKIRgSGESFKERLEALKELREAGLGLSTTLLVGLGDEDEEDDLEEL--ELLAEFRSPDRVSLFRLLPEEGTPLELAAPV 192

                ....*.
gi 33469023 335 GRYRSY 340
Cdd:cd01335 193 VPAEKL 198
PRK05799 PRK05799
oxygen-independent coproporphyrinogen III oxidase;
101-336 6.52e-09

oxygen-independent coproporphyrinogen III oxidase;


Pssm-ID: 180263 [Multi-domain]  Cd Length: 374  Bit Score: 57.69  E-value: 6.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469023  101 HISFTGNICIYCpggpdsDFeystQSYTGYEPTSMRAIRArydpflqtrhrieQLKQLGHSVDKVEFIVM---GGTFMAL 177
Cdd:PRK05799   9 HIPFCKQKCLYC------DF----PSYSGKEDLMMEYIKA-------------LSKEIRNSTKNKKIKSIfigGGTPTYL 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469023  178 PEEYrdyfirslhdalsghtSNNIHEAIKYSerSFTKCVGITIETRPDYCMKRHLSDMLTYGCTRLEIGVQSVYEDVARD 257
Cdd:PRK05799  66 SLEA----------------LEILKETIKKL--NKKEDLEFTVEGNPGTFTEEKLKILKSMGVNRLSIGLQAWQNSLLKY 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469023  258 TNRGHTVKAACESFHLAKDSGFKVVT-HMMPDLPNvgleRDIEQFIEFFENPA-FRPDGLKLYPTLVIRGTGLYELWKSG 335
Cdd:PRK05799 128 LGRIHTFEEFLENYKLARKLGFNNINvDLMFGLPN----QTLEDWKETLEKVVeLNPEHISCYSLIIEEGTPFYNLYENG 203

                 .
gi 33469023  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: 750.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469023    37 DLNKMKTKTAAKYGLASQPRLVDIIAAVPPHYRKILIPKLKAKPVRTASGIAVVAVMCKPHRCPHISftgniCIYCPGGP 116
Cdd:TIGR01211  16 DLEDLKLEVSRKYGLSKVPSNSEILNSAPDEEKKKLEPILRKKPVRTISGVAVVAVMTSPHRCPHGK-----CLYCPGGP 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469023   117 DSdfEYSTQSYTGYEPTSMRAIRARYDPFLQTRHRIEQLKQLGHSVDKVEFIVMGGTFMALPEEYRDYFIRSLHDALSGH 196
Cdd:TIGR01211  91 DS--ENSPQSYTGYEPAAMRGRQNDYDPYEQVTARLEQLEQIGHPVDKVELIIMGGTFPARDLDYQEWFIKRCLNAMNGF 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469023   197 TS-----NNIHEAIKYSERSFTKCVGITIETRPDYCMKRHLSDMLTYGCTRLEIGVQSVYEDVARDTNRGHTVKAACESF 271
Cdd:TIGR01211 169 DQelkgnSTLEEAIRINETSKHRCVGLTIETRPDYCREEHIDRMLKLGATRVELGVQTIYNDILERTKRGHTVRDVVEAT 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469023   272 HLAKDSGFKVVTHMMPDLPNVGLERDIEQFIEFFENPAFRPDGLKLYPTLVIRGTGLYELWKSGRYRSYSPSDLIELVAR 351
Cdd:TIGR01211 249 RLLRDAGLKVVYHIMPGLPGSSFERDLEMFREIFEDPRFKPDMLKIYPTLVTRGTELYELWKRGEYKPYTTEEAVELIVE 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469023   352 ILALVPPWTRVYRVQRDIPMPLVSSGVEHGNLRELAFARMKDLGIQCRDVRTREVGIQEIHHRVRPY-QVELVRRDYVAN 430
Cdd:TIGR01211 329 IKRMMPKWVRIQRIQRDIPAPLIVAGVKKSNLRELVYRRMKEHGITCRCIRCREVGHQMVKPVQPEEeNVELIVEEYAAS 408
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469023   431 GGWETFLSYEDPDQDILIGLLRLRKCSEETFRfELGGGVSIVRELHVYGSVVPVSSRDPTKFQHQGFGMLLMeEAERIAR 510
Cdd:TIGR01211 409 GGTEFFLSYEDPKNDILIGFLRLRFPSEPAHR-KEVDATALVRELHVYGSEVPIGERGDDEWQHRGYGRRLL-EEAERIA 486
                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 33469023   511 EEHGSGKMAVISGVGTRNYYRKIGYRLQGPYMVKML 546
Cdd:TIGR01211 487 AEEGSEKILVISGIGVREYYRKLGYELDGPYMSKRL 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: 737.63  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469023  34 KDVDLNKMKTKTAAKYGLASQPRLVDIIAAVPPHYRkiLIPKLKAKPVRTASGIAVVAVMCKPHRCPHisftgNICIYCP 113
Cdd:COG1243  14 KKKELEDLKLEVSRKYGLSKVPRNSDILNAAPPEER--LREILRRKPVRTISGVAVVAVMTSPHGCPH-----GRCVFCP 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469023 114 GGPDsdfEYSTQSYTGYEPTSMRAIRARYDPFLQTRHRIEQLKQLGHSVDKVEFIVMGGTFMALPEEYRDYFIRSLHDAL 193
Cdd:COG1243  87 GGPD---KDSPQSYTGEEPAALRAIKNRYDPYEQVRARLKQLETIGHTSDKVELIIMGGTFTALSLEYQEWFLKVALKAM 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469023 194 SGHtSNNIHEAIKYSERSFTKCVGITIETRPDYCMKRHLSDMLTYGCTRLEIGVQSVYEDVARDTNRGHTVKAACESFHL 273
Cdd:COG1243 164 NDF-GYDLEEAQRKNETAELRCVGITIETRPDYIDEEHLDQMLKYGVTRVELGVQSIYDDVLERTKRGHTVEDVVEATRL 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469023 274 AKDSGFKVVTHMMPDLPNVGLERDIEQFIEFFENPAFRPDGLKLYPTLVIRGTGLYELWKSGRYRSYSPSDLIELVARIL 353
Cdd:COG1243 243 LKDAGFKVGYHIMPGLPGSDFERDLESFREIFEDPRFRPDMLKIYPTLVIEGTELYEMWKRGLYKPYTTEEAVELIVEIY 322
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469023 354 ALVPPWTRVYRVQRDIPMPLVSSGVEHGNLRELAFARMKDLGIQCRDVRTREVGIQEIHHRVRPY--QVELVRRDYVANG 431
Cdd:COG1243 323 RLEPKWVRVIRIQRDIPAELIVDGVKKSNLRELVENRMREEGIKCRCIRCREVGIVVVKNVVIPPveQILLKREEYEASG 402
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469023 432 GWETFLSYEDPDQDILIGLLRLRKCSEETFRFELGGGVSIVRELHVYGSVVPVSSRdPTKFQHQGFGMLLMEEAERIARE 511
Cdd:COG1243 403 GTEIFLSYEDPKNDILIGFLRLREPSEGAHREEIDDKTAIVRELHVYGSEVPIGKR-EDEWQHRGYGRELLEEAERIARE 481
                       490       500       510
                ....*....|....*....|....*....|....*
gi 33469023 512 EHgSGKMAVISGVGTRNYYRKIGYRLQGPYMVKML 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 1.47e-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: 102.86  E-value: 1.47e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469023   312 PDGLKLYPTLVIRGTGLYELWKSGRYRSYSPSDLIELVARILALVPPWTRVYRVQRDIPMPLVSSGVEHG-NLRELAFAR 390
Cdd:pfam16199   1 PDGVKIHPLLVLKGTPLAELYERGEYKPLSLEEYVELVADFLELLPPDIVIHRLGGDAPKELLVAPPWHLpKLRVLNLIE 80
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
89-352 4.10e-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: 103.25  E-value: 4.10e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469023     89 VVAVMCKPHRCPHIsftgniCIYCpggpdsdfeystqsytgYEPTSMRAIRARYdpfLQTRHR-IEQLKQLGHSVDKVEF 167
Cdd:smart00729   1 PLALYIITRGCPRR------CTFC-----------------SFPSLRGKLRSRY---LEALVReIELLAEKGEKEGLVGT 54
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469023    168 IVM-GGTFMALPEEYRDYFIRSLHDALSghtsnniheaikysersFTKCVGITIETRPDYCMKRHLSDMLTYGCTRLEIG 246
Cdd:smart00729  55 VFIgGGTPTLLSPEQLEELLEAIREILG-----------------LAKDVEITIETRPDTLTEELLEALKEAGVNRVSLG 117
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469023    247 VQSVYEDVARDTNRGHTVKAACESFHLAKDSGF-KVVTHMMPDLPNVGLErDIEQFIEFFEnpAFRPDGLKLYPTLVIRG 325
Cdd:smart00729 118 VQSGDDEVLKAINRGHTVEDVLEAVELLREAGPiKVSTDLIVGLPGETEE-DFEETLKLLK--ELGPDRVSIFPLSPRPG 194
                          250       260
                   ....*....|....*....|....*..
gi 33469023    326 TGLYELWKsgryrSYSPSDLIELVARI 352
Cdd:smart00729 195 TPLAKMYK-----RLKPPTKEERAELL 216
YhcC COG1242
Radical SAM superfamily enzyme [General function prediction only];
216-373 7.11e-21

Radical SAM superfamily enzyme [General function prediction only];


Pssm-ID: 224163 [Multi-domain]  Cd Length: 312  Bit Score: 93.16  E-value: 7.11e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469023 216 VGITIETRPDyCMKRHLSDMLTYGCTR----LEIGVQSVYEDVARDTNRGHTVKAACESFHLAKDSGFKVVTHMMPDLPN 291
Cdd:COG1242 116 VGLSIGTRPD-CLPDDVLDLLAEYNKRyevwVELGLQTAHDKTLKRINRGHDFACYVDAVKRLRKRGIKVCTHLINGLPG 194
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469023 292 VGLERDIEQFIEFFENPAfrpDGLKLYPTLVIRGTGLYELWKSGRYRSYSPSDLIELVARILALVPPWTRVYRVQRDIPM 371
Cdd:COG1242 195 ETRDEMLETAKIVAELGV---DGIKLHPLHVVKGTPMEKMYEKGRLKFLSLEEYVELVCDQLEHLPPEVVIHRITGDAPR 271

                ..
gi 33469023 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 2.73e-14

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


Pssm-ID: 100105 [Multi-domain]  Cd Length: 204  Bit Score: 71.60  E-value: 2.73e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469023  96 PHRCPHIsftgniCIYCPGGPDSDFEystqsytgyeptsmrairaryDPFLQTRHRIEQLKQLGHSVDKVEFIVMGGTFM 175
Cdd:cd01335   4 TRGCNLN------CGFCSNPASKGRG---------------------PESPPEIEEILDIVLEAKERGVEVVILTGGEPL 56
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469023 176 ALPeeYRDYFIRSLHDALSGHTsnniheaikysersftkcvgITIETRPDYCMKRHLSDMLTYGCTRLEIGVQSVYEDVA 255
Cdd:cd01335  57 LYP--ELAELLRRLKKELPGFE--------------------ISIETNGTLLTEELLKELKELGLDGVGVSLDSGDEEVA 114
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469023 256 RDTN-RGHTVKAACESFHLAKDSGFKVVTHMMPDLPNVGLERDIEQFieFFENPAFRPDGLKLYPTLVIRGTGLYELWKS 334
Cdd:cd01335 115 DKIRgSGESFKERLEALKELREAGLGLSTTLLVGLGDEDEEDDLEEL--ELLAEFRSPDRVSLFRLLPEEGTPLELAAPV 192

                ....*.
gi 33469023 335 GRYRSY 340
Cdd:cd01335 193 VPAEKL 198
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
136-301 2.41e-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: 67.93  E-value: 2.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469023   136 RAIRARYDPFLQTRHRIEQLKQLGHSVDKVEFIVMGGTFMALPEEYRDYFIRSLHDALSGHTsnniheaikysersftkc 215
Cdd:pfam04055  15 PSIRARGKPRELSPEEILEEAKELKRLGVEVVILGGGEPLLLPDLVELLERLLKLEEAEGIR------------------ 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469023   216 vgITIETRPDYCMKRHLSDMLTYGCTRLEIGVQSVYEDVARDTNRGHTVKAACESFHLAKDSGFKVVTHMMPDLPNVGLE 295
Cdd:pfam04055  77 --ITLETNGTLLDEELLELLKEAGLDRVSIGLESGDDEVLKLINRGHTFEEVLEAIELLREAGIPVVTDNIVGLPGETDE 154

                  ....*.
gi 33469023   296 rDIEQF 301
Cdd:pfam04055 155 -DLEEL 159
HemN COG0635
Coproporphyrinogen III oxidase or related Fe-S oxidoreductase [Coenzyme transport and ...
101-348 4.06e-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: 4.06e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469023 101 HISFTGNICIYCpggpdsDF-------EYSTQSYTGYEPTSMRAIRARYDPflqtRHRIEQLkqlghsvdkveFIVmGGT 173
Cdd:COG0635  40 HIPFCVSKCPYC------DFnshvtkrGQPVDEYLDALLEEIELVAALLGG----QREVKTI-----------YFG-GGT 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469023 174 FMALPEEYRDYFIRSLHDALsghtsnniheaikyseRSFTKCVGITIETRPDYCMKRHLSDMLTYGCTRLEIGVQSVYED 253
Cdd:COG0635  98 PSLLSPEQLERLLKALRELF----------------NDLDPDAEITIEANPGTVEAEKFKALKEAGVNRISLGVQSFNDE 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469023 254 VARDTNRGHTVKAACESFHLAKDSGFK-VVTHMMPDLPN---VGLERDIEQFIEffenpaFRPDGLKLYPTLVIRGTGLY 329
Cdd:COG0635 162 VLKALGRIHDEEEAKEAVELARKAGFTsINIDLIYGLPGqtlESLKEDLEQALE------LGPDHLSLYSLAIEPGTKFA 235
                       250
                ....*....|....*....
gi 33469023 330 ELWKSGRyrsYSPSDLIEL 348
Cdd:COG0635 236 QRKIKGK---ALPDEDEKA 251
PRK05799 PRK05799
oxygen-independent coproporphyrinogen III oxidase;
101-336 6.52e-09

oxygen-independent coproporphyrinogen III oxidase;


Pssm-ID: 180263 [Multi-domain]  Cd Length: 374  Bit Score: 57.69  E-value: 6.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469023  101 HISFTGNICIYCpggpdsDFeystQSYTGYEPTSMRAIRArydpflqtrhrieQLKQLGHSVDKVEFIVM---GGTFMAL 177
Cdd:PRK05799   9 HIPFCKQKCLYC------DF----PSYSGKEDLMMEYIKA-------------LSKEIRNSTKNKKIKSIfigGGTPTYL 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469023  178 PEEYrdyfirslhdalsghtSNNIHEAIKYSerSFTKCVGITIETRPDYCMKRHLSDMLTYGCTRLEIGVQSVYEDVARD 257
Cdd:PRK05799  66 SLEA----------------LEILKETIKKL--NKKEDLEFTVEGNPGTFTEEKLKILKSMGVNRLSIGLQAWQNSLLKY 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469023  258 TNRGHTVKAACESFHLAKDSGFKVVT-HMMPDLPNvgleRDIEQFIEFFENPA-FRPDGLKLYPTLVIRGTGLYELWKSG 335
Cdd:PRK05799 128 LGRIHTFEEFLENYKLARKLGFNNINvDLMFGLPN----QTLEDWKETLEKVVeLNPEHISCYSLIIEEGTPFYNLYENG 203

                 .
gi 33469023  336 R 336
Cdd:PRK05799 204 K 204
PRK08207 PRK08207
coproporphyrinogen III oxidase; Provisional
109-352 2.71e-08

coproporphyrinogen III oxidase; Provisional


Pssm-ID: 236187 [Multi-domain]  Cd Length: 488  Bit Score: 56.43  E-value: 2.71e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469023  109 CIYCpggpdsdfeystqSYTGYEptsMRAIRARYDPFLQTRHR-IEQ----LKQLGHSVDKVEFivMGGTFMALPEEYRD 183
Cdd:PRK08207 177 CLYC-------------SFPSYP---IKGYKGLVEPYLEALHYeIEEigkyLKEKGLKITTIYF--GGGTPTSLTAEELE 238
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469023  184 YFIRSLHDALSGhtSNNIHEaikysersftkcvgITIET-RPDYCMKRHLSDMLTYGCTRLEIGVQSVYEDVARDTNRGH 262
Cdd:PRK08207 239 RLLEEIYENFPD--VKNVKE--------------FTVEAgRPDTITEEKLEVLKKYGVDRISINPQTMNDETLKAIGRHH 302
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469023  263 TVKAACESFHLAKDSGFKVVtHMmpD----LPNVGLErDIEQFIEFFEnpAFRPDGLKLYpTLVI-RGTGLYELWKsgRY 337
Cdd:PRK08207 303 TVEDIIEKFHLAREMGFDNI-NM--DliigLPGEGLE-EVKHTLEEIE--KLNPESLTVH-TLAIkRASRLTENKE--KY 373
                        250
                 ....*....|....*
gi 33469023  338 RSYSPSDLIELVARI 352
Cdd:PRK08207 374 KVADREEIEKMMEEA 388
PRK08446 PRK08446
coproporphyrinogen III oxidase family protein;
101-280 6.70e-08

coproporphyrinogen III oxidase family protein;


Pssm-ID: 181428 [Multi-domain]  Cd Length: 350  Bit Score: 54.58  E-value: 6.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469023  101 HISFTGNICIYCpggpdsdfeySTQSYT---GYEPTSMRAIRarydpfLQTRHRIEQLKqlghsVDKVE--FIvMGGTFM 175
Cdd:PRK08446   6 HIPFCESKCGYC----------AFNSYEnkhDLKKEYMQALC------LDLKFELEQFT-----DEKIEsvFI-GGGTPS 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469023  176 AL-PEEYRDYFIRslhdaLSGHTSNNIHeaikysersftkcvgITIETRPDYCMKRHLSDMLTYGCTRLEIGVQSVYEDV 254
Cdd:PRK08446  64 TVsAKFYEPIFEI-----ISPYLSKDCE---------------ITTEANPNSATKAWLKGMKNLGVNRISFGVQSFNEDK 123
                        170       180
                 ....*....|....*....|....*.
gi 33469023  255 ARDTNRGHTVKAACESFHLAKDSGFK 280
Cdd:PRK08446 124 LKFLGRIHSQKQIIKAIENAKKAGFE 149
PRK08599 PRK08599
oxygen-independent coproporphyrinogen III oxidase;
101-303 1.90e-05

oxygen-independent coproporphyrinogen III oxidase;


Pssm-ID: 236309 [Multi-domain]  Cd Length: 377  Bit Score: 46.78  E-value: 1.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469023  101 HISFTGNICIYCpggpdsDFE---YSTQ---SYTGYEPTSMRAIRARYDPFLQTrhrieqlkqlghsvdkveFIVMGGTF 174
Cdd:PRK08599   7 HIPFCEHICYYC------DFNkvfIKNQpvdEYLDALIKEMNTYAIRPFDKLKT------------------IYIGGGTP 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469023  175 MALPEEYRDYFIRSLHDALSghtsnniheaikysersFTKCVGITIETRPDYCMKRHLSDMLTYGCTRLEIGVQSVYEDV 254
Cdd:PRK08599  63 TALSAEQLERLLTAIHRNLP-----------------LSGLEEFTFEANPGDLTKEKLQVLKDSGVNRISLGVQTFNDEL 125
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 33469023  255 ARDTNRGHTVKAACESFHLAKDSGFKVVT-HMMPDLPNvgleRDIEQFIE 303
Cdd:PRK08599 126 LKKIGRTHNEEDVYEAIANAKKAGFDNISiDLIYALPG----QTIEDFKE 171
COG1244 COG1244
Uncharacterized Fe-S cluster-containing protein. MiaB family [General function prediction only] ...
155-338 4.41e-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: 4.41e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469023 155 LKQLGHSVDKVEF--------IVMGGTF---MALPEEYRDYFIRSLHDalsghtSNNIHEaikysersftkcvgITIETR 223
Cdd:COG1244  85 INQFDEAYSKYEGkfdefvvkIFTSGSFldpEEVPREARRYILERISE------NDNVKE--------------VVVESR 144
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469023 224 PDYCMKRHLSDMLTYGC---TRLEIGVQSVYEDVARDT-NRGHTVKAACESFHLAKDSGFKVVTHMMPDLPNVGLERDIE 299
Cdd:COG1244 145 PEFIREERLEEITEILEgkiVEVAIGLETANDKIREDSiNKGFTFEDFVRAAEIIRNYGAKVKTYLLLKPPFLSEKEAIE 224
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 33469023 300 QFIEFFENPAFRPDGLKLYPTLVIRGTgLYE-LWKSGRYR 338
Cdd:COG1244 225 DVISSIVAAKPGTDTISINPTNVQKGT-LVEkLWRRGLYR 263
PRK08208 PRK08208
coproporphyrinogen III oxidase family protein;
152-340 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 33469023  152 IEQLKQLGHSVDKVEF---IVMGGTFMALPEEYRDYFIRSLHDALSGHTSNniheaikysersftkcVGITIETRPDYCM 228
Cdd:PRK08208  77 IRQAEQVAEALAPARFasfAVGGGTPTLLNAAELEKLFDSVERVLGVDLGN----------------IPKSVETSPATTT 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469023  229 KRHLSDMLTYGCTRLEIGVQSVYEDVARDTNRGHTVKAACESFHLAKDSGFkvvthmmPDLpNVGLERDIE-QFIEFFEN 307
Cdd:PRK08208 141 AEKLALLAARGVNRLSIGVQSFHDSELHALHRPQKRADVHQALEWIRAAGF-------PIL-NIDLIYGIPgQTHASWME 212
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 33469023  308 P-----AFRPDGLKLYPTLVIRGTGLYEL---WKSGRYRSY 340
Cdd:PRK08208 213 SldqalVYRPEELFLYPLYVRPLTGLGRRaraWDDQRLSLY 253
PRK06294 PRK06294
coproporphyrinogen III oxidase; Provisional
218-303 1.16e-03

coproporphyrinogen III oxidase; Provisional


Pssm-ID: 180518 [Multi-domain]  Cd Length: 370  Bit Score: 41.28  E-value: 1.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469023  218 ITIETRPDYCMKRHLSDMLTYGCTRLEIGVQSVYEDVARDTNRGHTVKAACESFHLAKDSGFKVVT-HMMPDLPnvglER 296
Cdd:PRK06294  92 ITLEANPENLSESYIRALALTGINRISIGVQTFDDPLLKLLGRTHSSSKAIDAVQECSEHGFSNLSiDLIYGLP----TQ 167

                 ....*..
gi 33469023  297 DIEQFIE 303
Cdd:PRK06294 168 SLSDFIV 174
PRK05904 PRK05904
coproporphyrinogen III oxidase; Provisional
219-307 3.35e-03

coproporphyrinogen III oxidase; Provisional


Pssm-ID: 235641 [Multi-domain]  Cd Length: 353  Bit Score: 39.79  E-value: 3.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469023  219 TIETRPDYCMKRHLSDMLTYGCTRLEIGVQSVYEDVARDTNRGHTVKAACESFHLAKDSGFKVVT-HMMPDLPNVGLErD 297
Cdd:PRK05904  93 TIECNPELITQSQINLLKKNKVNRISLGVQSMNNNILKQLNRTHTIQDSKEAINLLHKNGIYNIScDFLYCLPILKLK-D 171
                         90
                 ....*....|
gi 33469023  298 IEQFIEFFEN 307
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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