NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|47575742|ref|NP_001001215|]
View 

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
39-548 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: 764.29  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575742    39 NLNKLKTKTSAKYGLSAQPRLVDIIAAVPPQYRKILVPKLKAKPIRTASGIAVVAVMCKPHRCPHINftgniCVYCPGGP 118
Cdd:TIGR01211  16 DLEDLKLEVSRKYGLSKVPSNSEILNSAPDEEKKKLEPILRKKPVRTISGVAVVAVMTSPHRCPHGK-----CLYCPGGP 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575742   119 DSdfEYSTQSYTGYEPTSMRAIRARYDPYLQTRHRVEQLKQLGHSVDKVEFIVMGGTFMALSEDYRDFFIRNLHDALSGH 198
Cdd:TIGR01211  91 DS--ENSPQSYTGYEPAAMRGRQNDYDPYEQVTARLEQLEQIGHPVDKVELIIMGGTFPARDLDYQEWFIKRCLNAMNGF 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575742   199 TS-----NSVSEAVRYSERSNTKCVGITIETRPDYCLKRHLSDMLSYGCTRLEIGVQSVYEDVARDTNRGHTVKAVCESF 273
Cdd:TIGR01211 169 DQelkgnSTLEEAIRINETSKHRCVGLTIETRPDYCREEHIDRMLKLGATRVELGVQTIYNDILERTKRGHTVRDVVEAT 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575742   274 HMAKDAGFKVVSHMMPDLPNVGLERDTEQFIEFFENPAFRPDGMKLYPTLVIRGTGLYELWKTGRYRSYSPSTLVDLVAR 353
Cdd:TIGR01211 249 RLLRDAGLKVVYHIMPGLPGSSFERDLEMFREIFEDPRFKPDMLKIYPTLVTRGTELYELWKRGEYKPYTTEEAVELIVE 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575742   354 ILALVPPWTRVYRVQRDIPMPLVSSGVEHGNLRELALARMKDLGTECRDVRTREVGIQEIHHKVRPY-QVELIRRDYVAN 432
Cdd:TIGR01211 329 IKRMMPKWVRIQRIQRDIPAPLIVAGVKKSNLRELVYRRMKEHGITCRCIRCREVGHQMVKPVQPEEeNVELIVEEYAAS 408
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575742   433 GGWETFLSYEDPEQDILIGLLRLRKCSEQSFRPELKgGVSIVRELHVYGSVVPISSRDPSKFQHQGFGMLLMeEAERIAR 512
Cdd:TIGR01211 409 GGTEFFLSYEDPKNDILIGFLRLRFPSEPAHRKEVD-ATALVRELHVYGSEVPIGERGDDEWQHRGYGRRLL-EEAERIA 486
                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 47575742   513 EEHGSCKIAVISGVGTRNYYRKLGYELEGPYMVKKL 548
Cdd:TIGR01211 487 AEEGSEKILVISGIGVREYYRKLGYELDGPYMSKRL 522
 
Name Accession Description Interval E-value
ELP3 TIGR01211
radical SAM enzyme/protein acetyltransferase, ELP3 family; This family includes elongator ...
39-548 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: 764.29  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575742    39 NLNKLKTKTSAKYGLSAQPRLVDIIAAVPPQYRKILVPKLKAKPIRTASGIAVVAVMCKPHRCPHINftgniCVYCPGGP 118
Cdd:TIGR01211  16 DLEDLKLEVSRKYGLSKVPSNSEILNSAPDEEKKKLEPILRKKPVRTISGVAVVAVMTSPHRCPHGK-----CLYCPGGP 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575742   119 DSdfEYSTQSYTGYEPTSMRAIRARYDPYLQTRHRVEQLKQLGHSVDKVEFIVMGGTFMALSEDYRDFFIRNLHDALSGH 198
Cdd:TIGR01211  91 DS--ENSPQSYTGYEPAAMRGRQNDYDPYEQVTARLEQLEQIGHPVDKVELIIMGGTFPARDLDYQEWFIKRCLNAMNGF 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575742   199 TS-----NSVSEAVRYSERSNTKCVGITIETRPDYCLKRHLSDMLSYGCTRLEIGVQSVYEDVARDTNRGHTVKAVCESF 273
Cdd:TIGR01211 169 DQelkgnSTLEEAIRINETSKHRCVGLTIETRPDYCREEHIDRMLKLGATRVELGVQTIYNDILERTKRGHTVRDVVEAT 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575742   274 HMAKDAGFKVVSHMMPDLPNVGLERDTEQFIEFFENPAFRPDGMKLYPTLVIRGTGLYELWKTGRYRSYSPSTLVDLVAR 353
Cdd:TIGR01211 249 RLLRDAGLKVVYHIMPGLPGSSFERDLEMFREIFEDPRFKPDMLKIYPTLVTRGTELYELWKRGEYKPYTTEEAVELIVE 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575742   354 ILALVPPWTRVYRVQRDIPMPLVSSGVEHGNLRELALARMKDLGTECRDVRTREVGIQEIHHKVRPY-QVELIRRDYVAN 432
Cdd:TIGR01211 329 IKRMMPKWVRIQRIQRDIPAPLIVAGVKKSNLRELVYRRMKEHGITCRCIRCREVGHQMVKPVQPEEeNVELIVEEYAAS 408
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575742   433 GGWETFLSYEDPEQDILIGLLRLRKCSEQSFRPELKgGVSIVRELHVYGSVVPISSRDPSKFQHQGFGMLLMeEAERIAR 512
Cdd:TIGR01211 409 GGTEFFLSYEDPKNDILIGFLRLRFPSEPAHRKEVD-ATALVRELHVYGSEVPIGERGDDEWQHRGYGRRLL-EEAERIA 486
                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 47575742   513 EEHGSCKIAVISGVGTRNYYRKLGYELEGPYMVKKL 548
Cdd:TIGR01211 487 AEEGSEKILVISGIGVREYYRKLGYELDGPYMSKRL 522
ELP3 COG1243
Histone acetyltransferase, component of the RNA polymerase elongator complex [Transcription, ...
36-548 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: 749.57  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575742  36 KDVNLNKLKTKTSAKYGLSAQPRLVDIIAAVPPQYRkiLVPKLKAKPIRTASGIAVVAVMCKPHRCPHinftgNICVYCP 115
Cdd:COG1243  14 KKKELEDLKLEVSRKYGLSKVPRNSDILNAAPPEER--LREILRRKPVRTISGVAVVAVMTSPHGCPH-----GRCVFCP 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575742 116 GGPDsdfEYSTQSYTGYEPTSMRAIRARYDPYLQTRHRVEQLKQLGHSVDKVEFIVMGGTFMALSEDYRDFFIRNLHDAL 195
Cdd:COG1243  87 GGPD---KDSPQSYTGEEPAALRAIKNRYDPYEQVRARLKQLETIGHTSDKVELIIMGGTFTALSLEYQEWFLKVALKAM 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575742 196 SGHtSNSVSEAVRYSERSNTKCVGITIETRPDYCLKRHLSDMLSYGCTRLEIGVQSVYEDVARDTNRGHTVKAVCESFHM 275
Cdd:COG1243 164 NDF-GYDLEEAQRKNETAELRCVGITIETRPDYIDEEHLDQMLKYGVTRVELGVQSIYDDVLERTKRGHTVEDVVEATRL 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575742 276 AKDAGFKVVSHMMPDLPNVGLERDTEQFIEFFENPAFRPDGMKLYPTLVIRGTGLYELWKTGRYRSYSPSTLVDLVARIL 355
Cdd:COG1243 243 LKDAGFKVGYHIMPGLPGSDFERDLESFREIFEDPRFRPDMLKIYPTLVIEGTELYEMWKRGLYKPYTTEEAVELIVEIY 322
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575742 356 ALVPPWTRVYRVQRDIPMPLVSSGVEHGNLRELALARMKDLGTECRDVRTREVGIQEIHHKVRPY--QVELIRRDYVANG 433
Cdd:COG1243 323 RLEPKWVRVIRIQRDIPAELIVDGVKKSNLRELVENRMREEGIKCRCIRCREVGIVVVKNVVIPPveQILLKREEYEASG 402
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575742 434 GWETFLSYEDPEQDILIGLLRLRKCSEQSFRPELKGGVSIVRELHVYGSVVPISSRdPSKFQHQGFGMLLMEEAERIARE 513
Cdd:COG1243 403 GTEIFLSYEDPKNDILIGFLRLREPSEGAHREEIDDKTAIVRELHVYGSEVPIGKR-EDEWQHRGYGRELLEEAERIARE 481
                       490       500       510
                ....*....|....*....|....*....|....*
gi 47575742 514 EHgSCKIAVISGVGTRNYYRKLGYELEGPYMVKKL 548
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 ...
314-392 4.15e-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: 101.70  E-value: 4.15e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575742   314 PDGMKLYPTLVIRGTGLYELWKTGRYRSYSPSTLVDLVARILALVPPWTRVYRVQRDIPMPLVSSGVEHG-NLRELALAR 392
Cdd:pfam16199   1 PDGVKIHPLLVLKGTPLAELYERGEYKPLSLEEYVELVADFLELLPPDIVIHRLGGDAPKELLVAPPWHLpKLRVLNLIE 80
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
91-335 4.62e-24

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


Pssm-ID: 214792 [Multi-domain]  Cd Length: 216  Bit Score: 100.17  E-value: 4.62e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575742     91 VVAVMCKPHRCPHInftgniCVYCPGGPDSdfeystqsytgyeptsmraiRARYDPYLQTRHR-VEQLKQLGHSVDKVEF 169
Cdd:smart00729   1 PLALYIITRGCPRR------CTFCSFPSLR--------------------GKLRSRYLEALVReIELLAEKGEKEGLVGT 54
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575742    170 IVMGGtfmalseDYRDFFIRNLHDALsghtsnsVSEAVRYSERSntKCVGITIETRPDYCLKRHLSDMLSYGCTRLEIGV 249
Cdd:smart00729  55 VFIGG-------GTPTLLSPEQLEEL-------LEAIREILGLA--KDVEITIETRPDTLTEELLEALKEAGVNRVSLGV 118
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575742    250 QSVYEDVARDTNRGHTVKAVCESFHMAKDAGF-KVVSHMMPDLPNVGLERDtEQFIEFFEnpAFRPDGMKLYPTLVIRGT 328
Cdd:smart00729 119 QSGDDEVLKAINRGHTVEDVLEAVELLREAGPiKVSTDLIVGLPGETEEDF-EETLKLLK--ELGPDRVSIFPLSPRPGT 195

                   ....*..
gi 47575742    329 GLYELWK 335
Cdd:smart00729 196 PLAKMYK 202
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
98-335 9.98e-13

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


Pssm-ID: 100105 [Multi-domain]  Cd Length: 204  Bit Score: 67.36  E-value: 9.98e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575742  98 PHRCPHInftgniCVYCPGGPDSDFEystqsytgyeptsmrairaryDPYLQTRHRVEQLKQLGHSVDKVEFIVMGGTFM 177
Cdd:cd01335   4 TRGCNLN------CGFCSNPASKGRG---------------------PESPPEIEEILDIVLEAKERGVEVVILTGGEPL 56
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575742 178 ALSEDYRdfFIRNLHDALSGHTsnsvseavrysersntkcvgITIETRPDYCLKRHLSDMLSYGCTRLEIGVQSVYEDVA 257
Cdd:cd01335  57 LYPELAE--LLRRLKKELPGFE--------------------ISIETNGTLLTEELLKELKELGLDGVGVSLDSGDEEVA 114
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47575742 258 RDTN-RGHTVKAVCESFHMAKDAGFKVVSHMMPDLPNVGLERDTEQFieFFENPAFRPDGMKLYPTLVIRGTGLYELWK 335
Cdd:cd01335 115 DKIRgSGESFKERLEALKELREAGLGLSTTLLVGLGDEDEEDDLEEL--ELLAEFRSPDRVSLFRLLPEEGTPLELAAP 191
PRK08207 PRK08207
coproporphyrinogen III oxidase; Provisional
111-297 1.19e-07

coproporphyrinogen III oxidase; Provisional


Pssm-ID: 236187 [Multi-domain]  Cd Length: 488  Bit Score: 54.11  E-value: 1.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575742  111 CVYCpggpdsdfeystqSYTGYEptsMRAIRARYDPYLQTRHR-VEQ----LKQLGHSVDKVEFivMGGTFMALSEDYRD 185
Cdd:PRK08207 177 CLYC-------------SFPSYP---IKGYKGLVEPYLEALHYeIEEigkyLKEKGLKITTIYF--GGGTPTSLTAEELE 238
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575742  186 FFIRNLHDALSGhtSNSVSEavrysersntkcvgITIET-RPDYCLKRHLSDMLSYGCTRLEIGVQSVYEDVARDTNRGH 264
Cdd:PRK08207 239 RLLEEIYENFPD--VKNVKE--------------FTVEAgRPDTITEEKLEVLKKYGVDRISINPQTMNDETLKAIGRHH 302
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 47575742  265 TVKAVCESFHMAKDAGFKVVShMmpD----LPNVGLE 297
Cdd:PRK08207 303 TVEDIIEKFHLAREMGFDNIN-M--DliigLPGEGLE 336
 
Name Accession Description Interval E-value
ELP3 TIGR01211
radical SAM enzyme/protein acetyltransferase, ELP3 family; This family includes elongator ...
39-548 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: 764.29  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575742    39 NLNKLKTKTSAKYGLSAQPRLVDIIAAVPPQYRKILVPKLKAKPIRTASGIAVVAVMCKPHRCPHINftgniCVYCPGGP 118
Cdd:TIGR01211  16 DLEDLKLEVSRKYGLSKVPSNSEILNSAPDEEKKKLEPILRKKPVRTISGVAVVAVMTSPHRCPHGK-----CLYCPGGP 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575742   119 DSdfEYSTQSYTGYEPTSMRAIRARYDPYLQTRHRVEQLKQLGHSVDKVEFIVMGGTFMALSEDYRDFFIRNLHDALSGH 198
Cdd:TIGR01211  91 DS--ENSPQSYTGYEPAAMRGRQNDYDPYEQVTARLEQLEQIGHPVDKVELIIMGGTFPARDLDYQEWFIKRCLNAMNGF 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575742   199 TS-----NSVSEAVRYSERSNTKCVGITIETRPDYCLKRHLSDMLSYGCTRLEIGVQSVYEDVARDTNRGHTVKAVCESF 273
Cdd:TIGR01211 169 DQelkgnSTLEEAIRINETSKHRCVGLTIETRPDYCREEHIDRMLKLGATRVELGVQTIYNDILERTKRGHTVRDVVEAT 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575742   274 HMAKDAGFKVVSHMMPDLPNVGLERDTEQFIEFFENPAFRPDGMKLYPTLVIRGTGLYELWKTGRYRSYSPSTLVDLVAR 353
Cdd:TIGR01211 249 RLLRDAGLKVVYHIMPGLPGSSFERDLEMFREIFEDPRFKPDMLKIYPTLVTRGTELYELWKRGEYKPYTTEEAVELIVE 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575742   354 ILALVPPWTRVYRVQRDIPMPLVSSGVEHGNLRELALARMKDLGTECRDVRTREVGIQEIHHKVRPY-QVELIRRDYVAN 432
Cdd:TIGR01211 329 IKRMMPKWVRIQRIQRDIPAPLIVAGVKKSNLRELVYRRMKEHGITCRCIRCREVGHQMVKPVQPEEeNVELIVEEYAAS 408
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575742   433 GGWETFLSYEDPEQDILIGLLRLRKCSEQSFRPELKgGVSIVRELHVYGSVVPISSRDPSKFQHQGFGMLLMeEAERIAR 512
Cdd:TIGR01211 409 GGTEFFLSYEDPKNDILIGFLRLRFPSEPAHRKEVD-ATALVRELHVYGSEVPIGERGDDEWQHRGYGRRLL-EEAERIA 486
                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 47575742   513 EEHGSCKIAVISGVGTRNYYRKLGYELEGPYMVKKL 548
Cdd:TIGR01211 487 AEEGSEKILVISGIGVREYYRKLGYELDGPYMSKRL 522
ELP3 COG1243
Histone acetyltransferase, component of the RNA polymerase elongator complex [Transcription, ...
36-548 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: 749.57  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575742  36 KDVNLNKLKTKTSAKYGLSAQPRLVDIIAAVPPQYRkiLVPKLKAKPIRTASGIAVVAVMCKPHRCPHinftgNICVYCP 115
Cdd:COG1243  14 KKKELEDLKLEVSRKYGLSKVPRNSDILNAAPPEER--LREILRRKPVRTISGVAVVAVMTSPHGCPH-----GRCVFCP 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575742 116 GGPDsdfEYSTQSYTGYEPTSMRAIRARYDPYLQTRHRVEQLKQLGHSVDKVEFIVMGGTFMALSEDYRDFFIRNLHDAL 195
Cdd:COG1243  87 GGPD---KDSPQSYTGEEPAALRAIKNRYDPYEQVRARLKQLETIGHTSDKVELIIMGGTFTALSLEYQEWFLKVALKAM 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575742 196 SGHtSNSVSEAVRYSERSNTKCVGITIETRPDYCLKRHLSDMLSYGCTRLEIGVQSVYEDVARDTNRGHTVKAVCESFHM 275
Cdd:COG1243 164 NDF-GYDLEEAQRKNETAELRCVGITIETRPDYIDEEHLDQMLKYGVTRVELGVQSIYDDVLERTKRGHTVEDVVEATRL 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575742 276 AKDAGFKVVSHMMPDLPNVGLERDTEQFIEFFENPAFRPDGMKLYPTLVIRGTGLYELWKTGRYRSYSPSTLVDLVARIL 355
Cdd:COG1243 243 LKDAGFKVGYHIMPGLPGSDFERDLESFREIFEDPRFRPDMLKIYPTLVIEGTELYEMWKRGLYKPYTTEEAVELIVEIY 322
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575742 356 ALVPPWTRVYRVQRDIPMPLVSSGVEHGNLRELALARMKDLGTECRDVRTREVGIQEIHHKVRPY--QVELIRRDYVANG 433
Cdd:COG1243 323 RLEPKWVRVIRIQRDIPAELIVDGVKKSNLRELVENRMREEGIKCRCIRCREVGIVVVKNVVIPPveQILLKREEYEASG 402
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575742 434 GWETFLSYEDPEQDILIGLLRLRKCSEQSFRPELKGGVSIVRELHVYGSVVPISSRdPSKFQHQGFGMLLMEEAERIARE 513
Cdd:COG1243 403 GTEIFLSYEDPKNDILIGFLRLREPSEGAHREEIDDKTAIVRELHVYGSEVPIGKR-EDEWQHRGYGRELLEEAERIARE 481
                       490       500       510
                ....*....|....*....|....*....|....*
gi 47575742 514 EHgSCKIAVISGVGTRNYYRKLGYELEGPYMVKKL 548
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 ...
314-392 4.15e-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: 101.70  E-value: 4.15e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575742   314 PDGMKLYPTLVIRGTGLYELWKTGRYRSYSPSTLVDLVARILALVPPWTRVYRVQRDIPMPLVSSGVEHG-NLRELALAR 392
Cdd:pfam16199   1 PDGVKIHPLLVLKGTPLAELYERGEYKPLSLEEYVELVADFLELLPPDIVIHRLGGDAPKELLVAPPWHLpKLRVLNLIE 80
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
91-335 4.62e-24

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


Pssm-ID: 214792 [Multi-domain]  Cd Length: 216  Bit Score: 100.17  E-value: 4.62e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575742     91 VVAVMCKPHRCPHInftgniCVYCPGGPDSdfeystqsytgyeptsmraiRARYDPYLQTRHR-VEQLKQLGHSVDKVEF 169
Cdd:smart00729   1 PLALYIITRGCPRR------CTFCSFPSLR--------------------GKLRSRYLEALVReIELLAEKGEKEGLVGT 54
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575742    170 IVMGGtfmalseDYRDFFIRNLHDALsghtsnsVSEAVRYSERSntKCVGITIETRPDYCLKRHLSDMLSYGCTRLEIGV 249
Cdd:smart00729  55 VFIGG-------GTPTLLSPEQLEEL-------LEAIREILGLA--KDVEITIETRPDTLTEELLEALKEAGVNRVSLGV 118
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575742    250 QSVYEDVARDTNRGHTVKAVCESFHMAKDAGF-KVVSHMMPDLPNVGLERDtEQFIEFFEnpAFRPDGMKLYPTLVIRGT 328
Cdd:smart00729 119 QSGDDEVLKAINRGHTVEDVLEAVELLREAGPiKVSTDLIVGLPGETEEDF-EETLKLLK--ELGPDRVSIFPLSPRPGT 195

                   ....*..
gi 47575742    329 GLYELWK 335
Cdd:smart00729 196 PLAKMYK 202
YhcC COG1242
Radical SAM superfamily enzyme [General function prediction only];
218-375 4.13e-20

Radical SAM superfamily enzyme [General function prediction only];


Pssm-ID: 224163 [Multi-domain]  Cd Length: 312  Bit Score: 91.23  E-value: 4.13e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575742 218 VGITIETRPDyCLKRHLSDMLSYGCTR----LEIGVQSVYEDVARDTNRGHTVKAVCESFHMAKDAGFKVVSHMMPDLPN 293
Cdd:COG1242 116 VGLSIGTRPD-CLPDDVLDLLAEYNKRyevwVELGLQTAHDKTLKRINRGHDFACYVDAVKRLRKRGIKVCTHLINGLPG 194
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575742 294 vgleRDTEQFIEFFENPAFRP-DGMKLYPTLVIRGTGLYELWKTGRYRSYSPSTLVDLVARILALVPPWTRVYRVQRDIP 372
Cdd:COG1242 195 ----ETRDEMLETAKIVAELGvDGIKLHPLHVVKGTPMEKMYEKGRLKFLSLEEYVELVCDQLEHLPPEVVIHRITGDAP 270

                ...
gi 47575742 373 MPL 375
Cdd:COG1242 271 RDT 273
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
99-297 1.92e-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: 1.92e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575742    99 HRCPHInftgniCVYCpggpdsdfeystqsytgyeptSMRAIRARYDPYLQTRHRVEQLKQLGHSVDKVEFIVMGGTFMA 178
Cdd:pfam04055   3 RGCNLR------CTYC---------------------AFPSIRARGKPRELSPEEILEEAKELKRLGVEVVILGGGEPLL 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575742   179 LSEDYRDFFIRNLHDALSGHTsnsvseavrysersntkcvgITIETRPDYCLKRHLSDMLSYGCTRLEIGVQSVYEDVAR 258
Cdd:pfam04055  56 LPDLVELLERLLKLEEAEGIR--------------------ITLETNGTLLDEELLELLKEAGLDRVSIGLESGDDEVLK 115
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 47575742   259 DTNRGHTVKAVCESFHMAKDAGFKVVSHMMPDLPNVGLE 297
Cdd:pfam04055 116 LINRGHTFEEVLEAIELLREAGIPVVTDNIVGLPGETDE 154
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
98-335 9.98e-13

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


Pssm-ID: 100105 [Multi-domain]  Cd Length: 204  Bit Score: 67.36  E-value: 9.98e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575742  98 PHRCPHInftgniCVYCPGGPDSDFEystqsytgyeptsmrairaryDPYLQTRHRVEQLKQLGHSVDKVEFIVMGGTFM 177
Cdd:cd01335   4 TRGCNLN------CGFCSNPASKGRG---------------------PESPPEIEEILDIVLEAKERGVEVVILTGGEPL 56
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575742 178 ALSEDYRdfFIRNLHDALSGHTsnsvseavrysersntkcvgITIETRPDYCLKRHLSDMLSYGCTRLEIGVQSVYEDVA 257
Cdd:cd01335  57 LYPELAE--LLRRLKKELPGFE--------------------ISIETNGTLLTEELLKELKELGLDGVGVSLDSGDEEVA 114
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47575742 258 RDTN-RGHTVKAVCESFHMAKDAGFKVVSHMMPDLPNVGLERDTEQFieFFENPAFRPDGMKLYPTLVIRGTGLYELWK 335
Cdd:cd01335 115 DKIRgSGESFKERLEALKELREAGLGLSTTLLVGLGDEDEEDDLEEL--ELLAEFRSPDRVSLFRLLPEEGTPLELAAP 191
HemN COG0635
Coproporphyrinogen III oxidase or related Fe-S oxidoreductase [Coenzyme transport and ...
103-358 4.34e-09

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


Pssm-ID: 223708 [Multi-domain]  Cd Length: 416  Bit Score: 58.44  E-value: 4.34e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575742 103 HINFTGNICVYCpggpdsDF-------EYSTQSYTGYEPTSMRAIRARYDPylqtRHRVEQLkqlghsvdkveFIVmGGT 175
Cdd:COG0635  40 HIPFCVSKCPYC------DFnshvtkrGQPVDEYLDALLEEIELVAALLGG----QREVKTI-----------YFG-GGT 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575742 176 FMALS-EDYRDFFirnlhdalsghtsnsvsEAVRYSERSNTKCVGITIETRPDYCLKRHLSDMLSYGCTRLEIGVQSVYE 254
Cdd:COG0635  98 PSLLSpEQLERLL-----------------KALRELFNDLDPDAEITIEANPGTVEAEKFKALKEAGVNRISLGVQSFND 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575742 255 DVARDTNRGHTVKAVCESFHMAKDAGFKVVS-HMMPDLPN---VGLERDTEQFIEffenpaFRPDGMKLYPTLVIRGTGL 330
Cdd:COG0635 161 EVLKALGRIHDEEEAKEAVELARKAGFTSINiDLIYGLPGqtlESLKEDLEQALE------LGPDHLSLYSLAIEPGTKF 234
                       250       260
                ....*....|....*....|....*...
gi 47575742 331 YELWKTGRyrsYSPSTlvDLVARILALV 358
Cdd:COG0635 235 AQRKIKGK---ALPDE--DEKADMYELV 257
PRK08207 PRK08207
coproporphyrinogen III oxidase; Provisional
111-297 1.19e-07

coproporphyrinogen III oxidase; Provisional


Pssm-ID: 236187 [Multi-domain]  Cd Length: 488  Bit Score: 54.11  E-value: 1.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575742  111 CVYCpggpdsdfeystqSYTGYEptsMRAIRARYDPYLQTRHR-VEQ----LKQLGHSVDKVEFivMGGTFMALSEDYRD 185
Cdd:PRK08207 177 CLYC-------------SFPSYP---IKGYKGLVEPYLEALHYeIEEigkyLKEKGLKITTIYF--GGGTPTSLTAEELE 238
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575742  186 FFIRNLHDALSGhtSNSVSEavrysersntkcvgITIET-RPDYCLKRHLSDMLSYGCTRLEIGVQSVYEDVARDTNRGH 264
Cdd:PRK08207 239 RLLEEIYENFPD--VKNVKE--------------FTVEAgRPDTITEEKLEVLKKYGVDRISINPQTMNDETLKAIGRHH 302
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 47575742  265 TVKAVCESFHMAKDAGFKVVShMmpD----LPNVGLE 297
Cdd:PRK08207 303 TVEDIIEKFHLAREMGFDNIN-M--DliigLPGEGLE 336
PRK05799 PRK05799
oxygen-independent coproporphyrinogen III oxidase;
103-338 1.39e-07

oxygen-independent coproporphyrinogen III oxidase;


Pssm-ID: 180263 [Multi-domain]  Cd Length: 374  Bit Score: 53.83  E-value: 1.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575742  103 HINFTGNICVYCpggpdsDFeystQSYTGYEPTSMRAIRArydpylqtrhrveQLKQLGHSVDKVEFIVM---GGTFMAL 179
Cdd:PRK05799   9 HIPFCKQKCLYC------DF----PSYSGKEDLMMEYIKA-------------LSKEIRNSTKNKKIKSIfigGGTPTYL 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575742  180 SEDYrdffIRNLHDALSghtsnsvseavRYSERSNtkcVGITIETRPDYCLKRHLSDMLSYGCTRLEIGVQSVYEDVARD 259
Cdd:PRK05799  66 SLEA----LEILKETIK-----------KLNKKED---LEFTVEGNPGTFTEEKLKILKSMGVNRLSIGLQAWQNSLLKY 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575742  260 TNRGHTVKAVCESFHMAKDAGFKVVS-HMMPDLPNVGLE--RDTEQFIeffenPAFRPDGMKLYPTLVIRGTGLYELWKT 336
Cdd:PRK05799 128 LGRIHTFEEFLENYKLARKLGFNNINvDLMFGLPNQTLEdwKETLEKV-----VELNPEHISCYSLIIEEGTPFYNLYEN 202

                 ..
gi 47575742  337 GR 338
Cdd:PRK05799 203 GK 204
PRK08446 PRK08446
coproporphyrinogen III oxidase family protein;
103-285 2.89e-07

coproporphyrinogen III oxidase family protein;


Pssm-ID: 181428 [Multi-domain]  Cd Length: 350  Bit Score: 52.65  E-value: 2.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575742  103 HINFTGNICVYCpggpdsdfeySTQSYT---GYEPTSMRAIrarydpYLQTRHrveQLKQLGHSVDKVEFIvMGGTFMAL 179
Cdd:PRK08446   6 HIPFCESKCGYC----------AFNSYEnkhDLKKEYMQAL------CLDLKF---ELEQFTDEKIESVFI-GGGTPSTV 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575742  180 S-EDYRDFFIRnlhdaLSGHTSNSVSeavrysersntkcvgITIETRPDYCLKRHLSDMLSYGCTRLEIGVQSVYEDVAR 258
Cdd:PRK08446  66 SaKFYEPIFEI-----ISPYLSKDCE---------------ITTEANPNSATKAWLKGMKNLGVNRISFGVQSFNEDKLK 125
                        170       180
                 ....*....|....*....|....*..
gi 47575742  259 DTNRGHTVKAVCESFHMAKDAGFKVVS 285
Cdd:PRK08446 126 FLGRIHSQKQIIKAIENAKKAGFENIS 152
PRK08599 PRK08599
oxygen-independent coproporphyrinogen III oxidase;
103-297 2.98e-07

oxygen-independent coproporphyrinogen III oxidase;


Pssm-ID: 236309 [Multi-domain]  Cd Length: 377  Bit Score: 52.56  E-value: 2.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575742  103 HINFTGNICVYCpggpdsDFE---YSTQ---SYTGYEPTSMRAIRARYDPYLQTrhrveqlkqlghsvdkveFIVMGGTF 176
Cdd:PRK08599   7 HIPFCEHICYYC------DFNkvfIKNQpvdEYLDALIKEMNTYAIRPFDKLKT------------------IYIGGGTP 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575742  177 MALSEDYRDFFIRNLHDALsghTSNSVSEavrysersntkcvgITIETRPDYCLKRHLSDMLSYGCTRLEIGVQSVYEDV 256
Cdd:PRK08599  63 TALSAEQLERLLTAIHRNL---PLSGLEE--------------FTFEANPGDLTKEKLQVLKDSGVNRISLGVQTFNDEL 125
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 47575742  257 ARDTNRGHTVKAVCESFHMAKDAGFKVVS-HMMPDLPNVGLE 297
Cdd:PRK08599 126 LKKIGRTHNEEDVYEAIANAKKAGFDNISiDLIYALPGQTIE 167
PRK08208 PRK08208
coproporphyrinogen III oxidase family protein;
103-399 7.21e-05

coproporphyrinogen III oxidase family protein;


Pssm-ID: 181292 [Multi-domain]  Cd Length: 430  Bit Score: 45.38  E-value: 7.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575742  103 HINFTGNICVYCpggpdsdfeySTQSYTGyeptsmrAIRARYDPYLQTRhrVEQLKQLGHSVDKVEF---IVMGGTFMAL 179
Cdd:PRK08208  45 HIPFCEMRCGFC----------NLFTRTG-------ADAEFIDSYLDAL--IRQAEQVAEALAPARFasfAVGGGTPTLL 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575742  180 SED--YRDFFIrnLHDALSGHTSNsvseavrysersntkcVGITIETRPDYCLKRHLSDMLSYGCTRLEIGVQSVYEDVA 257
Cdd:PRK08208 106 NAAelEKLFDS--VERVLGVDLGN----------------IPKSVETSPATTTAEKLALLAARGVNRLSIGVQSFHDSEL 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575742  258 RDTNRGHTVKAVCESFHMAKDAGFkvvshmmPDLpNV----GLERDT-EQFIEFFENP-AFRPDGMKLYPTLVIRGTGLY 331
Cdd:PRK08208 168 HALHRPQKRADVHQALEWIRAAGF-------PIL-NIdliyGIPGQThASWMESLDQAlVYRPEELFLYPLYVRPLTGLG 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47575742  332 ElwktgRYRSYSPSTLvdlvarilalvppwtRVYRVQRDIpmpLVSSGVEHGNLRELALARMKDLGTE 399
Cdd:PRK08208 240 R-----RARAWDDQRL---------------SLYRLARDL---LLEAGYTQTSMRMFRRNDAPDKGAP 284
PRK05904 PRK05904
coproporphyrinogen III oxidase; Provisional
221-309 1.51e-03

coproporphyrinogen III oxidase; Provisional


Pssm-ID: 235641 [Multi-domain]  Cd Length: 353  Bit Score: 40.95  E-value: 1.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575742  221 TIETRPDYCLKRHLSDMLSYGCTRLEIGVQSVYEDVARDTNRGHTVKAVCESFHMAKDAGFKVVS-HMMPDLPNVGLErD 299
Cdd:PRK05904  93 TIECNPELITQSQINLLKKNKVNRISLGVQSMNNNILKQLNRTHTIQDSKEAINLLHKNGIYNIScDFLYCLPILKLK-D 171
                         90
                 ....*....|
gi 47575742  300 TEQFIEFFEN 309
Cdd:PRK05904 172 LDEVFNFILK 181
PRK06294 PRK06294
coproporphyrinogen III oxidase; Provisional
220-297 1.57e-03

coproporphyrinogen III oxidase; Provisional


Pssm-ID: 180518 [Multi-domain]  Cd Length: 370  Bit Score: 40.90  E-value: 1.57e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47575742  220 ITIETRPDYCLKRHLSDMLSYGCTRLEIGVQSVYEDVARDTNRGHTVKAVCESFHMAKDAGFKVVS-HMMPDLPNVGLE 297
Cdd:PRK06294  92 ITLEANPENLSESYIRALALTGINRISIGVQTFDDPLLKLLGRTHSSSKAIDAVQECSEHGFSNLSiDLIYGLPTQSLS 170
COG1244 COG1244
Uncharacterized Fe-S cluster-containing protein. MiaB family [General function prediction only] ...
208-340 7.03e-03

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


Pssm-ID: 224165 [Multi-domain]  Cd Length: 358  Bit Score: 38.92  E-value: 7.03e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575742 208 RYSERSNTKCVgiTIETRPDYCLKRHLSDMLSYGC---TRLEIGVQSVYEDVARDT-NRGHTVKAVCESFHMAKDAGFKV 283
Cdd:COG1244 129 RISENDNVKEV--VVESRPEFIREERLEEITEILEgkiVEVAIGLETANDKIREDSiNKGFTFEDFVRAAEIIRNYGAKV 206
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 47575742 284 VSHMMPDLPNVGLERDTEQFIEFFENPAFRPDGMKLYPTLVIRGTgLYE-LWKTGRYR 340
Cdd:COG1244 207 KTYLLLKPPFLSEKEAIEDVISSIVAAKPGTDTISINPTNVQKGT-LVEkLWRRGLYR 263
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH