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Conserved domains on  [gi|2217308006|ref|XP_047290791|]
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NEDD8-activating enzyme E1 regulatory subunit isoform X1 [Homo sapiens]

Protein Classification

NEDD8-activating enzyme E1 regulatory subunit( domain architecture ID 10107339)

NEDD8-activating enzyme E1 regulatory subunit is a component of the dimeric UBA3-NAE1 E1 enzyme that activates NEDD8 by first adenylating its C-terminal glycine residue with ATP, thereafter linking this residue to the side chain of the catalytic cysteine, yielding a NEDD8-UBA3 thioester and free AMP

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
APPBP1_RUB cd01493
Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric ...
 1-443 0e+00

Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric activating enzyme (E1), specific for the Rub family of ubiquitin-like proteins (Ubls). E1 enzymes are part of a conjugation cascade to attach Ub or Ubls, covalently to substrate proteins consisting of activating (E1), conjugating (E2), and/or ligating (E3) enzymes. E1 activates ubiquitin(-like) by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and Ubls C-terminus. E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. Post-translational modification by Rub family of ubiquitin-like proteins (Ublps) activates SCF ubiquitin ligases and is involved in cell cycle control, signaling and embryogenesis. ABPP1 contains part of the adenylation domain.


:

Pssm-ID: 238770 [Multi-domain]  Cd Length: 425  Bit Score: 569.24  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308006   1 MEFLQELNSDVSGSFVEESPENLLDNDPSFFCRFTVVVATQLPESTSLRLADVLWNSQIPLLICRTYGLVGYMRIIIKEH 80
Cdd:cd01493    80 CELLQELNPDVNGSAVEESPEALLDNDPSFFSQFTVVIATNLPESTLLRLADVLWSANIPLLYVRSYGLYGYIRIQLKEH 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308006  81 PVIESHPDNALEDLRLDKPFPELREHFQSYDLDHMEKKDHSHTPWIVIIAKYLAQWYSETNGRIPKTYKEKEDFRDLIRQ 160
Cdd:cd01493   160 TIVESHPDNALEDLRLDNPFPELREHADSIDLDDMDPAEHSHTPYIVILIKYLEKWRSAHNGQLPSTYKEKKEFRDLVRS 239

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308006 161 GILKNengapEDEENFEEAIKNVNTALNTTQIPSSIEDIFNDDRCINITKQTPSFWILARALKEFVAKEgQGNLPVRGTI 240
Cdd:cd01493   240 LMRSN-----EDEENFEEAIKAVNKALNRTKIPSSVEEIFNDDRCENLTSQSSSFWIMARALKEFVAEE-NGLLPLPGTL 313

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308006 241 PDMIADSGKYIKLQNVYREKAKKDAAAVGNHVAKLLQSIGQAPESISEKELKLLCSNSAFLRVVRCRSLAeeygldtink 320
Cdd:cd01493   314 PDMTADTEKYIKLQNIYREKAEKDAAEVEKYVREILKSLGRSPDSISDKEIKLFCKNAAFLRVIRGRSLE---------- 383

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308006 321 deiissmdnpdneivlylmlravdrfhkqqgrypgvsnyqveedigklkscltgflqeyglsvmvkddyvhefcrygaae 400
Cdd:cd01493       --------------------------------------------------------------------------------

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 2217308006 401 pHTIAAFLGGAAAQEVIKIITKQFVIFNNTYIYSGMSQTSATF 443
Cdd:cd01493   384 -HNISAFMGGIAAQEVIKLITKQYVPIDNTFIFDGIRSKSATF 425
Ube1 super family cl36897
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 321-424 3.08e-07

ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino acids, of a multicopy family of eukaryotic proteins, many of which are designated ubiquitin-activating enzyme E1. Members have two copies of the ThiF family domain (pfam00899), a repeat found in ubiquitin-activating proteins (pfam02134), and other regions.


The actual alignment was detected with superfamily member TIGR01408:

Pssm-ID: 273603 [Multi-domain]  Cd Length: 1006  Bit Score: 52.97  E-value: 3.08e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308006  321 DEIISSMDNPDNEIVLYLMLRAVDRFHKQQGRYPGVSNYQVEEDIGKLKSCLTGFLQEYglSVMVKDDYVHEFCRYGAAE 400
Cdd:TIGR01408  268 KCLIVDFSKPERPPEIHTAFQALDQFQEKYSRKPNVGCQQDAEELLKLATSISETLEEK--VPDVDAKLVHWLSWTAQGF 345

                           90       100
                   ....*....|....*....|....
gi 2217308006  401 PHTIAAFLGGAAAQEVIKIITKQF 424
Cdd:TIGR01408  346 LSPMAAAVGGVVSQEVLKAVTGKF 369
 
Name Accession Description Interval E-value
APPBP1_RUB cd01493
Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric ...
 1-443 0e+00

Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric activating enzyme (E1), specific for the Rub family of ubiquitin-like proteins (Ubls). E1 enzymes are part of a conjugation cascade to attach Ub or Ubls, covalently to substrate proteins consisting of activating (E1), conjugating (E2), and/or ligating (E3) enzymes. E1 activates ubiquitin(-like) by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and Ubls C-terminus. E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. Post-translational modification by Rub family of ubiquitin-like proteins (Ublps) activates SCF ubiquitin ligases and is involved in cell cycle control, signaling and embryogenesis. ABPP1 contains part of the adenylation domain.


Pssm-ID: 238770 [Multi-domain]  Cd Length: 425  Bit Score: 569.24  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308006   1 MEFLQELNSDVSGSFVEESPENLLDNDPSFFCRFTVVVATQLPESTSLRLADVLWNSQIPLLICRTYGLVGYMRIIIKEH 80
Cdd:cd01493    80 CELLQELNPDVNGSAVEESPEALLDNDPSFFSQFTVVIATNLPESTLLRLADVLWSANIPLLYVRSYGLYGYIRIQLKEH 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308006  81 PVIESHPDNALEDLRLDKPFPELREHFQSYDLDHMEKKDHSHTPWIVIIAKYLAQWYSETNGRIPKTYKEKEDFRDLIRQ 160
Cdd:cd01493   160 TIVESHPDNALEDLRLDNPFPELREHADSIDLDDMDPAEHSHTPYIVILIKYLEKWRSAHNGQLPSTYKEKKEFRDLVRS 239

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308006 161 GILKNengapEDEENFEEAIKNVNTALNTTQIPSSIEDIFNDDRCINITKQTPSFWILARALKEFVAKEgQGNLPVRGTI 240
Cdd:cd01493   240 LMRSN-----EDEENFEEAIKAVNKALNRTKIPSSVEEIFNDDRCENLTSQSSSFWIMARALKEFVAEE-NGLLPLPGTL 313

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308006 241 PDMIADSGKYIKLQNVYREKAKKDAAAVGNHVAKLLQSIGQAPESISEKELKLLCSNSAFLRVVRCRSLAeeygldtink 320
Cdd:cd01493   314 PDMTADTEKYIKLQNIYREKAEKDAAEVEKYVREILKSLGRSPDSISDKEIKLFCKNAAFLRVIRGRSLE---------- 383

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308006 321 deiissmdnpdneivlylmlravdrfhkqqgrypgvsnyqveedigklkscltgflqeyglsvmvkddyvhefcrygaae 400
Cdd:cd01493       --------------------------------------------------------------------------------

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 2217308006 401 pHTIAAFLGGAAAQEVIKIITKQFVIFNNTYIYSGMSQTSATF 443
Cdd:cd01493   384 -HNISAFMGGIAAQEVIKLITKQYVPIDNTFIFDGIRSKSATF 425
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 321-424 3.08e-07

ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino acids, of a multicopy family of eukaryotic proteins, many of which are designated ubiquitin-activating enzyme E1. Members have two copies of the ThiF family domain (pfam00899), a repeat found in ubiquitin-activating proteins (pfam02134), and other regions.


Pssm-ID: 273603 [Multi-domain]  Cd Length: 1006  Bit Score: 52.97  E-value: 3.08e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308006  321 DEIISSMDNPDNEIVLYLMLRAVDRFHKQQGRYPGVSNYQVEEDIGKLKSCLTGFLQEYglSVMVKDDYVHEFCRYGAAE 400
Cdd:TIGR01408  268 KCLIVDFSKPERPPEIHTAFQALDQFQEKYSRKPNVGCQQDAEELLKLATSISETLEEK--VPDVDAKLVHWLSWTAQGF 345

                           90       100
                   ....*....|....*....|....
gi 2217308006  401 PHTIAAFLGGAAAQEVIKIITKQF 424
Cdd:TIGR01408  346 LSPMAAAVGGVVSQEVLKAVTGKF 369
 
Name Accession Description Interval E-value
APPBP1_RUB cd01493
Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric ...
 1-443 0e+00

Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric activating enzyme (E1), specific for the Rub family of ubiquitin-like proteins (Ubls). E1 enzymes are part of a conjugation cascade to attach Ub or Ubls, covalently to substrate proteins consisting of activating (E1), conjugating (E2), and/or ligating (E3) enzymes. E1 activates ubiquitin(-like) by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and Ubls C-terminus. E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. Post-translational modification by Rub family of ubiquitin-like proteins (Ublps) activates SCF ubiquitin ligases and is involved in cell cycle control, signaling and embryogenesis. ABPP1 contains part of the adenylation domain.


Pssm-ID: 238770 [Multi-domain]  Cd Length: 425  Bit Score: 569.24  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308006   1 MEFLQELNSDVSGSFVEESPENLLDNDPSFFCRFTVVVATQLPESTSLRLADVLWNSQIPLLICRTYGLVGYMRIIIKEH 80
Cdd:cd01493    80 CELLQELNPDVNGSAVEESPEALLDNDPSFFSQFTVVIATNLPESTLLRLADVLWSANIPLLYVRSYGLYGYIRIQLKEH 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308006  81 PVIESHPDNALEDLRLDKPFPELREHFQSYDLDHMEKKDHSHTPWIVIIAKYLAQWYSETNGRIPKTYKEKEDFRDLIRQ 160
Cdd:cd01493   160 TIVESHPDNALEDLRLDNPFPELREHADSIDLDDMDPAEHSHTPYIVILIKYLEKWRSAHNGQLPSTYKEKKEFRDLVRS 239

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308006 161 GILKNengapEDEENFEEAIKNVNTALNTTQIPSSIEDIFNDDRCINITKQTPSFWILARALKEFVAKEgQGNLPVRGTI 240
Cdd:cd01493   240 LMRSN-----EDEENFEEAIKAVNKALNRTKIPSSVEEIFNDDRCENLTSQSSSFWIMARALKEFVAEE-NGLLPLPGTL 313

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308006 241 PDMIADSGKYIKLQNVYREKAKKDAAAVGNHVAKLLQSIGQAPESISEKELKLLCSNSAFLRVVRCRSLAeeygldtink 320
Cdd:cd01493   314 PDMTADTEKYIKLQNIYREKAEKDAAEVEKYVREILKSLGRSPDSISDKEIKLFCKNAAFLRVIRGRSLE---------- 383

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308006 321 deiissmdnpdneivlylmlravdrfhkqqgrypgvsnyqveedigklkscltgflqeyglsvmvkddyvhefcrygaae 400
Cdd:cd01493       --------------------------------------------------------------------------------

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 2217308006 401 pHTIAAFLGGAAAQEVIKIITKQFVIFNNTYIYSGMSQTSATF 443
Cdd:cd01493   384 -HNISAFMGGIAAQEVIKLITKQYVPIDNTFIFDGIRSKSATF 425
E1-1_like cd01485
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ...
 1-77 7.26e-31

Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present universally in eukaryotic cells, is part of cascade to attach ubiquitin (Ub) covalently to substrate proteins. This cascade consists of activating (E1), conjugating (E2), and/or ligating (E3) enzymes and then targets them for degradation by the 26S proteasome. E1 activates ubiquitin by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and ubiquitin's C-terminus. The E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. A set of novel molecules with a structural similarity to Ub, called Ub-like proteins (Ubls), have similar conjugation cascades. In contrast to ubiquitin-E1, which is a single-chain protein with a weakly conserved two-fold repeat, many of the Ubls-E1are a heterodimer where each subunit corresponds to one half of a single-chain E1. This CD represents the family homologous to the first repeat of Ub-E1.


Pssm-ID: 238762 [Multi-domain]  Cd Length: 198  Bit Score: 117.52  E-value: 7.26e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217308006   1 MEFLQELNSDVSGSFVEESPENLLDNDPSFFCRFTVVVATQLPESTSLRLADVLWNSQIPLLICRTYGLVGYMRIII 77
Cdd:cd01485    81 YEFLQELNPNVKLSIVEEDSLSNDSNIEEYLQKFTLVIATEENYERTAKVNDVCRKHHIPFISCATYGLIGYAFFDF 157
E1-1_like cd01485
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ...
 403-443 8.59e-13

Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present universally in eukaryotic cells, is part of cascade to attach ubiquitin (Ub) covalently to substrate proteins. This cascade consists of activating (E1), conjugating (E2), and/or ligating (E3) enzymes and then targets them for degradation by the 26S proteasome. E1 activates ubiquitin by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and ubiquitin's C-terminus. The E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. A set of novel molecules with a structural similarity to Ub, called Ub-like proteins (Ubls), have similar conjugation cascades. In contrast to ubiquitin-E1, which is a single-chain protein with a weakly conserved two-fold repeat, many of the Ubls-E1are a heterodimer where each subunit corresponds to one half of a single-chain E1. This CD represents the family homologous to the first repeat of Ub-E1.


Pssm-ID: 238762 [Multi-domain]  Cd Length: 198  Bit Score: 67.06  E-value: 8.59e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2217308006 403 TIAAFLGGAAAQEVIKIITKQFVIFNNTYIYSGMSQTSATF 443
Cdd:cd01485   158 PIAAFLGGVVAQEAIKSISGKFTPLNNLYIYDGFESTGPMC 198
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 1-77 3.22e-10

Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes classical ubiquitin-activating enzymes E1, ubiquitin-like (ubl) activating enzymes and other mechanistic homologes, like MoeB, Thif1 and others. The common reaction mechanism catalyzed by MoeB, ThiF and the E1 enzymes begins with a nucleophilic attack of the C-terminal carboxylate of MoaD, ThiS and ubiquitin, respectively, on the alpha-phosphate of an ATP molecule bound at the active site of the activating enzymes, leading to the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of MoaD and ThiS.


Pssm-ID: 238760 [Multi-domain]  Cd Length: 143  Bit Score: 58.05  E-value: 3.22e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217308006   1 MEFLQELNSDVSGSFVEESPENllDNDPSFFCRFTVVVATQLPESTSLRLADVLWNSQIPLLICRTYGLVGYMRIII 77
Cdd:cd01483    59 ARRLNELNPGVNVTAVPEGISE--DNLDDFLDGVDLVIDAIDNIAVRRALNRACKELGIPVIDAGGLGLGGDIQVID 133
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 321-424 3.08e-07

ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino acids, of a multicopy family of eukaryotic proteins, many of which are designated ubiquitin-activating enzyme E1. Members have two copies of the ThiF family domain (pfam00899), a repeat found in ubiquitin-activating proteins (pfam02134), and other regions.


Pssm-ID: 273603 [Multi-domain]  Cd Length: 1006  Bit Score: 52.97  E-value: 3.08e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308006  321 DEIISSMDNPDNEIVLYLMLRAVDRFHKQQGRYPGVSNYQVEEDIGKLKSCLTGFLQEYglSVMVKDDYVHEFCRYGAAE 400
Cdd:TIGR01408  268 KCLIVDFSKPERPPEIHTAFQALDQFQEKYSRKPNVGCQQDAEELLKLATSISETLEEK--VPDVDAKLVHWLSWTAQGF 345

                           90       100
                   ....*....|....*....|....
gi 2217308006  401 PHTIAAFLGGAAAQEVIKIITKQF 424
Cdd:TIGR01408  346 LSPMAAAVGGVVSQEVLKAVTGKF 369
Aos1_SUMO cd01492
Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating ...
 404-437 9.88e-03

Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating enzyme (E1), specific for the SUMO family of ubiquitin-like proteins (Ubls). E1 enzymes are part of a conjugation cascade to attach Ub or Ubls, covalently to substrate proteins consisting of activating (E1), conjugating (E2), and/or ligating (E3) enzymes. E1 activates ubiquitin by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and Ubls C-terminus. The E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. Post-translational modification by SUMO family of ubiquitin-like proteins (Ublps) is involved in cell division, nuclear transport, the stress response and signal transduction. Aos1 contains part of the adenylation domain.


Pssm-ID: 238769 [Multi-domain]  Cd Length: 197  Bit Score: 37.27  E-value: 9.88e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2217308006 404 IAAFLGGAAAQEVIKIITKQFVIFNNTYIYSGMS 437
Cdd:cd01492   158 VAAVVGGILAQDVINALSKRESPLNNFFVFDGET 191
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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