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Conserved domains on  [gi|723747148|ref|XP_010313671|]
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NEDD8-activating enzyme E1 regulatory subunit AXR1 isoform X2 [Solanum lycopersicum]

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

Gene Ontology:  GO:0016567|GO:0045116|GO:0006974|GO:0031625|GO:0004839|GO:0046982|GO:0019781|GO:0006511
SCOP:  4000139|4007684

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 ...
 7-521 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: 609.31  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723747148   7 KYDRQLRIWGEKGQAALEKASICLLNCGPTGSETLKNLVLGGVGSITIVDGSKVEVGDLGNNFMVDESSVGQSKAECVCA 86
Cdd:cd01493    2 KYDRQLRLWGEHGQAALESAHVCLLNATATGTEILKNLVLPGIGSFTIVDGSKVDEEDLGNNFFLDASSLGKSRAEATCE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723747148  87 FLQELNDAVKAKFIEEHPEELIETNPSFFSQFTLVIATQLVEDSMVKLDRICREANIILIFARSYGLMGLVRISVKEHTV 166
Cdd:cd01493   82 LLQELNPDVNGSAVEESPEALLDNDPSFFSQFTVVIATNLPESTLLRLADVLWSANIPLLYVRSYGLYGYIRIQLKEHTI 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723747148 167 IESKPDHFLDDLRLNDPWPELRRFAETIDLNTTDAVVHKHTPYIIILVKMAEEWTNMHGGKFPSTREEKKQFKDLIKSKM 246
Cdd:cd01493  162 VESHPDNALEDLRLDNPFPELREHADSIDLDDMDPAEHSHTPYIVILIKYLEKWRSAHNGQLPSTYKEKKEFRDLVRSLM 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723747148 247 -STVDEENYKEAMEASFKVFSPVGIGPNLQKIINDSCAEV-DSNSSDFWVMVAAMKEFIASEgGGETPLEGSIPDMTSST 324
Cdd:cd01493  242 rSNEDEENFEEAIKAVNKALNRTKIPSSVEEIFNDDRCENlTSQSSSFWIMARALKEFVAEE-NGLLPLPGTLPDMTADT 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723747148 325 ELYVNLQKTYQAKAEADFLAMEQRVKNLLKKFSRDPASISKANIKSFCRNARKLAVCRYRlvedefnspaqpelqkyltd 404
Cdd:cd01493  321 EKYIKLQNIYREKAEKDAAEVEKYVREILKSLGRSPDSISDKEIKLFCKNAAFLRVIRGR-------------------- 380

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723747148 405 edygtaaglyillraadrfaanynkfpgqfdgemdedisrlkttavgllndlgcngssvsedlinemcrygaSELHVVAA 484
Cdd:cd01493  381 ------------------------------------------------------------------------SLEHNISA 388

                        490       500       510
                 ....*....|....*....|....*....|....*..
gi 723747148 485 FVGGVTSQEVIKLITRQFIPMSGTFIFNGIDHKSQLL 521
Cdd:cd01493  389 FMGGIAAQEVIKLITKQYVPIDNTFIFDGIRSKSATF 425
 
Name Accession Description Interval E-value
APPBP1_RUB cd01493
Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric ...
 7-521 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: 609.31  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723747148   7 KYDRQLRIWGEKGQAALEKASICLLNCGPTGSETLKNLVLGGVGSITIVDGSKVEVGDLGNNFMVDESSVGQSKAECVCA 86
Cdd:cd01493    2 KYDRQLRLWGEHGQAALESAHVCLLNATATGTEILKNLVLPGIGSFTIVDGSKVDEEDLGNNFFLDASSLGKSRAEATCE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723747148  87 FLQELNDAVKAKFIEEHPEELIETNPSFFSQFTLVIATQLVEDSMVKLDRICREANIILIFARSYGLMGLVRISVKEHTV 166
Cdd:cd01493   82 LLQELNPDVNGSAVEESPEALLDNDPSFFSQFTVVIATNLPESTLLRLADVLWSANIPLLYVRSYGLYGYIRIQLKEHTI 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723747148 167 IESKPDHFLDDLRLNDPWPELRRFAETIDLNTTDAVVHKHTPYIIILVKMAEEWTNMHGGKFPSTREEKKQFKDLIKSKM 246
Cdd:cd01493  162 VESHPDNALEDLRLDNPFPELREHADSIDLDDMDPAEHSHTPYIVILIKYLEKWRSAHNGQLPSTYKEKKEFRDLVRSLM 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723747148 247 -STVDEENYKEAMEASFKVFSPVGIGPNLQKIINDSCAEV-DSNSSDFWVMVAAMKEFIASEgGGETPLEGSIPDMTSST 324
Cdd:cd01493  242 rSNEDEENFEEAIKAVNKALNRTKIPSSVEEIFNDDRCENlTSQSSSFWIMARALKEFVAEE-NGLLPLPGTLPDMTADT 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723747148 325 ELYVNLQKTYQAKAEADFLAMEQRVKNLLKKFSRDPASISKANIKSFCRNARKLAVCRYRlvedefnspaqpelqkyltd 404
Cdd:cd01493  321 EKYIKLQNIYREKAEKDAAEVEKYVREILKSLGRSPDSISDKEIKLFCKNAAFLRVIRGR-------------------- 380

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723747148 405 edygtaaglyillraadrfaanynkfpgqfdgemdedisrlkttavgllndlgcngssvsedlinemcrygaSELHVVAA 484
Cdd:cd01493  381 ------------------------------------------------------------------------SLEHNISA 388

                        490       500       510
                 ....*....|....*....|....*....|....*..
gi 723747148 485 FVGGVTSQEVIKLITRQFIPMSGTFIFNGIDHKSQLL 521
Cdd:cd01493  389 FMGGIAAQEVIKLITKQYVPIDNTFIFDGIRSKSATF 425
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 8-158 7.97e-26

ThiF family; This domain is found in ubiquitin activating E1 family and members of the bacterial ThiF/MoeB/HesA family. It is repeated in Ubiquitin-activating enzyme E1.


Pssm-ID: 459987 [Multi-domain]  Cd Length: 238  Bit Score: 105.80  E-value: 7.97e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723747148    8 YDRQLRI--WGEKGQAALEKASICLLNCGPTGSETLKNLVLGGVGSITIVDGSKVEVGDLGNNFMVDESSVGQSKAECVC 85
Cdd:pfam00899   1 YSRQLALplIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 723747148   86 AFLQELNDAVKakfIEEHPEELIETNP-SFFSQFTLVI-ATqlveDSM---VKLDRICREANIILIFARSYGLMGLVR 158
Cdd:pfam00899  81 ERLREINPDVE---VEAYTERLTPENAeELIKSFDIVVdAT----DNFaarYLVNDACVKLGKPLIEAGVLGFKGQVT 151
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 8-158 5.61e-22

Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; Molybdopterin or thiamine biosynthesis adenylyltransferase is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 440244 [Multi-domain]  Cd Length: 244  Bit Score: 94.81  E-value: 5.61e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723747148   8 YDRQ--LRIWGEKGQAALEKASICLLNCGPTGSETLKNLVLGGVGSITIVDGSKVEVGDLGNNFMVDESSVGQSKAECVC 85
Cdd:COG0476    8 YSRQilLPEIGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADVGRPKVEAAA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723747148  86 AFLQELNDAVKakfIEEHPEELIETN-PSFFSQFTLVI------ATQLVedsmvkLDRICREANIILIFA---RSYGLMG 155
Cdd:COG0476   88 ERLRALNPDVE---VEAIPERLTEENaLELLAGADLVLdctdnfATRYL------LNDACVKLGIPLVSGaviGFEGQVT 158


                 ...
gi 723747148 156 LVR 158
Cdd:COG0476  159 VFI 161
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 8-515 4.55e-18

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: 88.02  E-value: 4.55e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723747148     8 YDRQLRIWGEKGQAALEKASICLLNCGPTGSETLKNLVLGGVGSITIVDGSKVEVGDLGNNFMVDESSVGQSKAECVCAF 87
Cdd:TIGR01408    7 YSRQLYVLGDEAMQKMAKSNVLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLSSNFFLSEDDVGRNRAEAVVKK 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723747148    88 LQELNDAVKAKFIEEhpeeliETNPSFFSQFTLVIATQLVEDSMVKLDRICRE--ANIILIFARSYGLMGLVrisvkeht 165
Cdd:TIGR01408   87 LAELNPYVHVSSSSV------PFNEEFLDKFQCVVLTEMSLPLQKEINDFCHSqcPPIAFISADVRGLFGSL-------- 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723747148   166 vieskpdhFLDdlrlndpwpelrrFAETIDLNTTDAvvhkHTPYIIILVKMaeewTNMHGGKFPSTREEKKQFKDliksk 245
Cdd:TIGR01408  153 --------FCD-------------FGDEFEVLDTDG----EEPKTGFIASI----TQANPGIVTCLENHRHKLET----- 198

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723747148   246 mstvdeenykeameASFKVFSPVgigpnlqkiindscaevdsnssdfwvmvaamkefiasegGGETPLEGSIPDMTSSTE 325
Cdd:TIGR01408  199 --------------GDFVTFREV---------------------------------------NGMTGLNDGSPRKITVIS 225

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723747148   326 LYvnlqkTYQAKAEADFlamEQRVKNLLKKFSRDPASIskaNIKSFcRNARKLAVCRYrlveDEFNSPAQPELqkyltde 405
Cdd:TIGR01408  226 PY-----SFSIGDTTEL---GPYLHGGIATQVKTPKTV---FFKSL-REQLKDPKCLI----VDFSKPERPPE------- 282

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723747148   406 dygtaagLYILLRAADRFAANYNKFPgqfDGEMDEDISRLKTTAVGLLNDLGCNGSSVSEDLINEMCRYGASELHVVAAF 485
Cdd:TIGR01408  283 -------IHTAFQALDQFQEKYSRKP---NVGCQQDAEELLKLATSISETLEEKVPDVDAKLVHWLSWTAQGFLSPMAAA 352

                          490       500       510
                   ....*....|....*....|....*....|
gi 723747148   486 VGGVTSQEVIKLITRQFIPMSGTFIFNGID 515
Cdd:TIGR01408  353 VGGVVSQEVLKAVTGKFSPLCQWFYFDSAE 382
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
2-134 4.76e-10

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 61.18  E-value: 4.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723747148   2 AEPKVKYDRQLRI--WGEKGQAALEKASICLLNCGPTGSETLKNLVLGGVGSITIVDGSKVEVGDLGNNFMVDESSVGQS 79
Cdd:PRK08762 110 DEQDERYSRHLRLpeVGEEGQRRLLEARVLLIGAGGLGSPAALYLAAAGVGTLGIVDHDVVDRSNLQRQILHTEDRVGQP 189

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 723747148  80 KAECVCAFLQELNDAVKakfIEEHPEELIETN-PSFFSQFTLVI-------ATQLVEDSMVKL 134
Cdd:PRK08762 190 KVDSAAQRLAALNPDVQ---VEAVQERVTSDNvEALLQDVDVVVdgadnfpTRYLLNDACVKL 249
 
Name Accession Description Interval E-value
APPBP1_RUB cd01493
Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric ...
 7-521 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: 609.31  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723747148   7 KYDRQLRIWGEKGQAALEKASICLLNCGPTGSETLKNLVLGGVGSITIVDGSKVEVGDLGNNFMVDESSVGQSKAECVCA 86
Cdd:cd01493    2 KYDRQLRLWGEHGQAALESAHVCLLNATATGTEILKNLVLPGIGSFTIVDGSKVDEEDLGNNFFLDASSLGKSRAEATCE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723747148  87 FLQELNDAVKAKFIEEHPEELIETNPSFFSQFTLVIATQLVEDSMVKLDRICREANIILIFARSYGLMGLVRISVKEHTV 166
Cdd:cd01493   82 LLQELNPDVNGSAVEESPEALLDNDPSFFSQFTVVIATNLPESTLLRLADVLWSANIPLLYVRSYGLYGYIRIQLKEHTI 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723747148 167 IESKPDHFLDDLRLNDPWPELRRFAETIDLNTTDAVVHKHTPYIIILVKMAEEWTNMHGGKFPSTREEKKQFKDLIKSKM 246
Cdd:cd01493  162 VESHPDNALEDLRLDNPFPELREHADSIDLDDMDPAEHSHTPYIVILIKYLEKWRSAHNGQLPSTYKEKKEFRDLVRSLM 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723747148 247 -STVDEENYKEAMEASFKVFSPVGIGPNLQKIINDSCAEV-DSNSSDFWVMVAAMKEFIASEgGGETPLEGSIPDMTSST 324
Cdd:cd01493  242 rSNEDEENFEEAIKAVNKALNRTKIPSSVEEIFNDDRCENlTSQSSSFWIMARALKEFVAEE-NGLLPLPGTLPDMTADT 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723747148 325 ELYVNLQKTYQAKAEADFLAMEQRVKNLLKKFSRDPASISKANIKSFCRNARKLAVCRYRlvedefnspaqpelqkyltd 404
Cdd:cd01493  321 EKYIKLQNIYREKAEKDAAEVEKYVREILKSLGRSPDSISDKEIKLFCKNAAFLRVIRGR-------------------- 380

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723747148 405 edygtaaglyillraadrfaanynkfpgqfdgemdedisrlkttavgllndlgcngssvsedlinemcrygaSELHVVAA 484
Cdd:cd01493  381 ------------------------------------------------------------------------SLEHNISA 388

                        490       500       510
                 ....*....|....*....|....*....|....*..
gi 723747148 485 FVGGVTSQEVIKLITRQFIPMSGTFIFNGIDHKSQLL 521
Cdd:cd01493  389 FMGGIAAQEVIKLITKQYVPIDNTFIFDGIRSKSATF 425
E1-1_like cd01485
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ...
 7-159 1.92e-44

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: 155.27  E-value: 1.92e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723747148   7 KYDRQLRIWGEKGQAALEKASICLLNCGPTGSETLKNLVLGGVGSITIVDGSKVEVGDLGNNFMVD--ESSVGQSKAECV 84
Cdd:cd01485    1 LYDRQIRLWGDEAQNKLRSAKVLIIGAGALGAEIAKNLVLAGIDSITIVDHRLVSTEDLGSNFFLDaeVSNSGMNRAAAS 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 723747148  85 CAFLQELNDAVKAKFIEEHPEELIETNPSFFSQFTLVIATQLVEDSMVKLDRICREANIILIFARSYGLMGLVRI 159
Cdd:cd01485   81 YEFLQELNPNVKLSIVEEDSLSNDSNIEEYLQKFTLVIATEENYERTAKVNDVCRKHHIPFISCATYGLIGYAFF 155
Aos1_SUMO cd01492
Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating ...
 8-157 2.31e-40

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: 144.36  E-value: 2.31e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723747148   8 YDRQLRIWGEKGQAALEKASICLLNCGPTGSETLKNLVLGGVGSITIVDGSKVEVGDLGNNFMVDESSVGQSKAECVCAF 87
Cdd:cd01492    4 YDRQIRLWGLEAQKRLRSARILLIGLKGLGAEIAKNLVLSGIGSLTILDDRTVTEEDLGAQFLIPAEDLGQNRAEASLER 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723747148  88 LQELNDAVKAKFIEehpEELIETNPSFFSQFTLVIATQLVEDSMVKLDRICREANIILIFARSYGLMGLV 157
Cdd:cd01492   84 LRALNPRVKVSVDT---DDISEKPEEFFSQFDVVVATELSRAELVKINELCRKLGVKFYATGVHGLFGFV 150
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 8-158 7.97e-26

ThiF family; This domain is found in ubiquitin activating E1 family and members of the bacterial ThiF/MoeB/HesA family. It is repeated in Ubiquitin-activating enzyme E1.


Pssm-ID: 459987 [Multi-domain]  Cd Length: 238  Bit Score: 105.80  E-value: 7.97e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723747148    8 YDRQLRI--WGEKGQAALEKASICLLNCGPTGSETLKNLVLGGVGSITIVDGSKVEVGDLGNNFMVDESSVGQSKAECVC 85
Cdd:pfam00899   1 YSRQLALplIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 723747148   86 AFLQELNDAVKakfIEEHPEELIETNP-SFFSQFTLVI-ATqlveDSM---VKLDRICREANIILIFARSYGLMGLVR 158
Cdd:pfam00899  81 ERLREINPDVE---VEAYTERLTPENAeELIKSFDIVVdAT----DNFaarYLVNDACVKLGKPLIEAGVLGFKGQVT 151
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 28-159 9.08e-25

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: 99.65  E-value: 9.08e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723747148  28 ICLLNCGPTGSETLKNLVLGGVGSITIVDGSKVEVGDLGNNFMVDESSVGQSKAECVCAFLQELNDAVKAKFIEEHPEEl 107
Cdd:cd01483    2 VLLVGLGGLGSEIALNLARSGVGKITLIDFDTVELSNLNRQFLARQADIGKPKAEVAARRLNELNPGVNVTAVPEGISE- 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 723747148 108 iETNPSFFSQFTLVIATQLVEDSMVKLDRICREANIILIFARSYGLMGLVRI 159
Cdd:cd01483   81 -DNLDDFLDGVDLVIDAIDNIAVRRALNRACKELGIPVIDAGGLGLGGDIQV 131
Ube1_repeat1 cd01491
Ubiquitin activating enzyme (E1), repeat 1. E1, a highly conserved small protein present ...
 8-155 1.97e-23

Ubiquitin activating enzyme (E1), repeat 1. 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. E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. Ubiquitin-E1 is a single-chain protein with a weakly conserved two-fold repeat. This CD represents the first repeat of Ub-E1.


Pssm-ID: 238768 [Multi-domain]  Cd Length: 286  Bit Score: 100.03  E-value: 1.97e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723747148   8 YDRQLRIWGEKGQAALEKASICLLNCGPTGSETLKNLVLGGVGSITIVDGSKVEVGDLGNNFMVDESSVGQSKAECVCAF 87
Cdd:cd01491    2 YSRQLYVLGHEAMKKLQKSNVLISGLGGLGVEIAKNLILAGVKSVTLHDTKPCSWSDLSSQFYLREEDIGKNRAEASQAR 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 723747148  88 LQELNDAVKAKFIEEhpeeliETNPSFFSQFTLVIATQLVEDSMVKLDRICREANIILIFARSYGLMG 155
Cdd:cd01491   82 LAELNPYVPVTVSTG------PLTTDELLKFQVVVLTDASLEDQLKINEFCHSPGIKFISADTRGLFG 143
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 8-158 5.61e-22

Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; Molybdopterin or thiamine biosynthesis adenylyltransferase is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 440244 [Multi-domain]  Cd Length: 244  Bit Score: 94.81  E-value: 5.61e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723747148   8 YDRQ--LRIWGEKGQAALEKASICLLNCGPTGSETLKNLVLGGVGSITIVDGSKVEVGDLGNNFMVDESSVGQSKAECVC 85
Cdd:COG0476    8 YSRQilLPEIGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADVGRPKVEAAA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723747148  86 AFLQELNDAVKakfIEEHPEELIETN-PSFFSQFTLVI------ATQLVedsmvkLDRICREANIILIFA---RSYGLMG 155
Cdd:COG0476   88 ERLRALNPDVE---VEAIPERLTEENaLELLAGADLVLdctdnfATRYL------LNDACVKLGIPLVSGaviGFEGQVT 158


                 ...
gi 723747148 156 LVR 158
Cdd:COG0476  159 VFI 161
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 8-158 1.14e-20

ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis family. The common reaction mechanism catalyzed by MoeB and ThiF, like other E1 enzymes, begins with a nucleophilic attack of the C-terminal carboxylate of MoaD and ThiS, 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. MoeB, as the MPT synthase (MoaE/MoaD complex) sulfurase, is involved in the biosynthesis of the molybdenum cofactor, a derivative of the tricyclic pterin, molybdopterin (MPT). ThiF catalyzes the adenylation of ThiS, as part of the biosynthesis pathway of thiamin pyrophosphate (vitamin B1).


Pssm-ID: 238386 [Multi-domain]  Cd Length: 228  Bit Score: 90.61  E-value: 1.14e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723747148   8 YDRQLRI--WGEKGQAALEKASICLLNCGPTGSETLKNLVLGGVGSITIVDGSKVEVGDLGNNFMVDESSVGQSKAECVC 85
Cdd:cd00757    2 YSRQILLpeIGEEGQEKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRQILHTEADVGQPKAEAAA 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 723747148  86 AFLQELNDAVKakfIEEHPEELIETN-PSFFSQFTLVI-ATQLVEDSMVkLDRICREANIILIFA---RSYGLMGLVR 158
Cdd:cd00757   82 ERLRAINPDVE---IEAYNERLDAENaEELIAGYDLVLdCTDNFATRYL-INDACVKLGKPLVSGavlGFEGQVTVFI 155
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 8-515 4.55e-18

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: 88.02  E-value: 4.55e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723747148     8 YDRQLRIWGEKGQAALEKASICLLNCGPTGSETLKNLVLGGVGSITIVDGSKVEVGDLGNNFMVDESSVGQSKAECVCAF 87
Cdd:TIGR01408    7 YSRQLYVLGDEAMQKMAKSNVLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLSSNFFLSEDDVGRNRAEAVVKK 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723747148    88 LQELNDAVKAKFIEEhpeeliETNPSFFSQFTLVIATQLVEDSMVKLDRICRE--ANIILIFARSYGLMGLVrisvkeht 165
Cdd:TIGR01408   87 LAELNPYVHVSSSSV------PFNEEFLDKFQCVVLTEMSLPLQKEINDFCHSqcPPIAFISADVRGLFGSL-------- 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723747148   166 vieskpdhFLDdlrlndpwpelrrFAETIDLNTTDAvvhkHTPYIIILVKMaeewTNMHGGKFPSTREEKKQFKDliksk 245
Cdd:TIGR01408  153 --------FCD-------------FGDEFEVLDTDG----EEPKTGFIASI----TQANPGIVTCLENHRHKLET----- 198

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723747148   246 mstvdeenykeameASFKVFSPVgigpnlqkiindscaevdsnssdfwvmvaamkefiasegGGETPLEGSIPDMTSSTE 325
Cdd:TIGR01408  199 --------------GDFVTFREV---------------------------------------NGMTGLNDGSPRKITVIS 225

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723747148   326 LYvnlqkTYQAKAEADFlamEQRVKNLLKKFSRDPASIskaNIKSFcRNARKLAVCRYrlveDEFNSPAQPELqkyltde 405
Cdd:TIGR01408  226 PY-----SFSIGDTTEL---GPYLHGGIATQVKTPKTV---FFKSL-REQLKDPKCLI----VDFSKPERPPE------- 282

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723747148   406 dygtaagLYILLRAADRFAANYNKFPgqfDGEMDEDISRLKTTAVGLLNDLGCNGSSVSEDLINEMCRYGASELHVVAAF 485
Cdd:TIGR01408  283 -------IHTAFQALDQFQEKYSRKP---NVGCQQDAEELLKLATSISETLEEKVPDVDAKLVHWLSWTAQGFLSPMAAA 352

                          490       500       510
                   ....*....|....*....|....*....|
gi 723747148   486 VGGVTSQEVIKLITRQFIPMSGTFIFNGID 515
Cdd:TIGR01408  353 VGGVVSQEVLKAVTGKFSPLCQWFYFDSAE 382
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 27-123 7.13e-11

Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 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. UBA3 contains both the nucleotide-binding motif involved in adenylation and the catalytic cysteine involved in the thioester intermediate and Ublp transfer to E2.


Pssm-ID: 238765 [Multi-domain]  Cd Length: 291  Bit Score: 63.14  E-value: 7.13e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723747148  27 SICLLNCGPTGSETLKNLVLGGVGSITIVDGSKVEVGDLGNNFMVDESSVGQSKAECVCAFLQELNDAVKakfIEEHPEE 106
Cdd:cd01488    1 KILVIGAGGLGCELLKNLALSGFRNIHVIDMDTIDVSNLNRQFLFREKDIGKPKAEVAAKFVNDRVPGVN---VTPHFGK 77

                         90
                 ....*....|....*..
gi 723747148 107 LIETNPSFFSQFTLVIA 123
Cdd:cd01488   78 IQDKDEEFYRQFNIIIC 94
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 34-165 2.03e-10

Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 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. UBA2 contains both the nucleotide-binding motif involved in adenylation and the catalytic cysteine involved in the thioester intermediate and Ublp transfer to E2.


Pssm-ID: 238766 [Multi-domain]  Cd Length: 312  Bit Score: 62.01  E-value: 2.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723747148  34 GPTGSETLKNLVLGGVGSITIVDGSKVEVGDLGNNFMVDESSVGQSKAECVCAFLQELNDAVKakfIEEHPEELIET--N 111
Cdd:cd01489    8 GGIGCELLKNLVLTGFGEIHIIDLDTIDLSNLNRQFLFRKKHVGKSKAQVAKEAVLSFNPNVK---IVAYHANIKDPdfN 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 723747148 112 PSFFSQFTLVIATQLVEDSMVKLDRICREANIILIFARSYGLMGLVRISVKEHT 165
Cdd:cd01489   85 VEFFKQFDLVFNALDNLAARRHVNKMCLAADVPLIESGTTGFLGQVQVIKKGKT 138
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 7-138 3.58e-10

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: 62.60  E-value: 3.58e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723747148     7 KYDRQLRIWGEKGQAALEKASICLLNCGPTGSETLKNLVLGGV-----GSITIVDGSKVEVGDLGNNFMVDESSVGQSKA 81
Cdd:TIGR01408  401 RYDAQIAVFGDTFQQKLQNLNIFLVGCGAIGCEMLKNFALMGVgtgkkGMITVTDPDLIEKSNLNRQFLFRPHHIGKPKS 480

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 723747148    82 ECVCAFLQELNDAVKakfIEEHPEELIET-----NPSFFSQFTLVI-ATQLVEDSMVkLDRIC 138
Cdd:TIGR01408  481 YTAADATLKINPQIK---IDAHQNRVGPEtetifNDEFYEKLDVVInALDNVEARRY-VDSRC 539
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
2-134 4.76e-10

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 61.18  E-value: 4.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723747148   2 AEPKVKYDRQLRI--WGEKGQAALEKASICLLNCGPTGSETLKNLVLGGVGSITIVDGSKVEVGDLGNNFMVDESSVGQS 79
Cdd:PRK08762 110 DEQDERYSRHLRLpeVGEEGQRRLLEARVLLIGAGGLGSPAALYLAAAGVGTLGIVDHDVVDRSNLQRQILHTEDRVGQP 189

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 723747148  80 KAECVCAFLQELNDAVKakfIEEHPEELIETN-PSFFSQFTLVI-------ATQLVEDSMVKL 134
Cdd:PRK08762 190 KVDSAAQRLAALNPDVQ---VEAVQERVTSDNvEALLQDVDVVVdgadnfpTRYLLNDACVKL 249
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 1-96 6.39e-10

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 60.66  E-value: 6.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723747148   1 MAEPKVKYDRQ--LRIWGEKGQAALEKASICLLNCGPTGSETLKNLVLGGVGSITIVDGSKVEVGDLGNNFMVDESSVGQ 78
Cdd:PRK05597   2 KNLDIARYRRQimLGEIGQQGQQSLFDAKVAVIGAGGLGSPALLYLAGAGVGHITIIDDDTVDLSNLHRQVIHSTAGVGQ 81

                         90
                 ....*....|....*...
gi 723747148  79 SKAECVCAFLQELNDAVK 96
Cdd:PRK05597  82 PKAESAREAMLALNPDVK 99
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
 27-165 8.88e-10

Ubiquitin activating enzyme (E1), repeat 2-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. 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 second repeat of Ub-E1.


Pssm-ID: 238761 [Multi-domain]  Cd Length: 234  Bit Score: 59.13  E-value: 8.88e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723747148  27 SICLLNCGPTGSETLKNLVLGGVGSITIVDGSKVEVGDLGNNFMVDESSVGQSKAECVCAFLQELNDAVKAKFIEEHPEE 106
Cdd:cd01484    1 KVLLVGAGGIGCELLKNLALMGFGQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKSEVAAEAVNDRNPNCKVVPYQNKVGP 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 723747148 107 LIETNPSFFSQFTLVI-ATQLVEDSMVkLDRICREANIILIFARSYGLMGLVRISVKEHT 165
Cdd:cd01484   81 EQDFNDTFFEQFHIIVnALDNIIARRY-VNGMLIFLIVPLIESGTEGFKGNAQVILPGMT 139
PTZ00245 PTZ00245
ubiquitin activating enzyme; Provisional
 6-95 4.31e-08

ubiquitin activating enzyme; Provisional


Pssm-ID: 140272  Cd Length: 287  Bit Score: 54.68  E-value: 4.31e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723747148   6 VKYDRQLRIWGEKGQAALEKASICLLNCGPTGSETLKNLVLGGVGSITIVDGSKVEVGDLGNNFMVDESSVGQSKAECVC 85
Cdd:PTZ00245   7 VRYDRQIRLWGKSTQQQLMHTSVALHGVAGAAAEAAKNLVLAGVRAVAVADEGLVTDADVCTNYLMQGEAGGTRGARALG 86

                         90
                 ....*....|
gi 723747148  86 AfLQELNDAV 95
Cdd:PTZ00245  87 A-LQRLNPHV 95
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 7-136 4.46e-08

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 55.10  E-value: 4.46e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723747148   7 KYDRQLRI--WGEKGQAALEKASICLLNCGPTGSETLKNLVLGGVGSITIVDGSKVEVGDLGNNFMVDESSVGQSKAECV 84
Cdd:PRK07878  22 RYSRHLIIpdVGVDGQKRLKNARVLVIGAGGLGSPTLLYLAAAGVGTLGIVEFDVVDESNLQRQVIHGQSDVGRSKAQSA 101

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 723747148  85 CAFLQELNDAVKAKFieeHPEELIETNP-SFFSQFTLVI------ATQ-LVEDSMVKLDR 136
Cdd:PRK07878 102 RDSIVEINPLVNVRL---HEFRLDPSNAvELFSQYDLILdgtdnfATRyLVNDAAVLAGK 158
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
 16-146 7.93e-07

Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli hypothetical protein ygdL. The common reaction mechanism catalyzed by E1-like enzymes begins with a nucleophilic attack of the C-terminal carboxylate of the ubiquitin-like substrate, 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 the substrate. The exact function of this family is unknown.


Pssm-ID: 238384 [Multi-domain]  Cd Length: 231  Bit Score: 50.30  E-value: 7.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723747148  16 GEKGQAALEKASICLLNCGPTGSETLKNLVLGGVGSITIVDGSKVEVGDLGNNFMVDESSVGQSKAECVCAFLQELN--- 92
Cdd:cd00755    2 GEEGLEKLRNAHVAVVGLGGVGSWAAEALARSGVGKLTLIDFDVVCVSNLNRQIHALLSTVGKPKVEVMAERIRDINpec 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 723747148  93 --DAVKAKFIEEHPEELIETNPSFfsqftLVIATQLVeDSMVKLDRICREANIILI 146
Cdd:cd00755   82 evDAVEEFLTPDNSEDLLGGDPDF-----VVDAIDSI-RAKVALIAYCRKRKIPVI 131
PRK08328 PRK08328
hypothetical protein; Provisional
 7-111 1.21e-06

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 49.79  E-value: 1.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723747148   7 KYDRQLRIWGEKGQAALEKASICLLNCGPTGSETLKNLVLGGVGSITIVDGSKVEVGDLGNNFMVDESSVGQ-SKAECVC 85
Cdd:PRK08328   9 RYDRQIMIFGVEGQEKLKKAKVAVVGVGGLGSPVAYYLAAAGVGRILLIDEQTPELSNLNRQILHWEEDLGKnPKPLSAK 88

                         90       100
                 ....*....|....*....|....*.
gi 723747148  86 AFLQELNDAVKakfIEEHPEELIETN 111
Cdd:PRK08328  89 WKLERFNSDIK---IETFVGRLSEEN 111
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
16-122 1.44e-06

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 49.08  E-value: 1.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723747148  16 GEKGQAALEKASICLLNCGPTGSETLKNLVLGGVGSITIVDGSKVEVGDLgN--NFMVDEssVGQSKAECVCAFLQELND 93
Cdd:PRK08644  19 TPKLLEKLKKAKVGIAGAGGLGSNIAVALARSGVGNLKLVDFDVVEPSNL-NrqQYFISQ--IGMPKVEALKENLLEINP 95

                         90       100       110
                 ....*....|....*....|....*....|
gi 723747148  94 AVKakfIEEHPEELIETN-PSFFSQFTLVI 122
Cdd:PRK08644  96 FVE---IEAHNEKIDEDNiEELFKDCDIVV 122
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 7-122 1.62e-06

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 49.46  E-value: 1.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723747148   7 KYDRQ--LRIWGEKGQAALEKASICLLNCGPTGSETLKNLVLGGVGSITIVDGSKVEVGDLGNNFMVDESSVGQSKAECV 84
Cdd:PRK05690  12 RYNRQiiLRGFDFDGQEKLKAARVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVSLSNLQRQVLHDDATIGQPKVESA 91

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 723747148  85 CAFLQELNDAVKakfIEEHPEELIETN-PSFFSQFTLVI 122
Cdd:PRK05690  92 RAALARINPHIA---IETINARLDDDElAALIAGHDLVL 127
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 7-153 4.71e-06

thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 48.84  E-value: 4.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723747148   7 KYDRQLR---IwGEKGQAALEKASICLLNCGPTGSETLKNLVLGGVGSITIVDGSKVEVGDLGNNFMVDESSVGQSKAEC 83
Cdd:PRK07688   4 RYSRQELfspI-GEEGQQKLREKHVLIIGAGALGTANAEMLVRAGVGKVTIVDRDYVEWSNLQRQQLYTESDVKNNLPKA 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 723747148  84 VCA--FLQELNDAVKAK-FIEEHPEELIEtnpSFFSQFTLVI-ATQLVEDSMVKLDrICREANIILIFA---RSYGL 153
Cdd:PRK07688  83 VAAkkRLEEINSDVRVEaIVQDVTAEELE---ELVTGVDLIIdATDNFETRFIVND-AAQKYGIPWIYGacvGSYGL 155
TcdA COG1179
tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ...
 8-146 9.26e-06

tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and biogenesis]; tRNA A37 threonylcarbamoyladenosine dehydratase is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440792  Cd Length: 247  Bit Score: 47.00  E-value: 9.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723747148   8 YDRQL----RIWGEKGQAALEKASICLLNCGPTGSETLKNLVLGGVGSITIVDGSKVEVGDLGNNFMVDESSVGQSKAEC 83
Cdd:COG1179    3 MERRFsrteRLYGEEGLERLANAHVAVVGLGGVGSWAAEALARSGVGRLTLVDLDDVCESNINRQLHALDSTVGRPKVEV 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 723747148  84 VCAFLQELN-----DAVKAKFIEEHPEELIETNPSFfsqftlVI-ATqlveDSM-VKLDRI--CREANIILI 146
Cdd:COG1179   83 MAERIRDINpdcevTAIDEFVTPENADELLSEDYDY------VIdAI----DSVsAKAALIawCRRRGIPII 144
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 1-110 4.65e-05

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 45.49  E-value: 4.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723747148   1 MAEpkvKYDRQLRI--WGEKGQAALEKASICLLNCGPTGSETLKNLVLGGVGSITIVDGSKVEVGDLGNNFMVDESSVGQ 78
Cdd:PRK12475   1 MQE---RYSRQILFsgIGEEGQRKIREKHVLIVGAGALGAANAEALVRAGIGKLTIADRDYVEWSNLQRQQLYTEEDAKQ 77

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 723747148  79 SKAECVCA--FLQELN-----DAVKAKFIEEHPEELIET 110
Cdd:PRK12475  78 KKPKAIAAkeHLRKINseveiVPVVTDVTVEELEELVKE 116
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
 30-123 7.16e-05

Ubiquitin activating enzyme (E1), repeat 2. 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. E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. Ubiquitin-E1 is a single-chain protein with a weakly conserved two-fold repeat. This CD represents the second repeat of Ub-E1.


Pssm-ID: 238767 [Multi-domain]  Cd Length: 435  Bit Score: 45.36  E-value: 7.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723747148  30 LLNCGPTGSETLKNLVLGGVGS-----ITIVDGSKVEVGDLGNNFMVDESSVGQSKAECVCAFLQELNDAVKakfIEEHP 104
Cdd:cd01490    4 LVGAGAIGCELLKNFALMGVGTgesgeITVTDMDNIEKSNLNRQFLFRPHDVGKPKSEVAAAAVKAMNPDLK---ITALQ 80

                         90       100
                 ....*....|....*....|....
gi 723747148 105 EEL-IET----NPSFFSQFTLVIA 123
Cdd:cd01490   81 NRVgPETehifNDEFWEKLDGVAN 104
PRK15116 PRK15116
sulfur acceptor protein CsdL; Provisional
 13-92 7.74e-05

sulfur acceptor protein CsdL; Provisional


Pssm-ID: 185071  Cd Length: 268  Bit Score: 44.41  E-value: 7.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723747148  13 RIWGEKGQAALEKASICLLNCGPTGSETLKNLVLGGVGSITIVDGSKVEVGDLGNNFMVDESSVGQSKAECVCAFLQELN 92
Cdd:PRK15116  18 RLYGEKALQLFADAHICVVGIGGVGSWAAEALARTGIGAITLIDMDDVCVTNTNRQIHALRDNVGLAKAEVMAERIRQIN 97
E1-1_like cd01485
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ...
 482-519 4.47e-04

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: 41.64  E-value: 4.47e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 723747148 482 VAAFVGGVTSQEVIKLITRQFIPMSGTFIFNGIDHKSQ 519
Cdd:cd01485  159 IAAFLGGVVAQEAIKSISGKFTPLNNLYIYDGFESTGP 196
Aos1_SUMO cd01492
Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating ...
 468-515 1.83e-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: 39.58  E-value: 1.83e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 723747148 468 INEMCR--------------YG---ASELHVVAAFVGGVTSQEVIKLITRQFIPMSGTFIFNGID 515
Cdd:cd01492  127 INELCRklgvkfyatgvhglFGfvfADLLAPVAAVVGGILAQDVINALSKRESPLNNFFVFDGET 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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