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Conserved domains on  [gi|41053883|ref|NP_956793|]
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NEDD8-activating enzyme E1 regulatory subunit [Danio rerio]

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 ...
 10-531 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: 720.24  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053883  10 QRYDRQLRLWGDHGQEALENAHVCLINATASGTEILKNLVLPGIGAFTIVDGHKVSGEDVGNNFFLSSSAIGKNRAQAAT 89
Cdd:cd01493   1 QKYDRQLRLWGEHGQAALESAHVCLLNATATGTEILKNLVLPGIGSFTIVDGSKVDEEDLGNNFFLDASSLGKSRAEATC 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053883  90 ELLQELNSDVSGNFVEESPDKLLDNDCEFFHRFSLVIAVQLPESTCLGLGAVLWEAGVPFLVCRTYGLIGYMRLIVKEHT 169
Cdd:cd01493  81 ELLQELNPDVNGSAVEESPEALLDNDPSFFSQFTVVIATNLPESTLLRLADVLWSANIPLLYVRSYGLYGYIRIQLKEHT 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053883 170 VVESHPDNALEDLRLDQPFTELKRHVESYDLDNMEKKDHSHTPWIIVVARYLEKWYNENNSQLPKNYKEKEAFRQLLREG 249
Cdd:cd01493 161 IVESHPDNALEDLRLDNPFPELREHADSIDLDDMDPAEHSHTPYIVILIKYLEKWRSAHNGQLPSTYKEKKEFRDLVRSL 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053883 250 ILKNengglEDEENFEEAIKNVNTALNPTKISSGTQDIFNAEQCENITSQSSSFWVMAHGVRDFVQNEgNGNLPVRGSIP 329
Cdd:cd01493 241 MRSN-----EDEENFEEAIKAVNKALNRTKIPSSVEEIFNDDRCENLTSQSSSFWIMARALKEFVAEE-NGLLPLPGTLP 314

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053883 330 DMIADSDKFIKLQNVYRDKAMRDAAVVSKHVEMLLQSVGKTPESISEQEIKLFCKNAAFLRVVRCRSLAdeysvdtfnkd 409
Cdd:cd01493 315 DMTADTEKYIKLQNIYREKAEKDAAEVEKYVREILKSLGRSPDSISDKEIKLFCKNAAFLRVIRGRSLE----------- 383

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053883 410 eitscmdspdsemvlylmlrsvdrfyqqhsrypgvynyqveedinklklcvnsllqeyslnvnvkddyihefcrygaaep 489
Cdd:cd01493     --------------------------------------------------------------------------------

                       490       500       510       520
                ....*....|....*....|....*....|....*....|..
gi 41053883 490 HTVAAFLGGSAAQEAIKIITHQFVPFNNTFLYNAMSQTSATF 531
Cdd:cd01493 384 HNISAFMGGIAAQEVIKLITKQYVPIDNTFIFDGIRSKSATF 425
 
Name Accession Description Interval E-value
APPBP1_RUB cd01493
Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric ...
 10-531 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: 720.24  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053883  10 QRYDRQLRLWGDHGQEALENAHVCLINATASGTEILKNLVLPGIGAFTIVDGHKVSGEDVGNNFFLSSSAIGKNRAQAAT 89
Cdd:cd01493   1 QKYDRQLRLWGEHGQAALESAHVCLLNATATGTEILKNLVLPGIGSFTIVDGSKVDEEDLGNNFFLDASSLGKSRAEATC 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053883  90 ELLQELNSDVSGNFVEESPDKLLDNDCEFFHRFSLVIAVQLPESTCLGLGAVLWEAGVPFLVCRTYGLIGYMRLIVKEHT 169
Cdd:cd01493  81 ELLQELNPDVNGSAVEESPEALLDNDPSFFSQFTVVIATNLPESTLLRLADVLWSANIPLLYVRSYGLYGYIRIQLKEHT 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053883 170 VVESHPDNALEDLRLDQPFTELKRHVESYDLDNMEKKDHSHTPWIIVVARYLEKWYNENNSQLPKNYKEKEAFRQLLREG 249
Cdd:cd01493 161 IVESHPDNALEDLRLDNPFPELREHADSIDLDDMDPAEHSHTPYIVILIKYLEKWRSAHNGQLPSTYKEKKEFRDLVRSL 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053883 250 ILKNengglEDEENFEEAIKNVNTALNPTKISSGTQDIFNAEQCENITSQSSSFWVMAHGVRDFVQNEgNGNLPVRGSIP 329
Cdd:cd01493 241 MRSN-----EDEENFEEAIKAVNKALNRTKIPSSVEEIFNDDRCENLTSQSSSFWIMARALKEFVAEE-NGLLPLPGTLP 314

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053883 330 DMIADSDKFIKLQNVYRDKAMRDAAVVSKHVEMLLQSVGKTPESISEQEIKLFCKNAAFLRVVRCRSLAdeysvdtfnkd 409
Cdd:cd01493 315 DMTADTEKYIKLQNIYREKAEKDAAEVEKYVREILKSLGRSPDSISDKEIKLFCKNAAFLRVIRGRSLE----------- 383

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053883 410 eitscmdspdsemvlylmlrsvdrfyqqhsrypgvynyqveedinklklcvnsllqeyslnvnvkddyihefcrygaaep 489
Cdd:cd01493     --------------------------------------------------------------------------------

                       490       500       510       520
                ....*....|....*....|....*....|....*....|..
gi 41053883 490 HTVAAFLGGSAAQEAIKIITHQFVPFNNTFLYNAMSQTSATF 531
Cdd:cd01493 384 HNISAFMGGIAAQEVIKLITKQYVPIDNTFIFDGIRSKSATF 425
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 12-169 1.60e-17

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: 81.92  E-value: 1.60e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053883    12 YDRQLRL--WGDHGQEALENAHVCLINATASGTEILKNLVLPGIGAFTIVDGHKVSGEDVGNNFFLSSSAIGKNRAQAAT 89
Cdd:pfam00899   1 YSRQLALplIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053883    90 ELLQELNSDVSgnfVEESPDKLLDNDC-EFFHRFSLVI-------AVQLPESTClglgavlWEAGVPFLVCRTYGLIGYM 161
Cdd:pfam00899  81 ERLREINPDVE---VEAYTERLTPENAeELIKSFDIVVdatdnfaARYLVNDAC-------VKLGKPLIEAGVLGFKGQV 150


                  ....*...
gi 41053883   162 RLIVKEHT 169
Cdd:pfam00899 151 TVVIPGKT 158
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 9-524 1.60e-16

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: 83.01  E-value: 1.60e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053883      9 EQRYDRQLRLWGDHGQEALENAHVCLINATASGTEILKNLVLPGIGAFTIVDGHKVSGEDVGNNFFLSSSAIGKNRAQAA 88
Cdd:TIGR01408    4 EALYSRQLYVLGDEAMQKMAKSNVLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLSSNFFLSEDDVGRNRAEAV 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053883     89 TELLQELNSDVSGNFVEESPDK-LLDN-DCEFFHRFSLVIAVQLPE---STClglgavlweAGVPFLVCRTYGLIGYMrl 163
Cdd:TIGR01408   84 VKKLAELNPYVHVSSSSVPFNEeFLDKfQCVVLTEMSLPLQKEINDfchSQC---------PPIAFISADVRGLFGSL-- 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053883    164 ivkehtvveshpdnaledlrldqpFTELKRHVESYDLDNMEkkdhshtPWIIVVArylekwyneNNSQlpknykEKEAFR 243
Cdd:TIGR01408  153 ------------------------FCDFGDEFEVLDTDGEE-------PKTGFIA---------SITQ------ANPGIV 186

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053883    244 QLLREGILKNENGgleDEENFEEAikNVNTALNPTKIssgtqdifnaeqcENITSQSssfwvmahgvrdfvqnegngnlP 323
Cdd:TIGR01408  187 TCLENHRHKLETG---DFVTFREV--NGMTGLNDGSP-------------RKITVIS----------------------P 226

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053883    324 VRGSIpdmiaDSDKFIklqnvyrDKAMRDAAVVSKhvemllqsvgKTPESISEQEIKlfcknaaflrvvrcRSLAD-EYS 402
Cdd:TIGR01408  227 YSFSI-----GDTTEL-------GPYLHGGIATQV----------KTPKTVFFKSLR--------------EQLKDpKCL 270

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053883    403 VDTFNKdeitscmdsPDSEMVLYLMLRSVDRFYQQHSRYPGVYNYQVEEDINKLKLCVNSLLQEYSLNVNvkDDYIHEFC 482
Cdd:TIGR01408  271 IVDFSK---------PERPPEIHTAFQALDQFQEKYSRKPNVGCQQDAEELLKLATSISETLEEKVPDVD--AKLVHWLS 339

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|..
gi 41053883    483 RYGAAEPHTVAAFLGGSAAQEAIKIITHQFVPFNNTFLYNAM 524
Cdd:TIGR01408  340 WTAQGFLSPMAAAVGGVVSQEVLKAVTGKFSPLCQWFYFDSA 381
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 10-126 1.95e-12

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: 67.08  E-value: 1.95e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053883  10 QRYDRQLRL--WGDHGQEALENAHVCLINATASGTEILKNLVLPGIGAFTIVDGHKVsgeDVGNnffL------SSSAIG 81
Cdd:COG0476   6 ERYSRQILLpeIGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVV---ELSN---LqrqilyTEADVG 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 41053883  82 KNRAQAATELLQELNSDVSgnfVEESPDKLLDNDC-EFFHRFSLVI 126
Cdd:COG0476  80 RPKVEAAAERLRALNPDVE---VEAIPERLTEENAlELLAGADLVL 122
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 6-126 3.26e-11

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 64.90  E-value: 3.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053883    6 TSKEQRYDRQLRL--WGDHGQEALENAHVCLINATASGTEILKNLVLPGIGAFTIVDGHKVSGEDVGNNFFLSSSAIGKN 83
Cdd:PRK05600  16 TSELRRTARQLALpgFGIEQQERLHNARVLVIGAGGLGCPAMQSLASAGVGTITLIDDDTVDVSNIHRQILFGASDVGRP 95

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 41053883   84 RAQAATELLQELNSDVSGNFVEESPDklLDNDCEFFHRFSLVI 126
Cdd:PRK05600  96 KVEVAAERLKEIQPDIRVNALRERLT--AENAVELLNGVDLVL 136
 
Name Accession Description Interval E-value
APPBP1_RUB cd01493
Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric ...
 10-531 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: 720.24  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053883  10 QRYDRQLRLWGDHGQEALENAHVCLINATASGTEILKNLVLPGIGAFTIVDGHKVSGEDVGNNFFLSSSAIGKNRAQAAT 89
Cdd:cd01493   1 QKYDRQLRLWGEHGQAALESAHVCLLNATATGTEILKNLVLPGIGSFTIVDGSKVDEEDLGNNFFLDASSLGKSRAEATC 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053883  90 ELLQELNSDVSGNFVEESPDKLLDNDCEFFHRFSLVIAVQLPESTCLGLGAVLWEAGVPFLVCRTYGLIGYMRLIVKEHT 169
Cdd:cd01493  81 ELLQELNPDVNGSAVEESPEALLDNDPSFFSQFTVVIATNLPESTLLRLADVLWSANIPLLYVRSYGLYGYIRIQLKEHT 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053883 170 VVESHPDNALEDLRLDQPFTELKRHVESYDLDNMEKKDHSHTPWIIVVARYLEKWYNENNSQLPKNYKEKEAFRQLLREG 249
Cdd:cd01493 161 IVESHPDNALEDLRLDNPFPELREHADSIDLDDMDPAEHSHTPYIVILIKYLEKWRSAHNGQLPSTYKEKKEFRDLVRSL 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053883 250 ILKNengglEDEENFEEAIKNVNTALNPTKISSGTQDIFNAEQCENITSQSSSFWVMAHGVRDFVQNEgNGNLPVRGSIP 329
Cdd:cd01493 241 MRSN-----EDEENFEEAIKAVNKALNRTKIPSSVEEIFNDDRCENLTSQSSSFWIMARALKEFVAEE-NGLLPLPGTLP 314

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053883 330 DMIADSDKFIKLQNVYRDKAMRDAAVVSKHVEMLLQSVGKTPESISEQEIKLFCKNAAFLRVVRCRSLAdeysvdtfnkd 409
Cdd:cd01493 315 DMTADTEKYIKLQNIYREKAEKDAAEVEKYVREILKSLGRSPDSISDKEIKLFCKNAAFLRVIRGRSLE----------- 383

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053883 410 eitscmdspdsemvlylmlrsvdrfyqqhsrypgvynyqveedinklklcvnsllqeyslnvnvkddyihefcrygaaep 489
Cdd:cd01493     --------------------------------------------------------------------------------

                       490       500       510       520
                ....*....|....*....|....*....|....*....|..
gi 41053883 490 HTVAAFLGGSAAQEAIKIITHQFVPFNNTFLYNAMSQTSATF 531
Cdd:cd01493 384 HNISAFMGGIAAQEVIKLITKQYVPIDNTFIFDGIRSKSATF 425
E1-1_like cd01485
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ...
 12-164 5.09e-63

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: 204.58  E-value: 5.09e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053883  12 YDRQLRLWGDHGQEALENAHVCLINATASGTEILKNLVLPGIGAFTIVDGHKVSGEDVGNNFFL--SSSAIGKNRAQAAT 89
Cdd:cd01485   2 YDRQIRLWGDEAQNKLRSAKVLIIGAGALGAEIAKNLVLAGIDSITIVDHRLVSTEDLGSNFFLdaEVSNSGMNRAAASY 81

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41053883  90 ELLQELNSDVSGNFVEESPDKLLDNDCEFFHRFSLVIAVQLPESTCLGLGAVLWEAGVPFLVCRTYGLIGYMRLI 164
Cdd:cd01485  82 EFLQELNPNVKLSIVEEDSLSNDSNIEEYLQKFTLVIATEENYERTAKVNDVCRKHHIPFISCATYGLIGYAFFD 156
Aos1_SUMO cd01492
Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating ...
 12-161 2.09e-37

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: 136.65  E-value: 2.09e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053883  12 YDRQLRLWGDHGQEALENAHVCLINATASGTEILKNLVLPGIGAFTIVDGHKVSGEDVGNNFFLSSSAIGKNRAQAATEL 91
Cdd:cd01492   4 YDRQIRLWGLEAQKRLRSARILLIGLKGLGAEIAKNLVLSGIGSLTILDDRTVTEEDLGAQFLIPAEDLGQNRAEASLER 83

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053883  92 LQELNSDVSgnfVEESPDKLLDNDCEFFHRFSLVIAVQLPESTCLGLGAVLWEAGVPFLVCRTYGLIGYM 161
Cdd:cd01492  84 LRALNPRVK---VSVDTDDISEKPEEFFSQFDVVVATELSRAELVKINELCRKLGVKFYATGVHGLFGFV 150
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 31-164 5.23e-22

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: 91.95  E-value: 5.23e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053883  31 HVCLINATASGTEILKNLVLPGIGAFTIVDGHKVSGEDVGNNFFLSSSAIGKNRAQAATELLQELNSDVSGNFVEESPDK 110
Cdd:cd01483   1 RVLLVGLGGLGSEIALNLARSGVGKITLIDFDTVELSNLNRQFLARQADIGKPKAEVAARRLNELNPGVNVTAVPEGISE 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 41053883 111 llDNDCEFFHRFSLVIAVQLPESTCLGLGAVLWEAGVPFLVCRTYGLIGYMRLI 164
Cdd:cd01483  81 --DNLDDFLDGVDLVIDAIDNIAVRRALNRACKELGIPVIDAGGLGLGGDIQVI 132
Ube1_repeat1 cd01491
Ubiquitin activating enzyme (E1), repeat 1. E1, a highly conserved small protein present ...
 12-160 5.98e-20

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: 90.02  E-value: 5.98e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053883  12 YDRQLRLWGDHGQEALENAHVCLINATASGTEILKNLVLPGIGAFTIVDGHKVSGEDVGNNFFLSSSAIGKNRAQAATEL 91
Cdd:cd01491   2 YSRQLYVLGHEAMKKLQKSNVLISGLGGLGVEIAKNLILAGVKSVTLHDTKPCSWSDLSSQFYLREEDIGKNRAEASQAR 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41053883  92 LQELNSDVSgnfVEESPDKLLDNdceFFHRFSLVIAVQLPESTCLGLGAVLWEAGVPFLVCRTYGLIGY 160
Cdd:cd01491  82 LAELNPYVP---VTVSTGPLTTD---ELLKFQVVVLTDASLEDQLKINEFCHSPGIKFISADTRGLFGS 144
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 12-169 1.60e-17

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: 81.92  E-value: 1.60e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053883    12 YDRQLRL--WGDHGQEALENAHVCLINATASGTEILKNLVLPGIGAFTIVDGHKVSGEDVGNNFFLSSSAIGKNRAQAAT 89
Cdd:pfam00899   1 YSRQLALplIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053883    90 ELLQELNSDVSgnfVEESPDKLLDNDC-EFFHRFSLVI-------AVQLPESTClglgavlWEAGVPFLVCRTYGLIGYM 161
Cdd:pfam00899  81 ERLREINPDVE---VEAYTERLTPENAeELIKSFDIVVdatdnfaARYLVNDAC-------VKLGKPLIEAGVLGFKGQV 150


                  ....*...
gi 41053883   162 RLIVKEHT 169
Cdd:pfam00899 151 TVVIPGKT 158
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 9-524 1.60e-16

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: 83.01  E-value: 1.60e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053883      9 EQRYDRQLRLWGDHGQEALENAHVCLINATASGTEILKNLVLPGIGAFTIVDGHKVSGEDVGNNFFLSSSAIGKNRAQAA 88
Cdd:TIGR01408    4 EALYSRQLYVLGDEAMQKMAKSNVLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLSSNFFLSEDDVGRNRAEAV 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053883     89 TELLQELNSDVSGNFVEESPDK-LLDN-DCEFFHRFSLVIAVQLPE---STClglgavlweAGVPFLVCRTYGLIGYMrl 163
Cdd:TIGR01408   84 VKKLAELNPYVHVSSSSVPFNEeFLDKfQCVVLTEMSLPLQKEINDfchSQC---------PPIAFISADVRGLFGSL-- 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053883    164 ivkehtvveshpdnaledlrldqpFTELKRHVESYDLDNMEkkdhshtPWIIVVArylekwyneNNSQlpknykEKEAFR 243
Cdd:TIGR01408  153 ------------------------FCDFGDEFEVLDTDGEE-------PKTGFIA---------SITQ------ANPGIV 186

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053883    244 QLLREGILKNENGgleDEENFEEAikNVNTALNPTKIssgtqdifnaeqcENITSQSssfwvmahgvrdfvqnegngnlP 323
Cdd:TIGR01408  187 TCLENHRHKLETG---DFVTFREV--NGMTGLNDGSP-------------RKITVIS----------------------P 226

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053883    324 VRGSIpdmiaDSDKFIklqnvyrDKAMRDAAVVSKhvemllqsvgKTPESISEQEIKlfcknaaflrvvrcRSLAD-EYS 402
Cdd:TIGR01408  227 YSFSI-----GDTTEL-------GPYLHGGIATQV----------KTPKTVFFKSLR--------------EQLKDpKCL 270

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053883    403 VDTFNKdeitscmdsPDSEMVLYLMLRSVDRFYQQHSRYPGVYNYQVEEDINKLKLCVNSLLQEYSLNVNvkDDYIHEFC 482
Cdd:TIGR01408  271 IVDFSK---------PERPPEIHTAFQALDQFQEKYSRKPNVGCQQDAEELLKLATSISETLEEKVPDVD--AKLVHWLS 339

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|..
gi 41053883    483 RYGAAEPHTVAAFLGGSAAQEAIKIITHQFVPFNNTFLYNAM 524
Cdd:TIGR01408  340 WTAQGFLSPMAAAVGGVVSQEVLKAVTGKFSPLCQWFYFDSA 381
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 10-126 1.95e-12

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: 67.08  E-value: 1.95e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053883  10 QRYDRQLRL--WGDHGQEALENAHVCLINATASGTEILKNLVLPGIGAFTIVDGHKVsgeDVGNnffL------SSSAIG 81
Cdd:COG0476   6 ERYSRQILLpeIGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVV---ELSN---LqrqilyTEADVG 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 41053883  82 KNRAQAATELLQELNSDVSgnfVEESPDKLLDNDC-EFFHRFSLVI 126
Cdd:COG0476  80 RPKVEAAAERLRALNPDVE---VEAIPERLTEENAlELLAGADLVL 122
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 11-99 3.23e-11

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: 63.27  E-value: 3.23e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053883  11 RYDRQLRL--WGDHGQEALENAHVCLINATASGTEILKNLVLPGIGAFTIVDGHKVsgeDVGN---NFFLSSSAIGKNRA 85
Cdd:cd00757   1 RYSRQILLpeIGEEGQEKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVV---ELSNlqrQILHTEADVGQPKA 77

                        90
                ....*....|....
gi 41053883  86 QAATELLQELNSDV 99
Cdd:cd00757  78 EAAAERLRAINPDV 91
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 6-126 3.26e-11

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 64.90  E-value: 3.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053883    6 TSKEQRYDRQLRL--WGDHGQEALENAHVCLINATASGTEILKNLVLPGIGAFTIVDGHKVSGEDVGNNFFLSSSAIGKN 83
Cdd:PRK05600  16 TSELRRTARQLALpgFGIEQQERLHNARVLVIGAGGLGCPAMQSLASAGVGTITLIDDDTVDVSNIHRQILFGASDVGRP 95

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 41053883   84 RAQAATELLQELNSDVSGNFVEESPDklLDNDCEFFHRFSLVI 126
Cdd:PRK05600  96 KVEVAAERLKEIQPDIRVNALRERLT--AENAVELLNGVDLVL 136
E1-1_like cd01485
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ...
 491-531 2.75e-10

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: 59.74  E-value: 2.75e-10
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 41053883 491 TVAAFLGGSAAQEAIKIITHQFVPFNNTFLYNAMSQTSATF 531
Cdd:cd01485 158 PIAAFLGGVVAQEAIKSISGKFTPLNNLYIYDGFESTGPMC 198
PTZ00245 PTZ00245
ubiquitin activating enzyme; Provisional
 11-100 4.15e-10

ubiquitin activating enzyme; Provisional


Pssm-ID: 140272  Cd Length: 287  Bit Score: 60.84  E-value: 4.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053883   11 RYDRQLRLWGDHGQEALENAHVCLINATASGTEILKNLVLPGIGAFTIVDGHKVSGEDVGNNFFLSSSAiGKNRAQAATE 90
Cdd:PTZ00245   8 RYDRQIRLWGKSTQQQLMHTSVALHGVAGAAAEAAKNLVLAGVRAVAVADEGLVTDADVCTNYLMQGEA-GGTRGARALG 86

                         90
                 ....*....|
gi 41053883   91 LLQELNSDVS 100
Cdd:PTZ00245  87 ALQRLNPHVS 96
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 5-99 1.23e-09

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 59.89  E-value: 1.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053883    5 KTSKEQRYDRQLRL--WGDHGQEALENAHVCLINATASGTEILKNLVLPGIGAFTIVDGHKVSGEDVGNNFFLSSSAIGK 82
Cdd:PRK05597   2 KNLDIARYRRQIMLgeIGQQGQQSLFDAKVAVIGAGGLGSPALLYLAGAGVGHITIIDDDTVDLSNLHRQVIHSTAGVGQ 81

                         90
                 ....*....|....*..
gi 41053883   83 NRAQAATELLQELNSDV 99
Cdd:PRK05597  82 PKAESAREAMLALNPDV 98
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 11-100 4.51e-08

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 55.00  E-value: 4.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053883   11 RYDRQLRLW--GDHGQEALENAHVCLINATASGTEILKNLVLPGIGAFTIVDGHKV-----------SGEDVGNNFflss 77
Cdd:PRK07688   4 RYSRQELFSpiGEEGQQKLREKHVLIIGAGALGTANAEMLVRAGVGKVTIVDRDYVewsnlqrqqlyTESDVKNNL---- 79

                         90       100
                 ....*....|....*....|...
gi 41053883   78 saigkNRAQAATELLQELNSDVS 100
Cdd:PRK07688  80 -----PKAVAAKKRLEEINSDVR 97
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 9-99 2.98e-07

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 52.43  E-value: 2.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053883    9 EQRYDRQLRL--WGDHGQEALENAHVCLINATASGTEILKNLVLPGIGAFTIVDGHKV-----------SGEDVGNNffl 75
Cdd:PRK12475   2 QERYSRQILFsgIGEEGQRKIREKHVLIVGAGALGAANAEALVRAGIGKLTIADRDYVewsnlqrqqlyTEEDAKQK--- 78

                         90       100
                 ....*....|....*....|....
gi 41053883   76 sssaigKNRAQAATELLQELNSDV 99
Cdd:PRK12475  79 ------KPKAIAAKEHLRKINSEV 96
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 11-146 7.97e-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: 52.20  E-value: 7.97e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053883     11 RYDRQLRLWGDHGQEALENAHVCLINATASGTEILKNLVLPGI-----GAFTIVDGHKVSGEDVGNNFFLSSSAIGKNRA 85
Cdd:TIGR01408  401 RYDAQIAVFGDTFQQKLQNLNIFLVGCGAIGCEMLKNFALMGVgtgkkGMITVTDPDLIEKSNLNRQFLFRPHHIGKPKS 480

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41053883     86 QAATELLQELNS----DVSGNFVEESPDKLLDNdcEFFHRFSLVI-------AVQLPESTCLGLGAVLWEAG 146
Cdd:TIGR01408  481 YTAADATLKINPqikiDAHQNRVGPETETIFND--EFYEKLDVVInaldnveARRYVDSRCLAFLKPLLESG 550
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 32-169 2.86e-06

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: 49.30  E-value: 2.86e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053883  32 VCLINATASGTEILKNLVLPGIGAFTIVDGHKVSGEDVGNNFFLSSSAIGKNRAQAATELLQELNSDVSgnfVEESPDKL 111
Cdd:cd01489   2 VLVVGAGGIGCELLKNLVLTGFGEIHIIDLDTIDLSNLNRQFLFRKKHVGKSKAQVAKEAVLSFNPNVK---IVAYHANI 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41053883 112 LDND--CEFFHRFSLVI-------AVQLPESTCLGLGAVLWEAGvpflvcrTYGLIGYMRLIVKEHT 169
Cdd:cd01489  79 KDPDfnVEFFKQFDLVFnaldnlaARRHVNKMCLAADVPLIESG-------TTGFLGQVQVIKKGKT 138
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 10-126 3.88e-06

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 49.32  E-value: 3.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053883   10 QRYDRQLRL--WGDHGQEALENAHVCLINATASGTEILKNLVLPGIGAFTIVDGHKVSGEDVGNNFFLSSSAIGKNRAQA 87
Cdd:PRK07878  21 ARYSRHLIIpdVGVDGQKRLKNARVLVIGAGGLGSPTLLYLAAAGVGTLGIVEFDVVDESNLQRQVIHGQSDVGRSKAQS 100

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 41053883   88 ATELLQELNSDVSGNFVEESPDKllDNDCEFFHRFSLVI 126
Cdd:PRK07878 101 ARDSIVEINPLVNVRLHEFRLDP--SNAVELFSQYDLIL 137
PRK08328 PRK08328
hypothetical protein; Provisional
 10-124 4.15e-06

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 48.25  E-value: 4.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053883   10 QRYDRQLRLWGDHGQEALENAHVCLINATASGTEILKNLVLPGIGAFTIVDGHKVSGEDVGNNFFLSSSAIGKN-RAQAA 88
Cdd:PRK08328   8 ERYDRQIMIFGVEGQEKLKKAKVAVVGVGGLGSPVAYYLAAAGVGRILLIDEQTPELSNLNRQILHWEEDLGKNpKPLSA 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 41053883   89 TELLQELNSDVS-----GNFVEESPDKLLDN-----DC--EFFHRFSL 124
Cdd:PRK08328  88 KWKLERFNSDIKietfvGRLSEENIDEVLKGvdvivDCldNFETRYLL 135
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 31-127 5.10e-06

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: 48.51  E-value: 5.10e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053883  31 HVCLINATASGTEILKNLVLPGIGAFTIVDGHKVsgeDVGN---NFFLSSSAIGKNRAQAATELLQELnsdVSGNFVEES 107
Cdd:cd01488   1 KILVIGAGGLGCELLKNLALSGFRNIHVIDMDTI---DVSNlnrQFLFREKDIGKPKAEVAAKFVNDR---VPGVNVTPH 74

                        90       100
                ....*....|....*....|
gi 41053883 108 PDKLLDNDCEFFHRFSLVIA 127
Cdd:cd01488  75 FGKIQDKDEEFYRQFNIIIC 94
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
 32-169 5.32e-06

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: 47.96  E-value: 5.32e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053883  32 VCLINATASGTEILKNLVLPGIGAFTIVDGHKVSGEDVGNNFFLSSSAIGKNRAQAATELLQELNSdvSGNFV---EESP 108
Cdd:cd01484   2 VLLVGAGGIGCELLKNLALMGFGQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKSEVAAEAVNDRNP--NCKVVpyqNKVG 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41053883 109 DKLLDNDcEFFHRFSLV-------IAVQLPESTCLGLGAVLWEAGvpflvcrTYGLIGYMRLIVKEHT 169
Cdd:cd01484  80 PEQDFND-TFFEQFHIIvnaldniIARRYVNGMLIFLIVPLIESG-------TEGFKGNAQVILPGMT 139
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 1-126 2.49e-04

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 42.91  E-value: 2.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053883    1 MTDPKTSKE-QRYDRQ--LRLWGDHGQEALENAHVCLINATASGTEILKNLVLPGIGAFTIVDGHKVSgedvgnnffLS- 76
Cdd:PRK05690   1 MMAELSDEEmLRYNRQiiLRGFDFDGQEKLKAARVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVS---------LSn 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053883   77 --------SSAIGKNRAQAATELLQELNSDVSGNFVeespDKLLDND--CEFFHRFSLVI 126
Cdd:PRK05690  72 lqrqvlhdDATIGQPKVESARAALARINPHIAIETI----NARLDDDelAALIAGHDLVL 127
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
9-106 4.79e-04

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 42.69  E-value: 4.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053883    9 EQRYDRQLRL--WGDHGQEALENAHVCLINATASGTEILKNLVLPGIGAFTIVDGHKVSGEDVGNNFFLSSSAIGKNRAQ 86
Cdd:PRK08762 113 DERYSRHLRLpeVGEEGQRRLLEARVLLIGAGGLGSPAALYLAAAGVGTLGIVDHDVVDRSNLQRQILHTEDRVGQPKVD 192

                         90       100
                 ....*....|....*....|
gi 41053883   87 AATELLQELNSDVSGNFVEE 106
Cdd:PRK08762 193 SAAQRLAALNPDVQVEAVQE 212
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
10-96 4.64e-03

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 39.33  E-value: 4.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053883   10 QRYDRQLRL--WGDHGQEALENAHVCLINATASGTEILKNLVLPGIGAFTIVDGHKVSGEDVGNNFFLSSSAIGKNRAQA 87
Cdd:PRK07411  17 ERYSRHLILpeVGLEGQKRLKAASVLCIGTGGLGSPLLLYLAAAGIGRIGIVDFDVVDSSNLQRQVIHGTSWVGKPKIES 96


                 ....*....
gi 41053883   88 ATELLQELN 96
Cdd:PRK07411  97 AKNRILEIN 105
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
24-160 6.29e-03

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 38.30  E-value: 6.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053883   24 QEALENAHVCLINATASGTEILKNLVLPGIGAFTIVDGHKVsgeDVGN----NFFLSSsaIGKNRAQAATELLQELNSDV 99
Cdd:PRK08644  23 LEKLKKAKVGIAGAGGLGSNIAVALARSGVGNLKLVDFDVV---EPSNlnrqQYFISQ--IGMPKVEALKENLLEINPFV 97

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41053883  100 SgnfVEESPDKLL-DNDCEFFHRFSLVI-AVQLPESTCLGLGAVLWEAGvPFLVCRTyGLIGY 160
Cdd:PRK08644  98 E---IEAHNEKIDeDNIEELFKDCDIVVeAFDNAETKAMLVETVLEHPG-KKLVAAS-GMAGY 155
PRK15116 PRK15116
sulfur acceptor protein CsdL; Provisional
 10-126 6.66e-03

sulfur acceptor protein CsdL; Provisional


Pssm-ID: 185071  Cd Length: 268  Bit Score: 38.63  E-value: 6.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053883   10 QRYDRQLRLWGDHGQEALENAHVCLINATASGTEILKNLVLPGIGAFTIVDGHKVSGEDVGNNFFLSSSAIGKNRAQAAT 89
Cdd:PRK15116  11 QRFGGTARLYGEKALQLFADAHICVVGIGGVGSWAAEALARTGIGAITLIDMDDVCVTNTNRQIHALRDNVGLAKAEVMA 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 41053883   90 ELLQELNSDVSGNFVEE--SPD---KLLDNDceffhrFSLVI 126
Cdd:PRK15116  91 ERIRQINPECRVTVVDDfiTPDnvaEYMSAG------FSYVI 126
Aos1_SUMO cd01492
Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating ...
 492-525 7.21e-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: 38.04  E-value: 7.21e-03
                        10        20        30
                ....*....|....*....|....*....|....
gi 41053883 492 VAAFLGGSAAQEAIKIITHQFVPFNNTFLYNAMS 525
Cdd:cd01492 158 VAAVVGGILAQDVINALSKRESPLNNFFVFDGET 191
Ube1_repeat1 cd01491
Ubiquitin activating enzyme (E1), repeat 1. E1, a highly conserved small protein present ...
 491-521 9.40e-03

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: 38.02  E-value: 9.40e-03
                        10        20        30
                ....*....|....*....|....*....|.
gi 41053883 491 TVAAFLGGSAAQEAIKIITHQFVPFNNtFLY 521
Cdd:cd01491 246 PMAAFFGGLAAQEVLKACSGKFTPLKQ-WLY 275
 
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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