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Conserved domains on  [gi|150865971|ref|XP_001385403|]
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predicted protein [Scheffersomyces stipitis CBS 6054]

Protein Classification

ubiquitin-activating E1 family protein( domain architecture ID 320623)

ubiquitin-activating E1 family protein is an activating enzyme similar to Osphranter rufus ubiquitin-activating enzyme E1 Y that activates ubiquitin by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding a ubiquitin-E1 thioester and free AMP

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
E1_enzyme_family super family cl22428
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 8-517 7.29e-179

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.


The actual alignment was detected with superfamily member cd01493:

Pssm-ID: 451392 [Multi-domain]  Cd Length: 425  Bit Score: 509.15  E-value: 7.29e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150865971   8 RYDRQLRLWASTGQTNLENSHICLINATPTGSEILKNLVLPGIGEFTIIDNRRVTPQDLSGNFFLKRQDLNQVLADAVKA 87
Cdd:cd01493    2 KYDRQLRLWGEHGQAALESAHVCLLNATATGTEILKNLVLPGIGSFTIVDGSKVDEEDLGNNFFLDASSLGKSRAEATCE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150865971  88 NLSELNSEVCGHSINRSIISILSEESHQFWdQFNVVIVSDYV-PQLELLKEILWNKKTPLLIVNTIGFYGSLNIIANEIT 166
Cdd:cd01493   82 LLQELNPDVNGSAVEESPEALLDNDPSFFS-QFTVVIATNLPeSTLLRLADVLWSANIPLLYVRSYGLYGYIRIQLKEHT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150865971 167 VIETHDPSRLYDLRIDKPWPELQAFVNSIDLDSLDDTDHAHVPYIVIYIKALQTWKVDHNGSVPQNYHEKKLFRSYIEQL 246
Cdd:cd01493  161 IVESHPDNALEDLRLDNPFPELREHADSIDLDDMDPAEHSHTPYIVILIKYLEKWRSAHNGQLPSTYKEKKEFRDLVRSL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150865971 247 SRNINLEANFIEASNSIHRALQTTGIPISIQKLFEkvTAANESFDASTPIFWIFIKALKRFVEKNDNQLPLPGTLPDMAS 326
Cdd:cd01493  241 MRSNEDEENFEEAIKAVNKALNRTKIPSSVEEIFN--DDRCENLTSQSSSFWIMARALKEFVAEENGLLPLPGTLPDMTA 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150865971 327 DTTSYLCLQTIYREKAWKDQELFTREVIKVLEEVGRSKEELNRDSITSFCKNSQMLYVTSGSKKLysssliqellnssnd 406
Cdd:cd01493  319 DTEKYIKLQNIYREKAEKDAAEVEKYVREILKSLGRSPDSISDKEIKLFCKNAAFLRVIRGRSLE--------------- 383

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150865971 407 aendpyntlgiyfailtynlfiekcnrsptlkdldlleilfadnilnrssvpssvittfrellshntrhyHNINSLMGGI 486
Cdd:cd01493  384 ----------------------------------------------------------------------HNISAFMGGI 393

                        490       500       510
                 ....*....|....*....|....*....|.
gi 150865971 487 ASQEVLKLATAQYTPLDNLFVFDGIRSVSEK 517
Cdd:cd01493  394 AAQEVIKLITKQYVPIDNTFIFDGIRSKSAT 424
 
Name Accession Description Interval E-value
APPBP1_RUB cd01493
Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric ...
 8-517 7.29e-179

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: 509.15  E-value: 7.29e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150865971   8 RYDRQLRLWASTGQTNLENSHICLINATPTGSEILKNLVLPGIGEFTIIDNRRVTPQDLSGNFFLKRQDLNQVLADAVKA 87
Cdd:cd01493    2 KYDRQLRLWGEHGQAALESAHVCLLNATATGTEILKNLVLPGIGSFTIVDGSKVDEEDLGNNFFLDASSLGKSRAEATCE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150865971  88 NLSELNSEVCGHSINRSIISILSEESHQFWdQFNVVIVSDYV-PQLELLKEILWNKKTPLLIVNTIGFYGSLNIIANEIT 166
Cdd:cd01493   82 LLQELNPDVNGSAVEESPEALLDNDPSFFS-QFTVVIATNLPeSTLLRLADVLWSANIPLLYVRSYGLYGYIRIQLKEHT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150865971 167 VIETHDPSRLYDLRIDKPWPELQAFVNSIDLDSLDDTDHAHVPYIVIYIKALQTWKVDHNGSVPQNYHEKKLFRSYIEQL 246
Cdd:cd01493  161 IVESHPDNALEDLRLDNPFPELREHADSIDLDDMDPAEHSHTPYIVILIKYLEKWRSAHNGQLPSTYKEKKEFRDLVRSL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150865971 247 SRNINLEANFIEASNSIHRALQTTGIPISIQKLFEkvTAANESFDASTPIFWIFIKALKRFVEKNDNQLPLPGTLPDMAS 326
Cdd:cd01493  241 MRSNEDEENFEEAIKAVNKALNRTKIPSSVEEIFN--DDRCENLTSQSSSFWIMARALKEFVAEENGLLPLPGTLPDMTA 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150865971 327 DTTSYLCLQTIYREKAWKDQELFTREVIKVLEEVGRSKEELNRDSITSFCKNSQMLYVTSGSKKLysssliqellnssnd 406
Cdd:cd01493  319 DTEKYIKLQNIYREKAEKDAAEVEKYVREILKSLGRSPDSISDKEIKLFCKNAAFLRVIRGRSLE--------------- 383

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150865971 407 aendpyntlgiyfailtynlfiekcnrsptlkdldlleilfadnilnrssvpssvittfrellshntrhyHNINSLMGGI 486
Cdd:cd01493  384 ----------------------------------------------------------------------HNISAFMGGI 393

                        490       500       510
                 ....*....|....*....|....*....|.
gi 150865971 487 ASQEVLKLATAQYTPLDNLFVFDGIRSVSEK 517
Cdd:cd01493  394 AAQEVIKLITKQYVPIDNTFIFDGIRSKSAT 424
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 9-166 2.58e-16

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: 78.45  E-value: 2.58e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150865971    9 YDRQLRL--WASTGQTNLENSHICLINATPTGSEILKNLVLPGIGEFTIIDNRRVTPQDLSGNFFLKRQDLNQVLADAVK 86
Cdd:pfam00899   1 YSRQLALplIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150865971   87 ANLSELNSEVCGHSINRSIIsilSEESHQFWDQFNVVI-VSDYVPQLELLKEILWNKKTPLLIVNTIGFYGSLNIIANEI 165
Cdd:pfam00899  81 ERLREINPDVEVEAYTERLT---PENAEELIKSFDIVVdATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVTVVIPGK 157


                  .
gi 150865971  166 T 166
Cdd:pfam00899 158 T 158
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 3-138 4.30e-14

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: 75.31  E-value: 4.30e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150865971     3 IDkESRYDRQLRLWASTGQTNLENSHICLINATPTGSEILKNLVLPGIGEFTIIDNRRVTPQDLSGNFFLKRQDLNQVLA 82
Cdd:TIGR01408    2 ID-EALYSRQLYVLGDEAMQKMAKSNVLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLSSNFFLSEDDVGRNRA 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 150865971    83 DAVKANLSELNSEVcghsinrsIISILSEESH-QFWDQFNVVIVSDYvpQLELLKEI 138
Cdd:TIGR01408   81 EAVVKKLAELNPYV--------HVSSSSVPFNeEFLDKFQCVVLTEM--SLPLQKEI 127
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 8-96 3.87e-11

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: 63.22  E-value: 3.87e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150865971   8 RYDRQLRLWAST--GQTNLENSHICLINATPTGSEILKNLVLPGIGEFTIIDNRRVtpqDLSgNffLKRQ------DLNQ 79
Cdd:COG0476    7 RYSRQILLPEIGeeGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVV---ELS-N--LQRQilyteaDVGR 80

                         90
                 ....*....|....*..
gi 150865971  80 VLADAVKANLSELNSEV 96
Cdd:COG0476   81 PKVEAAAERLRALNPDV 97
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 6-164 5.35e-07

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 51.65  E-value: 5.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150865971   6 ESRYDRQLRL--WASTGQTNLENSHICLINATPTGSEILKNLVLPGIGEFTIIDNRRVTPQDLSGNFFLKRQDLNQVL-- 81
Cdd:PRK12475   2 QERYSRQILFsgIGEEGQRKIREKHVLIVGAGALGAANAEALVRAGIGKLTIADRDYVEWSNLQRQQLYTEEDAKQKKpk 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150865971  82 ADAVKANLSELNSEVcghSINRSIISILSEESHQFWDQFNVVI-VSDYVPQLELLKEILWNKKTPLLIVNTIGFYG-SLN 159
Cdd:PRK12475  82 AIAAKEHLRKINSEV---EIVPVVTDVTVEELEELVKEVDLIIdATDNFDTRLLINDLSQKYNIPWIYGGCVGSYGvTYT 158


                 ....*
gi 150865971 160 IIANE 164
Cdd:PRK12475 159 IIPGK 163
 
Name Accession Description Interval E-value
APPBP1_RUB cd01493
Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric ...
 8-517 7.29e-179

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: 509.15  E-value: 7.29e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150865971   8 RYDRQLRLWASTGQTNLENSHICLINATPTGSEILKNLVLPGIGEFTIIDNRRVTPQDLSGNFFLKRQDLNQVLADAVKA 87
Cdd:cd01493    2 KYDRQLRLWGEHGQAALESAHVCLLNATATGTEILKNLVLPGIGSFTIVDGSKVDEEDLGNNFFLDASSLGKSRAEATCE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150865971  88 NLSELNSEVCGHSINRSIISILSEESHQFWdQFNVVIVSDYV-PQLELLKEILWNKKTPLLIVNTIGFYGSLNIIANEIT 166
Cdd:cd01493   82 LLQELNPDVNGSAVEESPEALLDNDPSFFS-QFTVVIATNLPeSTLLRLADVLWSANIPLLYVRSYGLYGYIRIQLKEHT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150865971 167 VIETHDPSRLYDLRIDKPWPELQAFVNSIDLDSLDDTDHAHVPYIVIYIKALQTWKVDHNGSVPQNYHEKKLFRSYIEQL 246
Cdd:cd01493  161 IVESHPDNALEDLRLDNPFPELREHADSIDLDDMDPAEHSHTPYIVILIKYLEKWRSAHNGQLPSTYKEKKEFRDLVRSL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150865971 247 SRNINLEANFIEASNSIHRALQTTGIPISIQKLFEkvTAANESFDASTPIFWIFIKALKRFVEKNDNQLPLPGTLPDMAS 326
Cdd:cd01493  241 MRSNEDEENFEEAIKAVNKALNRTKIPSSVEEIFN--DDRCENLTSQSSSFWIMARALKEFVAEENGLLPLPGTLPDMTA 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150865971 327 DTTSYLCLQTIYREKAWKDQELFTREVIKVLEEVGRSKEELNRDSITSFCKNSQMLYVTSGSKKLysssliqellnssnd 406
Cdd:cd01493  319 DTEKYIKLQNIYREKAEKDAAEVEKYVREILKSLGRSPDSISDKEIKLFCKNAAFLRVIRGRSLE--------------- 383

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150865971 407 aendpyntlgiyfailtynlfiekcnrsptlkdldlleilfadnilnrssvpssvittfrellshntrhyHNINSLMGGI 486
Cdd:cd01493  384 ----------------------------------------------------------------------HNISAFMGGI 393

                        490       500       510
                 ....*....|....*....|....*....|.
gi 150865971 487 ASQEVLKLATAQYTPLDNLFVFDGIRSVSEK 517
Cdd:cd01493  394 AAQEVIKLITKQYVPIDNTFIFDGIRSKSAT 424
E1-1_like cd01485
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ...
 9-156 1.89e-32

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: 122.92  E-value: 1.89e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150865971   9 YDRQLRLWASTGQTNLENSHICLINATPTGSEILKNLVLPGIGEFTIIDNRRVTPQDLSGNFFLKRQDLNQVL--ADAVK 86
Cdd:cd01485    2 YDRQIRLWGDEAQNKLRSAKVLIIGAGALGAEIAKNLVLAGIDSITIVDHRLVSTEDLGSNFFLDAEVSNSGMnrAAASY 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 150865971  87 ANLSELNSEVCGHSINRSIISILSeESHQFWDQFNVVIVSDyVPQLELLK--EILWNKKTPLLIVNTIGFYG 156
Cdd:cd01485   82 EFLQELNPNVKLSIVEEDSLSNDS-NIEEYLQKFTLVIATE-ENYERTAKvnDVCRKHHIPFISCATYGLIG 151
Aos1_SUMO cd01492
Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating ...
 9-158 2.76e-31

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: 119.70  E-value: 2.76e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150865971   9 YDRQLRLWASTGQTNLENSHICLINATPTGSEILKNLVLPGIGEFTIIDNRRVTPQDLSGNFFLKRQDLNQVLADAVKAN 88
Cdd:cd01492    4 YDRQIRLWGLEAQKRLRSARILLIGLKGLGAEIAKNLVLSGIGSLTILDDRTVTEEDLGAQFLIPAEDLGQNRAEASLER 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 150865971  89 LSELNSEVcGHSINRSIISILSEEshqFWDQFNVVIVSDyvPQLELLKEIlwNKKT-----PLLIVNTIGFYGSL 158
Cdd:cd01492   84 LRALNPRV-KVSVDTDDISEKPEE---FFSQFDVVVATE--LSRAELVKI--NELCrklgvKFYATGVHGLFGFV 150
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 28-161 8.52e-19

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: 83.09  E-value: 8.52e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150865971  28 HICLINATPTGSEILKNLVLPGIGEFTIIDNRRVTPQDLSGNFFLKRQDLNQVLADAVKANLSELNSEVCGHSINRSIIS 107
Cdd:cd01483    1 RVLLVGLGGLGSEIALNLARSGVGKITLIDFDTVELSNLNRQFLARQADIGKPKAEVAARRLNELNPGVNVTAVPEGISE 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 150865971 108 ILSEEshqFWDQFNVVIVS-DYVPQLELLKEILWNKKTPLLIVNTIGFYGSLNII 161
Cdd:cd01483   81 DNLDD---FLDGVDLVIDAiDNIAVRRALNRACKELGIPVIDAGGLGLGGDIQVI 132
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 9-166 2.58e-16

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: 78.45  E-value: 2.58e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150865971    9 YDRQLRL--WASTGQTNLENSHICLINATPTGSEILKNLVLPGIGEFTIIDNRRVTPQDLSGNFFLKRQDLNQVLADAVK 86
Cdd:pfam00899   1 YSRQLALplIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150865971   87 ANLSELNSEVCGHSINRSIIsilSEESHQFWDQFNVVI-VSDYVPQLELLKEILWNKKTPLLIVNTIGFYGSLNIIANEI 165
Cdd:pfam00899  81 ERLREINPDVEVEAYTERLT---PENAEELIKSFDIVVdATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVTVVIPGK 157


                  .
gi 150865971  166 T 166
Cdd:pfam00899 158 T 158
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 3-138 4.30e-14

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: 75.31  E-value: 4.30e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150865971     3 IDkESRYDRQLRLWASTGQTNLENSHICLINATPTGSEILKNLVLPGIGEFTIIDNRRVTPQDLSGNFFLKRQDLNQVLA 82
Cdd:TIGR01408    2 ID-EALYSRQLYVLGDEAMQKMAKSNVLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLSSNFFLSEDDVGRNRA 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 150865971    83 DAVKANLSELNSEVcghsinrsIISILSEESH-QFWDQFNVVIVSDYvpQLELLKEI 138
Cdd:TIGR01408   81 EAVVKKLAELNPYV--------HVSSSSVPFNeEFLDKFQCVVLTEM--SLPLQKEI 127
Ube1_repeat1 cd01491
Ubiquitin activating enzyme (E1), repeat 1. E1, a highly conserved small protein present ...
 9-158 1.17e-13

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: 71.53  E-value: 1.17e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150865971   9 YDRQLRLWASTGQTNLENSHICLINATPTGSEILKNLVLPGIGEFTIIDNRRVTPQDLSGNFFLKRQDLNQVLADAVKAN 88
Cdd:cd01491    2 YSRQLYVLGHEAMKKLQKSNVLISGLGGLGVEIAKNLILAGVKSVTLHDTKPCSWSDLSSQFYLREEDIGKNRAEASQAR 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 150865971  89 LSELNSEVCGHSINrsiisilSEESHQFWDQFNVVIVSDyvPQLELLKEI-LWNKKTP--LLIVNTIGFYGSL 158
Cdd:cd01491   82 LAELNPYVPVTVST-------GPLTTDELLKFQVVVLTD--ASLEDQLKInEFCHSPGikFISADTRGLFGSI 145
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 8-96 3.87e-11

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: 63.22  E-value: 3.87e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150865971   8 RYDRQLRLWAST--GQTNLENSHICLINATPTGSEILKNLVLPGIGEFTIIDNRRVtpqDLSgNffLKRQ------DLNQ 79
Cdd:COG0476    7 RYSRQILLPEIGeeGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVV---ELS-N--LQRQilyteaDVGR 80

                         90
                 ....*....|....*..
gi 150865971  80 VLADAVKANLSELNSEV 96
Cdd:COG0476   81 PKVEAAAERLRALNPDV 97
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 8-96 2.12e-07

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: 51.71  E-value: 2.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150865971   8 RYDRQLRL--WASTGQTNLENSHICLINATPTGSEILKNLVLPGIGEFTIIDNRRVtpqDLSgNffLKRQ------DLNQ 79
Cdd:cd00757    1 RYSRQILLpeIGEEGQEKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVV---ELS-N--LQRQilhteaDVGQ 74

                         90
                 ....*....|....*..
gi 150865971  80 VLADAVKANLSELNSEV 96
Cdd:cd00757   75 PKAEAAAERLRAINPDV 91
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 6-164 5.35e-07

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 51.65  E-value: 5.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150865971   6 ESRYDRQLRL--WASTGQTNLENSHICLINATPTGSEILKNLVLPGIGEFTIIDNRRVTPQDLSGNFFLKRQDLNQVL-- 81
Cdd:PRK12475   2 QERYSRQILFsgIGEEGQRKIREKHVLIVGAGALGAANAEALVRAGIGKLTIADRDYVEWSNLQRQQLYTEEDAKQKKpk 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150865971  82 ADAVKANLSELNSEVcghSINRSIISILSEESHQFWDQFNVVI-VSDYVPQLELLKEILWNKKTPLLIVNTIGFYG-SLN 159
Cdd:PRK12475  82 AIAAKEHLRKINSEV---EIVPVVTDVTVEELEELVKEVDLIIdATDNFDTRLLINDLSQKYNIPWIYGGCVGSYGvTYT 158


                 ....*
gi 150865971 160 IIANE 164
Cdd:PRK12475 159 IIPGK 163
PTZ00245 PTZ00245
ubiquitin activating enzyme; Provisional
 2-96 6.33e-07

ubiquitin activating enzyme; Provisional


Pssm-ID: 140272  Cd Length: 287  Bit Score: 51.21  E-value: 6.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150865971   2 LIDKES-RYDRQLRLWASTGQTNLENSHICLINATPTGSEILKNLVLPGIGEFTIIDNRRVTPQDLSGNFFLKRQDLNQV 80
Cdd:PTZ00245   1 MRDAEAvRYDRQIRLWGKSTQQQLMHTSVALHGVAGAAAEAAKNLVLAGVRAVAVADEGLVTDADVCTNYLMQGEAGGTR 80

                         90
                 ....*....|....*.
gi 150865971  81 LADAVKAnLSELNSEV 96
Cdd:PTZ00245  81 GARALGA-LQRLNPHV 95
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 7-196 6.73e-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: 6.73e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150865971     7 SRYDRQLRLWASTGQTNLENSHICLINATPTGSEILKNLVLPGI-----GEFTIIDNRRVTPQDLSGNFFLKRQDLNQ-- 79
Cdd:TIGR01408  400 DRYDAQIAVFGDTFQQKLQNLNIFLVGCGAIGCEMLKNFALMGVgtgkkGMITVTDPDLIEKSNLNRQFLFRPHHIGKpk 479

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150865971    80 --VLADAV-----KANLSELNSEVCGHSINrsiisILSEEshqFWDQFNVVIVS-DYV-PQLELLKEILWNKKtPLLIVN 150
Cdd:TIGR01408  480 syTAADATlkinpQIKIDAHQNRVGPETET-----IFNDE---FYEKLDVVINAlDNVeARRYVDSRCLAFLK-PLLESG 550

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 150865971   151 TIGFYGSLNIIANEITviETHDPSRlydlriDKPWPE-----LQAFVNSID 196
Cdd:TIGR01408  551 TLGTKGNTQVVVPHLT--ESYGSSR------DPPEKEipfctLKSFPAAIE 593
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 7-96 4.09e-06

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 49.10  E-value: 4.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150865971   7 SRYDRQLRL--WASTGQTNLENSHICLINATPTGSEILKNLVLPGIGEFTIIDNRRVtpqDLSGnffLKRQDLN------ 78
Cdd:PRK05597   7 ARYRRQIMLgeIGQQGQQSLFDAKVAVIGAGGLGSPALLYLAGAGVGHITIIDDDTV---DLSN---LHRQVIHstagvg 80

                         90
                 ....*....|....*...
gi 150865971  79 QVLADAVKANLSELNSEV 96
Cdd:PRK05597  81 QPKAESAREAMLALNPDV 98
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
 31-161 5.06e-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: 5.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150865971  31 LINATPTGSEILKNLVLPGIGEFTIIDNRRVTPQDLSGNFFLKRQDLNQVLAD-AVKA-NLSELNSEVCGHSINRSIISI 108
Cdd:cd01484    4 LVGAGGIGCELLKNLALMGFGQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKSEvAAEAvNDRNPNCKVVPYQNKVGPEQD 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 150865971 109 LSEEshqFWDQFNVVIVS-DYVPQLELLKEILWNKKTPLLIVNTIGFYGSLNII 161
Cdd:cd01484   84 FNDT---FFEQFHIIVNAlDNIIARRYVNGMLIFLIVPLIESGTEGFKGNAQVI 134
E1_ThiF_like cd01487
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ...
 28-161 8.08e-05

E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. 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: 238764 [Multi-domain]  Cd Length: 174  Bit Score: 43.52  E-value: 8.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150865971  28 HICLINATPTGSEILKNLVLPGIGEFTIIDNRRVTPQDLSGNFFLKRQdLNQVLADAVKANLSELNSEVcghSINRSIIS 107
Cdd:cd01487    1 KVGIAGAGGLGSNIAVLLARSGVGNLKLVDFDVVEPSNLNRQQYFLSQ-IGEPKVEALKENLREINPFV---KIEAINIK 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 150865971 108 ILSEESHQFWDQFNVVI--VSDYVPQLELLKEILWNKKTPLLIVNTIGFYGSLNII 161
Cdd:cd01487   77 IDENNLEGLFGDCDIVVeaFDNAETKAMLAESLLGNKNKPVVCASGMAGFGDSNNI 132
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 8-96 1.98e-04

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 43.44  E-value: 1.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150865971   8 RYDRQLrLWAS---TGQTNLENSHICLINATPTGSEILKNLVLPGIGEFTIIDNRRVTPQDLSGNFFLKRQDLNQVLADA 84
Cdd:PRK07688   4 RYSRQE-LFSPigeEGQQKLREKHVLIIGAGALGTANAEMLVRAGVGKVTIVDRDYVEWSNLQRQQLYTESDVKNNLPKA 82

                         90
                 ....*....|....
gi 150865971  85 VKAN--LSELNSEV 96
Cdd:PRK07688  83 VAAKkrLEEINSDV 96
Ube1_repeat1 cd01491
Ubiquitin activating enzyme (E1), repeat 1. E1, a highly conserved small protein present ...
 479-518 2.82e-04

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: 43.02  E-value: 2.82e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 150865971 479 INSLMGGIASQEVLKLATAQYTPLDNLFVFDGIRSVSEKW 518
Cdd:cd01491  247 MAAFFGGLAAQEVLKACSGKFTPLKQWLYFDALECLPEDE 286
E1-1_like cd01485
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ...
 479-517 3.72e-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: 3.72e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 150865971 479 INSLMGGIASQEVLKLATAQYTPLDNLFVFDGIRSVSEK 517
Cdd:cd01485  159 IAAFLGGVVAQEAIKSISGKFTPLNNLYIYDGFESTGPM 197
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 29-161 4.34e-04

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: 42.37  E-value: 4.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150865971  29 ICLINATPTGSEILKNLVLPGIGEFTIIDNRRVTPQDLSGNFFLKRQDLNQVLADAVKANLSELNSEVCGHSINRSIISI 108
Cdd:cd01489    2 VLVVGAGGIGCELLKNLVLTGFGEIHIIDLDTIDLSNLNRQFLFRKKHVGKSKAQVAKEAVLSFNPNVKIVAYHANIKDP 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 150865971 109 lsEESHQFWDQFNVVI-------VSDYVPQLELLKEIlwnkktPLLIVNTIGFYGSLNII 161
Cdd:cd01489   82 --DFNVEFFKQFDLVFnaldnlaARRHVNKMCLAADV------PLIESGTTGFLGQVQVI 133
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 1-124 5.31e-04

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 42.17  E-value: 5.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150865971   1 MLIDKE-SRYDRQLRL--WASTGQTNLENSHICLINATPTGSEILKNLVLPGIGEFTIIDNRRVTPQDLSGNFFLKRQDL 77
Cdd:PRK05600  13 QLPTSElRRTARQLALpgFGIEQQERLHNARVLVIGAGGLGCPAMQSLASAGVGTITLIDDDTVDVSNIHRQILFGASDV 92

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 150865971  78 NQVLADAVKANLSELNSEVcghSINRSIISILSEESHQFWDQFNVVI 124
Cdd:PRK05600  93 GRPKVEVAAERLKEIQPDI---RVNALRERLTAENAVELLNGVDLVL 136
PRK08328 PRK08328
hypothetical protein; Provisional
 1-78 5.71e-04

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 41.71  E-value: 5.71e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 150865971   1 MLIDKE-SRYDRQLRLWASTGQTNLENSHICLINATPTGSEILKNLVLPGIGEFTIIDNRrvTPQdLSGnffLKRQDLN 78
Cdd:PRK08328   1 MLSERElERYDRQIMIFGVEGQEKLKKAKVAVVGVGGLGSPVAYYLAAAGVGRILLIDEQ--TPE-LSN---LNRQILH 73
Aos1_SUMO cd01492
Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating ...
 481-513 1.46e-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: 39.97  E-value: 1.46e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 150865971 481 SLMGGIASQEVLKLATAQYTPLDNLFVFDGIRS 513
Cdd:cd01492  160 AVVGGILAQDVINALSKRESPLNNFFVFDGETS 192
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 28-124 2.93e-03

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: 39.65  E-value: 2.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150865971  28 HICLINATPTGSEILKNLVLPGIGEFTIIDNRRVTPQDLSGNFFLKRQDLNQVLAdAVKANLseLNSEVCGHSINRSIIS 107
Cdd:cd01488    1 KILVIGAGGLGCELLKNLALSGFRNIHVIDMDTIDVSNLNRQFLFREKDIGKPKA-EVAAKF--VNDRVPGVNVTPHFGK 77

                         90
                 ....*....|....*..
gi 150865971 108 ILSEEShQFWDQFNVVI 124
Cdd:cd01488   78 IQDKDE-EFYRQFNIII 93
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
4-96 4.54e-03

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 39.22  E-value: 4.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150865971   4 DKESRYDRQLRL--WASTGQTNLENSHICLINATPTGSEILKNLVLPGIGEFTIIDNRRVtpqDLSGnffLKRQDLN--- 78
Cdd:PRK08762 111 EQDERYSRHLRLpeVGEEGQRRLLEARVLLIGAGGLGSPAALYLAAAGVGTLGIVDHDVV---DRSN---LQRQILHted 184

                         90       100
                 ....*....|....*....|.
gi 150865971  79 ---QVLADAVKANLSELNSEV 96
Cdd:PRK08762 185 rvgQPKVDSAAQRLAALNPDV 205
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
24-96 7.53e-03

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 37.91  E-value: 7.53e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 150865971  24 LENSHICLINATPTGSEILKNLVLPGIGEFTIIDNRRVTPQDLSGNFFLKRQdLNQVLADAVKANLSELNSEV 96
Cdd:PRK08644  26 LKKAKVGIAGAGGLGSNIAVALARSGVGNLKLVDFDVVEPSNLNRQQYFISQ-IGMPKVEALKENLLEINPFV 97
 
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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