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Conserved domains on  [gi|209862989|ref|NP_001129557|]
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ubiquitin-like modifier-activating enzyme 1 [Mus musculus]

Protein Classification

ubiquitin-activating E1 family protein( domain architecture ID 1000537)

Ube1 (ubiquitin-activating E1) family protein similar to ubiquitin-activating enzyme E1 (UBA1) that catalyzes the first step in ubiquitin conjugation to mark cellular proteins for degradation through the ubiquitin-proteasome system

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ube1 super family cl36897
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 49-1055 0e+00

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


The actual alignment was detected with superfamily member TIGR01408:

Pssm-ID: 273603 [Multi-domain]  Cd Length: 1006  Bit Score: 1305.25  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989    49 DIDESLYSRQLYVLGHEAMKMLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTTQWADLSSQFYLREEDIGKNRA 128
Cdd:TIGR01408    1 EIDEALYSRQLYVLGDEAMQKMAKSNVLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLSSNFFLSEDDVGRNRA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989   129 EVSQPRLAELNSYVPVTAYTGPLVEDFLSSFQVVVLTNSPLEAQLRVGEFCHSR--GIKLVVADTRGLFGQLFCDFGEEM 206
Cdd:TIGR01408   81 EAVVKKLAELNPYVHVSSSSVPFNEEFLDKFQCVVLTEMSLPLQKEINDFCHSQcpPIAFISADVRGLFGSLFCDFGDEF 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989   207 VLTDSNGEQPLSAMVSMVTKDNPGVVTCLDEARHGFETGDFVSFSEVQGMIQLNGCQPMEIKVLGPYTFSICDTSNFSDY 286
Cdd:TIGR01408  161 EVLDTDGEEPKTGFIASITQANPGIVTCLENHRHKLETGDFVTFREVNGMTGLNDGSPRKITVISPYSFSIGDTTELGPY 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989   287 IRGGIVSQVKVPKKISFKSLPASLVEPDFVMTDFAKYSRPAQLHIGFQALHQFCALHNQPPRPRNEEDATELVGLAQAVN 366
Cdd:TIGR01408  241 LHGGIATQVKTPKTVFFKSLREQLKDPKCLIVDFSKPERPPEIHTAFQALDQFQEKYSRKPNVGCQQDAEELLKLATSIS 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989   367 arSPPSVKQNSLDEDLIRKLAYVAAGDLAPINAFIGGLAAQEVMKACSGKFMPIMQWLYFDALECLPEDKEAlTEEKCLP 446
Cdd:TIGR01408  321 --ETLEEKVPDVDAKLVHWLSWTAQGFLSPMAAAVGGVVSQEVLKAVTGKFSPLCQWFYFDSAESLPSLGKP-ECEEFLP 397

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989   447 RQNRYDGQVAVFGSDFQEKLSKQKYFLVGAGAIGCELLKNFAMIGLGCGEGGEVVVTDMDTIEKSNLNRQFLFRPWDVTK 526
Cdd:TIGR01408  398 RGDRYDAQIAVFGDTFQQKLQNLNIFLVGCGAIGCEMLKNFALMGVGTGKKGMITVTDPDLIEKSNLNRQFLFRPHHIGK 477

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989   527 LKSDTAAAAVRQMNPYIQVTSHQNRVGPDTERIYDDDFFQNLDGVANALDNIDARMYMDRRCVYYRKPLLESGTLGTKGN 606
Cdd:TIGR01408  478 PKSYTAADATLKINPQIKIDAHQNRVGPETETIFNDEFYEKLDVVINALDNVEARRYVDSRCLAFLKPLLESGTLGTKGN 557

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989   607 VQVVIPFLTESYSSSQDPPEKSIPICTLKNFPNAIEHTLQWARDEFEGLFKQPAENVNQYL-TDSKFVERTLRLAGTQPL 685
Cdd:TIGR01408  558 TQVVVPHLTESYGSSRDPPEKEIPFCTLKSFPAAIEHTIQWARDKFEGLFSHKPSLVNKYLsSPSSAEEVLQKIQSGHSR 637

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989   686 EVLEAVQRSLVLQRPQTWGDCVTWACHHWHTQYCNNIRQLLHNFPPDQLTSSGAPFWSGPKRCPHPLTFDVNNTLHLDYV 765
Cdd:TIGR01408  638 EGLEQIIKLLSKEKPRNFSQCVEWARLKFEKYFNNKALQLLHCFPLDIRTSTGSPFWSSPKRPPSPLKFDLNEPLHLSFI 717

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989   766 MAAANLFAQTYGLTGSQ---DRAAVASLLQSVQVPEFTPKSGVKIHVSDQELQSANASVDDSR-LEELKATLPSPDKLPG 841
Cdd:TIGR01408  718 QAAAKLYATVYGIPFAEedlSADALLNILSEVKIPEFKPRSNKKIQTDETARKPDTAPIDDRNaIFQLEKAILSNEATKS 797

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989   842 -FKMYPIDFEKDDDSNFHMDFIVAASNLRAENYDISPADRHKSKLIAGKIIPAIATTTAAVVGLVCLELYKVVQGHQQLD 920
Cdd:TIGR01408  798 dFRMAPLSFEKDDDHNGHIDFITAASNLRAKNYSIEPADRFKTKFIAGKIIPAIATSTATVSGLVCLELIKVTDGGYKFE 877

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989   921 SYKNGFLNLALPFFGFSEPLAAPRHQYYNQEW-TLWDRFEVQGlqpngeEMTLKQFLDYFKTEHKLEITMLSQGVSMLYS 999
Cdd:TIGR01408  878 VYKNCFLNLAIPLFVFTEPTEVRKTKIRNGISfTIWDRWTLHG------DFTLLEFINAVKEKYGLEPTMVSQGVKLLYV 951

                          970       980       990      1000      1010
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 209862989  1000 FFMPaaKLKERLDQPMTEIVSRVSKRKLGRHVRALVLELCCNDESGEDVEVPYVRY 1055
Cdd:TIGR01408  952 PVMP--GHAERLKLKMHKLVKPTTKKKLPPYRVHLTVSFACDDDGDEDVPGPPVRI 1005
 
Name Accession Description Interval E-value
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 49-1055 0e+00

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: 1305.25  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989    49 DIDESLYSRQLYVLGHEAMKMLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTTQWADLSSQFYLREEDIGKNRA 128
Cdd:TIGR01408    1 EIDEALYSRQLYVLGDEAMQKMAKSNVLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLSSNFFLSEDDVGRNRA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989   129 EVSQPRLAELNSYVPVTAYTGPLVEDFLSSFQVVVLTNSPLEAQLRVGEFCHSR--GIKLVVADTRGLFGQLFCDFGEEM 206
Cdd:TIGR01408   81 EAVVKKLAELNPYVHVSSSSVPFNEEFLDKFQCVVLTEMSLPLQKEINDFCHSQcpPIAFISADVRGLFGSLFCDFGDEF 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989   207 VLTDSNGEQPLSAMVSMVTKDNPGVVTCLDEARHGFETGDFVSFSEVQGMIQLNGCQPMEIKVLGPYTFSICDTSNFSDY 286
Cdd:TIGR01408  161 EVLDTDGEEPKTGFIASITQANPGIVTCLENHRHKLETGDFVTFREVNGMTGLNDGSPRKITVISPYSFSIGDTTELGPY 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989   287 IRGGIVSQVKVPKKISFKSLPASLVEPDFVMTDFAKYSRPAQLHIGFQALHQFCALHNQPPRPRNEEDATELVGLAQAVN 366
Cdd:TIGR01408  241 LHGGIATQVKTPKTVFFKSLREQLKDPKCLIVDFSKPERPPEIHTAFQALDQFQEKYSRKPNVGCQQDAEELLKLATSIS 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989   367 arSPPSVKQNSLDEDLIRKLAYVAAGDLAPINAFIGGLAAQEVMKACSGKFMPIMQWLYFDALECLPEDKEAlTEEKCLP 446
Cdd:TIGR01408  321 --ETLEEKVPDVDAKLVHWLSWTAQGFLSPMAAAVGGVVSQEVLKAVTGKFSPLCQWFYFDSAESLPSLGKP-ECEEFLP 397

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989   447 RQNRYDGQVAVFGSDFQEKLSKQKYFLVGAGAIGCELLKNFAMIGLGCGEGGEVVVTDMDTIEKSNLNRQFLFRPWDVTK 526
Cdd:TIGR01408  398 RGDRYDAQIAVFGDTFQQKLQNLNIFLVGCGAIGCEMLKNFALMGVGTGKKGMITVTDPDLIEKSNLNRQFLFRPHHIGK 477

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989   527 LKSDTAAAAVRQMNPYIQVTSHQNRVGPDTERIYDDDFFQNLDGVANALDNIDARMYMDRRCVYYRKPLLESGTLGTKGN 606
Cdd:TIGR01408  478 PKSYTAADATLKINPQIKIDAHQNRVGPETETIFNDEFYEKLDVVINALDNVEARRYVDSRCLAFLKPLLESGTLGTKGN 557

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989   607 VQVVIPFLTESYSSSQDPPEKSIPICTLKNFPNAIEHTLQWARDEFEGLFKQPAENVNQYL-TDSKFVERTLRLAGTQPL 685
Cdd:TIGR01408  558 TQVVVPHLTESYGSSRDPPEKEIPFCTLKSFPAAIEHTIQWARDKFEGLFSHKPSLVNKYLsSPSSAEEVLQKIQSGHSR 637

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989   686 EVLEAVQRSLVLQRPQTWGDCVTWACHHWHTQYCNNIRQLLHNFPPDQLTSSGAPFWSGPKRCPHPLTFDVNNTLHLDYV 765
Cdd:TIGR01408  638 EGLEQIIKLLSKEKPRNFSQCVEWARLKFEKYFNNKALQLLHCFPLDIRTSTGSPFWSSPKRPPSPLKFDLNEPLHLSFI 717

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989   766 MAAANLFAQTYGLTGSQ---DRAAVASLLQSVQVPEFTPKSGVKIHVSDQELQSANASVDDSR-LEELKATLPSPDKLPG 841
Cdd:TIGR01408  718 QAAAKLYATVYGIPFAEedlSADALLNILSEVKIPEFKPRSNKKIQTDETARKPDTAPIDDRNaIFQLEKAILSNEATKS 797

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989   842 -FKMYPIDFEKDDDSNFHMDFIVAASNLRAENYDISPADRHKSKLIAGKIIPAIATTTAAVVGLVCLELYKVVQGHQQLD 920
Cdd:TIGR01408  798 dFRMAPLSFEKDDDHNGHIDFITAASNLRAKNYSIEPADRFKTKFIAGKIIPAIATSTATVSGLVCLELIKVTDGGYKFE 877

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989   921 SYKNGFLNLALPFFGFSEPLAAPRHQYYNQEW-TLWDRFEVQGlqpngeEMTLKQFLDYFKTEHKLEITMLSQGVSMLYS 999
Cdd:TIGR01408  878 VYKNCFLNLAIPLFVFTEPTEVRKTKIRNGISfTIWDRWTLHG------DFTLLEFINAVKEKYGLEPTMVSQGVKLLYV 951

                          970       980       990      1000      1010
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 209862989  1000 FFMPaaKLKERLDQPMTEIVSRVSKRKLGRHVRALVLELCCNDESGEDVEVPYVRY 1055
Cdd:TIGR01408  952 PVMP--GHAERLKLKMHKLVKPTTKKKLPPYRVHLTVSFACDDDGDEDVPGPPVRI 1005
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
 470-1011 0e+00

Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present universally in eukaryotic cells, is part of cascade to attach ubiquitin (Ub) covalently to substrate proteins. This cascade consists of activating (E1), conjugating (E2), and/or ligating (E3) enzymes and then targets them for degradation by the 26S proteasome. E1 activates ubiquitin by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and ubiquitin's C-terminus. E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. Ubiquitin-E1 is a single-chain protein with a weakly conserved two-fold repeat. This CD represents the second repeat of Ub-E1.


Pssm-ID: 238767 [Multi-domain]  Cd Length: 435  Bit Score: 871.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989  470 KYFLVGAGAIGCELLKNFAMIGLGCGEGGEVVVTDMDTIEKSNLNRQFLFRPWDVTKLKSDTAAAAVRQMNPYIQVTSHQ 549
Cdd:cd01490     1 KVFLVGAGAIGCELLKNFALMGVGTGESGEITVTDMDNIEKSNLNRQFLFRPHDVGKPKSEVAAAAVKAMNPDLKITALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989  550 NRVGPDTERIYDDDFFQNLDGVANALDNIDARMYMDRRCVYYRKPLLESGTLGTKGNVQVVIPFLTESYSSSQDPPEKSI 629
Cdd:cd01490    81 NRVGPETEHIFNDEFWEKLDGVANALDNVDARMYVDRRCVYYRKPLLESGTLGTKGNTQVVIPHLTESYSSSRDPPEKSI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989  630 PICTLKNFPNAIEHTLQWARDEFEGLFKQPAENVNQYLtdskfvertlrlagtqplevleavqrslvlqrpqtWGDCVTW 709
Cdd:cd01490   161 PLCTLKNFPNAIEHTIQWARDEFEGLFKQPPENVNQYL-----------------------------------FEDCVRW 205

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989  710 ACHHWHTQYCNNIRQLLHNFPPDQLTSSGAPFWSGPKRCPHPLTFDVNNTLHLDYVMAAANLFAQTYGLTGsqdraavas 789
Cdd:cd01490   206 ARLLFEKYFNNNIKQLLHNFPPDAVTSDGAPFWSGPKRCPTPLEFDVNNPLHLDFVLAAANLYAEVYGIPG--------- 276

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989  790 llqsvqvpeftpksgvkihvsdqelqsanasvddsrleelkatlpspdklpgfkmypidFEKDDDSNFHMDFIVAASNLR 869
Cdd:cd01490   277 -----------------------------------------------------------FEKDDDTNFHMDFITAASNLR 297

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989  870 AENYDISPADRHKSKLIAGKIIPAIATTTAAVVGLVCLELYKVVQGHQQLDSYKNGFLNLALPFFGFSEPLAAPRHQY-Y 948
Cdd:cd01490   298 ARNYSIPPADRHKTKRIAGKIIPAIATTTAAVTGLVCLELYKVVDGKRPLEAYKNAFLNLALPFFAFSEPIPAPKVKYaY 377

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 209862989  949 NQEWTLWDRFEVQGLQPNGEEMTlkqflDYFKTEHKLEITMLSQGVSMLYSFFMPAAKLKERL 1011
Cdd:cd01490   378 DEEWTIWDRFEVKGKQTLQELLI-----DYFKEKYGLEVTMLSQGVSMLYSSFMPPAKLKERL 435
UBA_E1_SCCH pfam10585
Ubiquitin-activating enzyme, SCCH domain; Ubiquitin-activating enzyme (E1 enzyme) activates ...
 638-884 1.06e-149

Ubiquitin-activating enzyme, SCCH domain; Ubiquitin-activating enzyme (E1 enzyme) activates ubiquitin by first adenylating with ATP its C-terminal glycine residue and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding an ubiquitin-E1 thiolester and free AMP. Later the ubiquitin moiety is transferred to a cysteine residue on one of the many forms of ubiquitin-conjugating enzymes (E2). This domain carries the last of five conserved cysteines that is part of the active site of the enzyme, responsible for ubiquitin thiolester complex formation, the active site being represented by the sequence motif PICTLKNFP. The catalytic cysteine domain contains the E1 active site cysteine, and is divided in two half-domains, FCCH and SCCH, for 'first' and 'second' catalytic cysteine half-domain, respectively. This is the SCCH domain in which resides the catalytic cysteine.


Pssm-ID: 463157  Cd Length: 254  Bit Score: 445.91  E-value: 1.06e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989   638 PNAIEHTLQWARDEFEGLFKQPAENVNQYL-TDSKFVERTLRLAGTQPLEVLEAVQRSLVLQRPQTWGDCVTWACHHWHT 716
Cdd:pfam10585    1 PNAIEHTIQWARDEFEGLFVQPPEEVNKYLqPPQNFIESLLKQGGGQKLETLESVRKSLVTERPKTFEDCVAWARLKFEK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989   717 QYCNNIRQLLHNFPPDQLTSSGAPFWSGPKRCPHPLTFDVNNTLHLDYVMAAANLFAQTYGLTGSQDRAAVASLLQSVQV 796
Cdd:pfam10585   81 LFNNDIKQLLYNFPPDHKTSSGAPFWSGPKRPPTPLEFDPNNPLHLDFVVAAANLRAQVYGIPGSRDREAIAKVLSKVKV 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989   797 PEFTPKSGVKIHVSDQELQSANASV--DDSRLEELKATLP----SPDKLPGFKMYPIDFEKDDDSNFHMDFIVAASNLRA 870
Cdd:pfam10585  161 PEFKPKSGVKIQVNDEEAADPNAESedDEDELDELLEELPklavSPSSLAGFRLNPIEFEKDDDTNFHIDFITAASNLRA 240

                          250
                   ....*....|....
gi 209862989   871 ENYDISPADRHKSK 884
Cdd:pfam10585  241 RNYGIPPADRHKTK 254
UBA_e1_C smart00985
Ubiquitin-activating enzyme e1 C-terminal domain; This presumed domain found at the C terminus ...
 922-1053 4.00e-69

Ubiquitin-activating enzyme e1 C-terminal domain; This presumed domain found at the C terminus of Ubiquitin-activating enzyme e1 proteins is functionally uncharacterised.


Pssm-ID: 214955  Cd Length: 128  Bit Score: 226.37  E-value: 4.00e-69
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989    922 YKNGFLNLALPFFGFSEPLAAPRHQYYNQ-EWTLWDRFEVQGLqpngeEMTLKQFLDYFKTEHKLEITMLSQGVSMLYSF 1000
Cdd:smart00985    1 YKNAFLNLALPFFAFSEPIAAPKTKYRDKdKWTLWDRLEVPGG-----DITLKELLDYFEEKYGLEVTMLSQGVSLLYSS 75

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|...
gi 209862989   1001 FMPAAKLKERLDQPMTEIVSRVSKRKLGRHVRALVLELCCNDESGEDVEVPYV 1053
Cdd:smart00985   76 FMPPKKHKERLDLPVTELVEQVTKKKLPPHVKYLVLEVSCEDEDDEDVEVPYI 128
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 450-612 2.37e-33

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: 129.09  E-value: 2.37e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989  450 RYDGQVAV--FGSDFQEKLSKQKYFLVGAGAIGCELLKNFAMIGLGcgeggEVVVTDMDTIEKSNLNRQFLFRPWDVTKL 527
Cdd:COG0476     7 RYSRQILLpeIGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVG-----TLTLVDDDVVELSNLQRQILYTEADVGRP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989  528 KSDTAAAAVRQMNPYIQVTSHQNRVGPDTEriydDDFFQNLDGVANALDNIDARMYMDRRCVYYRKPLLESGTLGTKGNV 607
Cdd:COG0476    82 KVEAAAERLRALNPDVEVEAIPERLTEENA----LELLAGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIGFEGQV 157


                  ....*
gi 209862989  608 QVVIP 612
Cdd:COG0476   158 TVFIP 162
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 450-599 1.85e-17

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 82.97  E-value: 1.85e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989  450 RYDGQVAVFGSDF--QEKLSKQKYFLVGAGAIGCELLKNFAMIGLGcgeggEVVVTDMDTIEKSNLNRQFLFRPWDVTKL 527
Cdd:PRK05690   12 RYNRQIILRGFDFdgQEKLKAARVLVVGLGGLGCAASQYLAAAGVG-----TLTLVDFDTVSLSNLQRQVLHDDATIGQP 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 209862989  528 KSDTAAAAVRQMNPYIQVTSHQNRVgpdteriyDDDFFQNL----DGVANALDNIDARMYMDRRCVYYRKPLLeSG 599
Cdd:PRK05690   87 KVESARAALARINPHIAIETINARL--------DDDELAALiaghDLVLDCTDNVATRNQLNRACFAAKKPLV-SG 153
 
Name Accession Description Interval E-value
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 49-1055 0e+00

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: 1305.25  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989    49 DIDESLYSRQLYVLGHEAMKMLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTTQWADLSSQFYLREEDIGKNRA 128
Cdd:TIGR01408    1 EIDEALYSRQLYVLGDEAMQKMAKSNVLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLSSNFFLSEDDVGRNRA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989   129 EVSQPRLAELNSYVPVTAYTGPLVEDFLSSFQVVVLTNSPLEAQLRVGEFCHSR--GIKLVVADTRGLFGQLFCDFGEEM 206
Cdd:TIGR01408   81 EAVVKKLAELNPYVHVSSSSVPFNEEFLDKFQCVVLTEMSLPLQKEINDFCHSQcpPIAFISADVRGLFGSLFCDFGDEF 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989   207 VLTDSNGEQPLSAMVSMVTKDNPGVVTCLDEARHGFETGDFVSFSEVQGMIQLNGCQPMEIKVLGPYTFSICDTSNFSDY 286
Cdd:TIGR01408  161 EVLDTDGEEPKTGFIASITQANPGIVTCLENHRHKLETGDFVTFREVNGMTGLNDGSPRKITVISPYSFSIGDTTELGPY 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989   287 IRGGIVSQVKVPKKISFKSLPASLVEPDFVMTDFAKYSRPAQLHIGFQALHQFCALHNQPPRPRNEEDATELVGLAQAVN 366
Cdd:TIGR01408  241 LHGGIATQVKTPKTVFFKSLREQLKDPKCLIVDFSKPERPPEIHTAFQALDQFQEKYSRKPNVGCQQDAEELLKLATSIS 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989   367 arSPPSVKQNSLDEDLIRKLAYVAAGDLAPINAFIGGLAAQEVMKACSGKFMPIMQWLYFDALECLPEDKEAlTEEKCLP 446
Cdd:TIGR01408  321 --ETLEEKVPDVDAKLVHWLSWTAQGFLSPMAAAVGGVVSQEVLKAVTGKFSPLCQWFYFDSAESLPSLGKP-ECEEFLP 397

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989   447 RQNRYDGQVAVFGSDFQEKLSKQKYFLVGAGAIGCELLKNFAMIGLGCGEGGEVVVTDMDTIEKSNLNRQFLFRPWDVTK 526
Cdd:TIGR01408  398 RGDRYDAQIAVFGDTFQQKLQNLNIFLVGCGAIGCEMLKNFALMGVGTGKKGMITVTDPDLIEKSNLNRQFLFRPHHIGK 477

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989   527 LKSDTAAAAVRQMNPYIQVTSHQNRVGPDTERIYDDDFFQNLDGVANALDNIDARMYMDRRCVYYRKPLLESGTLGTKGN 606
Cdd:TIGR01408  478 PKSYTAADATLKINPQIKIDAHQNRVGPETETIFNDEFYEKLDVVINALDNVEARRYVDSRCLAFLKPLLESGTLGTKGN 557

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989   607 VQVVIPFLTESYSSSQDPPEKSIPICTLKNFPNAIEHTLQWARDEFEGLFKQPAENVNQYL-TDSKFVERTLRLAGTQPL 685
Cdd:TIGR01408  558 TQVVVPHLTESYGSSRDPPEKEIPFCTLKSFPAAIEHTIQWARDKFEGLFSHKPSLVNKYLsSPSSAEEVLQKIQSGHSR 637

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989   686 EVLEAVQRSLVLQRPQTWGDCVTWACHHWHTQYCNNIRQLLHNFPPDQLTSSGAPFWSGPKRCPHPLTFDVNNTLHLDYV 765
Cdd:TIGR01408  638 EGLEQIIKLLSKEKPRNFSQCVEWARLKFEKYFNNKALQLLHCFPLDIRTSTGSPFWSSPKRPPSPLKFDLNEPLHLSFI 717

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989   766 MAAANLFAQTYGLTGSQ---DRAAVASLLQSVQVPEFTPKSGVKIHVSDQELQSANASVDDSR-LEELKATLPSPDKLPG 841
Cdd:TIGR01408  718 QAAAKLYATVYGIPFAEedlSADALLNILSEVKIPEFKPRSNKKIQTDETARKPDTAPIDDRNaIFQLEKAILSNEATKS 797

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989   842 -FKMYPIDFEKDDDSNFHMDFIVAASNLRAENYDISPADRHKSKLIAGKIIPAIATTTAAVVGLVCLELYKVVQGHQQLD 920
Cdd:TIGR01408  798 dFRMAPLSFEKDDDHNGHIDFITAASNLRAKNYSIEPADRFKTKFIAGKIIPAIATSTATVSGLVCLELIKVTDGGYKFE 877

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989   921 SYKNGFLNLALPFFGFSEPLAAPRHQYYNQEW-TLWDRFEVQGlqpngeEMTLKQFLDYFKTEHKLEITMLSQGVSMLYS 999
Cdd:TIGR01408  878 VYKNCFLNLAIPLFVFTEPTEVRKTKIRNGISfTIWDRWTLHG------DFTLLEFINAVKEKYGLEPTMVSQGVKLLYV 951

                          970       980       990      1000      1010
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 209862989  1000 FFMPaaKLKERLDQPMTEIVSRVSKRKLGRHVRALVLELCCNDESGEDVEVPYVRY 1055
Cdd:TIGR01408  952 PVMP--GHAERLKLKMHKLVKPTTKKKLPPYRVHLTVSFACDDDGDEDVPGPPVRI 1005
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
 470-1011 0e+00

Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present universally in eukaryotic cells, is part of cascade to attach ubiquitin (Ub) covalently to substrate proteins. This cascade consists of activating (E1), conjugating (E2), and/or ligating (E3) enzymes and then targets them for degradation by the 26S proteasome. E1 activates ubiquitin by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and ubiquitin's C-terminus. E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. Ubiquitin-E1 is a single-chain protein with a weakly conserved two-fold repeat. This CD represents the second repeat of Ub-E1.


Pssm-ID: 238767 [Multi-domain]  Cd Length: 435  Bit Score: 871.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989  470 KYFLVGAGAIGCELLKNFAMIGLGCGEGGEVVVTDMDTIEKSNLNRQFLFRPWDVTKLKSDTAAAAVRQMNPYIQVTSHQ 549
Cdd:cd01490     1 KVFLVGAGAIGCELLKNFALMGVGTGESGEITVTDMDNIEKSNLNRQFLFRPHDVGKPKSEVAAAAVKAMNPDLKITALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989  550 NRVGPDTERIYDDDFFQNLDGVANALDNIDARMYMDRRCVYYRKPLLESGTLGTKGNVQVVIPFLTESYSSSQDPPEKSI 629
Cdd:cd01490    81 NRVGPETEHIFNDEFWEKLDGVANALDNVDARMYVDRRCVYYRKPLLESGTLGTKGNTQVVIPHLTESYSSSRDPPEKSI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989  630 PICTLKNFPNAIEHTLQWARDEFEGLFKQPAENVNQYLtdskfvertlrlagtqplevleavqrslvlqrpqtWGDCVTW 709
Cdd:cd01490   161 PLCTLKNFPNAIEHTIQWARDEFEGLFKQPPENVNQYL-----------------------------------FEDCVRW 205

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989  710 ACHHWHTQYCNNIRQLLHNFPPDQLTSSGAPFWSGPKRCPHPLTFDVNNTLHLDYVMAAANLFAQTYGLTGsqdraavas 789
Cdd:cd01490   206 ARLLFEKYFNNNIKQLLHNFPPDAVTSDGAPFWSGPKRCPTPLEFDVNNPLHLDFVLAAANLYAEVYGIPG--------- 276

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989  790 llqsvqvpeftpksgvkihvsdqelqsanasvddsrleelkatlpspdklpgfkmypidFEKDDDSNFHMDFIVAASNLR 869
Cdd:cd01490   277 -----------------------------------------------------------FEKDDDTNFHMDFITAASNLR 297

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989  870 AENYDISPADRHKSKLIAGKIIPAIATTTAAVVGLVCLELYKVVQGHQQLDSYKNGFLNLALPFFGFSEPLAAPRHQY-Y 948
Cdd:cd01490   298 ARNYSIPPADRHKTKRIAGKIIPAIATTTAAVTGLVCLELYKVVDGKRPLEAYKNAFLNLALPFFAFSEPIPAPKVKYaY 377

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 209862989  949 NQEWTLWDRFEVQGLQPNGEEMTlkqflDYFKTEHKLEITMLSQGVSMLYSFFMPAAKLKERL 1011
Cdd:cd01490   378 DEEWTIWDRFEVKGKQTLQELLI-----DYFKEKYGLEVTMLSQGVSMLYSSFMPPAKLKERL 435
Ube1_repeat1 cd01491
Ubiquitin activating enzyme (E1), repeat 1. E1, a highly conserved small protein present ...
 54-436 8.09e-179

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: 522.21  E-value: 8.09e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989   54 LYSRQLYVLGHEAMKMLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTTQWADLSSQFYLREEDIGKNRAEVSQP 133
Cdd:cd01491     1 LYSRQLYVLGHEAMKKLQKSNVLISGLGGLGVEIAKNLILAGVKSVTLHDTKPCSWSDLSSQFYLREEDIGKNRAEASQA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989  134 RLAELNSYVPVTAYTGPLVEDFLSSFQVVVLTNSPLEAQLRVGEFCHSRGIKLVVADTRGLFGQLFCDFGEEMVLTDSNG 213
Cdd:cd01491    81 RLAELNPYVPVTVSTGPLTTDELLKFQVVVLTDASLEDQLKINEFCHSPGIKFISADTRGLFGSIFCDFGDEFTVYDPNG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989  214 EQPLSAMVSMVTKDNPGVVTCLDEARHGFETGDFVSFSEVQGMIQLNGCQPMEIKVLGPYTFSICDTSNFSDYIRGGIVS 293
Cdd:cd01491   161 EEPKSGMISSISKDNPGVVTCLDETRHGFEDGDYVTFSEVEGMTELNGCEPRKIKVKGPYTFSIGDTSSFSEYIRGGIVT 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989  294 QVKvpkkisfkslpaslvepdfvmtdfakysrpaqlhigfqalhqfcalhnqpprprneedatelvglaqavnarsppsv 373
Cdd:cd01491   241 QVK----------------------------------------------------------------------------- 243

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 209862989  374 kqnsldedlirklayvaagdLAPINAFIGGLAAQEVMKACSGKFMPIMQWLYFDALECLPEDK 436
Cdd:cd01491   244 --------------------LSPMAAFFGGLAAQEVLKACSGKFTPLKQWLYFDALECLPEDE 286
UBA_E1_SCCH pfam10585
Ubiquitin-activating enzyme, SCCH domain; Ubiquitin-activating enzyme (E1 enzyme) activates ...
 638-884 1.06e-149

Ubiquitin-activating enzyme, SCCH domain; Ubiquitin-activating enzyme (E1 enzyme) activates ubiquitin by first adenylating with ATP its C-terminal glycine residue and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding an ubiquitin-E1 thiolester and free AMP. Later the ubiquitin moiety is transferred to a cysteine residue on one of the many forms of ubiquitin-conjugating enzymes (E2). This domain carries the last of five conserved cysteines that is part of the active site of the enzyme, responsible for ubiquitin thiolester complex formation, the active site being represented by the sequence motif PICTLKNFP. The catalytic cysteine domain contains the E1 active site cysteine, and is divided in two half-domains, FCCH and SCCH, for 'first' and 'second' catalytic cysteine half-domain, respectively. This is the SCCH domain in which resides the catalytic cysteine.


Pssm-ID: 463157  Cd Length: 254  Bit Score: 445.91  E-value: 1.06e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989   638 PNAIEHTLQWARDEFEGLFKQPAENVNQYL-TDSKFVERTLRLAGTQPLEVLEAVQRSLVLQRPQTWGDCVTWACHHWHT 716
Cdd:pfam10585    1 PNAIEHTIQWARDEFEGLFVQPPEEVNKYLqPPQNFIESLLKQGGGQKLETLESVRKSLVTERPKTFEDCVAWARLKFEK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989   717 QYCNNIRQLLHNFPPDQLTSSGAPFWSGPKRCPHPLTFDVNNTLHLDYVMAAANLFAQTYGLTGSQDRAAVASLLQSVQV 796
Cdd:pfam10585   81 LFNNDIKQLLYNFPPDHKTSSGAPFWSGPKRPPTPLEFDPNNPLHLDFVVAAANLRAQVYGIPGSRDREAIAKVLSKVKV 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989   797 PEFTPKSGVKIHVSDQELQSANASV--DDSRLEELKATLP----SPDKLPGFKMYPIDFEKDDDSNFHMDFIVAASNLRA 870
Cdd:pfam10585  161 PEFKPKSGVKIQVNDEEAADPNAESedDEDELDELLEELPklavSPSSLAGFRLNPIEFEKDDDTNFHIDFITAASNLRA 240

                          250
                   ....*....|....
gi 209862989   871 ENYDISPADRHKSK 884
Cdd:pfam10585  241 RNYGIPPADRHKTK 254
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
 470-653 3.35e-78

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: 255.97  E-value: 3.35e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989  470 KYFLVGAGAIGCELLKNFAMIGLGcgeggEVVVTDMDTIEKSNLNRQFLFRPWDVTKLKSDTAAAAVRQMNPYIQVTSHQ 549
Cdd:cd01484     1 KVLLVGAGGIGCELLKNLALMGFG-----QIHVIDMDTIDVSNLNRQFLFRPKDIGRPKSEVAAEAVNDRNPNCKVVPYQ 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989  550 NRVGPdtERIYDDDFFQNLDGVANALDNIDARMYMDRRCVYYRKPLLESGTLGTKGNVQVVIPFLTESYSSSQDPPEKSI 629
Cdd:cd01484    76 NKVGP--EQDFNDTFFEQFHIIVNALDNIIARRYVNGMLIFLIVPLIESGTEGFKGNAQVILPGMTECIECTLYPPQKNF 153

                         170       180
                  ....*....|....*....|....
gi 209862989  630 PICTLKNFPNAIEHTLQWARDEFE 653
Cdd:cd01484   154 PMCTIASMPRLPEHCIEWARMLQW 177
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 451-637 5.70e-70

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: 233.30  E-value: 5.70e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989   451 YDGQVA--VFGSDFQEKLSKQKYFLVGAGAIGCELLKNFAMIGLGcgeggEVVVTDMDTIEKSNLNRQFLFRPWDVTKLK 528
Cdd:pfam00899    1 YSRQLAlpLIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVG-----KITLVDFDTVELSNLNRQFLFREADIGKPK 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989   529 SDTAAAAVRQMNPYIQVTSHQNRVGPDTeriyDDDFFQNLDGVANALDNIDARMYMDRRCVYYRKPLLESGTLGTKGNVQ 608
Cdd:pfam00899   76 AEVAAERLREINPDVEVEAYTERLTPEN----AEELIKSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVT 151

                          170       180       190
                   ....*....|....*....|....*....|.
gi 209862989   609 VVIPFLTESYS--SSQDPPEKSIPICTLKNF 637
Cdd:pfam00899  152 VVIPGKTPCYRclFPEDPPPKLVPSCTVAGV 182
UBA_e1_C smart00985
Ubiquitin-activating enzyme e1 C-terminal domain; This presumed domain found at the C terminus ...
 922-1053 4.00e-69

Ubiquitin-activating enzyme e1 C-terminal domain; This presumed domain found at the C terminus of Ubiquitin-activating enzyme e1 proteins is functionally uncharacterised.


Pssm-ID: 214955  Cd Length: 128  Bit Score: 226.37  E-value: 4.00e-69
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989    922 YKNGFLNLALPFFGFSEPLAAPRHQYYNQ-EWTLWDRFEVQGLqpngeEMTLKQFLDYFKTEHKLEITMLSQGVSMLYSF 1000
Cdd:smart00985    1 YKNAFLNLALPFFAFSEPIAAPKTKYRDKdKWTLWDRLEVPGG-----DITLKELLDYFEEKYGLEVTMLSQGVSLLYSS 75

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|...
gi 209862989   1001 FMPAAKLKERLDQPMTEIVSRVSKRKLGRHVRALVLELCCNDESGEDVEVPYV 1053
Cdd:smart00985   76 FMPPKKHKERLDLPVTELVEQVTKKKLPPHVKYLVLEVSCEDEDDEDVEVPYI 128
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 470-929 1.75e-56

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: 197.99  E-value: 1.75e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989  470 KYFLVGAGAIGCELLKNFAMIGLGcgeggEVVVTDMDTIEKSNLNRQFLFRPWDVTKLKSDTAAAAVRQMNPYIQVTSHQ 549
Cdd:cd01489     1 KVLVVGAGGIGCELLKNLVLTGFG-----EIHIIDLDTIDLSNLNRQFLFRKKHVGKSKAQVAKEAVLSFNPNVKIVAYH 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989  550 NRVgpdTERIYDDDFFQNLDGVANALDNIDARMYMDRRCVYYRKPLLESGTLGTKGNVQVVIPFLTESYSSSQDPPEKSI 629
Cdd:cd01489    76 ANI---KDPDFNVEFFKQFDLVFNALDNLAARRHVNKMCLAADVPLIESGTTGFLGQVQVIKKGKTECYECQPKETPKTF 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989  630 PICTLKNFPNAIEHTLQWARDE---FEGLFKQpaenvnqyltdskfvertlrlagtqplevleavqrslvlqrpqtwgdc 706
Cdd:cd01489   153 PVCTIRSTPSQPIHCIVWAKSLfflFNKVFKD------------------------------------------------ 184

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989  707 vtwachhwhtqycnNIRQLLHNfppDQLtssgapfWSGPKRcPHPLTFDvnntlhldyvmaaanlfaqtygltgsqdraa 786
Cdd:cd01489   185 --------------DIERLLSM---EEL-------WKTRKP-PVPLSWK------------------------------- 208

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989  787 vasllqsvqvpeftpksgvkihvsdqelqsanasvddsrleelkatlpspdklpgfkmyPIDFEKDDDSNfhMDFIVAAS 866
Cdd:cd01489   209 -----------------------------------------------------------ELTFDKDDQDA--LDFVAAAA 227

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 209862989  867 NLRAENYDISPADRHKSKLIAGKIIPAIATTTAAVVGLVCLELYKVVQGHqqLDSYKNGFLNL 929
Cdd:cd01489   228 NLRSHVFGIPMKSRFDIKQMAGNIIPAIATTNAIIAGLIVLEALKVLSGD--KEQCRTVFLNL 288
E1_UFD pfam09358
Ubiquitin fold domain; The ubiquitin fold domain is found at the C-terminus of ...
 955-1053 4.28e-50

Ubiquitin fold domain; The ubiquitin fold domain is found at the C-terminus of ubiquitin-activating E1 family enzymes. This domain binds to E2 enzymes.


Pssm-ID: 462768  Cd Length: 93  Bit Score: 171.57  E-value: 4.28e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989   955 WDRFEVQGlqpngeEMTLKQFLDYFKTEHKLEITMLSQGVSMLYSFFMPAAKLKERLDQPMTEIVSRVSKRKLGRHVRAL 1034
Cdd:pfam09358    1 WDRFEVEG------DMTLQELLDYFKEKYGLEVTMLSYGVSLLYSSFMPPKKHKERLPMKISELVEEVSKKPIPPHQKYL 74

                           90
                   ....*....|....*....
gi 209862989  1035 VLELCCNDESGEDVEVPYV 1053
Cdd:pfam09358   75 VLEVSCEDEDGEDVEVPYV 93
E1-1_like cd01485
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ...
 54-202 2.63e-45

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: 161.82  E-value: 2.63e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989   54 LYSRQLYVLGHEAMKMLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTTQWADLSSQFYLREE--DIGKNRAEVS 131
Cdd:cd01485     1 LYDRQIRLWGDEAQNKLRSAKVLIIGAGALGAEIAKNLVLAGIDSITIVDHRLVSTEDLGSNFFLDAEvsNSGMNRAAAS 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 209862989  132 QPRLAELNSYVPVTAYTGP------LVEDFLSSFQVVVLTNSPLEAQLRVGEFCHSRGIKLVVADTRGLFGQLFCDF 202
Cdd:cd01485    81 YEFLQELNPNVKLSIVEEDslsndsNIEEYLQKFTLVIATEENYERTAKVNDVCRKHHIPFISCATYGLIGYAFFDF 157
E1_FCCH pfam16190
Ubiquitin-activating enzyme E1 FCCH domain; This domain is found in the ubiquitin-activating ...
 227-296 7.22e-44

Ubiquitin-activating enzyme E1 FCCH domain; This domain is found in the ubiquitin-activating E1 family enzymes.


Pssm-ID: 465054 [Multi-domain]  Cd Length: 70  Bit Score: 153.02  E-value: 7.22e-44
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989   227 DNPGVVTCLDEARHGFETGDFVSFSEVQGMIQLNGCQPMEIKVLGPYTFSICDTSNFSDYIRGGIVSQVK 296
Cdd:pfam16190    1 DNPGVVTCLDDTRHGLEDGDYVTFSEVEGMTELNGCEPRKIKVLGPYTFSIGDTSSFSPYLRGGIVTQVK 70
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 55-199 5.17e-43

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: 156.65  E-value: 5.17e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989    55 YSRQLY--VLGHEAMKMLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTTQWADLSSQFYLREEDIGKNRAEVSQ 132
Cdd:pfam00899    1 YSRQLAlpLIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAA 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 209862989   133 PRLAELNSYVPVTAYTGPL----VEDFLSSFQVVVLTNSPLEAQLRVGEFCHSRGIKLVVADTRGLFGQLF 199
Cdd:pfam00899   81 ERLREINPDVEVEAYTERLtpenAEELIKSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVT 151
Aos1_SUMO cd01492
Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating ...
 54-201 7.62e-41

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: 148.98  E-value: 7.62e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989   54 LYSRQLYVLGHEAMKMLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTTQWADLSSQFYLREEDIGKNRAEVSQP 133
Cdd:cd01492     3 LYDRQIRLWGLEAQKRLRSARILLIGLKGLGAEIAKNLVLSGIGSLTILDDRTVTEEDLGAQFLIPAEDLGQNRAEASLE 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 209862989  134 RLAELNSYVPVTAYTGPLVE---DFLSSFQVVVLTNSPLEAQLRVGEFCHSRGIKLVVADTRGLFGQLFCD 201
Cdd:cd01492    83 RLRALNPRVKVSVDTDDISEkpeEFFSQFDVVVATELSRAELVKINELCRKLGVKFYATGVHGLFGFVFAD 153
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 470-649 1.74e-40

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: 151.35  E-value: 1.74e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989  470 KYFLVGAGAIGCELLKNFAMIGLGcgeggEVVVTDMDTIEKSNLNRQFLFRPWDVTKLKSDTAAAAVRQMNPYIQVTSHQ 549
Cdd:cd01488     1 KILVIGAGGLGCELLKNLALSGFR-----NIHVIDMDTIDVSNLNRQFLFREKDIGKPKAEVAAKFVNDRVPGVNVTPHF 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989  550 NRVgpdteRIYDDDFFQNLDGVANALDNIDARMYMDRRCVY--------YRKPLLESGTLGTKGNVQVVIPFLTESYSSS 621
Cdd:cd01488    76 GKI-----QDKDEEFYRQFNIIICGLDSIEARRWINGTLVSlllyedpeSIIPLIDGGTEGFKGHARVILPGITACIECS 150

                         170       180       190
                  ....*....|....*....|....*....|
gi 209862989  622 QD--PPEKSIPICTLKNFPNAIEHTLQWAR 649
Cdd:cd01488   151 LDlfPPQVTFPLCTIANTPRLPEHCIEYAS 180
E1_4HB pfam16191
Ubiquitin-activating enzyme E1 four-helix bundle; This domain is found in the ...
 297-366 2.14e-34

Ubiquitin-activating enzyme E1 four-helix bundle; This domain is found in the ubiquitin-activating E1 family enzymes.


Pssm-ID: 465055  Cd Length: 70  Bit Score: 125.65  E-value: 2.14e-34
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989   297 VPKKISFKSLPASLVEPDFVMTDFAKYSRPAQLHIGFQALHQFCALHNQPPRPRNEEDATELVGLAQAVN 366
Cdd:pfam16191    1 MPKTLSFKSLEESLKEPEFLISDFAKFDRPAQLHLAFQALHAFQEKHGRLPRPWNEEDAEEVVKLAKELN 70
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 450-612 2.37e-33

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: 129.09  E-value: 2.37e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989  450 RYDGQVAV--FGSDFQEKLSKQKYFLVGAGAIGCELLKNFAMIGLGcgeggEVVVTDMDTIEKSNLNRQFLFRPWDVTKL 527
Cdd:COG0476     7 RYSRQILLpeIGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVG-----TLTLVDDDVVELSNLQRQILYTEADVGRP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989  528 KSDTAAAAVRQMNPYIQVTSHQNRVGPDTEriydDDFFQNLDGVANALDNIDARMYMDRRCVYYRKPLLESGTLGTKGNV 607
Cdd:COG0476    82 KVEAAAERLRALNPDVEVEAIPERLTEENA----LELLAGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIGFEGQV 157


                  ....*
gi 209862989  608 QVVIP 612
Cdd:COG0476   158 TVFIP 162
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 450-632 2.81e-33

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: 128.36  E-value: 2.81e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989  450 RYDGQVAV--FGSDFQEKLSKQKYFLVGAGAIGCELLKNFAMIGLGcgeggEVVVTDMDTIEKSNLNRQFLFRPWDVTKL 527
Cdd:cd00757     1 RYSRQILLpeIGEEGQEKLKNARVLVVGAGGLGSPAAEYLAAAGVG-----KLGLVDDDVVELSNLQRQILHTEADVGQP 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989  528 KSDTAAAAVRQMNPYIQVTSHQNRVGPDTEriydDDFFQNLDGVANALDNIDARMYMDRRCVYYRKPLLESGTLGTKGNV 607
Cdd:cd00757    76 KAEAAAERLRAINPDVEIEAYNERLDAENA----EELIAGYDLVLDCTDNFATRYLINDACVKLGKPLVSGAVLGFEGQV 151

                         170       180
                  ....*....|....*....|....*.
gi 209862989  608 QVVIPFLTESYSSS-QDPPEKSIPIC 632
Cdd:cd00757   152 TVFIPGEGPCYRCLfPEPPPPGVPSC 177
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 472-611 7.16e-32

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: 121.22  E-value: 7.16e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989  472 FLVGAGAIGCELLKNFAMIGLGcgeggEVVVTDMDTIEKSNLNRQFLFRPWDVTKLKSDTAAAAVRQMNPYIQVTSHQNR 551
Cdd:cd01483     3 LLVGLGGLGSEIALNLARSGVG-----KITLIDFDTVELSNLNRQFLARQADIGKPKAEVAARRLNELNPGVNVTAVPEG 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989  552 VGPDTeriyDDDFFQNLDGVANALDNIDARMYMDRRCVYYRKPLLESGTLGTKGNVQVVI 611
Cdd:cd01483    78 ISEDN----LDDFLDGVDLVIDAIDNIAVRRALNRACKELGIPVIDAGGLGLGGDIQVID 133
APPBP1_RUB cd01493
Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric ...
 55-428 9.42e-24

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: 105.46  E-value: 9.42e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989   55 YSRQLYVLGHEAMKMLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTTQWADLSSQFYLREEDIGKNRAEVSQPR 134
Cdd:cd01493     3 YDRQLRLWGEHGQAALESAHVCLLNATATGTEILKNLVLPGIGSFTIVDGSKVDEEDLGNNFFLDASSLGKSRAEATCEL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989  135 LAELNSYVPVTAYTGPLVE------DFLSSFQVVVLTNSPLEAQLRVGEFCHSRGIKLVVADTRGLFGQL------FC-- 200
Cdd:cd01493    83 LQELNPDVNGSAVEESPEAlldndpSFFSQFTVVIATNLPESTLLRLADVLWSANIPLLYVRSYGLYGYIriqlkeHTiv 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989  201 DFGEEMVLTDSNGEQPLSAMVSMVtkdnpgvvtcldeARHGFETGDFVSFSEVQGMIQLngcqpmeIKVL--------GP 272
Cdd:cd01493   163 ESHPDNALEDLRLDNPFPELREHA-------------DSIDLDDMDPAEHSHTPYIVIL-------IKYLekwrsahnGQ 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989  273 YTFSICDTSNFSDYIRGGIVSQ-----VKVPKKISFKSL-----PASLVEpdfVMTDFAK---YSRPAQLHIGFQALHQF 339
Cdd:cd01493   223 LPSTYKEKKEFRDLVRSLMRSNedeenFEEAIKAVNKALnrtkiPSSVEE---IFNDDRCenlTSQSSSFWIMARALKEF 299

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989  340 CALHNQ-PP----------------------RPRNEEDATELVGLAQAV---NARSPPSVKQNSLdEDLIRKLAYVAA-- 391
Cdd:cd01493   300 VAEENGlLPlpgtlpdmtadtekyiklqniyREKAEKDAAEVEKYVREIlksLGRSPDSISDKEI-KLFCKNAAFLRVir 378

                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 209862989  392 --GDLAPINAFIGGLAAQEVMKACSGKFMPIMQWLYFDA 428
Cdd:cd01493   379 grSLEHNISAFMGGIAAQEVIKLITKQYVPIDNTFIFDG 417
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 75-198 5.36e-20

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: 87.32  E-value: 5.36e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989   75 VLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTTQWADLSSQFYLREEDIGKNRAEVSQPRLAELNSYVPVTAYT----GP 150
Cdd:cd01483     2 VLLVGLGGLGSEIALNLARSGVGKITLIDFDTVELSNLNRQFLARQADIGKPKAEVAARRLNELNPGVNVTAVPegisED 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 209862989  151 LVEDFLSSFQVVVLTNSPLEAQLRVGEFCHSRGIKLVVADTRGLFGQL 198
Cdd:cd01483    82 NLDDFLDGVDLVIDAIDNIAVRRALNRACKELGIPVIDAGGLGLGGDI 129
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 450-599 1.85e-17

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 82.97  E-value: 1.85e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989  450 RYDGQVAVFGSDF--QEKLSKQKYFLVGAGAIGCELLKNFAMIGLGcgeggEVVVTDMDTIEKSNLNRQFLFRPWDVTKL 527
Cdd:PRK05690   12 RYNRQIILRGFDFdgQEKLKAARVLVVGLGGLGCAASQYLAAAGVG-----TLTLVDFDTVSLSNLQRQVLHDDATIGQP 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 209862989  528 KSDTAAAAVRQMNPYIQVTSHQNRVgpdteriyDDDFFQNL----DGVANALDNIDARMYMDRRCVYYRKPLLeSG 599
Cdd:PRK05690   87 KVESARAALARINPHIAIETINARL--------DDDELAALiaghDLVLDCTDNVATRNQLNRACFAAKKPLV-SG 153
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
459-612 3.97e-16

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 81.60  E-value: 3.97e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989  459 GSDFQEKLSKQKYFLVGAGAIGCELLKNFAMIGLGcgeggEVVVTDMDTIEKSNLNRQFLFRPWDVTKLKSDTAAAAVRQ 538
Cdd:PRK08762  126 GEEGQRRLLEARVLLIGAGGLGSPAALYLAAAGVG-----TLGIVDHDVVDRSNLQRQILHTEDRVGQPKVDSAAQRLAA 200

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 209862989  539 MNPYIQVTSHQNRVGPDTEriydDDFFQNLDGVANALDNIDARMYMDRRCVYYRKPLLESGTLGTKGNVQVVIP 612
Cdd:PRK08762  201 LNPDVQVEAVQERVTSDNV----EALLQDVDVVVDGADNFPTRYLLNDACVKLGKPLVYGAVFRFEGQVSVFDA 270
PRK08328 PRK08328
hypothetical protein; Provisional
 55-198 2.25e-15

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 76.76  E-value: 2.25e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989   55 YSRQLYVLGHEAMKMLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTTQWADLSSQFYLREEDIGKNRAEVSQP- 133
Cdd:PRK08328   10 YDRQIMIFGVEGQEKLKKAKVAVVGVGGLGSPVAYYLAAAGVGRILLIDEQTPELSNLNRQILHWEEDLGKNPKPLSAKw 89

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 209862989  134 RLAELNSYVPVTAYTGPL----VEDFLSSFQVVVLTNSPLEAQLRVGEFCHSRGIKLVVADTRGLFGQL 198
Cdd:PRK08328   90 KLERFNSDIKIETFVGRLseenIDEVLKGVDVIVDCLDNFETRYLLDDYAHKKGIPLVHGAVEGTYGQV 158
PRK08328 PRK08328
hypothetical protein; Provisional
 450-617 3.47e-15

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 75.99  E-value: 3.47e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989  450 RYDGQVAVFGSDFQEKLSKQKYFLVGAGAIGCELLKNFAMIGLgcgegGEVVVTDMDTIEKSNLNRQFLFRPWDVTK-LK 528
Cdd:PRK08328    9 RYDRQIMIFGVEGQEKLKKAKVAVVGVGGLGSPVAYYLAAAGV-----GRILLIDEQTPELSNLNRQILHWEEDLGKnPK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989  529 SDTAAAAVRQMNPYIQVTSHQNRVgpDTERIydDDFFQNLDGVANALDNIDARMYMDRRCVYYRKPLLESGTLGTKGNVQ 608
Cdd:PRK08328   84 PLSAKWKLERFNSDIKIETFVGRL--SEENI--DEVLKGVDVIVDCLDNFETRYLLDDYAHKKGIPLVHGAVEGTYGQVT 159


                  ....*....
gi 209862989  609 VVIPFLTES 617
Cdd:PRK08328  160 TIVPGKTKR 168
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 449-612 7.37e-15

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 77.34  E-value: 7.37e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989  449 NRYDGQV--AVFGSDFQEKLSKQKYFLVGAGAIGCELLKNFAMIGLGcgeggEVVVTDMDTIEKSNLNRQFLFRPWDVTK 526
Cdd:PRK07688    3 ERYSRQElfSPIGEEGQQKLREKHVLIIGAGALGTANAEMLVRAGVG-----KVTIVDRDYVEWSNLQRQQLYTESDVKN 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989  527 LKSDTAAAAVR--QMNPYIQVTSHQNRVGPdtERIydDDFFQNLDGVANALDNIDARMYMDRRCVYYRKPLLESGTLGTK 604
Cdd:PRK07688   78 NLPKAVAAKKRleEINSDVRVEAIVQDVTA--EEL--EELVTGVDLIIDATDNFETRFIVNDAAQKYGIPWIYGACVGSY 153


                  ....*...
gi 209862989  605 GNVQVVIP 612
Cdd:PRK07688  154 GLSYTIIP 161
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 440-581 2.19e-14

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 76.07  E-value: 2.19e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989  440 TEEKCLPRQNRYDGqvavFGSDFQEKLSKQKYFLVGAGAIGCELLKNFAMIGLGcgeggEVVVTDMDTIEKSNLNRQFLF 519
Cdd:PRK05600   17 SELRRTARQLALPG----FGIEQQERLHNARVLVIGAGGLGCPAMQSLASAGVG-----TITLIDDDTVDVSNIHRQILF 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 209862989  520 RPWDVTKLKSDTAAAAVRQMNPYIQVTSHQNRVGPDTERiyddDFFQNLDGVANALDNIDAR 581
Cdd:PRK05600   88 GASDVGRPKVEVAAERLKEIQPDIRVNALRERLTAENAV----ELLNGVDLVLDGSDSFATK 145
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 55-224 2.93e-14

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: 73.62  E-value: 2.93e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989   55 YSRQ--LYVLGHEAMKMLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTTQWADLSSQFYLREEDIGKNRAEVSQ 132
Cdd:COG0476     8 YSRQilLPEIGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADVGRPKVEAAA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989  133 PRLAELNSYVPVTAYTGPL----VEDFLSSFQVVV--LTNspLEAQLRVGEFCHSRGIKLVVADTRGLFGQLF------- 199
Cdd:COG0476    88 ERLRALNPDVEVEAIPERLteenALELLAGADLVLdcTDN--FATRYLLNDACVKLGIPLVSGAVIGFEGQVTvfipgdt 165

                         170       180       190
                  ....*....|....*....|....*....|
gi 209862989  200 ----CDFGEEMVLTDSNGEQP-LSAMVSMV 224
Cdd:COG0476   166 pcyrCLFPEPPEPGPSCAEAGvLGPLVGVI 195
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 55-198 5.35e-14

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: 72.51  E-value: 5.35e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989   55 YSRQLYV--LGHEAMKMLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTTQWADLSSQFYLREEDIGKNRAEVSQ 132
Cdd:cd00757     2 YSRQILLpeIGEEGQEKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRQILHTEADVGQPKAEAAA 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 209862989  133 PRLAELNSYVPVTAY----TGPLVEDFLSSFQVVV--LTNspLEAQLRVGEFCHSRGIKLVVADTRGLFGQL 198
Cdd:cd00757    82 ERLRAINPDVEIEAYnerlDAENAEELIAGYDLVLdcTDN--FATRYLINDACVKLGKPLVSGAVLGFEGQV 151
Aos1_SUMO cd01492
Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating ...
 451-605 3.20e-12

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: 66.55  E-value: 3.20e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989  451 YDGQVAVFGSDFQEKLSKQKYFLVGAGAIGCELLKNFAMIGLgcgegGEVVVTDMDTIEKSNLNRQFLFRPWDVTKLKSD 530
Cdd:cd01492     4 YDRQIRLWGLEAQKRLRSARILLIGLKGLGAEIAKNLVLSGI-----GSLTILDDRTVTEEDLGAQFLIPAEDLGQNRAE 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 209862989  531 TAAAAVRQMNPYIQVTShqnrvgpDTERI--YDDDFFQNLDGV-ANALDNiDARMYMDRRCVYYRKPLLESGTLGTKG 605
Cdd:cd01492    79 ASLERLRALNPRVKVSV-------DTDDIseKPEEFFSQFDVVvATELSR-AELVKINELCRKLGVKFYATGVHGLFG 148
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 459-594 3.71e-12

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 69.35  E-value: 3.71e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989  459 GSDFQEKLSKQKYFLVGAGAIGCELLKNFAMIGLGCgeggeVVVTDMDTIEKSNLNRQFLFRPWDVTKLKSDTAAAAVRQ 538
Cdd:PRK07878   33 GVDGQKRLKNARVLVIGAGGLGSPTLLYLAAAGVGT-----LGIVEFDVVDESNLQRQVIHGQSDVGRSKAQSARDSIVE 107

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 209862989  539 MNPYIQVTSHQNRVGPDTERiyddDFFQNLDGVANALDNIDARMYMDRRCVYYRKP 594
Cdd:PRK07878  108 INPLVNVRLHEFRLDPSNAV----ELFSQYDLILDGTDNFATRYLVNDAAVLAGKP 159
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
 458-604 5.85e-12

Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli hypothetical protein ygdL. The common reaction mechanism catalyzed by E1-like enzymes begins with a nucleophilic attack of the C-terminal carboxylate of the ubiquitin-like substrate, on the alpha-phosphate of an ATP molecule bound at the active site of the activating enzymes, leading to the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of the substrate. The exact function of this family is unknown.


Pssm-ID: 238384 [Multi-domain]  Cd Length: 231  Bit Score: 66.47  E-value: 5.85e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989  458 FGSDFQEKLSKQKYFLVGAGAIGcellkNFAMIGL---GCGEggeVVVTDMDTIEKSNLNRQFLFRPWDVTKLKSDTAAA 534
Cdd:cd00755     1 YGEEGLEKLRNAHVAVVGLGGVG-----SWAAEALarsGVGK---LTLIDFDVVCVSNLNRQIHALLSTVGKPKVEVMAE 72

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989  535 AVRQMNPYIQVTSHQNRVGPDTEriyDDDFFQNLDGVANALDNIDARMYMDRRCVYYRKPLLESGTLGTK 604
Cdd:cd00755    73 RIRDINPECEVDAVEEFLTPDNS---EDLLGGDPDFVVDAIDSIRAKVALIAYCRKRKIPVISSMGAGGK 139
E1-1_like cd01485
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ...
 451-545 4.67e-11

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: 63.21  E-value: 4.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989  451 YDGQVAVFGSDFQEKLSKQKYFLVGAGAIGCELLKNFAMIGLgcgegGEVVVTDMDTIEKSNLNRQFLFRPWDVT--KLK 528
Cdd:cd01485     2 YDRQIRLWGDEAQNKLRSAKVLIIGAGALGAEIAKNLVLAGI-----DSITIVDHRLVSTEDLGSNFFLDAEVSNsgMNR 76

                          90
                  ....*....|....*..
gi 209862989  529 SDTAAAAVRQMNPYIQV 545
Cdd:cd01485    77 AAASYEFLQELNPNVKL 93
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 448-638 8.47e-11

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 64.75  E-value: 8.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989  448 QNRYDGQVAV--FGSDFQEKLSKQKYFLVGAGAIGCELLKNFAMIGLGcgeggEVVVTDMDTIEKSNLNRQFLFRPWDVT 525
Cdd:PRK12475    2 QERYSRQILFsgIGEEGQRKIREKHVLIVGAGALGAANAEALVRAGIG-----KLTIADRDYVEWSNLQRQQLYTEEDAK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989  526 KLKSDTAAAA--VRQMNPYIQVTSHQNRVGPDTERiyddDFFQNLDGVANALDNIDARMYMDRRCVYYRKPLLESGTLGT 603
Cdd:PRK12475   77 QKKPKAIAAKehLRKINSEVEIVPVVTDVTVEELE----ELVKEVDLIIDATDNFDTRLLINDLSQKYNIPWIYGGCVGS 152

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 209862989  604 KGNVQVVIPFLTESYSssqdppeksipiCTLKNFP 638
Cdd:PRK12475  153 YGVTYTIIPGKTPCLR------------CLMEHVP 175
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
451-580 8.92e-11

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 62.57  E-value: 8.92e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989  451 YDGQVAVFGSDFQEKLSKQKYFLVGAGAIGCELLKNFAMIGLGcgeggEVVVTDMDTIEKSNLNRQFLFrPWDVTKLKSD 530
Cdd:PRK08644   11 EAMLASRHTPKLLEKLKKAKVGIAGAGGLGSNIAVALARSGVG-----NLKLVDFDVVEPSNLNRQQYF-ISQIGMPKVE 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 209862989  531 TAAAAVRQMNPYIQVTSHQNRVgpDTERIydDDFFQNLDGVANALDNIDA 580
Cdd:PRK08644   85 ALKENLLEINPFVEIEAHNEKI--DEDNI--EELFKDCDIVVEAFDNAET 130
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 450-581 1.28e-10

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 64.51  E-value: 1.28e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989  450 RYDGQVAV--FGSDFQEKLSKQKYFLVGAGAIGCELLKNFAMIGLGcgeggEVVVTDMDTIEKSNLNRQFLFRPWDVTKL 527
Cdd:PRK05597    8 RYRRQIMLgeIGQQGQQSLFDAKVAVIGAGGLGSPALLYLAGAGVG-----HITIIDDDTVDLSNLHRQVIHSTAGVGQP 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 209862989  528 KSDTAAAAVRQMNPYIQVTSHQNRVGPDTERiyddDFFQNLDGVANALDNIDAR 581
Cdd:PRK05597   83 KAESAREAMLALNPDVKVTVSVRRLTWSNAL----DELRDADVILDGSDNFDTR 132
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 74-164 3.95e-10

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: 61.99  E-value: 3.95e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989   74 SVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTTQWADLSSQFYLREEDIGKNRAEVSQPRLAELNSYVPVTAYTGPLV- 152
Cdd:cd01488     1 KILVIGAGGLGCELLKNLALSGFRNIHVIDMDTIDVSNLNRQFLFREKDIGKPKAEVAAKFVNDRVPGVNVTPHFGKIQd 80

                          90
                  ....*....|....
gi 209862989  153 --EDFLSSFQVVVL 164
Cdd:cd01488    81 kdEEFYRQFNIIIC 94
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 75-198 4.89e-10

Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating enzyme (E1), specific for the SUMO family of ubiquitin-like proteins (Ubls). E1 enzymes are part of a conjugation cascade to attach Ub or Ubls, covalently to substrate proteins consisting of activating (E1), conjugating (E2), and/or ligating (E3) enzymes. E1 activates ubiquitin by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and Ubls C-terminus. The E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. Post-translational modification by SUMO family of ubiquitin-like proteins (Ublps) is involved in cell division, nuclear transport, the stress response and signal transduction. UBA2 contains both the nucleotide-binding motif involved in adenylation and the catalytic cysteine involved in the thioester intermediate and Ublp transfer to E2.


Pssm-ID: 238766 [Multi-domain]  Cd Length: 312  Bit Score: 62.01  E-value: 4.89e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989   75 VLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTTQWADLSSQFYLREEDIGKNRAEVSQPRLAELNSYVPVTAYTGPLVE- 153
Cdd:cd01489     2 VLVVGAGGIGCELLKNLVLTGFGEIHIIDLDTIDLSNLNRQFLFRKKHVGKSKAQVAKEAVLSFNPNVKIVAYHANIKDp 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 209862989  154 ----DFLSSFQVVV--LTNspLEAQLRVGEFCHSRGIKLVVADTRGLFGQL 198
Cdd:cd01489    82 dfnvEFFKQFDLVFnaLDN--LAARRHVNKMCLAADVPLIESGTTGFLGQV 130
TcdA COG1179
tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ...
 473-599 6.58e-10

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


Pssm-ID: 440792  Cd Length: 247  Bit Score: 60.87  E-value: 6.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989  473 LVGAGAIgcELLKN--FAMIGLG-----CGEG------GEVVVTDMDTIEKSNLNRQF--LfrpwDVT--KLKSDTAAAA 535
Cdd:COG1179    13 LYGEEGL--ERLANahVAVVGLGgvgswAAEAlarsgvGRLTLVDLDDVCESNINRQLhaL----DSTvgRPKVEVMAER 86

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 209862989  536 VRQMNPYIQVTSHQNRVGPDTeriYDDDFFQNLDGVANALDNIDARMYMDRRCVYYRKPLLESG 599
Cdd:COG1179    87 IRDINPDCEVTAIDEFVTPEN---ADELLSEDYDYVIDAIDSVSAKAALIAWCRRRGIPIISSM 147
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
 74-196 1.84e-08

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: 56.43  E-value: 1.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989   74 SVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTTQWADLSSQFYLREEDIGKNRAEVSQPRLAELNSYVPVTAYTGPLVE 153
Cdd:cd01484     1 KVLLVGAGGIGCELLKNLALMGFGQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKSEVAAEAVNDRNPNCKVVPYQNKVGP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 209862989  154 D------FLSSFQVVVLTNSPLEAQLRVGEFCHSRGIKLVVADTRGLFG 196
Cdd:cd01484    81 EqdfndtFFEQFHIIVNALDNIIARRYVNGMLIFLIVPLIESGTEGFKG 129
Ube1_repeat1 cd01491
Ubiquitin activating enzyme (E1), repeat 1. E1, a highly conserved small protein present ...
 451-550 2.47e-08

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: 56.51  E-value: 2.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989  451 YDGQVAVFGSDFQEKLSKQKYFLVGAGAIGCELLKNFAMIGLGcgeggEVVVTDMDTIEKSNLNRQFLFRPWDVTKLKSD 530
Cdd:cd01491     2 YSRQLYVLGHEAMKKLQKSNVLISGLGGLGVEIAKNLILAGVK-----SVTLHDTKPCSWSDLSSQFYLREEDIGKNRAE 76

                          90       100
                  ....*....|....*....|
gi 209862989  531 TAAAAVRQMNPYIQVTSHQN 550
Cdd:cd01491    77 ASQARLAELNPYVPVTVSTG 96
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
459-594 2.59e-08

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 57.44  E-value: 2.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989  459 GSDFQEKLSKQKYFLVGAGAIGCELLKNFAMIGLGcgeggEVVVTDMDTIEKSNLNRQFLFRPWDVTKLKSDTAAAAVRQ 538
Cdd:PRK07411   29 GLEGQKRLKAASVLCIGTGGLGSPLLLYLAAAGIG-----RIGIVDFDVVDSSNLQRQVIHGTSWVGKPKIESAKNRILE 103

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 209862989  539 MNPYIQVTSHQNRVGPDTERiyddDFFQNLDGVANALDNIDARMYMDRRCVYYRKP 594
Cdd:PRK07411  104 INPYCQVDLYETRLSSENAL----DILAPYDVVVDGTDNFPTRYLVNDACVLLNKP 155
E1_ThiF_like cd01487
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ...
 473-581 8.19e-08

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: 53.15  E-value: 8.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989  473 LVGAGAIGCELLKNFAMIGLGcgeggEVVVTDMDTIEKSNLNRQFlFRPWDVTKLKSDTAAAAVRQMNPYIQVTSHQNRV 552
Cdd:cd01487     4 IAGAGGLGSNIAVLLARSGVG-----NLKLVDFDVVEPSNLNRQQ-YFLSQIGEPKVEALKENLREINPFVKIEAINIKI 77

                          90       100
                  ....*....|....*....|....*....
gi 209862989  553 gpDTERIYddDFFQNLDGVANALDNIDAR 581
Cdd:cd01487    78 --DENNLE--GLFGDCDIVVEAFDNAETK 102
PTZ00245 PTZ00245
ubiquitin activating enzyme; Provisional
 55-144 9.04e-07

ubiquitin activating enzyme; Provisional


Pssm-ID: 140272  Cd Length: 287  Bit Score: 51.98  E-value: 9.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989   55 YSRQLYVLGHEAMKMLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTTQWADLSSQfYLREEDIGKNRAEVSQPR 134
Cdd:PTZ00245    9 YDRQIRLWGKSTQQQLMHTSVALHGVAGAAAEAAKNLVLAGVRAVAVADEGLVTDADVCTN-YLMQGEAGGTRGARALGA 87

                          90
                  ....*....|
gi 209862989  135 LAELNSYVPV 144
Cdd:PTZ00245   88 LQRLNPHVSV 97
PRK08223 PRK08223
hypothetical protein; Validated
 463-612 4.38e-06

hypothetical protein; Validated


Pssm-ID: 181302 [Multi-domain]  Cd Length: 287  Bit Score: 49.68  E-value: 4.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989  463 QEKLSKQKYFLVGAGAIGCELLKNFAMIGLGCgeggeVVVTDMDTIEKSNLNRQF------LFRPwdvtklKSDTAAAAV 536
Cdd:PRK08223   22 QQRLRNSRVAIAGLGGVGGIHLLTLARLGIGK-----FTIADFDVFELRNFNRQAgammstLGRP------KAEVLAEMV 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989  537 RQMNPYIQVTSHQNRVGPDTEriydDDFfqnLDGVANALDNIDARMYMDRRCVY---YRK--PLLESGTLGTKGNVQVVI 611
Cdd:PRK08223   91 RDINPELEIRAFPEGIGKENA----DAF---LDGVDVYVDGLDFFEFDARRLVFaacQQRgiPALTAAPLGMGTALLVFD 163


                  .
gi 209862989  612 P 612
Cdd:PRK08223  164 P 164
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 55-163 8.18e-06

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 48.30  E-value: 8.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989   55 YSRQLyVL------GHEAMKmlqTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTTQWADLSSQFYLREEDIGKNRA 128
Cdd:PRK05690   13 YNRQI-ILrgfdfdGQEKLK---AARVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVSLSNLQRQVLHDDATIGQPKV 88

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 209862989  129 EVSQPRLAELNSYVPVTAYTGPLVEDFL----SSFQVVV 163
Cdd:PRK05690   89 ESARAALARINPHIAIETINARLDDDELaaliAGHDLVL 127
PRK15116 PRK15116
sulfur acceptor protein CsdL; Provisional
 450-602 9.37e-06

sulfur acceptor protein CsdL; Provisional


Pssm-ID: 185071  Cd Length: 268  Bit Score: 48.65  E-value: 9.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989  450 RYDGQVAVFGSDFQEKLSKQKYFLVGAGAIGCELLKNFAMIGLGCgeggeVVVTDMDTIEKSNLNRQFLFRPWDVTKLKS 529
Cdd:PRK15116   12 RFGGTARLYGEKALQLFADAHICVVGIGGVGSWAAEALARTGIGA-----ITLIDMDDVCVTNTNRQIHALRDNVGLAKA 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 209862989  530 DTAAAAVRQMNPYIQVTSHQNRVGPDTERIYDDdffQNLDGVANALDNIDARMYMDRRCVYYRKPLLESGTLG 602
Cdd:PRK15116   87 EVMAERIRQINPECRVTVVDDFITPDNVAEYMS---AGFSYVIDAIDSVRPKAALIAYCRRNKIPLVTTGGAG 156
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 55-154 1.04e-05

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 48.84  E-value: 1.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989   55 YSRQLYV--LGHEAMKMLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTTQWADLSSQFYLREEDIGKN--RAEV 130
Cdd:PRK07688    5 YSRQELFspIGEEGQQKLREKHVLIIGAGALGTANAEMLVRAGVGKVTIVDRDYVEWSNLQRQQLYTESDVKNNlpKAVA 84

                          90       100
                  ....*....|....*....|....
gi 209862989  131 SQPRLAELNSYVPVTAytgpLVED 154
Cdd:PRK07688   85 AKKRLEEINSDVRVEA----IVQD 104
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 894-949 1.57e-05

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: 47.64  E-value: 1.57e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 209862989   894 IATTTAAVVGLVCLELYKVVQGHqQLDSYKNGFLNLALPFFGFSEPLAAPRHQYYN 949
Cdd:pfam00899  183 LGPTTAVVAGLQALEALKLLLGK-GEPNLAGRLLQFDALTMTFRELRLALKNPNCP 237
APPBP1_RUB cd01493
Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric ...
 450-541 2.52e-05

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: 48.07  E-value: 2.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989  450 RYDGQVAVFGSDFQEKLSKQKYFLVGAGAIGCELLKNFAMIGLgcgegGEVVVTDMDTIEKSNLNRQFLFRPWDVTKLKS 529
Cdd:cd01493     2 KYDRQLRLWGEHGQAALESAHVCLLNATATGTEILKNLVLPGI-----GSFTIVDGSKVDEEDLGNNFFLDASSLGKSRA 76

                          90
                  ....*....|..
gi 209862989  530 DTAAAAVRQMNP 541
Cdd:cd01493    77 EATCELLQELNP 88
PRK14851 PRK14851
hypothetical protein; Provisional
 455-612 4.58e-05

hypothetical protein; Provisional


Pssm-ID: 184853 [Multi-domain]  Cd Length: 679  Bit Score: 47.55  E-value: 4.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989  455 VAVFGSDFQEKLSKQKYFLVGAGAIGCELLKNFAMIGLGcgeggEVVVTDMDTIEKSNLNRQFLFRPWDVTKLKSDTAAA 534
Cdd:PRK14851   30 IGLFTPGEQERLAEAKVAIPGMGGVGGVHLITMVRTGIG-----RFHIADFDQFEPVNVNRQFGARVPSFGRPKLAVMKE 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989  535 AVRQMNPYIQVTshqnrvgPDTERIYDDDFFQNLDGVANALDNIDARMYMDRRCVYYRK-----PLLESGTLGTKGNVQV 609
Cdd:PRK14851  105 QALSINPFLEIT-------PFPAGINADNMDAFLDGVDVVLDGLDFFQFEIRRTLFNMArekgiPVITAGPLGYSSAMLV 177


                  ...
gi 209862989  610 VIP 612
Cdd:PRK14851  178 FTP 180
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
 74-163 6.43e-05

Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present universally in eukaryotic cells, is part of cascade to attach ubiquitin (Ub) covalently to substrate proteins. This cascade consists of activating (E1), conjugating (E2), and/or ligating (E3) enzymes and then targets them for degradation by the 26S proteasome. E1 activates ubiquitin by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and ubiquitin's C-terminus. E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. Ubiquitin-E1 is a single-chain protein with a weakly conserved two-fold repeat. This CD represents the second repeat of Ub-E1.


Pssm-ID: 238767 [Multi-domain]  Cd Length: 435  Bit Score: 46.51  E-value: 6.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989   74 SVLVSGLRGLGVEIAKNIILGGVKA-----VTLHDQGTTQWADLSSQFYLREEDIGKNRAEVSQPRLAELNSYVPVTAYT 148
Cdd:cd01490     1 KVFLVGAGAIGCELLKNFALMGVGTgesgeITVTDMDNIEKSNLNRQFLFRPHDVGKPKSEVAAAAVKAMNPDLKITALQ 80

                          90       100
                  ....*....|....*....|...
gi 209862989  149 ---GPLVE-----DFLSSFQVVV 163
Cdd:cd01490    81 nrvGPETEhifndEFWEKLDGVA 103
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 56-148 8.74e-05

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 46.03  E-value: 8.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989   56 SRQLYV--LGHEAMKMLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTTQWADLSSQFYLREEDIGKNRAEVSQP 133
Cdd:PRK05600   23 ARQLALpgFGIEQQERLHNARVLVIGAGGLGCPAMQSLASAGVGTITLIDDDTVDVSNIHRQILFGASDVGRPKVEVAAE 102

                          90
                  ....*....|....*
gi 209862989  134 RLAELNSYVPVTAYT 148
Cdd:PRK05600  103 RLKEIQPDIRVNALR 117
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 55-147 2.30e-04

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 44.72  E-value: 2.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989   55 YSRQLYV--LGHEAMKMLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTTQWADLSSQFYLREEDIG--KNRAEV 130
Cdd:PRK12475    5 YSRQILFsgIGEEGQRKIREKHVLIVGAGALGAANAEALVRAGIGKLTIADRDYVEWSNLQRQQLYTEEDAKqkKPKAIA 84

                          90
                  ....*....|....*..
gi 209862989  131 SQPRLAELNSYVPVTAY 147
Cdd:PRK12475   85 AKEHLRKINSEVEIVPV 101
PRK14852 PRK14852
hypothetical protein; Provisional
 463-612 7.52e-04

hypothetical protein; Provisional


Pssm-ID: 184854 [Multi-domain]  Cd Length: 989  Bit Score: 43.53  E-value: 7.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989  463 QEKLSKQKYFLVGAGAIGCELLKNFAMIGLGcgeggEVVVTDMDTIEKSNLNRQFLFRPWDVTKLKSDTAAAAVRQMNPY 542
Cdd:PRK14852  327 QRRLLRSRVAIAGLGGVGGIHLMTLARTGIG-----NFNLADFDAYSPVNLNRQYGASIASFGRGKLDVMTERALSVNPF 401

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 209862989  543 IQVTSHQNRVGPDTeriyDDDFFQNLDGVANALD--NIDARMYMDRRCVYYRKPLLESGTLGTKGNVQVVIP 612
Cdd:PRK14852  402 LDIRSFPEGVAAET----IDAFLKDVDLLVDGIDffALDIRRRLFNRALELGIPVITAGPLGYSCALLVFMP 469
E1_ThiF_like cd01487
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ...
 74-146 1.04e-03

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: 41.21  E-value: 1.04e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 209862989   74 SVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTTQWADLSSQFYlREEDIGKNRAEVSQPRLAELNSYVPVTA 146
Cdd:cd01487     1 KVGIAGAGGLGSNIAVLLARSGVGNLKLVDFDVVEPSNLNRQQY-FLSQIGEPKVEALKENLREINPFVKIEA 72
Apg7 cd01486
Apg7 is an E1-like protein, that activates two different ubiquitin-like proteins, Apg12 and ...
 470-548 1.39e-03

Apg7 is an E1-like protein, that activates two different ubiquitin-like proteins, Apg12 and Apg8, and assigns them to specific E2 enzymes, Apg10 and Apg3, respectively. This leads to the covalent conjugation of Apg8 with phosphatidylethanolamine, an important step in autophagy. Autophagy is a dynamic membrane phenomenon for bulk protein degradation in the lysosome/vacuole.


Pssm-ID: 238763 [Multi-domain]  Cd Length: 307  Bit Score: 41.98  E-value: 1.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989  470 KYFLVGAGAIGCellkNFAMIGLGCGEgGEVVVTDMDTIEKSNLNRQFLFRPWDVT--KLKSDTAAAAVRQMNPYIQVTS 547
Cdd:cd01486     1 KCLLLGAGTLGC----NVARNLLGWGV-RHITFVDSGKVSYSNPVRQSLFTFEDCKggKPKAEAAAERLKEIFPSIDATG 75


                  .
gi 209862989  548 H 548
Cdd:cd01486    76 I 76
PRK07877 PRK07877
Rv1355c family protein;
463-579 1.67e-03

Rv1355c family protein;


Pssm-ID: 236122 [Multi-domain]  Cd Length: 722  Bit Score: 42.28  E-value: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989  463 QEKLSKQKYFLVGAgAIGCELLKNFAMIGLGcgegGEVVVTDMDTIEKSNLNRQflfrPWDVTKL---KSDTAAAAVRQM 539
Cdd:PRK07877  102 QERLGRLRIGVVGL-SVGHAIAHTLAAEGLC----GELRLADFDTLELSNLNRV----PAGVFDLgvnKAVVAARRIAEL 172

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 209862989  540 NPYIQVTSHQNRVGPDTEriydDDFFQNLDGVANALDNID 579
Cdd:PRK07877  173 DPYLPVEVFTDGLTEDNV----DAFLDGLDVVVEECDSLD 208
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
48-163 4.54e-03

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 40.77  E-value: 4.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989   48 ADIDESLYSRQLYV--LGHEAMKMLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTTQWADLSSQFYLREEDIGK 125
Cdd:PRK08762  109 TDEQDERYSRHLRLpeVGEEGQRRLLEARVLLIGAGGLGSPAALYLAAAGVGTLGIVDHDVVDRSNLQRQILHTEDRVGQ 188

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 209862989  126 NRAEVSQPRLAELNSYVPVTAY----TGPLVEDFLSSFQVVV 163
Cdd:PRK08762  189 PKVDSAAQRLAALNPDVQVEAVqervTSDNVEALLQDVDVVV 230
E1_like_apg7 TIGR01381
E1-like protein-activating enzyme Gsa7p/Apg7p; This model represents a family of eukaryotic ...
 464-548 4.92e-03

E1-like protein-activating enzyme Gsa7p/Apg7p; This model represents a family of eukaryotic proteins found in animals, plants, and yeasts, including Apg7p (YHR171W) from Saccharomyces cerevisiae and GSA7 from Pichia pastoris. Members are about 650 to 700 residues in length and include a central domain of about 150 residues shared with the ThiF/MoeB/HesA family of proteins. A low level of similarity to ubiquitin-activating enzyme E1 is described in a paper on peroxisome autophagy mediated by GSA7, and is the basis of the name ubiquitin activating enzyme E1-like protein. Members of the family appear to be involved in protein lipidation events analogous to ubiquitination and required for membrane fusion events during autophagy.


Pssm-ID: 273590 [Multi-domain]  Cd Length: 664  Bit Score: 40.69  E-value: 4.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989   464 EKLSKQKYFLVGAGAIGCELLKnfAMIGLGCgegGEVVVTDMDTIEKSNLNRQFLFRPWDV---TKLKSDTAAAAVRQMN 540
Cdd:TIGR01381  334 ERYSQLKVLLLGAGTLGCNVAR--CLIGWGV---RHITFVDNGKVSYSNPVRQSLSNFEDCllgGRGKAETAQKALKRIF 408


                   ....*...
gi 209862989   541 PYIQVTSH 548
Cdd:TIGR01381  409 PSIQATGH 416
PRK07877 PRK07877
Rv1355c family protein;
122-195 6.86e-03

Rv1355c family protein;


Pssm-ID: 236122 [Multi-domain]  Cd Length: 722  Bit Score: 40.36  E-value: 6.86e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 209862989  122 DIGKNRAEVSQPRLAELNSYVPVTAYTGPL----VEDFLSSFQVVVLTNSPLEAQLRVGEFCHSRGIKLVVA-DTRGLF 195
Cdd:PRK07877  156 DLGVNKAVVAARRIAELDPYLPVEVFTDGLtednVDAFLDGLDVVVEECDSLDVKVLLREAARARRIPVLMAtSDRGLL 234
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 55-144 7.46e-03

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 40.08  E-value: 7.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862989   55 YSRQLYV--LGHEAMKMLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTTQWADLSSQFYLREEDIGKNRAEVSQ 132
Cdd:PRK07878   23 YSRHLIIpdVGVDGQKRLKNARVLVIGAGGLGSPTLLYLAAAGVGTLGIVEFDVVDESNLQRQVIHGQSDVGRSKAQSAR 102

                          90
                  ....*....|..
gi 209862989  133 PRLAELNSYVPV 144
Cdd:PRK07878  103 DSIVEINPLVNV 114
 
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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