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Conserved domains on  [gi|768033354|ref|XP_011542256|]
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ubiquitin-like modifier-activating enzyme 1 isoform X4 [Homo sapiens]

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 ...
 63-1069 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: 1325.28  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354    63 DIDEGLYSRQLYVLGHEAMKRLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREEDIGKNRA 142
Cdd:TIGR01408    1 EIDEALYSRQLYVLGDEAMQKMAKSNVLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLSSNFFLSEDDVGRNRA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354   143 EVSQPRLAELNSYVPVTAYTGPLVEDFLSGFQVVVLTNTPLEDQLRVGEFCHNR--GIKLVVADTRGLFGQLFCDFGEEM 220
Cdd:TIGR01408   81 EAVVKKLAELNPYVHVSSSSVPFNEEFLDKFQCVVLTEMSLPLQKEINDFCHSQcpPIAFISADVRGLFGSLFCDFGDEF 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354   221 ILTDSNGEQPLSAMVSMVTKDNPGVVTCLDEARHGFESGDFVSFSEVQGMVELNGNQPMEIKVLGPYTFSICDTSNFSDY 300
Cdd:TIGR01408  161 EVLDTDGEEPKTGFIASITQANPGIVTCLENHRHKLETGDFVTFREVNGMTGLNDGSPRKITVISPYSFSIGDTTELGPY 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354   301 IRGGIVSQVKVPKKISFKSLVASLAEPDFVVTDFAKFSRPAQLHIGFQALHQFCAQHGRPPRPRNEEDAAELVALAQAVN 380
Cdd:TIGR01408  241 LHGGIATQVKTPKTVFFKSLREQLKDPKCLIVDFSKPERPPEIHTAFQALDQFQEKYSRKPNVGCQQDAEELLKLATSIS 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354   381 ARALPAVQqnNLDEDLIRKLAYVAAGDLAPINAFIGGLAAQEVMKACSGKFMPIMQWLYFDALECLPEDKEVLTEDkCLQ 460
Cdd:TIGR01408  321 ETLEEKVP--DVDAKLVHWLSWTAQGFLSPMAAAVGGVVSQEVLKAVTGKFSPLCQWFYFDSAESLPSLGKPECEE-FLP 397

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354   461 RQNRYDGQVAVFGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGCGEGGEIIVTDMDTIEKSNLNRQFLFRPWDVTK 540
Cdd:TIGR01408  398 RGDRYDAQIAVFGDTFQQKLQNLNIFLVGCGAIGCEMLKNFALMGVGTGKKGMITVTDPDLIEKSNLNRQFLFRPHHIGK 477

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354   541 LKSDTAAAAVRQMNPHIRVTSHQNRVGPDTERIYDDDFFQNLDGVANALDNVDARMYMDRRCVYYRKPLLESGTLGTKGN 620
Cdd:TIGR01408  478 PKSYTAADATLKINPQIKIDAHQNRVGPETETIFNDEFYEKLDVVINALDNVEARRYVDSRCLAFLKPLLESGTLGTKGN 557

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354   621 VQVVIPFLTESYSSSQDPPEKSIPICTLKNFPNAIEHTLQWARDEFEGLFKQPAENVNQYLTDP-KFVERTLRLAGTQPL 699
Cdd:TIGR01408  558 TQVVVPHLTESYGSSRDPPEKEIPFCTLKSFPAAIEHTIQWARDKFEGLFSHKPSLVNKYLSSPsSAEEVLQKIQSGHSR 637

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354   700 EVLEAVQRSLVLQRPQTWADCVTWACHHWHTQYSNNIRQLLHNFPPDQLTSSGAPFWSGPKRCPHPLTFDVNNPLHLDYV 779
Cdd:TIGR01408  638 EGLEQIIKLLSKEKPRNFSQCVEWARLKFEKYFNNKALQLLHCFPLDIRTSTGSPFWSSPKRPPSPLKFDLNEPLHLSFI 717

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354   780 MAAANLFAQTYGLTGSQ---DRAAVATFLQSVQVPEFTPKSGVKIHVSDQELQSANASVDDSR-LEELKATLPSPDKLPG 855
Cdd:TIGR01408  718 QAAAKLYATVYGIPFAEedlSADALLNILSEVKIPEFKPRSNKKIQTDETARKPDTAPIDDRNaIFQLEKAILSNEATKS 797

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354   856 -FKMYPIDFEKDDDSNFHMDFIVAASNLRAENYDIPSADRHKSKLIAGKIIPAIATTTAAVVGLVCLELYKVVQGHRQLD 934
Cdd:TIGR01408  798 dFRMAPLSFEKDDDHNGHIDFITAASNLRAKNYSIEPADRFKTKFIAGKIIPAIATSTATVSGLVCLELIKVTDGGYKFE 877

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354   935 SYKNGFLNLALPFFGFSEPLAAPRHQYYNQEW-TLWDRFEVQGlqpngeEMTLKQFLDYFKTEHKLEITMLSQGVSMLYS 1013
Cdd:TIGR01408  878 VYKNCFLNLAIPLFVFTEPTEVRKTKIRNGISfTIWDRWTLHG------DFTLLEFINAVKEKYGLEPTMVSQGVKLLYV 951

                          970       980       990      1000      1010
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 768033354  1014 FFMPaaKLKERLDQPMTEIVSRVSKRKLGRHVRALVLELCCNDESGEDVEVPYVRY 1069
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 ...
 63-1069 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: 1325.28  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354    63 DIDEGLYSRQLYVLGHEAMKRLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREEDIGKNRA 142
Cdd:TIGR01408    1 EIDEALYSRQLYVLGDEAMQKMAKSNVLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLSSNFFLSEDDVGRNRA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354   143 EVSQPRLAELNSYVPVTAYTGPLVEDFLSGFQVVVLTNTPLEDQLRVGEFCHNR--GIKLVVADTRGLFGQLFCDFGEEM 220
Cdd:TIGR01408   81 EAVVKKLAELNPYVHVSSSSVPFNEEFLDKFQCVVLTEMSLPLQKEINDFCHSQcpPIAFISADVRGLFGSLFCDFGDEF 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354   221 ILTDSNGEQPLSAMVSMVTKDNPGVVTCLDEARHGFESGDFVSFSEVQGMVELNGNQPMEIKVLGPYTFSICDTSNFSDY 300
Cdd:TIGR01408  161 EVLDTDGEEPKTGFIASITQANPGIVTCLENHRHKLETGDFVTFREVNGMTGLNDGSPRKITVISPYSFSIGDTTELGPY 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354   301 IRGGIVSQVKVPKKISFKSLVASLAEPDFVVTDFAKFSRPAQLHIGFQALHQFCAQHGRPPRPRNEEDAAELVALAQAVN 380
Cdd:TIGR01408  241 LHGGIATQVKTPKTVFFKSLREQLKDPKCLIVDFSKPERPPEIHTAFQALDQFQEKYSRKPNVGCQQDAEELLKLATSIS 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354   381 ARALPAVQqnNLDEDLIRKLAYVAAGDLAPINAFIGGLAAQEVMKACSGKFMPIMQWLYFDALECLPEDKEVLTEDkCLQ 460
Cdd:TIGR01408  321 ETLEEKVP--DVDAKLVHWLSWTAQGFLSPMAAAVGGVVSQEVLKAVTGKFSPLCQWFYFDSAESLPSLGKPECEE-FLP 397

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354   461 RQNRYDGQVAVFGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGCGEGGEIIVTDMDTIEKSNLNRQFLFRPWDVTK 540
Cdd:TIGR01408  398 RGDRYDAQIAVFGDTFQQKLQNLNIFLVGCGAIGCEMLKNFALMGVGTGKKGMITVTDPDLIEKSNLNRQFLFRPHHIGK 477

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354   541 LKSDTAAAAVRQMNPHIRVTSHQNRVGPDTERIYDDDFFQNLDGVANALDNVDARMYMDRRCVYYRKPLLESGTLGTKGN 620
Cdd:TIGR01408  478 PKSYTAADATLKINPQIKIDAHQNRVGPETETIFNDEFYEKLDVVINALDNVEARRYVDSRCLAFLKPLLESGTLGTKGN 557

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354   621 VQVVIPFLTESYSSSQDPPEKSIPICTLKNFPNAIEHTLQWARDEFEGLFKQPAENVNQYLTDP-KFVERTLRLAGTQPL 699
Cdd:TIGR01408  558 TQVVVPHLTESYGSSRDPPEKEIPFCTLKSFPAAIEHTIQWARDKFEGLFSHKPSLVNKYLSSPsSAEEVLQKIQSGHSR 637

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354   700 EVLEAVQRSLVLQRPQTWADCVTWACHHWHTQYSNNIRQLLHNFPPDQLTSSGAPFWSGPKRCPHPLTFDVNNPLHLDYV 779
Cdd:TIGR01408  638 EGLEQIIKLLSKEKPRNFSQCVEWARLKFEKYFNNKALQLLHCFPLDIRTSTGSPFWSSPKRPPSPLKFDLNEPLHLSFI 717

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354   780 MAAANLFAQTYGLTGSQ---DRAAVATFLQSVQVPEFTPKSGVKIHVSDQELQSANASVDDSR-LEELKATLPSPDKLPG 855
Cdd:TIGR01408  718 QAAAKLYATVYGIPFAEedlSADALLNILSEVKIPEFKPRSNKKIQTDETARKPDTAPIDDRNaIFQLEKAILSNEATKS 797

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354   856 -FKMYPIDFEKDDDSNFHMDFIVAASNLRAENYDIPSADRHKSKLIAGKIIPAIATTTAAVVGLVCLELYKVVQGHRQLD 934
Cdd:TIGR01408  798 dFRMAPLSFEKDDDHNGHIDFITAASNLRAKNYSIEPADRFKTKFIAGKIIPAIATSTATVSGLVCLELIKVTDGGYKFE 877

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354   935 SYKNGFLNLALPFFGFSEPLAAPRHQYYNQEW-TLWDRFEVQGlqpngeEMTLKQFLDYFKTEHKLEITMLSQGVSMLYS 1013
Cdd:TIGR01408  878 VYKNCFLNLAIPLFVFTEPTEVRKTKIRNGISfTIWDRWTLHG------DFTLLEFINAVKEKYGLEPTMVSQGVKLLYV 951

                          970       980       990      1000      1010
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 768033354  1014 FFMPaaKLKERLDQPMTEIVSRVSKRKLGRHVRALVLELCCNDESGEDVEVPYVRY 1069
Cdd:TIGR01408  952 PVMP--GHAERLKLKMHKLVKPTTKKKLPPYRVHLTVSFACDDDGDEDVPGPPVRI 1005
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
 484-1025 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: 884.32  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354  484 KYFLVGAGAIGCELLKNFAMIGLGCGEGGEIIVTDMDTIEKSNLNRQFLFRPWDVTKLKSDTAAAAVRQMNPHIRVTSHQ 563
Cdd:cd01490     1 KVFLVGAGAIGCELLKNFALMGVGTGESGEITVTDMDNIEKSNLNRQFLFRPHDVGKPKSEVAAAAVKAMNPDLKITALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354  564 NRVGPDTERIYDDDFFQNLDGVANALDNVDARMYMDRRCVYYRKPLLESGTLGTKGNVQVVIPFLTESYSSSQDPPEKSI 643
Cdd:cd01490    81 NRVGPETEHIFNDEFWEKLDGVANALDNVDARMYVDRRCVYYRKPLLESGTLGTKGNTQVVIPHLTESYSSSRDPPEKSI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354  644 PICTLKNFPNAIEHTLQWARDEFEGLFKQPAENVNQYLtdpkfvertlrlagtqplevleavqrslvlqrpqtWADCVTW 723
Cdd:cd01490   161 PLCTLKNFPNAIEHTIQWARDEFEGLFKQPPENVNQYL-----------------------------------FEDCVRW 205

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354  724 ACHHWHTQYSNNIRQLLHNFPPDQLTSSGAPFWSGPKRCPHPLTFDVNNPLHLDYVMAAANLFAQTYGLTGsqdraavat 803
Cdd:cd01490   206 ARLLFEKYFNNNIKQLLHNFPPDAVTSDGAPFWSGPKRCPTPLEFDVNNPLHLDFVLAAANLYAEVYGIPG--------- 276

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354  804 flqsvqvpeftpksgvkihvsdqelqsanasvddsrleelkatlpspdklpgfkmypidFEKDDDSNFHMDFIVAASNLR 883
Cdd:cd01490   277 -----------------------------------------------------------FEKDDDTNFHMDFITAASNLR 297

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354  884 AENYDIPSADRHKSKLIAGKIIPAIATTTAAVVGLVCLELYKVVQGHRQLDSYKNGFLNLALPFFGFSEPLAAPRHQY-Y 962
Cdd:cd01490   298 ARNYSIPPADRHKTKRIAGKIIPAIATTTAAVTGLVCLELYKVVDGKRPLEAYKNAFLNLALPFFAFSEPIPAPKVKYaY 377

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768033354  963 NQEWTLWDRFEVQGLQPNGEEMTlkqflDYFKTEHKLEITMLSQGVSMLYSFFMPAAKLKERL 1025
Cdd:cd01490   378 DEEWTIWDRFEVKGKQTLQELLI-----DYFKEKYGLEVTMLSQGVSMLYSSFMPPAKLKERL 435
UBA_E1_SCCH pfam10585
Ubiquitin-activating enzyme, SCCH domain; Ubiquitin-activating enzyme (E1 enzyme) activates ...
 652-898 1.14e-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: 1.14e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354   652 PNAIEHTLQWARDEFEGLFKQPAENVNQYLTDP-KFVERTLRLAGTQPLEVLEAVQRSLVLQRPQTWADCVTWACHHWHT 730
Cdd:pfam10585    1 PNAIEHTIQWARDEFEGLFVQPPEEVNKYLQPPqNFIESLLKQGGGQKLETLESVRKSLVTERPKTFEDCVAWARLKFEK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354   731 QYSNNIRQLLHNFPPDQLTSSGAPFWSGPKRCPHPLTFDVNNPLHLDYVMAAANLFAQTYGLTGSQDRAAVATFLQSVQV 810
Cdd:pfam10585   81 LFNNDIKQLLYNFPPDHKTSSGAPFWSGPKRPPTPLEFDPNNPLHLDFVVAAANLRAQVYGIPGSRDREAIAKVLSKVKV 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354   811 PEFTPKSGVKIHVSDQELQSANASV--DDSRLEELKATLP----SPDKLPGFKMYPIDFEKDDDSNFHMDFIVAASNLRA 884
Cdd:pfam10585  161 PEFKPKSGVKIQVNDEEAADPNAESedDEDELDELLEELPklavSPSSLAGFRLNPIEFEKDDDTNFHIDFITAASNLRA 240

                          250
                   ....*....|....
gi 768033354   885 ENYDIPSADRHKSK 898
Cdd:pfam10585  241 RNYGIPPADRHKTK 254
UBA_e1_C smart00985
Ubiquitin-activating enzyme e1 C-terminal domain; This presumed domain found at the C terminus ...
 936-1067 4.79e-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: 4.79e-69
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354    936 YKNGFLNLALPFFGFSEPLAAPRHQYYNQ-EWTLWDRFEVQGLqpngeEMTLKQFLDYFKTEHKLEITMLSQGVSMLYSF 1014
Cdd:smart00985    1 YKNAFLNLALPFFAFSEPIAAPKTKYRDKdKWTLWDRLEVPGG-----DITLKELLDYFEEKYGLEVTMLSQGVSLLYSS 75

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|...
gi 768033354   1015 FMPAAKLKERLDQPMTEIVSRVSKRKLGRHVRALVLELCCNDESGEDVEVPYV 1067
Cdd:smart00985   76 FMPPKKHKERLDLPVTELVEQVTKKKLPPHVKYLVLEVSCEDEDDEDVEVPYI 128
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 464-626 1.32e-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: 129.86  E-value: 1.32e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354  464 RYDGQVAV--FGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGcgeggEIIVTDMDTIEKSNLNRQFLFRPWDVTKL 541
Cdd:COG0476     7 RYSRQILLpeIGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVG-----TLTLVDDDVVELSNLQRQILYTEADVGRP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354  542 KSDTAAAAVRQMNPHIRVTSHQNRVGPDTEriydDDFFQNLDGVANALDNVDARMYMDRRCVYYRKPLLESGTLGTKGNV 621
Cdd:COG0476    82 KVEAAAERLRALNPDVEVEAIPERLTEENA----LELLAGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIGFEGQV 157


                  ....*
gi 768033354  622 QVVIP 626
Cdd:COG0476   158 TVFIP 162
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 464-609 6.89e-19

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 87.21  E-value: 6.89e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354  464 RYDGQVAV--FGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGcgeggEIIVTDMDTIEKSNLNRQFLFRPWDVTKL 541
Cdd:PRK05690   12 RYNRQIILrgFDFDGQEKLKAARVLVVGLGGLGCAASQYLAAAGVG-----TLTLVDFDTVSLSNLQRQVLHDDATIGQP 86

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768033354  542 KSDTAAAAVRQMNPHIRVTSHQNRVGPDTEriydDDFFQNLDGVANALDNVDARMYMDRRCVYYRKPL 609
Cdd:PRK05690   87 KVESARAALARINPHIAIETINARLDDDEL----AALIAGHDLVLDCTDNVATRNQLNRACFAAKKPL 150
 
Name Accession Description Interval E-value
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 63-1069 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: 1325.28  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354    63 DIDEGLYSRQLYVLGHEAMKRLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREEDIGKNRA 142
Cdd:TIGR01408    1 EIDEALYSRQLYVLGDEAMQKMAKSNVLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLSSNFFLSEDDVGRNRA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354   143 EVSQPRLAELNSYVPVTAYTGPLVEDFLSGFQVVVLTNTPLEDQLRVGEFCHNR--GIKLVVADTRGLFGQLFCDFGEEM 220
Cdd:TIGR01408   81 EAVVKKLAELNPYVHVSSSSVPFNEEFLDKFQCVVLTEMSLPLQKEINDFCHSQcpPIAFISADVRGLFGSLFCDFGDEF 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354   221 ILTDSNGEQPLSAMVSMVTKDNPGVVTCLDEARHGFESGDFVSFSEVQGMVELNGNQPMEIKVLGPYTFSICDTSNFSDY 300
Cdd:TIGR01408  161 EVLDTDGEEPKTGFIASITQANPGIVTCLENHRHKLETGDFVTFREVNGMTGLNDGSPRKITVISPYSFSIGDTTELGPY 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354   301 IRGGIVSQVKVPKKISFKSLVASLAEPDFVVTDFAKFSRPAQLHIGFQALHQFCAQHGRPPRPRNEEDAAELVALAQAVN 380
Cdd:TIGR01408  241 LHGGIATQVKTPKTVFFKSLREQLKDPKCLIVDFSKPERPPEIHTAFQALDQFQEKYSRKPNVGCQQDAEELLKLATSIS 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354   381 ARALPAVQqnNLDEDLIRKLAYVAAGDLAPINAFIGGLAAQEVMKACSGKFMPIMQWLYFDALECLPEDKEVLTEDkCLQ 460
Cdd:TIGR01408  321 ETLEEKVP--DVDAKLVHWLSWTAQGFLSPMAAAVGGVVSQEVLKAVTGKFSPLCQWFYFDSAESLPSLGKPECEE-FLP 397

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354   461 RQNRYDGQVAVFGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGCGEGGEIIVTDMDTIEKSNLNRQFLFRPWDVTK 540
Cdd:TIGR01408  398 RGDRYDAQIAVFGDTFQQKLQNLNIFLVGCGAIGCEMLKNFALMGVGTGKKGMITVTDPDLIEKSNLNRQFLFRPHHIGK 477

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354   541 LKSDTAAAAVRQMNPHIRVTSHQNRVGPDTERIYDDDFFQNLDGVANALDNVDARMYMDRRCVYYRKPLLESGTLGTKGN 620
Cdd:TIGR01408  478 PKSYTAADATLKINPQIKIDAHQNRVGPETETIFNDEFYEKLDVVINALDNVEARRYVDSRCLAFLKPLLESGTLGTKGN 557

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354   621 VQVVIPFLTESYSSSQDPPEKSIPICTLKNFPNAIEHTLQWARDEFEGLFKQPAENVNQYLTDP-KFVERTLRLAGTQPL 699
Cdd:TIGR01408  558 TQVVVPHLTESYGSSRDPPEKEIPFCTLKSFPAAIEHTIQWARDKFEGLFSHKPSLVNKYLSSPsSAEEVLQKIQSGHSR 637

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354   700 EVLEAVQRSLVLQRPQTWADCVTWACHHWHTQYSNNIRQLLHNFPPDQLTSSGAPFWSGPKRCPHPLTFDVNNPLHLDYV 779
Cdd:TIGR01408  638 EGLEQIIKLLSKEKPRNFSQCVEWARLKFEKYFNNKALQLLHCFPLDIRTSTGSPFWSSPKRPPSPLKFDLNEPLHLSFI 717

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354   780 MAAANLFAQTYGLTGSQ---DRAAVATFLQSVQVPEFTPKSGVKIHVSDQELQSANASVDDSR-LEELKATLPSPDKLPG 855
Cdd:TIGR01408  718 QAAAKLYATVYGIPFAEedlSADALLNILSEVKIPEFKPRSNKKIQTDETARKPDTAPIDDRNaIFQLEKAILSNEATKS 797

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354   856 -FKMYPIDFEKDDDSNFHMDFIVAASNLRAENYDIPSADRHKSKLIAGKIIPAIATTTAAVVGLVCLELYKVVQGHRQLD 934
Cdd:TIGR01408  798 dFRMAPLSFEKDDDHNGHIDFITAASNLRAKNYSIEPADRFKTKFIAGKIIPAIATSTATVSGLVCLELIKVTDGGYKFE 877

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354   935 SYKNGFLNLALPFFGFSEPLAAPRHQYYNQEW-TLWDRFEVQGlqpngeEMTLKQFLDYFKTEHKLEITMLSQGVSMLYS 1013
Cdd:TIGR01408  878 VYKNCFLNLAIPLFVFTEPTEVRKTKIRNGISfTIWDRWTLHG------DFTLLEFINAVKEKYGLEPTMVSQGVKLLYV 951

                          970       980       990      1000      1010
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 768033354  1014 FFMPaaKLKERLDQPMTEIVSRVSKRKLGRHVRALVLELCCNDESGEDVEVPYVRY 1069
Cdd:TIGR01408  952 PVMP--GHAERLKLKMHKLVKPTTKKKLPPYRVHLTVSFACDDDGDEDVPGPPVRI 1005
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
 484-1025 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: 884.32  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354  484 KYFLVGAGAIGCELLKNFAMIGLGCGEGGEIIVTDMDTIEKSNLNRQFLFRPWDVTKLKSDTAAAAVRQMNPHIRVTSHQ 563
Cdd:cd01490     1 KVFLVGAGAIGCELLKNFALMGVGTGESGEITVTDMDNIEKSNLNRQFLFRPHDVGKPKSEVAAAAVKAMNPDLKITALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354  564 NRVGPDTERIYDDDFFQNLDGVANALDNVDARMYMDRRCVYYRKPLLESGTLGTKGNVQVVIPFLTESYSSSQDPPEKSI 643
Cdd:cd01490    81 NRVGPETEHIFNDEFWEKLDGVANALDNVDARMYVDRRCVYYRKPLLESGTLGTKGNTQVVIPHLTESYSSSRDPPEKSI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354  644 PICTLKNFPNAIEHTLQWARDEFEGLFKQPAENVNQYLtdpkfvertlrlagtqplevleavqrslvlqrpqtWADCVTW 723
Cdd:cd01490   161 PLCTLKNFPNAIEHTIQWARDEFEGLFKQPPENVNQYL-----------------------------------FEDCVRW 205

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354  724 ACHHWHTQYSNNIRQLLHNFPPDQLTSSGAPFWSGPKRCPHPLTFDVNNPLHLDYVMAAANLFAQTYGLTGsqdraavat 803
Cdd:cd01490   206 ARLLFEKYFNNNIKQLLHNFPPDAVTSDGAPFWSGPKRCPTPLEFDVNNPLHLDFVLAAANLYAEVYGIPG--------- 276

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354  804 flqsvqvpeftpksgvkihvsdqelqsanasvddsrleelkatlpspdklpgfkmypidFEKDDDSNFHMDFIVAASNLR 883
Cdd:cd01490   277 -----------------------------------------------------------FEKDDDTNFHMDFITAASNLR 297

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354  884 AENYDIPSADRHKSKLIAGKIIPAIATTTAAVVGLVCLELYKVVQGHRQLDSYKNGFLNLALPFFGFSEPLAAPRHQY-Y 962
Cdd:cd01490   298 ARNYSIPPADRHKTKRIAGKIIPAIATTTAAVTGLVCLELYKVVDGKRPLEAYKNAFLNLALPFFAFSEPIPAPKVKYaY 377

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768033354  963 NQEWTLWDRFEVQGLQPNGEEMTlkqflDYFKTEHKLEITMLSQGVSMLYSFFMPAAKLKERL 1025
Cdd:cd01490   378 DEEWTIWDRFEVKGKQTLQELLI-----DYFKEKYGLEVTMLSQGVSMLYSSFMPPAKLKERL 435
Ube1_repeat1 cd01491
Ubiquitin activating enzyme (E1), repeat 1. E1, a highly conserved small protein present ...
 68-450 5.90e-180

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: 525.68  E-value: 5.90e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354   68 LYSRQLYVLGHEAMKRLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREEDIGKNRAEVSQP 147
Cdd:cd01491     1 LYSRQLYVLGHEAMKKLQKSNVLISGLGGLGVEIAKNLILAGVKSVTLHDTKPCSWSDLSSQFYLREEDIGKNRAEASQA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354  148 RLAELNSYVPVTAYTGPLVEDFLSGFQVVVLTNTPLEDQLRVGEFCHNRGIKLVVADTRGLFGQLFCDFGEEMILTDSNG 227
Cdd:cd01491    81 RLAELNPYVPVTVSTGPLTTDELLKFQVVVLTDASLEDQLKINEFCHSPGIKFISADTRGLFGSIFCDFGDEFTVYDPNG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354  228 EQPLSAMVSMVTKDNPGVVTCLDEARHGFESGDFVSFSEVQGMVELNGNQPMEIKVLGPYTFSICDTSNFSDYIRGGIVS 307
Cdd:cd01491   161 EEPKSGMISSISKDNPGVVTCLDETRHGFEDGDYVTFSEVEGMTELNGCEPRKIKVKGPYTFSIGDTSSFSEYIRGGIVT 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354  308 QVKvpkkisfkslvaslaepdfvvtdfakfsrpaqlhigfqalhqfcaqhgrpprprneedaaelvalaqavnaralpav 387
Cdd:cd01491   241 QVK----------------------------------------------------------------------------- 243

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768033354  388 qqnnldedlirklayvaagdLAPINAFIGGLAAQEVMKACSGKFMPIMQWLYFDALECLPEDK 450
Cdd:cd01491   244 --------------------LSPMAAFFGGLAAQEVLKACSGKFTPLKQWLYFDALECLPEDE 286
UBA_E1_SCCH pfam10585
Ubiquitin-activating enzyme, SCCH domain; Ubiquitin-activating enzyme (E1 enzyme) activates ...
 652-898 1.14e-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: 1.14e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354   652 PNAIEHTLQWARDEFEGLFKQPAENVNQYLTDP-KFVERTLRLAGTQPLEVLEAVQRSLVLQRPQTWADCVTWACHHWHT 730
Cdd:pfam10585    1 PNAIEHTIQWARDEFEGLFVQPPEEVNKYLQPPqNFIESLLKQGGGQKLETLESVRKSLVTERPKTFEDCVAWARLKFEK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354   731 QYSNNIRQLLHNFPPDQLTSSGAPFWSGPKRCPHPLTFDVNNPLHLDYVMAAANLFAQTYGLTGSQDRAAVATFLQSVQV 810
Cdd:pfam10585   81 LFNNDIKQLLYNFPPDHKTSSGAPFWSGPKRPPTPLEFDPNNPLHLDFVVAAANLRAQVYGIPGSRDREAIAKVLSKVKV 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354   811 PEFTPKSGVKIHVSDQELQSANASV--DDSRLEELKATLP----SPDKLPGFKMYPIDFEKDDDSNFHMDFIVAASNLRA 884
Cdd:pfam10585  161 PEFKPKSGVKIQVNDEEAADPNAESedDEDELDELLEELPklavSPSSLAGFRLNPIEFEKDDDTNFHIDFITAASNLRA 240

                          250
                   ....*....|....
gi 768033354   885 ENYDIPSADRHKSK 898
Cdd:pfam10585  241 RNYGIPPADRHKTK 254
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
 484-667 6.42e-79

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: 257.89  E-value: 6.42e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354  484 KYFLVGAGAIGCELLKNFAMIGLGcgeggEIIVTDMDTIEKSNLNRQFLFRPWDVTKLKSDTAAAAVRQMNPHIRVTSHQ 563
Cdd:cd01484     1 KVLLVGAGGIGCELLKNLALMGFG-----QIHVIDMDTIDVSNLNRQFLFRPKDIGRPKSEVAAEAVNDRNPNCKVVPYQ 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354  564 NRVGPdtERIYDDDFFQNLDGVANALDNVDARMYMDRRCVYYRKPLLESGTLGTKGNVQVVIPFLTESYSSSQDPPEKSI 643
Cdd:cd01484    76 NKVGP--EQDFNDTFFEQFHIIVNALDNIIARRYVNGMLIFLIVPLIESGTEGFKGNAQVILPGMTECIECTLYPPQKNF 153

                         170       180
                  ....*....|....*....|....
gi 768033354  644 PICTLKNFPNAIEHTLQWARDEFE 667
Cdd:cd01484   154 PMCTIASMPRLPEHCIEWARMLQW 177
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 465-651 2.57e-69

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: 231.38  E-value: 2.57e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354   465 YDGQVA--VFGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGcgeggEIIVTDMDTIEKSNLNRQFLFRPWDVTKLK 542
Cdd:pfam00899    1 YSRQLAlpLIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVG-----KITLVDFDTVELSNLNRQFLFREADIGKPK 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354   543 SDTAAAAVRQMNPHIRVTSHQNRVGPDTeriyDDDFFQNLDGVANALDNVDARMYMDRRCVYYRKPLLESGTLGTKGNVQ 622
Cdd:pfam00899   76 AEVAAERLREINPDVEVEAYTERLTPEN----AEELIKSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVT 151

                          170       180       190
                   ....*....|....*....|....*....|.
gi 768033354   623 VVIPFLTESYS--SSQDPPEKSIPICTLKNF 651
Cdd:pfam00899  152 VVIPGKTPCYRclFPEDPPPKLVPSCTVAGV 182
UBA_e1_C smart00985
Ubiquitin-activating enzyme e1 C-terminal domain; This presumed domain found at the C terminus ...
 936-1067 4.79e-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: 4.79e-69
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354    936 YKNGFLNLALPFFGFSEPLAAPRHQYYNQ-EWTLWDRFEVQGLqpngeEMTLKQFLDYFKTEHKLEITMLSQGVSMLYSF 1014
Cdd:smart00985    1 YKNAFLNLALPFFAFSEPIAAPKTKYRDKdKWTLWDRLEVPGG-----DITLKELLDYFEEKYGLEVTMLSQGVSLLYSS 75

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|...
gi 768033354   1015 FMPAAKLKERLDQPMTEIVSRVSKRKLGRHVRALVLELCCNDESGEDVEVPYV 1067
Cdd:smart00985   76 FMPPKKHKERLDLPVTELVEQVTKKKLPPHVKYLVLEVSCEDEDDEDVEVPYI 128
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 484-943 4.85e-58

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: 202.61  E-value: 4.85e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354  484 KYFLVGAGAIGCELLKNFAMIGLGcgeggEIIVTDMDTIEKSNLNRQFLFRPWDVTKLKSDTAAAAVRQMNPHIRVTSHQ 563
Cdd:cd01489     1 KVLVVGAGGIGCELLKNLVLTGFG-----EIHIIDLDTIDLSNLNRQFLFRKKHVGKSKAQVAKEAVLSFNPNVKIVAYH 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354  564 NRVgpdTERIYDDDFFQNLDGVANALDNVDARMYMDRRCVYYRKPLLESGTLGTKGNVQVVIPFLTESYSSSQDPPEKSI 643
Cdd:cd01489    76 ANI---KDPDFNVEFFKQFDLVFNALDNLAARRHVNKMCLAADVPLIESGTTGFLGQVQVIKKGKTECYECQPKETPKTF 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354  644 PICTLKNFPNAIEHTLQWARDE---FEGLFKQpaenvnqyltdpkfvertlrlagtqplevleavqrslvlqrpqtwadc 720
Cdd:cd01489   153 PVCTIRSTPSQPIHCIVWAKSLfflFNKVFKD------------------------------------------------ 184

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354  721 vtwachhwhtqysnNIRQLLHNfppDQLtssgapfWSGPKRcPHPLTFDvnnplhldyvmaaanlfaqtygltgsqdraa 800
Cdd:cd01489   185 --------------DIERLLSM---EEL-------WKTRKP-PVPLSWK------------------------------- 208

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354  801 vatflqsvqvpeftpksgvkihvsdqelqsanasvddsrleelkatlpspdklpgfkmyPIDFEKDDDSNfhMDFIVAAS 880
Cdd:cd01489   209 -----------------------------------------------------------ELTFDKDDQDA--LDFVAAAA 227

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768033354  881 NLRAENYDIPSADRHKSKLIAGKIIPAIATTTAAVVGLVCLELYKVVQGHrqLDSYKNGFLNL 943
Cdd:cd01489   228 NLRSHVFGIPMKSRFDIKQMAGNIIPAIATTNAIIAGLIVLEALKVLSGD--KEQCRTVFLNL 288
E1_UFD pfam09358
Ubiquitin fold domain; The ubiquitin fold domain is found at the C-terminus of ...
 969-1067 4.35e-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: 4.35e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354   969 WDRFEVQGlqpngeEMTLKQFLDYFKTEHKLEITMLSQGVSMLYSFFMPAAKLKERLDQPMTEIVSRVSKRKLGRHVRAL 1048
Cdd:pfam09358    1 WDRFEVEG------DMTLQELLDYFKEKYGLEVTMLSYGVSLLYSSFMPPKKHKERLPMKISELVEEVSKKPIPPHQKYL 74

                           90
                   ....*....|....*....
gi 768033354  1049 VLELCCNDESGEDVEVPYV 1067
Cdd:pfam09358   75 VLEVSCEDEDGEDVEVPYV 93
E1-1_like cd01485
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ...
 68-231 7.75e-47

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: 166.44  E-value: 7.75e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354   68 LYSRQLYVLGHEAMKRLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREE--DIGKNRAEVS 145
Cdd:cd01485     1 LYDRQIRLWGDEAQNKLRSAKVLIIGAGALGAEIAKNLVLAGIDSITIVDHRLVSTEDLGSNFFLDAEvsNSGMNRAAAS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354  146 QPRLAELNSYVPVTAYTGP------LVEDFLSGFQVVVLTNTPLEDQLRVGEFCHNRGIKLVVADTRGLFGQLFCDF--- 216
Cdd:cd01485    81 YEFLQELNPNVKLSIVEEDslsndsNIEEYLQKFTLVIATEENYERTAKVNDVCRKHHIPFISCATYGLIGYAFFDFpia 160

                         170       180
                  ....*....|....*....|..
gi 768033354  217 -------GEEMILTDSNGEQPL 231
Cdd:cd01485   161 aflggvvAQEAIKSISGKFTPL 182
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 69-213 5.20e-44

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: 159.73  E-value: 5.20e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354    69 YSRQLY--VLGHEAMKRLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREEDIGKNRAEVSQ 146
Cdd:pfam00899    1 YSRQLAlpLIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAA 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768033354   147 PRLAELNSYVPVTAYTGPL----VEDFLSGFQVVVLTNTPLEDQLRVGEFCHNRGIKLVVADTRGLFGQLF 213
Cdd:pfam00899   81 ERLREINPDVEVEAYTERLtpenAEELIKSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVT 151
E1_FCCH pfam16190
Ubiquitin-activating enzyme E1 FCCH domain; This domain is found in the ubiquitin-activating ...
 241-310 5.96e-43

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: 150.33  E-value: 5.96e-43
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354   241 DNPGVVTCLDEARHGFESGDFVSFSEVQGMVELNGNQPMEIKVLGPYTFSICDTSNFSDYIRGGIVSQVK 310
Cdd:pfam16190    1 DNPGVVTCLDDTRHGLEDGDYVTFSEVEGMTELNGCEPRKIKVLGPYTFSIGDTSSFSPYLRGGIVTQVK 70
Aos1_SUMO cd01492
Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating ...
 68-215 1.33e-42

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: 153.99  E-value: 1.33e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354   68 LYSRQLYVLGHEAMKRLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREEDIGKNRAEVSQP 147
Cdd:cd01492     3 LYDRQIRLWGLEAQKRLRSARILLIGLKGLGAEIAKNLVLSGIGSLTILDDRTVTEEDLGAQFLIPAEDLGQNRAEASLE 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768033354  148 RLAELNSYVPVTAYTGPLVE---DFLSGFQVVVLTNTPLEDQLRVGEFCHNRGIKLVVADTRGLFGQLFCD 215
Cdd:cd01492    83 RLRALNPRVKVSVDTDDISEkpeEFFSQFDVVVATELSRAELVKINELCRKLGVKFYATGVHGLFGFVFAD 153
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 484-663 1.34e-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: 151.74  E-value: 1.34e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354  484 KYFLVGAGAIGCELLKNFAMIGLGcgeggEIIVTDMDTIEKSNLNRQFLFRPWDVTKLKSDTAAAAVRQMNPHIRVTSHQ 563
Cdd:cd01488     1 KILVIGAGGLGCELLKNLALSGFR-----NIHVIDMDTIDVSNLNRQFLFREKDIGKPKAEVAAKFVNDRVPGVNVTPHF 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354  564 NRVgpdteRIYDDDFFQNLDGVANALDNVDARMYMDRRCVY--------YRKPLLESGTLGTKGNVQVVIPFLTESYSSS 635
Cdd:cd01488    76 GKI-----QDKDEEFYRQFNIIICGLDSIEARRWINGTLVSlllyedpeSIIPLIDGGTEGFKGHARVILPGITACIECS 150

                         170       180       190
                  ....*....|....*....|....*....|
gi 768033354  636 QD--PPEKSIPICTLKNFPNAIEHTLQWAR 663
Cdd:cd01488   151 LDlfPPQVTFPLCTIANTPRLPEHCIEYAS 180
E1_4HB pfam16191
Ubiquitin-activating enzyme E1 four-helix bundle; This domain is found in the ...
 311-380 3.53e-38

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: 136.43  E-value: 3.53e-38
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354   311 VPKKISFKSLVASLAEPDFVVTDFAKFSRPAQLHIGFQALHQFCAQHGRPPRPRNEEDAAELVALAQAVN 380
Cdd:pfam16191    1 MPKTLSFKSLEESLKEPEFLISDFAKFDRPAQLHLAFQALHAFQEKHGRLPRPWNEEDAEEVVKLAKELN 70
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 464-646 1.13e-34

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: 132.60  E-value: 1.13e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354  464 RYDGQVAV--FGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGcgeggEIIVTDMDTIEKSNLNRQFLFRPWDVTKL 541
Cdd:cd00757     1 RYSRQILLpeIGEEGQEKLKNARVLVVGAGGLGSPAAEYLAAAGVG-----KLGLVDDDVVELSNLQRQILHTEADVGQP 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354  542 KSDTAAAAVRQMNPHIRVTSHQNRVGPDTEriydDDFFQNLDGVANALDNVDARMYMDRRCVYYRKPLLESGTLGTKGNV 621
Cdd:cd00757    76 KAEAAAERLRAINPDVEIEAYNERLDAENA----EELIAGYDLVLDCTDNFATRYLINDACVKLGKPLVSGAVLGFEGQV 151

                         170       180
                  ....*....|....*....|....*.
gi 768033354  622 QVVIPFLTESYSSS-QDPPEKSIPIC 646
Cdd:cd00757   152 TVFIPGEGPCYRCLfPEPPPPGVPSC 177
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 464-626 1.32e-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: 129.86  E-value: 1.32e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354  464 RYDGQVAV--FGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGcgeggEIIVTDMDTIEKSNLNRQFLFRPWDVTKL 541
Cdd:COG0476     7 RYSRQILLpeIGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVG-----TLTLVDDDVVELSNLQRQILYTEADVGRP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354  542 KSDTAAAAVRQMNPHIRVTSHQNRVGPDTEriydDDFFQNLDGVANALDNVDARMYMDRRCVYYRKPLLESGTLGTKGNV 621
Cdd:COG0476    82 KVEAAAERLRALNPDVEVEAIPERLTEENA----LELLAGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIGFEGQV 157


                  ....*
gi 768033354  622 QVVIP 626
Cdd:COG0476   158 TVFIP 162
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 486-625 9.90e-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: 120.84  E-value: 9.90e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354  486 FLVGAGAIGCELLKNFAMIGLGcgeggEIIVTDMDTIEKSNLNRQFLFRPWDVTKLKSDTAAAAVRQMNPHIRVTSHQNR 565
Cdd:cd01483     3 LLVGLGGLGSEIALNLARSGVG-----KITLIDFDTVELSNLNRQFLARQADIGKPKAEVAARRLNELNPGVNVTAVPEG 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354  566 VGPDTeriyDDDFFQNLDGVANALDNVDARMYMDRRCVYYRKPLLESGTLGTKGNVQVVI 625
Cdd:cd01483    78 ISEDN----LDDFLDGVDLVIDAIDNIAVRRALNRACKELGIPVIDAGGLGLGGDIQVID 133
APPBP1_RUB cd01493
Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric ...
 69-442 2.33e-23

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: 104.31  E-value: 2.33e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354   69 YSRQLYVLGHEAMKRLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREEDIGKNRAEVSQPR 148
Cdd:cd01493     3 YDRQLRLWGEHGQAALESAHVCLLNATATGTEILKNLVLPGIGSFTIVDGSKVDEEDLGNNFFLDASSLGKSRAEATCEL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354  149 LAELNSYVPVTAYTGPLVE------DFLSGFQVVVLTNTPLEDQLRVGEFCHNRGIKLVVADTRGLFGQLFCDFGEEMIl 222
Cdd:cd01493    83 LQELNPDVNGSAVEESPEAlldndpSFFSQFTVVIATNLPESTLLRLADVLWSANIPLLYVRSYGLYGYIRIQLKEHTI- 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354  223 TDSNGEQPLSAMvsmvTKDNPgvvtcldearhgfesgdfvsFSEVQGMVE---LNGNQPME----------IKVL----- 284
Cdd:cd01493   162 VESHPDNALEDL----RLDNP--------------------FPELREHADsidLDDMDPAEhshtpyivilIKYLekwrs 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354  285 ---GPYTFSICDTSNFSDYIRGGIVSQvkvPKKISFKSLVASlaepdfVVTDFAKFSRPAQLHIGFQ------------- 348
Cdd:cd01493   218 ahnGQLPSTYKEKKEFRDLVRSLMRSN---EDEENFEEAIKA------VNKALNRTKIPSSVEEIFNddrcenltsqsss 288

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354  349 ------ALHQFCA-QHGRPP----------------------RPRNEEDAAELVALAQAV-NARALPAvqqNNLDEDLI- 397
Cdd:cd01493   289 fwimarALKEFVAeENGLLPlpgtlpdmtadtekyiklqniyREKAEKDAAEVEKYVREIlKSLGRSP---DSISDKEIk 365

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 768033354  398 ---RKLAYVAA----GDLAPINAFIGGLAAQEVMKACSGKFMPIMQWLYFDA 442
Cdd:cd01493   366 lfcKNAAFLRVirgrSLEHNISAFMGGIAAQEVIKLITKQYVPIDNTFIFDG 417
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 89-212 3.19e-21

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: 90.79  E-value: 3.19e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354   89 VLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREEDIGKNRAEVSQPRLAELNSYVPVTAYT----GP 164
Cdd:cd01483     2 VLLVGLGGLGSEIALNLARSGVGKITLIDFDTVELSNLNRQFLARQADIGKPKAEVAARRLNELNPGVNVTAVPegisED 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 768033354  165 LVEDFLSGFQVVVLTNTPLEDQLRVGEFCHNRGIKLVVADTRGLFGQL 212
Cdd:cd01483    82 NLDDFLDGVDLVIDAIDNIAVRRALNRACKELGIPVIDAGGLGLGGDI 129
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 464-609 6.89e-19

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 87.21  E-value: 6.89e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354  464 RYDGQVAV--FGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGcgeggEIIVTDMDTIEKSNLNRQFLFRPWDVTKL 541
Cdd:PRK05690   12 RYNRQIILrgFDFDGQEKLKAARVLVVGLGGLGCAASQYLAAAGVG-----TLTLVDFDTVSLSNLQRQVLHDDATIGQP 86

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768033354  542 KSDTAAAAVRQMNPHIRVTSHQNRVGPDTEriydDDFFQNLDGVANALDNVDARMYMDRRCVYYRKPL 609
Cdd:PRK05690   87 KVESARAALARINPHIAIETINARLDDDEL----AALIAGHDLVLDCTDNVATRNQLNRACFAAKKPL 150
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
473-626 1.77e-16

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 82.75  E-value: 1.77e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354  473 GSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGcgeggEIIVTDMDTIEKSNLNRQFLFRPWDVTKLKSDTAAAAVRQ 552
Cdd:PRK08762  126 GEEGQRRLLEARVLLIGAGGLGSPAALYLAAAGVG-----TLGIVDHDVVDRSNLQRQILHTEDRVGQPKVDSAAQRLAA 200

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768033354  553 MNPHIRVTSHQNRVGPDTEriydDDFFQNLDGVANALDNVDARMYMDRRCVYYRKPLLESGTLGTKGNVQVVIP 626
Cdd:PRK08762  201 LNPDVQVEAVQERVTSDNV----EALLQDVDVVVDGADNFPTRYLLNDACVKLGKPLVYGAVFRFEGQVSVFDA 270
PRK08328 PRK08328
hypothetical protein; Provisional
 69-212 3.30e-16

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 79.07  E-value: 3.30e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354   69 YSRQLYVLGHEAMKRLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREEDIGKNRAEVSQP- 147
Cdd:PRK08328   10 YDRQIMIFGVEGQEKLKKAKVAVVGVGGLGSPVAYYLAAAGVGRILLIDEQTPELSNLNRQILHWEEDLGKNPKPLSAKw 89

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768033354  148 RLAELNSYVPVTAYTGPL----VEDFLSGFQVVVLTNTPLEDQLRVGEFCHNRGIKLVVADTRGLFGQL 212
Cdd:PRK08328   90 KLERFNSDIKIETFVGRLseenIDEVLKGVDVIVDCLDNFETRYLLDDYAHKKGIPLVHGAVEGTYGQV 158
PRK08328 PRK08328
hypothetical protein; Provisional
 464-631 2.35e-15

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 76.76  E-value: 2.35e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354  464 RYDGQVAVFGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLgcgegGEIIVTDMDTIEKSNLNRQFLFRPWDVTK-LK 542
Cdd:PRK08328    9 RYDRQIMIFGVEGQEKLKKAKVAVVGVGGLGSPVAYYLAAAGV-----GRILLIDEQTPELSNLNRQILHWEEDLGKnPK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354  543 SDTAAAAVRQMNPHIRVTSHQNRVgpDTERIydDDFFQNLDGVANALDNVDARMYMDRRCVYYRKPLLESGTLGTKGNVQ 622
Cdd:PRK08328   84 PLSAKWKLERFNSDIKIETFVGRL--SEENI--DEVLKGVDVIVDCLDNFETRYLLDDYAHKKGIPLVHGAVEGTYGQVT 159


                  ....*....
gi 768033354  623 VVIPFLTES 631
Cdd:PRK08328  160 TIVPGKTKR 168
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 69-238 4.24e-15

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: 75.94  E-value: 4.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354   69 YSRQ--LYVLGHEAMKRLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREEDIGKNRAEVSQ 146
Cdd:COG0476     8 YSRQilLPEIGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADVGRPKVEAAA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354  147 PRLAELNSYVPVTAYTGPL----VEDFLSGFQVVV--LTNtpLEDQLRVGEFCHNRGIKLVVADTRGLFGQLF------- 213
Cdd:COG0476    88 ERLRALNPDVEVEAIPERLteenALELLAGADLVLdcTDN--FATRYLLNDACVKLGIPLVSGAVIGFEGQVTvfipgdt 165

                         170       180       190
                  ....*....|....*....|....*....|
gi 768033354  214 ----CDFGEEMILTDSNGEQP-LSAMVSMV 238
Cdd:COG0476   166 pcyrCLFPEPPEPGPSCAEAGvLGPLVGVI 195
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 454-595 5.07e-15

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 78.00  E-value: 5.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354  454 TEDKCLQRQNRYDGqvavFGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGcgeggEIIVTDMDTIEKSNLNRQFLF 533
Cdd:PRK05600   17 SELRRTARQLALPG----FGIEQQERLHNARVLVIGAGGLGCPAMQSLASAGVG-----TITLIDDDTVDVSNIHRQILF 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768033354  534 RPWDVTKLKSDTAAAAVRQMNPHIRVTSHQNRVGPDTERiyddDFFQNLDGVANALDNVDAR 595
Cdd:PRK05600   88 GASDVGRPKVEVAAERLKEIQPDIRVNALRERLTAENAV----ELLNGVDLVLDGSDSFATK 145
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 69-212 1.76e-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: 74.05  E-value: 1.76e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354   69 YSRQLYV--LGHEAMKRLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREEDIGKNRAEVSQ 146
Cdd:cd00757     2 YSRQILLpeIGEEGQEKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRQILHTEADVGQPKAEAAA 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768033354  147 PRLAELNSYVPVTAY----TGPLVEDFLSGFQVVV--LTNtpLEDQLRVGEFCHNRGIKLVVADTRGLFGQL 212
Cdd:cd00757    82 ERLRAINPDVEIEAYnerlDAENAEELIAGYDLVLdcTDN--FATRYLINDACVKLGKPLVSGAVLGFEGQV 151
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 463-626 7.38e-14

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 74.26  E-value: 7.38e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354  463 NRYDGQV--AVFGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGcgeggEIIVTDMDTIEKSNLNRQFLFRPWDVTK 540
Cdd:PRK07688    3 ERYSRQElfSPIGEEGQQKLREKHVLIIGAGALGTANAEMLVRAGVG-----KVTIVDRDYVEWSNLQRQQLYTESDVKN 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354  541 LKSDTAAAAVR--QMNPHIRVTSHQNRVGPdtERIydDDFFQNLDGVANALDNVDARMYMDRRCVYYRKPLLESGTLGTK 618
Cdd:PRK07688   78 NLPKAVAAKKRleEINSDVRVEAIVQDVTA--EEL--EELVTGVDLIIDATDNFETRFIVNDAAQKYGIPWIYGACVGSY 153


                  ....*...
gi 768033354  619 GNVQVVIP 626
Cdd:PRK07688  154 GLSYTIIP 161
Aos1_SUMO cd01492
Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating ...
 465-619 1.98e-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: 67.32  E-value: 1.98e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354  465 YDGQVAVFGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLgcgegGEIIVTDMDTIEKSNLNRQFLFRPWDVTKLKSD 544
Cdd:cd01492     4 YDRQIRLWGLEAQKRLRSARILLIGLKGLGAEIAKNLVLSGI-----GSLTILDDRTVTEEDLGAQFLIPAEDLGQNRAE 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768033354  545 TAAAAVRQMNPHIRVTShqnrvgpDTERI--YDDDFFQNLDGV-ANALDNvDARMYMDRRCVYYRKPLLESGTLGTKG 619
Cdd:cd01492    79 ASLERLRALNPRVKVSV-------DTDDIseKPEEFFSQFDVVvATELSR-AELVKINELCRKLGVKFYATGVHGLFG 148
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
 472-618 4.28e-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: 66.86  E-value: 4.28e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354  472 FGSDLQEKLGKQKYFLVGAGAIGcellkNFAMIGL---GCGEggeIIVTDMDTIEKSNLNRQFLFRPWDVTKLKSDTAAA 548
Cdd:cd00755     1 YGEEGLEKLRNAHVAVVGLGGVG-----SWAAEALarsGVGK---LTLIDFDVVCVSNLNRQIHALLSTVGKPKVEVMAE 72

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354  549 AVRQMNPHIRVTSHQNRVGPDTEriyDDDFFQNLDGVANALDNVDARMYMDRRCVYYRKPLLESGTLGTK 618
Cdd:cd00755    73 RIRDINPECEVDAVEEFLTPDNS---EDLLGGDPDFVVDAIDSIRAKVALIAYCRKRKIPVISSMGAGGK 139
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 473-608 5.34e-12

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 68.97  E-value: 5.34e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354  473 GSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGcgeggEIIVTDMDTIEKSNLNRQFLFRPWDVTKLKSDTAAAAVRQ 552
Cdd:PRK07878   33 GVDGQKRLKNARVLVIGAGGLGSPTLLYLAAAGVG-----TLGIVEFDVVDESNLQRQVIHGQSDVGRSKAQSARDSIVE 107

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 768033354  553 MNPHIRVTSHQNRVGPDTERiyddDFFQNLDGVANALDNVDARMYMDRRCVYYRKP 608
Cdd:PRK07878  108 INPLVNVRLHEFRLDPSNAV----ELFSQYDLILDGTDNFATRYLVNDAAVLAGKP 159
TcdA COG1179
tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ...
 487-613 1.72e-11

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: 65.49  E-value: 1.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354  487 LVGAGAIgcELLKN--FAMIGLG-----CGEG------GEIIVTDMDTIEKSNLNRQF--LfrpwDVT--KLKSDTAAAA 549
Cdd:COG1179    13 LYGEEGL--ERLANahVAVVGLGgvgswAAEAlarsgvGRLTLVDLDDVCESNINRQLhaL----DSTvgRPKVEVMAER 86

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768033354  550 VRQMNPHIRVTSHQNRVGPDTeriYDDDFFQNLDGVANALDNVDARMYMDRRCVYYRKPLLESG 613
Cdd:COG1179    87 IRDINPDCEVTAIDEFVTPEN---ADELLSEDYDYVIDAIDSVSAKAALIAWCRRRGIPIISSM 147
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 464-595 5.05e-11

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 65.66  E-value: 5.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354  464 RYDGQVAV--FGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGcgeggEIIVTDMDTIEKSNLNRQFLFRPWDVTKL 541
Cdd:PRK05597    8 RYRRQIMLgeIGQQGQQSLFDAKVAVIGAGGLGSPALLYLAGAGVG-----HITIIDDDTVDLSNLHRQVIHSTAGVGQP 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 768033354  542 KSDTAAAAVRQMNPHIRVTSHQNRVGPDTERiyddDFFQNLDGVANALDNVDAR 595
Cdd:PRK05597   83 KAESAREAMLALNPDVKVTVSVRRLTWSNAL----DELRDADVILDGSDNFDTR 132
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
465-594 9.58e-11

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 62.57  E-value: 9.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354  465 YDGQVAVFGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGcgeggEIIVTDMDTIEKSNLNRQFLFrPWDVTKLKSD 544
Cdd:PRK08644   11 EAMLASRHTPKLLEKLKKAKVGIAGAGGLGSNIAVALARSGVG-----NLKLVDFDVVEPSNLNRQQYF-ISQIGMPKVE 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 768033354  545 TAAAAVRQMNPHIRVTSHQNRVgpDTERIydDDFFQNLDGVANALDNVDA 594
Cdd:PRK08644   85 ALKENLLEINPFVEIEAHNEKI--DEDNI--EELFKDCDIVVEAFDNAET 130
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 88-178 1.67e-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: 63.14  E-value: 1.67e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354   88 SVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREEDIGKNRAEVSQPRLAELNSYVPVTAYTGPLV- 166
Cdd:cd01488     1 KILVIGAGGLGCELLKNLALSGFRNIHVIDMDTIDVSNLNRQFLFREKDIGKPKAEVAAKFVNDRVPGVNVTPHFGKIQd 80

                          90
                  ....*....|....
gi 768033354  167 --EDFLSGFQVVVL 178
Cdd:cd01488    81 kdEEFYRQFNIIIC 94
E1-1_like cd01485
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ...
 465-559 2.08e-10

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


Pssm-ID: 238762 [Multi-domain]  Cd Length: 198  Bit Score: 61.28  E-value: 2.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354  465 YDGQVAVFGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLgcgegGEIIVTDMDTIEKSNLNRQFLFRPWDVT--KLK 542
Cdd:cd01485     2 YDRQIRLWGDEAQNKLRSAKVLIIGAGALGAEIAKNLVLAGI-----DSITIVDHRLVSTEDLGSNFFLDAEVSNsgMNR 76

                          90
                  ....*....|....*..
gi 768033354  543 SDTAAAAVRQMNPHIRV 559
Cdd:cd01485    77 AAASYEFLQELNPNVKL 93
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 462-652 2.74e-10

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 63.21  E-value: 2.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354  462 QNRYDGQVAV--FGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGcgeggEIIVTDMDTIEKSNLNRQFLFRPWDVT 539
Cdd:PRK12475    2 QERYSRQILFsgIGEEGQRKIREKHVLIVGAGALGAANAEALVRAGIG-----KLTIADRDYVEWSNLQRQQLYTEEDAK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354  540 KLKSDTAAAA--VRQMNPHIRVTSHQNRVGPDTERiyddDFFQNLDGVANALDNVDARMYMDRRCVYYRKPLLESGTLGT 617
Cdd:PRK12475   77 QKKPKAIAAKehLRKINSEVEIVPVVTDVTVEELE----ELVKEVDLIIDATDNFDTRLLINDLSQKYNIPWIYGGCVGS 152

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 768033354  618 KGNVQVVIPFLTESYSssqdppeksipiCTLKNFP 652
Cdd:PRK12475  153 YGVTYTIIPGKTPCLR------------CLMEHVP 175
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 89-212 1.19e-08

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: 57.77  E-value: 1.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354   89 VLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREEDIGKNRAEVSQPRLAELNSYVPVTAYTGPLVE- 167
Cdd:cd01489     2 VLVVGAGGIGCELLKNLVLTGFGEIHIIDLDTIDLSNLNRQFLFRKKHVGKSKAQVAKEAVLSFNPNVKIVAYHANIKDp 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 768033354  168 ----DFLSGFQVVV--LTNtpLEDQLRVGEFCHNRGIKLVVADTRGLFGQL 212
Cdd:cd01489    82 dfnvEFFKQFDLVFnaLDN--LAARRHVNKMCLAADVPLIESGTTGFLGQV 130
E1_ThiF_like cd01487
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ...
 487-595 4.19e-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: 53.92  E-value: 4.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354  487 LVGAGAIGCELLKNFAMIGLGcgeggEIIVTDMDTIEKSNLNRQFlFRPWDVTKLKSDTAAAAVRQMNPHIRVTSHQNRV 566
Cdd:cd01487     4 IAGAGGLGSNIAVLLARSGVG-----NLKLVDFDVVEPSNLNRQQ-YFLSQIGEPKVEALKENLREINPFVKIEAINIKI 77

                          90       100
                  ....*....|....*....|....*....
gi 768033354  567 gpDTERIYddDFFQNLDGVANALDNVDAR 595
Cdd:cd01487    78 --DENNLE--GLFGDCDIVVEAFDNAETK 102
PTZ00245 PTZ00245
ubiquitin activating enzyme; Provisional
 69-185 1.93e-07

ubiquitin activating enzyme; Provisional


Pssm-ID: 140272  Cd Length: 287  Bit Score: 53.91  E-value: 1.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354   69 YSRQLYVLGHEAMKRLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQfYLREEDIGKNRAEVSQPR 148
Cdd:PTZ00245    9 YDRQIRLWGKSTQQQLMHTSVALHGVAGAAAEAAKNLVLAGVRAVAVADEGLVTDADVCTN-YLMQGEAGGTRGARALGA 87

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 768033354  149 LAELNSYvpVTAYTGPLVEDFLSGFQVVVLTNTPLED 185
Cdd:PTZ00245   88 LQRLNPH--VSVYDAVTKLDGSSGTRVTMAAVITEED 122
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
473-608 2.88e-07

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 53.97  E-value: 2.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354  473 GSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGcgeggEIIVTDMDTIEKSNLNRQFLFRPWDVTKLKSDTAAAAVRQ 552
Cdd:PRK07411   29 GLEGQKRLKAASVLCIGTGGLGSPLLLYLAAAGIG-----RIGIVDFDVVDSSNLQRQVIHGTSWVGKPKIESAKNRILE 103

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 768033354  553 MNPHIRVTSHQNRVGPDTERiyddDFFQNLDGVANALDNVDARMYMDRRCVYYRKP 608
Cdd:PRK07411  104 INPYCQVDLYETRLSSENAL----DILAPYDVVVDGTDNFPTRYLVNDACVLLNKP 155
PRK15116 PRK15116
sulfur acceptor protein CsdL; Provisional
 464-616 5.17e-07

sulfur acceptor protein CsdL; Provisional


Pssm-ID: 185071  Cd Length: 268  Bit Score: 52.50  E-value: 5.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354  464 RYDGQVAVFGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGCgeggeIIVTDMDTIEKSNLNRQFLFRPWDVTKLKS 543
Cdd:PRK15116   12 RFGGTARLYGEKALQLFADAHICVVGIGGVGSWAAEALARTGIGA-----ITLIDMDDVCVTNTNRQIHALRDNVGLAKA 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768033354  544 DTAAAAVRQMNPHIRVTSHQNRVGPDTERIYDDdffQNLDGVANALDNVDARMYMDRRCVYYRKPLLESGTLG 616
Cdd:PRK15116   87 EVMAERIRQINPECRVTVVDDFITPDNVAEYMS---AGFSYVIDAIDSVRPKAALIAYCRRNKIPLVTTGGAG 156
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
 88-163 8.32e-07

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: 51.43  E-value: 8.32e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768033354   88 SVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREEDIGKNRAEVSQPRLAELNSYVPVTAYTG 163
Cdd:cd01484     1 KVLLVGAGGIGCELLKNLALMGFGQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKSEVAAEAVNDRNPNCKVVPYQN 76
Ube1_repeat1 cd01491
Ubiquitin activating enzyme (E1), repeat 1. E1, a highly conserved small protein present ...
 465-564 1.59e-06

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: 51.11  E-value: 1.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354  465 YDGQVAVFGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGcgeggEIIVTDMDTIEKSNLNRQFLFRPWDVTKLKSD 544
Cdd:cd01491     2 YSRQLYVLGHEAMKKLQKSNVLISGLGGLGVEIAKNLILAGVK-----SVTLHDTKPCSWSDLSSQFYLREEDIGKNRAE 76

                          90       100
                  ....*....|....*....|
gi 768033354  545 TAAAAVRQMNPHIRVTSHQN 564
Cdd:cd01491    77 ASQARLAELNPYVPVTVSTG 96
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 69-168 2.43e-06

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 50.76  E-value: 2.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354   69 YSRQLYV--LGHEAMKRLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREEDIGKN--RAEV 144
Cdd:PRK07688    5 YSRQELFspIGEEGQQKLREKHVLIIGAGALGTANAEMLVRAGVGKVTIVDRDYVEWSNLQRQQLYTESDVKNNlpKAVA 84

                          90       100
                  ....*....|....*....|....
gi 768033354  145 SQPRLAELNSYVPVTAytgpLVED 168
Cdd:PRK07688   85 AKKRLEEINSDVRVEA----IVQD 104
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 69-177 2.44e-06

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 50.23  E-value: 2.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354   69 YSRQ--LYVLGHEAMKRLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREEDIGKNRAEVSQ 146
Cdd:PRK05690   13 YNRQiiLRGFDFDGQEKLKAARVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVSLSNLQRQVLHDDATIGQPKVESAR 92

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 768033354  147 PRLAELNSYVPVTAYTGPLVEDFL----SGFQVVV 177
Cdd:PRK05690   93 AALARINPHIAIETINARLDDDELaaliAGHDLVL 127
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 70-162 8.28e-06

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 49.49  E-value: 8.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354   70 SRQLYV--LGHEAMKRLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREEDIGKNRAEVSQP 147
Cdd:PRK05600   23 ARQLALpgFGIEQQERLHNARVLVIGAGGLGCPAMQSLASAGVGTITLIDDDTVDVSNIHRQILFGASDVGRPKVEVAAE 102

                          90
                  ....*....|....*
gi 768033354  148 RLAELNSYVPVTAYT 162
Cdd:PRK05600  103 RLKEIQPDIRVNALR 117
APPBP1_RUB cd01493
Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric ...
 464-579 9.15e-06

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: 49.23  E-value: 9.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354  464 RYDGQVAVFGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLgcgegGEIIVTDMDTIEKSNLNRQFLFRPWDVTKLKS 543
Cdd:cd01493     2 KYDRQLRLWGEHGQAALESAHVCLLNATATGTEILKNLVLPGI-----GSFTIVDGSKVDEEDLGNNFFLDASSLGKSRA 76

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 768033354  544 DTAAAAVRQMNPHirVTSHQNRVGPDTERIYDDDFF 579
Cdd:cd01493    77 EATCELLQELNPD--VNGSAVEESPEALLDNDPSFF 110
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 908-963 1.13e-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: 48.02  E-value: 1.13e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 768033354   908 IATTTAAVVGLVCLELYKVVQGHRqLDSYKNGFLNLALPFFGFSEPLAAPRHQYYN 963
Cdd:pfam00899  183 LGPTTAVVAGLQALEALKLLLGKG-EPNLAGRLLQFDALTMTFRELRLALKNPNCP 237
PRK08223 PRK08223
hypothetical protein; Validated
 477-626 2.41e-05

hypothetical protein; Validated


Pssm-ID: 181302 [Multi-domain]  Cd Length: 287  Bit Score: 47.37  E-value: 2.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354  477 QEKLGKQKYFLVGAGAIGCELLKNFAMIGLGCgeggeIIVTDMDTIEKSNLNRQF------LFRPwdvtklKSDTAAAAV 550
Cdd:PRK08223   22 QQRLRNSRVAIAGLGGVGGIHLLTLARLGIGK-----FTIADFDVFELRNFNRQAgammstLGRP------KAEVLAEMV 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354  551 RQMNPHIRVTSHQNRVGPDTEriydDDFfqnLDGVANALDNVDARMYMDRRCVY---YRK--PLLESGTLGTKGNVQVVI 625
Cdd:PRK08223   91 RDINPELEIRAFPEGIGKENA----DAF---LDGVDVYVDGLDFFEFDARRLVFaacQQRgiPALTAAPLGMGTALLVFD 163


                  .
gi 768033354  626 P 626
Cdd:PRK08223  164 P 164
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 69-161 4.87e-05

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 46.65  E-value: 4.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354   69 YSRQLYV--LGHEAMKRLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREEDIG--KNRAEV 144
Cdd:PRK12475    5 YSRQILFsgIGEEGQRKIREKHVLIVGAGALGAANAEALVRAGIGKLTIADRDYVEWSNLQRQQLYTEEDAKqkKPKAIA 84

                          90
                  ....*....|....*..
gi 768033354  145 SQPRLAELNSYVPVTAY 161
Cdd:PRK12475   85 AKEHLRKINSEVEIVPV 101
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
69-177 9.02e-05

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 46.16  E-value: 9.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354   69 YSRQLYV--LGHEAMKRLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREEDIGKNRAEVSQ 146
Cdd:PRK08762  116 YSRHLRLpeVGEEGQRRLLEARVLLIGAGGLGSPAALYLAAAGVGTLGIVDHDVVDRSNLQRQILHTEDRVGQPKVDSAA 195

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 768033354  147 PRLAELNSYVPVTAY----TGPLVEDFLSGFQVVV 177
Cdd:PRK08762  196 QRLAALNPDVQVEAVqervTSDNVEALLQDVDVVV 230
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
 88-177 1.11e-04

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: 46.13  E-value: 1.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354   88 SVLVSGLRGLGVEIAKNIILGGVKA-----VTLHDQGTAQWADLSSQFYLREEDIGKNRAEVSQPRLAELNSYVPVTAYT 162
Cdd:cd01490     1 KVFLVGAGAIGCELLKNFALMGVGTgesgeITVTDMDNIEKSNLNRQFLFRPHDVGKPKSEVAAAAVKAMNPDLKITALQ 80

                          90       100
                  ....*....|....*....|...
gi 768033354  163 ---GPLVE-----DFLSGFQVVV 177
Cdd:cd01490    81 nrvGPETEhifndEFWEKLDGVA 103
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
63-177 3.96e-04

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 42.92  E-value: 3.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354   63 DIDEGLYSRqlyvLGHEAMKRLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYlREEDIGKNRA 142
Cdd:PRK08644    9 EFEAMLASR----HTPKLLEKLKKAKVGIAGAGGLGSNIAVALARSGVGNLKLVDFDVVEPSNLNRQQY-FISQIGMPKV 83

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 768033354  143 EVSQPRLAELNSYVPVTAY----TGPLVEDFLSGFQVVV 177
Cdd:PRK08644   84 EALKENLLEINPFVEIEAHnekiDEDNIEELFKDCDIVV 122
PRK14851 PRK14851
hypothetical protein; Provisional
 469-626 5.06e-04

hypothetical protein; Provisional


Pssm-ID: 184853 [Multi-domain]  Cd Length: 679  Bit Score: 44.08  E-value: 5.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354  469 VAVFGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGcgeggEIIVTDMDTIEKSNLNRQFLFRPWDVTKLKSDTAAA 548
Cdd:PRK14851   30 IGLFTPGEQERLAEAKVAIPGMGGVGGVHLITMVRTGIG-----RFHIADFDQFEPVNVNRQFGARVPSFGRPKLAVMKE 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354  549 AVRQMNPHIRVTshqnrvgPDTERIYDDDFFQNLDGVANALDNVDARMYMDRRCVYYRK-----PLLESGTLGTKGNVQV 623
Cdd:PRK14851  105 QALSINPFLEIT-------PFPAGINADNMDAFLDGVDVVLDGLDFFQFEIRRTLFNMArekgiPVITAGPLGYSSAMLV 177


                  ...
gi 768033354  624 VIP 626
Cdd:PRK14851  178 FTP 180
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 69-158 5.80e-04

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 43.54  E-value: 5.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354   69 YSRQLYV--LGHEAMKRLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREEDIGKNRAEVSQ 146
Cdd:PRK07878   23 YSRHLIIpdVGVDGQKRLKNARVLVIGAGGLGSPTLLYLAAAGVGTLGIVEFDVVDESNLQRQVIHGQSDVGRSKAQSAR 102

                          90
                  ....*....|..
gi 768033354  147 PRLAELNSYVPV 158
Cdd:PRK07878  103 DSIVEINPLVNV 114
E1_ThiF_like cd01487
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ...
 88-160 1.12e-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: 1.12e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768033354   88 SVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYlREEDIGKNRAEVSQPRLAELNSYVPVTA 160
Cdd:cd01487     1 KVGIAGAGGLGSNIAVLLARSGVGNLKLVDFDVVEPSNLNRQQY-FLSQIGEPKVEALKENLREINPFVKIEA 72
Apg7 cd01486
Apg7 is an E1-like protein, that activates two different ubiquitin-like proteins, Apg12 and ...
 484-562 1.30e-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: 1.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354  484 KYFLVGAGAIGCellkNFAMIGLGCGEgGEIIVTDMDTIEKSNLNRQFLFRPWDVT--KLKSDTAAAAVRQMNPHIRVTS 561
Cdd:cd01486     1 KCLLLGAGTLGC----NVARNLLGWGV-RHITFVDSGKVSYSNPVRQSLFTFEDCKggKPKAEAAAERLKEIFPSIDATG 75


                  .
gi 768033354  562 H 562
Cdd:cd01486    76 I 76
PRK14852 PRK14852
hypothetical protein; Provisional
 477-626 6.92e-03

hypothetical protein; Provisional


Pssm-ID: 184854 [Multi-domain]  Cd Length: 989  Bit Score: 40.45  E-value: 6.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033354  477 QEKLGKQKYFLVGAGAIGCELLKNFAMIGLGcgeggEIIVTDMDTIEKSNLNRQFLFRPWDVTKLKSDTAAAAVRQMNPH 556
Cdd:PRK14852  327 QRRLLRSRVAIAGLGGVGGIHLMTLARTGIG-----NFNLADFDAYSPVNLNRQYGASIASFGRGKLDVMTERALSVNPF 401

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768033354  557 IRVTSHQNRVGPDTeriyDDDFFQNLDGVANALD--NVDARMYMDRRCVYYRKPLLESGTLGTKGNVQVVIP 626
Cdd:PRK14852  402 LDIRSFPEGVAAET----IDAFLKDVDLLVDGIDffALDIRRRLFNRALELGIPVITAGPLGYSCALLVFMP 469
PRK07877 PRK07877
Rv1355c family protein;
136-209 7.52e-03

Rv1355c family protein;


Pssm-ID: 236122 [Multi-domain]  Cd Length: 722  Bit Score: 40.36  E-value: 7.52e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768033354  136 DIGKNRAEVSQPRLAELNSYVPVTAYTGPL----VEDFLSGFQVVVLTNTPLEDQLRVGEFCHNRGIKLVVA-DTRGLF 209
Cdd:PRK07877  156 DLGVNKAVVAARRIAELDPYLPVEVFTDGLtednVDAFLDGLDVVVEECDSLDVKVLLREAARARRIPVLMAtSDRGLL 234
 
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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