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Conserved domains on  [gi|1261214665|ref|NP_001343972|]
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ubiquitin-like modifier-activating enzyme 1 Y [Mus musculus]

Protein Classification

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ube1 super family cl36897
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 48-1055 0e+00

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


The actual alignment was detected with superfamily member TIGR01408:

Pssm-ID: 273603 [Multi-domain]  Cd Length: 1006  Bit Score: 1296.78  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665   48 DIDESLYSRQLYVLGHEAMKHLQASSVLISGLQGLGVEIAKNIILGGVKAVTLHDQGIAQWADLSSQFCLREEDIGKNRA 127
Cdd:TIGR01408    1 EIDEALYSRQLYVLGDEAMQKMAKSNVLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLSSNFFLSEDDVGRNRA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  128 EISQPRLAELNSYVPVFAYTGPLIEEFLSGFQVVVLTNTPLEYQLQVGEFCHSH--GIKLVVADTRGLVGQLFCDFGEEM 205
Cdd:TIGR01408   81 EAVVKKLAELNPYVHVSSSSVPFNEEFLDKFQCVVLTEMSLPLQKEINDFCHSQcpPIAFISADVRGLFGSLFCDFGDEF 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  206 ILTDSNGEQPLSAMVSMITKENPGIVTCLEDSRHGFESGDFISFTEVQGMSELNGIGPIEIKVLGPYTFSICDTSSFSEY 285
Cdd:TIGR01408  161 EVLDTDGEEPKTGFIASITQANPGIVTCLENHRHKLETGDFVTFREVNGMTGLNDGSPRKITVISPYSFSIGDTTELGPY 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  286 IRGGIVSQVKVPRKINFKPLLASLAEPEFVVTDFAKCCHPAQLHIGFQALHQFCTQHSRPPRPHNEEDAEELVTLAQSVN 365
Cdd:TIGR01408  241 LHGGIATQVKTPKTVFFKSLREQLKDPKCLIVDFSKPERPPEIHTAFQALDQFQEKYSRKPNVGCQQDAEELLKLATSIS 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  366 AQALPAVQQdcLDIDLIRKLAYVAAGDLAPMNAFFGGLAAQEVMKACSGKFMPIRQWLYFDALECLPEhRVAFMEDKCLP 445
Cdd:TIGR01408  321 ETLEEKVPD--VDAKLVHWLSWTAQGFLSPMAAAVGGVVSQEVLKAVTGKFSPLCQWFYFDSAESLPS-LGKPECEEFLP 397

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  446 HQNRYDGQVAVFGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGCGEDGEITVTDMDTIEKSNLNRQFLFRPWDITK 525
Cdd:TIGR01408  398 RGDRYDAQIAVFGDTFQQKLQNLNIFLVGCGAIGCEMLKNFALMGVGTGKKGMITVTDPDLIEKSNLNRQFLFRPHHIGK 477

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  526 LKSETAAAAVRDINPHIRIFSHQNRVGPETEHVYDDDFFQKLDGVANALDNVDARLYVDRRCVYYRKPLLESGTLGTKGN 605
Cdd:TIGR01408  478 PKSYTAADATLKINPQIKIDAHQNRVGPETETIFNDEFYEKLDVVINALDNVEARRYVDSRCLAFLKPLLESGTLGTKGN 557

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  606 VQVVVPFLTESYSSSQDPPEKSIPICTLKNFPNAIEHTVQWARDEFEGLFKQSAENVNQYLTDPKFMERTLQLAGT-QPL 684
Cdd:TIGR01408  558 TQVVVPHLTESYGSSRDPPEKEIPFCTLKSFPAAIEHTIQWARDKFEGLFSHKPSLVNKYLSSPSSAEEVLQKIQSgHSR 637

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  685 EVLEAIHCSLVLQRPQTWADCVTWAYQHWHTQYSHNIQQLLHNFPPAQLTSSGALFWSGPKRCPHPLTFDINNPLHLDYV 764
Cdd:TIGR01408  638 EGLEQIIKLLSKEKPRNFSQCVEWARLKFEKYFNNKALQLLHCFPLDIRTSTGSPFWSSPKRPPSPLKFDLNEPLHLSFI 717

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  765 MAAANLFAQTYGLGGSQ---DCAVVAKLLQSLPVPKFAPKSGIRIHVSEQELQSTSATTIDDSHLEELKTALPTPDKLLG 841
Cdd:TIGR01408  718 QAAAKLYATVYGIPFAEedlSADALLNILSEVKIPEFKPRSNKKIQTDETARKPDTAPIDDRNAIFQLEKAILSNEATKS 797

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  842 -FKMYPIDFEKDDDSNFHMDFIVAASNLRAENYGISPADRHKSKLIAGKIIPAIATTTSAIVGLVCLELYKVVQGHQQLE 920
Cdd:TIGR01408  798 dFRMAPLSFEKDDDHNGHIDFITAASNLRAKNYSIEPADRFKTKFIAGKIIPAIATSTATVSGLVCLELIKVTDGGYKFE 877

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  921 SYKNSFINLALPLFSFSAPLAPECHQYYDQEW-TLWDRFDVQGlqpsgeEMTLKQFLDYFKTEHKLEVIMLSQGVSMLYS 999
Cdd:TIGR01408  878 VYKNCFLNLAIPLFVFTEPTEVRKTKIRNGISfTIWDRWTLHG------DFTLLEFINAVKEKYGLEPTMVSQGVKLLYV 951

                          970       980       990      1000      1010
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1261214665 1000 VFMPasKLKERLDQPMTEIVSCVSKQKLGHHVKSLVFELCCNSDSGDDIEVPYVRY 1055
Cdd:TIGR01408  952 PVMP--GHAERLKLKMHKLVKPTTKKKLPPYRVHLTVSFACDDDGDEDVPGPPVRI 1005
 
Name Accession Description Interval E-value
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 48-1055 0e+00

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


Pssm-ID: 273603 [Multi-domain]  Cd Length: 1006  Bit Score: 1296.78  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665   48 DIDESLYSRQLYVLGHEAMKHLQASSVLISGLQGLGVEIAKNIILGGVKAVTLHDQGIAQWADLSSQFCLREEDIGKNRA 127
Cdd:TIGR01408    1 EIDEALYSRQLYVLGDEAMQKMAKSNVLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLSSNFFLSEDDVGRNRA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  128 EISQPRLAELNSYVPVFAYTGPLIEEFLSGFQVVVLTNTPLEYQLQVGEFCHSH--GIKLVVADTRGLVGQLFCDFGEEM 205
Cdd:TIGR01408   81 EAVVKKLAELNPYVHVSSSSVPFNEEFLDKFQCVVLTEMSLPLQKEINDFCHSQcpPIAFISADVRGLFGSLFCDFGDEF 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  206 ILTDSNGEQPLSAMVSMITKENPGIVTCLEDSRHGFESGDFISFTEVQGMSELNGIGPIEIKVLGPYTFSICDTSSFSEY 285
Cdd:TIGR01408  161 EVLDTDGEEPKTGFIASITQANPGIVTCLENHRHKLETGDFVTFREVNGMTGLNDGSPRKITVISPYSFSIGDTTELGPY 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  286 IRGGIVSQVKVPRKINFKPLLASLAEPEFVVTDFAKCCHPAQLHIGFQALHQFCTQHSRPPRPHNEEDAEELVTLAQSVN 365
Cdd:TIGR01408  241 LHGGIATQVKTPKTVFFKSLREQLKDPKCLIVDFSKPERPPEIHTAFQALDQFQEKYSRKPNVGCQQDAEELLKLATSIS 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  366 AQALPAVQQdcLDIDLIRKLAYVAAGDLAPMNAFFGGLAAQEVMKACSGKFMPIRQWLYFDALECLPEhRVAFMEDKCLP 445
Cdd:TIGR01408  321 ETLEEKVPD--VDAKLVHWLSWTAQGFLSPMAAAVGGVVSQEVLKAVTGKFSPLCQWFYFDSAESLPS-LGKPECEEFLP 397

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  446 HQNRYDGQVAVFGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGCGEDGEITVTDMDTIEKSNLNRQFLFRPWDITK 525
Cdd:TIGR01408  398 RGDRYDAQIAVFGDTFQQKLQNLNIFLVGCGAIGCEMLKNFALMGVGTGKKGMITVTDPDLIEKSNLNRQFLFRPHHIGK 477

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  526 LKSETAAAAVRDINPHIRIFSHQNRVGPETEHVYDDDFFQKLDGVANALDNVDARLYVDRRCVYYRKPLLESGTLGTKGN 605
Cdd:TIGR01408  478 PKSYTAADATLKINPQIKIDAHQNRVGPETETIFNDEFYEKLDVVINALDNVEARRYVDSRCLAFLKPLLESGTLGTKGN 557

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  606 VQVVVPFLTESYSSSQDPPEKSIPICTLKNFPNAIEHTVQWARDEFEGLFKQSAENVNQYLTDPKFMERTLQLAGT-QPL 684
Cdd:TIGR01408  558 TQVVVPHLTESYGSSRDPPEKEIPFCTLKSFPAAIEHTIQWARDKFEGLFSHKPSLVNKYLSSPSSAEEVLQKIQSgHSR 637

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  685 EVLEAIHCSLVLQRPQTWADCVTWAYQHWHTQYSHNIQQLLHNFPPAQLTSSGALFWSGPKRCPHPLTFDINNPLHLDYV 764
Cdd:TIGR01408  638 EGLEQIIKLLSKEKPRNFSQCVEWARLKFEKYFNNKALQLLHCFPLDIRTSTGSPFWSSPKRPPSPLKFDLNEPLHLSFI 717

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  765 MAAANLFAQTYGLGGSQ---DCAVVAKLLQSLPVPKFAPKSGIRIHVSEQELQSTSATTIDDSHLEELKTALPTPDKLLG 841
Cdd:TIGR01408  718 QAAAKLYATVYGIPFAEedlSADALLNILSEVKIPEFKPRSNKKIQTDETARKPDTAPIDDRNAIFQLEKAILSNEATKS 797

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  842 -FKMYPIDFEKDDDSNFHMDFIVAASNLRAENYGISPADRHKSKLIAGKIIPAIATTTSAIVGLVCLELYKVVQGHQQLE 920
Cdd:TIGR01408  798 dFRMAPLSFEKDDDHNGHIDFITAASNLRAKNYSIEPADRFKTKFIAGKIIPAIATSTATVSGLVCLELIKVTDGGYKFE 877

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  921 SYKNSFINLALPLFSFSAPLAPECHQYYDQEW-TLWDRFDVQGlqpsgeEMTLKQFLDYFKTEHKLEVIMLSQGVSMLYS 999
Cdd:TIGR01408  878 VYKNCFLNLAIPLFVFTEPTEVRKTKIRNGISfTIWDRWTLHG------DFTLLEFINAVKEKYGLEPTMVSQGVKLLYV 951

                          970       980       990      1000      1010
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1261214665 1000 VFMPasKLKERLDQPMTEIVSCVSKQKLGHHVKSLVFELCCNSDSGDDIEVPYVRY 1055
Cdd:TIGR01408  952 PVMP--GHAERLKLKMHKLVKPTTKKKLPPYRVHLTVSFACDDDGDEDVPGPPVRI 1005
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
 469-1011 0e+00

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


Pssm-ID: 238767 [Multi-domain]  Cd Length: 435  Bit Score: 844.65  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  469 KYFLVGAGAIGCELLKNFAMIGLGCGEDGEITVTDMDTIEKSNLNRQFLFRPWDITKLKSETAAAAVRDINPHIRIFSHQ 548
Cdd:cd01490      1 KVFLVGAGAIGCELLKNFALMGVGTGESGEITVTDMDNIEKSNLNRQFLFRPHDVGKPKSEVAAAAVKAMNPDLKITALQ 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  549 NRVGPETEHVYDDDFFQKLDGVANALDNVDARLYVDRRCVYYRKPLLESGTLGTKGNVQVVVPFLTESYSSSQDPPEKSI 628
Cdd:cd01490     81 NRVGPETEHIFNDEFWEKLDGVANALDNVDARMYVDRRCVYYRKPLLESGTLGTKGNTQVVIPHLTESYSSSRDPPEKSI 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  629 PICTLKNFPNAIEHTVQWARDEFEGLFKQSAENVNQYLtdpkfmertlqlagtqplevleaihcslvlqrpqtWADCVTW 708
Cdd:cd01490    161 PLCTLKNFPNAIEHTIQWARDEFEGLFKQPPENVNQYL-----------------------------------FEDCVRW 205

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  709 AYQHWHTQYSHNIQQLLHNFPPAQLTSSGALFWSGPKRCPHPLTFDINNPLHLDYVMAAANLFAQTYGLGGsqdcavvak 788
Cdd:cd01490    206 ARLLFEKYFNNNIKQLLHNFPPDAVTSDGAPFWSGPKRCPTPLEFDVNNPLHLDFVLAAANLYAEVYGIPG--------- 276

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  789 llqslpvpkfapksgirihvseqelqstsattiddshleelktalptpdkllgfkmypidFEKDDDSNFHMDFIVAASNL 868
Cdd:cd01490    277 ------------------------------------------------------------FEKDDDTNFHMDFITAASNL 296

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  869 RAENYGISPADRHKSKLIAGKIIPAIATTTSAIVGLVCLELYKVVQGHQQLESYKNSFINLALPLFSFSAPLAPECHQY- 947
Cdd:cd01490    297 RARNYSIPPADRHKTKRIAGKIIPAIATTTAAVTGLVCLELYKVVDGKRPLEAYKNAFLNLALPFFAFSEPIPAPKVKYa 376

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1261214665  948 YDQEWTLWDRFDVQGLQPSGEEMTlkqflDYFKTEHKLEVIMLSQGVSMLYSVFMPASKLKERL 1011
Cdd:cd01490    377 YDEEWTIWDRFEVKGKQTLQELLI-----DYFKEKYGLEVTMLSQGVSMLYSSFMPPAKLKERL 435
UBA_E1_SCCH pfam10585
Ubiquitin-activating enzyme, SCCH domain; Ubiquitin-activating enzyme (E1 enzyme) activates ...
 637-884 3.22e-139

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: 418.56  E-value: 3.22e-139
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  637 PNAIEHTVQWARDEFEGLFKQSAENVNQYLTDP-KFMERTLQLAGTQPLEVLEAIHCSLVLQRPQTWADCVTWAYQHWHT 715
Cdd:pfam10585    1 PNAIEHTIQWARDEFEGLFVQPPEEVNKYLQPPqNFIESLLKQGGGQKLETLESVRKSLVTERPKTFEDCVAWARLKFEK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  716 QYSHNIQQLLHNFPPAQLTSSGALFWSGPKRCPHPLTFDINNPLHLDYVMAAANLFAQTYGLGGSQDCAVVAKLLQSLPV 795
Cdd:pfam10585   81 LFNNDIKQLLYNFPPDHKTSSGAPFWSGPKRPPTPLEFDPNNPLHLDFVVAAANLRAQVYGIPGSRDREAIAKVLSKVKV 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  796 PKFAPKSGIRIHVSEQELQSTSA-TTIDDSHLEELKTALP----TPDKLLGFKMYPIDFEKDDDSNFHMDFIVAASNLRA 870
Cdd:pfam10585  161 PEFKPKSGVKIQVNDEEAADPNAeSEDDEDELDELLEELPklavSPSSLAGFRLNPIEFEKDDDTNFHIDFITAASNLRA 240

                          250
                   ....*....|....
gi 1261214665  871 ENYGISPADRHKSK 884
Cdd:pfam10585  241 RNYGIPPADRHKTK 254
UBA_e1_C smart00985
Ubiquitin-activating enzyme e1 C-terminal domain; This presumed domain found at the C terminus ...
 922-1053 9.49e-63

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: 208.65  E-value: 9.49e-63
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665   922 YKNSFINLALPLFSFSAPLAPECHQYYDQ-EWTLWDRFDVQGLqpsgeEMTLKQFLDYFKTEHKLEVIMLSQGVSMLYSV 1000
Cdd:smart00985    1 YKNAFLNLALPFFAFSEPIAAPKTKYRDKdKWTLWDRLEVPGG-----DITLKELLDYFEEKYGLEVTMLSQGVSLLYSS 75

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1261214665  1001 FMPASKLKERLDQPMTEIVSCVSKQKLGHHVKSLVFELCCNSDSGDDIEVPYV 1053
Cdd:smart00985   76 FMPPKKHKERLDLPVTELVEQVTKKKLPPHVKYLVLEVSCEDEDDEDVEVPYI 128
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 449-611 3.65e-34

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: 131.40  E-value: 3.65e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  449 RYDGQVAV--FGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGcgedgEITVTDMDTIEKSNLNRQFLFRPWDITKL 526
Cdd:COG0476      7 RYSRQILLpeIGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVG-----TLTLVDDDVVELSNLQRQILYTEADVGRP 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  527 KSETAAAAVRDINPHIRIFSHQNRVGPETEhvydDDFFQKLDGVANALDNVDARLYVDRRCVYYRKPLLESGTLGTKGNV 606
Cdd:COG0476     82 KVEAAAERLRALNPDVEVEAIPERLTEENA----LELLAGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIGFEGQV 157


                   ....*
gi 1261214665  607 QVVVP 611
Cdd:COG0476    158 TVFIP 162
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 449-598 7.17e-21

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 92.99  E-value: 7.17e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  449 RYDGQVAV--FGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGcgedgEITVTDMDTIEKSNLNRQFLFRPWDITKL 526
Cdd:PRK05690    12 RYNRQIILrgFDFDGQEKLKAARVLVVGLGGLGCAASQYLAAAGVG-----TLTLVDFDTVSLSNLQRQVLHDDATIGQP 86

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1261214665  527 KSETAAAAVRDINPHIRIFSHQNRVgpetehvyDDDFFQKL----DGVANALDNVDARLYVDRRCVYYRKPLLeSG 598
Cdd:PRK05690    87 KVESARAALARINPHIAIETINARL--------DDDELAALiaghDLVLDCTDNVATRNQLNRACFAAKKPLV-SG 153
 
Name Accession Description Interval E-value
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 48-1055 0e+00

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


Pssm-ID: 273603 [Multi-domain]  Cd Length: 1006  Bit Score: 1296.78  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665   48 DIDESLYSRQLYVLGHEAMKHLQASSVLISGLQGLGVEIAKNIILGGVKAVTLHDQGIAQWADLSSQFCLREEDIGKNRA 127
Cdd:TIGR01408    1 EIDEALYSRQLYVLGDEAMQKMAKSNVLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLSSNFFLSEDDVGRNRA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  128 EISQPRLAELNSYVPVFAYTGPLIEEFLSGFQVVVLTNTPLEYQLQVGEFCHSH--GIKLVVADTRGLVGQLFCDFGEEM 205
Cdd:TIGR01408   81 EAVVKKLAELNPYVHVSSSSVPFNEEFLDKFQCVVLTEMSLPLQKEINDFCHSQcpPIAFISADVRGLFGSLFCDFGDEF 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  206 ILTDSNGEQPLSAMVSMITKENPGIVTCLEDSRHGFESGDFISFTEVQGMSELNGIGPIEIKVLGPYTFSICDTSSFSEY 285
Cdd:TIGR01408  161 EVLDTDGEEPKTGFIASITQANPGIVTCLENHRHKLETGDFVTFREVNGMTGLNDGSPRKITVISPYSFSIGDTTELGPY 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  286 IRGGIVSQVKVPRKINFKPLLASLAEPEFVVTDFAKCCHPAQLHIGFQALHQFCTQHSRPPRPHNEEDAEELVTLAQSVN 365
Cdd:TIGR01408  241 LHGGIATQVKTPKTVFFKSLREQLKDPKCLIVDFSKPERPPEIHTAFQALDQFQEKYSRKPNVGCQQDAEELLKLATSIS 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  366 AQALPAVQQdcLDIDLIRKLAYVAAGDLAPMNAFFGGLAAQEVMKACSGKFMPIRQWLYFDALECLPEhRVAFMEDKCLP 445
Cdd:TIGR01408  321 ETLEEKVPD--VDAKLVHWLSWTAQGFLSPMAAAVGGVVSQEVLKAVTGKFSPLCQWFYFDSAESLPS-LGKPECEEFLP 397

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  446 HQNRYDGQVAVFGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGCGEDGEITVTDMDTIEKSNLNRQFLFRPWDITK 525
Cdd:TIGR01408  398 RGDRYDAQIAVFGDTFQQKLQNLNIFLVGCGAIGCEMLKNFALMGVGTGKKGMITVTDPDLIEKSNLNRQFLFRPHHIGK 477

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  526 LKSETAAAAVRDINPHIRIFSHQNRVGPETEHVYDDDFFQKLDGVANALDNVDARLYVDRRCVYYRKPLLESGTLGTKGN 605
Cdd:TIGR01408  478 PKSYTAADATLKINPQIKIDAHQNRVGPETETIFNDEFYEKLDVVINALDNVEARRYVDSRCLAFLKPLLESGTLGTKGN 557

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  606 VQVVVPFLTESYSSSQDPPEKSIPICTLKNFPNAIEHTVQWARDEFEGLFKQSAENVNQYLTDPKFMERTLQLAGT-QPL 684
Cdd:TIGR01408  558 TQVVVPHLTESYGSSRDPPEKEIPFCTLKSFPAAIEHTIQWARDKFEGLFSHKPSLVNKYLSSPSSAEEVLQKIQSgHSR 637

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  685 EVLEAIHCSLVLQRPQTWADCVTWAYQHWHTQYSHNIQQLLHNFPPAQLTSSGALFWSGPKRCPHPLTFDINNPLHLDYV 764
Cdd:TIGR01408  638 EGLEQIIKLLSKEKPRNFSQCVEWARLKFEKYFNNKALQLLHCFPLDIRTSTGSPFWSSPKRPPSPLKFDLNEPLHLSFI 717

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  765 MAAANLFAQTYGLGGSQ---DCAVVAKLLQSLPVPKFAPKSGIRIHVSEQELQSTSATTIDDSHLEELKTALPTPDKLLG 841
Cdd:TIGR01408  718 QAAAKLYATVYGIPFAEedlSADALLNILSEVKIPEFKPRSNKKIQTDETARKPDTAPIDDRNAIFQLEKAILSNEATKS 797

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  842 -FKMYPIDFEKDDDSNFHMDFIVAASNLRAENYGISPADRHKSKLIAGKIIPAIATTTSAIVGLVCLELYKVVQGHQQLE 920
Cdd:TIGR01408  798 dFRMAPLSFEKDDDHNGHIDFITAASNLRAKNYSIEPADRFKTKFIAGKIIPAIATSTATVSGLVCLELIKVTDGGYKFE 877

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  921 SYKNSFINLALPLFSFSAPLAPECHQYYDQEW-TLWDRFDVQGlqpsgeEMTLKQFLDYFKTEHKLEVIMLSQGVSMLYS 999
Cdd:TIGR01408  878 VYKNCFLNLAIPLFVFTEPTEVRKTKIRNGISfTIWDRWTLHG------DFTLLEFINAVKEKYGLEPTMVSQGVKLLYV 951

                          970       980       990      1000      1010
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1261214665 1000 VFMPasKLKERLDQPMTEIVSCVSKQKLGHHVKSLVFELCCNSDSGDDIEVPYVRY 1055
Cdd:TIGR01408  952 PVMP--GHAERLKLKMHKLVKPTTKKKLPPYRVHLTVSFACDDDGDEDVPGPPVRI 1005
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
 469-1011 0e+00

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


Pssm-ID: 238767 [Multi-domain]  Cd Length: 435  Bit Score: 844.65  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  469 KYFLVGAGAIGCELLKNFAMIGLGCGEDGEITVTDMDTIEKSNLNRQFLFRPWDITKLKSETAAAAVRDINPHIRIFSHQ 548
Cdd:cd01490      1 KVFLVGAGAIGCELLKNFALMGVGTGESGEITVTDMDNIEKSNLNRQFLFRPHDVGKPKSEVAAAAVKAMNPDLKITALQ 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  549 NRVGPETEHVYDDDFFQKLDGVANALDNVDARLYVDRRCVYYRKPLLESGTLGTKGNVQVVVPFLTESYSSSQDPPEKSI 628
Cdd:cd01490     81 NRVGPETEHIFNDEFWEKLDGVANALDNVDARMYVDRRCVYYRKPLLESGTLGTKGNTQVVIPHLTESYSSSRDPPEKSI 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  629 PICTLKNFPNAIEHTVQWARDEFEGLFKQSAENVNQYLtdpkfmertlqlagtqplevleaihcslvlqrpqtWADCVTW 708
Cdd:cd01490    161 PLCTLKNFPNAIEHTIQWARDEFEGLFKQPPENVNQYL-----------------------------------FEDCVRW 205

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  709 AYQHWHTQYSHNIQQLLHNFPPAQLTSSGALFWSGPKRCPHPLTFDINNPLHLDYVMAAANLFAQTYGLGGsqdcavvak 788
Cdd:cd01490    206 ARLLFEKYFNNNIKQLLHNFPPDAVTSDGAPFWSGPKRCPTPLEFDVNNPLHLDFVLAAANLYAEVYGIPG--------- 276

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  789 llqslpvpkfapksgirihvseqelqstsattiddshleelktalptpdkllgfkmypidFEKDDDSNFHMDFIVAASNL 868
Cdd:cd01490    277 ------------------------------------------------------------FEKDDDTNFHMDFITAASNL 296

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  869 RAENYGISPADRHKSKLIAGKIIPAIATTTSAIVGLVCLELYKVVQGHQQLESYKNSFINLALPLFSFSAPLAPECHQY- 947
Cdd:cd01490    297 RARNYSIPPADRHKTKRIAGKIIPAIATTTAAVTGLVCLELYKVVDGKRPLEAYKNAFLNLALPFFAFSEPIPAPKVKYa 376

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1261214665  948 YDQEWTLWDRFDVQGLQPSGEEMTlkqflDYFKTEHKLEVIMLSQGVSMLYSVFMPASKLKERL 1011
Cdd:cd01490    377 YDEEWTIWDRFEVKGKQTLQELLI-----DYFKEKYGLEVTMLSQGVSMLYSSFMPPAKLKERL 435
Ube1_repeat1 cd01491
Ubiquitin activating enzyme (E1), repeat 1. E1, a highly conserved small protein present ...
 53-433 9.00e-172

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: 504.11  E-value: 9.00e-172
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665   53 LYSRQLYVLGHEAMKHLQASSVLISGLQGLGVEIAKNIILGGVKAVTLHDQGIAQWADLSSQFCLREEDIGKNRAEISQP 132
Cdd:cd01491      1 LYSRQLYVLGHEAMKKLQKSNVLISGLGGLGVEIAKNLILAGVKSVTLHDTKPCSWSDLSSQFYLREEDIGKNRAEASQA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  133 RLAELNSYVPVFAYTGPLIEEFLSGFQVVVLTNTPLEYQLQVGEFCHSHGIKLVVADTRGLVGQLFCDFGEEMILTDSNG 212
Cdd:cd01491     81 RLAELNPYVPVTVSTGPLTTDELLKFQVVVLTDASLEDQLKINEFCHSPGIKFISADTRGLFGSIFCDFGDEFTVYDPNG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  213 EQPLSAMVSMITKENPGIVTCLEDSRHGFESGDFISFTEVQGMSELNGIGPIEIKVLGPYTFSICDTSSFSEYIRGGIVS 292
Cdd:cd01491    161 EEPKSGMISSISKDNPGVVTCLDETRHGFEDGDYVTFSEVEGMTELNGCEPRKIKVKGPYTFSIGDTSSFSEYIRGGIVT 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  293 QVKvprkinfkpllaslaepefvvtdfakcchpaqlhigfqalhqfctqhsrpprphneedaeelvtlaqsvnaqalpav 372
Cdd:cd01491    241 QVK----------------------------------------------------------------------------- 243

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1261214665  373 qqdcldidlirklayvaagdLAPMNAFFGGLAAQEVMKACSGKFMPIRQWLYFDALECLPE 433
Cdd:cd01491    244 --------------------LSPMAAFFGGLAAQEVLKACSGKFTPLKQWLYFDALECLPE 284
UBA_E1_SCCH pfam10585
Ubiquitin-activating enzyme, SCCH domain; Ubiquitin-activating enzyme (E1 enzyme) activates ...
 637-884 3.22e-139

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: 418.56  E-value: 3.22e-139
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  637 PNAIEHTVQWARDEFEGLFKQSAENVNQYLTDP-KFMERTLQLAGTQPLEVLEAIHCSLVLQRPQTWADCVTWAYQHWHT 715
Cdd:pfam10585    1 PNAIEHTIQWARDEFEGLFVQPPEEVNKYLQPPqNFIESLLKQGGGQKLETLESVRKSLVTERPKTFEDCVAWARLKFEK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  716 QYSHNIQQLLHNFPPAQLTSSGALFWSGPKRCPHPLTFDINNPLHLDYVMAAANLFAQTYGLGGSQDCAVVAKLLQSLPV 795
Cdd:pfam10585   81 LFNNDIKQLLYNFPPDHKTSSGAPFWSGPKRPPTPLEFDPNNPLHLDFVVAAANLRAQVYGIPGSRDREAIAKVLSKVKV 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  796 PKFAPKSGIRIHVSEQELQSTSA-TTIDDSHLEELKTALP----TPDKLLGFKMYPIDFEKDDDSNFHMDFIVAASNLRA 870
Cdd:pfam10585  161 PEFKPKSGVKIQVNDEEAADPNAeSEDDEDELDELLEELPklavSPSSLAGFRLNPIEFEKDDDTNFHIDFITAASNLRA 240

                          250
                   ....*....|....
gi 1261214665  871 ENYGISPADRHKSK 884
Cdd:pfam10585  241 RNYGIPPADRHKTK 254
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
 469-680 1.20e-80

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: 262.51  E-value: 1.20e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  469 KYFLVGAGAIGCELLKNFAMIGLGcgedgEITVTDMDTIEKSNLNRQFLFRPWDITKLKSETAAAAVRDINPHIRIFSHQ 548
Cdd:cd01484      1 KVLLVGAGGIGCELLKNLALMGFG-----QIHVIDMDTIDVSNLNRQFLFRPKDIGRPKSEVAAEAVNDRNPNCKVVPYQ 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  549 NRVGPETehVYDDDFFQKLDGVANALDNVDARLYVDRRCVYYRKPLLESGTLGTKGNVQVVVPFLTESYSSSQDPPEKSI 628
Cdd:cd01484     76 NKVGPEQ--DFNDTFFEQFHIIVNALDNIIARRYVNGMLIFLIVPLIESGTEGFKGNAQVILPGMTECIECTLYPPQKNF 153

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1261214665  629 PICTLKNFPNAIEHTVQWARDEFEG-------LFKQSAENVNQYLTDPKFMERTLQLAG 680
Cdd:cd01484    154 PMCTIASMPRLPEHCIEWARMLQWDdpehiqfIFQASNERASQYNIRGVTYFLTKGVAG 212
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 450-636 8.76e-70

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


Pssm-ID: 459987 [Multi-domain]  Cd Length: 238  Bit Score: 232.92  E-value: 8.76e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  450 YDGQVA--VFGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGcgedgEITVTDMDTIEKSNLNRQFLFRPWDITKLK 527
Cdd:pfam00899    1 YSRQLAlpLIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVG-----KITLVDFDTVELSNLNRQFLFREADIGKPK 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  528 SETAAAAVRDINPHIRIFSHQNRVGPETehvyDDDFFQKLDGVANALDNVDARLYVDRRCVYYRKPLLESGTLGTKGNVQ 607
Cdd:pfam00899   76 AEVAAERLREINPDVEVEAYTERLTPEN----AEELIKSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVT 151

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1261214665  608 VVVPFLTESYS--SSQDPPEKSIPICTLKNF 636
Cdd:pfam00899  152 VVIPGKTPCYRclFPEDPPPKLVPSCTVAGV 182
UBA_e1_C smart00985
Ubiquitin-activating enzyme e1 C-terminal domain; This presumed domain found at the C terminus ...
 922-1053 9.49e-63

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: 208.65  E-value: 9.49e-63
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665   922 YKNSFINLALPLFSFSAPLAPECHQYYDQ-EWTLWDRFDVQGLqpsgeEMTLKQFLDYFKTEHKLEVIMLSQGVSMLYSV 1000
Cdd:smart00985    1 YKNAFLNLALPFFAFSEPIAAPKTKYRDKdKWTLWDRLEVPGG-----DITLKELLDYFEEKYGLEVTMLSQGVSLLYSS 75

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1261214665  1001 FMPASKLKERLDQPMTEIVSCVSKQKLGHHVKSLVFELCCNSDSGDDIEVPYV 1053
Cdd:smart00985   76 FMPPKKHKERLDLPVTELVEQVTKKKLPPHVKYLVLEVSCEDEDDEDVEVPYI 128
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 469-929 5.67e-57

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: 199.53  E-value: 5.67e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  469 KYFLVGAGAIGCELLKNFAMIGLGcgedgEITVTDMDTIEKSNLNRQFLFRPWDITKLKSETAAAAVRDINPHIRIFSHQ 548
Cdd:cd01489      1 KVLVVGAGGIGCELLKNLVLTGFG-----EIHIIDLDTIDLSNLNRQFLFRKKHVGKSKAQVAKEAVLSFNPNVKIVAYH 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  549 NRVgpeTEHVYDDDFFQKLDGVANALDNVDARLYVDRRCVYYRKPLLESGTLGTKGNVQVVVPFLTESYSSSQDPPEKSI 628
Cdd:cd01489     76 ANI---KDPDFNVEFFKQFDLVFNALDNLAARRHVNKMCLAADVPLIESGTTGFLGQVQVIKKGKTECYECQPKETPKTF 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  629 PICTLKNFPNAIEHTVQWARDE---FEGLFKQsaeNVNQYLTdpkfMERTlqlagtqplevleaihcslvlqrpqtwadc 705
Cdd:cd01489    153 PVCTIRSTPSQPIHCIVWAKSLfflFNKVFKD---DIERLLS----MEEL------------------------------ 195

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  706 vtwayqhwhtqyshniqqllhnfppaqltssgalfWSGPKRcphpltfdinnplhldyvmaaanlfaqtyglggsqdcav 785
Cdd:cd01489    196 -----------------------------------WKTRKP--------------------------------------- 201

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  786 vakllqslPVPkfapksgirihvseqelqstsattIDDSHLEelktalptpdkllgfkmypidFEKDDDSNfhMDFIVAA 865
Cdd:cd01489    202 --------PVP------------------------LSWKELT---------------------FDKDDQDA--LDFVAAA 226

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1261214665  866 SNLRAENYGISPADRHKSKLIAGKIIPAIATTTSAIVGLVCLELYKVVQGHqqLESYKNSFINL 929
Cdd:cd01489    227 ANLRSHVFGIPMKSRFDIKQMAGNIIPAIATTNAIIAGLIVLEALKVLSGD--KEQCRTVFLNL 288
E1_UFD pfam09358
Ubiquitin fold domain; The ubiquitin fold domain is found at the C-terminus of ...
 955-1053 1.15e-45

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: 158.86  E-value: 1.15e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  955 WDRFDVQGlqpsgeEMTLKQFLDYFKTEHKLEVIMLSQGVSMLYSVFMPASKLKERLDQPMTEIVSCVSKQKLGHHVKSL 1034
Cdd:pfam09358    1 WDRFEVEG------DMTLQELLDYFKEKYGLEVTMLSYGVSLLYSSFMPPKKHKERLPMKISELVEEVSKKPIPPHQKYL 74

                           90
                   ....*....|....*....
gi 1261214665 1035 VFELCCNSDSGDDIEVPYV 1053
Cdd:pfam09358   75 VLEVSCEDEDGEDVEVPYV 93
E1-1_like cd01485
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ...
 53-216 4.87e-45

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


Pssm-ID: 238762 [Multi-domain]  Cd Length: 198  Bit Score: 161.05  E-value: 4.87e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665   53 LYSRQLYVLGHEAMKHLQASSVLISGLQGLGVEIAKNIILGGVKAVTLHDQGIAQWADLSSQFCLREE--DIGKNRAEIS 130
Cdd:cd01485      1 LYDRQIRLWGDEAQNKLRSAKVLIIGAGALGAEIAKNLVLAGIDSITIVDHRLVSTEDLGSNFFLDAEvsNSGMNRAAAS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  131 QPRLAELNSYVPVFAYTGP------LIEEFLSGFQVVVLTNTPLEYQLQVGEFCHSHGIKLVVADTRGLVGQLFCDF--- 201
Cdd:cd01485     81 YEFLQELNPNVKLSIVEEDslsndsNIEEYLQKFTLVIATEENYERTAKVNDVCRKHHIPFISCATYGLIGYAFFDFpia 160

                          170       180
                   ....*....|....*....|..
gi 1261214665  202 -------GEEMILTDSNGEQPL 216
Cdd:cd01485    161 aflggvvAQEAIKSISGKFTPL 182
E1_FCCH pfam16190
Ubiquitin-activating enzyme E1 FCCH domain; This domain is found in the ubiquitin-activating ...
 226-295 3.65e-42

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: 148.02  E-value: 3.65e-42
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  226 ENPGIVTCLEDSRHGFESGDFISFTEVQGMSELNGIGPIEIKVLGPYTFSICDTSSFSEYIRGGIVSQVK 295
Cdd:pfam16190    1 DNPGVVTCLDDTRHGLEDGDYVTFSEVEGMTELNGCEPRKIKVLGPYTFSIGDTSSFSPYLRGGIVTQVK 70
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 469-648 1.66e-40

Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating enzyme (E1), specific for the Rub family of ubiquitin-like proteins (Ubls). E1 enzymes are part of a conjugation cascade to attach Ub or Ubls, covalently to substrate proteins. consisting of activating (E1), conjugating (E2), and/or ligating (E3) enzymes. E1 activates ubiquitin(-like) by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and Ubls C-terminus. E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. Post-translational modification by Rub family of ubiquitin-like proteins (Ublps) activates SCF ubiquitin ligases and is involved in cell cycle control, signaling and embryogenesis. UBA3 contains both the nucleotide-binding motif involved in adenylation and the catalytic cysteine involved in the thioester intermediate and Ublp transfer to E2.


Pssm-ID: 238765 [Multi-domain]  Cd Length: 291  Bit Score: 151.35  E-value: 1.66e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  469 KYFLVGAGAIGCELLKNFAMIGLGcgedgEITVTDMDTIEKSNLNRQFLFRPWDITKLKSETAAAAVRDINPHIRIFSHQ 548
Cdd:cd01488      1 KILVIGAGGLGCELLKNLALSGFR-----NIHVIDMDTIDVSNLNRQFLFREKDIGKPKAEVAAKFVNDRVPGVNVTPHF 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  549 NRVgpeteHVYDDDFFQKLDGVANALDNVDARLYVDRRCVY--------YRKPLLESGTLGTKGNVQVVVPFLTESYSSS 620
Cdd:cd01488     76 GKI-----QDKDEEFYRQFNIIICGLDSIEARRWINGTLVSlllyedpeSIIPLIDGGTEGFKGHARVILPGITACIECS 150

                          170       180       190
                   ....*....|....*....|....*....|
gi 1261214665  621 QD--PPEKSIPICTLKNFPNAIEHTVQWAR 648
Cdd:cd01488    151 LDlfPPQVTFPLCTIANTPRLPEHCIEYAS 180
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 54-198 2.10e-39

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: 146.25  E-value: 2.10e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665   54 YSRQLY--VLGHEAMKHLQASSVLISGLQGLGVEIAKNIILGGVKAVTLHDQGIAQWADLSSQFCLREEDIGKNRAEISQ 131
Cdd:pfam00899    1 YSRQLAlpLIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAA 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1261214665  132 PRLAELNSYVPVFAYTGPL----IEEFLSGFQVVVLTNTPLEYQLQVGEFCHSHGIKLVVADTRGLVGQLF 198
Cdd:pfam00899   81 ERLREINPDVEVEAYTERLtpenAEELIKSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVT 151
Aos1_SUMO cd01492
Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating ...
 53-200 2.42e-39

Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating enzyme (E1), specific for the SUMO family of ubiquitin-like proteins (Ubls). E1 enzymes are part of a conjugation cascade to attach Ub or Ubls, covalently to substrate proteins consisting of activating (E1), conjugating (E2), and/or ligating (E3) enzymes. E1 activates ubiquitin by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and Ubls C-terminus. The E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. Post-translational modification by SUMO family of ubiquitin-like proteins (Ublps) is involved in cell division, nuclear transport, the stress response and signal transduction. Aos1 contains part of the adenylation domain.


Pssm-ID: 238769 [Multi-domain]  Cd Length: 197  Bit Score: 144.74  E-value: 2.42e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665   53 LYSRQLYVLGHEAMKHLQASSVLISGLQGLGVEIAKNIILGGVKAVTLHDQGIAQWADLSSQFCLREEDIGKNRAEISQP 132
Cdd:cd01492      3 LYDRQIRLWGLEAQKRLRSARILLIGLKGLGAEIAKNLVLSGIGSLTILDDRTVTEEDLGAQFLIPAEDLGQNRAEASLE 82

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1261214665  133 RLAELNSYVPVFAYTGPLIE---EFLSGFQVVVLTNTPLEYQLQVGEFCHSHGIKLVVADTRGLVGQLFCD 200
Cdd:cd01492     83 RLRALNPRVKVSVDTDDISEkpeEFFSQFDVVVATELSRAELVKINELCRKLGVKFYATGVHGLFGFVFAD 153
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 449-631 1.19e-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: 132.22  E-value: 1.19e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  449 RYDGQVAV--FGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGcgedgEITVTDMDTIEKSNLNRQFLFRPWDITKL 526
Cdd:cd00757      1 RYSRQILLpeIGEEGQEKLKNARVLVVGAGGLGSPAAEYLAAAGVG-----KLGLVDDDVVELSNLQRQILHTEADVGQP 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  527 KSETAAAAVRDINPHIRIFSHQNRVGPETEHvyddDFFQKLDGVANALDNVDARLYVDRRCVYYRKPLLESGTLGTKGNV 606
Cdd:cd00757     76 KAEAAAERLRAINPDVEIEAYNERLDAENAE----ELIAGYDLVLDCTDNFATRYLINDACVKLGKPLVSGAVLGFEGQV 151

                          170       180
                   ....*....|....*....|....*.
gi 1261214665  607 QVVVPFLTESYSSS-QDPPEKSIPIC 631
Cdd:cd00757    152 TVFIPGEGPCYRCLfPEPPPPGVPSC 177
E1_4HB pfam16191
Ubiquitin-activating enzyme E1 four-helix bundle; This domain is found in the ...
 296-365 2.18e-34

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


Pssm-ID: 465055  Cd Length: 70  Bit Score: 125.65  E-value: 2.18e-34
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  296 VPRKINFKPLLASLAEPEFVVTDFAKCCHPAQLHIGFQALHQFCTQHSRPPRPHNEEDAEELVTLAQSVN 365
Cdd:pfam16191    1 MPKTLSFKSLEESLKEPEFLISDFAKFDRPAQLHLAFQALHAFQEKHGRLPRPWNEEDAEEVVKLAKELN 70
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 449-611 3.65e-34

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: 131.40  E-value: 3.65e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  449 RYDGQVAV--FGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGcgedgEITVTDMDTIEKSNLNRQFLFRPWDITKL 526
Cdd:COG0476      7 RYSRQILLpeIGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVG-----TLTLVDDDVVELSNLQRQILYTEADVGRP 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  527 KSETAAAAVRDINPHIRIFSHQNRVGPETEhvydDDFFQKLDGVANALDNVDARLYVDRRCVYYRKPLLESGTLGTKGNV 606
Cdd:COG0476     82 KVEAAAERLRALNPDVEVEAIPERLTEENA----LELLAGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIGFEGQV 157


                   ....*
gi 1261214665  607 QVVVP 611
Cdd:COG0476    158 TVFIP 162
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 471-609 3.81e-32

Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes classical ubiquitin-activating enzymes E1, ubiquitin-like (ubl) activating enzymes and other mechanistic homologes, like MoeB, Thif1 and others. The common reaction mechanism catalyzed by MoeB, ThiF and the E1 enzymes begins with a nucleophilic attack of the C-terminal carboxylate of MoaD, ThiS and ubiquitin, respectively, on the alpha-phosphate of an ATP molecule bound at the active site of the activating enzymes, leading to the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of MoaD and ThiS.


Pssm-ID: 238760 [Multi-domain]  Cd Length: 143  Bit Score: 121.99  E-value: 3.81e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  471 FLVGAGAIGCELLKNFAMIGLGcgedgEITVTDMDTIEKSNLNRQFLFRPWDITKLKSETAAAAVRDINPHIRIFSHQNR 550
Cdd:cd01483      3 LLVGLGGLGSEIALNLARSGVG-----KITLIDFDTVELSNLNRQFLARQADIGKPKAEVAARRLNELNPGVNVTAVPEG 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1261214665  551 VGPETehvyDDDFFQKLDGVANALDNVDARLYVDRRCVYYRKPLLESGTLGTKGNVQVV 609
Cdd:cd01483     78 ISEDN----LDDFLDGVDLVIDAIDNIAVRRALNRACKELGIPVIDAGGLGLGGDIQVI 132
APPBP1_RUB cd01493
Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric ...
 54-195 4.25e-22

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: 100.46  E-value: 4.25e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665   54 YSRQLYVLGHEAMKHLQASSVLISGLQGLGVEIAKNIILGGVKAVTLHDQGIAQWADLSSQFCLREEDIGKNRAEISQPR 133
Cdd:cd01493      3 YDRQLRLWGEHGQAALESAHVCLLNATATGTEILKNLVLPGIGSFTIVDGSKVDEEDLGNNFFLDASSLGKSRAEATCEL 82

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1261214665  134 LAELNSYVpvfayTGPLIEE-----------FLSGFQVVVLTNTPLEYQLQVGEFCHSHGIKLVVADTRGLVG 195
Cdd:cd01493     83 LQELNPDV-----NGSAVEEspealldndpsFFSQFTVVIATNLPESTLLRLADVLWSANIPLLYVRSYGLYG 150
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 449-598 7.17e-21

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 92.99  E-value: 7.17e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  449 RYDGQVAV--FGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGcgedgEITVTDMDTIEKSNLNRQFLFRPWDITKL 526
Cdd:PRK05690    12 RYNRQIILrgFDFDGQEKLKAARVLVVGLGGLGCAASQYLAAAGVG-----TLTLVDFDTVSLSNLQRQVLHDDATIGQP 86

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1261214665  527 KSETAAAAVRDINPHIRIFSHQNRVgpetehvyDDDFFQKL----DGVANALDNVDARLYVDRRCVYYRKPLLeSG 598
Cdd:PRK05690    87 KVESARAALARINPHIAIETINARL--------DDDELAALiaghDLVLDCTDNVATRNQLNRACFAAKKPLV-SG 153
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 74-197 4.34e-17

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: 78.85  E-value: 4.34e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665   74 VLISGLQGLGVEIAKNIILGGVKAVTLHDQGIAQWADLSSQFCLREEDIGKNRAEISQPRLAELNSYV---PVFAYTGP- 149
Cdd:cd01483      2 VLLVGLGGLGSEIALNLARSGVGKITLIDFDTVELSNLNRQFLARQADIGKPKAEVAARRLNELNPGVnvtAVPEGISEd 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1261214665  150 LIEEFLSGFQVVVLTNTPLEYQLQVGEFCHSHGIKLVVADTRGLVGQL 197
Cdd:cd01483     82 NLDDFLDGVDLVIDAIDNIAVRRALNRACKELGIPVIDAGGLGLGGDI 129
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
458-611 2.45e-16

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 81.98  E-value: 2.45e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  458 GSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGcgedgEITVTDMDTIEKSNLNRQFLFRPWDITKLKSETAAAAVRD 537
Cdd:PRK08762   126 GEEGQRRLLEARVLLIGAGGLGSPAALYLAAAGVG-----TLGIVDHDVVDRSNLQRQILHTEDRVGQPKVDSAAQRLAA 200

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1261214665  538 INPHIRIFSHQNRVGPETEhvydDDFFQKLDGVANALDNVDARLYVDRRCVYYRKPLLESGTLGTKGNVQVVVP 611
Cdd:PRK08762   201 LNPDVQVEAVQERVTSDNV----EALLQDVDVVVDGADNFPTRYLLNDACVKLGKPLVYGAVFRFEGQVSVFDA 270
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 457-583 7.71e-16

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 80.69  E-value: 7.71e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  457 FGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGcgedgEITVTDMDTIEKSNLNRQFLFRPWDITKLKSETAAAAVR 536
Cdd:PRK05600    31 FGIEQQERLHNARVLVIGAGGLGCPAMQSLASAGVG-----TITLIDDDTVDVSNIHRQILFGASDVGRPKVEVAAERLK 105

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1261214665  537 DINPHIRIFSHQNRVGPETEHvyddDFFQKLDGVANALDNVDARLYV 583
Cdd:PRK05600   106 EIQPDIRVNALRERLTAENAV----ELLNGVDLVLDGSDSFATKFLV 148
PRK08328 PRK08328
hypothetical protein; Provisional
 54-197 8.06e-15

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 74.83  E-value: 8.06e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665   54 YSRQLYVLGHEAMKHLQASSVLISGLQGLGVEIAKNIILGGVKAVTLHDQGIAQWADLSSQFCLREEDIGKNRAEISQP- 132
Cdd:PRK08328    10 YDRQIMIFGVEGQEKLKKAKVAVVGVGGLGSPVAYYLAAAGVGRILLIDEQTPELSNLNRQILHWEEDLGKNPKPLSAKw 89

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1261214665  133 RLAELNSYVPVFAYTGPL----IEEFLSGFQVVV--LTNTPLEYQLQvgEFCHSHGIKLVVADTRGLVGQL 197
Cdd:PRK08328    90 KLERFNSDIKIETFVGRLseenIDEVLKGVDVIVdcLDNFETRYLLD--DYAHKKGIPLVHGAVEGTYGQV 158
PRK08328 PRK08328
hypothetical protein; Provisional
 449-616 1.13e-14

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 74.45  E-value: 1.13e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  449 RYDGQVAVFGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLgcgedGEITVTDMDTIEKSNLNRQFLFRPWDITK-LK 527
Cdd:PRK08328     9 RYDRQIMIFGVEGQEKLKKAKVAVVGVGGLGSPVAYYLAAAGV-----GRILLIDEQTPELSNLNRQILHWEEDLGKnPK 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  528 SETAAAAVRDINPHIRIFSHQNRVGPETEhvydDDFFQKLDGVANALDNVDARLYVDRRCVYYRKPLLESGTLGTKGNVQ 607
Cdd:PRK08328    84 PLSAKWKLERFNSDIKIETFVGRLSEENI----DEVLKGVDVIVDCLDNFETRYLLDDYAHKKGIPLVHGAVEGTYGQVT 159


                   ....*....
gi 1261214665  608 VVVPFLTES 616
Cdd:PRK08328   160 TIVPGKTKR 168
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 54-223 1.39e-14

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


Pssm-ID: 440244 [Multi-domain]  Cd Length: 244  Bit Score: 74.40  E-value: 1.39e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665   54 YSRQ--LYVLGHEAMKHLQASSVLISGLQGLGVEIAKNIILGGVKAVTLHDQGIAQWADLSSQFCLREEDIGKNRAEISQ 131
Cdd:COG0476      8 YSRQilLPEIGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADVGRPKVEAAA 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  132 PRLAELNSYVPVFAYTGPL----IEEFLSGFQVVV--LTNTPLEYQLQvgEFCHSHGIKLVVADTRGLVGQLF------- 198
Cdd:COG0476     88 ERLRALNPDVEVEAIPERLteenALELLAGADLVLdcTDNFATRYLLN--DACVKLGIPLVSGAVIGFEGQVTvfipgdt 165

                          170       180       190
                   ....*....|....*....|....*....|
gi 1261214665  199 ----CDFGEEMILTDSNGEQP-LSAMVSMI 223
Cdd:COG0476    166 pcyrCLFPEPPEPGPSCAEAGvLGPLVGVI 195
Aos1_SUMO cd01492
Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating ...
 450-604 2.01e-14

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: 73.09  E-value: 2.01e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  450 YDGQVAVFGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGcgedgEITVTDMDTIEKSNLNRQFLFRPWDITKLKSE 529
Cdd:cd01492      4 YDRQIRLWGLEAQKRLRSARILLIGLKGLGAEIAKNLVLSGIG-----SLTILDDRTVTEEDLGAQFLIPAEDLGQNRAE 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1261214665  530 TAAAAVRDINPHIrifshqnRVGPETEHV--YDDDFFQKLDGV-ANALDNvDARLYVDRRCVYYRKPLLESGTLGTKG 604
Cdd:cd01492     79 ASLERLRALNPRV-------KVSVDTDDIseKPEEFFSQFDVVvATELSR-AELVKINELCRKLGVKFYATGVHGLFG 148
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 54-197 2.57e-13

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: 70.58  E-value: 2.57e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665   54 YSRQLYV--LGHEAMKHLQASSVLISGLQGLGVEIAKNIILGGVKAVTLHDQGIAQWADLSSQFCLREEDIGKNRAEISQ 131
Cdd:cd00757      2 YSRQILLpeIGEEGQEKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRQILHTEADVGQPKAEAAA 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1261214665  132 PRLAELNSYVPVFAY----TGPLIEEFLSGFQVVV--LTNTPLEYQLQvgEFCHSHGIKLVVADTRGLVGQL 197
Cdd:cd00757     82 ERLRAINPDVEIEAYnerlDAENAEELIAGYDLVLdcTDNFATRYLIN--DACVKLGKPLVSGAVLGFEGQV 151
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 458-593 3.90e-13

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 72.43  E-value: 3.90e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  458 GSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGCgedgeITVTDMDTIEKSNLNRQFLFRPWDITKLKSETAAAAVRD 537
Cdd:PRK07878    33 GVDGQKRLKNARVLVIGAGGLGSPTLLYLAAAGVGT-----LGIVEFDVVDESNLQRQVIHGQSDVGRSKAQSARDSIVE 107

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1261214665  538 INPHIRIFSHQNRVGPETEHvyddDFFQKLDGVANALDNVDARLYVDRRCVYYRKP 593
Cdd:PRK07878   108 INPLVNVRLHEFRLDPSNAV----ELFSQYDLILDGTDNFATRYLVNDAAVLAGKP 159
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
 457-603 5.42e-13

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: 69.56  E-value: 5.42e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  457 FGSDLQEKLGKQKYFLVGAGAIGcellkNFAMIGL---GCGEdgeITVTDMDTIEKSNLNRQFLFRPWDITKLKSETAAA 533
Cdd:cd00755      1 YGEEGLEKLRNAHVAVVGLGGVG-----SWAAEALarsGVGK---LTLIDFDVVCVSNLNRQIHALLSTVGKPKVEVMAE 72

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  534 AVRDINPHIRIFSHQNRVGPETEHVYdddFFQKLDGVANALDNVDARLYVDRRCVYYRKPLLESGTLGTK 603
Cdd:cd00755     73 RIRDINPECEVDAVEEFLTPDNSEDL---LGGDPDFVVDAIDSIRAKVALIAYCRKRKIPVISSMGAGGK 139
TcdA COG1179
tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ...
 472-598 2.09e-12

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: 68.18  E-value: 2.09e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  472 LVGAGAIgcELLKN--FAMIGLG-----CGED------GEITVTDMDTIEKSNLNRQflfrpwdI-----T--KLKSETA 531
Cdd:COG1179     13 LYGEEGL--ERLANahVAVVGLGgvgswAAEAlarsgvGRLTLVDLDDVCESNINRQ-------LhaldsTvgRPKVEVM 83

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1261214665  532 AAAVRDINPHIRIFSHQNRVGPETehvYDDDFFQKLDGVANALDNVDARLYVDRRCVYYRKPLLESG 598
Cdd:COG1179     84 AERIRDINPDCEVTAIDEFVTPEN---ADELLSEDYDYVIDAIDSVSAKAALIAWCRRRGIPIISSM 147
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 446-611 2.50e-12

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 69.25  E-value: 2.50e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  446 HQNRYDGQV--AVFGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGcgedgEITVTDMDTIEKSNLNRQFLFRPWDI 523
Cdd:PRK07688     1 MNERYSRQElfSPIGEEGQQKLREKHVLIIGAGALGTANAEMLVRAGVG-----KVTIVDRDYVEWSNLQRQQLYTESDV 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  524 TKLKSETAAAAVR--DINPHIRIFSHQNRVGPETEhvydDDFFQKLDGVANALDNVDARLYVDRRCVYYRKPLLESGTLG 601
Cdd:PRK07688    76 KNNLPKAVAAKKRleEINSDVRVEAIVQDVTAEEL----EELVTGVDLIIDATDNFETRFIVNDAAQKYGIPWIYGACVG 151

                          170
                   ....*....|
gi 1261214665  602 TKGNVQVVVP 611
Cdd:PRK07688   152 SYGLSYTIIP 161
E1-1_like cd01485
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ...
 450-570 4.11e-12

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: 66.29  E-value: 4.11e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  450 YDGQVAVFGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLgcgedGEITVTDMDTIEKSNLNRQFLFRPW--DITKLK 527
Cdd:cd01485      2 YDRQIRLWGDEAQNKLRSAKVLIIGAGALGAEIAKNLVLAGI-----DSITIVDHRLVSTEDLGSNFFLDAEvsNSGMNR 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1261214665  528 SETAAAAVRDINPHIRIFSHQNRvgPETEHVYDDDFFQKLDGV 570
Cdd:cd01485     77 AAASYEFLQELNPNVKLSIVEED--SLSNDSNIEEYLQKFTLV 117
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 447-637 1.59e-11

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 67.06  E-value: 1.59e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  447 QNRYDGQVAV--FGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGcgedgEITVTDMDTIEKSNLNRQFLFRPWDIT 524
Cdd:PRK12475     2 QERYSRQILFsgIGEEGQRKIREKHVLIVGAGALGAANAEALVRAGIG-----KLTIADRDYVEWSNLQRQQLYTEEDAK 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  525 KLKSETAAAA--VRDINPHIRIFSHQNRVGPETEhvydDDFFQKLDGVANALDNVDARLYVDRRCVYYRKPLLESGTLGT 602
Cdd:PRK12475    77 QKKPKAIAAKehLRKINSEVEIVPVVTDVTVEEL----EELVKEVDLIIDATDNFDTRLLINDLSQKYNIPWIYGGCVGS 152

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1261214665  603 KGNVQVVVPFLTESYSssqdppeksipiCTLKNFP 637
Cdd:PRK12475   153 YGVTYTIIPGKTPCLR------------CLMEHVP 175
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
450-579 4.61e-11

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 63.34  E-value: 4.61e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  450 YDGQVAVFGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGcgedgEITVTDMDTIEKSNLNRQFLFrPWDITKLKSE 529
Cdd:PRK08644    11 EAMLASRHTPKLLEKLKKAKVGIAGAGGLGSNIAVALARSGVG-----NLKLVDFDVVEPSNLNRQQYF-ISQIGMPKVE 84

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1261214665  530 TAAAAVRDINPHIRIFSHQNRVGPETEHvyddDFFQKLDGVANALDNVDA 579
Cdd:PRK08644    85 ALKENLLEINPFVEIEAHNEKIDEDNIE----ELFKDCDIVVEAFDNAET 130
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 449-580 2.13e-10

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 63.74  E-value: 2.13e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  449 RYDGQVAV--FGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGcgedgEITVTDMDTIEKSNLNRQFLFRPWDITKL 526
Cdd:PRK05597     8 RYRRQIMLgeIGQQGQQSLFDAKVAVIGAGGLGSPALLYLAGAGVG-----HITIIDDDTVDLSNLHRQVIHSTAGVGQP 82

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1261214665  527 KSETAAAAVRDINPHIRIFSHQNRVGPETEHvyddDFFQKLDGVANALDNVDAR 580
Cdd:PRK05597    83 KAESAREAMLALNPDVKVTVSVRRLTWSNAL----DELRDADVILDGSDNFDTR 132
E1_ThiF_like cd01487
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ...
 472-580 3.41e-09

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: 57.39  E-value: 3.41e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  472 LVGAGAIGCELLKNFAMIGLGcgedgEITVTDMDTIEKSNLNRQFlFRPWDITKLKSETAAAAVRDINPHIRIFSHQNRV 551
Cdd:cd01487      4 IAGAGGLGSNIAVLLARSGVG-----NLKLVDFDVVEPSNLNRQQ-YFLSQIGEPKVEALKENLREINPFVKIEAINIKI 77

                           90       100
                   ....*....|....*....|....*....
gi 1261214665  552 gpETEHVYddDFFQKLDGVANALDNVDAR 580
Cdd:cd01487     78 --DENNLE--GLFGDCDIVVEAFDNAETK 102
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
458-593 1.57e-08

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 58.21  E-value: 1.57e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  458 GSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGcgedgEITVTDMDTIEKSNLNRQFLFRPWDITKLKSETAAAAVRD 537
Cdd:PRK07411    29 GLEGQKRLKAASVLCIGTGGLGSPLLLYLAAAGIG-----RIGIVDFDVVDSSNLQRQVIHGTSWVGKPKIESAKNRILE 103

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1261214665  538 INPHIRIFSHQNRVGPETEHvyddDFFQKLDGVANALDNVDARLYVDRRCVYYRKP 593
Cdd:PRK07411   104 INPYCQVDLYETRLSSENAL----DILAPYDVVVDGTDNFPTRYLVNDACVLLNKP 155
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 73-163 5.98e-08

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: 55.44  E-value: 5.98e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665   73 SVLISGLQGLGVEIAKNIILGGVKAVTLHDQGIAQWADLSSQFCLREEDIGKNRAEISQPRLAELNSYVPVFAYTGPLI- 151
Cdd:cd01488      1 KILVIGAGGLGCELLKNLALSGFRNIHVIDMDTIDVSNLNRQFLFREKDIGKPKAEVAAKFVNDRVPGVNVTPHFGKIQd 80

                           90
                   ....*....|....
gi 1261214665  152 --EEFLSGFQVVVL 163
Cdd:cd01488     81 kdEEFYRQFNIIIC 94
PRK08223 PRK08223
hypothetical protein; Validated
 462-611 2.49e-07

hypothetical protein; Validated


Pssm-ID: 181302 [Multi-domain]  Cd Length: 287  Bit Score: 53.53  E-value: 2.49e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  462 QEKLGKQKYFLVGAGAIGCELLKNFAMIGLGCgedgeITVTDMDTIEKSNLNRQF------LFRPwditklKSETAAAAV 535
Cdd:PRK08223    22 QQRLRNSRVAIAGLGGVGGIHLLTLARLGIGK-----FTIADFDVFELRNFNRQAgammstLGRP------KAEVLAEMV 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  536 RDINPHIRIFSHQNRVGPETEhvydDDFfqkLDGVANALDNVDARLYVDRRCVY---YRK--PLLESGTLGTKGNVQVVV 610
Cdd:PRK08223    91 RDINPELEIRAFPEGIGKENA----DAF---LDGVDVYVDGLDFFEFDARRLVFaacQQRgiPALTAAPLGMGTALLVFD 163


                   .
gi 1261214665  611 P 611
Cdd:PRK08223   164 P 164
APPBP1_RUB cd01493
Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric ...
 449-642 2.50e-07

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: 54.23  E-value: 2.50e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  449 RYDGQVAVFGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLgcgedGEITVTDMDTIEKSNLNRQFLFRPWDITKLKS 528
Cdd:cd01493      2 KYDRQLRLWGEHGQAALESAHVCLLNATATGTEILKNLVLPGI-----GSFTIVDGSKVDEEDLGNNFFLDASSLGKSRA 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  529 ETAAAAVRDINPHIRI-FSHQNrvgPETEHVYDDDFFQKLDGV--ANALDNVDARLyvDRRCVYYRKPLLESGTLGTKGN 605
Cdd:cd01493     77 EATCELLQELNPDVNGsAVEES---PEALLDNDPSFFSQFTVViaTNLPESTLLRL--ADVLWSANIPLLYVRSYGLYGY 151

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1261214665  606 VQVVVPFLT--ESYsssqdpPEKSIPICTLKN-FPNAIEH 642
Cdd:cd01493    152 IRIQLKEHTivESH------PDNALEDLRLDNpFPELREH 185
PTZ00245 PTZ00245
ubiquitin activating enzyme; Provisional
 54-144 2.88e-07

ubiquitin activating enzyme; Provisional


Pssm-ID: 140272  Cd Length: 287  Bit Score: 53.52  E-value: 2.88e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665   54 YSRQLYVLGHEAMKHLQASSVLISGLQGLGVEIAKNIILGGVKAVTLHDQGIAQWADLSSQFCLREEDiGKNRAEISQPR 133
Cdd:PTZ00245     9 YDRQIRLWGKSTQQQLMHTSVALHGVAGAAAEAAKNLVLAGVRAVAVADEGLVTDADVCTNYLMQGEA-GGTRGARALGA 87

                           90
                   ....*....|.
gi 1261214665  134 LAELNSYVPVF 144
Cdd:PTZ00245    88 LQRLNPHVSVY 98
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 54-186 6.44e-07

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 51.77  E-value: 6.44e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665   54 YSRQLyVL------GHEAMKhlqASSVLISGLQGLGVEIAKNIILGGVKAVTLHDQGIAQWADLSSQFCLREEDIGKNRA 127
Cdd:PRK05690    13 YNRQI-ILrgfdfdGQEKLK---AARVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVSLSNLQRQVLHDDATIGQPKV 88

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1261214665  128 EISQPRLAELNSYVPVFAYTGPL----IEEFLSGFQVVVLTNTPLEYQLQVGEFCHSHGIKLV 186
Cdd:PRK05690    89 ESARAALARINPHIAIETINARLdddeLAALIAGHDLVLDCTDNVATRNQLNRACFAAKKPLV 151
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 54-183 1.79e-06

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 51.15  E-value: 1.79e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665   54 YSRQLYV--LGHEAMKHLQASSVLISGLQGLGVEIAKNIILGGVKAVTLHDQGIAQWADLSSQFCLREEDIGKN--RAEI 129
Cdd:PRK07688     5 YSRQELFspIGEEGQQKLREKHVLIIGAGALGTANAEMLVRAGVGKVTIVDRDYVEWSNLQRQQLYTESDVKNNlpKAVA 84

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1261214665  130 SQPRLAELNSYVPVFAY----TGPLIEEFLSGFQVVVLTNTPLEYQLQVGEFCHSHGI 183
Cdd:PRK07688    85 AKKRLEEINSDVRVEAIvqdvTAEELEELVTGVDLIIDATDNFETRFIVNDAAQKYGI 142
Ube1_repeat1 cd01491
Ubiquitin activating enzyme (E1), repeat 1. E1, a highly conserved small protein present ...
 450-549 3.40e-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: 49.96  E-value: 3.40e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  450 YDGQVAVFGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLgcgedGEITVTDMDTIEKSNLNRQFLFRPWDITKLKSE 529
Cdd:cd01491      2 YSRQLYVLGHEAMKKLQKSNVLISGLGGLGVEIAKNLILAGV-----KSVTLHDTKPCSWSDLSSQFYLREEDIGKNRAE 76

                           90       100
                   ....*....|....*....|
gi 1261214665  530 TAAAAVRDINPHIRIFSHQN 549
Cdd:cd01491     77 ASQARLAELNPYVPVTVSTG 96
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 74-197 3.40e-06

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


Pssm-ID: 238766 [Multi-domain]  Cd Length: 312  Bit Score: 50.07  E-value: 3.40e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665   74 VLISGLQGLGVEIAKNIILGGVKAVTLHDQGIAQWADLSSQFCLREEDIGKNRAEISQPRLAELNSYVPVFAYTGPLIE- 152
Cdd:cd01489      2 VLVVGAGGIGCELLKNLVLTGFGEIHIIDLDTIDLSNLNRQFLFRKKHVGKSKAQVAKEAVLSFNPNVKIVAYHANIKDp 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1261214665  153 ----EFLSGFQVVV--LTNtpLEYQLQVGEFCHSHGIKLVVADTRGLVGQL 197
Cdd:cd01489     82 dfnvEFFKQFDLVFnaLDN--LAARRHVNKMCLAADVPLIESGTTGFLGQV 130
PRK15116 PRK15116
sulfur acceptor protein CsdL; Provisional
 449-601 5.12e-06

sulfur acceptor protein CsdL; Provisional


Pssm-ID: 185071  Cd Length: 268  Bit Score: 49.42  E-value: 5.12e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  449 RYDGQVAVFGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGCgedgeITVTDMDTIEKSNLNRQFLFRPWDITKLKS 528
Cdd:PRK15116    12 RFGGTARLYGEKALQLFADAHICVVGIGGVGSWAAEALARTGIGA-----ITLIDMDDVCVTNTNRQIHALRDNVGLAKA 86

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1261214665  529 ETAAAAVRDINPHIRIFSHQNRVGPETEHVYDDDFFqklDGVANALDNVDARLYVDRRCVYYRKPLLESGTLG 601
Cdd:PRK15116    87 EVMAERIRQINPECRVTVVDDFITPDNVAEYMSAGF---SYVIDAIDSVRPKAALIAYCRRNKIPLVTTGGAG 156
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
 73-195 7.99e-06

Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present universally in eukaryotic cells, is part of cascade to attach ubiquitin (Ub) covalently to substrate proteins. This cascade consists of activating (E1), conjugating (E2), and/or ligating (E3) enzymes and then targets them for degradation by the 26S proteasome. E1 activates ubiquitin by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and ubiquitin's C-terminus. E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. A set of novel molecules with a structural similarity to Ub, called Ub-like proteins (Ubls), have similar conjugation cascades. In contrast to ubiquitin-E1, which is a single-chain protein with a weakly conserved two-fold repeat, many of the Ubls-E1are a heterodimer where each subunit corresponds to one half of a single-chain E1. This CD represents the family homologous to the second repeat of Ub-E1.


Pssm-ID: 238761 [Multi-domain]  Cd Length: 234  Bit Score: 48.34  E-value: 7.99e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665   73 SVLISGLQGLGVEIAKNIILGGVKAVTLHDQGIAQWADLSSQFCLREEDIGKNRAEISQPRLAELN---SYVPVFAYTGP 149
Cdd:cd01484      1 KVLLVGAGGIGCELLKNLALMGFGQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKSEVAAEAVNDRNpncKVVPYQNKVGP 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1261214665  150 LI---EEFLSGFQVVVLTNTPLEYQLQVGEFCHSHGIKLVVADTRGLVG 195
Cdd:cd01484     81 EQdfnDTFFEQFHIIVNALDNIIARRYVNGMLIFLIVPLIESGTEGFKG 129
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 54-183 4.13e-05

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 47.03  E-value: 4.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665   54 YSRQLYV--LGHEAMKHLQASSVLISGLQGLGVEIAKNIILGGVKAVTLHDQGIAQWADLSSQFCLREEDIG--KNRAEI 129
Cdd:PRK12475     5 YSRQILFsgIGEEGQRKIREKHVLIVGAGALGAANAEALVRAGIGKLTIADRDYVEWSNLQRQQLYTEEDAKqkKPKAIA 84

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1261214665  130 SQPRLAELNSYVPVFAY----TGPLIEEFLSGFQVVVLTNTPLEYQLQVGEFCHSHGI 183
Cdd:PRK12475    85 AKEHLRKINSEVEIVPVvtdvTVEELEELVKEVDLIIDATDNFDTRLLINDLSQKYNI 142
Apg7 cd01486
Apg7 is an E1-like protein, that activates two different ubiquitin-like proteins, Apg12 and ...
 469-542 7.10e-05

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: 46.21  E-value: 7.10e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1261214665  469 KYFLVGAGAIGCellkNFAMIGLGCGEDgEITVTDMDTIEKSNLNRQFLFRPWDIT--KLKSETAAAAVRDINPHI 542
Cdd:cd01486      1 KCLLLGAGTLGC----NVARNLLGWGVR-HITFVDSGKVSYSNPVRQSLFTFEDCKggKPKAEAAAERLKEIFPSI 71
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
31-197 8.14e-05

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 46.16  E-value: 8.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665   31 FGVPPGPTNEmsknkemdiDESLYSRQLYV--LGHEAMKHLQASSVLISGLQGLGVEIAKNIILGGVKAVTLHDQGIAQW 108
Cdd:PRK08762   102 LERPRLLTDE---------QDERYSRHLRLpeVGEEGQRRLLEARVLLIGAGGLGSPAALYLAAAGVGTLGIVDHDVVDR 172

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  109 ADLSSQFCLREEDIGKNRAEISQPRLAELNSYVPVFAY----TGPLIEEFLSGFQVVV--LTNTPLEYqlQVGEFCHSHG 182
Cdd:PRK08762   173 SNLQRQILHTEDRVGQPKVDSAAQRLAALNPDVQVEAVqervTSDNVEALLQDVDVVVdgADNFPTRY--LLNDACVKLG 250

                          170
                   ....*....|....*
gi 1261214665  183 IKLVVADTRGLVGQL 197
Cdd:PRK08762   251 KPLVYGAVFRFEGQV 265
PRK14851 PRK14851
hypothetical protein; Provisional
 446-611 2.20e-04

hypothetical protein; Provisional


Pssm-ID: 184853 [Multi-domain]  Cd Length: 679  Bit Score: 45.24  E-value: 2.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  446 HQNRYDGQVAVFGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGcgedgEITVTDMDTIEKSNLNRQFLFRPWDITK 525
Cdd:PRK14851    22 REAAFSRNIGLFTPGEQERLAEAKVAIPGMGGVGGVHLITMVRTGIG-----RFHIADFDQFEPVNVNRQFGARVPSFGR 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  526 LKSETAAAAVRDINPHIRIFSHqnrvgPETEHVYDDDFFqkLDGVANALDNVDARLYVDRRCVYYRK-----PLLESGTL 600
Cdd:PRK14851    97 PKLAVMKEQALSINPFLEITPF-----PAGINADNMDAF--LDGVDVVLDGLDFFQFEIRRTLFNMArekgiPVITAGPL 169

                          170
                   ....*....|.
gi 1261214665  601 GTKGNVQVVVP 611
Cdd:PRK14851   170 GYSSAMLVFTP 180
PRK14852 PRK14852
hypothetical protein; Provisional
 462-611 3.83e-03

hypothetical protein; Provisional


Pssm-ID: 184854 [Multi-domain]  Cd Length: 989  Bit Score: 41.22  E-value: 3.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665  462 QEKLGKQKYFLVGAGAIGCELLKNFAMIGLGcgedgEITVTDMDTIEKSNLNRQFLFRPWDITKLKSETAAAAVRDINPH 541
Cdd:PRK14852   327 QRRLLRSRVAIAGLGGVGGIHLMTLARTGIG-----NFNLADFDAYSPVNLNRQYGASIASFGRGKLDVMTERALSVNPF 401

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1261214665  542 IRIFSHQNRVGPETehvyDDDFFQKLDGVANALD--NVDARLYVDRRCVYYRKPLLESGTLGTKGNVQVVVP 611
Cdd:PRK14852   402 LDIRSFPEGVAAET----IDAFLKDVDLLVDGIDffALDIRRRLFNRALELGIPVITAGPLGYSCALLVFMP 469
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
 73-162 3.84e-03

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: 41.12  E-value: 3.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665   73 SVLISGLQGLGVEIAKNIILGGVKA-----VTLHDQGIAQWADLSSQFCLREEDIGKNRAEISQPRLAELNSYVPVFAYT 147
Cdd:cd01490      1 KVFLVGAGAIGCELLKNFALMGVGTgesgeITVTDMDNIEKSNLNRQFLFRPHDVGKPKSEVAAAAVKAMNPDLKITALQ 80

                           90       100
                   ....*....|....*....|...
gi 1261214665  148 ---GPLIE-----EFLSGFQVVV 162
Cdd:cd01490     81 nrvGPETEhifndEFWEKLDGVA 103
E1_ThiF_like cd01487
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ...
 73-162 4.14e-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: 39.29  E-value: 4.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261214665   73 SVLISGLQGLGVEIAKNIILGGVKAVTLHDQGIAQWADLSSQFcLREEDIGKNRAEISQPRLAELNSYVPVFAYTGPL-- 150
Cdd:cd01487      1 KVGIAGAGGLGSNIAVLLARSGVGNLKLVDFDVVEPSNLNRQQ-YFLSQIGEPKVEALKENLREINPFVKIEAINIKIde 79

                           90
                   ....*....|....
gi 1261214665  151 --IEEFLSGFQVVV 162
Cdd:cd01487     80 nnLEGLFGDCDIVV 93
 
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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