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Conserved domains on  [gi|2098122732|ref|XP_043661511|]
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LOW QUALITY PROTEIN: ubiquitin-like modifier-activating enzyme 1 [Drosophila teissieri]

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 ...
 31-968 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: 1143.47  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732   31 VLQLHDLSSQFYLTEADIGKNRAEASCAQLAELNSYVRTVSHTGPLTEEFLRKFRVVVLTNSDGEEQQRIGKFAHEN--G 108
Cdd:TIGR01408   58 KCQAWDLSSNFFLSEDDVGRNRAEAVVKKLAELNPYVHVSSSSVPFNEEFLDKFQCVVLTEMSLPLQKEINDFCHSQcpP 137

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732  109 IALIIAETRGLFAKVFCDFGESFTIYDQDGTQPISTMIASITHDAQGVVTCLDETRHGFNDGDYVTFSEVQGMQELNGCQ 188
Cdd:TIGR01408  138 IAFISADVRGLFGSLFCDFGDEFEVLDTDGEEPKTGFIASITQANPGIVTCLENHRHKLETGDFVTFREVNGMTGLNDGS 217

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732  189 PLKITVLGPYTFSIGDTSKFGEYKSGGVATQVKMPKTISFKSLAQASEEPEFLISDFAKLDSPATLHVAFNALSCYRKAH 268
Cdd:TIGR01408  218 PRKITVISPYSFSIGDTTELGPYLHGGIATQVKTPKTVFFKSLREQLKDPKCLIVDFSKPERPPEIHTAFQALDQFQEKY 297

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732  269 nGVLPRPWNEEDANSFLEVVRASSSA------EVDEKLVLQFAKICSGNTCPLDAAVGGIVAQEVLKACSGKFTPIYQWL 342
Cdd:TIGR01408  298 -SRKPNVGCQQDAEELLKLATSISETleekvpDVDAKLVHWLSWTAQGFLSPMAAAVGGVVSQEVLKAVTGKFSPLCQWF 376

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732  343 YFDALECLPTEG-VEEADAQPVGSRYDSQIAIFGKKFQEKLADSKWFIVGAGAIGCELLKNFGMLGLGTG-KGQIFVTDM 420
Cdd:TIGR01408  377 YFDSAESLPSLGkPECEEFLPRGDRYDAQIAVFGDTFQQKLQNLNIFLVGCGAIGCEMLKNFALMGVGTGkKGMITVTDP 456

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732  421 DLIEKSNLNRQFLFRPHDVQKPKSMTAADAIKRMNPEVNVTAYELRVGAETEKVFSEDFFGKLDGVANALDNVDARIYMD 500
Cdd:TIGR01408  457 DLIEKSNLNRQFLFRPHHIGKPKSYTAADATLKINPQIKIDAHQNRVGPETETIFNDEFYEKLDVVINALDNVEARRYVD 536

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732  501 RKCIFNRIPLVETGTLGTLGNVQVIVPFATESYSSSQD*PEKSIPICTLKNFPNAIEHTLQWARDAFEGVFKQSAENAAQ 580
Cdd:TIGR01408  537 SRCLAFLKPLLESGTLGTKGNTQVVVPHLTESYGSSRDPPEKEIPFCTLKSFPAAIEHTIQWARDKFEGLFSHKPSLVNK 616

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732  581 YIADP-QFTERIAKLPGIQPLDILDSIKKALIDDKPKSFAHCVEWARLYWEDQYVNQIKQLLFNFPPDQITSSGQPFWSG 659
Cdd:TIGR01408  617 YLSSPsSAEEVLQKIQSGHSREGLEQIIKLLSKEKPRNFSQCVEWARLKFEKYFNNKALQLLHCFPLDIRTSTGSPFWSS 696

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732  660 PKRCPDPLVFDVNDPMHLDFIYAGANLRAEVYGI---EQVRNRETIAELVQKVKVPEFKPRSGVKIETNEAAAAASANNF 736
Cdd:TIGR01408  697 PKRPPSPLKFDLNEPLHLSFIQAAAKLYATVYGIpfaEEDLSADALLNILSEVKIPEFKPRSNKKIQTDETARKPDTAPI 776

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732  737 DdgelDQDRVDKIISELLKNADKTS--KITPLEFEKDDDSNLHMDFIVACSNLRAANYKISPADRHKSKLIAGKIIPAIA 814
Cdd:TIGR01408  777 D----DRNAIFQLEKAILSNEATKSdfRMAPLSFEKDDDHNGHIDFITAASNLRAKNYSIEPADRFKTKFIAGKIIPAIA 852

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732  815 TTTSVLSGLAVLEVIKLIVGHRDLVKFKNGFANLALPFMAFSEPVPAAKNTYYGKEW-TLWDRFEVTGELSLQEFLNYFE 893
Cdd:TIGR01408  853 TSTATVSGLVCLELIKVTDGGYKFEVYKNCFLNLAIPLFVFTEPTEVRKTKIRNGISfTIWDRWTLHGDFTLLEFINAVK 932

                          890       900       910       920       930       940       950
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2098122732  894 ENEKLKITMLSQGVSMLYSFFMPKAKcsERLPLPMSEVVRRVSKRRLEPHERSLVFEICCNDVDGEDVEVPYVRY 968
Cdd:TIGR01408  933 EKYGLEPTMVSQGVKLLYVPVMPGHA--ERLKLKMHKLVKPTTKKKLPPYRVHLTVSFACDDDGDEDVPGPPVRI 1005
 
Name Accession Description Interval E-value
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 31-968 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: 1143.47  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732   31 VLQLHDLSSQFYLTEADIGKNRAEASCAQLAELNSYVRTVSHTGPLTEEFLRKFRVVVLTNSDGEEQQRIGKFAHEN--G 108
Cdd:TIGR01408   58 KCQAWDLSSNFFLSEDDVGRNRAEAVVKKLAELNPYVHVSSSSVPFNEEFLDKFQCVVLTEMSLPLQKEINDFCHSQcpP 137

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732  109 IALIIAETRGLFAKVFCDFGESFTIYDQDGTQPISTMIASITHDAQGVVTCLDETRHGFNDGDYVTFSEVQGMQELNGCQ 188
Cdd:TIGR01408  138 IAFISADVRGLFGSLFCDFGDEFEVLDTDGEEPKTGFIASITQANPGIVTCLENHRHKLETGDFVTFREVNGMTGLNDGS 217

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732  189 PLKITVLGPYTFSIGDTSKFGEYKSGGVATQVKMPKTISFKSLAQASEEPEFLISDFAKLDSPATLHVAFNALSCYRKAH 268
Cdd:TIGR01408  218 PRKITVISPYSFSIGDTTELGPYLHGGIATQVKTPKTVFFKSLREQLKDPKCLIVDFSKPERPPEIHTAFQALDQFQEKY 297

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732  269 nGVLPRPWNEEDANSFLEVVRASSSA------EVDEKLVLQFAKICSGNTCPLDAAVGGIVAQEVLKACSGKFTPIYQWL 342
Cdd:TIGR01408  298 -SRKPNVGCQQDAEELLKLATSISETleekvpDVDAKLVHWLSWTAQGFLSPMAAAVGGVVSQEVLKAVTGKFSPLCQWF 376

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732  343 YFDALECLPTEG-VEEADAQPVGSRYDSQIAIFGKKFQEKLADSKWFIVGAGAIGCELLKNFGMLGLGTG-KGQIFVTDM 420
Cdd:TIGR01408  377 YFDSAESLPSLGkPECEEFLPRGDRYDAQIAVFGDTFQQKLQNLNIFLVGCGAIGCEMLKNFALMGVGTGkKGMITVTDP 456

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732  421 DLIEKSNLNRQFLFRPHDVQKPKSMTAADAIKRMNPEVNVTAYELRVGAETEKVFSEDFFGKLDGVANALDNVDARIYMD 500
Cdd:TIGR01408  457 DLIEKSNLNRQFLFRPHHIGKPKSYTAADATLKINPQIKIDAHQNRVGPETETIFNDEFYEKLDVVINALDNVEARRYVD 536

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732  501 RKCIFNRIPLVETGTLGTLGNVQVIVPFATESYSSSQD*PEKSIPICTLKNFPNAIEHTLQWARDAFEGVFKQSAENAAQ 580
Cdd:TIGR01408  537 SRCLAFLKPLLESGTLGTKGNTQVVVPHLTESYGSSRDPPEKEIPFCTLKSFPAAIEHTIQWARDKFEGLFSHKPSLVNK 616

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732  581 YIADP-QFTERIAKLPGIQPLDILDSIKKALIDDKPKSFAHCVEWARLYWEDQYVNQIKQLLFNFPPDQITSSGQPFWSG 659
Cdd:TIGR01408  617 YLSSPsSAEEVLQKIQSGHSREGLEQIIKLLSKEKPRNFSQCVEWARLKFEKYFNNKALQLLHCFPLDIRTSTGSPFWSS 696

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732  660 PKRCPDPLVFDVNDPMHLDFIYAGANLRAEVYGI---EQVRNRETIAELVQKVKVPEFKPRSGVKIETNEAAAAASANNF 736
Cdd:TIGR01408  697 PKRPPSPLKFDLNEPLHLSFIQAAAKLYATVYGIpfaEEDLSADALLNILSEVKIPEFKPRSNKKIQTDETARKPDTAPI 776

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732  737 DdgelDQDRVDKIISELLKNADKTS--KITPLEFEKDDDSNLHMDFIVACSNLRAANYKISPADRHKSKLIAGKIIPAIA 814
Cdd:TIGR01408  777 D----DRNAIFQLEKAILSNEATKSdfRMAPLSFEKDDDHNGHIDFITAASNLRAKNYSIEPADRFKTKFIAGKIIPAIA 852

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732  815 TTTSVLSGLAVLEVIKLIVGHRDLVKFKNGFANLALPFMAFSEPVPAAKNTYYGKEW-TLWDRFEVTGELSLQEFLNYFE 893
Cdd:TIGR01408  853 TSTATVSGLVCLELIKVTDGGYKFEVYKNCFLNLAIPLFVFTEPTEVRKTKIRNGISfTIWDRWTLHGDFTLLEFINAVK 932

                          890       900       910       920       930       940       950
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2098122732  894 ENEKLKITMLSQGVSMLYSFFMPKAKcsERLPLPMSEVVRRVSKRRLEPHERSLVFEICCNDVDGEDVEVPYVRY 968
Cdd:TIGR01408  933 EKYGLEPTMVSQGVKLLYVPVMPGHA--ERLKLKMHKLVKPTTKKKLPPYRVHLTVSFACDDDGDEDVPGPPVRI 1005
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
 386-924 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: 794.57  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 386 KWFIVGAGAIGCELLKNFGMLGLGTG-KGQIFVTDMDLIEKSNLNRQFLFRPHDVQKPKSMTAADAIKRMNPEVNVTAYE 464
Cdd:cd01490     1 KVFLVGAGAIGCELLKNFALMGVGTGeSGEITVTDMDNIEKSNLNRQFLFRPHDVGKPKSEVAAAAVKAMNPDLKITALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 465 LRVGAETEKVFSEDFFGKLDGVANALDNVDARIYMDRKCIFNRIPLVETGTLGTLGNVQVIVPFATESYSSSQD*PEKSI 544
Cdd:cd01490    81 NRVGPETEHIFNDEFWEKLDGVANALDNVDARMYVDRRCVYYRKPLLESGTLGTKGNTQVVIPHLTESYSSSRDPPEKSI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 545 PICTLKNFPNAIEHTLQWARDAFEGVFKQSAENAAQYIadpqfteriaklpgiqpldildsikkaliddkpksFAHCVEW 624
Cdd:cd01490   161 PLCTLKNFPNAIEHTIQWARDEFEGLFKQPPENVNQYL-----------------------------------FEDCVRW 205

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 625 ARLYWEDQYVNQIKQLLFNFPPDQITSSGQPFWSGPKRCPDPLVFDVNDPMHLDFIYAGANLRAEVYGIEQvrnretiae 704
Cdd:cd01490   206 ARLLFEKYFNNNIKQLLHNFPPDAVTSDGAPFWSGPKRCPTPLEFDVNNPLHLDFVLAAANLYAEVYGIPG--------- 276

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 705 lvqkvkvpefkprsgvkietneaaaaasannfddgeldqdrvdkiisellknadktskitpleFEKDDDSNLHMDFIVAC 784
Cdd:cd01490   277 ---------------------------------------------------------------FEKDDDTNFHMDFITAA 293

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 785 SNLRAANYKISPADRHKSKLIAGKIIPAIATTTSVLSGLAVLEVIKLIVGHRDLVKFKNGFANLALPFMAFSEPVPAAKN 864
Cdd:cd01490   294 SNLRARNYSIPPADRHKTKRIAGKIIPAIATTTAAVTGLVCLELYKVVDGKRPLEAYKNAFLNLALPFFAFSEPIPAPKV 373

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2098122732 865 TY-YGKEWTLWDRFEVTGELSLQEFL-NYFEENEKLKITMLSQGVSMLYSFFMPKAKCSERL 924
Cdd:cd01490   374 KYaYDEEWTIWDRFEVKGKQTLQELLiDYFKEKYGLEVTMLSQGVSMLYSSFMPPAKLKERL 435
UBA_E1_SCCH pfam10585
Ubiquitin-activating enzyme, SCCH domain; Ubiquitin-activating enzyme (E1 enzyme) activates ...
 553-803 5.54e-133

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: 400.07  E-value: 5.54e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 553 PNAIEHTLQWARDAFEGVFKQSAENAAQYIADPQ-FTERIAKLPGIQPLDILDSIKKALIDDKPKSFAHCVEWARLYWED 631
Cdd:pfam10585   1 PNAIEHTIQWARDEFEGLFVQPPEEVNKYLQPPQnFIESLLKQGGGQKLETLESVRKSLVTERPKTFEDCVAWARLKFEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 632 QYVNQIKQLLFNFPPDQITSSGQPFWSGPKRCPDPLVFDVNDPMHLDFIYAGANLRAEVYGIEQVRNRETIAELVQKVKV 711
Cdd:pfam10585  81 LFNNDIKQLLYNFPPDHKTSSGAPFWSGPKRPPTPLEFDPNNPLHLDFVVAAANLRAQVYGIPGSRDREAIAKVLSKVKV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 712 PEFKPRSGVKIETNEAAAAASANNFDDgelDQDRVDKIISELLKNADKTS-----KITPLEFEKDDDSNLHMDFIVACSN 786
Cdd:pfam10585 161 PEFKPKSGVKIQVNDEEAADPNAESED---DEDELDELLEELPKLAVSPSslagfRLNPIEFEKDDDTNFHIDFITAASN 237

                         250
                  ....*....|....*..
gi 2098122732 787 LRAANYKISPADRHKSK 803
Cdd:pfam10585 238 LRARNYGIPPADRHKTK 254
UBA_e1_C smart00985
Ubiquitin-activating enzyme e1 C-terminal domain; This presumed domain found at the C terminus ...
 841-966 5.20e-64

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: 211.73  E-value: 5.20e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732  841 FKNGFANLALPFMAFSEPVPAAKNTYYGK-EWTLWDRFEVTG-ELSLQEFLNYFEENEKLKITMLSQGVSMLYSFFMPKA 918
Cdd:smart00985   1 YKNAFLNLALPFFAFSEPIAAPKTKYRDKdKWTLWDRLEVPGgDITLKELLDYFEEKYGLEVTMLSQGVSLLYSSFMPPK 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 2098122732  919 KCSERLPLPMSEVVRRVSKRRLEPHERSLVFEICCNDVDGEDVEVPYV 966
Cdd:smart00985  81 KHKERLDLPVTELVEQVTKKKLPPHVKYLVLEVSCEDEDDEDVEVPYI 128
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 366-534 4.45e-36

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: 136.80  E-value: 4.45e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 366 RYDSQIAI--FGKKFQEKLADSKWFIVGAGAIGCELLKNFGMLGLGTgkgqIFVTDMDLIEKSNLNRQFLFRPHDVQKPK 443
Cdd:COG0476     7 RYSRQILLpeIGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGT----LTLVDDDVVELSNLQRQILYTEADVGRPK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 444 SMTAADAIKRMNPEVNVTAYELRVGAETEkvfsEDFFGKLDGVANALDNVDARIYMDRKCIFNRIPLVETGTLGTLGNVQ 523
Cdd:COG0476    83 VEAAAERLRALNPDVEVEAIPERLTEENA----LELLAGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIGFEGQVT 158

                         170
                  ....*....|.
gi 2098122732 524 VIVPFATESYS 534
Cdd:COG0476   159 VFIPGDTPCYR 169
PRK08328 PRK08328
hypothetical protein; Provisional
 366-532 7.46e-20

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 89.47  E-value: 7.46e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 366 RYDSQIAIFGKKFQEKLADSKWFIVGAGAIGCELLKNFGMLGLGTgkgqIFVTDMDLIEKSNLNRQFLFRPHDVQK-PKS 444
Cdd:PRK08328    9 RYDRQIMIFGVEGQEKLKKAKVAVVGVGGLGSPVAYYLAAAGVGR----ILLIDEQTPELSNLNRQILHWEEDLGKnPKP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 445 MTAADAIKRMNPEVNVTAYELRVGAETekvfSEDFFGKLDGVANALDNVDARIYMDRKCIFNRIPLVETGTLGTLGNVQV 524
Cdd:PRK08328   85 LSAKWKLERFNSDIKIETFVGRLSEEN----IDEVLKGVDVIVDCLDNFETRYLLDDYAHKKGIPLVHGAVEGTYGQVTT 160


                  ....*...
gi 2098122732 525 IVPFATES 532
Cdd:PRK08328  161 IVPGKTKR 168
 
Name Accession Description Interval E-value
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 31-968 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: 1143.47  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732   31 VLQLHDLSSQFYLTEADIGKNRAEASCAQLAELNSYVRTVSHTGPLTEEFLRKFRVVVLTNSDGEEQQRIGKFAHEN--G 108
Cdd:TIGR01408   58 KCQAWDLSSNFFLSEDDVGRNRAEAVVKKLAELNPYVHVSSSSVPFNEEFLDKFQCVVLTEMSLPLQKEINDFCHSQcpP 137

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732  109 IALIIAETRGLFAKVFCDFGESFTIYDQDGTQPISTMIASITHDAQGVVTCLDETRHGFNDGDYVTFSEVQGMQELNGCQ 188
Cdd:TIGR01408  138 IAFISADVRGLFGSLFCDFGDEFEVLDTDGEEPKTGFIASITQANPGIVTCLENHRHKLETGDFVTFREVNGMTGLNDGS 217

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732  189 PLKITVLGPYTFSIGDTSKFGEYKSGGVATQVKMPKTISFKSLAQASEEPEFLISDFAKLDSPATLHVAFNALSCYRKAH 268
Cdd:TIGR01408  218 PRKITVISPYSFSIGDTTELGPYLHGGIATQVKTPKTVFFKSLREQLKDPKCLIVDFSKPERPPEIHTAFQALDQFQEKY 297

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732  269 nGVLPRPWNEEDANSFLEVVRASSSA------EVDEKLVLQFAKICSGNTCPLDAAVGGIVAQEVLKACSGKFTPIYQWL 342
Cdd:TIGR01408  298 -SRKPNVGCQQDAEELLKLATSISETleekvpDVDAKLVHWLSWTAQGFLSPMAAAVGGVVSQEVLKAVTGKFSPLCQWF 376

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732  343 YFDALECLPTEG-VEEADAQPVGSRYDSQIAIFGKKFQEKLADSKWFIVGAGAIGCELLKNFGMLGLGTG-KGQIFVTDM 420
Cdd:TIGR01408  377 YFDSAESLPSLGkPECEEFLPRGDRYDAQIAVFGDTFQQKLQNLNIFLVGCGAIGCEMLKNFALMGVGTGkKGMITVTDP 456

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732  421 DLIEKSNLNRQFLFRPHDVQKPKSMTAADAIKRMNPEVNVTAYELRVGAETEKVFSEDFFGKLDGVANALDNVDARIYMD 500
Cdd:TIGR01408  457 DLIEKSNLNRQFLFRPHHIGKPKSYTAADATLKINPQIKIDAHQNRVGPETETIFNDEFYEKLDVVINALDNVEARRYVD 536

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732  501 RKCIFNRIPLVETGTLGTLGNVQVIVPFATESYSSSQD*PEKSIPICTLKNFPNAIEHTLQWARDAFEGVFKQSAENAAQ 580
Cdd:TIGR01408  537 SRCLAFLKPLLESGTLGTKGNTQVVVPHLTESYGSSRDPPEKEIPFCTLKSFPAAIEHTIQWARDKFEGLFSHKPSLVNK 616

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732  581 YIADP-QFTERIAKLPGIQPLDILDSIKKALIDDKPKSFAHCVEWARLYWEDQYVNQIKQLLFNFPPDQITSSGQPFWSG 659
Cdd:TIGR01408  617 YLSSPsSAEEVLQKIQSGHSREGLEQIIKLLSKEKPRNFSQCVEWARLKFEKYFNNKALQLLHCFPLDIRTSTGSPFWSS 696

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732  660 PKRCPDPLVFDVNDPMHLDFIYAGANLRAEVYGI---EQVRNRETIAELVQKVKVPEFKPRSGVKIETNEAAAAASANNF 736
Cdd:TIGR01408  697 PKRPPSPLKFDLNEPLHLSFIQAAAKLYATVYGIpfaEEDLSADALLNILSEVKIPEFKPRSNKKIQTDETARKPDTAPI 776

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732  737 DdgelDQDRVDKIISELLKNADKTS--KITPLEFEKDDDSNLHMDFIVACSNLRAANYKISPADRHKSKLIAGKIIPAIA 814
Cdd:TIGR01408  777 D----DRNAIFQLEKAILSNEATKSdfRMAPLSFEKDDDHNGHIDFITAASNLRAKNYSIEPADRFKTKFIAGKIIPAIA 852

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732  815 TTTSVLSGLAVLEVIKLIVGHRDLVKFKNGFANLALPFMAFSEPVPAAKNTYYGKEW-TLWDRFEVTGELSLQEFLNYFE 893
Cdd:TIGR01408  853 TSTATVSGLVCLELIKVTDGGYKFEVYKNCFLNLAIPLFVFTEPTEVRKTKIRNGISfTIWDRWTLHGDFTLLEFINAVK 932

                          890       900       910       920       930       940       950
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2098122732  894 ENEKLKITMLSQGVSMLYSFFMPKAKcsERLPLPMSEVVRRVSKRRLEPHERSLVFEICCNDVDGEDVEVPYVRY 968
Cdd:TIGR01408  933 EKYGLEPTMVSQGVKLLYVPVMPGHA--ERLKLKMHKLVKPTTKKKLPPYRVHLTVSFACDDDGDEDVPGPPVRI 1005
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
 386-924 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: 794.57  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 386 KWFIVGAGAIGCELLKNFGMLGLGTG-KGQIFVTDMDLIEKSNLNRQFLFRPHDVQKPKSMTAADAIKRMNPEVNVTAYE 464
Cdd:cd01490     1 KVFLVGAGAIGCELLKNFALMGVGTGeSGEITVTDMDNIEKSNLNRQFLFRPHDVGKPKSEVAAAAVKAMNPDLKITALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 465 LRVGAETEKVFSEDFFGKLDGVANALDNVDARIYMDRKCIFNRIPLVETGTLGTLGNVQVIVPFATESYSSSQD*PEKSI 544
Cdd:cd01490    81 NRVGPETEHIFNDEFWEKLDGVANALDNVDARMYVDRRCVYYRKPLLESGTLGTKGNTQVVIPHLTESYSSSRDPPEKSI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 545 PICTLKNFPNAIEHTLQWARDAFEGVFKQSAENAAQYIadpqfteriaklpgiqpldildsikkaliddkpksFAHCVEW 624
Cdd:cd01490   161 PLCTLKNFPNAIEHTIQWARDEFEGLFKQPPENVNQYL-----------------------------------FEDCVRW 205

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 625 ARLYWEDQYVNQIKQLLFNFPPDQITSSGQPFWSGPKRCPDPLVFDVNDPMHLDFIYAGANLRAEVYGIEQvrnretiae 704
Cdd:cd01490   206 ARLLFEKYFNNNIKQLLHNFPPDAVTSDGAPFWSGPKRCPTPLEFDVNNPLHLDFVLAAANLYAEVYGIPG--------- 276

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 705 lvqkvkvpefkprsgvkietneaaaaasannfddgeldqdrvdkiisellknadktskitpleFEKDDDSNLHMDFIVAC 784
Cdd:cd01490   277 ---------------------------------------------------------------FEKDDDTNFHMDFITAA 293

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 785 SNLRAANYKISPADRHKSKLIAGKIIPAIATTTSVLSGLAVLEVIKLIVGHRDLVKFKNGFANLALPFMAFSEPVPAAKN 864
Cdd:cd01490   294 SNLRARNYSIPPADRHKTKRIAGKIIPAIATTTAAVTGLVCLELYKVVDGKRPLEAYKNAFLNLALPFFAFSEPIPAPKV 373

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2098122732 865 TY-YGKEWTLWDRFEVTGELSLQEFL-NYFEENEKLKITMLSQGVSMLYSFFMPKAKCSERL 924
Cdd:cd01490   374 KYaYDEEWTIWDRFEVKGKQTLQELLiDYFKEKYGLEVTMLSQGVSMLYSSFMPPAKLKERL 435
UBA_E1_SCCH pfam10585
Ubiquitin-activating enzyme, SCCH domain; Ubiquitin-activating enzyme (E1 enzyme) activates ...
 553-803 5.54e-133

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: 400.07  E-value: 5.54e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 553 PNAIEHTLQWARDAFEGVFKQSAENAAQYIADPQ-FTERIAKLPGIQPLDILDSIKKALIDDKPKSFAHCVEWARLYWED 631
Cdd:pfam10585   1 PNAIEHTIQWARDEFEGLFVQPPEEVNKYLQPPQnFIESLLKQGGGQKLETLESVRKSLVTERPKTFEDCVAWARLKFEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 632 QYVNQIKQLLFNFPPDQITSSGQPFWSGPKRCPDPLVFDVNDPMHLDFIYAGANLRAEVYGIEQVRNRETIAELVQKVKV 711
Cdd:pfam10585  81 LFNNDIKQLLYNFPPDHKTSSGAPFWSGPKRPPTPLEFDPNNPLHLDFVVAAANLRAQVYGIPGSRDREAIAKVLSKVKV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 712 PEFKPRSGVKIETNEAAAAASANNFDDgelDQDRVDKIISELLKNADKTS-----KITPLEFEKDDDSNLHMDFIVACSN 786
Cdd:pfam10585 161 PEFKPKSGVKIQVNDEEAADPNAESED---DEDELDELLEELPKLAVSPSslagfRLNPIEFEKDDDTNFHIDFITAASN 237

                         250
                  ....*....|....*..
gi 2098122732 787 LRAANYKISPADRHKSK 803
Cdd:pfam10585 238 LRARNYGIPPADRHKTK 254
Ube1_repeat1 cd01491
Ubiquitin activating enzyme (E1), repeat 1. E1, a highly conserved small protein present ...
 33-354 9.39e-125

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: 380.07  E-value: 9.39e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732  33 QLHDLSSQFYLTEADIGKNRAEASCAQLAELNSYVRTVSHTGPLTEEFLRKFRVVVLTNSDGEEQQRIGKFAHENGIALI 112
Cdd:cd01491    55 SWSDLSSQFYLREEDIGKNRAEASQARLAELNPYVPVTVSTGPLTTDELLKFQVVVLTDASLEDQLKINEFCHSPGIKFI 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 113 IAETRGLFAKVFCDFGESFTIYDQDGTQPISTMIASITHDAQGVVTCLDETRHGFNDGDYVTFSEVQGMQELNGCQPLKI 192
Cdd:cd01491   135 SADTRGLFGSIFCDFGDEFTVYDPNGEEPKSGMISSISKDNPGVVTCLDETRHGFEDGDYVTFSEVEGMTELNGCEPRKI 214

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 193 TVLGPYTFSIGDTSKFGEYKSGGVATQVKMpktisfkslaqaseepeflisdfakldspatlhvafnalscyrkahngvl 272
Cdd:cd01491   215 KVKGPYTFSIGDTSSFSEYIRGGIVTQVKL-------------------------------------------------- 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 273 prpwneedansflevvrasssaevdeklvlqfakicsgntCPLDAAVGGIVAQEVLKACSGKFTPIYQWLYFDALECLPT 352
Cdd:cd01491   245 ----------------------------------------SPMAAFFGGLAAQEVLKACSGKFTPLKQWLYFDALECLPE 284


                  ..
gi 2098122732 353 EG 354
Cdd:cd01491   285 DE 286
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
 386-581 2.78e-70

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: 233.24  E-value: 2.78e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 386 KWFIVGAGAIGCELLKNFGMLGLGtgkgQIFVTDMDLIEKSNLNRQFLFRPHDVQKPKSMTAADAIKRMNPEVNVTAYEL 465
Cdd:cd01484     1 KVLLVGAGGIGCELLKNLALMGFG----QIHVIDMDTIDVSNLNRQFLFRPKDIGRPKSEVAAEAVNDRNPNCKVVPYQN 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 466 RVGaeTEKVFSEDFFGKLDGVANALDNVDARIYMDRKCIFNRIPLVETGTLGTLGNVQVIVPFATESYSSSQD*PEKSIP 545
Cdd:cd01484    77 KVG--PEQDFNDTFFEQFHIIVNALDNIIARRYVNGMLIFLIVPLIESGTEGFKGNAQVILPGMTECIECTLYPPQKNFP 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2098122732 546 ICTLKNFPNAIEHTLQWARDAFEG-------VFKQSAENAAQY 581
Cdd:cd01484   155 MCTIASMPRLPEHCIEWARMLQWDdpehiqfIFQASNERASQY 197
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 367-552 8.66e-67

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: 223.67  E-value: 8.66e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 367 YDSQIAI--FGKKFQEKLADSKWFIVGAGAIGCELLKNFGMLGLGtgkgQIFVTDMDLIEKSNLNRQFLFRPHDVQKPKS 444
Cdd:pfam00899   1 YSRQLALplIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVG----KITLVDFDTVELSNLNRQFLFREADIGKPKA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 445 MTAADAIKRMNPEVNVTAYELRVGAETekvfSEDFFGKLDGVANALDNVDARIYMDRKCIFNRIPLVETGTLGTLGNVQV 524
Cdd:pfam00899  77 EVAAERLREINPDVEVEAYTERLTPEN----AEELIKSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVTV 152

                         170       180       190
                  ....*....|....*....|....*....|
gi 2098122732 525 IVPFATESYS--SSQD*PEKSIPICTLKNF 552
Cdd:pfam00899 153 VIPGKTPCYRclFPEDPPPKLVPSCTVAGV 182
UBA_e1_C smart00985
Ubiquitin-activating enzyme e1 C-terminal domain; This presumed domain found at the C terminus ...
 841-966 5.20e-64

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: 211.73  E-value: 5.20e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732  841 FKNGFANLALPFMAFSEPVPAAKNTYYGK-EWTLWDRFEVTG-ELSLQEFLNYFEENEKLKITMLSQGVSMLYSFFMPKA 918
Cdd:smart00985   1 YKNAFLNLALPFFAFSEPIAAPKTKYRDKdKWTLWDRLEVPGgDITLKELLDYFEEKYGLEVTMLSQGVSLLYSSFMPPK 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 2098122732  919 KCSERLPLPMSEVVRRVSKRRLEPHERSLVFEICCNDVDGEDVEVPYV 966
Cdd:smart00985  81 KHKERLDLPVTELVEQVTKKKLPPHVKYLVLEVSCEDEDDEDVEVPYI 128
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 386-848 2.46e-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: 199.91  E-value: 2.46e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 386 KWFIVGAGAIGCELLKNFGMlglgTGKGQIFVTDMDLIEKSNLNRQFLFRPHDVQKPKSMTAADAIKRMNPEVNVTAYEL 465
Cdd:cd01489     1 KVLVVGAGGIGCELLKNLVL----TGFGEIHIIDLDTIDLSNLNRQFLFRKKHVGKSKAQVAKEAVLSFNPNVKIVAYHA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 466 RVgaeTEKVFSEDFFGKLDGVANALDNVDARIYMDRKCIFNRIPLVETGTLGTLGNVQVIVPFATESYSSSQD*PEKSIP 545
Cdd:cd01489    77 NI---KDPDFNVEFFKQFDLVFNALDNLAARRHVNKMCLAADVPLIESGTTGFLGQVQVIKKGKTECYECQPKETPKTFP 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 546 ICTLKNFPNaiehtlqwardafegvfkqsaenaaqyiadpqfteriaklpgiQPLdildsikkaliddkpksfaHCVEWA 625
Cdd:cd01489   154 VCTIRSTPS-------------------------------------------QPI-------------------HCIVWA 171

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 626 rlywedqyvnqiKQLLFNFPPdqitssgqpfwsgpkrcpdplVFDVNdpmhldfiyaganlraevygIEQVRnreTIAEL 705
Cdd:cd01489   172 ------------KSLFFLFNK---------------------VFKDD--------------------IERLL---SMEEL 195

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 706 VQKVKVPEfkprsgvkietneaaaaasannfddgELDqdrvdkiisellknadktskITPLEFEKDDDSNlhMDFIVACS 785
Cdd:cd01489   196 WKTRKPPV--------------------------PLS--------------------WKELTFDKDDQDA--LDFVAAAA 227

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2098122732 786 NLRAANYKISPADRHKSKLIAGKIIPAIATTTSVLSGLAVLEVIKLIVGHRDlvKFKNGFANL 848
Cdd:cd01489   228 NLRSHVFGIPMKSRFDIKQMAGNIIPAIATTNAIIAGLIVLEALKVLSGDKE--QCRTVFLNL 288
E1_UFD pfam09358
Ubiquitin fold domain; The ubiquitin fold domain is found at the C-terminus of ...
 874-966 1.01e-47

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: 164.64  E-value: 1.01e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 874 WDRFEVTGELSLQEFLNYFEENEKLKITMLSQGVSMLYSFFMPKAKCSERLPLPMSEVVRRVSKRRLEPHERSLVFEICC 953
Cdd:pfam09358   1 WDRFEVEGDMTLQELLDYFKEKYGLEVTMLSYGVSLLYSSFMPPKKHKERLPMKISELVEEVSKKPIPPHQKYLVLEVSC 80

                          90
                  ....*....|...
gi 2098122732 954 NDVDGEDVEVPYV 966
Cdd:pfam09358  81 EDEDGEDVEVPYV 93
E1_FCCH pfam16190
Ubiquitin-activating enzyme E1 FCCH domain; This domain is found in the ubiquitin-activating ...
 152-221 8.09e-45

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: 155.33  E-value: 8.09e-45
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 152 DAQGVVTCLDETRHGFNDGDYVTFSEVQGMQELNGCQPLKITVLGPYTFSIGDTSKFGEYKSGGVATQVK 221
Cdd:pfam16190   1 DNPGVVTCLDDTRHGLEDGDYVTFSEVEGMTELNGCEPRKIKVLGPYTFSIGDTSSFSPYLRGGIVTQVK 70
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 386-581 1.73e-38

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: 145.58  E-value: 1.73e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 386 KWFIVGAGAIGCELLKNFGMLGLGtgkgQIFVTDMDLIEKSNLNRQFLFRPHDVQKPKSMTAADAIKRMNPEVNVTAYEL 465
Cdd:cd01488     1 KILVIGAGGLGCELLKNLALSGFR----NIHVIDMDTIDVSNLNRQFLFREKDIGKPKAEVAAKFVNDRVPGVNVTPHFG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 466 RVgaeteKVFSEDFFGKLDGVANALDNVDAR-----------IYMDRKCIfnrIPLVETGTLGTLGNVQVIVPFATESYS 534
Cdd:cd01488    77 KI-----QDKDEEFYRQFNIIICGLDSIEARrwingtlvsllLYEDPESI---IPLIDGGTEGFKGHARVILPGITACIE 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2098122732 535 SSQD*--PEKSIPICTLKNFPNAIEHTLQWAR------------------DAFEGVFKQSAENAAQY 581
Cdd:cd01488   149 CSLDLfpPQVTFPLCTIANTPRLPEHCIEYASliqwpkefpfvpldgddpEHIEWLYQKALERAAQF 215
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 366-534 4.45e-36

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: 136.80  E-value: 4.45e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 366 RYDSQIAI--FGKKFQEKLADSKWFIVGAGAIGCELLKNFGMLGLGTgkgqIFVTDMDLIEKSNLNRQFLFRPHDVQKPK 443
Cdd:COG0476     7 RYSRQILLpeIGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGT----LTLVDDDVVELSNLQRQILYTEADVGRPK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 444 SMTAADAIKRMNPEVNVTAYELRVGAETEkvfsEDFFGKLDGVANALDNVDARIYMDRKCIFNRIPLVETGTLGTLGNVQ 523
Cdd:COG0476    83 VEAAAERLRALNPDVEVEAIPERLTEENA----LELLAGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIGFEGQVT 158

                         170
                  ....*....|.
gi 2098122732 524 VIVPFATESYS 534
Cdd:COG0476   159 VFIPGDTPCYR 169
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 366-547 7.36e-35

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: 132.99  E-value: 7.36e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 366 RYDSQIAI--FGKKFQEKLADSKWFIVGAGAIGCELLKNFGMLGLGTgkgqIFVTDMDLIEKSNLNRQFLFRPHDVQKPK 443
Cdd:cd00757     1 RYSRQILLpeIGEEGQEKLKNARVLVVGAGGLGSPAAEYLAAAGVGK----LGLVDDDVVELSNLQRQILHTEADVGQPK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 444 SMTAADAIKRMNPEVNVTAYELRVGAETEkvfsEDFFGKLDGVANALDNVDARIYMDRKCIFNRIPLVETGTLGTLGNVQ 523
Cdd:cd00757    77 AEAAAERLRAINPDVEIEAYNERLDAENA----EELIAGYDLVLDCTDNFATRYLINDACVKLGKPLVSGAVLGFEGQVT 152

                         170       180
                  ....*....|....*....|....*
gi 2098122732 524 VIVPFATESYSSS-QD*PEKSIPIC 547
Cdd:cd00757   153 VFIPGEGPCYRCLfPEPPPPGVPSC 177
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 388-525 5.73e-33

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: 124.30  E-value: 5.73e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 388 FIVGAGAIGCELLKNFGMlglgTGKGQIFVTDMDLIEKSNLNRQFLFRPHDVQKPKSMTAADAIKRMNPEVNVTAYELRV 467
Cdd:cd01483     3 LLVGLGGLGSEIALNLAR----SGVGKITLIDFDTVELSNLNRQFLARQADIGKPKAEVAARRLNELNPGVNVTAVPEGI 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2098122732 468 GAETEkvfsEDFFGKLDGVANALDNVDARIYMDRKCIFNRIPLVETGTLGTLGNVQVI 525
Cdd:cd01483    79 SEDNL----DDFLDGVDLVIDAIDNIAVRRALNRACKELGIPVIDAGGLGLGGDIQVI 132
E1_4HB pfam16191
Ubiquitin-activating enzyme E1 four-helix bundle; This domain is found in the ...
 222-290 6.30e-31

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: 115.63  E-value: 6.30e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2098122732 222 MPKTISFKSLAQASEEPEFLISDFAKLDSPATLHVAFNALSCYRKAHnGVLPRPWNEEDANSFLEVVRA 290
Cdd:pfam16191   1 MPKTLSFKSLEESLKEPEFLISDFAKFDRPAQLHLAFQALHAFQEKH-GRLPRPWNEEDAEEVVKLAKE 68
PRK08328 PRK08328
hypothetical protein; Provisional
 366-532 7.46e-20

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 89.47  E-value: 7.46e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 366 RYDSQIAIFGKKFQEKLADSKWFIVGAGAIGCELLKNFGMLGLGTgkgqIFVTDMDLIEKSNLNRQFLFRPHDVQK-PKS 444
Cdd:PRK08328    9 RYDRQIMIFGVEGQEKLKKAKVAVVGVGGLGSPVAYYLAAAGVGR----ILLIDEQTPELSNLNRQILHWEEDLGKnPKP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 445 MTAADAIKRMNPEVNVTAYELRVGAETekvfSEDFFGKLDGVANALDNVDARIYMDRKCIFNRIPLVETGTLGTLGNVQV 524
Cdd:PRK08328   85 LSAKWKLERFNSDIKIETFVGRLSEEN----IDEVLKGVDVIVDCLDNFETRYLLDDYAHKKGIPLVHGAVEGTYGQVTT 160


                  ....*...
gi 2098122732 525 IVPFATES 532
Cdd:PRK08328  161 IVPGKTKR 168
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 366-531 9.56e-18

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 83.74  E-value: 9.56e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 366 RYDSQIAI--FGKKFQEKLADSKWFIVGAGAIGCELLKNFGMLGLGTgkgqIFVTDMDLIEKSNLNRQFLFRPHDVQKPK 443
Cdd:PRK05690   12 RYNRQIILrgFDFDGQEKLKAARVLVVGLGGLGCAASQYLAAAGVGT----LTLVDFDTVSLSNLQRQVLHDDATIGQPK 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 444 SMTAADAIKRMNPEVNVTAYELRvgaetekvFSEDFFGKL----DGVANALDNVDARIYMDRKCIFNRIPLVeTGTLGTL 519
Cdd:PRK05690   88 VESARAALARINPHIAIETINAR--------LDDDELAALiaghDLVLDCTDNVATRNQLNRACFAAKKPLV-SGAAIRM 158

                         170
                  ....*....|...
gi 2098122732 520 -GNVQVIVPFATE 531
Cdd:PRK05690  159 eGQVTVFTYQDDE 171
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 366-527 1.88e-17

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 84.66  E-value: 1.88e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 366 RYDSQI--AIFGKKFQEKLADSKWFIVGAGAIGCELLKNFGMLGLGTgkgqIFVTDMDLIEKSNLNRQFLFRPHDVQK-- 441
Cdd:PRK07688    4 RYSRQElfSPIGEEGQQKLREKHVLIIGAGALGTANAEMLVRAGVGK----VTIVDRDYVEWSNLQRQQLYTESDVKNnl 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 442 PKSMTAADAIKRMNPEVNVTAYELRVGAETekvfSEDFFGKLDGVANALDNVDARIYMDRKCIFNRIPLVETGTLGTLGN 521
Cdd:PRK07688   80 PKAVAAKKRLEEINSDVRVEAIVQDVTAEE----LEELVTGVDLIIDATDNFETRFIVNDAAQKYGIPWIYGACVGSYGL 155


                  ....*.
gi 2098122732 522 VQVIVP 527
Cdd:PRK07688  156 SYTIIP 161
E1-1_like cd01485
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ...
 33-127 5.14e-17

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: 80.54  E-value: 5.14e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732  33 QLHDLSSQFYL--TEADIGKNRAEASCAQLAELNSYVRTVSHTGP------LTEEFLRKFRVVVLTNSDGEEQQRIGKFA 104
Cdd:cd01485    55 STEDLGSNFFLdaEVSNSGMNRAAASYEFLQELNPNVKLSIVEEDslsndsNIEEYLQKFTLVIATEENYERTAKVNDVC 134

                          90       100
                  ....*....|....*....|...
gi 2098122732 105 HENGIALIIAETRGLFAKVFCDF 127
Cdd:cd01485   135 RKHHIPFISCATYGLIGYAFFDF 157
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 374-547 2.47e-16

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 81.85  E-value: 2.47e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 374 FGKKFQEKLADSKWFIVGAGAIGCELLKNFGMLGLGTgkgqIFVTDMDLIEKSNLNRQFLFRPHDVQKPKSMTAADAIKR 453
Cdd:PRK05600   31 FGIEQQERLHNARVLVIGAGGLGCPAMQSLASAGVGT----ITLIDDDTVDVSNIHRQILFGASDVGRPKVEVAAERLKE 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 454 MNPEVNVTAYELRVGAETekvfSEDFFGKLDGVANALDNVDARIYMDRKCIFNRIPLVETGTLGTLGNVQVIVPFATESY 533
Cdd:PRK05600  107 IQPDIRVNALRERLTAEN----AVELLNGVDLVLDGSDSFATKFLVADAAEITGTPLVWGTVLRFHGELAVFNSGPDHRG 182

                         170
                  ....*....|....*....
gi 2098122732 534 SSSQD*-PEK----SIPIC 547
Cdd:PRK05600  183 VGLRDLfPEQpsgdSIPDC 201
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 366-553 3.60e-16

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 80.93  E-value: 3.60e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 366 RYDSQIAI--FGKKFQEKLADSKWFIVGAGAIGCELLKNFGMLGLGTgkgqIFVTDMDLIEKSNLNRQFLFRPHDVQ--K 441
Cdd:PRK12475    4 RYSRQILFsgIGEEGQRKIREKHVLIVGAGALGAANAEALVRAGIGK----LTIADRDYVEWSNLQRQQLYTEEDAKqkK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 442 PKSMTAADAIKRMNPEVNVTAYELRVGAETekvfSEDFFGKLDGVANALDNVDARIYMDRKCIFNRIPLVETGTLGTLGN 521
Cdd:PRK12475   80 PKAIAAKEHLRKINSEVEIVPVVTDVTVEE----LEELVKEVDLIIDATDNFDTRLLINDLSQKYNIPWIYGGCVGSYGV 155

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2098122732 522 VQVIVPFATESYSssqd*peksipiCTLKNFP 553
Cdd:PRK12475  156 TYTIIPGKTPCLR------------CLMEHVP 175
Aos1_SUMO cd01492
Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating ...
 367-520 3.62e-16

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: 78.10  E-value: 3.62e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 367 YDSQIAIFGKKFQEKLADSKWFIVGAGAIGCELLKNFGMLGLGTgkgqIFVTDMDLIEKSNLNRQFLFRPHDVQKPKSMT 446
Cdd:cd01492     4 YDRQIRLWGLEAQKRLRSARILLIGLKGLGAEIAKNLVLSGIGS----LTILDDRTVTEEDLGAQFLIPAEDLGQNRAEA 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2098122732 447 AADAIKRMNPEVNVTayelrVGAETEKVFSEDFFGKLDGV-ANALDNvDARIYMDRKCIFNRIPLVETGTLGTLG 520
Cdd:cd01492    80 SLERLRALNPRVKVS-----VDTDDISEKPEEFFSQFDVVvATELSR-AELVKINELCRKLGVKFYATGVHGLFG 148
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
 374-514 1.51e-15

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: 76.87  E-value: 1.51e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 374 FGKKFQEKLADSKWFIVGAGAIG---CELLknfgmlgLGTGKGQIFVTDMDLIEKSNLNRQFLFRPHDVQKPKSMTAADA 450
Cdd:cd00755     1 YGEEGLEKLRNAHVAVVGLGGVGswaAEAL-------ARSGVGKLTLIDFDVVCVSNLNRQIHALLSTVGKPKVEVMAER 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2098122732 451 IKRMNPEVNVTAYELRVGAET-EKVFSEDFfgklDGVANALDNVDARIYMDRKCIFNRIPLVETG 514
Cdd:cd00755    74 IRDINPECEVDAVEEFLTPDNsEDLLGGDP----DFVVDAIDSIRAKVALIAYCRKRKIPVISSM 134
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
375-527 3.59e-15

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 78.51  E-value: 3.59e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 375 GKKFQEKLADSKWFIVGAGAIGCELLKNFGMLGLGTgkgqIFVTDMDLIEKSNLNRQFLFRPHDVQKPKSMTAADAIKRM 454
Cdd:PRK08762  126 GEEGQRRLLEARVLLIGAGGLGSPAALYLAAAGVGT----LGIVDHDVVDRSNLQRQILHTEDRVGQPKVDSAAQRLAAL 201

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2098122732 455 NPEVNVTAYELRVGAETEKVFSEDFfgklDGVANALDNVDARIYMDRKCIFNRIPLVETGTLGTLGNVQVIVP 527
Cdd:PRK08762  202 NPDVQVEAVQERVTSDNVEALLQDV----DVVVDGADNFPTRYLLNDACVKLGKPLVYGAVFRFEGQVSVFDA 270
Aos1_SUMO cd01492
Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating ...
 36-126 1.21e-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: 73.48  E-value: 1.21e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732  36 DLSSQFYLTEADIGKNRAEASCAQLAELNSYVRTVSHTGPLTE---EFLRKFRVVVLTNSDGEEQQRIGKFAHENGIALI 112
Cdd:cd01492    60 DLGAQFLIPAEDLGQNRAEASLERLRALNPRVKVSVDTDDISEkpeEFFSQFDVVVATELSRAELVKINELCRKLGVKFY 139

                          90
                  ....*....|....
gi 2098122732 113 IAETRGLFAKVFCD 126
Cdd:cd01492   140 ATGVHGLFGFVFAD 153
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 365-496 1.25e-13

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 73.37  E-value: 1.25e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 365 SRYDSQIAI--FGKKFQEKLADSKWFIVGAGAIGCELLknfgmLGL-GTGKGQIFVTDMDLIEKSNLNRQFLFRPHDVQK 441
Cdd:PRK05597    7 ARYRRQIMLgeIGQQGQQSLFDAKVAVIGAGGLGSPAL-----LYLaGAGVGHITIIDDDTVDLSNLHRQVIHSTAGVGQ 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2098122732 442 PKSMTAADAIKRMNPEVNVTAYELRVGAETEKVFSEDFFGKLDGVanalDNVDAR 496
Cdd:PRK05597   82 PKAESAREAMLALNPDVKVTVSVRRLTWSNALDELRDADVILDGS----DNFDTR 132
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
371-495 1.58e-13

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 70.66  E-value: 1.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 371 IAIFGKKFQEKLADSKWFIVGAGaigcellknfgmlGLG---------TGKGQIFVTDMDLIEKSNLNRQFLFrPHDVQK 441
Cdd:PRK08644   15 ASRHTPKLLEKLKKAKVGIAGAG-------------GLGsniavalarSGVGNLKLVDFDVVEPSNLNRQQYF-ISQIGM 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2098122732 442 PKSMTAADAIKRMNPEVNVTAYELRVGAETekvfSEDFFGKLDGVANALDNVDA 495
Cdd:PRK08644   81 PKVEALKENLLEINPFVEIEAHNEKIDEDN----IEELFKDCDIVVEAFDNAET 130
E1-1_like cd01485
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ...
 367-529 2.25e-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: 67.06  E-value: 2.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 367 YDSQIAIFGKKFQEKLADSKWFIVGAGAIGCELLKNFGMLGLGTgkgqIFVTDMDLIEKSNLNRQFLFRPHDVQ--KPKS 444
Cdd:cd01485     2 YDRQIRLWGDEAQNKLRSAKVLIIGAGALGAEIAKNLVLAGIDS----ITIVDHRLVSTEDLGSNFFLDAEVSNsgMNRA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 445 MTAADAIKRMNPEVNVTAyelrVGAETEKVFS--EDFFGKLDGVANALDNVDARIYMDRKCIFNRIPLVETGTLGTLGNV 522
Cdd:cd01485    78 AASYEFLQELNPNVKLSI----VEEDSLSNDSniEEYLQKFTLVIATEENYERTAKVNDVCRKHHIPFISCATYGLIGYA 153


                  ....*..
gi 2098122732 523 QVIVPFA 529
Cdd:cd01485   154 FFDFPIA 160
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 366-511 3.47e-12

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 69.35  E-value: 3.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 366 RYDSQIAI--FGKKFQEKLADSKWFIVGAGAIGCELLKNFGMLGLGTgkgqIFVTDMDLIEKSNLNRQFLFRPHDVQKPK 443
Cdd:PRK07878   22 RYSRHLIIpdVGVDGQKRLKNARVLVIGAGGLGSPTLLYLAAAGVGT----LGIVEFDVVDESNLQRQVIHGQSDVGRSK 97

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2098122732 444 SMTAADAIKRMNPEVNVTAYELRVGAETEKvfseDFFGKLDGVANALDNVDARIYMDRKCIFNRIPLV 511
Cdd:PRK07878   98 AQSARDSIVEINPLVNVRLHEFRLDPSNAV----ELFSQYDLILDGTDNFATRYLVNDAAVLAGKPYV 161
TcdA COG1179
tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ...
 373-514 6.20e-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: 66.64  E-value: 6.20e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 373 IFGKKFQEKLADSKWFIVGAGAIG---CEllknfgmlGLG-TGKGQIFVTDMDLIEKSNLNRQfLFRPHD-VQKPKSMTA 447
Cdd:COG1179    13 LYGEEGLERLANAHVAVVGLGGVGswaAE--------ALArSGVGRLTLVDLDDVCESNINRQ-LHALDStVGRPKVEVM 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2098122732 448 ADAIKRMNPEVNVTAYELRVGAET-EKVFSEDFfgklDGVANALDNVDARIYMDRKCIFNRIPLVETG 514
Cdd:COG1179    84 AERIRDINPDCEVTAIDEFVTPENaDELLSEDY----DYVIDAIDSVSAKAALIAWCRRRGIPIISSM 147
E1_ThiF_like cd01487
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ...
 389-496 1.15e-10

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: 61.24  E-value: 1.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 389 IVGAGAIGcellKNFGMLGLGTGKGQIFVTDMDLIEKSNLNRQFlFRPHDVQKPKSMTAADAIKRMNPEVNVTAYELRVG 468
Cdd:cd01487     4 IAGAGGLG----SNIAVLLARSGVGNLKLVDFDVVEPSNLNRQQ-YFLSQIGEPKVEALKENLREINPFVKIEAINIKID 78

                          90       100
                  ....*....|....*....|....*...
gi 2098122732 469 AETekvfSEDFFGKLDGVANALDNVDAR 496
Cdd:cd01487    79 ENN----LEGLFGDCDIVVEAFDNAETK 102
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 34-124 2.67e-10

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: 61.50  E-value: 2.67e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732  34 LHDLSSQFYLTEADIGKNRAEASCAQLAELNSYVRTVSHTGPLT----EEFLRKFRVVVLTNSDGEEQQRIGKFAHENGI 109
Cdd:pfam00899  57 LSNLNRQFLFREADIGKPKAEVAAERLREINPDVEVEAYTERLTpenaEELIKSFDIVVDATDNFAARYLVNDACVKLGK 136

                          90
                  ....*....|....*
gi 2098122732 110 ALIIAETRGLFAKVF 124
Cdd:pfam00899 137 PLIEAGVLGFKGQVT 151
PRK15116 PRK15116
sulfur acceptor protein CsdL; Provisional
 365-517 5.08e-10

sulfur acceptor protein CsdL; Provisional


Pssm-ID: 185071  Cd Length: 268  Bit Score: 61.36  E-value: 5.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 365 SRYDSQIAIFGKKFQEKLADSKWFIVGAGAIG---CELLKNfgmlglgTGKGQIFVTDMDLIEKSNLNRQFLFRPHDVQK 441
Cdd:PRK15116   11 QRFGGTARLYGEKALQLFADAHICVVGIGGVGswaAEALAR-------TGIGAITLIDMDDVCVTNTNRQIHALRDNVGL 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2098122732 442 PKSMTAADAIKRMNPEVNVTAYELRVGAE-TEKVFSEDFfgklDGVANALDNVDARIYMDRKCIFNRIPLVETGTLG 517
Cdd:PRK15116   84 AKAEVMAERIRQINPECRVTVVDDFITPDnVAEYMSAGF----SYVIDAIDSVRPKAALIAYCRRNKIPLVTTGGAG 156
PRK14851 PRK14851
hypothetical protein; Provisional
 347-527 6.43e-10

hypothetical protein; Provisional


Pssm-ID: 184853 [Multi-domain]  Cd Length: 679  Bit Score: 62.96  E-value: 6.43e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 347 LECLPTEGVEEADAQPVGSrYDSQIAIFGKKFQEKLADSKWFIVGAGAIGCELLKNFgmlgLGTGKGQIFVTDMDLIEKS 426
Cdd:PRK14851    7 LETLQTLGISSAAEYREAA-FSRNIGLFTPGEQERLAEAKVAIPGMGGVGGVHLITM----VRTGIGRFHIADFDQFEPV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 427 NLNRQFLFRPHDVQKPKSMTAADAIKRMNPEVNVTAYELRVGAETEKVFsedffgkLDGVANALDNVDARIYMDRKCIFN 506
Cdd:PRK14851   82 NVNRQFGARVPSFGRPKLAVMKEQALSINPFLEITPFPAGINADNMDAF-------LDGVDVVLDGLDFFQFEIRRTLFN 154

                         170       180
                  ....*....|....*....|....*.
gi 2098122732 507 R-----IPLVETGTLGTLGNVQVIVP 527
Cdd:PRK14851  155 MarekgIPVITAGPLGYSSAMLVFTP 180
APPBP1_RUB cd01493
Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric ...
 366-527 1.35e-08

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: 58.08  E-value: 1.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 366 RYDSQIAIFGKKFQEKLADSKWFIVGAGAIGCELLKNfgmLGLGtGKGQIFVTDMDLIEKSNLNRQFLFRPHDVQKPKSM 445
Cdd:cd01493     2 KYDRQLRLWGEHGQAALESAHVCLLNATATGTEILKN---LVLP-GIGSFTIVDGSKVDEEDLGNNFFLDASSLGKSRAE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 446 TAADAIKRMNPEVNVTAYELRVGAETEKvfSEDFFGKLDGV--ANALDNVDARiyMDRKCIFNRIPLVETGTLGTLGNVQ 523
Cdd:cd01493    78 ATCELLQELNPDVNGSAVEESPEALLDN--DPSFFSQFTVViaTNLPESTLLR--LADVLWSANIPLLYVRSYGLYGYIR 153


                  ....
gi 2098122732 524 VIVP 527
Cdd:cd01493   154 IQLK 157
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
379-511 2.39e-08

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 57.44  E-value: 2.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 379 QEKLADSKWFIVGAGAIGCELLKNFGMLGLGtgkgQIFVTDMDLIEKSNLNRQFLFRPHDVQKPKSMTAADAIKRMNPEV 458
Cdd:PRK07411   33 QKRLKAASVLCIGTGGLGSPLLLYLAAAGIG----RIGIVDFDVVDSSNLQRQVIHGTSWVGKPKIESAKNRILEINPYC 108

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2098122732 459 NVTAYELRVGAETekvfSEDFFGKLDGVANALDNVDARIYMDRKCIFNRIPLV 511
Cdd:PRK07411  109 QVDLYETRLSSEN----ALDILAPYDVVVDGTDNFPTRYLVNDACVLLNKPNV 157
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 31-120 1.77e-07

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: 51.50  E-value: 1.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732  31 VLQLHDLSSQFYLTEADIGKNRAEASCAQLAELNSYVRTVSHT----GPLTEEFLRKFRVVVLTNSDGEEQQRIGKFAHE 106
Cdd:cd01483    33 TVELSNLNRQFLARQADIGKPKAEVAARRLNELNPGVNVTAVPegisEDNLDDFLDGVDLVIDAIDNIAVRRALNRACKE 112

                          90
                  ....*....|....
gi 2098122732 107 NGIALIIAETRGLF 120
Cdd:cd01483   113 LGIPVIDAGGLGLG 126
Apg7 cd01486
Apg7 is an E1-like protein, that activates two different ubiquitin-like proteins, Apg12 and ...
 386-467 2.06e-07

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: 53.92  E-value: 2.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 386 KWFIVGAGAIGCELLKNFgmlgLGTGKGQIFVTDMDLIEKSNLNRQFLFRPHDVQ--KPKSMTAADAIKRMNPEVNVTAY 463
Cdd:cd01486     1 KCLLLGAGTLGCNVARNL----LGWGVRHITFVDSGKVSYSNPVRQSLFTFEDCKggKPKAEAAAERLKEIFPSIDATGI 76


                  ....
gi 2098122732 464 ELRV 467
Cdd:cd01486    77 VLSI 80
PRK08223 PRK08223
hypothetical protein; Validated
 379-527 5.69e-07

hypothetical protein; Validated


Pssm-ID: 181302 [Multi-domain]  Cd Length: 287  Bit Score: 52.38  E-value: 5.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 379 QEKLADSKWFIVGAGAIGCELLKNFGMLGLGtgkgQIFVTDMDLIEKSNLNRQFLFRPHDVQKPKSMTAADAIKRMNPEV 458
Cdd:PRK08223   22 QQRLRNSRVAIAGLGGVGGIHLLTLARLGIG----KFTIADFDVFELRNFNRQAGAMMSTLGRPKAEVLAEMVRDINPEL 97

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2098122732 459 NVTAYELRVGAETEKVFsedffgkLDGVANALDNVDARIYMDRKCIFNR-----IPLVETGTLGTLGNVQVIVP 527
Cdd:PRK08223   98 EIRAFPEGIGKENADAF-------LDGVDVYVDGLDFFEFDARRLVFAAcqqrgIPALTAAPLGMGTALLVFDP 164
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 813-868 7.48e-07

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: 51.49  E-value: 7.48e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2098122732 813 IATTTSVLSGLAVLEVIKLIVGHrDLVKFKNGFANLALPFMAFSEPVPAAKNTYYG 868
Cdd:pfam00899 183 LGPTTAVVAGLQALEALKLLLGK-GEPNLAGRLLQFDALTMTFRELRLALKNPNCP 237
APPBP1_RUB cd01493
Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric ...
 36-119 2.65e-06

Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric activating enzyme (E1), specific for the Rub family of ubiquitin-like proteins (Ubls). E1 enzymes are part of a conjugation cascade to attach Ub or Ubls, covalently to substrate proteins consisting of activating (E1), conjugating (E2), and/or ligating (E3) enzymes. E1 activates ubiquitin(-like) by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and Ubls C-terminus. E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. Post-translational modification by Rub family of ubiquitin-like proteins (Ublps) activates SCF ubiquitin ligases and is involved in cell cycle control, signaling and embryogenesis. ABPP1 contains part of the adenylation domain.


Pssm-ID: 238770 [Multi-domain]  Cd Length: 425  Bit Score: 50.77  E-value: 2.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732  36 DLSSQFYLTEADIGKNRAEASCAQLAELNSYV----RTVSHTGPLTE--EFLRKFRVVVLTNSDGEEQQRIGKFAHENGI 109
Cdd:cd01493    59 DLGNNFFLDASSLGKSRAEATCELLQELNPDVngsaVEESPEALLDNdpSFFSQFTVVIATNLPESTLLRLADVLWSANI 138

                          90
                  ....*....|
gi 2098122732 110 ALIIAETRGL 119
Cdd:cd01493   139 PLLYVRSYGL 148
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 34-114 1.53e-05

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: 47.43  E-value: 1.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732  34 LHDLSSQFYLTEADIGKNRAEASCAQLAELNSYVRTVSHTGPLTE----EFLRKFRVVVltnsDG----EEQQRIGKFAH 105
Cdd:COG0476    64 LSNLQRQILYTEADVGRPKVEAAAERLRALNPDVEVEAIPERLTEenalELLAGADLVL----DCtdnfATRYLLNDACV 139


                  ....*....
gi 2098122732 106 ENGIALIIA 114
Cdd:COG0476   140 KLGIPLVSG 148
Ube1_repeat1 cd01491
Ubiquitin activating enzyme (E1), repeat 1. E1, a highly conserved small protein present ...
 367-464 1.96e-05

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: 47.65  E-value: 1.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 367 YDSQIAIFGKKFQEKLADSKWFIVGAGAIGCELLKNfgmLGLGtGKGQIFVTDMDLIEKSNLNRQFLFRPHDVQKPKSMT 446
Cdd:cd01491     2 YSRQLYVLGHEAMKKLQKSNVLISGLGGLGVEIAKN---LILA-GVKSVTLHDTKPCSWSDLSSQFYLREEDIGKNRAEA 77

                          90
                  ....*....|....*...
gi 2098122732 447 AADAIKRMNPEVNVTAYE 464
Cdd:cd01491    78 SQARLAELNPYVPVTVST 95
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 367-462 5.65e-05

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: 47.19  E-value: 5.65e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732  367 YDSQIAIFGKKFQEKLADSKWFIVGAGAIGCELLKNFGMLGLGTgkgqIFVTDMDLIEKSNLNRQFLFRPHDVQKPKSMT 446
Cdd:TIGR01408    7 YSRQLYVLGDEAMQKMAKSNVLISGMGGLGLEIAKNLVLAGVKS----VTLHDTEKCQAWDLSSNFFLSEDDVGRNRAEA 82

                           90
                   ....*....|....*.
gi 2098122732  447 AADAIKRMNPEVNVTA 462
Cdd:TIGR01408   83 VVKKLAELNPYVHVSS 98
Aos1_SUMO cd01492
Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating ...
 314-349 1.07e-04

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: 44.20  E-value: 1.07e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2098122732 314 PLDAAVGGIVAQEVLKACSGKFTPIYQWLYFDALEC 349
Cdd:cd01492   157 PVAAVVGGILAQDVINALSKRESPLNNFFVFDGETS 192
E1_like_apg7 TIGR01381
E1-like protein-activating enzyme Gsa7p/Apg7p; This model represents a family of eukaryotic ...
 380-478 1.68e-04

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


Pssm-ID: 273590 [Multi-domain]  Cd Length: 664  Bit Score: 45.32  E-value: 1.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 380 EKLADSKWFIVGAGAIGCELLKNFgmlgLGTGKGQIFVTDMDLIEKSNLNRQFLFRPHDVQ---KPKSMTAADAIKRMNP 456
Cdd:TIGR01381 334 ERYSQLKVLLLGAGTLGCNVARCL----IGWGVRHITFVDNGKVSYSNPVRQSLSNFEDCLlggRGKAETAQKALKRIFP 409

                          90       100
                  ....*....|....*....|..
gi 2098122732 457 EVNVTAYELRVGAETEKVFSED 478
Cdd:TIGR01381 410 SIQATGHRLTVPMPGHPIDEKD 431
PRK14852 PRK14852
hypothetical protein; Provisional
 379-527 2.85e-03

hypothetical protein; Provisional


Pssm-ID: 184854 [Multi-domain]  Cd Length: 989  Bit Score: 41.60  E-value: 2.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 379 QEKLADSKWFIVGAGAIGCELLKNFGMlglgTGKGQIFVTDMDLIEKSNLNRQFLFRPHDVQKPKSMTAADAIKRMNPEV 458
Cdd:PRK14852  327 QRRLLRSRVAIAGLGGVGGIHLMTLAR----TGIGNFNLADFDAYSPVNLNRQYGASIASFGRGKLDVMTERALSVNPFL 402

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2098122732 459 NVTAYELRVGAETEKVFSEDFFGKLDGVA-NALDnvdariymDRKCIFNR-----IPLVETGTLGTLGNVQVIVP 527
Cdd:PRK14852  403 DIRSFPEGVAAETIDAFLKDVDLLVDGIDfFALD--------IRRRLFNRalelgIPVITAGPLGYSCALLVFMP 469
PRK07877 PRK07877
Rv1355c family protein;
413-519 5.32e-03

Rv1355c family protein;


Pssm-ID: 236122 [Multi-domain]  Cd Length: 722  Bit Score: 40.74  E-value: 5.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098122732 413 GQIFVTDMDLIEKSNLNRQflfrP---HDVQKPKSMTAADAIKRMNPEVNVTAYELRVGAETekvfSEDFFGKLDGVANA 489
Cdd:PRK07877  132 GELRLADFDTLELSNLNRV----PagvFDLGVNKAVVAARRIAELDPYLPVEVFTDGLTEDN----VDAFLDGLDVVVEE 203

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2098122732 490 LDNVDARIYMDRKCIFNRIP-LVETGTLGTL 519
Cdd:PRK07877  204 CDSLDVKVLLREAARARRIPvLMATSDRGLL 234
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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