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Conserved domains on  [gi|38045948|ref|NP_003326|]
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ubiquitin-like modifier-activating enzyme 7 [Homo sapiens]

Protein Classification

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ube1 super family cl36897
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 10-1010 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: 817.59  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948     10 LDEELYSRQLYVLGSPAMQRIQGARVLVSGLQGLGAEVAKNLVLMGVGSLTLHDPHPTCWSDLAAQFLLSEQDLERSRAE 89
Cdd:TIGR01408    2 IDEALYSRQLYVLGDEAMQKMAKSNVLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLSSNFFLSEDDVGRNRAE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948     90 ASQELLAQLNRAVQVVVHTGDITEDLLLDFQVVVLTAAKLEEQLKVGTLCHKH--GVCFLAADTRGLVGQLFCDFGEDFT 167
Cdd:TIGR01408   82 AVVKKLAELNPYVHVSSSSVPFNEEFLDKFQCVVLTEMSLPLQKEINDFCHSQcpPIAFISADVRGLFGSLFCDFGDEFE 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948    168 VQDPTEAEPLTAAIQHISQGSPGILTLRKGaNTHYFRDGDLVTFSGIEGMVELNDCDPRSIHVREDGSLEIGDTTTFSRY 247
Cdd:TIGR01408  162 VLDTDGEEPKTGFIASITQANPGIVTCLEN-HRHKLETGDFVTFREVNGMTGLNDGSPRKITVISPYSFSIGDTTELGPY 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948    248 LRGGAITEVKRPKTVRHKSLDTALLQPHVVAQSSQEVHHAHCLHQAFCALHKFQHLHGRPPQPWDPVDAETVVGLARDLE 327
Cdd:TIGR01408  241 LHGGIATQVKTPKTVFFKSLREQLKDPKCLIVDFSKPERPPEIHTAFQALDQFQEKYSRKPNVGCQQDAEELLKLATSIS 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948    328 plkrTEEEPLEEPLDEALVRTVALSSAGVLSPMVAMLGAVAAQEVLKAISRKFMPLDQWLYFDALDCLPEDGEllPSPED 407
Cdd:TIGR01408  321 ----ETLEEKVPDVDAKLVHWLSWTAQGFLSPMAAAVGGVVSQEVLKAVTGKFSPLCQWFYFDSAESLPSLGK--PECEE 394

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948    408 CALRGSRYDGQIAVFGAGFQEKLRRQHYLLVGAGAIGCELLKVFALVGLGAGNSGGLTVVDMDHIERSNLSRQFLFRSQD 487
Cdd:TIGR01408  395 FLPRGDRYDAQIAVFGDTFQQKLQNLNIFLVGCGAIGCEMLKNFALMGVGTGKKGMITVTDPDLIEKSNLNRQFLFRPHH 474

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948    488 VGRPKAEVAAAAARGLNPDLQVIPLTYPLDPTTEHIYGDNFFSRVDGVAAALDSFQARRYVAARCTHYLKPLLEAGTSGT 567
Cdd:TIGR01408  475 IGKPKSYTAADATLKINPQIKIDAHQNRVGPETETIFNDEFYEKLDVVINALDNVEARRYVDSRCLAFLKPLLESGTLGT 554

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948    568 WGSATVFMPHVTEayrAPASAAASEDAPYPVCTVRYFPSTAEHTLQWARHEFEELFRLSAETINHHQQAHTS----LADM 643
Cdd:TIGR01408  555 KGNTQVVVPHLTE---SYGSSRDPPEKEIPFCTLKSFPAAIEHTIQWARDKFEGLFSHKPSLVNKYLSSPSSaeevLQKI 631

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948    644 DEPQTLTLLKPVLGVLRV-RPQNWQDCVAWALGHWKLCFHYGIKQLLRHFPPNKVLEDGTPFWSGPKQCPQPLEFDTNQD 722
Cdd:TIGR01408  632 QSGHSREGLEQIIKLLSKeKPRNFSQCVEWARLKFEKYFNNKALQLLHCFPLDIRTSTGSPFWSSPKRPPSPLKFDLNEP 711

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948    723 THLLYVLAAANLYAQMHGLPgSQDWTALRE-LLKLLPQPDPQQMAPifASNLELASASAEFGPEQQ--------KELNKA 793
Cdd:TIGR01408  712 LHLSFIQAAAKLYATVYGIP-FAEEDLSADaLLNILSEVKIPEFKP--RSNKKIQTDETARKPDTApiddrnaiFQLEKA 788

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948    794 LEVWS--VGP-PLKPLMFEKDDDSNFHVDFVVAAASLRCQNYGIPPVNRAQSKRIVGQIIPAIATTTAAVAGLLGLELYK 870
Cdd:TIGR01408  789 ILSNEatKSDfRMAPLSFEKDDDHNGHIDFITAASNLRAKNYSIEPADRFKTKFIAGKIIPAIATSTATVSGLVCLELIK 868

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948    871 VVSGPRPRSAFRHSYLHLAENYLIRYMPFAPAIQTFHHLKWTS-WDRLKVPaGQPerTLESLLAHLQEQHGLRVRILLHG 949
Cdd:TIGR01408  869 VTDGGYKFEVYKNCFLNLAIPLFVFTEPTEVRKTKIRNGISFTiWDRWTLH-GDF--TLLEFINAVKEKYGLEPTMVSQG 945

                          970       980       990      1000      1010      1020
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 38045948    950 SALLYAAGWSpeKQAQHLPLRVTELVQQLTGQAPAPGQRVLVLELSCE-GDDEDTAFPPLHY 1010
Cdd:TIGR01408  946 VKLLYVPVMP--GHAERLKLKMHKLVKPTTKKKLPPYRVHLTVSFACDdDGDEDVPGPPVRI 1005
 
Name Accession Description Interval E-value
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 10-1010 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: 817.59  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948     10 LDEELYSRQLYVLGSPAMQRIQGARVLVSGLQGLGAEVAKNLVLMGVGSLTLHDPHPTCWSDLAAQFLLSEQDLERSRAE 89
Cdd:TIGR01408    2 IDEALYSRQLYVLGDEAMQKMAKSNVLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLSSNFFLSEDDVGRNRAE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948     90 ASQELLAQLNRAVQVVVHTGDITEDLLLDFQVVVLTAAKLEEQLKVGTLCHKH--GVCFLAADTRGLVGQLFCDFGEDFT 167
Cdd:TIGR01408   82 AVVKKLAELNPYVHVSSSSVPFNEEFLDKFQCVVLTEMSLPLQKEINDFCHSQcpPIAFISADVRGLFGSLFCDFGDEFE 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948    168 VQDPTEAEPLTAAIQHISQGSPGILTLRKGaNTHYFRDGDLVTFSGIEGMVELNDCDPRSIHVREDGSLEIGDTTTFSRY 247
Cdd:TIGR01408  162 VLDTDGEEPKTGFIASITQANPGIVTCLEN-HRHKLETGDFVTFREVNGMTGLNDGSPRKITVISPYSFSIGDTTELGPY 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948    248 LRGGAITEVKRPKTVRHKSLDTALLQPHVVAQSSQEVHHAHCLHQAFCALHKFQHLHGRPPQPWDPVDAETVVGLARDLE 327
Cdd:TIGR01408  241 LHGGIATQVKTPKTVFFKSLREQLKDPKCLIVDFSKPERPPEIHTAFQALDQFQEKYSRKPNVGCQQDAEELLKLATSIS 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948    328 plkrTEEEPLEEPLDEALVRTVALSSAGVLSPMVAMLGAVAAQEVLKAISRKFMPLDQWLYFDALDCLPEDGEllPSPED 407
Cdd:TIGR01408  321 ----ETLEEKVPDVDAKLVHWLSWTAQGFLSPMAAAVGGVVSQEVLKAVTGKFSPLCQWFYFDSAESLPSLGK--PECEE 394

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948    408 CALRGSRYDGQIAVFGAGFQEKLRRQHYLLVGAGAIGCELLKVFALVGLGAGNSGGLTVVDMDHIERSNLSRQFLFRSQD 487
Cdd:TIGR01408  395 FLPRGDRYDAQIAVFGDTFQQKLQNLNIFLVGCGAIGCEMLKNFALMGVGTGKKGMITVTDPDLIEKSNLNRQFLFRPHH 474

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948    488 VGRPKAEVAAAAARGLNPDLQVIPLTYPLDPTTEHIYGDNFFSRVDGVAAALDSFQARRYVAARCTHYLKPLLEAGTSGT 567
Cdd:TIGR01408  475 IGKPKSYTAADATLKINPQIKIDAHQNRVGPETETIFNDEFYEKLDVVINALDNVEARRYVDSRCLAFLKPLLESGTLGT 554

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948    568 WGSATVFMPHVTEayrAPASAAASEDAPYPVCTVRYFPSTAEHTLQWARHEFEELFRLSAETINHHQQAHTS----LADM 643
Cdd:TIGR01408  555 KGNTQVVVPHLTE---SYGSSRDPPEKEIPFCTLKSFPAAIEHTIQWARDKFEGLFSHKPSLVNKYLSSPSSaeevLQKI 631

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948    644 DEPQTLTLLKPVLGVLRV-RPQNWQDCVAWALGHWKLCFHYGIKQLLRHFPPNKVLEDGTPFWSGPKQCPQPLEFDTNQD 722
Cdd:TIGR01408  632 QSGHSREGLEQIIKLLSKeKPRNFSQCVEWARLKFEKYFNNKALQLLHCFPLDIRTSTGSPFWSSPKRPPSPLKFDLNEP 711

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948    723 THLLYVLAAANLYAQMHGLPgSQDWTALRE-LLKLLPQPDPQQMAPifASNLELASASAEFGPEQQ--------KELNKA 793
Cdd:TIGR01408  712 LHLSFIQAAAKLYATVYGIP-FAEEDLSADaLLNILSEVKIPEFKP--RSNKKIQTDETARKPDTApiddrnaiFQLEKA 788

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948    794 LEVWS--VGP-PLKPLMFEKDDDSNFHVDFVVAAASLRCQNYGIPPVNRAQSKRIVGQIIPAIATTTAAVAGLLGLELYK 870
Cdd:TIGR01408  789 ILSNEatKSDfRMAPLSFEKDDDHNGHIDFITAASNLRAKNYSIEPADRFKTKFIAGKIIPAIATSTATVSGLVCLELIK 868

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948    871 VVSGPRPRSAFRHSYLHLAENYLIRYMPFAPAIQTFHHLKWTS-WDRLKVPaGQPerTLESLLAHLQEQHGLRVRILLHG 949
Cdd:TIGR01408  869 VTDGGYKFEVYKNCFLNLAIPLFVFTEPTEVRKTKIRNGISFTiWDRWTLH-GDF--TLLEFINAVKEKYGLEPTMVSQG 945

                          970       980       990      1000      1010      1020
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 38045948    950 SALLYAAGWSpeKQAQHLPLRVTELVQQLTGQAPAPGQRVLVLELSCE-GDDEDTAFPPLHY 1010
Cdd:TIGR01408  946 VKLLYVPVMP--GHAERLKLKMHKLVKPTTKKKLPPYRVHLTVSFACDdDGDEDVPGPPVRI 1005
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
 434-967 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: 632.40  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948  434 HYLLVGAGAIGCELLKVFALVGLGAGNSGGLTVVDMDHIERSNLSRQFLFRSQDVGRPKAEVAAAAARGLNPDLQVIPLT 513
Cdd:cd01490    1 KVFLVGAGAIGCELLKNFALMGVGTGESGEITVTDMDNIEKSNLNRQFLFRPHDVGKPKSEVAAAAVKAMNPDLKITALQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948  514 YPLDPTTEHIYGDNFFSRVDGVAAALDSFQARRYVAARCTHYLKPLLEAGTSGTWGSATVFMPHVTEayrAPASAAASED 593
Cdd:cd01490   81 NRVGPETEHIFNDEFWEKLDGVANALDNVDARMYVDRRCVYYRKPLLESGTLGTKGNTQVVIPHLTE---SYSSSRDPPE 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948  594 APYPVCTVRYFPSTAEHTLQWARHEFEELFRLSAETINHHQqahtsladmdepqtltllkpvlgvlrvrpqnWQDCVAWA 673
Cdd:cd01490  158 KSIPLCTLKNFPNAIEHTIQWARDEFEGLFKQPPENVNQYL-------------------------------FEDCVRWA 206

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948  674 LGHWKLCFHYGIKQLLRHFPPNKVLEDGTPFWSGPKQCPQPLEFDTNQDTHLLYVLAAANLYAQMHGLPGsqdwtalrel 753
Cdd:cd01490  207 RLLFEKYFNNNIKQLLHNFPPDAVTSDGAPFWSGPKRCPTPLEFDVNNPLHLDFVLAAANLYAEVYGIPG---------- 276

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948  754 lkllpqpdpqqmapifasnlelasasaefgpeqqkelnkalevwsvgpplkplmFEKDDDSNFHVDFVVAAASLRCQNYG 833
Cdd:cd01490  277 ------------------------------------------------------FEKDDDTNFHMDFITAASNLRARNYS 302

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948  834 IPPVNRAQSKRIVGQIIPAIATTTAAVAGLLGLELYKVVSGPRPRSAFRHSYLHLAENYLIRYMPFAPAIQTF-HHLKWT 912
Cdd:cd01490  303 IPPADRHKTKRIAGKIIPAIATTTAAVTGLVCLELYKVVDGKRPLEAYKNAFLNLALPFFAFSEPIPAPKVKYaYDEEWT 382

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 38045948  913 SWDRLKVPAGQPERtlESLLAHLQEQHGLRVRILLHGSALLYAAGWSPEKQAQHL 967
Cdd:cd01490  383 IWDRFEVKGKQTLQ--ELLIDYFKEKYGLEVTMLSQGVSMLYSSFMPPAKLKERL 435
UBA_E1_SCCH pfam10585
Ubiquitin-activating enzyme, SCCH domain; Ubiquitin-activating enzyme (E1 enzyme) activates ...
 605-843 2.24e-110

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: 341.90  E-value: 2.24e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948    605 PSTAEHTLQWARHEFEELFRLSAETINHHQQAH----TSLADMDEPQTLTLLKPVLGVL-RVRPQNWQDCVAWALGHWKL 679
Cdd:pfam10585    1 PNAIEHTIQWARDEFEGLFVQPPEEVNKYLQPPqnfiESLLKQGGGQKLETLESVRKSLvTERPKTFEDCVAWARLKFEK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948    680 CFHYGIKQLLRHFPPNKVLEDGTPFWSGPKQCPQPLEFDTNQDTHLLYVLAAANLYAQMHGLPGSQDWTALRELLKLLPQ 759
Cdd:pfam10585   81 LFNNDIKQLLYNFPPDHKTSSGAPFWSGPKRPPTPLEFDPNNPLHLDFVVAAANLRAQVYGIPGSRDREAIAKVLSKVKV 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948    760 PD--PQQMAPIFASNLELASASA--EFGPEQQKELNKALEVWSVGPP------LKPLMFEKDDDSNFHVDFVVAAASLRC 829
Cdd:pfam10585  161 PEfkPKSGVKIQVNDEEAADPNAesEDDEDELDELLEELPKLAVSPSslagfrLNPIEFEKDDDTNFHIDFITAASNLRA 240

                          250
                   ....*....|....
gi 38045948    830 QNYGIPPVNRAQSK 843
Cdd:pfam10585  241 RNYGIPPADRHKTK 254
UBA_e1_C smart00985
Ubiquitin-activating enzyme e1 C-terminal domain; This presumed domain found at the C terminus ...
 881-1008 1.21e-51

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: 177.07  E-value: 1.21e-51
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948     881 FRHSYLHLAENYLIRYMPFAPAIQTFHH-LKWTSWDRLKVPagQPERTLESLLAHLQEQHGLRVRILLHGSALLYAAGWS 959
Cdd:smart00985    1 YKNAFLNLALPFFAFSEPIAAPKTKYRDkDKWTLWDRLEVP--GGDITLKELLDYFEEKYGLEVTMLSQGVSLLYSSFMP 78

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|
gi 38045948     960 PEKQAQHLPLRVTELVQQLTGQAPAPGQRVLVLELSCEG-DDEDTAFPPL 1008
Cdd:smart00985   79 PKKHKERLDLPVTELVEQVTKKKLPPHVKYLVLEVSCEDeDDEDVEVPYI 128
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 414-579 3.71e-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: 137.18  E-value: 3.71e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948  414 RYDGQIAVFGAGF--QEKLRRQHYLLVGAGAIGCELLkvFALVGLGAGNsggLTVVDMDHIERSNLSRQFLFRSQDVGRP 491
Cdd:COG0476    7 RYSRQILLPEIGEegQEKLKAARVLVVGAGGLGSPVA--LYLAAAGVGT---LTLVDDDVVELSNLQRQILYTEADVGRP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948  492 KAEVAAAAARGLNPDLQVIPLTYPLDPTTehiyGDNFFSRVDGVAAALDSFQARRYVAARCTHYLKPLLEAGTSGTWGSA 571
Cdd:COG0476   82 KVEAAAERLRALNPDVEVEAIPERLTEEN----ALELLAGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIGFEGQV 157


                 ....*...
gi 38045948  572 TVFMPHVT 579
Cdd:COG0476  158 TVFIPGDT 165
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 414-580 2.32e-20

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 91.44  E-value: 2.32e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948   414 RYDGQIAVFGAGF--QEKLRRQHYLLVGAGAIGCELLKVFALVGLGAgnsggLTVVDMDHIERSNLSRQFLFRSQDVGRP 491
Cdd:PRK05690   12 RYNRQIILRGFDFdgQEKLKAARVLVVGLGGLGCAASQYLAAAGVGT-----LTLVDFDTVSLSNLQRQVLHDDATIGQP 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948   492 KAEVAAAAARGLNPDLQVIPLTYPLDPTTehiyGDNFFSRVDGVAAALDSFQARRYVAARCTHYLKPLLEAGTSGTWGSA 571
Cdd:PRK05690   87 KVESARAALARINPHIAIETINARLDDDE----LAALIAGHDLVLDCTDNVATRNQLNRACFAAKKPLVSGAAIRMEGQV 162


                  ....*....
gi 38045948   572 TVFMPHVTE 580
Cdd:PRK05690  163 TVFTYQDDE 171
 
Name Accession Description Interval E-value
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 10-1010 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: 817.59  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948     10 LDEELYSRQLYVLGSPAMQRIQGARVLVSGLQGLGAEVAKNLVLMGVGSLTLHDPHPTCWSDLAAQFLLSEQDLERSRAE 89
Cdd:TIGR01408    2 IDEALYSRQLYVLGDEAMQKMAKSNVLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLSSNFFLSEDDVGRNRAE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948     90 ASQELLAQLNRAVQVVVHTGDITEDLLLDFQVVVLTAAKLEEQLKVGTLCHKH--GVCFLAADTRGLVGQLFCDFGEDFT 167
Cdd:TIGR01408   82 AVVKKLAELNPYVHVSSSSVPFNEEFLDKFQCVVLTEMSLPLQKEINDFCHSQcpPIAFISADVRGLFGSLFCDFGDEFE 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948    168 VQDPTEAEPLTAAIQHISQGSPGILTLRKGaNTHYFRDGDLVTFSGIEGMVELNDCDPRSIHVREDGSLEIGDTTTFSRY 247
Cdd:TIGR01408  162 VLDTDGEEPKTGFIASITQANPGIVTCLEN-HRHKLETGDFVTFREVNGMTGLNDGSPRKITVISPYSFSIGDTTELGPY 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948    248 LRGGAITEVKRPKTVRHKSLDTALLQPHVVAQSSQEVHHAHCLHQAFCALHKFQHLHGRPPQPWDPVDAETVVGLARDLE 327
Cdd:TIGR01408  241 LHGGIATQVKTPKTVFFKSLREQLKDPKCLIVDFSKPERPPEIHTAFQALDQFQEKYSRKPNVGCQQDAEELLKLATSIS 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948    328 plkrTEEEPLEEPLDEALVRTVALSSAGVLSPMVAMLGAVAAQEVLKAISRKFMPLDQWLYFDALDCLPEDGEllPSPED 407
Cdd:TIGR01408  321 ----ETLEEKVPDVDAKLVHWLSWTAQGFLSPMAAAVGGVVSQEVLKAVTGKFSPLCQWFYFDSAESLPSLGK--PECEE 394

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948    408 CALRGSRYDGQIAVFGAGFQEKLRRQHYLLVGAGAIGCELLKVFALVGLGAGNSGGLTVVDMDHIERSNLSRQFLFRSQD 487
Cdd:TIGR01408  395 FLPRGDRYDAQIAVFGDTFQQKLQNLNIFLVGCGAIGCEMLKNFALMGVGTGKKGMITVTDPDLIEKSNLNRQFLFRPHH 474

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948    488 VGRPKAEVAAAAARGLNPDLQVIPLTYPLDPTTEHIYGDNFFSRVDGVAAALDSFQARRYVAARCTHYLKPLLEAGTSGT 567
Cdd:TIGR01408  475 IGKPKSYTAADATLKINPQIKIDAHQNRVGPETETIFNDEFYEKLDVVINALDNVEARRYVDSRCLAFLKPLLESGTLGT 554

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948    568 WGSATVFMPHVTEayrAPASAAASEDAPYPVCTVRYFPSTAEHTLQWARHEFEELFRLSAETINHHQQAHTS----LADM 643
Cdd:TIGR01408  555 KGNTQVVVPHLTE---SYGSSRDPPEKEIPFCTLKSFPAAIEHTIQWARDKFEGLFSHKPSLVNKYLSSPSSaeevLQKI 631

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948    644 DEPQTLTLLKPVLGVLRV-RPQNWQDCVAWALGHWKLCFHYGIKQLLRHFPPNKVLEDGTPFWSGPKQCPQPLEFDTNQD 722
Cdd:TIGR01408  632 QSGHSREGLEQIIKLLSKeKPRNFSQCVEWARLKFEKYFNNKALQLLHCFPLDIRTSTGSPFWSSPKRPPSPLKFDLNEP 711

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948    723 THLLYVLAAANLYAQMHGLPgSQDWTALRE-LLKLLPQPDPQQMAPifASNLELASASAEFGPEQQ--------KELNKA 793
Cdd:TIGR01408  712 LHLSFIQAAAKLYATVYGIP-FAEEDLSADaLLNILSEVKIPEFKP--RSNKKIQTDETARKPDTApiddrnaiFQLEKA 788

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948    794 LEVWS--VGP-PLKPLMFEKDDDSNFHVDFVVAAASLRCQNYGIPPVNRAQSKRIVGQIIPAIATTTAAVAGLLGLELYK 870
Cdd:TIGR01408  789 ILSNEatKSDfRMAPLSFEKDDDHNGHIDFITAASNLRAKNYSIEPADRFKTKFIAGKIIPAIATSTATVSGLVCLELIK 868

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948    871 VVSGPRPRSAFRHSYLHLAENYLIRYMPFAPAIQTFHHLKWTS-WDRLKVPaGQPerTLESLLAHLQEQHGLRVRILLHG 949
Cdd:TIGR01408  869 VTDGGYKFEVYKNCFLNLAIPLFVFTEPTEVRKTKIRNGISFTiWDRWTLH-GDF--TLLEFINAVKEKYGLEPTMVSQG 945

                          970       980       990      1000      1010      1020
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 38045948    950 SALLYAAGWSpeKQAQHLPLRVTELVQQLTGQAPAPGQRVLVLELSCE-GDDEDTAFPPLHY 1010
Cdd:TIGR01408  946 VKLLYVPVMP--GHAERLKLKMHKLVKPTTKKKLPPYRVHLTVSFACDdDGDEDVPGPPVRI 1005
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
 434-967 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: 632.40  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948  434 HYLLVGAGAIGCELLKVFALVGLGAGNSGGLTVVDMDHIERSNLSRQFLFRSQDVGRPKAEVAAAAARGLNPDLQVIPLT 513
Cdd:cd01490    1 KVFLVGAGAIGCELLKNFALMGVGTGESGEITVTDMDNIEKSNLNRQFLFRPHDVGKPKSEVAAAAVKAMNPDLKITALQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948  514 YPLDPTTEHIYGDNFFSRVDGVAAALDSFQARRYVAARCTHYLKPLLEAGTSGTWGSATVFMPHVTEayrAPASAAASED 593
Cdd:cd01490   81 NRVGPETEHIFNDEFWEKLDGVANALDNVDARMYVDRRCVYYRKPLLESGTLGTKGNTQVVIPHLTE---SYSSSRDPPE 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948  594 APYPVCTVRYFPSTAEHTLQWARHEFEELFRLSAETINHHQqahtsladmdepqtltllkpvlgvlrvrpqnWQDCVAWA 673
Cdd:cd01490  158 KSIPLCTLKNFPNAIEHTIQWARDEFEGLFKQPPENVNQYL-------------------------------FEDCVRWA 206

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948  674 LGHWKLCFHYGIKQLLRHFPPNKVLEDGTPFWSGPKQCPQPLEFDTNQDTHLLYVLAAANLYAQMHGLPGsqdwtalrel 753
Cdd:cd01490  207 RLLFEKYFNNNIKQLLHNFPPDAVTSDGAPFWSGPKRCPTPLEFDVNNPLHLDFVLAAANLYAEVYGIPG---------- 276

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948  754 lkllpqpdpqqmapifasnlelasasaefgpeqqkelnkalevwsvgpplkplmFEKDDDSNFHVDFVVAAASLRCQNYG 833
Cdd:cd01490  277 ------------------------------------------------------FEKDDDTNFHMDFITAASNLRARNYS 302

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948  834 IPPVNRAQSKRIVGQIIPAIATTTAAVAGLLGLELYKVVSGPRPRSAFRHSYLHLAENYLIRYMPFAPAIQTF-HHLKWT 912
Cdd:cd01490  303 IPPADRHKTKRIAGKIIPAIATTTAAVTGLVCLELYKVVDGKRPLEAYKNAFLNLALPFFAFSEPIPAPKVKYaYDEEWT 382

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 38045948  913 SWDRLKVPAGQPERtlESLLAHLQEQHGLRVRILLHGSALLYAAGWSPEKQAQHL 967
Cdd:cd01490  383 IWDRFEVKGKQTLQ--ELLIDYFKEKYGLEVTMLSQGVSMLYSSFMPPAKLKERL 435
Ube1_repeat1 cd01491
Ubiquitin activating enzyme (E1), repeat 1. E1, a highly conserved small protein present ...
 14-399 2.61e-149

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: 444.79  E-value: 2.61e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948   14 LYSRQLYVLGSPAMQRIQGARVLVSGLQGLGAEVAKNLVLMGVGSLTLHDPHPTCWSDLAAQFLLSEQDLERSRAEASQE 93
Cdd:cd01491    1 LYSRQLYVLGHEAMKKLQKSNVLISGLGGLGVEIAKNLILAGVKSVTLHDTKPCSWSDLSSQFYLREEDIGKNRAEASQA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948   94 LLAQLNRAVQVVVHTGDITEDLLLDFQVVVLTAAKLEEQLKVGTLCHKHGVCFLAADTRGLVGQLFCDFGEDFTVQDPTE 173
Cdd:cd01491   81 RLAELNPYVPVTVSTGPLTTDELLKFQVVVLTDASLEDQLKINEFCHSPGIKFISADTRGLFGSIFCDFGDEFTVYDPNG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948  174 AEPLTAAIQHISQGSPGILTlRKGANTHYFRDGDLVTFSGIEGMVELNDCDPRSIHVREDGSLEIGDTTTFSRYLRGGAI 253
Cdd:cd01491  161 EEPKSGMISSISKDNPGVVT-CLDETRHGFEDGDYVTFSEVEGMTELNGCEPRKIKVKGPYTFSIGDTSSFSEYIRGGIV 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948  254 TEVKrpktvrhksldtallqphvvaqssqevhhahclhqafcalhkfqhlhgrppqpwdpvdaetvvglardleplkrte 333
Cdd:cd01491  240 TQVK---------------------------------------------------------------------------- 243

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 38045948  334 eepleepldealvrtvalssagvLSPMVAMLGAVAAQEVLKAISRKFMPLDQWLYFDALDCLPEDG 399
Cdd:cd01491  244 -----------------------LSPMAAFFGGLAAQEVLKACSGKFTPLKQWLYFDALECLPEDE 286
UBA_E1_SCCH pfam10585
Ubiquitin-activating enzyme, SCCH domain; Ubiquitin-activating enzyme (E1 enzyme) activates ...
 605-843 2.24e-110

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: 341.90  E-value: 2.24e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948    605 PSTAEHTLQWARHEFEELFRLSAETINHHQQAH----TSLADMDEPQTLTLLKPVLGVL-RVRPQNWQDCVAWALGHWKL 679
Cdd:pfam10585    1 PNAIEHTIQWARDEFEGLFVQPPEEVNKYLQPPqnfiESLLKQGGGQKLETLESVRKSLvTERPKTFEDCVAWARLKFEK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948    680 CFHYGIKQLLRHFPPNKVLEDGTPFWSGPKQCPQPLEFDTNQDTHLLYVLAAANLYAQMHGLPGSQDWTALRELLKLLPQ 759
Cdd:pfam10585   81 LFNNDIKQLLYNFPPDHKTSSGAPFWSGPKRPPTPLEFDPNNPLHLDFVVAAANLRAQVYGIPGSRDREAIAKVLSKVKV 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948    760 PD--PQQMAPIFASNLELASASA--EFGPEQQKELNKALEVWSVGPP------LKPLMFEKDDDSNFHVDFVVAAASLRC 829
Cdd:pfam10585  161 PEfkPKSGVKIQVNDEEAADPNAesEDDEDELDELLEELPKLAVSPSslagfrLNPIEFEKDDDTNFHIDFITAASNLRA 240

                          250
                   ....*....|....
gi 38045948    830 QNYGIPPVNRAQSK 843
Cdd:pfam10585  241 RNYGIPPADRHKTK 254
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 415-580 1.65e-55

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: 192.47  E-value: 1.65e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948    415 YDGQIA--VFGAGFQEKLRRQHYLLVGAGAIGCELLKVFALVGLGagnsgGLTVVDMDHIERSNLSRQFLFRSQDVGRPK 492
Cdd:pfam00899    1 YSRQLAlpLIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVG-----KITLVDFDTVELSNLNRQFLFREADIGKPK 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948    493 AEVAAAAARGLNPDLQVIPLTYPLDPTTehiyGDNFFSRVDGVAAALDSFQARRYVAARCTHYLKPLLEAGTSGTWGSAT 572
Cdd:pfam00899   76 AEVAAERLREINPDVEVEAYTERLTPEN----AEELIKSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVT 151


                   ....*...
gi 38045948    573 VFMPHVTE 580
Cdd:pfam00899  152 VVIPGKTP 159
UBA_e1_C smart00985
Ubiquitin-activating enzyme e1 C-terminal domain; This presumed domain found at the C terminus ...
 881-1008 1.21e-51

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: 177.07  E-value: 1.21e-51
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948     881 FRHSYLHLAENYLIRYMPFAPAIQTFHH-LKWTSWDRLKVPagQPERTLESLLAHLQEQHGLRVRILLHGSALLYAAGWS 959
Cdd:smart00985    1 YKNAFLNLALPFFAFSEPIAAPKTKYRDkDKWTLWDRLEVP--GGDITLKELLDYFEEKYGLEVTMLSQGVSLLYSSFMP 78

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|
gi 38045948     960 PEKQAQHLPLRVTELVQQLTGQAPAPGQRVLVLELSCEG-DDEDTAFPPL 1008
Cdd:smart00985   79 PKKHKERLDLPVTELVEQVTKKKLPPHVKYLVLEVSCEDeDDEDVEVPYI 128
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
 436-630 2.58e-47

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: 168.91  E-value: 2.58e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948  436 LLVGAGAIGCELLKVFALVGLGAgnsggLTVVDMDHIERSNLSRQFLFRSQDVGRPKAEVAAAAARGLNPDLQVIPLTYP 515
Cdd:cd01484    3 LLVGAGGIGCELLKNLALMGFGQ-----IHVIDMDTIDVSNLNRQFLFRPKDIGRPKSEVAAEAVNDRNPNCKVVPYQNK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948  516 LDPttEHIYGDNFFSRVDGVAAALDSFQARRYVAARCTHYLKPLLEAGTSGTWGSATVFMPHVTEayrAPASAAASEDAP 595
Cdd:cd01484   78 VGP--EQDFNDTFFEQFHIIVNALDNIIARRYVNGMLIFLIVPLIESGTEGFKGNAQVILPGMTE---CIECTLYPPQKN 152

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 38045948  596 YPVCTVRYFPSTAEHTLQWARHEFEElfrlSAETI 630
Cdd:cd01484  153 FPMCTIASMPRLPEHCIEWARMLQWD----DPEHI 183
Aos1_SUMO cd01492
Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating ...
 13-161 6.52e-39

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


Pssm-ID: 238769 [Multi-domain]  Cd Length: 197  Bit Score: 143.59  E-value: 6.52e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948   13 ELYSRQLYVLGSPAMQRIQGARVLVSGLQGLGAEVAKNLVLMGVGSLTLHDPHPTCWSDLAAQFLLSEQDLERSRAEASQ 92
Cdd:cd01492    2 ALYDRQIRLWGLEAQKRLRSARILLIGLKGLGAEIAKNLVLSGIGSLTILDDRTVTEEDLGAQFLIPAEDLGQNRAEASL 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 38045948   93 ELLAQLNRAVQVVVHTGDITE---DLLLDFQVVVLTAAKLEEQLKVGTLCHKHGVCFLAADTRGLVGQLFCD 161
Cdd:cd01492   82 ERLRALNPRVKVSVDTDDISEkpeEFFSQFDVVVATELSRAELVKINELCRKLGVKFYATGVHGLFGFVFAD 153
E1-1_like cd01485
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ...
 14-162 1.94e-38

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: 142.18  E-value: 1.94e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948   14 LYSRQLYVLGSPAMQRIQGARVLVSGLQGLGAEVAKNLVLMGVGSLTLHDPHPTCWSDLAAQFLL--SEQDLERSRAEAS 91
Cdd:cd01485    1 LYDRQIRLWGDEAQNKLRSAKVLIIGAGALGAEIAKNLVLAGIDSITIVDHRLVSTEDLGSNFFLdaEVSNSGMNRAAAS 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 38045948   92 QELLAQLNRAVQVVVHTGDI------TEDLLLDFQVVVLTAAKLEEQLKVGTLCHKHGVCFLAADTRGLVGQLFCDF 162
Cdd:cd01485   81 YEFLQELNPNVKLSIVEEDSlsndsnIEEYLQKFTLVIATEENYERTAKVNDVCRKHHIPFISCATYGLIGYAFFDF 157
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 436-624 2.16e-36

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: 140.21  E-value: 2.16e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948  436 LLVGAGAIGCELLKVFALVGLGAgnsggLTVVDMDHIERSNLSRQFLFRSQDVGRPKAEVAAAAARGLNPDLQVIPLTyp 515
Cdd:cd01489    3 LVVGAGGIGCELLKNLVLTGFGE-----IHIIDLDTIDLSNLNRQFLFRKKHVGKSKAQVAKEAVLSFNPNVKIVAYH-- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948  516 lDPTTEHIYGDNFFSRVDGVAAALDSFQARRYVAARCTHYLKPLLEAGTSGTWGSATVFMPHVTEayrAPASAAASEDAP 595
Cdd:cd01489   76 -ANIKDPDFNVEFFKQFDLVFNALDNLAARRHVNKMCLAADVPLIESGTTGFLGQVQVIKKGKTE---CYECQPKETPKT 151

                        170       180       190
                 ....*....|....*....|....*....|..
gi 38045948  596 YPVCTVRYFPSTAEHTLQWARHE---FEELFR 624
Cdd:cd01489  152 FPVCTIRSTPSQPIHCIVWAKSLfflFNKVFK 183
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 414-579 3.71e-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: 137.18  E-value: 3.71e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948  414 RYDGQIAVFGAGF--QEKLRRQHYLLVGAGAIGCELLkvFALVGLGAGNsggLTVVDMDHIERSNLSRQFLFRSQDVGRP 491
Cdd:COG0476    7 RYSRQILLPEIGEegQEKLKAARVLVVGAGGLGSPVA--LYLAAAGVGT---LTLVDDDVVELSNLQRQILYTEADVGRP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948  492 KAEVAAAAARGLNPDLQVIPLTYPLDPTTehiyGDNFFSRVDGVAAALDSFQARRYVAARCTHYLKPLLEAGTSGTWGSA 571
Cdd:COG0476   82 KVEAAAERLRALNPDVEVEAIPERLTEEN----ALELLAGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIGFEGQV 157


                 ....*...
gi 38045948  572 TVFMPHVT 579
Cdd:COG0476  158 TVFIPGDT 165
E1_UFD pfam09358
Ubiquitin fold domain; The ubiquitin fold domain is found at the C-terminus of ...
 914-1008 3.39e-34

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: 126.12  E-value: 3.39e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948    914 WDRLKVPAgqpERTLESLLAHLQEQHGLRVRILLHGSALLYAAGWSPEKQAQHLPLRVTELVQQLTGQAPAPGQRVLVLE 993
Cdd:pfam09358    1 WDRFEVEG---DMTLQELLDYFKEKYGLEVTMLSYGVSLLYSSFMPPKKHKERLPMKISELVEEVSKKPIPPHQKYLVLE 77

                           90
                   ....*....|....*.
gi 38045948    994 LSCEGDD-EDTAFPPL 1008
Cdd:pfam09358   78 VSCEDEDgEDVEVPYV 93
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 414-579 1.50e-31

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: 123.36  E-value: 1.50e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948  414 RYDGQIAV--FGAGFQEKLRRQHYLLVGAGAIGCELLkvFALVGLGAGNsggLTVVDMDHIERSNLSRQFLFRSQDVGRP 491
Cdd:cd00757    1 RYSRQILLpeIGEEGQEKLKNARVLVVGAGGLGSPAA--EYLAAAGVGK---LGLVDDDVVELSNLQRQILHTEADVGQP 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948  492 KAEVAAAAARGLNPDLQVIPLTYPLDPTTEHIygdnFFSRVDGVAAALDSFQARRYVAARCTHYLKPLLEAGTSGTWGSA 571
Cdd:cd00757   76 KAEAAAERLRAINPDVEIEAYNERLDAENAEE----LIAGYDLVLDCTDNFATRYLINDACVKLGKPLVSGAVLGFEGQV 151


                 ....*...
gi 38045948  572 TVFMPHVT 579
Cdd:cd00757  152 TVFIPGEG 159
E1_FCCH pfam16190
Ubiquitin-activating enzyme E1 FCCH domain; This domain is found in the ubiquitin-activating ...
 187-257 4.33e-31

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: 116.43  E-value: 4.33e-31
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 38045948    187 GSPGILTLRKGANtHYFRDGDLVTFSGIEGMVELNDCDPRSIHVREDGSLEIGDTTTFSRYLRGGAITEVK 257
Cdd:pfam16190    1 DNPGVVTCLDDTR-HGLEDGDYVTFSEVEGMTELNGCEPRKIKVLGPYTFSIGDTSSFSPYLRGGIVTQVK 70
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 436-616 5.41e-31

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: 123.62  E-value: 5.41e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948  436 LLVGAGAIGCELLKVFALVGLGagnsgGLTVVDMDHIERSNLSRQFLFRSQDVGRPKAEVAAAAARGLNPDLQVIPltYP 515
Cdd:cd01488    3 LVIGAGGLGCELLKNLALSGFR-----NIHVIDMDTIDVSNLNRQFLFREKDIGKPKAEVAAKFVNDRVPGVNVTP--HF 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948  516 LDPTTehiYGDNFFSRVDGVAAALDSFQARRYVAA------RCTHY--LKPLLEAGTSGTWGSATVFMPHVTeAYRAPAS 587
Cdd:cd01488   76 GKIQD---KDEEFYRQFNIIICGLDSIEARRWINGtlvsllLYEDPesIIPLIDGGTEGFKGHARVILPGIT-ACIECSL 151

                        170       180
                 ....*....|....*....|....*....
gi 38045948  588 AAASEDAPYPVCTVRYFPSTAEHTLQWAR 616
Cdd:cd01488  152 DLFPPQVTFPLCTIANTPRLPEHCIEYAS 180
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 15-181 6.90e-29

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: 116.20  E-value: 6.90e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948     15 YSRQLY--VLGSPAMQRIQGARVLVSGLQGLGAEVAKNLVLMGVGSLTLHDPHPTCWSDLAAQFLLSEQDLERSRAEASQ 92
Cdd:pfam00899    1 YSRQLAlpLIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948     93 ELLAQLNRAVQVVVHTGDIT----EDLLLDFQVVVLTAAKLEEQLKVGTLCHKHGVCFLAADTRGLVGQLF--------- 159
Cdd:pfam00899   81 ERLREINPDVEVEAYTERLTpenaEELIKSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVTvvipgktpc 160

                          170       180       190
                   ....*....|....*....|....*....|
gi 38045948    160 --CDFGED---FTVQDPTEAE---PLTAAI 181
Cdd:pfam00899  161 yrCLFPEDpppKLVPSCTVAGvlgPTTAVV 190
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 436-575 1.19e-24

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: 100.81  E-value: 1.19e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948  436 LLVGAGAIGCELLKvfALVGLGAGNsggLTVVDMDHIERSNLSRQFLFRSQDVGRPKAEVAAAAARGLNPDLQVipLTYP 515
Cdd:cd01483    3 LLVGLGGLGSEIAL--NLARSGVGK---ITLIDFDTVELSNLNRQFLARQADIGKPKAEVAARRLNELNPGVNV--TAVP 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948  516 LDPTTEHIygDNFFSRVDGVAAALDSFQARRYVAARCTHYLKPLLEAGTSGTWGSATVFM 575
Cdd:cd01483   76 EGISEDNL--DDFLDGVDLVIDAIDNIAVRRALNRACKELGIPVIDAGGLGLGGDIQVID 133
E1_4HB pfam16191
Ubiquitin-activating enzyme E1 four-helix bundle; This domain is found in the ...
 258-326 2.80e-24

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: 96.76  E-value: 2.80e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 38045948    258 RPKTVRHKSLDTALLQPHVVAQSSQEVHHAHCLHQAFCALHKFQHLHGRPPQPWDPVDAETVVGLARDL 326
Cdd:pfam16191    1 MPKTLSFKSLEESLKEPEFLISDFAKFDRPAQLHLAFQALHAFQEKHGRLPRPWNEEDAEEVVKLAKEL 69
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 414-580 2.32e-20

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 91.44  E-value: 2.32e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948   414 RYDGQIAVFGAGF--QEKLRRQHYLLVGAGAIGCELLKVFALVGLGAgnsggLTVVDMDHIERSNLSRQFLFRSQDVGRP 491
Cdd:PRK05690   12 RYNRQIILRGFDFdgQEKLKAARVLVVGLGGLGCAASQYLAAAGVGT-----LTLVDFDTVSLSNLQRQVLHDDATIGQP 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948   492 KAEVAAAAARGLNPDLQVIPLTYPLDPTTehiyGDNFFSRVDGVAAALDSFQARRYVAARCTHYLKPLLEAGTSGTWGSA 571
Cdd:PRK05690   87 KVESARAALARINPHIAIETINARLDDDE----LAALIAGHDLVLDCTDNVATRNQLNRACFAAKKPLVSGAAIRMEGQV 162


                  ....*....
gi 38045948   572 TVFMPHVTE 580
Cdd:PRK05690  163 TVFTYQDDE 171
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 11-144 6.60e-20

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: 90.19  E-value: 6.60e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948   11 DEEL--YSRQ--LYVLGSPAMQRIQGARVLVSGLQGLGAEVAKNLVLMGVGSLTLHDPHPTCWSDLAAQFLLSEQDLERS 86
Cdd:COG0476    2 DEELerYSRQilLPEIGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADVGRP 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 38045948   87 RAEASQELLAQLNRAVQVVVHTGDITEDLLLDF--QV-VVLTAA-KLEEQLKVGTLCHKHGV 144
Cdd:COG0476   82 KVEAAAERLRALNPDVEVEAIPERLTEENALELlaGAdLVLDCTdNFATRYLLNDACVKLGI 143
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 422-578 6.10e-18

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 86.86  E-value: 6.10e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948   422 FGAGFQEKLRRQHYLLVGAGAIGCELLKVFALVGLGAgnsggLTVVDMDHIERSNLSRQFLFRSQDVGRPKAEVAAAAAR 501
Cdd:PRK05600   31 FGIEQQERLHNARVLVIGAGGLGCPAMQSLASAGVGT-----ITLIDDDTVDVSNIHRQILFGASDVGRPKVEVAAERLK 105

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 38045948   502 GLNPDLQVIPLTYPLDPTTEHiygdNFFSRVDGVAAALDSFQARRYV--AARCThylkplleaGTSGTWGSATVFMPHV 578
Cdd:PRK05600  106 EIQPDIRVNALRERLTAENAV----ELLNGVDLVLDGSDSFATKFLVadAAEIT---------GTPLVWGTVLRFHGEL 171
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 34-158 7.39e-18

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: 81.16  E-value: 7.39e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948   34 RVLVSGLQGLGAEVAKNLVLMGVGSLTLHDP---HPtcwSDLAAQFLLSEQDLERSRAEASQELLAQLNRAVQVVVHTGD 110
Cdd:cd01483    1 RVLLVGLGGLGSEIALNLARSGVGKITLIDFdtvEL---SNLNRQFLARQADIGKPKAEVAARRLNELNPGVNVTAVPEG 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 38045948  111 ITEDLLLDFQ----VVVLTAAKLEEQLKVGTLCHKHGVCFLAADTRGLVGQL 158
Cdd:cd01483   78 ISEDNLDDFLdgvdLVIDAIDNIAVRRALNRACKELGIPVIDAGGLGLGGDI 129
APPBP1_RUB cd01493
Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric ...
 15-156 8.43e-18

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: 86.97  E-value: 8.43e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948   15 YSRQLYVLGSPAMQRIQGARVLVSGLQGLGAEVAKNLVLMGVGSLTLHDPHPTCWSDLAAQFLLSEQDLERSRAEASQEL 94
Cdd:cd01493    3 YDRQLRLWGEHGQAALESAHVCLLNATATGTEILKNLVLPGIGSFTIVDGSKVDEEDLGNNFFLDASSLGKSRAEATCEL 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38045948   95 LAQLNRAVqvvvhTGDITE---DLLLD--------FQVVVLTAAKLEEQLKVGTLCHKHGVCFLAADTRGLVG 156
Cdd:cd01493   83 LQELNPDV-----NGSAVEespEALLDndpsffsqFTVVIATNLPESTLLRLADVLWSANIPLLYVRSYGLYG 150
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 15-123 2.21e-16

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: 79.44  E-value: 2.21e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948   15 YSRQLYV--LGSPAMQRIQGARVLVSGLQGLGAEVAKNLVLMGVGSLTLHDPHPTCWSDLAAQFLLSEQDLERSRAEASQ 92
Cdd:cd00757    2 YSRQILLpeIGEEGQEKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRQILHTEADVGQPKAEAAA 81

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 38045948   93 ELLAQLNRAVQVVVHTGDIT----EDLLLDFQVVV 123
Cdd:cd00757   82 ERLRAINPDVEIEAYNERLDaenaEELIAGYDLVL 116
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 414-579 9.91e-16

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 79.65  E-value: 9.91e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948   414 RYDGQI--AVFGAGFQEKLRRQHYLLVGAGAIGCELLKvfALVGLGAGNsggLTVVDMDHIERSNLSRQFLFRSQDV--G 489
Cdd:PRK07688    4 RYSRQElfSPIGEEGQQKLREKHVLIIGAGALGTANAE--MLVRAGVGK---VTIVDRDYVEWSNLQRQQLYTESDVknN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948   490 RPKAEVAAAAARGLNPDLQVIPLTypLDPTTEHIygDNFFSRVDGVAAALDSFQARRYVAARCTHYLKPLLEAGTSGTWG 569
Cdd:PRK07688   79 LPKAVAAKKRLEEINSDVRVEAIV--QDVTAEEL--EELVTGVDLIIDATDNFETRFIVNDAAQKYGIPWIYGACVGSYG 154

                         170
                  ....*....|
gi 38045948   570 SATVFMPHVT 579
Cdd:PRK07688  155 LSYTIIPGKT 164
Aos1_SUMO cd01492
Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating ...
 415-571 1.10e-15

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: 76.56  E-value: 1.10e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948  415 YDGQIAVFGAGFQEKLRRQHYLLVGAGAIGCELLKVFALVGLGAgnsggLTVVDMDHIERSNLSRQFLFRSQDVGRPKAE 494
Cdd:cd01492    4 YDRQIRLWGLEAQKRLRSARILLIGLKGLGAEIAKNLVLSGIGS-----LTILDDRTVTEEDLGAQFLIPAEDLGQNRAE 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 38045948  495 VAAAAARGLNPDLQVIPLTyplDPTTEHiyGDNFFSRVDGVAAALDSFQARRYVAARCTHYLKPLLEAGTSGTWGSA 571
Cdd:cd01492   79 ASLERLRALNPRVKVSVDT---DDISEK--PEEFFSQFDVVVATELSRAELVKINELCRKLGVKFYATGVHGLFGFV 150
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
 422-567 8.07e-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: 74.95  E-value: 8.07e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948  422 FGAGFQEKLRRQHYLLVGAGAIG---CELLkvfALVGLGAgnsggLTVVDMDHIERSNLSRQFLFRSQDVGRPKAEVAAA 498
Cdd:cd00755    1 YGEEGLEKLRNAHVAVVGLGGVGswaAEAL---ARSGVGK-----LTLIDFDVVCVSNLNRQIHALLSTVGKPKVEVMAE 72

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 38045948  499 AARGLNPDLQVIPLTYPLDPTTEHiygDNFFSRVDGVAAALDSFQARRYVAARCTHYLKPLLEAGTSGT 567
Cdd:cd00755   73 RIRDINPECEVDAVEEFLTPDNSE---DLLGGDPDFVVDAIDSIRAKVALIAYCRKRKIPVISSMGAGG 138
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
427-576 2.57e-14

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 75.82  E-value: 2.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948   427 QEKLRRQHYLLVGAGAIGCEllkvfALVGLGAGNSGGLTVVDMDHIERSNLSRQFLFRSQDVGRPKAEVAAAAARGLNPD 506
Cdd:PRK08762  130 QRRLLEARVLLIGAGGLGSP-----AALYLAAAGVGTLGIVDHDVVDRSNLQRQILHTEDRVGQPKVDSAAQRLAALNPD 204

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948   507 LQVIplTYPLDPTTEHIygDNFFSRVDGVAAALDSFQARRYVAARCTHYLKPLLEAGTSGTWGSATVFMP 576
Cdd:PRK08762  205 VQVE--AVQERVTSDNV--EALLQDVDVVVDGADNFPTRYLLNDACVKLGKPLVYGAVFRFEGQVSVFDA 270
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 414-579 3.04e-14

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 75.15  E-value: 3.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948   414 RYDGQIAVFGAGF--QEKLRRQHYLLVGAGAIGCELLKVFALVGLGAgnsggLTVVDMDHIERSNLSRQFLFRSQDVG-- 489
Cdd:PRK12475    4 RYSRQILFSGIGEegQRKIREKHVLIVGAGALGAANAEALVRAGIGK-----LTIADRDYVEWSNLQRQQLYTEEDAKqk 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948   490 RPKAEVAAAAARGLNPDLQVIPltYPLDPTTEHIygDNFFSRVDGVAAALDSFQARRYVAARCTHYLKPLLEAGTSGTWG 569
Cdd:PRK12475   79 KPKAIAAKEHLRKINSEVEIVP--VVTDVTVEEL--EELVKEVDLIIDATDNFDTRLLINDLSQKYNIPWIYGGCVGSYG 154

                         170
                  ....*....|
gi 38045948   570 SATVFMPHVT 579
Cdd:PRK12475  155 VTYTIIPGKT 164
PRK08328 PRK08328
hypothetical protein; Provisional
 414-580 3.74e-14

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 72.91  E-value: 3.74e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948   414 RYDGQIAVFGAGFQEKLRRQHYLLVGAGAIGCELLKVFALVGLGAgnsggLTVVDMDHIERSNLSRQFLFRSQDVGR-PK 492
Cdd:PRK08328    9 RYDRQIMIFGVEGQEKLKKAKVAVVGVGGLGSPVAYYLAAAGVGR-----ILLIDEQTPELSNLNRQILHWEEDLGKnPK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948   493 AEVAAAAARGLNPDLQVIplTYPLDPTTEHIygDNFFSRVDGVAAALDSFQARRYVAARCTHYLKPLLEAGTSGTWGSAT 572
Cdd:PRK08328   84 PLSAKWKLERFNSDIKIE--TFVGRLSEENI--DEVLKGVDVIVDCLDNFETRYLLDDYAHKKGIPLVHGAVEGTYGQVT 159


                  ....*...
gi 38045948   573 VFMPHVTE 580
Cdd:PRK08328  160 TIVPGKTK 167
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 413-570 6.07e-14

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 74.52  E-value: 6.07e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948   413 SRYDGQIAV--FGAGFQEKLRRQHYLLVGAGAIGCEllkvfALVGLGAGNSGGLTVVDMDHIERSNLSRQFLFRSQDVGR 490
Cdd:PRK05597    7 ARYRRQIMLgeIGQQGQQSLFDAKVAVIGAGGLGSP-----ALLYLAGAGVGHITIIDDDTVDLSNLHRQVIHSTAGVGQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948   491 PKAEVAAAAARGLNPDLQVIPLTYPLDPTTehiyGDNFFSRVDGVAAALDSFQArRYVAARCTHYLkplleaGTSGTWGS 570
Cdd:PRK05597   82 PKAESAREAMLALNPDVKVTVSVRRLTWSN----ALDELRDADVILDGSDNFDT-RHLASWAAARL------GIPHVWAS 150
TcdA COG1179
tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ...
 422-552 5.56e-13

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: 69.73  E-value: 5.56e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948  422 FGAGFQEKLRRQHYLLVGAGAIG---CEllkvfALVGLGAGNsggLTVVDMDHIERSNLSRQFL-FRSQdVGRPKAEVAA 497
Cdd:COG1179   14 YGEEGLERLANAHVAVVGLGGVGswaAE-----ALARSGVGR---LTLVDLDDVCESNINRQLHaLDST-VGRPKVEVMA 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 38045948  498 AAARGLNPDLQVIPLTYPLDPTTEHIYgdnFFSRVDGVAAALDSFQARRYVAARC 552
Cdd:COG1179   85 ERIRDINPDCEVTAIDEFVTPENADEL---LSEDYDYVIDAIDSVSAKAALIAWC 136
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 12-144 1.88e-12

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 69.76  E-value: 1.88e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948    12 EELYSRQLYV--LGSPAMQRIQGARVLVSGLQGLGAEVAKNLVLMGVGSLTLHDPHPTCWSDLAAQFLLSEQDLE--RSR 87
Cdd:PRK12475    2 QERYSRQILFsgIGEEGQRKIREKHVLIVGAGALGAANAEALVRAGIGKLTIADRDYVEWSNLQRQQLYTEEDAKqkKPK 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 38045948    88 AEASQELLAQLNRAVQVVVHTGDIT----EDLLLDFQVVVLTAAKLEEQLKVGTLCHKHGV 144
Cdd:PRK12475   82 AIAAKEHLRKINSEVEIVPVVTDVTveelEELVKEVDLIIDATDNFDTRLLINDLSQKYNI 142
PRK08328 PRK08328
hypothetical protein; Provisional
 13-158 3.42e-12

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 67.13  E-value: 3.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948    13 ELYSRQLYVLGSPAMQRIQGARVLVSGLQGLGAEVAKNLVLMGVGSLTLHDPHPTCWSDLAAQFLLSEQDLER-SRAEAS 91
Cdd:PRK08328    8 ERYDRQIMIFGVEGQEKLKKAKVAVVGVGGLGSPVAYYLAAAGVGRILLIDEQTPELSNLNRQILHWEEDLGKnPKPLSA 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 38045948    92 QELLAQLNRAVQVVVHTGDITE----DLLLDFQVVVLTAAKLEEQLKVGTLCHKHGVCFLAADTRGLVGQL 158
Cdd:PRK08328   88 KWKLERFNSDIKIETFVGRLSEenidEVLKGVDVIVDCLDNFETRYLLDDYAHKKGIPLVHGAVEGTYGQV 158
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 13-147 5.84e-12

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 68.10  E-value: 5.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948    13 ELYSRQLYV--LGSPAMQRIQGARVLVSGLQGLGAEVAKNLVLMGVGSLTLHDPHPTCWSDLAAQFLLSEQDLERS--RA 88
Cdd:PRK07688    3 ERYSRQELFspIGEEGQQKLREKHVLIIGAGALGTANAEMLVRAGVGKVTIVDRDYVEWSNLQRQQLYTESDVKNNlpKA 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38045948    89 EASQELLAQLNRAVQVVVHTGDIT----EDLLLDFQVVVLTAAKLEEQLKVGTLCHKHGVCFL 147
Cdd:PRK07688   83 VAAKKRLEEINSDVRVEAIVQDVTaeelEELVTGVDLIIDATDNFETRFIVNDAAQKYGIPWI 145
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
422-571 1.33e-11

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 64.88  E-value: 1.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948   422 FGAGFQEKLRRQHYLLVGAGAIG--CELlkvfALVGLGAGNsggLTVVDMDHIERSNLSRQFLFRSQdVGRPKAEVAAAA 499
Cdd:PRK08644   18 HTPKLLEKLKKAKVGIAGAGGLGsnIAV----ALARSGVGN---LKLVDFDVVEPSNLNRQQYFISQ-IGMPKVEALKEN 89

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38045948   500 ARGLNPDLQVIPLTYPLDPttEHIygDNFFSRVDGVAAALDSFQARRYVAARC-THYLKPLLEAGTSGTWGSA 571
Cdd:PRK08644   90 LLEINPFVEIEAHNEKIDE--DNI--EELFKDCDIVVEAFDNAETKAMLVETVlEHPGKKLVAASGMAGYGDS 158
E1-1_like cd01485
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ...
 415-509 5.58e-11

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


Pssm-ID: 238762 [Multi-domain]  Cd Length: 198  Bit Score: 62.82  E-value: 5.58e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948  415 YDGQIAVFGAGFQEKLRRQHYLLVGAGAIGCELLKVFALVGLGAgnsggLTVVDMDHIERSNLSRQFLFRSQDV--GRPK 492
Cdd:cd01485    2 YDRQIRLWGDEAQNKLRSAKVLIIGAGALGAEIAKNLVLAGIDS-----ITIVDHRLVSTEDLGSNFFLDAEVSnsGMNR 76

                         90
                 ....*....|....*..
gi 38045948  493 AEVAAAAARGLNPDLQV 509
Cdd:cd01485   77 AAASYEFLQELNPNVKL 93
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 427-570 9.40e-11

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 65.11  E-value: 9.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948   427 QEKLRRQHYLLVGAGAIGCEllkvfALVGLGAGNSGGLTVVDMDHIERSNLSRQFLFRSQDVGRPKAEVAAAAARGLNPD 506
Cdd:PRK07878   37 QKRLKNARVLVIGAGGLGSP-----TLLYLAAAGVGTLGIVEFDVVDESNLQRQVIHGQSDVGRSKAQSARDSIVEINPL 111

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 38045948   507 LQVIPLTYPLDPttehiygDN---FFSRVDGVAAALDSFQARRYVAARCTHYLKPLLeagtsgtWGS 570
Cdd:PRK07878  112 VNVRLHEFRLDP-------SNaveLFSQYDLILDGTDNFATRYLVNDAAVLAGKPYV-------WGS 164
APPBP1_RUB cd01493
Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric ...
 414-506 9.48e-11

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: 65.02  E-value: 9.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948  414 RYDGQIAVFGAGFQEKLRRQHYLLVGAGAIGCELLKVFALVGLgagnsGGLTVVDMDHIERSNLSRQFLFRSQDVGRPKA 493
Cdd:cd01493    2 KYDRQLRLWGEHGQAALESAHVCLLNATATGTEILKNLVLPGI-----GSFTIVDGSKVDEEDLGNNFFLDASSLGKSRA 76

                         90
                 ....*....|...
gi 38045948  494 EVAAAAARGLNPD 506
Cdd:cd01493   77 EATCELLQELNPD 89
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 8-176 4.51e-10

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 61.01  E-value: 4.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948     8 KLLDEEL--YSRQ--LYVLGSPAMQRIQGARVLVSGLQGLGAEVAKNLVLMGVGSLTLHDPHPTCWSDLAAQFLLSEQDL 83
Cdd:PRK05690    4 ELSDEEMlrYNRQiiLRGFDFDGQEKLKAARVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVSLSNLQRQVLHDDATI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948    84 ERSRAEASQELLAQLNRAVQVVVHTGDITED----LLLDFQVVVLTAAKLEEQLKVGTLCHKHGVCFLAADTRGLVGQLf 159
Cdd:PRK05690   84 GQPKVESARAALARINPHIAIETINARLDDDelaaLIAGHDLVLDCTDNVATRNQLNRACFAAKKPLVSGAAIRMEGQV- 162

                         170
                  ....*....|....*..
gi 38045948   160 cdfgedfTVQDPTEAEP 176
Cdd:PRK05690  163 -------TVFTYQDDEP 172
PRK15116 PRK15116
sulfur acceptor protein CsdL; Provisional
 413-566 1.30e-09

sulfur acceptor protein CsdL; Provisional


Pssm-ID: 185071  Cd Length: 268  Bit Score: 60.20  E-value: 1.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948   413 SRYDGQIAVFGAGFQEKLRRQHYLLVGAGAIGCELLKVFALVGLGAgnsggLTVVDMDHIERSNLSRQFLFRSQDVGRPK 492
Cdd:PRK15116   11 QRFGGTARLYGEKALQLFADAHICVVGIGGVGSWAAEALARTGIGA-----ITLIDMDDVCVTNTNRQIHALRDNVGLAK 85

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 38045948   493 AEVAAAAARGLNPDLQVIPLTYPLDPTTEHIYGDNFFSRvdgVAAALDSFQARRYVAARCTHYLKPLLEAGTSG 566
Cdd:PRK15116   86 AEVMAERIRQINPECRVTVVDDFITPDNVAEYMSAGFSY---VIDAIDSVRPKAALIAYCRRNKIPLVTTGGAG 156
PRK08223 PRK08223
hypothetical protein; Validated
 427-576 1.75e-09

hypothetical protein; Validated


Pssm-ID: 181302 [Multi-domain]  Cd Length: 287  Bit Score: 60.08  E-value: 1.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948   427 QEKLRRQHYLLVGAGAIGCELLKVFALVGLGAgnsggLTVVDMDHIERSNLSRQFLFRSQDVGRPKAEVAAAAARGLNPD 506
Cdd:PRK08223   22 QQRLRNSRVAIAGLGGVGGIHLLTLARLGIGK-----FTIADFDVFELRNFNRQAGAMMSTLGRPKAEVLAEMVRDINPE 96

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 38045948   507 LQVipLTYPLDPTTEHIygDNFFSRVDGVAAALD--SFQARRYVAARCTHYLKPLLEAGTSGTWGSATVFMP 576
Cdd:PRK08223   97 LEI--RAFPEGIGKENA--DAFLDGVDVYVDGLDffEFDARRLVFAACQQRGIPALTAAPLGMGTALLVFDP 164
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 34-124 3.52e-09

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: 59.29  E-value: 3.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948   34 RVLVSGLQGLGAEVAKNLVLMGVGSLTLHDPHPTCWSDLAAQFLLSEQDLERSRAEASQELLAQLNRAVQVVVHTGDIT- 112
Cdd:cd01488    1 KILVIGAGGLGCELLKNLALSGFRNIHVIDMDTIDVSNLNRQFLFREKDIGKPKAEVAAKFVNDRVPGVNVTPHFGKIQd 80

                         90
                 ....*....|....
gi 38045948  113 --EDLLLDFQVVVL 124
Cdd:cd01488   81 kdEEFYRQFNIIIC 94
Ube1_repeat1 cd01491
Ubiquitin activating enzyme (E1), repeat 1. E1, a highly conserved small protein present ...
 415-570 6.81e-09

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: 58.05  E-value: 6.81e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948  415 YDGQIAVFGAGFQEKLRRQHYLLVGAGAIGCELLKVFALVGLGAgnsggLTVVDMDHIERSNLSRQFLFRSQDVGRPKAE 494
Cdd:cd01491    2 YSRQLYVLGHEAMKKLQKSNVLISGLGGLGVEIAKNLILAGVKS-----VTLHDTKPCSWSDLSSQFYLREEDIGKNRAE 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 38045948  495 VAAAAARGLNPDLQVIPLTYPLDpttehiygDNFFSRVDGVAAALDSFQARRYVAARCTHYLKPLLEAGTSGTWGS 570
Cdd:cd01491   77 ASQARLAELNPYVPVTVSTGPLT--------TDELLKFQVVVLTDASLEDQLKINEFCHSPGIKFISADTRGLFGS 144
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 34-158 1.34e-08

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


Pssm-ID: 238766 [Multi-domain]  Cd Length: 312  Bit Score: 57.77  E-value: 1.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948   34 RVLVSGLQGLGAEVAKNLVLMGVGSLTLHDPHPTCWSDLAAQFLLSEQDLERSRAEASQELLAQLNRAVQVVVHTGDITE 113
Cdd:cd01489    1 KVLVVGAGGIGCELLKNLVLTGFGEIHIIDLDTIDLSNLNRQFLFRKKHVGKSKAQVAKEAVLSFNPNVKIVAYHANIKD 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 38045948  114 DlllDFQV-------VVLTAA-KLEEQLKVGTLCHKHGVCFLAADTRGLVGQL 158
Cdd:cd01489   81 P---DFNVeffkqfdLVFNALdNLAARRHVNKMCLAADVPLIESGTTGFLGQV 130
E1_ThiF_like cd01487
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ...
 434-571 1.82e-08

E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. The common reaction mechanism catalyzed by E1-like enzymes begins with a nucleophilic attack of the C-terminal carboxylate of the ubiquitin-like substrate, on the alpha-phosphate of an ATP molecule bound at the active site of the activating enzymes, leading to the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of the substrate. The exact function of this family is unknown.


Pssm-ID: 238764 [Multi-domain]  Cd Length: 174  Bit Score: 55.08  E-value: 1.82e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948  434 HYLLVGAGAIGCELlkVFALVGLGAGNsggLTVVDMDHIERSNLSRQFlFRSQDVGRPKAEVAAAAARGLNPDLQVIPLT 513
Cdd:cd01487    1 KVGIAGAGGLGSNI--AVLLARSGVGN---LKLVDFDVVEPSNLNRQQ-YFLSQIGEPKVEALKENLREINPFVKIEAIN 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 38045948  514 YPLDptTEHIYGdnFFSRVDGVAAALDSFQARRYVA-ARCTHYLKPLLEAGTSGTWGSA 571
Cdd:cd01487   75 IKID--ENNLEG--LFGDCDIVVEAFDNAETKAMLAeSLLGNKNKPVVCASGMAGFGDS 129
PRK14851 PRK14851
hypothetical protein; Provisional
 419-576 1.98e-08

hypothetical protein; Provisional


Pssm-ID: 184853 [Multi-domain]  Cd Length: 679  Bit Score: 58.33  E-value: 1.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948   419 IAVFGAGFQEKLRRQHYLLVGAGAIGCELLKVFALVGLGAGNsggltVVDMDHIERSNLSRQFLFRSQDVGRPKAEVAAA 498
Cdd:PRK14851   30 IGLFTPGEQERLAEAKVAIPGMGGVGGVHLITMVRTGIGRFH-----IADFDQFEPVNVNRQFGARVPSFGRPKLAVMKE 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948   499 AARGLNPDLQVIPltYPLDPTTEHIygDNFFSRVDGVAAALDSFQ--ARRYVAARCTHYLKPLLEAGTSGTWGSATVFMP 576
Cdd:PRK14851  105 QALSINPFLEITP--FPAGINADNM--DAFLDGVDVVLDGLDFFQfeIRRTLFNMAREKGIPVITAGPLGYSSAMLVFTP 180
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
 22-144 3.72e-08

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: 55.30  E-value: 3.72e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948   22 LGSPAMQRIQGARVLVSGLQGLGAEVAKNLVLMGVGSLTLHDPHPTCWSDLAAQFLLSEQDLERSRAEASQELLAQLNRA 101
Cdd:cd00755    1 YGEEGLEKLRNAHVAVVGLGGVGSWAAEALARSGVGKLTLIDFDVVCVSNLNRQIHALLSTVGKPKVEVMAERIRDINPE 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 38045948  102 VQVVVH----TGDITEDLLL-DFQVVV-----LTAakleeqlKVGTL--CHKHGV 144
Cdd:cd00755   81 CEVDAVeeflTPDNSEDLLGgDPDFVVdaidsIRA-------KVALIayCRKRKI 128
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 6-107 4.08e-08

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 56.64  E-value: 4.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948     6 ASKLLDEEL--YSRQLYV--LGSPAMQRIQGARVLVSGLQGLGAEVAKNLVLMGVGSLTLHDPHPTCWSDLAAQFLLSEQ 81
Cdd:PRK07878   12 AAELTRDEVarYSRHLIIpdVGVDGQKRLKNARVLVIGAGGLGSPTLLYLAAAGVGTLGIVEFDVVDESNLQRQVIHGQS 91

                          90       100
                  ....*....|....*....|....*.
gi 38045948    82 DLERSRAEASQELLAQLNRAVQVVVH 107
Cdd:PRK07878   92 DVGRSKAQSARDSIVEINPLVNVRLH 117
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
11-123 7.86e-08

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 55.79  E-value: 7.86e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948    11 DEELYSRQLYV--LGSPAMQRIQGARVLVSGLQGLGAEVAKNLVLMGVGSLTLHDPHPTCWSDLAAQFLLSEQDLERSRA 88
Cdd:PRK08762  112 QDERYSRHLRLpeVGEEGQRRLLEARVLLIGAGGLGSPAALYLAAAGVGTLGIVDHDVVDRSNLQRQILHTEDRVGQPKV 191

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 38045948    89 EASQELLAQLNRAVQVVVH----TGDITEDLLLDFQVVV 123
Cdd:PRK08762  192 DSAAQRLAALNPDVQVEAVqervTSDNVEALLQDVDVVV 230
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
28-123 2.69e-07

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 52.17  E-value: 2.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948    28 QRIQGARVLVSGLQGLGAEVAKNLVLMGVGSLTLHD-----PhptcwSDLAAQFLLSEQdLERSRAEASQELLAQLNRAV 102
Cdd:PRK08644   24 EKLKKAKVGIAGAGGLGSNIAVALARSGVGNLKLVDfdvveP-----SNLNRQQYFISQ-IGMPKVEALKENLLEINPFV 97

                          90       100
                  ....*....|....*....|....*
gi 38045948   103 QVVVHTGDITED----LLLDFQVVV 123
Cdd:PRK08644   98 EIEAHNEKIDEDnieeLFKDCDIVV 122
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 8-119 7.43e-07

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 52.57  E-value: 7.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948     8 KLLDEELYSRQ--LYVLGSPAMQRIQGARVLVSGLQGLGAEVAKNLVLMGVGSLTLHDPHPTCWSDLAAQFLLSEQDLER 85
Cdd:PRK05597    2 KNLDIARYRRQimLGEIGQQGQQSLFDAKVAVIGAGGLGSPALLYLAGAGVGHITIIDDDTVDLSNLHRQVIHSTAGVGQ 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 38045948    86 SRAEASQELLAQLNRAVQVVVHTGDITEDLLLDF 119
Cdd:PRK05597   82 PKAESAREAMLALNPDVKVTVSVRRLTWSNALDE 115
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
 34-111 7.86e-07

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


Pssm-ID: 238761 [Multi-domain]  Cd Length: 234  Bit Score: 51.43  E-value: 7.86e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 38045948   34 RVLVSGLQGLGAEVAKNLVLMGVGSLTLHDPHPTCWSDLAAQFLLSEQDLERSRAEASQELLAQLNRAVQVVVHTGDI 111
Cdd:cd01484    1 KVLLVGAGGIGCELLKNLALMGFGQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKSEVAAEAVNDRNPNCKVVPYQNKV 78
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 1-114 1.02e-06

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 52.19  E-value: 1.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948     1 MDALDASKLLDEELY--SRQLYV--LGSPAMQRIQGARVLVSGLQGLGAEVAKNLVLMGVGSLTLHDPHPTCWSDLAAQF 76
Cdd:PRK05600    6 HTLSPFMQLPTSELRrtARQLALpgFGIEQQERLHNARVLVIGAGGLGCPAMQSLASAGVGTITLIDDDTVDVSNIHRQI 85

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 38045948    77 LLSEQDLERSRAEASQELLAQLNRAVQVVVHTGDITED 114
Cdd:PRK05600   86 LFGASDVGRPKVEVAAERLKEIQPDIRVNALRERLTAE 123
E1_ThiF_like cd01487
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ...
 34-123 2.60e-06

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: 48.92  E-value: 2.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948   34 RVLVSGLQGLGAEVAKNLVLMGVGSLTLHDPHPTCWSDLAAQFLLSEQdLERSRAEASQELLAQLNRAVQVVVHTGDITE 113
Cdd:cd01487    1 KVGIAGAGGLGSNIAVLLARSGVGNLKLVDFDVVEPSNLNRQQYFLSQ-IGEPKVEALKENLREINPFVKIEAINIKIDE 79

                         90
                 ....*....|....
gi 38045948  114 D----LLLDFQVVV 123
Cdd:cd01487   80 NnlegLFGDCDIVV 93
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
427-574 2.96e-06

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 50.89  E-value: 2.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948   427 QEKLRRQHYLLVGAGAIGCELLKVFALVGLGAgnsggLTVVDMDHIERSNLSRQFLFRSQDVGRPKAEVAAAAARGLNPD 506
Cdd:PRK07411   33 QKRLKAASVLCIGTGGLGSPLLLYLAAAGIGR-----IGIVDFDVVDSSNLQRQVIHGTSWVGKPKIESAKNRILEINPY 107

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 38045948   507 LQVIplTYPLDPTTEHIYgdNFFSRVDGVAAALDSFQARRYVAARCTHYLKPLLEAGTSGTWGSATVF 574
Cdd:PRK07411  108 CQVD--LYETRLSSENAL--DILAPYDVVVDGTDNFPTRYLVNDACVLLNKPNVYGSIFRFEGQATVF 171
PRK14852 PRK14852
hypothetical protein; Provisional
 427-576 2.41e-05

hypothetical protein; Provisional


Pssm-ID: 184854 [Multi-domain]  Cd Length: 989  Bit Score: 48.54  E-value: 2.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948   427 QEKLRRQHYLLVGAGAIGCELLKVFALVGLGAGNsggltVVDMDHIERSNLSRQFLFRSQDVGRPKAEVAAAAARGLNPD 506
Cdd:PRK14852  327 QRRLLRSRVAIAGLGGVGGIHLMTLARTGIGNFN-----LADFDAYSPVNLNRQYGASIASFGRGKLDVMTERALSVNPF 401

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 38045948   507 LQVipLTYPLDPTTEHIygDNFFSRVDGVAAALDSF--QARRYVAARCTHYLKPLLEAGTSGTWGSATVFMP 576
Cdd:PRK14852  402 LDI--RSFPEGVAAETI--DAFLKDVDLLVDGIDFFalDIRRRLFNRALELGIPVITAGPLGYSCALLVFMP 469
Apg7 cd01486
Apg7 is an E1-like protein, that activates two different ubiquitin-like proteins, Apg12 and ...
 436-509 8.33e-05

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


Pssm-ID: 238763 [Multi-domain]  Cd Length: 307  Bit Score: 45.83  E-value: 8.33e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 38045948  436 LLVGAGAIGCELLKvfALVGLGAGNsggLTVVDMDHIERSNLSRQFLFRSQDV--GRPKAEVAAAAARGLNPDLQV 509
Cdd:cd01486    3 LLLGAGTLGCNVAR--NLLGWGVRH---ITFVDSGKVSYSNPVRQSLFTFEDCkgGKPKAEAAAERLKEIFPSIDA 73
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
 34-126 1.97e-04

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


Pssm-ID: 238767 [Multi-domain]  Cd Length: 435  Bit Score: 44.97  E-value: 1.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948   34 RVLVSGLQGLGAEVAKNLVLMGVGS-----LTLHDPHPTCWSDLAAQFLLSEQDLERSRAEASQELLAQLNRAVQVVVHT 108
Cdd:cd01490    1 KVFLVGAGAIGCELLKNFALMGVGTgesgeITVTDMDNIEKSNLNRQFLFRPHDVGKPKSEVAAAAVKAMNPDLKITALQ 80

                         90       100
                 ....*....|....*....|....*
gi 38045948  109 ---GDITEDLLLD-F---QVVVLTA 126
Cdd:cd01490   81 nrvGPETEHIFNDeFwekLDGVANA 105
PRK15116 PRK15116
sulfur acceptor protein CsdL; Provisional
 18-114 4.99e-04

sulfur acceptor protein CsdL; Provisional


Pssm-ID: 185071  Cd Length: 268  Bit Score: 43.25  E-value: 4.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948    18 QLYvlGSPAMQRIQGARVLVSGLQGLGAEVAKNLVLMGVGSLTLHDPHPTCWSDLAAQFLLSEQDLERSRAEASQELLAQ 97
Cdd:PRK15116   18 RLY--GEKALQLFADAHICVVGIGGVGSWAAEALARTGIGAITLIDMDDVCVTNTNRQIHALRDNVGLAKAEVMAERIRQ 95

                          90
                  ....*....|....*..
gi 38045948    98 LNRAVQVVVHTGDITED 114
Cdd:PRK15116   96 INPECRVTVVDDFITPD 112
TcdA COG1179
tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ...
 22-123 1.98e-03

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: 41.22  E-value: 1.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948   22 LGSPAMQRIQGARVLVSGLQGLGAEVAKNLVLMGVGSLTLHDphptcwSD----------LAAqfLLSEqdLERSRAEAS 91
Cdd:COG1179   14 YGEEGLERLANAHVAVVGLGGVGSWAAEALARSGVGRLTLVD------LDdvcesninrqLHA--LDST--VGRPKVEVM 83

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 38045948   92 QELLAQLNRAVQVVVHTGDITED-----LLLDFQVVV 123
Cdd:COG1179   84 AERIRDINPDCEVTAIDEFVTPEnadelLSEDYDYVI 120
E1_like_apg7 TIGR01381
E1-like protein-activating enzyme Gsa7p/Apg7p; This model represents a family of eukaryotic ...
 436-545 2.17e-03

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


Pssm-ID: 273590 [Multi-domain]  Cd Length: 664  Bit Score: 41.85  E-value: 2.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045948    436 LLVGAGAIGCELLKVfaLVGLGAGNsggLTVVDMDHIERSNLSRQFLFRSQDV---GRPKAEVAAAAARGLNPDLQV--- 509
Cdd:TIGR01381  342 LLLGAGTLGCNVARC--LIGWGVRH---ITFVDNGKVSYSNPVRQSLSNFEDCllgGRGKAETAQKALKRIFPSIQAtgh 416

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 38045948    510 ---IPLT-YPLDPTTE-HIYGD-----NFFSRVDGVAAALDSFQAR 545
Cdd:TIGR01381  417 rltVPMPgHPIDEKDVpELEKDiarleQLIKDHDVVFLLLDSREAR 462
 
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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