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Conserved domains on  [gi|150417996|ref|NP_060697|]
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ubiquitin-like modifier-activating enzyme 6 [Homo sapiens]

Protein Classification

Ube1 family protein( domain architecture ID 11492432)

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

EC:  6.2.1.45
Gene Ontology:  GO:0036211|GO:0008641|GO:0005524

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 38-1046 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: 1834.52  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996    38 EIDDALYSRQRYVLGDTAMQKMAKSHVFLSGMGGLGLEIAKNLVLAGIKAVTIHDTEKCQAWDLGTNFFLSEDDVVnkRN 117
Cdd:TIGR01408    1 EIDEALYSRQLYVLGDEAMQKMAKSNVLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLSSNFFLSEDDVG--RN 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996   118 RAEAVLKHIAELNPYVHVTSSSVPFNETtdlsFLDKYQCVVLTEMKLPLQKKINDFCRSQCPPIKFISADVHGIWSRLFC 197
Cdd:TIGR01408   79 RAEAVVKKLAELNPYVHVSSSSVPFNEE----FLDKFQCVVLTEMSLPLQKEINDFCHSQCPPIAFISADVRGLFGSLFC 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996   198 DFGDEFEVLDTTGEEPKEIFISNITQANPGIVTCLENHPHKLETGQFLTFREINGMTGLN-GSIQQITVISPFSFSIGDT 276
Cdd:TIGR01408  155 DFGDEFEVLDTDGEEPKTGFIASITQANPGIVTCLENHRHKLETGDFVTFREVNGMTGLNdGSPRKITVISPYSFSIGDT 234

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996   277 TELEPYLHGGIAVQVKTPKTVFFESLERQLKHPKCLIVDFSNPEAPLEIHTAMLALDQFQEKYSRKPNVGCQQDSEELLK 356
Cdd:TIGR01408  235 TELGPYLHGGIATQVKTPKTVFFKSLREQLKDPKCLIVDFSKPERPPEIHTAFQALDQFQEKYSRKPNVGCQQDAEELLK 314

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996   357 LATSISETLEEK-PDVNADIVHWLSWTAQGFLSPLAAAVGGVASQEVLKAVTGKFSPLCQWLYLEAADIVESLGKPECEE 435
Cdd:TIGR01408  315 LATSISETLEEKvPDVDAKLVHWLSWTAQGFLSPMAAAVGGVVSQEVLKAVTGKFSPLCQWFYFDSAESLPSLGKPECEE 394

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996   436 FLPRGDRYDALRACIGDTLCQKLQNLNIFLVGCGAIGCEMLKNFALLGVGTSkEKGMITVTDPDLIEKSNLNRQFLFRPH 515
Cdd:TIGR01408  395 FLPRGDRYDAQIAVFGDTFQQKLQNLNIFLVGCGAIGCEMLKNFALMGVGTG-KKGMITVTDPDLIEKSNLNRQFLFRPH 473

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996   516 HIQKPKSYTAADATLKINSQIKIDAHLNKVCPTTETIYNDEFYTKQDVIITALDNVEARRYVDSRCLANLRPLLDSGTMG 595
Cdd:TIGR01408  474 HIGKPKSYTAADATLKINPQIKIDAHQNRVGPETETIFNDEFYEKLDVVINALDNVEARRYVDSRCLAFLKPLLESGTLG 553

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996   596 TKGHTEVIVPHLTESYNSHRDPPEEEIPFCTLKSFPAAIEHTIQWARDKFESSFSHKPSLFNKFWQTYSSAEEVLQKIQS 675
Cdd:TIGR01408  554 TKGNTQVVVPHLTESYGSSRDPPEKEIPFCTLKSFPAAIEHTIQWARDKFEGLFSHKPSLVNKYLSSPSSAEEVLQKIQS 633

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996   676 GHSLEGCFQVIKLLS-RRPRNWSQCVELARLKFEKYFNHKALQLLHCFPLDIRLKDGSLFWQSPKRPPSPIKFDLNEPLH 754
Cdd:TIGR01408  634 GHSREGLEQIIKLLSkEKPRNFSQCVEWARLKFEKYFNNKALQLLHCFPLDIRTSTGSPFWSSPKRPPSPLKFDLNEPLH 713

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996   755 LSFLQNAAKLYATVYCIPFAEEDLSADALLNILSEVKIQEFKP-SNKVVQTDETARKPDHVPIsseDERNAIFQLEKAIL 833
Cdd:TIGR01408  714 LSFIQAAAKLYATVYGIPFAEEDLSADALLNILSEVKIPEFKPrSNKKIQTDETARKPDTAPI---DDRNAIFQLEKAIL 790

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996   834 SNEATKSDLQMAVLSFEKDDDHNGHIDFITAASNLRAKMYSIEPADRFKTKRIAGKIIPAIATTTATVSGLVALEMIKVT 913
Cdd:TIGR01408  791 SNEATKSDFRMAPLSFEKDDDHNGHIDFITAASNLRAKNYSIEPADRFKTKFIAGKIIPAIATSTATVSGLVCLELIKVT 870

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996   914 -GGYPFEAYKNCFLNLAIPIVVFTETTEVRKTKIRNGISFTIWDRWTVHGkeDFTLLDFINAVKEKYGIEPTMVVQGVKM 992
Cdd:TIGR01408  871 dGGYKFEVYKNCFLNLAIPLFVFTEPTEVRKTKIRNGISFTIWDRWTLHG--DFTLLEFINAVKEKYGLEPTMVSQGVKL 948

                          970       980       990      1000      1010
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 150417996   993 LYVPVMPGHAKRLKLTMHKLVKPTTEKKY----VDLTVSFAPDIDGDEDLPGPPVRYY 1046
Cdd:TIGR01408  949 LYVPVMPGHAERLKLKMHKLVKPTTKKKLppyrVHLTVSFACDDDGDEDVPGPPVRIY 1006
 
Name Accession Description Interval E-value
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 38-1046 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: 1834.52  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996    38 EIDDALYSRQRYVLGDTAMQKMAKSHVFLSGMGGLGLEIAKNLVLAGIKAVTIHDTEKCQAWDLGTNFFLSEDDVVnkRN 117
Cdd:TIGR01408    1 EIDEALYSRQLYVLGDEAMQKMAKSNVLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLSSNFFLSEDDVG--RN 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996   118 RAEAVLKHIAELNPYVHVTSSSVPFNETtdlsFLDKYQCVVLTEMKLPLQKKINDFCRSQCPPIKFISADVHGIWSRLFC 197
Cdd:TIGR01408   79 RAEAVVKKLAELNPYVHVSSSSVPFNEE----FLDKFQCVVLTEMSLPLQKEINDFCHSQCPPIAFISADVRGLFGSLFC 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996   198 DFGDEFEVLDTTGEEPKEIFISNITQANPGIVTCLENHPHKLETGQFLTFREINGMTGLN-GSIQQITVISPFSFSIGDT 276
Cdd:TIGR01408  155 DFGDEFEVLDTDGEEPKTGFIASITQANPGIVTCLENHRHKLETGDFVTFREVNGMTGLNdGSPRKITVISPYSFSIGDT 234

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996   277 TELEPYLHGGIAVQVKTPKTVFFESLERQLKHPKCLIVDFSNPEAPLEIHTAMLALDQFQEKYSRKPNVGCQQDSEELLK 356
Cdd:TIGR01408  235 TELGPYLHGGIATQVKTPKTVFFKSLREQLKDPKCLIVDFSKPERPPEIHTAFQALDQFQEKYSRKPNVGCQQDAEELLK 314

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996   357 LATSISETLEEK-PDVNADIVHWLSWTAQGFLSPLAAAVGGVASQEVLKAVTGKFSPLCQWLYLEAADIVESLGKPECEE 435
Cdd:TIGR01408  315 LATSISETLEEKvPDVDAKLVHWLSWTAQGFLSPMAAAVGGVVSQEVLKAVTGKFSPLCQWFYFDSAESLPSLGKPECEE 394

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996   436 FLPRGDRYDALRACIGDTLCQKLQNLNIFLVGCGAIGCEMLKNFALLGVGTSkEKGMITVTDPDLIEKSNLNRQFLFRPH 515
Cdd:TIGR01408  395 FLPRGDRYDAQIAVFGDTFQQKLQNLNIFLVGCGAIGCEMLKNFALMGVGTG-KKGMITVTDPDLIEKSNLNRQFLFRPH 473

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996   516 HIQKPKSYTAADATLKINSQIKIDAHLNKVCPTTETIYNDEFYTKQDVIITALDNVEARRYVDSRCLANLRPLLDSGTMG 595
Cdd:TIGR01408  474 HIGKPKSYTAADATLKINPQIKIDAHQNRVGPETETIFNDEFYEKLDVVINALDNVEARRYVDSRCLAFLKPLLESGTLG 553

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996   596 TKGHTEVIVPHLTESYNSHRDPPEEEIPFCTLKSFPAAIEHTIQWARDKFESSFSHKPSLFNKFWQTYSSAEEVLQKIQS 675
Cdd:TIGR01408  554 TKGNTQVVVPHLTESYGSSRDPPEKEIPFCTLKSFPAAIEHTIQWARDKFEGLFSHKPSLVNKYLSSPSSAEEVLQKIQS 633

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996   676 GHSLEGCFQVIKLLS-RRPRNWSQCVELARLKFEKYFNHKALQLLHCFPLDIRLKDGSLFWQSPKRPPSPIKFDLNEPLH 754
Cdd:TIGR01408  634 GHSREGLEQIIKLLSkEKPRNFSQCVEWARLKFEKYFNNKALQLLHCFPLDIRTSTGSPFWSSPKRPPSPLKFDLNEPLH 713

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996   755 LSFLQNAAKLYATVYCIPFAEEDLSADALLNILSEVKIQEFKP-SNKVVQTDETARKPDHVPIsseDERNAIFQLEKAIL 833
Cdd:TIGR01408  714 LSFIQAAAKLYATVYGIPFAEEDLSADALLNILSEVKIPEFKPrSNKKIQTDETARKPDTAPI---DDRNAIFQLEKAIL 790

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996   834 SNEATKSDLQMAVLSFEKDDDHNGHIDFITAASNLRAKMYSIEPADRFKTKRIAGKIIPAIATTTATVSGLVALEMIKVT 913
Cdd:TIGR01408  791 SNEATKSDFRMAPLSFEKDDDHNGHIDFITAASNLRAKNYSIEPADRFKTKFIAGKIIPAIATSTATVSGLVCLELIKVT 870

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996   914 -GGYPFEAYKNCFLNLAIPIVVFTETTEVRKTKIRNGISFTIWDRWTVHGkeDFTLLDFINAVKEKYGIEPTMVVQGVKM 992
Cdd:TIGR01408  871 dGGYKFEVYKNCFLNLAIPLFVFTEPTEVRKTKIRNGISFTIWDRWTLHG--DFTLLEFINAVKEKYGLEPTMVSQGVKL 948

                          970       980       990      1000      1010
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 150417996   993 LYVPVMPGHAKRLKLTMHKLVKPTTEKKY----VDLTVSFAPDIDGDEDLPGPPVRYY 1046
Cdd:TIGR01408  949 LYVPVMPGHAERLKLKMHKLVKPTTKKKLppyrVHLTVSFACDDDGDEDVPGPPVRIY 1006
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
 462-1005 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: 750.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996  462 NIFLVGCGAIGCEMLKNFALLGVGTsKEKGMITVTDPDLIEKSNLNRQFLFRPHHIQKPKSYTAADATLKINSQIKIDAH 541
Cdd:cd01490     1 KVFLVGAGAIGCELLKNFALMGVGT-GESGEITVTDMDNIEKSNLNRQFLFRPHDVGKPKSEVAAAAVKAMNPDLKITAL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996  542 LNKVCPTTETIYNDEFYTKQDVIITALDNVEARRYVDSRCLANLRPLLDSGTMGTKGHTEVIVPHLTESYNSHRDPPEEE 621
Cdd:cd01490    80 QNRVGPETEHIFNDEFWEKLDGVANALDNVDARMYVDRRCVYYRKPLLESGTLGTKGNTQVVIPHLTESYSSSRDPPEKS 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996  622 IPFCTLKSFPAAIEHTIQWARDKFESSFSHKPSLFNKFWqtyssaeevlqkiqsghslegcfqvikllsrrprnWSQCVE 701
Cdd:cd01490   160 IPLCTLKNFPNAIEHTIQWARDEFEGLFKQPPENVNQYL-----------------------------------FEDCVR 204

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996  702 LARLKFEKYFNHKALQLLHCFPLDIRLKDGSLFWQSPKRPPSPIKFDLNEPLHLSFLQNAAKLYATVYCIPfaeedlsad 781
Cdd:cd01490   205 WARLLFEKYFNNNIKQLLHNFPPDAVTSDGAPFWSGPKRCPTPLEFDVNNPLHLDFVLAAANLYAEVYGIP--------- 275

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996  782 allnilsevkiqefkpsnkvvqtdetarkpdhvpissedernaifqlekailsneatksdlqmavlSFEKDDDHNGHIDF 861
Cdd:cd01490   276 ------------------------------------------------------------------GFEKDDDTNFHMDF 289

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996  862 ITAASNLRAKMYSIEPADRFKTKRIAGKIIPAIATTTATVSGLVALEMIKVTGGY-PFEAYKNCFLNLAIPIVVFTETTE 940
Cdd:cd01490   290 ITAASNLRARNYSIPPADRHKTKRIAGKIIPAIATTTAAVTGLVCLELYKVVDGKrPLEAYKNAFLNLALPFFAFSEPIP 369

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 150417996  941 VRKTKIRNGISFTIWDRWTVHGKEDFTLLDFiNAVKEKYGIEPTMVVQGVKMLYVPVMPG--HAKRL 1005
Cdd:cd01490   370 APKVKYAYDEEWTIWDRFEVKGKQTLQELLI-DYFKEKYGLEVTMLSQGVSMLYSSFMPPakLKERL 435
UBA_E1_SCCH pfam10585
Ubiquitin-activating enzyme, SCCH domain; Ubiquitin-activating enzyme (E1 enzyme) activates ...
 631-884 9.97e-112

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: 346.52  E-value: 9.97e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996   631 PAAIEHTIQWARDKFESSFSHKPSLFNKFWQTYSSAEEVLQKIQSGHSLEGCFQVIKLL-SRRPRNWSQCVELARLKFEK 709
Cdd:pfam10585    1 PNAIEHTIQWARDEFEGLFVQPPEEVNKYLQPPQNFIESLLKQGGGQKLETLESVRKSLvTERPKTFEDCVAWARLKFEK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996   710 YFNHKALQLLHCFPLDIRLKDGSLFWQSPKRPPSPIKFDLNEPLHLSFLQNAAKLYATVYCIPfaeEDLSADALLNILSE 789
Cdd:pfam10585   81 LFNNDIKQLLYNFPPDHKTSSGAPFWSGPKRPPTPLEFDPNNPLHLDFVVAAANLRAQVYGIP---GSRDREAIAKVLSK 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996   790 VKIQEFKPSNKVVQ--TDETARKPDHVPISSEDERNAIFQLEKAILSNEATKSDLQMAVLSFEKDDDHNGHIDFITAASN 867
Cdd:pfam10585  158 VKVPEFKPKSGVKIqvNDEEAADPNAESEDDEDELDELLEELPKLAVSPSSLAGFRLNPIEFEKDDDTNFHIDFITAASN 237

                          250
                   ....*....|....*..
gi 150417996   868 LRAKMYSIEPADRFKTK 884
Cdd:pfam10585  238 LRARNYGIPPADRHKTK 254
UBA_e1_C smart00985
Ubiquitin-activating enzyme e1 C-terminal domain; This presumed domain found at the C terminus ...
 921-1043 1.04e-41

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: 148.95  E-value: 1.04e-41
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996    921 YKNCFLNLAIPIVVFTETTEVRKTKIRNGISFTIWDRWTVHGKeDFTLLDFINAVKEKYGIEPTMVVQGVKMLYVPVMP- 999
Cdd:smart00985    1 YKNAFLNLALPFFAFSEPIAAPKTKYRDKDKWTLWDRLEVPGG-DITLKELLDYFEEKYGLEVTMLSQGVSLLYSSFMPp 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 150417996   1000 -GHAKRLKLTMHKLVKPTTEK------KYVDLTVSFAPdiDGDEDLPGPPV 1043
Cdd:smart00985   80 kKHKERLDLPVTELVEQVTKKklpphvKYLVLEVSCED--EDDEDVEVPYI 128
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 441-621 2.91e-28

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: 114.46  E-value: 2.91e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996  441 DRYD---ALRAcIGDTLCQKLQNLNIFLVGCGAIGCEMLKNFALLGVGTskekgmITVTDPDLIEKSNLNRQFLFRPHHI 517
Cdd:COG0476     6 ERYSrqiLLPE-IGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGT------LTLVDDDVVELSNLQRQILYTEADV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996  518 QKPKSYTAADATLKINSQIKIDAHLNKVcpTTETIynDEFYTKQDVIITALDNVEARRYVDSRCLANLRPLLDSGTMGTK 597
Cdd:COG0476    79 GRPKVEAAAERLRALNPDVEVEAIPERL--TEENA--LELLAGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIGFE 154

                         170       180
                  ....*....|....*....|....*
gi 150417996  598 GHTEVIVPHLTESYNS-HRDPPEEE 621
Cdd:COG0476   155 GQVTVFIPGDTPCYRClFPEPPEPG 179
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 441-608 3.52e-15

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 78.11  E-value: 3.52e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996  441 DRYD--ALRACIGDTLCQKLQNLNIFLVGCGAIGCEMLKNFALLGVGTskekgmITVTDPDLIEKSNLNRQFLFRPHHIQ 518
Cdd:PRK07688    3 ERYSrqELFSPIGEEGQQKLREKHVLIIGAGALGTANAEMLVRAGVGK------VTIVDRDYVEWSNLQRQQLYTESDVK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996  519 K--PKSYTAADATLKINSQIKIDAHLNKVcpTTETIynDEFYTKQDVIITALDNVEARRYVDSRCLANLRPLLDSGTMGT 596
Cdd:PRK07688   77 NnlPKAVAAKKRLEEINSDVRVEAIVQDV--TAEEL--EELVTGVDLIIDATDNFETRFIVNDAAQKYGIPWIYGACVGS 152

                         170
                  ....*....|..
gi 150417996  597 KGHTEVIVPHLT 608
Cdd:PRK07688  153 YGLSYTIIPGKT 164
 
Name Accession Description Interval E-value
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 38-1046 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: 1834.52  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996    38 EIDDALYSRQRYVLGDTAMQKMAKSHVFLSGMGGLGLEIAKNLVLAGIKAVTIHDTEKCQAWDLGTNFFLSEDDVVnkRN 117
Cdd:TIGR01408    1 EIDEALYSRQLYVLGDEAMQKMAKSNVLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLSSNFFLSEDDVG--RN 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996   118 RAEAVLKHIAELNPYVHVTSSSVPFNETtdlsFLDKYQCVVLTEMKLPLQKKINDFCRSQCPPIKFISADVHGIWSRLFC 197
Cdd:TIGR01408   79 RAEAVVKKLAELNPYVHVSSSSVPFNEE----FLDKFQCVVLTEMSLPLQKEINDFCHSQCPPIAFISADVRGLFGSLFC 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996   198 DFGDEFEVLDTTGEEPKEIFISNITQANPGIVTCLENHPHKLETGQFLTFREINGMTGLN-GSIQQITVISPFSFSIGDT 276
Cdd:TIGR01408  155 DFGDEFEVLDTDGEEPKTGFIASITQANPGIVTCLENHRHKLETGDFVTFREVNGMTGLNdGSPRKITVISPYSFSIGDT 234

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996   277 TELEPYLHGGIAVQVKTPKTVFFESLERQLKHPKCLIVDFSNPEAPLEIHTAMLALDQFQEKYSRKPNVGCQQDSEELLK 356
Cdd:TIGR01408  235 TELGPYLHGGIATQVKTPKTVFFKSLREQLKDPKCLIVDFSKPERPPEIHTAFQALDQFQEKYSRKPNVGCQQDAEELLK 314

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996   357 LATSISETLEEK-PDVNADIVHWLSWTAQGFLSPLAAAVGGVASQEVLKAVTGKFSPLCQWLYLEAADIVESLGKPECEE 435
Cdd:TIGR01408  315 LATSISETLEEKvPDVDAKLVHWLSWTAQGFLSPMAAAVGGVVSQEVLKAVTGKFSPLCQWFYFDSAESLPSLGKPECEE 394

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996   436 FLPRGDRYDALRACIGDTLCQKLQNLNIFLVGCGAIGCEMLKNFALLGVGTSkEKGMITVTDPDLIEKSNLNRQFLFRPH 515
Cdd:TIGR01408  395 FLPRGDRYDAQIAVFGDTFQQKLQNLNIFLVGCGAIGCEMLKNFALMGVGTG-KKGMITVTDPDLIEKSNLNRQFLFRPH 473

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996   516 HIQKPKSYTAADATLKINSQIKIDAHLNKVCPTTETIYNDEFYTKQDVIITALDNVEARRYVDSRCLANLRPLLDSGTMG 595
Cdd:TIGR01408  474 HIGKPKSYTAADATLKINPQIKIDAHQNRVGPETETIFNDEFYEKLDVVINALDNVEARRYVDSRCLAFLKPLLESGTLG 553

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996   596 TKGHTEVIVPHLTESYNSHRDPPEEEIPFCTLKSFPAAIEHTIQWARDKFESSFSHKPSLFNKFWQTYSSAEEVLQKIQS 675
Cdd:TIGR01408  554 TKGNTQVVVPHLTESYGSSRDPPEKEIPFCTLKSFPAAIEHTIQWARDKFEGLFSHKPSLVNKYLSSPSSAEEVLQKIQS 633

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996   676 GHSLEGCFQVIKLLS-RRPRNWSQCVELARLKFEKYFNHKALQLLHCFPLDIRLKDGSLFWQSPKRPPSPIKFDLNEPLH 754
Cdd:TIGR01408  634 GHSREGLEQIIKLLSkEKPRNFSQCVEWARLKFEKYFNNKALQLLHCFPLDIRTSTGSPFWSSPKRPPSPLKFDLNEPLH 713

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996   755 LSFLQNAAKLYATVYCIPFAEEDLSADALLNILSEVKIQEFKP-SNKVVQTDETARKPDHVPIsseDERNAIFQLEKAIL 833
Cdd:TIGR01408  714 LSFIQAAAKLYATVYGIPFAEEDLSADALLNILSEVKIPEFKPrSNKKIQTDETARKPDTAPI---DDRNAIFQLEKAIL 790

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996   834 SNEATKSDLQMAVLSFEKDDDHNGHIDFITAASNLRAKMYSIEPADRFKTKRIAGKIIPAIATTTATVSGLVALEMIKVT 913
Cdd:TIGR01408  791 SNEATKSDFRMAPLSFEKDDDHNGHIDFITAASNLRAKNYSIEPADRFKTKFIAGKIIPAIATSTATVSGLVCLELIKVT 870

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996   914 -GGYPFEAYKNCFLNLAIPIVVFTETTEVRKTKIRNGISFTIWDRWTVHGkeDFTLLDFINAVKEKYGIEPTMVVQGVKM 992
Cdd:TIGR01408  871 dGGYKFEVYKNCFLNLAIPLFVFTEPTEVRKTKIRNGISFTIWDRWTLHG--DFTLLEFINAVKEKYGLEPTMVSQGVKL 948

                          970       980       990      1000      1010
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 150417996   993 LYVPVMPGHAKRLKLTMHKLVKPTTEKKY----VDLTVSFAPDIDGDEDLPGPPVRYY 1046
Cdd:TIGR01408  949 LYVPVMPGHAERLKLKMHKLVKPTTKKKLppyrVHLTVSFACDDDGDEDVPGPPVRIY 1006
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
 462-1005 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: 750.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996  462 NIFLVGCGAIGCEMLKNFALLGVGTsKEKGMITVTDPDLIEKSNLNRQFLFRPHHIQKPKSYTAADATLKINSQIKIDAH 541
Cdd:cd01490     1 KVFLVGAGAIGCELLKNFALMGVGT-GESGEITVTDMDNIEKSNLNRQFLFRPHDVGKPKSEVAAAAVKAMNPDLKITAL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996  542 LNKVCPTTETIYNDEFYTKQDVIITALDNVEARRYVDSRCLANLRPLLDSGTMGTKGHTEVIVPHLTESYNSHRDPPEEE 621
Cdd:cd01490    80 QNRVGPETEHIFNDEFWEKLDGVANALDNVDARMYVDRRCVYYRKPLLESGTLGTKGNTQVVIPHLTESYSSSRDPPEKS 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996  622 IPFCTLKSFPAAIEHTIQWARDKFESSFSHKPSLFNKFWqtyssaeevlqkiqsghslegcfqvikllsrrprnWSQCVE 701
Cdd:cd01490   160 IPLCTLKNFPNAIEHTIQWARDEFEGLFKQPPENVNQYL-----------------------------------FEDCVR 204

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996  702 LARLKFEKYFNHKALQLLHCFPLDIRLKDGSLFWQSPKRPPSPIKFDLNEPLHLSFLQNAAKLYATVYCIPfaeedlsad 781
Cdd:cd01490   205 WARLLFEKYFNNNIKQLLHNFPPDAVTSDGAPFWSGPKRCPTPLEFDVNNPLHLDFVLAAANLYAEVYGIP--------- 275

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996  782 allnilsevkiqefkpsnkvvqtdetarkpdhvpissedernaifqlekailsneatksdlqmavlSFEKDDDHNGHIDF 861
Cdd:cd01490   276 ------------------------------------------------------------------GFEKDDDTNFHMDF 289

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996  862 ITAASNLRAKMYSIEPADRFKTKRIAGKIIPAIATTTATVSGLVALEMIKVTGGY-PFEAYKNCFLNLAIPIVVFTETTE 940
Cdd:cd01490   290 ITAASNLRARNYSIPPADRHKTKRIAGKIIPAIATTTAAVTGLVCLELYKVVDGKrPLEAYKNAFLNLALPFFAFSEPIP 369

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 150417996  941 VRKTKIRNGISFTIWDRWTVHGKEDFTLLDFiNAVKEKYGIEPTMVVQGVKMLYVPVMPG--HAKRL 1005
Cdd:cd01490   370 APKVKYAYDEEWTIWDRFEVKGKQTLQELLI-DYFKEKYGLEVTMLSQGVSMLYSSFMPPakLKERL 435
Ube1_repeat1 cd01491
Ubiquitin activating enzyme (E1), repeat 1. E1, a highly conserved small protein present ...
 43-432 2.58e-150

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: 448.64  E-value: 2.58e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996   43 LYSRQRYVLGDTAMQKMAKSHVFLSGMGGLGLEIAKNLVLAGIKAVTIHDTEKCQAWDLGTNFFLSEDDVvnKRNRAEAV 122
Cdd:cd01491     1 LYSRQLYVLGHEAMKKLQKSNVLISGLGGLGVEIAKNLILAGVKSVTLHDTKPCSWSDLSSQFYLREEDI--GKNRAEAS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996  123 LKHIAELNPYVHVTSSSVPFNETtdlsFLDKYQCVVLTEMKLPLQKKINDFCRSqcPPIKFISADVHGIWSRLFCDFGDE 202
Cdd:cd01491    79 QARLAELNPYVPVTVSTGPLTTD----ELLKFQVVVLTDASLEDQLKINEFCHS--PGIKFISADTRGLFGSIFCDFGDE 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996  203 FEVLDTTGEEPKEIFISNITQANPGIVTCLENHPHKLETGQFLTFREINGMTGLNGSIQQ-ITVISPFSFSIGDTTELEP 281
Cdd:cd01491   153 FTVYDPNGEEPKSGMISSISKDNPGVVTCLDETRHGFEDGDYVTFSEVEGMTELNGCEPRkIKVKGPYTFSIGDTSSFSE 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996  282 YLHGGIAVQVKtpktvffeslerqlkhpkclivdfsnpeapleihtamlaldqfqekysrkpnvgcqqdseellklatsi 361
Cdd:cd01491   233 YIRGGIVTQVK--------------------------------------------------------------------- 243

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 150417996  362 setleekpdvnadivhwlswtaqgfLSPLAAAVGGVASQEVLKAVTGKFSPLCQWLYLEAadiVESLGKPE 432
Cdd:cd01491   244 -------------------------LSPMAAFFGGLAAQEVLKACSGKFTPLKQWLYFDA---LECLPEDE 286
UBA_E1_SCCH pfam10585
Ubiquitin-activating enzyme, SCCH domain; Ubiquitin-activating enzyme (E1 enzyme) activates ...
 631-884 9.97e-112

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: 346.52  E-value: 9.97e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996   631 PAAIEHTIQWARDKFESSFSHKPSLFNKFWQTYSSAEEVLQKIQSGHSLEGCFQVIKLL-SRRPRNWSQCVELARLKFEK 709
Cdd:pfam10585    1 PNAIEHTIQWARDEFEGLFVQPPEEVNKYLQPPQNFIESLLKQGGGQKLETLESVRKSLvTERPKTFEDCVAWARLKFEK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996   710 YFNHKALQLLHCFPLDIRLKDGSLFWQSPKRPPSPIKFDLNEPLHLSFLQNAAKLYATVYCIPfaeEDLSADALLNILSE 789
Cdd:pfam10585   81 LFNNDIKQLLYNFPPDHKTSSGAPFWSGPKRPPTPLEFDPNNPLHLDFVVAAANLRAQVYGIP---GSRDREAIAKVLSK 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996   790 VKIQEFKPSNKVVQ--TDETARKPDHVPISSEDERNAIFQLEKAILSNEATKSDLQMAVLSFEKDDDHNGHIDFITAASN 867
Cdd:pfam10585  158 VKVPEFKPKSGVKIqvNDEEAADPNAESEDDEDELDELLEELPKLAVSPSSLAGFRLNPIEFEKDDDTNFHIDFITAASN 237

                          250
                   ....*....|....*..
gi 150417996   868 LRAKMYSIEPADRFKTK 884
Cdd:pfam10585  238 LRARNYGIPPADRHKTK 254
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
 463-651 2.81e-66

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: 222.84  E-value: 2.81e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996  463 IFLVGCGAIGCEMLKNFALLGVGTskekgmITVTDPDLIEKSNLNRQFLFRPHHIQKPKSYTAADATLKINSQIKIDAHL 542
Cdd:cd01484     2 VLLVGAGGIGCELLKNLALMGFGQ------IHVIDMDTIDVSNLNRQFLFRPKDIGRPKSEVAAEAVNDRNPNCKVVPYQ 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996  543 NKVCPttETIYNDEFYTKQDVIITALDNVEARRYVDSRCLANLRPLLDSGTMGTKGHTEVIVPHLTESYNSHRDPPEEEI 622
Cdd:cd01484    76 NKVGP--EQDFNDTFFEQFHIIVNALDNIIARRYVNGMLIFLIVPLIESGTEGFKGNAQVILPGMTECIECTLYPPQKNF 153

                         170       180
                  ....*....|....*....|....*....
gi 150417996  623 PFCTLKSFPAAIEHTIQWARDKFESSFSH 651
Cdd:cd01484   154 PMCTIASMPRLPEHCIEWARMLQWDDPEH 182
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 463-928 1.07e-56

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


Pssm-ID: 238766 [Multi-domain]  Cd Length: 312  Bit Score: 198.76  E-value: 1.07e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996  463 IFLVGCGAIGCEMLKNFALLGVGTskekgmITVTDPDLIEKSNLNRQFLFRPHHIQKPKSYTAADATLKINSQIKIDAHL 542
Cdd:cd01489     2 VLVVGAGGIGCELLKNLVLTGFGE------IHIIDLDTIDLSNLNRQFLFRKKHVGKSKAQVAKEAVLSFNPNVKIVAYH 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996  543 NKVcptTETIYNDEFYTKQDVIITALDNVEARRYVDSRCLANLRPLLDSGTMGTKGHTEVIVPHLTESYNSHRDPPEEEI 622
Cdd:cd01489    76 ANI---KDPDFNVEFFKQFDLVFNALDNLAARRHVNKMCLAADVPLIESGTTGFLGQVQVIKKGKTECYECQPKETPKTF 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996  623 PFCTLKSFPAAIEHTIQWARDKFessfshkpSLFNKFwqtyssaeevlqkiqsghslegcfqvikllsrrprnwsqcvel 702
Cdd:cd01489   153 PVCTIRSTPSQPIHCIVWAKSLF--------FLFNKV------------------------------------------- 181

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996  703 arlkfekyfnhkalqllhcFPLDI-RLKDGSLFWQSPKRPpspikfdlneplhlsflqnaaklyatvycipfaeedlsad 781
Cdd:cd01489   182 -------------------FKDDIeRLLSMEELWKTRKPP---------------------------------------- 202

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996  782 allnilsevkiqefkpsnkvvqtdetarkpdhVPISSEDernaifqlekailsneatksdlqmavLSFEKDDDHNghIDF 861
Cdd:cd01489   203 --------------------------------VPLSWKE--------------------------LTFDKDDQDA--LDF 222

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 150417996  862 ITAASNLRAKMYSIEPADRFKTKRIAGKIIPAIATTTATVSGLVALEMIKVTGGYpFEAYKNCFLNL 928
Cdd:cd01489   223 VAAAANLRSHVFGIPMKSRFDIKQMAGNIIPAIATTNAIIAGLIVLEALKVLSGD-KEQCRTVFLNL 288
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 443-630 1.92e-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: 1.92e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996   443 YDALRAC--IGDTLCQKLQNLNIFLVGCGAIGCEMLKNFALLGVGTskekgmITVTDPDLIEKSNLNRQFLFRPHHIQKP 520
Cdd:pfam00899    1 YSRQLALplIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGK------ITLVDFDTVELSNLNRQFLFREADIGKP 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996   521 KSYTAADATLKINSQIKIDAHLNKVCPTTetiyNDEFYTKQDVIITALDNVEARRYVDSRCLANLRPLLDSGTMGTKGHT 600
Cdd:pfam00899   75 KAEVAAERLREINPDVEVEAYTERLTPEN----AEELIKSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQV 150

                          170       180       190
                   ....*....|....*....|....*....|..
gi 150417996   601 EVIVPHLTESYNSH--RDPPEEEIPFCTLKSF 630
Cdd:pfam00899  151 TVVIPGKTPCYRCLfpEDPPPKLVPSCTVAGV 182
E1-1_like cd01485
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ...
 43-199 7.61e-44

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: 157.58  E-value: 7.61e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996   43 LYSRQRYVLGDTAMQKMAKSHVFLSGMGGLGLEIAKNLVLAGIKAVTIHDTEKCQAWDLGTNFFLSEDDVVNKRNRAEAV 122
Cdd:cd01485     1 LYDRQIRLWGDEAQNKLRSAKVLIIGAGALGAEIAKNLVLAGIDSITIVDHRLVSTEDLGSNFFLDAEVSNSGMNRAAAS 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 150417996  123 LKHIAELNPYVHVT--SSSVPFNETTDLSFLDKYQCVVLTEMKLPLQKKINDFCRSQcpPIKFISADVHGIWSRLFCDF 199
Cdd:cd01485    81 YEFLQELNPNVKLSivEEDSLSNDSNIEEYLQKFTLVIATEENYERTAKVNDVCRKH--HIPFISCATYGLIGYAFFDF 157
UBA_e1_C smart00985
Ubiquitin-activating enzyme e1 C-terminal domain; This presumed domain found at the C terminus ...
 921-1043 1.04e-41

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: 148.95  E-value: 1.04e-41
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996    921 YKNCFLNLAIPIVVFTETTEVRKTKIRNGISFTIWDRWTVHGKeDFTLLDFINAVKEKYGIEPTMVVQGVKMLYVPVMP- 999
Cdd:smart00985    1 YKNAFLNLALPFFAFSEPIAAPKTKYRDKDKWTLWDRLEVPGG-DITLKELLDYFEEKYGLEVTMLSQGVSLLYSSFMPp 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 150417996   1000 -GHAKRLKLTMHKLVKPTTEK------KYVDLTVSFAPdiDGDEDLPGPPV 1043
Cdd:smart00985   80 kKHKERLDLPVTELVEQVTKKklpphvKYLVLEVSCED--EDDEDVEVPYI 128
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 463-642 3.81e-39

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: 147.50  E-value: 3.81e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996  463 IFLVGCGAIGCEMLKNFALLGVGTskekgmITVTDPDLIEKSNLNRQFLFRPHHIQKPKSYTAADATLKINSQIKIDAHL 542
Cdd:cd01488     2 ILVIGAGGLGCELLKNLALSGFRN------IHVIDMDTIDVSNLNRQFLFREKDIGKPKAEVAAKFVNDRVPGVNVTPHF 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996  543 NKVcptteTIYNDEFYTKQDVIITALDNVEARRYVDSRCL--------ANLRPLLDSGTMGTKGHTEVIVPHLTESYNSH 614
Cdd:cd01488    76 GKI-----QDKDEEFYRQFNIIICGLDSIEARRWINGTLVslllyedpESIIPLIDGGTEGFKGHARVILPGITACIECS 150

                         170       180       190
                  ....*....|....*....|....*....|
gi 150417996  615 RD--PPEEEIPFCTLKSFPAAIEHTIQWAR 642
Cdd:cd01488   151 LDlfPPQVTFPLCTIANTPRLPEHCIEYAS 180
Aos1_SUMO cd01492
Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating ...
 42-198 2.53e-34

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: 130.49  E-value: 2.53e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996   42 ALYSRQRYVLGDTAMQKMAKSHVFLSGMGGLGLEIAKNLVLAGIKAVTIHDTEKCQAWDLGTNFFLSEDDVvnKRNRAEA 121
Cdd:cd01492     2 ALYDRQIRLWGLEAQKRLRSARILLIGLKGLGAEIAKNLVLSGIGSLTILDDRTVTEEDLGAQFLIPAEDL--GQNRAEA 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 150417996  122 VLKHIAELNPYVHVTSSSVPFNETTDlSFLDKYQCVVLTEMKLPLQKKINDFCRSQcpPIKFISADVHGIWSRLFCD 198
Cdd:cd01492    80 SLERLRALNPRVKVSVDTDDISEKPE-EFFSQFDVVVATELSRAELVKINELCRKL--GVKFYATGVHGLFGFVFAD 153
E1_FCCH pfam16190
Ubiquitin-activating enzyme E1 FCCH domain; This domain is found in the ubiquitin-activating ...
 225-292 9.42e-33

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: 121.05  E-value: 9.42e-33
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 150417996   225 NPGIVTCLENHPHKLETGQFLTFREINGMTGLNGS-IQQITVISPFSFSIGDTTELEPYLHGGIAVQVK 292
Cdd:pfam16190    2 NPGVVTCLDDTRHGLEDGDYVTFSEVEGMTELNGCePRKIKVLGPYTFSIGDTSSFSPYLRGGIVTQVK 70
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 463-603 8.28e-30

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: 115.44  E-value: 8.28e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996  463 IFLVGCGAIGCEMLKNFALLGVGTskekgmITVTDPDLIEKSNLNRQFLFRPHHIQKPKSYTAADATLKINSQIKIDAHL 542
Cdd:cd01483     2 VLLVGLGGLGSEIALNLARSGVGK------ITLIDFDTVELSNLNRQFLARQADIGKPKAEVAARRLNELNPGVNVTAVP 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 150417996  543 NKVcpttETIYNDEFYTKQDVIITALDNVEARRYVDSRCLANLRPLLDSGTMGTKGHTEVI 603
Cdd:cd01483    76 EGI----SEDNLDDFLDGVDLVIDAIDNIAVRRALNRACKELGIPVIDAGGLGLGGDIQVI 132
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 441-621 2.91e-28

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: 114.46  E-value: 2.91e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996  441 DRYD---ALRAcIGDTLCQKLQNLNIFLVGCGAIGCEMLKNFALLGVGTskekgmITVTDPDLIEKSNLNRQFLFRPHHI 517
Cdd:COG0476     6 ERYSrqiLLPE-IGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGT------LTLVDDDVVELSNLQRQILYTEADV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996  518 QKPKSYTAADATLKINSQIKIDAHLNKVcpTTETIynDEFYTKQDVIITALDNVEARRYVDSRCLANLRPLLDSGTMGTK 597
Cdd:COG0476    79 GRPKVEAAAERLRALNPDVEVEAIPERL--TEENA--LELLAGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIGFE 154

                         170       180
                  ....*....|....*....|....*
gi 150417996  598 GHTEVIVPHLTESYNS-HRDPPEEE 621
Cdd:COG0476   155 GQVTVFIPGDTPCYRClFPEPPEPG 179
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 456-625 1.05e-27

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: 112.19  E-value: 1.05e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996  456 QKLQNLNIFLVGCGAIGCEMLKNFALLGVGTskekgmITVTDPDLIEKSNLNRQFLFRPHHIQKPKSYTAADATLKINSQ 535
Cdd:cd00757    17 EKLKNARVLVVGAGGLGSPAAEYLAAAGVGK------LGLVDDDVVELSNLQRQILHTEADVGQPKAEAAAERLRAINPD 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996  536 IKIDAHLNKVcpTTETIynDEFYTKQDVIITALDNVEARRYVDSRCLANLRPLLDSGTMGTKGHTEVIVPHLTESYN-SH 614
Cdd:cd00757    91 VEIEAYNERL--DAENA--EELIAGYDLVLDCTDNFATRYLINDACVKLGKPLVSGAVLGFEGQVTVFIPGEGPCYRcLF 166

                         170
                  ....*....|.
gi 150417996  615 RDPPEEEIPFC 625
Cdd:cd00757   167 PEPPPPGVPSC 177
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 44-232 1.40e-26

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: 109.27  E-value: 1.40e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996    44 YSRQRY--VLGDTAMQKMAKSHVFLSGMGGLGLEIAKNLVLAGIKAVTIHDTEKCQAWDLGTNFFLSEDDVvnKRNRAEA 121
Cdd:pfam00899    1 YSRQLAlpLIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADI--GKPKAEV 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996   122 VLKHIAELNPYVHVTSSSVPFNETTDLSFLDKYQCVVLTEMKLPLQKKINDFC-RSQcppIKFISADVHGIWSRLF---- 196
Cdd:pfam00899   79 AAERLREINPDVEVEAYTERLTPENAEELIKSFDIVVDATDNFAARYLVNDACvKLG---KPLIEAGVLGFKGQVTvvip 155

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 150417996   197 -------CDFGDefevlDTTGEEPKEIFISNITQANPGIVTCL 232
Cdd:pfam00899  156 gktpcyrCLFPE-----DPPPKLVPSCTVAGVLGPTTAVVAGL 193
E1_4HB pfam16191
Ubiquitin-activating enzyme E1 four-helix bundle; This domain is found in the ...
 293-362 1.45e-23

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: 94.83  E-value: 1.45e-23
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996   293 TPKTVFFESLERQLKHPKCLIVDFSNPEAPLEIHTAMLALDQFQEKYSRKPNVGCQQDSEELLKLATSIS 362
Cdd:pfam16191    1 MPKTLSFKSLEESLKEPEFLISDFAKFDRPAQLHLAFQALHAFQEKHGRLPRPWNEEDAEEVVKLAKELN 70
E1_UFD pfam09358
Ubiquitin fold domain; The ubiquitin fold domain is found at the C-terminus of ...
 955-1043 1.89e-20

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: 86.83  E-value: 1.89e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996   955 WDRWTVHGkeDFTLLDFINAVKEKYGIEPTMVVQGVKMLYVPVMPG--HAKRLKLTMHKLVKPTTEK------KYVDLTV 1026
Cdd:pfam09358    1 WDRFEVEG--DMTLQELLDYFKEKYGLEVTMLSYGVSLLYSSFMPPkkHKERLPMKISELVEEVSKKpipphqKYLVLEV 78

                           90
                   ....*....|....*..
gi 150417996  1027 SFapDIDGDEDLPGPPV 1043
Cdd:pfam09358   79 SC--EDEDGEDVEVPYV 93
APPBP1_RUB cd01493
Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric ...
 44-177 7.47e-19

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: 90.44  E-value: 7.47e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996   44 YSRQRYVLGDTAMQKMAKSHVFLSGMGGLGLEIAKNLVLAGIKAVTIHDTEKCQAWDLGTNFFLSEDDVvnKRNRAEAVL 123
Cdd:cd01493     3 YDRQLRLWGEHGQAALESAHVCLLNATATGTEILKNLVLPGIGSFTIVDGSKVDEEDLGNNFFLDASSL--GKSRAEATC 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 150417996  124 KHIAELNPyvHVTSSSVPFNETT----DLSFLDKYQCVVLTEMKLPLQKKINDFCRSQ 177
Cdd:cd01493    81 ELLQELNP--DVNGSAVEESPEAlldnDPSFFSQFTVVIATNLPESTLLRLADVLWSA 136
adenyl_thiF TIGR02356
thiazole biosynthesis adenylyltransferase ThiF, E. coli subfamily; Members of the HesA/MoeB ...
 456-606 2.66e-18

thiazole biosynthesis adenylyltransferase ThiF, E. coli subfamily; Members of the HesA/MoeB/ThiF family of proteins (pfam00899) include a number of members encoded in the midst of thiamine biosynthetic operons. This mix of known and putative ThiF proteins shows a deep split in phylogenetic trees, with the Escherichia. coli ThiF and the E. coli MoeB proteins seemingly more closely related than E. coli ThiF and Campylobacter (for example) ThiF. This model represents the more widely distributed clade of ThiF proteins such found in E. coli. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]


Pssm-ID: 274094  Cd Length: 202  Bit Score: 84.33  E-value: 2.66e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996   456 QKLQNLNIFLVGCGAIGCEMLKNFALLGVGTskekgmITVTDPDLIEKSNLNRQFLFRPHHIQKPKSYTAADATLKINSQ 535
Cdd:TIGR02356   17 QRLLNSHVLIIGAGGLGSPAALYLAGAGVGT------IVIVDDDHVDLSNLQRQILFTEEDVGRPKVEVAAQRLRELNSD 90

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 150417996   536 IKIDAHLNKVcptTETIYNDEFyTKQDVIITALDNVEARRYVDSRCLANLRPLLDSGTMGTKGHTEVIVPH 606
Cdd:TIGR02356   91 IQVTALKERV---TAENLELLI-NNVDLVLDCTDNFATRYLINDACVALGTPLISAAVVGFGGQLMVFDPG 157
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 63-175 2.82e-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: 82.32  E-value: 2.82e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996   63 HVFLSGMGGLGLEIAKNLVLAGIKAVTIHDTEKCQAWDLGTNFFLSEDDVvnKRNRAEAVLKHIAELNPYVHVTSSSVPF 142
Cdd:cd01483     1 RVLLVGLGGLGSEIALNLARSGVGKITLIDFDTVELSNLNRQFLARQADI--GKPKAEVAARRLNELNPGVNVTAVPEGI 78

                          90       100       110
                  ....*....|....*....|....*....|...
gi 150417996  143 NETTDLSFLDKYQCVVLTEMKLPLQKKINDFCR 175
Cdd:cd01483    79 SEDNLDDFLDGVDLVIDAIDNIAVRRALNRACK 111
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 441-608 3.52e-15

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 78.11  E-value: 3.52e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996  441 DRYD--ALRACIGDTLCQKLQNLNIFLVGCGAIGCEMLKNFALLGVGTskekgmITVTDPDLIEKSNLNRQFLFRPHHIQ 518
Cdd:PRK07688    3 ERYSrqELFSPIGEEGQQKLREKHVLIIGAGALGTANAEMLVRAGVGK------VTIVDRDYVEWSNLQRQQLYTESDVK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996  519 K--PKSYTAADATLKINSQIKIDAHLNKVcpTTETIynDEFYTKQDVIITALDNVEARRYVDSRCLANLRPLLDSGTMGT 596
Cdd:PRK07688   77 NnlPKAVAAKKRLEEINSDVRVEAIVQDV--TAEEL--EELVTGVDLIIDATDNFETRFIVNDAAQKYGIPWIYGACVGS 152

                         170
                  ....*....|..
gi 150417996  597 KGHTEVIVPHLT 608
Cdd:PRK07688  153 YGLSYTIIPGKT 164
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 450-608 4.96e-15

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 77.85  E-value: 4.96e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996  450 IGDTLCQKLQNLNIFLVGCGAIGCEMLKNFALLGVGTskekgmITVTDPDLIEKSNLNRQFLFRPHHIQ--KPKSYTAAD 527
Cdd:PRK12475   14 IGEEGQRKIREKHVLIVGAGALGAANAEALVRAGIGK------LTIADRDYVEWSNLQRQQLYTEEDAKqkKPKAIAAKE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996  528 ATLKINSQIKIDAHLNKVCPttETIynDEFYTKQDVIITALDNVEARRYVDSRCLANLRPLLDSGTMGTKGHTEVIVPHL 607
Cdd:PRK12475   88 HLRKINSEVEIVPVVTDVTV--EEL--EELVKEVDLIIDATDNFDTRLLINDLSQKYNIPWIYGGCVGSYGVTYTIIPGK 163


                  .
gi 150417996  608 T 608
Cdd:PRK12475  164 T 164
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
 450-597 5.80e-13

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


Pssm-ID: 238384 [Multi-domain]  Cd Length: 231  Bit Score: 69.56  E-value: 5.80e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996  450 IGDTLCQKLQNLNIFLVGCGAIG---CEMLknfALLGVGTskekgmITVTDPDLIEKSNLNRQFLFRPHHIQKPKSYTAA 526
Cdd:cd00755     1 YGEEGLEKLRNAHVAVVGLGGVGswaAEAL---ARSGVGK------LTLIDFDVVCVSNLNRQIHALLSTVGKPKVEVMA 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 150417996  527 DATLKINSQIKIDAHLNKVCPTTEtiynDEFYTKQ-DVIITALDNVEARRYVDSRCLANLRPLLDSGTMGTK 597
Cdd:cd00755    72 ERIRDINPECEVDAVEEFLTPDNS----EDLLGGDpDFVVDAIDSIRAKVALIAYCRKRKIPVISSMGAGGK 139
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
443-575 2.46e-12

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 67.19  E-value: 2.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996  443 YDALRACIGDTLCQKLQNLNIFLVGCGAIGcemlKNFALL----GVGTskekgmITVTDPDLIEKSNLNRQFLFrPHHIQ 518
Cdd:PRK08644   11 EAMLASRHTPKLLEKLKKAKVGIAGAGGLG----SNIAVAlarsGVGN------LKLVDFDVVEPSNLNRQQYF-ISQIG 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 150417996  519 KPKSYTAADATLKINSQIKIDAHLNKVcpTTETIynDEFYTKQDVIITALDNVEARR 575
Cdd:PRK08644   80 MPKVEALKENLLEINPFVEIEAHNEKI--DEDNI--EELFKDCDIVVEAFDNAETKA 132
PRK08328 PRK08328
hypothetical protein; Provisional
 441-610 3.64e-12

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 67.13  E-value: 3.64e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996  441 DRYDALRACIGDTLCQKLQNLNIFLVGCGAIGCEMLKNFALLGVGTskekgmITVTDPDLIEKSNLNRQFLFRPHHIQK- 519
Cdd:PRK08328    8 ERYDRQIMIFGVEGQEKLKKAKVAVVGVGGLGSPVAYYLAAAGVGR------ILLIDEQTPELSNLNRQILHWEEDLGKn 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996  520 PKSYTAADATLKINSQIKIDAHLNKVcpTTETIynDEFYTKQDVIITALDNVEARRYVDSRCLANLRPLLDSGTMGTKGH 599
Cdd:PRK08328   82 PKPLSAKWKLERFNSDIKIETFVGRL--SEENI--DEVLKGVDVIVDCLDNFETRYLLDDYAHKKGIPLVHGAVEGTYGQ 157

                         170
                  ....*....|.
gi 150417996  600 TEVIVPHLTES 610
Cdd:PRK08328  158 VTTIVPGKTKR 168
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 456-595 7.97e-12

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 66.41  E-value: 7.97e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996  456 QKLQNLNIFLVGCGAIGCEMLKNFALLGVGTskekgmITVTDPDLIEKSNLNRQFLFRPHHIQKPKSYTAADATLKINSQ 535
Cdd:PRK05690   28 EKLKAARVLVVGLGGLGCAASQYLAAAGVGT------LTLVDFDTVSLSNLQRQVLHDDATIGQPKVESARAALARINPH 101

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996  536 IKIDAHlNKVCPTTETiynDEFYTKQDVIITALDNVEARRYVDSRCLANLRPLLdSGTMG 595
Cdd:PRK05690  102 IAIETI-NARLDDDEL---AALIAGHDLVLDCTDNVATRNQLNRACFAAKKPLV-SGAAI 156
Aos1_SUMO cd01492
Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating ...
 456-598 2.54e-11

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: 63.85  E-value: 2.54e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996  456 QKLQNLNIFLVGCGAIGCEMLKNFALLGVGTskekgmITVTDPDLIEKSNLNRQFLFRPHHIQKPKSYTAADATLKINSQ 535
Cdd:cd01492    17 KRLRSARILLIGLKGLGAEIAKNLVLSGIGS------LTILDDRTVTEEDLGAQFLIPAEDLGQNRAEASLERLRALNPR 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 150417996  536 IKIDAhlnkvcpTTETI--YNDEFYTKQDVII-TALDNVEARRyVDSRCLANLRPLLDSGTMGTKG 598
Cdd:cd01492    91 VKVSV-------DTDDIseKPEEFFSQFDVVVaTELSRAELVK-INELCRKLGVKFYATGVHGLFG 148
E1_ThiF_like cd01487
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ...
 463-575 3.50e-11

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: 62.78  E-value: 3.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996  463 IFLVGCGAIGCEMLKNFALLGVGTskekgmITVTDPDLIEKSNLNRQFlFRPHHIQKPKSYTAADATLKINSQIKIDAHL 542
Cdd:cd01487     2 VGIAGAGGLGSNIAVLLARSGVGN------LKLVDFDVVEPSNLNRQQ-YFLSQIGEPKVEALKENLREINPFVKIEAIN 74

                          90       100       110
                  ....*....|....*....|....*....|...
gi 150417996  543 NKVcpttETIYNDEFYTKQDVIITALDNVEARR 575
Cdd:cd01487    75 IKI----DENNLEGLFGDCDIVVEAFDNAETKA 103
Ube1_repeat1 cd01491
Ubiquitin activating enzyme (E1), repeat 1. E1, a highly conserved small protein present ...
 451-578 6.78e-11

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: 64.21  E-value: 6.78e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996  451 GDTLCQKLQNLNIFLVGCGAIGCEMLKNFALLGVGTskekgmITVTDPDLIEKSNLNRQFLFRPHHIQKPKSyTAADATL 530
Cdd:cd01491    10 GHEAMKKLQKSNVLISGLGGLGVEIAKNLILAGVKS------VTLHDTKPCSWSDLSSQFYLREEDIGKNRA-EASQARL 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 150417996  531 K-INSQIKIDAHlnkvcptTETIYNDEFYTKQDVIITALDNVEARRYVD 578
Cdd:cd01491    83 AeLNPYVPVTVS-------TGPLTTDELLKFQVVVLTDASLEDQLKINE 124
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 456-570 1.50e-10

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 64.13  E-value: 1.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996  456 QKLQNLNIFLVGCGAIGCEMLKNFALLGVGTskekgmITVTDPDLIEKSNLNRQFLFRPHHIQKPKSYTAADATLKINSQ 535
Cdd:PRK05600   37 ERLHNARVLVIGAGGLGCPAMQSLASAGVGT------ITLIDDDTVDVSNIHRQILFGASDVGRPKVEVAAERLKEIQPD 110

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 150417996  536 IKIDAHLNKVcpTTETIYndEFYTKQDVIITALDN 570
Cdd:PRK05600  111 IRVNALRERL--TAENAV--ELLNGVDLVLDGSDS 141
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
456-626 3.21e-10

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 63.11  E-value: 3.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996  456 QKLQNLNIFLVGCGAIGCEMLKNFALLGVGTskekgmITVTDPDLIEKSNLNRQFLFRPHHIQKPKSYTAADATLKINSQ 535
Cdd:PRK08762  131 RRLLEARVLLIGAGGLGSPAALYLAAAGVGT------LGIVDHDVVDRSNLQRQILHTEDRVGQPKVDSAAQRLAALNPD 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996  536 IKIDAHLNKVcpTTETIynDEFYTKQDVIITALDNVEARRYVDSRCLANLRPLLDSGTMGTKGHTEVIVPhltesyNSHR 615
Cdd:PRK08762  205 VQVEAVQERV--TSDNV--EALLQDVDVVVDGADNFPTRYLLNDACVKLGKPLVYGAVFRFEGQVSVFDA------GRQR 274

                         170       180
                  ....*....|....*....|...
gi 150417996  616 D------------PPEEEIPFCT 626
Cdd:PRK08762  275 GqapcyrclfpepPPPELAPSCA 297
E1-1_like cd01485
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ...
 443-605 3.95e-10

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


Pssm-ID: 238762 [Multi-domain]  Cd Length: 198  Bit Score: 60.51  E-value: 3.95e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996  443 YDALRACIGDTLCQKLQNLNIFLVGCGAIGCEMLKNFALLGVGTskekgmITVTDPDLIEKSNLNRQFLFRPHH--IQKP 520
Cdd:cd01485     2 YDRQIRLWGDEAQNKLRSAKVLIIGAGALGAEIAKNLVLAGIDS------ITIVDHRLVSTEDLGSNFFLDAEVsnSGMN 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996  521 KSYTAADATLKINSQIKidahLNKVCPTTETIYND--EFYTKQDVIITALDNVEARRYVDSRCLANLRPLLDSGTMGTKG 598
Cdd:cd01485    76 RAAASYEFLQELNPNVK----LSIVEEDSLSNDSNieEYLQKFTLVIATEENYERTAKVNDVCRKHHIPFISCATYGLIG 151


                  ....*..
gi 150417996  599 HTEVIVP 605
Cdd:cd01485   152 YAFFDFP 158
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 44-233 5.05e-10

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: 60.91  E-value: 5.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996   44 YSRQR--YVLGDTAMQKMAKSHVFLSGMGGLGLEIAKNLVLAGIKAVTI--HDTekcqaWDLgTN----FFLSEDDVvnK 115
Cdd:COG0476     8 YSRQIllPEIGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLvdDDV-----VEL-SNlqrqILYTEADV--G 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996  116 RNRAEAVLKHIAELNPYVHVTSSSVPFNETTDLSFLDKYQCVV------LTemklplQKKINDFCRSQCPPikFISADVH 189
Cdd:COG0476    80 RPKVEAAAERLRALNPDVEVEAIPERLTEENALELLAGADLVLdctdnfAT------RYLLNDACVKLGIP--LVSGAVI 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 150417996  190 GIWSRLF-----------CDFGDEFEVLDTTGEEPkeifisnITQANPGIVTCLE 233
Cdd:COG0476   152 GFEGQVTvfipgdtpcyrCLFPEPPEPGPSCAEAG-------VLGPLVGVIGSLQ 199
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 44-136 3.78e-08

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 56.54  E-value: 3.78e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996   44 YSRQRYV--LGDTAMQKMAKSHVFLSGMGGLGLEIAKNLVLAGIKAVTIHDTEKCQAWDLGTNFFLSEDDVVNKRNRAEA 121
Cdd:PRK07688    5 YSRQELFspIGEEGQQKLREKHVLIIGAGALGTANAEMLVRAGVGKVTIVDRDYVEWSNLQRQQLYTESDVKNNLPKAVA 84

                          90
                  ....*....|....*
gi 150417996  122 VLKHIAELNPYVHVT 136
Cdd:PRK07688   85 AKKRLEEINSDVRVE 99
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 456-585 3.92e-08

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 56.42  E-value: 3.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996  456 QKLQNLNIFLVGCGAIGCEMLKNFALLGVGTskekgmITVTDPDLIEKSNLNRQFLFRPHHIQKPKSYTAADATLKINSQ 535
Cdd:PRK05597   24 QSLFDAKVAVIGAGGLGSPALLYLAGAGVGH------ITIIDDDTVDLSNLHRQVIHSTAGVGQPKAESAREAMLALNPD 97

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 150417996  536 IKIDAHLNKVCPTTETiyndEFYTKQDVIITALDNVEArRYVDSRCLANL 585
Cdd:PRK05597   98 VKVTVSVRRLTWSNAL----DELRDADVILDGSDNFDT-RHLASWAAARL 142
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 456-584 1.93e-07

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 54.71  E-value: 1.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996  456 QKLQNLNIFLVGCGAIGCEMLKNFALLGVGTskekgmITVTDPDLIEKSNLNRQFLFRPHHIQKPKSYTAADATLKINSQ 535
Cdd:PRK07878   38 KRLKNARVLVIGAGGLGSPTLLYLAAAGVGT------LGIVEFDVVDESNLQRQVIHGQSDVGRSKAQSARDSIVEINPL 111

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 150417996  536 IKIDAHLNKVCPTTETiyndEFYTKQDVIITALDNVeARRYV--DSRCLAN 584
Cdd:PRK07878  112 VNVRLHEFRLDPSNAV----ELFSQYDLILDGTDNF-ATRYLvnDAAVLAG 157
PTZ00245 PTZ00245
ubiquitin activating enzyme; Provisional
 37-146 3.05e-07

ubiquitin activating enzyme; Provisional


Pssm-ID: 140272  Cd Length: 287  Bit Score: 53.14  E-value: 3.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996   37 VEIDDALYSRQRYVLGDTAMQKMAKSHVFLSGMGGLGLEIAKNLVLAGIKAVTIHDTEKCQAWDLGTNFFLSEDDVVNKR 116
Cdd:PTZ00245    2 RDAEAVRYDRQIRLWGKSTQQQLMHTSVALHGVAGAAAEAAKNLVLAGVRAVAVADEGLVTDADVCTNYLMQGEAGGTRG 81

                          90       100       110
                  ....*....|....*....|....*....|
gi 150417996  117 NRAEAVLKhiaELNPYVHVTSSSVPFNETT 146
Cdd:PTZ00245   82 ARALGALQ---RLNPHVSVYDAVTKLDGSS 108
APPBP1_RUB cd01493
Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric ...
 458-653 3.84e-07

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


Pssm-ID: 238770 [Multi-domain]  Cd Length: 425  Bit Score: 53.85  E-value: 3.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996  458 LQNLNIFLVGCGAIGCEMLKNFALLGVGTskekgmITVTDPDLIEKSNLNRQFLFRPHHIQKPKSYTAADATLKINSQIK 537
Cdd:cd01493    18 LESAHVCLLNATATGTEILKNLVLPGIGS------FTIVDGSKVDEEDLGNNFFLDASSLGKSRAEATCELLQELNPDVN 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996  538 IDAHLNKvcPTTETIYNDEFYTKQDVII-TALDNVEARRYVDSrcLANLR-PLLDSGTMGTKGHTEVIVPHLTeSYNSHR 615
Cdd:cd01493    92 GSAVEES--PEALLDNDPSFFSQFTVVIaTNLPESTLLRLADV--LWSANiPLLYVRSYGLYGYIRIQLKEHT-IVESHP 166

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 150417996  616 DPPEEEI----PFCTLKSFPAAIEhtiqwARDKFESSFSHKP 653
Cdd:cd01493   167 DNALEDLrldnPFPELREHADSID-----LDDMDPAEHSHTP 203
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 44-135 7.80e-07

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 52.43  E-value: 7.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996   44 YSRQRYV--LGDTAMQKMAKSHVFLSGMGGLGLEIAKNLVLAGIKAVTIHDTEKCQAWDLGTNFFLSEDDVVNKRNRAEA 121
Cdd:PRK12475    5 YSRQILFsgIGEEGQRKIREKHVLIVGAGALGAANAEALVRAGIGKLTIADRDYVEWSNLQRQQLYTEEDAKQKKPKAIA 84

                          90
                  ....*....|....
gi 150417996  122 VLKHIAELNPYVHV 135
Cdd:PRK12475   85 AKEHLRKINSEVEI 98
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 44-158 1.32e-06

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: 50.55  E-value: 1.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996   44 YSRQRYV--LGDTAMQKMAKSHVFLSGMGGLGLEIAKNLVLAGIKAVTIHDTEKCQAWDLGTNFFLSEDDVvnKRNRAEA 121
Cdd:cd00757     2 YSRQILLpeIGEEGQEKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRQILHTEADV--GQPKAEA 79

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 150417996  122 VLKHIAELNPYVHVTSSSVPFNETTDLSFLDKYQCVV 158
Cdd:cd00757    80 AAERLRAINPDVEIEAYNERLDAENAEELIAGYDLVL 116
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
456-582 8.66e-06

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 49.35  E-value: 8.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996  456 QKLQNLNIFLVGCGAIGCEMLKNFALLGVGTskekgmITVTDPDLIEKSNLNRQFLFRPHHIQKPKSYTAADATLKINSQ 535
Cdd:PRK07411   34 KRLKAASVLCIGTGGLGSPLLLYLAAAGIGR------IGIVDFDVVDSSNLQRQVIHGTSWVGKPKIESAKNRILEINPY 107

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 150417996  536 IKIDAHlnkvcPTTETIYND-EFYTKQDVIITALDNVEARRYVDSRCL 582
Cdd:PRK07411  108 CQVDLY-----ETRLSSENAlDILAPYDVVVDGTDNFPTRYLVNDACV 150
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 39-158 2.60e-05

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 47.56  E-value: 2.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996   39 IDDALYSRQRYV--LGDTAMQKMAKSHVFLSGMGGLGLEIAKNLVLAGIKAVTIHDTEKCQAWDLGTNFFLSEDDVvnKR 116
Cdd:PRK05597    4 LDIARYRRQIMLgeIGQQGQQSLFDAKVAVIGAGGLGSPALLYLAGAGVGHITIIDDDTVDLSNLHRQVIHSTAGV--GQ 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 150417996  117 NRAEAVLKHIAELNPYVHVTSSSVPFNETTDLSFLDKYQCVV 158
Cdd:PRK05597   82 PKAESAREAMLALNPDVKVTVSVRRLTWSNALDELRDADVIL 123
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 63-159 3.81e-04

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: 43.50  E-value: 3.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996   63 HVFLSGMGGLGLEIAKNLVLAGIKAVTIHDTEKCQAWDLGTNFFLSEDDVvnKRNRAEAVLKHIAELNPYVHVTsssvPF 142
Cdd:cd01488     1 KILVIGAGGLGCELLKNLALSGFRNIHVIDMDTIDVSNLNRQFLFREKDI--GKPKAEVAAKFVNDRVPGVNVT----PH 74

                          90       100
                  ....*....|....*....|
gi 150417996  143 N---ETTDLSFLDKYQCVVL 159
Cdd:cd01488    75 FgkiQDKDEEFYRQFNIIIC 94
E1_ThiF_like cd01487
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ...
 63-135 5.62e-04

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


Pssm-ID: 238764 [Multi-domain]  Cd Length: 174  Bit Score: 41.98  E-value: 5.62e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 150417996   63 HVFLSGMGGLGLEIAKNLVLAGIKAVTIHDTEKCQAWDLGTNFFLSEDdvVNkRNRAEAVLKHIAELNPYVHV 135
Cdd:cd01487     1 KVGIAGAGGLGSNIAVLLARSGVGNLKLVDFDVVEPSNLNRQQYFLSQ--IG-EPKVEALKENLREINPFVKI 70
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
 64-181 1.03e-03

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: 41.80  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996   64 VFLSGMGGLGLEIAKNLVLAGIKAVTIHDTEKCQAWDLGTNFFLSEDDVvnKRNRAEAVLKHIAELNPYVHVTS--SSVP 141
Cdd:cd01484     2 VLLVGAGGIGCELLKNLALMGFGQIHVIDMDTIDVSNLNRQFLFRPKDI--GRPKSEVAAEAVNDRNPNCKVVPyqNKVG 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 150417996  142 FNETTDLSFLDKYQCVVLTEMKLPLQKKINDFCRSQCPPI 181
Cdd:cd01484    80 PEQDFNDTFFEQFHIIVNALDNIIARRYVNGMLIFLIVPL 119
PRK08223 PRK08223
hypothetical protein; Validated
 456-595 1.26e-03

hypothetical protein; Validated


Pssm-ID: 181302 [Multi-domain]  Cd Length: 287  Bit Score: 41.98  E-value: 1.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996  456 QKLQNLNIFLVGCGAIGCEMLKNFALLGVGTskekgmITVTDPDLIEKSNLNRQFLFRPHHIQKPKSYTAADATLKINSQ 535
Cdd:PRK08223   23 QRLRNSRVAIAGLGGVGGIHLLTLARLGIGK------FTIADFDVFELRNFNRQAGAMMSTLGRPKAEVLAEMVRDINPE 96

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 150417996  536 IKIDAHLNKVcpTTETIynDEFYTKQDVIITALD--NVEARRYVDSRCLANLRPLLDSGTMG 595
Cdd:PRK08223   97 LEIRAFPEGI--GKENA--DAFLDGVDVYVDGLDffEFDARRLVFAACQQRGIPALTAAPLG 154
PRK15116 PRK15116
sulfur acceptor protein CsdL; Provisional
 36-136 4.75e-03

sulfur acceptor protein CsdL; Provisional


Pssm-ID: 185071  Cd Length: 268  Bit Score: 40.17  E-value: 4.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996   36 SVEIDDALysRQRY-----VLGDTAMQKMAKSHVFLSGMGGLGLEIAKNLVLAGIKAVTIHDTekcqawdlgtnfflseD 110
Cdd:PRK15116    2 SVVISDAW--RQRFggtarLYGEKALQLFADAHICVVGIGGVGSWAAEALARTGIGAITLIDM----------------D 63

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 150417996  111 DV-VNKRNR-------------AEAVLKHIAELNPYVHVT 136
Cdd:PRK15116   64 DVcVTNTNRqihalrdnvglakAEVMAERIRQINPECRVT 103
PRK14851 PRK14851
hypothetical protein; Provisional
 467-621 9.36e-03

hypothetical protein; Provisional


Pssm-ID: 184853 [Multi-domain]  Cd Length: 679  Bit Score: 39.84  E-value: 9.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996  467 GCGAIGCEMLKNFALLGVGTskekgmITVTDPDLIEKSNLNRQFLFRPHHIQKPKSYTAADATLKINSQIKIDAHlnkvc 546
Cdd:PRK14851   50 GMGGVGGVHLITMVRTGIGR------FHIADFDQFEPVNVNRQFGARVPSFGRPKLAVMKEQALSINPFLEITPF----- 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150417996  547 PTTETIYN-DEFYTKQDVIITALD--NVEARRYVDSRCLANLRPLLDSGTMGTKGHTEVIVPH---LTESYNSHRDPPEE 620
Cdd:PRK14851  119 PAGINADNmDAFLDGVDVVLDGLDffQFEIRRTLFNMAREKGIPVITAGPLGYSSAMLVFTPQgmgFDDYFNIGGKMPEE 198


                  .
gi 150417996  621 E 621
Cdd:PRK14851  199 Q 199
 
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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