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Conserved domains on  [gi|23510338|ref|NP_003325|]
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ubiquitin-like modifier-activating enzyme 1 [Homo sapiens]

Protein Classification

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ube1 super family cl36897
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 49-1055 0e+00

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


The actual alignment was detected with superfamily member TIGR01408:

Pssm-ID: 273603 [Multi-domain]  Cd Length: 1006  Bit Score: 1324.51  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338     49 DIDEGLYSRQLYVLGHEAMKRLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREEDIGKNRA 128
Cdd:TIGR01408    1 EIDEALYSRQLYVLGDEAMQKMAKSNVLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLSSNFFLSEDDVGRNRA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338    129 EVSQPRLAELNSYVPVTAYTGPLVEDFLSGFQVVVLTNTPLEDQLRVGEFCHNR--GIKLVVADTRGLFGQLFCDFGEEM 206
Cdd:TIGR01408   81 EAVVKKLAELNPYVHVSSSSVPFNEEFLDKFQCVVLTEMSLPLQKEINDFCHSQcpPIAFISADVRGLFGSLFCDFGDEF 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338    207 ILTDSNGEQPLSAMVSMVTKDNPGVVTCLDEARHGFESGDFVSFSEVQGMVELNGNQPMEIKVLGPYTFSICDTSNFSDY 286
Cdd:TIGR01408  161 EVLDTDGEEPKTGFIASITQANPGIVTCLENHRHKLETGDFVTFREVNGMTGLNDGSPRKITVISPYSFSIGDTTELGPY 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338    287 IRGGIVSQVKVPKKISFKSLVASLAEPDFVVTDFAKFSRPAQLHIGFQALHQFCAQHGRPPRPRNEEDAAELVALAQAVN 366
Cdd:TIGR01408  241 LHGGIATQVKTPKTVFFKSLREQLKDPKCLIVDFSKPERPPEIHTAFQALDQFQEKYSRKPNVGCQQDAEELLKLATSIS 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338    367 ARALPAVQqnNLDEDLIRKLAYVAAGDLAPINAFIGGLAAQEVMKACSGKFMPIMQWLYFDALECLPEDKEVLTEDkCLQ 446
Cdd:TIGR01408  321 ETLEEKVP--DVDAKLVHWLSWTAQGFLSPMAAAVGGVVSQEVLKAVTGKFSPLCQWFYFDSAESLPSLGKPECEE-FLP 397

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338    447 RQNRYDGQVAVFGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGCGEGGEIIVTDMDTIEKSNLNRQFLFRPWDVTK 526
Cdd:TIGR01408  398 RGDRYDAQIAVFGDTFQQKLQNLNIFLVGCGAIGCEMLKNFALMGVGTGKKGMITVTDPDLIEKSNLNRQFLFRPHHIGK 477

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338    527 LKSDTAAAAVRQMNPHIRVTSHQNRVGPDTERIYDDDFFQNLDGVANALDNVDARMYMDRRCVYYRKPLLESGTLGTKGN 606
Cdd:TIGR01408  478 PKSYTAADATLKINPQIKIDAHQNRVGPETETIFNDEFYEKLDVVINALDNVEARRYVDSRCLAFLKPLLESGTLGTKGN 557

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338    607 VQVVIPFLTESYSSSQDPPEKSIPICTLKNFPNAIEHTLQWARDEFEGLFKQPAENVNQYLTDP-KFVERTLRLAGTQPL 685
Cdd:TIGR01408  558 TQVVVPHLTESYGSSRDPPEKEIPFCTLKSFPAAIEHTIQWARDKFEGLFSHKPSLVNKYLSSPsSAEEVLQKIQSGHSR 637

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338    686 EVLEAVQRSLVLQRPQTWADCVTWACHHWHTQYSNNIRQLLHNFPPDQLTSSGAPFWSGPKRCPHPLTFDVNNPLHLDYV 765
Cdd:TIGR01408  638 EGLEQIIKLLSKEKPRNFSQCVEWARLKFEKYFNNKALQLLHCFPLDIRTSTGSPFWSSPKRPPSPLKFDLNEPLHLSFI 717

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338    766 MAAANLFAQTYGLTGSQ---DRAAVATFLQSVQVPEFTPKSGVKIHVSDQELQSANASVDDSR-LEELKATLPSPDKLPG 841
Cdd:TIGR01408  718 QAAAKLYATVYGIPFAEedlSADALLNILSEVKIPEFKPRSNKKIQTDETARKPDTAPIDDRNaIFQLEKAILSNEATKS 797

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338    842 -FKMYPIDFEKDDDSNFHMDFIVAASNLRAENYDIPSADRHKSKLIAGKIIPAIATTTAAVVGLVCLELYKVVQGHRQLD 920
Cdd:TIGR01408  798 dFRMAPLSFEKDDDHNGHIDFITAASNLRAKNYSIEPADRFKTKFIAGKIIPAIATSTATVSGLVCLELIKVTDGGYKFE 877

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338    921 SYKNGFLNLALPFFGFSEPLAAPRHQYYNQEW-TLWDRFEVQGlqpngeEMTLKQFLDYFKTEHKLEITMLSQGVSMLYS 999
Cdd:TIGR01408  878 VYKNCFLNLAIPLFVFTEPTEVRKTKIRNGISfTIWDRWTLHG------DFTLLEFINAVKEKYGLEPTMVSQGVKLLYV 951

                          970       980       990      1000      1010
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 23510338   1000 FFMPaaKLKERLDQPMTEIVSRVSKRKLGRHVRALVLELCCNDESGEDVEVPYVRY 1055
Cdd:TIGR01408  952 PVMP--GHAERLKLKMHKLVKPTTKKKLPPYRVHLTVSFACDDDGDEDVPGPPVRI 1005
 
Name Accession Description Interval E-value
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 49-1055 0e+00

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


Pssm-ID: 273603 [Multi-domain]  Cd Length: 1006  Bit Score: 1324.51  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338     49 DIDEGLYSRQLYVLGHEAMKRLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREEDIGKNRA 128
Cdd:TIGR01408    1 EIDEALYSRQLYVLGDEAMQKMAKSNVLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLSSNFFLSEDDVGRNRA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338    129 EVSQPRLAELNSYVPVTAYTGPLVEDFLSGFQVVVLTNTPLEDQLRVGEFCHNR--GIKLVVADTRGLFGQLFCDFGEEM 206
Cdd:TIGR01408   81 EAVVKKLAELNPYVHVSSSSVPFNEEFLDKFQCVVLTEMSLPLQKEINDFCHSQcpPIAFISADVRGLFGSLFCDFGDEF 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338    207 ILTDSNGEQPLSAMVSMVTKDNPGVVTCLDEARHGFESGDFVSFSEVQGMVELNGNQPMEIKVLGPYTFSICDTSNFSDY 286
Cdd:TIGR01408  161 EVLDTDGEEPKTGFIASITQANPGIVTCLENHRHKLETGDFVTFREVNGMTGLNDGSPRKITVISPYSFSIGDTTELGPY 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338    287 IRGGIVSQVKVPKKISFKSLVASLAEPDFVVTDFAKFSRPAQLHIGFQALHQFCAQHGRPPRPRNEEDAAELVALAQAVN 366
Cdd:TIGR01408  241 LHGGIATQVKTPKTVFFKSLREQLKDPKCLIVDFSKPERPPEIHTAFQALDQFQEKYSRKPNVGCQQDAEELLKLATSIS 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338    367 ARALPAVQqnNLDEDLIRKLAYVAAGDLAPINAFIGGLAAQEVMKACSGKFMPIMQWLYFDALECLPEDKEVLTEDkCLQ 446
Cdd:TIGR01408  321 ETLEEKVP--DVDAKLVHWLSWTAQGFLSPMAAAVGGVVSQEVLKAVTGKFSPLCQWFYFDSAESLPSLGKPECEE-FLP 397

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338    447 RQNRYDGQVAVFGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGCGEGGEIIVTDMDTIEKSNLNRQFLFRPWDVTK 526
Cdd:TIGR01408  398 RGDRYDAQIAVFGDTFQQKLQNLNIFLVGCGAIGCEMLKNFALMGVGTGKKGMITVTDPDLIEKSNLNRQFLFRPHHIGK 477

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338    527 LKSDTAAAAVRQMNPHIRVTSHQNRVGPDTERIYDDDFFQNLDGVANALDNVDARMYMDRRCVYYRKPLLESGTLGTKGN 606
Cdd:TIGR01408  478 PKSYTAADATLKINPQIKIDAHQNRVGPETETIFNDEFYEKLDVVINALDNVEARRYVDSRCLAFLKPLLESGTLGTKGN 557

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338    607 VQVVIPFLTESYSSSQDPPEKSIPICTLKNFPNAIEHTLQWARDEFEGLFKQPAENVNQYLTDP-KFVERTLRLAGTQPL 685
Cdd:TIGR01408  558 TQVVVPHLTESYGSSRDPPEKEIPFCTLKSFPAAIEHTIQWARDKFEGLFSHKPSLVNKYLSSPsSAEEVLQKIQSGHSR 637

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338    686 EVLEAVQRSLVLQRPQTWADCVTWACHHWHTQYSNNIRQLLHNFPPDQLTSSGAPFWSGPKRCPHPLTFDVNNPLHLDYV 765
Cdd:TIGR01408  638 EGLEQIIKLLSKEKPRNFSQCVEWARLKFEKYFNNKALQLLHCFPLDIRTSTGSPFWSSPKRPPSPLKFDLNEPLHLSFI 717

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338    766 MAAANLFAQTYGLTGSQ---DRAAVATFLQSVQVPEFTPKSGVKIHVSDQELQSANASVDDSR-LEELKATLPSPDKLPG 841
Cdd:TIGR01408  718 QAAAKLYATVYGIPFAEedlSADALLNILSEVKIPEFKPRSNKKIQTDETARKPDTAPIDDRNaIFQLEKAILSNEATKS 797

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338    842 -FKMYPIDFEKDDDSNFHMDFIVAASNLRAENYDIPSADRHKSKLIAGKIIPAIATTTAAVVGLVCLELYKVVQGHRQLD 920
Cdd:TIGR01408  798 dFRMAPLSFEKDDDHNGHIDFITAASNLRAKNYSIEPADRFKTKFIAGKIIPAIATSTATVSGLVCLELIKVTDGGYKFE 877

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338    921 SYKNGFLNLALPFFGFSEPLAAPRHQYYNQEW-TLWDRFEVQGlqpngeEMTLKQFLDYFKTEHKLEITMLSQGVSMLYS 999
Cdd:TIGR01408  878 VYKNCFLNLAIPLFVFTEPTEVRKTKIRNGISfTIWDRWTLHG------DFTLLEFINAVKEKYGLEPTMVSQGVKLLYV 951

                          970       980       990      1000      1010
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 23510338   1000 FFMPaaKLKERLDQPMTEIVSRVSKRKLGRHVRALVLELCCNDESGEDVEVPYVRY 1055
Cdd:TIGR01408  952 PVMP--GHAERLKLKMHKLVKPTTKKKLPPYRVHLTVSFACDDDGDEDVPGPPVRI 1005
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
 470-1011 0e+00

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


Pssm-ID: 238767 [Multi-domain]  Cd Length: 435  Bit Score: 884.32  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338  470 KYFLVGAGAIGCELLKNFAMIGLGCGEGGEIIVTDMDTIEKSNLNRQFLFRPWDVTKLKSDTAAAAVRQMNPHIRVTSHQ 549
Cdd:cd01490    1 KVFLVGAGAIGCELLKNFALMGVGTGESGEITVTDMDNIEKSNLNRQFLFRPHDVGKPKSEVAAAAVKAMNPDLKITALQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338  550 NRVGPDTERIYDDDFFQNLDGVANALDNVDARMYMDRRCVYYRKPLLESGTLGTKGNVQVVIPFLTESYSSSQDPPEKSI 629
Cdd:cd01490   81 NRVGPETEHIFNDEFWEKLDGVANALDNVDARMYVDRRCVYYRKPLLESGTLGTKGNTQVVIPHLTESYSSSRDPPEKSI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338  630 PICTLKNFPNAIEHTLQWARDEFEGLFKQPAENVNQYLtdpkfvertlrlagtqplevleavqrslvlqrpqtWADCVTW 709
Cdd:cd01490  161 PLCTLKNFPNAIEHTIQWARDEFEGLFKQPPENVNQYL-----------------------------------FEDCVRW 205

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338  710 ACHHWHTQYSNNIRQLLHNFPPDQLTSSGAPFWSGPKRCPHPLTFDVNNPLHLDYVMAAANLFAQTYGLTGsqdraavat 789
Cdd:cd01490  206 ARLLFEKYFNNNIKQLLHNFPPDAVTSDGAPFWSGPKRCPTPLEFDVNNPLHLDFVLAAANLYAEVYGIPG--------- 276

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338  790 flqsvqvpeftpksgvkihvsdqelqsanasvddsrleelkatlpspdklpgfkmypidFEKDDDSNFHMDFIVAASNLR 869
Cdd:cd01490  277 -----------------------------------------------------------FEKDDDTNFHMDFITAASNLR 297

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338  870 AENYDIPSADRHKSKLIAGKIIPAIATTTAAVVGLVCLELYKVVQGHRQLDSYKNGFLNLALPFFGFSEPLAAPRHQY-Y 948
Cdd:cd01490  298 ARNYSIPPADRHKTKRIAGKIIPAIATTTAAVTGLVCLELYKVVDGKRPLEAYKNAFLNLALPFFAFSEPIPAPKVKYaY 377

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23510338  949 NQEWTLWDRFEVQGLQPNGEEMTlkqflDYFKTEHKLEITMLSQGVSMLYSFFMPAAKLKERL 1011
Cdd:cd01490  378 DEEWTIWDRFEVKGKQTLQELLI-----DYFKEKYGLEVTMLSQGVSMLYSSFMPPAKLKERL 435
UBA_E1_SCCH pfam10585
Ubiquitin-activating enzyme, SCCH domain; Ubiquitin-activating enzyme (E1 enzyme) activates ...
 638-884 1.15e-149

Ubiquitin-activating enzyme, SCCH domain; Ubiquitin-activating enzyme (E1 enzyme) activates ubiquitin by first adenylating with ATP its C-terminal glycine residue and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding an ubiquitin-E1 thiolester and free AMP. Later the ubiquitin moiety is transferred to a cysteine residue on one of the many forms of ubiquitin-conjugating enzymes (E2). This domain carries the last of five conserved cysteines that is part of the active site of the enzyme, responsible for ubiquitin thiolester complex formation, the active site being represented by the sequence motif PICTLKNFP. The catalytic cysteine domain contains the E1 active site cysteine, and is divided in two half-domains, FCCH and SCCH, for 'first' and 'second' catalytic cysteine half-domain, respectively. This is the SCCH domain in which resides the catalytic cysteine.


Pssm-ID: 463157  Cd Length: 254  Bit Score: 445.52  E-value: 1.15e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338    638 PNAIEHTLQWARDEFEGLFKQPAENVNQYLTDP-KFVERTLRLAGTQPLEVLEAVQRSLVLQRPQTWADCVTWACHHWHT 716
Cdd:pfam10585    1 PNAIEHTIQWARDEFEGLFVQPPEEVNKYLQPPqNFIESLLKQGGGQKLETLESVRKSLVTERPKTFEDCVAWARLKFEK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338    717 QYSNNIRQLLHNFPPDQLTSSGAPFWSGPKRCPHPLTFDVNNPLHLDYVMAAANLFAQTYGLTGSQDRAAVATFLQSVQV 796
Cdd:pfam10585   81 LFNNDIKQLLYNFPPDHKTSSGAPFWSGPKRPPTPLEFDPNNPLHLDFVVAAANLRAQVYGIPGSRDREAIAKVLSKVKV 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338    797 PEFTPKSGVKIHVSDQELQSANASV--DDSRLEELKATLP----SPDKLPGFKMYPIDFEKDDDSNFHMDFIVAASNLRA 870
Cdd:pfam10585  161 PEFKPKSGVKIQVNDEEAADPNAESedDEDELDELLEELPklavSPSSLAGFRLNPIEFEKDDDTNFHIDFITAASNLRA 240

                          250
                   ....*....|....
gi 23510338    871 ENYDIPSADRHKSK 884
Cdd:pfam10585  241 RNYGIPPADRHKTK 254
UBA_e1_C smart00985
Ubiquitin-activating enzyme e1 C-terminal domain; This presumed domain found at the C terminus ...
 922-1053 4.00e-69

Ubiquitin-activating enzyme e1 C-terminal domain; This presumed domain found at the C terminus of Ubiquitin-activating enzyme e1 proteins is functionally uncharacterised.


Pssm-ID: 214955  Cd Length: 128  Bit Score: 226.37  E-value: 4.00e-69
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338     922 YKNGFLNLALPFFGFSEPLAAPRHQYYNQ-EWTLWDRFEVQGLqpngeEMTLKQFLDYFKTEHKLEITMLSQGVSMLYSF 1000
Cdd:smart00985    1 YKNAFLNLALPFFAFSEPIAAPKTKYRDKdKWTLWDRLEVPGG-----DITLKELLDYFEEKYGLEVTMLSQGVSLLYSS 75

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|...
gi 23510338    1001 FMPAAKLKERLDQPMTEIVSRVSKRKLGRHVRALVLELCCNDESGEDVEVPYV 1053
Cdd:smart00985   76 FMPPKKHKERLDLPVTELVEQVTKKKLPPHVKYLVLEVSCEDEDDEDVEVPYI 128
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 450-612 1.30e-33

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


Pssm-ID: 440244 [Multi-domain]  Cd Length: 244  Bit Score: 129.86  E-value: 1.30e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338  450 RYDGQVAV--FGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGcgeggEIIVTDMDTIEKSNLNRQFLFRPWDVTKL 527
Cdd:COG0476    7 RYSRQILLpeIGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVG-----TLTLVDDDVVELSNLQRQILYTEADVGRP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338  528 KSDTAAAAVRQMNPHIRVTSHQNRVGPDTEriydDDFFQNLDGVANALDNVDARMYMDRRCVYYRKPLLESGTLGTKGNV 607
Cdd:COG0476   82 KVEAAAERLRALNPDVEVEAIPERLTEENA----LELLAGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIGFEGQV 157


                 ....*
gi 23510338  608 QVVIP 612
Cdd:COG0476  158 TVFIP 162
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 450-595 6.66e-19

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 87.21  E-value: 6.66e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338   450 RYDGQVAV--FGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGcgeggEIIVTDMDTIEKSNLNRQFLFRPWDVTKL 527
Cdd:PRK05690   12 RYNRQIILrgFDFDGQEKLKAARVLVVGLGGLGCAASQYLAAAGVG-----TLTLVDFDTVSLSNLQRQVLHDDATIGQP 86

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23510338   528 KSDTAAAAVRQMNPHIRVTSHQNRVGPDTEriydDDFFQNLDGVANALDNVDARMYMDRRCVYYRKPL 595
Cdd:PRK05690   87 KVESARAALARINPHIAIETINARLDDDEL----AALIAGHDLVLDCTDNVATRNQLNRACFAAKKPL 150
 
Name Accession Description Interval E-value
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 49-1055 0e+00

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


Pssm-ID: 273603 [Multi-domain]  Cd Length: 1006  Bit Score: 1324.51  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338     49 DIDEGLYSRQLYVLGHEAMKRLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREEDIGKNRA 128
Cdd:TIGR01408    1 EIDEALYSRQLYVLGDEAMQKMAKSNVLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLSSNFFLSEDDVGRNRA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338    129 EVSQPRLAELNSYVPVTAYTGPLVEDFLSGFQVVVLTNTPLEDQLRVGEFCHNR--GIKLVVADTRGLFGQLFCDFGEEM 206
Cdd:TIGR01408   81 EAVVKKLAELNPYVHVSSSSVPFNEEFLDKFQCVVLTEMSLPLQKEINDFCHSQcpPIAFISADVRGLFGSLFCDFGDEF 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338    207 ILTDSNGEQPLSAMVSMVTKDNPGVVTCLDEARHGFESGDFVSFSEVQGMVELNGNQPMEIKVLGPYTFSICDTSNFSDY 286
Cdd:TIGR01408  161 EVLDTDGEEPKTGFIASITQANPGIVTCLENHRHKLETGDFVTFREVNGMTGLNDGSPRKITVISPYSFSIGDTTELGPY 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338    287 IRGGIVSQVKVPKKISFKSLVASLAEPDFVVTDFAKFSRPAQLHIGFQALHQFCAQHGRPPRPRNEEDAAELVALAQAVN 366
Cdd:TIGR01408  241 LHGGIATQVKTPKTVFFKSLREQLKDPKCLIVDFSKPERPPEIHTAFQALDQFQEKYSRKPNVGCQQDAEELLKLATSIS 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338    367 ARALPAVQqnNLDEDLIRKLAYVAAGDLAPINAFIGGLAAQEVMKACSGKFMPIMQWLYFDALECLPEDKEVLTEDkCLQ 446
Cdd:TIGR01408  321 ETLEEKVP--DVDAKLVHWLSWTAQGFLSPMAAAVGGVVSQEVLKAVTGKFSPLCQWFYFDSAESLPSLGKPECEE-FLP 397

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338    447 RQNRYDGQVAVFGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGCGEGGEIIVTDMDTIEKSNLNRQFLFRPWDVTK 526
Cdd:TIGR01408  398 RGDRYDAQIAVFGDTFQQKLQNLNIFLVGCGAIGCEMLKNFALMGVGTGKKGMITVTDPDLIEKSNLNRQFLFRPHHIGK 477

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338    527 LKSDTAAAAVRQMNPHIRVTSHQNRVGPDTERIYDDDFFQNLDGVANALDNVDARMYMDRRCVYYRKPLLESGTLGTKGN 606
Cdd:TIGR01408  478 PKSYTAADATLKINPQIKIDAHQNRVGPETETIFNDEFYEKLDVVINALDNVEARRYVDSRCLAFLKPLLESGTLGTKGN 557

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338    607 VQVVIPFLTESYSSSQDPPEKSIPICTLKNFPNAIEHTLQWARDEFEGLFKQPAENVNQYLTDP-KFVERTLRLAGTQPL 685
Cdd:TIGR01408  558 TQVVVPHLTESYGSSRDPPEKEIPFCTLKSFPAAIEHTIQWARDKFEGLFSHKPSLVNKYLSSPsSAEEVLQKIQSGHSR 637

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338    686 EVLEAVQRSLVLQRPQTWADCVTWACHHWHTQYSNNIRQLLHNFPPDQLTSSGAPFWSGPKRCPHPLTFDVNNPLHLDYV 765
Cdd:TIGR01408  638 EGLEQIIKLLSKEKPRNFSQCVEWARLKFEKYFNNKALQLLHCFPLDIRTSTGSPFWSSPKRPPSPLKFDLNEPLHLSFI 717

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338    766 MAAANLFAQTYGLTGSQ---DRAAVATFLQSVQVPEFTPKSGVKIHVSDQELQSANASVDDSR-LEELKATLPSPDKLPG 841
Cdd:TIGR01408  718 QAAAKLYATVYGIPFAEedlSADALLNILSEVKIPEFKPRSNKKIQTDETARKPDTAPIDDRNaIFQLEKAILSNEATKS 797

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338    842 -FKMYPIDFEKDDDSNFHMDFIVAASNLRAENYDIPSADRHKSKLIAGKIIPAIATTTAAVVGLVCLELYKVVQGHRQLD 920
Cdd:TIGR01408  798 dFRMAPLSFEKDDDHNGHIDFITAASNLRAKNYSIEPADRFKTKFIAGKIIPAIATSTATVSGLVCLELIKVTDGGYKFE 877

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338    921 SYKNGFLNLALPFFGFSEPLAAPRHQYYNQEW-TLWDRFEVQGlqpngeEMTLKQFLDYFKTEHKLEITMLSQGVSMLYS 999
Cdd:TIGR01408  878 VYKNCFLNLAIPLFVFTEPTEVRKTKIRNGISfTIWDRWTLHG------DFTLLEFINAVKEKYGLEPTMVSQGVKLLYV 951

                          970       980       990      1000      1010
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 23510338   1000 FFMPaaKLKERLDQPMTEIVSRVSKRKLGRHVRALVLELCCNDESGEDVEVPYVRY 1055
Cdd:TIGR01408  952 PVMP--GHAERLKLKMHKLVKPTTKKKLPPYRVHLTVSFACDDDGDEDVPGPPVRI 1005
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
 470-1011 0e+00

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


Pssm-ID: 238767 [Multi-domain]  Cd Length: 435  Bit Score: 884.32  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338  470 KYFLVGAGAIGCELLKNFAMIGLGCGEGGEIIVTDMDTIEKSNLNRQFLFRPWDVTKLKSDTAAAAVRQMNPHIRVTSHQ 549
Cdd:cd01490    1 KVFLVGAGAIGCELLKNFALMGVGTGESGEITVTDMDNIEKSNLNRQFLFRPHDVGKPKSEVAAAAVKAMNPDLKITALQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338  550 NRVGPDTERIYDDDFFQNLDGVANALDNVDARMYMDRRCVYYRKPLLESGTLGTKGNVQVVIPFLTESYSSSQDPPEKSI 629
Cdd:cd01490   81 NRVGPETEHIFNDEFWEKLDGVANALDNVDARMYVDRRCVYYRKPLLESGTLGTKGNTQVVIPHLTESYSSSRDPPEKSI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338  630 PICTLKNFPNAIEHTLQWARDEFEGLFKQPAENVNQYLtdpkfvertlrlagtqplevleavqrslvlqrpqtWADCVTW 709
Cdd:cd01490  161 PLCTLKNFPNAIEHTIQWARDEFEGLFKQPPENVNQYL-----------------------------------FEDCVRW 205

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338  710 ACHHWHTQYSNNIRQLLHNFPPDQLTSSGAPFWSGPKRCPHPLTFDVNNPLHLDYVMAAANLFAQTYGLTGsqdraavat 789
Cdd:cd01490  206 ARLLFEKYFNNNIKQLLHNFPPDAVTSDGAPFWSGPKRCPTPLEFDVNNPLHLDFVLAAANLYAEVYGIPG--------- 276

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338  790 flqsvqvpeftpksgvkihvsdqelqsanasvddsrleelkatlpspdklpgfkmypidFEKDDDSNFHMDFIVAASNLR 869
Cdd:cd01490  277 -----------------------------------------------------------FEKDDDTNFHMDFITAASNLR 297

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338  870 AENYDIPSADRHKSKLIAGKIIPAIATTTAAVVGLVCLELYKVVQGHRQLDSYKNGFLNLALPFFGFSEPLAAPRHQY-Y 948
Cdd:cd01490  298 ARNYSIPPADRHKTKRIAGKIIPAIATTTAAVTGLVCLELYKVVDGKRPLEAYKNAFLNLALPFFAFSEPIPAPKVKYaY 377

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23510338  949 NQEWTLWDRFEVQGLQPNGEEMTlkqflDYFKTEHKLEITMLSQGVSMLYSFFMPAAKLKERL 1011
Cdd:cd01490  378 DEEWTIWDRFEVKGKQTLQELLI-----DYFKEKYGLEVTMLSQGVSMLYSSFMPPAKLKERL 435
Ube1_repeat1 cd01491
Ubiquitin activating enzyme (E1), repeat 1. E1, a highly conserved small protein present ...
 54-436 3.10e-180

Ubiquitin activating enzyme (E1), repeat 1. E1, a highly conserved small protein present universally in eukaryotic cells, is part of cascade to attach ubiquitin (Ub) covalently to substrate proteins. This cascade consists of activating (E1), conjugating (E2), and/or ligating (E3) enzymes and then targets them for degradation by the 26S proteasome. E1 activates ubiquitin by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and ubiquitin's C-terminus. E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. Ubiquitin-E1 is a single-chain protein with a weakly conserved two-fold repeat. This CD represents the first repeat of Ub-E1.


Pssm-ID: 238768 [Multi-domain]  Cd Length: 286  Bit Score: 526.07  E-value: 3.10e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338   54 LYSRQLYVLGHEAMKRLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREEDIGKNRAEVSQP 133
Cdd:cd01491    1 LYSRQLYVLGHEAMKKLQKSNVLISGLGGLGVEIAKNLILAGVKSVTLHDTKPCSWSDLSSQFYLREEDIGKNRAEASQA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338  134 RLAELNSYVPVTAYTGPLVEDFLSGFQVVVLTNTPLEDQLRVGEFCHNRGIKLVVADTRGLFGQLFCDFGEEMILTDSNG 213
Cdd:cd01491   81 RLAELNPYVPVTVSTGPLTTDELLKFQVVVLTDASLEDQLKINEFCHSPGIKFISADTRGLFGSIFCDFGDEFTVYDPNG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338  214 EQPLSAMVSMVTKDNPGVVTCLDEARHGFESGDFVSFSEVQGMVELNGNQPMEIKVLGPYTFSICDTSNFSDYIRGGIVS 293
Cdd:cd01491  161 EEPKSGMISSISKDNPGVVTCLDETRHGFEDGDYVTFSEVEGMTELNGCEPRKIKVKGPYTFSIGDTSSFSEYIRGGIVT 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338  294 QVKvpkkisfkslvaslaepdfvvtdfakfsrpaqlhigfqalhqfcaqhgrpprprneedaaelvalaqavnaralpav 373
Cdd:cd01491  241 QVK----------------------------------------------------------------------------- 243

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23510338  374 qqnnldedlirklayvaagdLAPINAFIGGLAAQEVMKACSGKFMPIMQWLYFDALECLPEDK 436
Cdd:cd01491  244 --------------------LSPMAAFFGGLAAQEVLKACSGKFTPLKQWLYFDALECLPEDE 286
UBA_E1_SCCH pfam10585
Ubiquitin-activating enzyme, SCCH domain; Ubiquitin-activating enzyme (E1 enzyme) activates ...
 638-884 1.15e-149

Ubiquitin-activating enzyme, SCCH domain; Ubiquitin-activating enzyme (E1 enzyme) activates ubiquitin by first adenylating with ATP its C-terminal glycine residue and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding an ubiquitin-E1 thiolester and free AMP. Later the ubiquitin moiety is transferred to a cysteine residue on one of the many forms of ubiquitin-conjugating enzymes (E2). This domain carries the last of five conserved cysteines that is part of the active site of the enzyme, responsible for ubiquitin thiolester complex formation, the active site being represented by the sequence motif PICTLKNFP. The catalytic cysteine domain contains the E1 active site cysteine, and is divided in two half-domains, FCCH and SCCH, for 'first' and 'second' catalytic cysteine half-domain, respectively. This is the SCCH domain in which resides the catalytic cysteine.


Pssm-ID: 463157  Cd Length: 254  Bit Score: 445.52  E-value: 1.15e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338    638 PNAIEHTLQWARDEFEGLFKQPAENVNQYLTDP-KFVERTLRLAGTQPLEVLEAVQRSLVLQRPQTWADCVTWACHHWHT 716
Cdd:pfam10585    1 PNAIEHTIQWARDEFEGLFVQPPEEVNKYLQPPqNFIESLLKQGGGQKLETLESVRKSLVTERPKTFEDCVAWARLKFEK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338    717 QYSNNIRQLLHNFPPDQLTSSGAPFWSGPKRCPHPLTFDVNNPLHLDYVMAAANLFAQTYGLTGSQDRAAVATFLQSVQV 796
Cdd:pfam10585   81 LFNNDIKQLLYNFPPDHKTSSGAPFWSGPKRPPTPLEFDPNNPLHLDFVVAAANLRAQVYGIPGSRDREAIAKVLSKVKV 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338    797 PEFTPKSGVKIHVSDQELQSANASV--DDSRLEELKATLP----SPDKLPGFKMYPIDFEKDDDSNFHMDFIVAASNLRA 870
Cdd:pfam10585  161 PEFKPKSGVKIQVNDEEAADPNAESedDEDELDELLEELPklavSPSSLAGFRLNPIEFEKDDDTNFHIDFITAASNLRA 240

                          250
                   ....*....|....
gi 23510338    871 ENYDIPSADRHKSK 884
Cdd:pfam10585  241 RNYGIPPADRHKTK 254
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
 470-653 5.64e-79

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


Pssm-ID: 238761 [Multi-domain]  Cd Length: 234  Bit Score: 257.89  E-value: 5.64e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338  470 KYFLVGAGAIGCELLKNFAMIGLGcgeggEIIVTDMDTIEKSNLNRQFLFRPWDVTKLKSDTAAAAVRQMNPHIRVTSHQ 549
Cdd:cd01484    1 KVLLVGAGGIGCELLKNLALMGFG-----QIHVIDMDTIDVSNLNRQFLFRPKDIGRPKSEVAAEAVNDRNPNCKVVPYQ 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338  550 NRVGPdtERIYDDDFFQNLDGVANALDNVDARMYMDRRCVYYRKPLLESGTLGTKGNVQVVIPFLTESYSSSQDPPEKSI 629
Cdd:cd01484   76 NKVGP--EQDFNDTFFEQFHIIVNALDNIIARRYVNGMLIFLIVPLIESGTEGFKGNAQVILPGMTECIECTLYPPQKNF 153

                        170       180
                 ....*....|....*....|....
gi 23510338  630 PICTLKNFPNAIEHTLQWARDEFE 653
Cdd:cd01484  154 PMCTIASMPRLPEHCIEWARMLQW 177
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 451-637 2.35e-69

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


Pssm-ID: 459987 [Multi-domain]  Cd Length: 238  Bit Score: 231.38  E-value: 2.35e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338    451 YDGQVA--VFGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGcgeggEIIVTDMDTIEKSNLNRQFLFRPWDVTKLK 528
Cdd:pfam00899    1 YSRQLAlpLIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVG-----KITLVDFDTVELSNLNRQFLFREADIGKPK 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338    529 SDTAAAAVRQMNPHIRVTSHQNRVGPDTeriyDDDFFQNLDGVANALDNVDARMYMDRRCVYYRKPLLESGTLGTKGNVQ 608
Cdd:pfam00899   76 AEVAAERLREINPDVEVEAYTERLTPEN----AEELIKSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVT 151

                          170       180       190
                   ....*....|....*....|....*....|.
gi 23510338    609 VVIPFLTESYS--SSQDPPEKSIPICTLKNF 637
Cdd:pfam00899  152 VVIPGKTPCYRclFPEDPPPKLVPSCTVAGV 182
UBA_e1_C smart00985
Ubiquitin-activating enzyme e1 C-terminal domain; This presumed domain found at the C terminus ...
 922-1053 4.00e-69

Ubiquitin-activating enzyme e1 C-terminal domain; This presumed domain found at the C terminus of Ubiquitin-activating enzyme e1 proteins is functionally uncharacterised.


Pssm-ID: 214955  Cd Length: 128  Bit Score: 226.37  E-value: 4.00e-69
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338     922 YKNGFLNLALPFFGFSEPLAAPRHQYYNQ-EWTLWDRFEVQGLqpngeEMTLKQFLDYFKTEHKLEITMLSQGVSMLYSF 1000
Cdd:smart00985    1 YKNAFLNLALPFFAFSEPIAAPKTKYRDKdKWTLWDRLEVPGG-----DITLKELLDYFEEKYGLEVTMLSQGVSLLYSS 75

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|...
gi 23510338    1001 FMPAAKLKERLDQPMTEIVSRVSKRKLGRHVRALVLELCCNDESGEDVEVPYV 1053
Cdd:smart00985   76 FMPPKKHKERLDLPVTELVEQVTKKKLPPHVKYLVLEVSCEDEDDEDVEVPYI 128
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 470-929 4.64e-58

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


Pssm-ID: 238766 [Multi-domain]  Cd Length: 312  Bit Score: 202.61  E-value: 4.64e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338  470 KYFLVGAGAIGCELLKNFAMIGLGcgeggEIIVTDMDTIEKSNLNRQFLFRPWDVTKLKSDTAAAAVRQMNPHIRVTSHQ 549
Cdd:cd01489    1 KVLVVGAGGIGCELLKNLVLTGFG-----EIHIIDLDTIDLSNLNRQFLFRKKHVGKSKAQVAKEAVLSFNPNVKIVAYH 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338  550 NRVgpdTERIYDDDFFQNLDGVANALDNVDARMYMDRRCVYYRKPLLESGTLGTKGNVQVVIPFLTESYSSSQDPPEKSI 629
Cdd:cd01489   76 ANI---KDPDFNVEFFKQFDLVFNALDNLAARRHVNKMCLAADVPLIESGTTGFLGQVQVIKKGKTECYECQPKETPKTF 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338  630 PICTLKNFPNAIEHTLQWARDE---FEGLFKQpaenvnqyltdpkfvertlrlagtqplevleavqrslvlqrpqtwadc 706
Cdd:cd01489  153 PVCTIRSTPSQPIHCIVWAKSLfflFNKVFKD------------------------------------------------ 184

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338  707 vtwachhwhtqysnNIRQLLHNfppDQLtssgapfWSGPKRcPHPLTFDvnnplhldyvmaaanlfaqtygltgsqdraa 786
Cdd:cd01489  185 --------------DIERLLSM---EEL-------WKTRKP-PVPLSWK------------------------------- 208

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338  787 vatflqsvqvpeftpksgvkihvsdqelqsanasvddsrleelkatlpspdklpgfkmyPIDFEKDDDSNfhMDFIVAAS 866
Cdd:cd01489  209 -----------------------------------------------------------ELTFDKDDQDA--LDFVAAAA 227

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23510338  867 NLRAENYDIPSADRHKSKLIAGKIIPAIATTTAAVVGLVCLELYKVVQGHrqLDSYKNGFLNL 929
Cdd:cd01489  228 NLRSHVFGIPMKSRFDIKQMAGNIIPAIATTNAIIAGLIVLEALKVLSGD--KEQCRTVFLNL 288
E1_UFD pfam09358
Ubiquitin fold domain; The ubiquitin fold domain is found at the C-terminus of ...
 955-1053 4.28e-50

Ubiquitin fold domain; The ubiquitin fold domain is found at the C-terminus of ubiquitin-activating E1 family enzymes. This domain binds to E2 enzymes.


Pssm-ID: 462768  Cd Length: 93  Bit Score: 171.57  E-value: 4.28e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338    955 WDRFEVQGlqpngeEMTLKQFLDYFKTEHKLEITMLSQGVSMLYSFFMPAAKLKERLDQPMTEIVSRVSKRKLGRHVRAL 1034
Cdd:pfam09358    1 WDRFEVEG------DMTLQELLDYFKEKYGLEVTMLSYGVSLLYSSFMPPKKHKERLPMKISELVEEVSKKPIPPHQKYL 74

                           90
                   ....*....|....*....
gi 23510338   1035 VLELCCNDESGEDVEVPYV 1053
Cdd:pfam09358   75 VLEVSCEDEDGEDVEVPYV 93
E1-1_like cd01485
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ...
 54-217 7.61e-47

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


Pssm-ID: 238762 [Multi-domain]  Cd Length: 198  Bit Score: 166.44  E-value: 7.61e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338   54 LYSRQLYVLGHEAMKRLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREE--DIGKNRAEVS 131
Cdd:cd01485    1 LYDRQIRLWGDEAQNKLRSAKVLIIGAGALGAEIAKNLVLAGIDSITIVDHRLVSTEDLGSNFFLDAEvsNSGMNRAAAS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338  132 QPRLAELNSYVPVTAYTGP------LVEDFLSGFQVVVLTNTPLEDQLRVGEFCHNRGIKLVVADTRGLFGQLFCDF--- 202
Cdd:cd01485   81 YEFLQELNPNVKLSIVEEDslsndsNIEEYLQKFTLVIATEENYERTAKVNDVCRKHHIPFISCATYGLIGYAFFDFpia 160

                        170       180
                 ....*....|....*....|..
gi 23510338  203 -------GEEMILTDSNGEQPL 217
Cdd:cd01485  161 aflggvvAQEAIKSISGKFTPL 182
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 55-199 5.11e-44

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


Pssm-ID: 459987 [Multi-domain]  Cd Length: 238  Bit Score: 159.73  E-value: 5.11e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338     55 YSRQLY--VLGHEAMKRLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREEDIGKNRAEVSQ 132
Cdd:pfam00899    1 YSRQLAlpLIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAA 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23510338    133 PRLAELNSYVPVTAYTGPL----VEDFLSGFQVVVLTNTPLEDQLRVGEFCHNRGIKLVVADTRGLFGQLF 199
Cdd:pfam00899   81 ERLREINPDVEVEAYTERLtpenAEELIKSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVT 151
E1_FCCH pfam16190
Ubiquitin-activating enzyme E1 FCCH domain; This domain is found in the ubiquitin-activating ...
 227-296 5.88e-43

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


Pssm-ID: 465054 [Multi-domain]  Cd Length: 70  Bit Score: 150.33  E-value: 5.88e-43
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338    227 DNPGVVTCLDEARHGFESGDFVSFSEVQGMVELNGNQPMEIKVLGPYTFSICDTSNFSDYIRGGIVSQVK 296
Cdd:pfam16190    1 DNPGVVTCLDDTRHGLEDGDYVTFSEVEGMTELNGCEPRKIKVLGPYTFSIGDTSSFSPYLRGGIVTQVK 70
Aos1_SUMO cd01492
Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating ...
 54-201 1.30e-42

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


Pssm-ID: 238769 [Multi-domain]  Cd Length: 197  Bit Score: 153.99  E-value: 1.30e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338   54 LYSRQLYVLGHEAMKRLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREEDIGKNRAEVSQP 133
Cdd:cd01492    3 LYDRQIRLWGLEAQKRLRSARILLIGLKGLGAEIAKNLVLSGIGSLTILDDRTVTEEDLGAQFLIPAEDLGQNRAEASLE 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23510338  134 RLAELNSYVPVTAYTGPLVE---DFLSGFQVVVLTNTPLEDQLRVGEFCHNRGIKLVVADTRGLFGQLFCD 201
Cdd:cd01492   83 RLRALNPRVKVSVDTDDISEkpeEFFSQFDVVVATELSRAELVKINELCRKLGVKFYATGVHGLFGFVFAD 153
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 470-649 1.32e-40

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


Pssm-ID: 238765 [Multi-domain]  Cd Length: 291  Bit Score: 151.74  E-value: 1.32e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338  470 KYFLVGAGAIGCELLKNFAMIGLGcgeggEIIVTDMDTIEKSNLNRQFLFRPWDVTKLKSDTAAAAVRQMNPHIRVTSHQ 549
Cdd:cd01488    1 KILVIGAGGLGCELLKNLALSGFR-----NIHVIDMDTIDVSNLNRQFLFREKDIGKPKAEVAAKFVNDRVPGVNVTPHF 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338  550 NRVgpdteRIYDDDFFQNLDGVANALDNVDARMYMDRRCVY--------YRKPLLESGTLGTKGNVQVVIPFLTESYSSS 621
Cdd:cd01488   76 GKI-----QDKDEEFYRQFNIIICGLDSIEARRWINGTLVSlllyedpeSIIPLIDGGTEGFKGHARVILPGITACIECS 150

                        170       180       190
                 ....*....|....*....|....*....|
gi 23510338  622 QD--PPEKSIPICTLKNFPNAIEHTLQWAR 649
Cdd:cd01488  151 LDlfPPQVTFPLCTIANTPRLPEHCIEYAS 180
E1_4HB pfam16191
Ubiquitin-activating enzyme E1 four-helix bundle; This domain is found in the ...
 297-366 3.92e-38

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


Pssm-ID: 465055  Cd Length: 70  Bit Score: 136.43  E-value: 3.92e-38
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338    297 VPKKISFKSLVASLAEPDFVVTDFAKFSRPAQLHIGFQALHQFCAQHGRPPRPRNEEDAAELVALAQAVN 366
Cdd:pfam16191    1 MPKTLSFKSLEESLKEPEFLISDFAKFDRPAQLHLAFQALHAFQEKHGRLPRPWNEEDAEEVVKLAKELN 70
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 450-632 1.06e-34

ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis family. The common reaction mechanism catalyzed by MoeB and ThiF, like other E1 enzymes, begins with a nucleophilic attack of the C-terminal carboxylate of MoaD and ThiS, respectively, on the alpha-phosphate of an ATP molecule bound at the active site of the activating enzymes, leading to the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of MoaD and ThiS. MoeB, as the MPT synthase (MoaE/MoaD complex) sulfurase, is involved in the biosynthesis of the molybdenum cofactor, a derivative of the tricyclic pterin, molybdopterin (MPT). ThiF catalyzes the adenylation of ThiS, as part of the biosynthesis pathway of thiamin pyrophosphate (vitamin B1).


Pssm-ID: 238386 [Multi-domain]  Cd Length: 228  Bit Score: 132.60  E-value: 1.06e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338  450 RYDGQVAV--FGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGcgeggEIIVTDMDTIEKSNLNRQFLFRPWDVTKL 527
Cdd:cd00757    1 RYSRQILLpeIGEEGQEKLKNARVLVVGAGGLGSPAAEYLAAAGVG-----KLGLVDDDVVELSNLQRQILHTEADVGQP 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338  528 KSDTAAAAVRQMNPHIRVTSHQNRVGPDTEriydDDFFQNLDGVANALDNVDARMYMDRRCVYYRKPLLESGTLGTKGNV 607
Cdd:cd00757   76 KAEAAAERLRAINPDVEIEAYNERLDAENA----EELIAGYDLVLDCTDNFATRYLINDACVKLGKPLVSGAVLGFEGQV 151

                        170       180
                 ....*....|....*....|....*.
gi 23510338  608 QVVIPFLTESYSSS-QDPPEKSIPIC 632
Cdd:cd00757  152 TVFIPGEGPCYRCLfPEPPPPGVPSC 177
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 450-612 1.30e-33

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


Pssm-ID: 440244 [Multi-domain]  Cd Length: 244  Bit Score: 129.86  E-value: 1.30e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338  450 RYDGQVAV--FGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGcgeggEIIVTDMDTIEKSNLNRQFLFRPWDVTKL 527
Cdd:COG0476    7 RYSRQILLpeIGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVG-----TLTLVDDDVVELSNLQRQILYTEADVGRP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338  528 KSDTAAAAVRQMNPHIRVTSHQNRVGPDTEriydDDFFQNLDGVANALDNVDARMYMDRRCVYYRKPLLESGTLGTKGNV 607
Cdd:COG0476   82 KVEAAAERLRALNPDVEVEAIPERLTEENA----LELLAGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIGFEGQV 157


                 ....*
gi 23510338  608 QVVIP 612
Cdd:COG0476  158 TVFIP 162
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 472-611 9.76e-32

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


Pssm-ID: 238760 [Multi-domain]  Cd Length: 143  Bit Score: 120.84  E-value: 9.76e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338  472 FLVGAGAIGCELLKNFAMIGLGcgeggEIIVTDMDTIEKSNLNRQFLFRPWDVTKLKSDTAAAAVRQMNPHIRVTSHQNR 551
Cdd:cd01483    3 LLVGLGGLGSEIALNLARSGVG-----KITLIDFDTVELSNLNRQFLARQADIGKPKAEVAARRLNELNPGVNVTAVPEG 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338  552 VGPDTeriyDDDFFQNLDGVANALDNVDARMYMDRRCVYYRKPLLESGTLGTKGNVQVVI 611
Cdd:cd01483   78 ISEDN----LDDFLDGVDLVIDAIDNIAVRRALNRACKELGIPVIDAGGLGLGGDIQVID 133
APPBP1_RUB cd01493
Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric ...
 55-428 2.29e-23

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


Pssm-ID: 238770 [Multi-domain]  Cd Length: 425  Bit Score: 104.31  E-value: 2.29e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338   55 YSRQLYVLGHEAMKRLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREEDIGKNRAEVSQPR 134
Cdd:cd01493    3 YDRQLRLWGEHGQAALESAHVCLLNATATGTEILKNLVLPGIGSFTIVDGSKVDEEDLGNNFFLDASSLGKSRAEATCEL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338  135 LAELNSYVPVTAYTGPLVE------DFLSGFQVVVLTNTPLEDQLRVGEFCHNRGIKLVVADTRGLFGQLFCDFGEEMIl 208
Cdd:cd01493   83 LQELNPDVNGSAVEESPEAlldndpSFFSQFTVVIATNLPESTLLRLADVLWSANIPLLYVRSYGLYGYIRIQLKEHTI- 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338  209 TDSNGEQPLSAMvsmvTKDNPgvvtcldearhgfesgdfvsFSEVQGMVE---LNGNQPME----------IKVL----- 270
Cdd:cd01493  162 VESHPDNALEDL----RLDNP--------------------FPELREHADsidLDDMDPAEhshtpyivilIKYLekwrs 217

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338  271 ---GPYTFSICDTSNFSDYIRGGIVSQvkvPKKISFKSLVASlaepdfVVTDFAKFSRPAQLHIGFQ------------- 334
Cdd:cd01493  218 ahnGQLPSTYKEKKEFRDLVRSLMRSN---EDEENFEEAIKA------VNKALNRTKIPSSVEEIFNddrcenltsqsss 288

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338  335 ------ALHQFCA-QHGRPP----------------------RPRNEEDAAELVALAQAV-NARALPAvqqNNLDEDLI- 383
Cdd:cd01493  289 fwimarALKEFVAeENGLLPlpgtlpdmtadtekyiklqniyREKAEKDAAEVEKYVREIlKSLGRSP---DSISDKEIk 365

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 23510338  384 ---RKLAYVAA----GDLAPINAFIGGLAAQEVMKACSGKFMPIMQWLYFDA 428
Cdd:cd01493  366 lfcKNAAFLRVirgrSLEHNISAFMGGIAAQEVIKLITKQYVPIDNTFIFDG 417
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 75-198 3.14e-21

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


Pssm-ID: 238760 [Multi-domain]  Cd Length: 143  Bit Score: 90.79  E-value: 3.14e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338   75 VLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREEDIGKNRAEVSQPRLAELNSYVPVTAYT----GP 150
Cdd:cd01483    2 VLLVGLGGLGSEIALNLARSGVGKITLIDFDTVELSNLNRQFLARQADIGKPKAEVAARRLNELNPGVNVTAVPegisED 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 23510338  151 LVEDFLSGFQVVVLTNTPLEDQLRVGEFCHNRGIKLVVADTRGLFGQL 198
Cdd:cd01483   82 NLDDFLDGVDLVIDAIDNIAVRRALNRACKELGIPVIDAGGLGLGGDI 129
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 450-595 6.66e-19

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 87.21  E-value: 6.66e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338   450 RYDGQVAV--FGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGcgeggEIIVTDMDTIEKSNLNRQFLFRPWDVTKL 527
Cdd:PRK05690   12 RYNRQIILrgFDFDGQEKLKAARVLVVGLGGLGCAASQYLAAAGVG-----TLTLVDFDTVSLSNLQRQVLHDDATIGQP 86

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23510338   528 KSDTAAAAVRQMNPHIRVTSHQNRVGPDTEriydDDFFQNLDGVANALDNVDARMYMDRRCVYYRKPL 595
Cdd:PRK05690   87 KVESARAALARINPHIAIETINARLDDDEL----AALIAGHDLVLDCTDNVATRNQLNRACFAAKKPL 150
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
459-612 1.75e-16

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 82.75  E-value: 1.75e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338   459 GSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGcgeggEIIVTDMDTIEKSNLNRQFLFRPWDVTKLKSDTAAAAVRQ 538
Cdd:PRK08762  126 GEEGQRRLLEARVLLIGAGGLGSPAALYLAAAGVG-----TLGIVDHDVVDRSNLQRQILHTEDRVGQPKVDSAAQRLAA 200

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23510338   539 MNPHIRVTSHQNRVGPDTEriydDDFFQNLDGVANALDNVDARMYMDRRCVYYRKPLLESGTLGTKGNVQVVIP 612
Cdd:PRK08762  201 LNPDVQVEAVQERVTSDNV----EALLQDVDVVVDGADNFPTRYLLNDACVKLGKPLVYGAVFRFEGQVSVFDA 270
PRK08328 PRK08328
hypothetical protein; Provisional
 55-198 3.32e-16

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 79.07  E-value: 3.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338    55 YSRQLYVLGHEAMKRLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREEDIGKNRAEVSQP- 133
Cdd:PRK08328   10 YDRQIMIFGVEGQEKLKKAKVAVVGVGGLGSPVAYYLAAAGVGRILLIDEQTPELSNLNRQILHWEEDLGKNPKPLSAKw 89

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23510338   134 RLAELNSYVPVTAYTGPL----VEDFLSGFQVVVLTNTPLEDQLRVGEFCHNRGIKLVVADTRGLFGQL 198
Cdd:PRK08328   90 KLERFNSDIKIETFVGRLseenIDEVLKGVDVIVDCLDNFETRYLLDDYAHKKGIPLVHGAVEGTYGQV 158
PRK08328 PRK08328
hypothetical protein; Provisional
 450-617 2.29e-15

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 76.76  E-value: 2.29e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338   450 RYDGQVAVFGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLgcgegGEIIVTDMDTIEKSNLNRQFLFRPWDVTK-LK 528
Cdd:PRK08328    9 RYDRQIMIFGVEGQEKLKKAKVAVVGVGGLGSPVAYYLAAAGV-----GRILLIDEQTPELSNLNRQILHWEEDLGKnPK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338   529 SDTAAAAVRQMNPHIRVTSHQNRVgpDTERIydDDFFQNLDGVANALDNVDARMYMDRRCVYYRKPLLESGTLGTKGNVQ 608
Cdd:PRK08328   84 PLSAKWKLERFNSDIKIETFVGRL--SEENI--DEVLKGVDVIVDCLDNFETRYLLDDYAHKKGIPLVHGAVEGTYGQVT 159


                  ....*....
gi 23510338   609 VVIPFLTES 617
Cdd:PRK08328  160 TIVPGKTKR 168
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 55-224 4.06e-15

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


Pssm-ID: 440244 [Multi-domain]  Cd Length: 244  Bit Score: 76.32  E-value: 4.06e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338   55 YSRQ--LYVLGHEAMKRLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREEDIGKNRAEVSQ 132
Cdd:COG0476    8 YSRQilLPEIGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADVGRPKVEAAA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338  133 PRLAELNSYVPVTAYTGPL----VEDFLSGFQVVV--LTNtpLEDQLRVGEFCHNRGIKLVVADTRGLFGQLF------- 199
Cdd:COG0476   88 ERLRALNPDVEVEAIPERLteenALELLAGADLVLdcTDN--FATRYLLNDACVKLGIPLVSGAVIGFEGQVTvfipgdt 165

                        170       180       190
                 ....*....|....*....|....*....|
gi 23510338  200 ----CDFGEEMILTDSNGEQP-LSAMVSMV 224
Cdd:COG0476  166 pcyrCLFPEPPEPGPSCAEAGvLGPLVGVI 195
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 440-581 5.31e-15

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 78.00  E-value: 5.31e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338   440 TEDKCLQRQNRYDGqvavFGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGcgeggEIIVTDMDTIEKSNLNRQFLF 519
Cdd:PRK05600   17 SELRRTARQLALPG----FGIEQQERLHNARVLVIGAGGLGCPAMQSLASAGVG-----TITLIDDDTVDVSNIHRQILF 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23510338   520 RPWDVTKLKSDTAAAAVRQMNPHIRVTSHQNRVGPDTERiyddDFFQNLDGVANALDNVDAR 581
Cdd:PRK05600   88 GASDVGRPKVEVAAERLKEIQPDIRVNALRERLTAENAV----ELLNGVDLVLDGSDSFATK 145
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 55-198 1.64e-14

ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis family. The common reaction mechanism catalyzed by MoeB and ThiF, like other E1 enzymes, begins with a nucleophilic attack of the C-terminal carboxylate of MoaD and ThiS, respectively, on the alpha-phosphate of an ATP molecule bound at the active site of the activating enzymes, leading to the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of MoaD and ThiS. MoeB, as the MPT synthase (MoaE/MoaD complex) sulfurase, is involved in the biosynthesis of the molybdenum cofactor, a derivative of the tricyclic pterin, molybdopterin (MPT). ThiF catalyzes the adenylation of ThiS, as part of the biosynthesis pathway of thiamin pyrophosphate (vitamin B1).


Pssm-ID: 238386 [Multi-domain]  Cd Length: 228  Bit Score: 74.05  E-value: 1.64e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338   55 YSRQLYV--LGHEAMKRLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREEDIGKNRAEVSQ 132
Cdd:cd00757    2 YSRQILLpeIGEEGQEKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRQILHTEADVGQPKAEAAA 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23510338  133 PRLAELNSYVPVTAY----TGPLVEDFLSGFQVVV--LTNtpLEDQLRVGEFCHNRGIKLVVADTRGLFGQL 198
Cdd:cd00757   82 ERLRAINPDVEIEAYnerlDAENAEELIAGYDLVLdcTDN--FATRYLINDACVKLGKPLVSGAVLGFEGQV 151
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 449-612 7.26e-14

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 74.26  E-value: 7.26e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338   449 NRYDGQV--AVFGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGcgeggEIIVTDMDTIEKSNLNRQFLFRPWDVTK 526
Cdd:PRK07688    3 ERYSRQElfSPIGEEGQQKLREKHVLIIGAGALGTANAEMLVRAGVG-----KVTIVDRDYVEWSNLQRQQLYTESDVKN 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338   527 LKSDTAAAAVR--QMNPHIRVTSHQNRVGPdtERIydDDFFQNLDGVANALDNVDARMYMDRRCVYYRKPLLESGTLGTK 604
Cdd:PRK07688   78 NLPKAVAAKKRleEINSDVRVEAIVQDVTA--EEL--EELVTGVDLIIDATDNFETRFIVNDAAQKYGIPWIYGACVGSY 153


                  ....*...
gi 23510338   605 GNVQVVIP 612
Cdd:PRK07688  154 GLSYTIIP 161
Aos1_SUMO cd01492
Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating ...
 451-605 1.95e-12

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


Pssm-ID: 238769 [Multi-domain]  Cd Length: 197  Bit Score: 67.32  E-value: 1.95e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338  451 YDGQVAVFGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLgcgegGEIIVTDMDTIEKSNLNRQFLFRPWDVTKLKSD 530
Cdd:cd01492    4 YDRQIRLWGLEAQKRLRSARILLIGLKGLGAEIAKNLVLSGI-----GSLTILDDRTVTEEDLGAQFLIPAEDLGQNRAE 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23510338  531 TAAAAVRQMNPHIRVTShqnrvgpDTERI--YDDDFFQNLDGV-ANALDNvDARMYMDRRCVYYRKPLLESGTLGTKG 605
Cdd:cd01492   79 ASLERLRALNPRVKVSV-------DTDDIseKPEEFFSQFDVVvATELSR-AELVKINELCRKLGVKFYATGVHGLFG 148
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
 458-604 4.21e-12

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


Pssm-ID: 238384 [Multi-domain]  Cd Length: 231  Bit Score: 66.86  E-value: 4.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338  458 FGSDLQEKLGKQKYFLVGAGAIGcellkNFAMIGL---GCGEggeIIVTDMDTIEKSNLNRQFLFRPWDVTKLKSDTAAA 534
Cdd:cd00755    1 YGEEGLEKLRNAHVAVVGLGGVG-----SWAAEALarsGVGK---LTLIDFDVVCVSNLNRQIHALLSTVGKPKVEVMAE 72

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338  535 AVRQMNPHIRVTSHQNRVGPDTEriyDDDFFQNLDGVANALDNVDARMYMDRRCVYYRKPLLESGTLGTK 604
Cdd:cd00755   73 RIRDINPECEVDAVEEFLTPDNS---EDLLGGDPDFVVDAIDSIRAKVALIAYCRKRKIPVISSMGAGGK 139
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 459-594 5.25e-12

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 68.97  E-value: 5.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338   459 GSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGcgeggEIIVTDMDTIEKSNLNRQFLFRPWDVTKLKSDTAAAAVRQ 538
Cdd:PRK07878   33 GVDGQKRLKNARVLVIGAGGLGSPTLLYLAAAGVG-----TLGIVEFDVVDESNLQRQVIHGQSDVGRSKAQSARDSIVE 107

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 23510338   539 MNPHIRVTSHQNRVGPDTERiyddDFFQNLDGVANALDNVDARMYMDRRCVYYRKP 594
Cdd:PRK07878  108 INPLVNVRLHEFRLDPSNAV----ELFSQYDLILDGTDNFATRYLVNDAAVLAGKP 159
TcdA COG1179
tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ...
 473-599 1.70e-11

tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and biogenesis]; tRNA A37 threonylcarbamoyladenosine dehydratase is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440792  Cd Length: 247  Bit Score: 65.49  E-value: 1.70e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338  473 LVGAGAIgcELLKN--FAMIGLG-----CGEG------GEIIVTDMDTIEKSNLNRQF--LfrpwDVT--KLKSDTAAAA 535
Cdd:COG1179   13 LYGEEGL--ERLANahVAVVGLGgvgswAAEAlarsgvGRLTLVDLDDVCESNINRQLhaL----DSTvgRPKVEVMAER 86

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23510338  536 VRQMNPHIRVTSHQNRVGPDTeriYDDDFFQNLDGVANALDNVDARMYMDRRCVYYRKPLLESG 599
Cdd:COG1179   87 IRDINPDCEVTAIDEFVTPEN---ADELLSEDYDYVIDAIDSVSAKAALIAWCRRRGIPIISSM 147
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 450-581 4.97e-11

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 65.66  E-value: 4.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338   450 RYDGQVAV--FGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGcgeggEIIVTDMDTIEKSNLNRQFLFRPWDVTKL 527
Cdd:PRK05597    8 RYRRQIMLgeIGQQGQQSLFDAKVAVIGAGGLGSPALLYLAGAGVG-----HITIIDDDTVDLSNLHRQVIHSTAGVGQP 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 23510338   528 KSDTAAAAVRQMNPHIRVTSHQNRVGPDTERiyddDFFQNLDGVANALDNVDAR 581
Cdd:PRK05597   83 KAESAREAMLALNPDVKVTVSVRRLTWSNAL----DELRDADVILDGSDNFDTR 132
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
451-580 9.17e-11

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 62.57  E-value: 9.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338   451 YDGQVAVFGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGcgeggEIIVTDMDTIEKSNLNRQFLFrPWDVTKLKSD 530
Cdd:PRK08644   11 EAMLASRHTPKLLEKLKKAKVGIAGAGGLGSNIAVALARSGVG-----NLKLVDFDVVEPSNLNRQQYF-ISQIGMPKVE 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 23510338   531 TAAAAVRQMNPHIRVTSHQNRVgpDTERIydDDFFQNLDGVANALDNVDA 580
Cdd:PRK08644   85 ALKENLLEINPFVEIEAHNEKI--DEDNI--EELFKDCDIVVEAFDNAET 130
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 74-164 1.65e-10

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


Pssm-ID: 238765 [Multi-domain]  Cd Length: 291  Bit Score: 63.14  E-value: 1.65e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338   74 SVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREEDIGKNRAEVSQPRLAELNSYVPVTAYTGPLV- 152
Cdd:cd01488    1 KILVIGAGGLGCELLKNLALSGFRNIHVIDMDTIDVSNLNRQFLFREKDIGKPKAEVAAKFVNDRVPGVNVTPHFGKIQd 80

                         90
                 ....*....|....
gi 23510338  153 --EDFLSGFQVVVL 164
Cdd:cd01488   81 kdEEFYRQFNIIIC 94
E1-1_like cd01485
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ...
 451-545 2.05e-10

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


Pssm-ID: 238762 [Multi-domain]  Cd Length: 198  Bit Score: 61.28  E-value: 2.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338  451 YDGQVAVFGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLgcgegGEIIVTDMDTIEKSNLNRQFLFRPWDVT--KLK 528
Cdd:cd01485    2 YDRQIRLWGDEAQNKLRSAKVLIIGAGALGAEIAKNLVLAGI-----DSITIVDHRLVSTEDLGSNFFLDAEVSNsgMNR 76

                         90
                 ....*....|....*..
gi 23510338  529 SDTAAAAVRQMNPHIRV 545
Cdd:cd01485   77 AAASYEFLQELNPNVKL 93
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 448-638 2.70e-10

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 63.21  E-value: 2.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338   448 QNRYDGQVAV--FGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGcgeggEIIVTDMDTIEKSNLNRQFLFRPWDVT 525
Cdd:PRK12475    2 QERYSRQILFsgIGEEGQRKIREKHVLIVGAGALGAANAEALVRAGIG-----KLTIADRDYVEWSNLQRQQLYTEEDAK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338   526 KLKSDTAAAA--VRQMNPHIRVTSHQNRVGPDTERiyddDFFQNLDGVANALDNVDARMYMDRRCVYYRKPLLESGTLGT 603
Cdd:PRK12475   77 QKKPKAIAAKehLRKINSEVEIVPVVTDVTVEELE----ELVKEVDLIIDATDNFDTRLLINDLSQKYNIPWIYGGCVGS 152

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 23510338   604 KGNVQVVIPFLTESYSssqdppeksipiCTLKNFP 638
Cdd:PRK12475  153 YGVTYTIIPGKTPCLR------------CLMEHVP 175
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 75-198 1.17e-08

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


Pssm-ID: 238766 [Multi-domain]  Cd Length: 312  Bit Score: 57.77  E-value: 1.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338   75 VLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREEDIGKNRAEVSQPRLAELNSYVPVTAYTGPLVE- 153
Cdd:cd01489    2 VLVVGAGGIGCELLKNLVLTGFGEIHIIDLDTIDLSNLNRQFLFRKKHVGKSKAQVAKEAVLSFNPNVKIVAYHANIKDp 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 23510338  154 ----DFLSGFQVVV--LTNtpLEDQLRVGEFCHNRGIKLVVADTRGLFGQL 198
Cdd:cd01489   82 dfnvEFFKQFDLVFnaLDN--LAARRHVNKMCLAADVPLIESGTTGFLGQV 130
E1_ThiF_like cd01487
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ...
 473-581 4.13e-08

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


Pssm-ID: 238764 [Multi-domain]  Cd Length: 174  Bit Score: 53.92  E-value: 4.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338  473 LVGAGAIGCELLKNFAMIGLGcgeggEIIVTDMDTIEKSNLNRQFlFRPWDVTKLKSDTAAAAVRQMNPHIRVTSHQNRV 552
Cdd:cd01487    4 IAGAGGLGSNIAVLLARSGVG-----NLKLVDFDVVEPSNLNRQQ-YFLSQIGEPKVEALKENLREINPFVKIEAINIKI 77

                         90       100
                 ....*....|....*....|....*....
gi 23510338  553 gpDTERIYddDFFQNLDGVANALDNVDAR 581
Cdd:cd01487   78 --DENNLE--GLFGDCDIVVEAFDNAETK 102
PTZ00245 PTZ00245
ubiquitin activating enzyme; Provisional
 55-171 1.89e-07

ubiquitin activating enzyme; Provisional


Pssm-ID: 140272  Cd Length: 287  Bit Score: 53.91  E-value: 1.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338    55 YSRQLYVLGHEAMKRLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQfYLREEDIGKNRAEVSQPR 134
Cdd:PTZ00245    9 YDRQIRLWGKSTQQQLMHTSVALHGVAGAAAEAAKNLVLAGVRAVAVADEGLVTDADVCTN-YLMQGEAGGTRGARALGA 87

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 23510338   135 LAELNSYvpVTAYTGPLVEDFLSGFQVVVLTNTPLED 171
Cdd:PTZ00245   88 LQRLNPH--VSVYDAVTKLDGSSGTRVTMAAVITEED 122
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
459-594 2.81e-07

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 53.97  E-value: 2.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338   459 GSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGcgeggEIIVTDMDTIEKSNLNRQFLFRPWDVTKLKSDTAAAAVRQ 538
Cdd:PRK07411   29 GLEGQKRLKAASVLCIGTGGLGSPLLLYLAAAGIG-----RIGIVDFDVVDSSNLQRQVIHGTSWVGKPKIESAKNRILE 103

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 23510338   539 MNPHIRVTSHQNRVGPDTERiyddDFFQNLDGVANALDNVDARMYMDRRCVYYRKP 594
Cdd:PRK07411  104 INPYCQVDLYETRLSSENAL----DILAPYDVVVDGTDNFPTRYLVNDACVLLNKP 155
PRK15116 PRK15116
sulfur acceptor protein CsdL; Provisional
 450-602 5.10e-07

sulfur acceptor protein CsdL; Provisional


Pssm-ID: 185071  Cd Length: 268  Bit Score: 52.50  E-value: 5.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338   450 RYDGQVAVFGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGCgeggeIIVTDMDTIEKSNLNRQFLFRPWDVTKLKS 529
Cdd:PRK15116   12 RFGGTARLYGEKALQLFADAHICVVGIGGVGSWAAEALARTGIGA-----ITLIDMDDVCVTNTNRQIHALRDNVGLAKA 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23510338   530 DTAAAAVRQMNPHIRVTSHQNRVGPDTERIYDDdffQNLDGVANALDNVDARMYMDRRCVYYRKPLLESGTLG 602
Cdd:PRK15116   87 EVMAERIRQINPECRVTVVDDFITPDNVAEYMS---AGFSYVIDAIDSVRPKAALIAYCRRNKIPLVTTGGAG 156
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
 74-149 8.20e-07

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


Pssm-ID: 238761 [Multi-domain]  Cd Length: 234  Bit Score: 51.43  E-value: 8.20e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23510338   74 SVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREEDIGKNRAEVSQPRLAELNSYVPVTAYTG 149
Cdd:cd01484    1 KVLLVGAGGIGCELLKNLALMGFGQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKSEVAAEAVNDRNPNCKVVPYQN 76
Ube1_repeat1 cd01491
Ubiquitin activating enzyme (E1), repeat 1. E1, a highly conserved small protein present ...
 451-550 1.52e-06

Ubiquitin activating enzyme (E1), repeat 1. E1, a highly conserved small protein present universally in eukaryotic cells, is part of cascade to attach ubiquitin (Ub) covalently to substrate proteins. This cascade consists of activating (E1), conjugating (E2), and/or ligating (E3) enzymes and then targets them for degradation by the 26S proteasome. E1 activates ubiquitin by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and ubiquitin's C-terminus. E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. Ubiquitin-E1 is a single-chain protein with a weakly conserved two-fold repeat. This CD represents the first repeat of Ub-E1.


Pssm-ID: 238768 [Multi-domain]  Cd Length: 286  Bit Score: 51.11  E-value: 1.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338  451 YDGQVAVFGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGcgeggEIIVTDMDTIEKSNLNRQFLFRPWDVTKLKSD 530
Cdd:cd01491    2 YSRQLYVLGHEAMKKLQKSNVLISGLGGLGVEIAKNLILAGVK-----SVTLHDTKPCSWSDLSSQFYLREEDIGKNRAE 76

                         90       100
                 ....*....|....*....|
gi 23510338  531 TAAAAVRQMNPHIRVTSHQN 550
Cdd:cd01491   77 ASQARLAELNPYVPVTVSTG 96
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 55-154 2.39e-06

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 50.76  E-value: 2.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338    55 YSRQLYV--LGHEAMKRLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREEDIGKN--RAEV 130
Cdd:PRK07688    5 YSRQELFspIGEEGQQKLREKHVLIIGAGALGTANAEMLVRAGVGKVTIVDRDYVEWSNLQRQQLYTESDVKNNlpKAVA 84

                          90       100
                  ....*....|....*....|....
gi 23510338   131 SQPRLAELNSYVPVTAytgpLVED 154
Cdd:PRK07688   85 AKKRLEEINSDVRVEA----IVQD 104
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 55-163 2.41e-06

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 50.23  E-value: 2.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338    55 YSRQ--LYVLGHEAMKRLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREEDIGKNRAEVSQ 132
Cdd:PRK05690   13 YNRQiiLRGFDFDGQEKLKAARVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVSLSNLQRQVLHDDATIGQPKVESAR 92

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 23510338   133 PRLAELNSYVPVTAYTGPLVEDFL----SGFQVVV 163
Cdd:PRK05690   93 AALARINPHIAIETINARLDDDELaaliAGHDLVL 127
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 56-148 8.37e-06

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 49.49  E-value: 8.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338    56 SRQLYV--LGHEAMKRLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREEDIGKNRAEVSQP 133
Cdd:PRK05600   23 ARQLALpgFGIEQQERLHNARVLVIGAGGLGCPAMQSLASAGVGTITLIDDDTVDVSNIHRQILFGASDVGRPKVEVAAE 102

                          90
                  ....*....|....*
gi 23510338   134 RLAELNSYVPVTAYT 148
Cdd:PRK05600  103 RLKEIQPDIRVNALR 117
APPBP1_RUB cd01493
Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric ...
 450-565 9.00e-06

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


Pssm-ID: 238770 [Multi-domain]  Cd Length: 425  Bit Score: 49.23  E-value: 9.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338  450 RYDGQVAVFGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLgcgegGEIIVTDMDTIEKSNLNRQFLFRPWDVTKLKS 529
Cdd:cd01493    2 KYDRQLRLWGEHGQAALESAHVCLLNATATGTEILKNLVLPGI-----GSFTIVDGSKVDEEDLGNNFFLDASSLGKSRA 76

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 23510338  530 DTAAAAVRQMNPHirVTSHQNRVGPDTERIYDDDFF 565
Cdd:cd01493   77 EATCELLQELNPD--VNGSAVEESPEALLDNDPSFF 110
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 894-949 1.12e-05

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


Pssm-ID: 459987 [Multi-domain]  Cd Length: 238  Bit Score: 48.02  E-value: 1.12e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 23510338    894 IATTTAAVVGLVCLELYKVVQGHRqLDSYKNGFLNLALPFFGFSEPLAAPRHQYYN 949
Cdd:pfam00899  183 LGPTTAVVAGLQALEALKLLLGKG-EPNLAGRLLQFDALTMTFRELRLALKNPNCP 237
PRK08223 PRK08223
hypothetical protein; Validated
 463-612 2.46e-05

hypothetical protein; Validated


Pssm-ID: 181302 [Multi-domain]  Cd Length: 287  Bit Score: 47.37  E-value: 2.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338   463 QEKLGKQKYFLVGAGAIGCELLKNFAMIGLGCgeggeIIVTDMDTIEKSNLNRQF------LFRPwdvtklKSDTAAAAV 536
Cdd:PRK08223   22 QQRLRNSRVAIAGLGGVGGIHLLTLARLGIGK-----FTIADFDVFELRNFNRQAgammstLGRP------KAEVLAEMV 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338   537 RQMNPHIRVTSHQNRVGPDTEriydDDFfqnLDGVANALDNVDARMYMDRRCVY---YRK--PLLESGTLGTKGNVQVVI 611
Cdd:PRK08223   91 RDINPELEIRAFPEGIGKENA----DAF---LDGVDVYVDGLDFFEFDARRLVFaacQQRgiPALTAAPLGMGTALLVFD 163


                  .
gi 23510338   612 P 612
Cdd:PRK08223  164 P 164
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 55-147 4.80e-05

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 46.65  E-value: 4.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338    55 YSRQLYV--LGHEAMKRLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREEDIG--KNRAEV 130
Cdd:PRK12475    5 YSRQILFsgIGEEGQRKIREKHVLIVGAGALGAANAEALVRAGIGKLTIADRDYVEWSNLQRQQLYTEEDAKqkKPKAIA 84

                          90
                  ....*....|....*..
gi 23510338   131 SQPRLAELNSYVPVTAY 147
Cdd:PRK12475   85 AKEHLRKINSEVEIVPV 101
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
55-163 9.04e-05

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 46.16  E-value: 9.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338    55 YSRQLYV--LGHEAMKRLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREEDIGKNRAEVSQ 132
Cdd:PRK08762  116 YSRHLRLpeVGEEGQRRLLEARVLLIGAGGLGSPAALYLAAAGVGTLGIVDHDVVDRSNLQRQILHTEDRVGQPKVDSAA 195

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 23510338   133 PRLAELNSYVPVTAY----TGPLVEDFLSGFQVVV 163
Cdd:PRK08762  196 QRLAALNPDVQVEAVqervTSDNVEALLQDVDVVV 230
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
 74-163 1.09e-04

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


Pssm-ID: 238767 [Multi-domain]  Cd Length: 435  Bit Score: 46.13  E-value: 1.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338   74 SVLVSGLRGLGVEIAKNIILGGVKA-----VTLHDQGTAQWADLSSQFYLREEDIGKNRAEVSQPRLAELNSYVPVTAYT 148
Cdd:cd01490    1 KVFLVGAGAIGCELLKNFALMGVGTgesgeITVTDMDNIEKSNLNRQFLFRPHDVGKPKSEVAAAAVKAMNPDLKITALQ 80

                         90       100
                 ....*....|....*....|...
gi 23510338  149 ---GPLVE-----DFLSGFQVVV 163
Cdd:cd01490   81 nrvGPETEhifndEFWEKLDGVA 103
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
49-163 3.70e-04

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 42.92  E-value: 3.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338    49 DIDEGLYSRqlyvLGHEAMKRLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYlREEDIGKNRA 128
Cdd:PRK08644    9 EFEAMLASR----HTPKLLEKLKKAKVGIAGAGGLGSNIAVALARSGVGNLKLVDFDVVEPSNLNRQQY-FISQIGMPKV 83

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 23510338   129 EVSQPRLAELNSYVPVTAY----TGPLVEDFLSGFQVVV 163
Cdd:PRK08644   84 EALKENLLEINPFVEIEAHnekiDEDNIEELFKDCDIVV 122
PRK14851 PRK14851
hypothetical protein; Provisional
 455-612 5.07e-04

hypothetical protein; Provisional


Pssm-ID: 184853 [Multi-domain]  Cd Length: 679  Bit Score: 44.08  E-value: 5.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338   455 VAVFGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGcgeggEIIVTDMDTIEKSNLNRQFLFRPWDVTKLKSDTAAA 534
Cdd:PRK14851   30 IGLFTPGEQERLAEAKVAIPGMGGVGGVHLITMVRTGIG-----RFHIADFDQFEPVNVNRQFGARVPSFGRPKLAVMKE 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338   535 AVRQMNPHIRVTshqnrvgPDTERIYDDDFFQNLDGVANALDNVDARMYMDRRCVYYRK-----PLLESGTLGTKGNVQV 609
Cdd:PRK14851  105 QALSINPFLEIT-------PFPAGINADNMDAFLDGVDVVLDGLDFFQFEIRRTLFNMArekgiPVITAGPLGYSSAMLV 177


                  ...
gi 23510338   610 VIP 612
Cdd:PRK14851  178 FTP 180
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 55-144 5.71e-04

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 43.54  E-value: 5.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338    55 YSRQLYV--LGHEAMKRLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREEDIGKNRAEVSQ 132
Cdd:PRK07878   23 YSRHLIIpdVGVDGQKRLKNARVLVIGAGGLGSPTLLYLAAAGVGTLGIVEFDVVDESNLQRQVIHGQSDVGRSKAQSAR 102

                          90
                  ....*....|..
gi 23510338   133 PRLAELNSYVPV 144
Cdd:PRK07878  103 DSIVEINPLVNV 114
E1_ThiF_like cd01487
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ...
 74-146 1.10e-03

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


Pssm-ID: 238764 [Multi-domain]  Cd Length: 174  Bit Score: 41.21  E-value: 1.10e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23510338   74 SVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYlREEDIGKNRAEVSQPRLAELNSYVPVTA 146
Cdd:cd01487    1 KVGIAGAGGLGSNIAVLLARSGVGNLKLVDFDVVEPSNLNRQQY-FLSQIGEPKVEALKENLREINPFVKIEA 72
Apg7 cd01486
Apg7 is an E1-like protein, that activates two different ubiquitin-like proteins, Apg12 and ...
 470-548 1.28e-03

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


Pssm-ID: 238763 [Multi-domain]  Cd Length: 307  Bit Score: 41.98  E-value: 1.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338  470 KYFLVGAGAIGCellkNFAMIGLGCGEgGEIIVTDMDTIEKSNLNRQFLFRPWDVT--KLKSDTAAAAVRQMNPHIRVTS 547
Cdd:cd01486    1 KCLLLGAGTLGC----NVARNLLGWGV-RHITFVDSGKVSYSNPVRQSLFTFEDCKggKPKAEAAAERLKEIFPSIDATG 75


                 .
gi 23510338  548 H 548
Cdd:cd01486   76 I 76
PRK14852 PRK14852
hypothetical protein; Provisional
 463-612 7.05e-03

hypothetical protein; Provisional


Pssm-ID: 184854 [Multi-domain]  Cd Length: 989  Bit Score: 40.45  E-value: 7.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510338   463 QEKLGKQKYFLVGAGAIGCELLKNFAMIGLGcgeggEIIVTDMDTIEKSNLNRQFLFRPWDVTKLKSDTAAAAVRQMNPH 542
Cdd:PRK14852  327 QRRLLRSRVAIAGLGGVGGIHLMTLARTGIG-----NFNLADFDAYSPVNLNRQYGASIASFGRGKLDVMTERALSVNPF 401

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23510338   543 IRVTSHQNRVGPDTeriyDDDFFQNLDGVANALD--NVDARMYMDRRCVYYRKPLLESGTLGTKGNVQVVIP 612
Cdd:PRK14852  402 LDIRSFPEGVAAET----IDAFLKDVDLLVDGIDffALDIRRRLFNRALELGIPVITAGPLGYSCALLVFMP 469
PRK07877 PRK07877
Rv1355c family protein;
122-195 7.41e-03

Rv1355c family protein;


Pssm-ID: 236122 [Multi-domain]  Cd Length: 722  Bit Score: 40.36  E-value: 7.41e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23510338   122 DIGKNRAEVSQPRLAELNSYVPVTAYTGPL----VEDFLSGFQVVVLTNTPLEDQLRVGEFCHNRGIKLVVA-DTRGLF 195
Cdd:PRK07877  156 DLGVNKAVVAARRIAELDPYLPVEVFTDGLtednVDAFLDGLDVVVEECDSLDVKVLLREAARARRIPVLMAtSDRGLL 234
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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