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Conserved domains on  [gi|2217394013|ref|XP_047298379|]
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ubiquitin-like modifier-activating enzyme 1 isoform X5 [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 ...
 55-1061 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: 1324.90  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013   55 DIDEGLYSRQLYVLGHEAMKRLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREEDIGKNRA 134
Cdd:TIGR01408    1 EIDEALYSRQLYVLGDEAMQKMAKSNVLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLSSNFFLSEDDVGRNRA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  135 EVSQPRLAELNSYVPVTAYTGPLVEDFLSGFQVVVLTNTPLEDQLRVGEFCHNR--GIKLVVADTRGLFGQLFCDFGEEM 212
Cdd:TIGR01408   81 EAVVKKLAELNPYVHVSSSSVPFNEEFLDKFQCVVLTEMSLPLQKEINDFCHSQcpPIAFISADVRGLFGSLFCDFGDEF 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  213 ILTDSNGEQPLSAMVSMVTKDNPGVVTCLDEARHGFESGDFVSFSEVQGMVELNGNQPMEIKVLGPYTFSICDTSNFSDY 292
Cdd:TIGR01408  161 EVLDTDGEEPKTGFIASITQANPGIVTCLENHRHKLETGDFVTFREVNGMTGLNDGSPRKITVISPYSFSIGDTTELGPY 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  293 IRGGIVSQVKVPKKISFKSLVASLAEPDFVVTDFAKFSRPAQLHIGFQALHQFCAQHGRPPRPRNEEDAAELVALAQAVN 372
Cdd:TIGR01408  241 LHGGIATQVKTPKTVFFKSLREQLKDPKCLIVDFSKPERPPEIHTAFQALDQFQEKYSRKPNVGCQQDAEELLKLATSIS 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  373 ARALPAVQqnNLDEDLIRKLAYVAAGDLAPINAFIGGLAAQEVMKACSGKFMPIMQWLYFDALECLPEDKEVLTEDkCLQ 452
Cdd:TIGR01408  321 ETLEEKVP--DVDAKLVHWLSWTAQGFLSPMAAAVGGVVSQEVLKAVTGKFSPLCQWFYFDSAESLPSLGKPECEE-FLP 397

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  453 RQNRYDGQVAVFGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGCGEGGEIIVTDMDTIEKSNLNRQFLFRPWDVTK 532
Cdd:TIGR01408  398 RGDRYDAQIAVFGDTFQQKLQNLNIFLVGCGAIGCEMLKNFALMGVGTGKKGMITVTDPDLIEKSNLNRQFLFRPHHIGK 477

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  533 LKSDTAAAAVRQMNPHIRVTSHQNRVGPDTERIYDDDFFQNLDGVANALDNVDARMYMDRRCVYYRKPLLESGTLGTKGN 612
Cdd:TIGR01408  478 PKSYTAADATLKINPQIKIDAHQNRVGPETETIFNDEFYEKLDVVINALDNVEARRYVDSRCLAFLKPLLESGTLGTKGN 557

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  613 VQVVIPFLTESYSSSQDPPEKSIPICTLKNFPNAIEHTLQWARDEFEGLFKQPAENVNQYLTDP-KFVERTLRLAGTQPL 691
Cdd:TIGR01408  558 TQVVVPHLTESYGSSRDPPEKEIPFCTLKSFPAAIEHTIQWARDKFEGLFSHKPSLVNKYLSSPsSAEEVLQKIQSGHSR 637

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  692 EVLEAVQRSLVLQRPQTWADCVTWACHHWHTQYSNNIRQLLHNFPPDQLTSSGAPFWSGPKRCPHPLTFDVNNPLHLDYV 771
Cdd:TIGR01408  638 EGLEQIIKLLSKEKPRNFSQCVEWARLKFEKYFNNKALQLLHCFPLDIRTSTGSPFWSSPKRPPSPLKFDLNEPLHLSFI 717

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  772 MAAANLFAQTYGLTGSQ---DRAAVATFLQSVQVPEFTPKSGVKIHVSDQELQSANASVDDSR-LEELKATLPSPDKLPG 847
Cdd:TIGR01408  718 QAAAKLYATVYGIPFAEedlSADALLNILSEVKIPEFKPRSNKKIQTDETARKPDTAPIDDRNaIFQLEKAILSNEATKS 797

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  848 -FKMYPIDFEKDDDSNFHMDFIVAASNLRAENYDIPSADRHKSKLIAGKIIPAIATTTAAVVGLVCLELYKVVQGHRQLD 926
Cdd:TIGR01408  798 dFRMAPLSFEKDDDHNGHIDFITAASNLRAKNYSIEPADRFKTKFIAGKIIPAIATSTATVSGLVCLELIKVTDGGYKFE 877

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  927 SYKNGFLNLALPFFGFSEPLAAPRHQYYNQEW-TLWDRFEVQGlqpngeEMTLKQFLDYFKTEHKLEITMLSQGVSMLYS 1005
Cdd:TIGR01408  878 VYKNCFLNLAIPLFVFTEPTEVRKTKIRNGISfTIWDRWTLHG------DFTLLEFINAVKEKYGLEPTMVSQGVKLLYV 951

                          970       980       990      1000      1010
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217394013 1006 FFMPaaKLKERLDQPMTEIVSRVSKRKLGRHVRALVLELCCNDESGEDVEVPYVRY 1061
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 ...
 55-1061 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: 1324.90  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013   55 DIDEGLYSRQLYVLGHEAMKRLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREEDIGKNRA 134
Cdd:TIGR01408    1 EIDEALYSRQLYVLGDEAMQKMAKSNVLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLSSNFFLSEDDVGRNRA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  135 EVSQPRLAELNSYVPVTAYTGPLVEDFLSGFQVVVLTNTPLEDQLRVGEFCHNR--GIKLVVADTRGLFGQLFCDFGEEM 212
Cdd:TIGR01408   81 EAVVKKLAELNPYVHVSSSSVPFNEEFLDKFQCVVLTEMSLPLQKEINDFCHSQcpPIAFISADVRGLFGSLFCDFGDEF 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  213 ILTDSNGEQPLSAMVSMVTKDNPGVVTCLDEARHGFESGDFVSFSEVQGMVELNGNQPMEIKVLGPYTFSICDTSNFSDY 292
Cdd:TIGR01408  161 EVLDTDGEEPKTGFIASITQANPGIVTCLENHRHKLETGDFVTFREVNGMTGLNDGSPRKITVISPYSFSIGDTTELGPY 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  293 IRGGIVSQVKVPKKISFKSLVASLAEPDFVVTDFAKFSRPAQLHIGFQALHQFCAQHGRPPRPRNEEDAAELVALAQAVN 372
Cdd:TIGR01408  241 LHGGIATQVKTPKTVFFKSLREQLKDPKCLIVDFSKPERPPEIHTAFQALDQFQEKYSRKPNVGCQQDAEELLKLATSIS 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  373 ARALPAVQqnNLDEDLIRKLAYVAAGDLAPINAFIGGLAAQEVMKACSGKFMPIMQWLYFDALECLPEDKEVLTEDkCLQ 452
Cdd:TIGR01408  321 ETLEEKVP--DVDAKLVHWLSWTAQGFLSPMAAAVGGVVSQEVLKAVTGKFSPLCQWFYFDSAESLPSLGKPECEE-FLP 397

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  453 RQNRYDGQVAVFGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGCGEGGEIIVTDMDTIEKSNLNRQFLFRPWDVTK 532
Cdd:TIGR01408  398 RGDRYDAQIAVFGDTFQQKLQNLNIFLVGCGAIGCEMLKNFALMGVGTGKKGMITVTDPDLIEKSNLNRQFLFRPHHIGK 477

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  533 LKSDTAAAAVRQMNPHIRVTSHQNRVGPDTERIYDDDFFQNLDGVANALDNVDARMYMDRRCVYYRKPLLESGTLGTKGN 612
Cdd:TIGR01408  478 PKSYTAADATLKINPQIKIDAHQNRVGPETETIFNDEFYEKLDVVINALDNVEARRYVDSRCLAFLKPLLESGTLGTKGN 557

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  613 VQVVIPFLTESYSSSQDPPEKSIPICTLKNFPNAIEHTLQWARDEFEGLFKQPAENVNQYLTDP-KFVERTLRLAGTQPL 691
Cdd:TIGR01408  558 TQVVVPHLTESYGSSRDPPEKEIPFCTLKSFPAAIEHTIQWARDKFEGLFSHKPSLVNKYLSSPsSAEEVLQKIQSGHSR 637

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  692 EVLEAVQRSLVLQRPQTWADCVTWACHHWHTQYSNNIRQLLHNFPPDQLTSSGAPFWSGPKRCPHPLTFDVNNPLHLDYV 771
Cdd:TIGR01408  638 EGLEQIIKLLSKEKPRNFSQCVEWARLKFEKYFNNKALQLLHCFPLDIRTSTGSPFWSSPKRPPSPLKFDLNEPLHLSFI 717

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  772 MAAANLFAQTYGLTGSQ---DRAAVATFLQSVQVPEFTPKSGVKIHVSDQELQSANASVDDSR-LEELKATLPSPDKLPG 847
Cdd:TIGR01408  718 QAAAKLYATVYGIPFAEedlSADALLNILSEVKIPEFKPRSNKKIQTDETARKPDTAPIDDRNaIFQLEKAILSNEATKS 797

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  848 -FKMYPIDFEKDDDSNFHMDFIVAASNLRAENYDIPSADRHKSKLIAGKIIPAIATTTAAVVGLVCLELYKVVQGHRQLD 926
Cdd:TIGR01408  798 dFRMAPLSFEKDDDHNGHIDFITAASNLRAKNYSIEPADRFKTKFIAGKIIPAIATSTATVSGLVCLELIKVTDGGYKFE 877

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  927 SYKNGFLNLALPFFGFSEPLAAPRHQYYNQEW-TLWDRFEVQGlqpngeEMTLKQFLDYFKTEHKLEITMLSQGVSMLYS 1005
Cdd:TIGR01408  878 VYKNCFLNLAIPLFVFTEPTEVRKTKIRNGISfTIWDRWTLHG------DFTLLEFINAVKEKYGLEPTMVSQGVKLLYV 951

                          970       980       990      1000      1010
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217394013 1006 FFMPaaKLKERLDQPMTEIVSRVSKRKLGRHVRALVLELCCNDESGEDVEVPYVRY 1061
Cdd:TIGR01408  952 PVMP--GHAERLKLKMHKLVKPTTKKKLPPYRVHLTVSFACDDDGDEDVPGPPVRI 1005
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
 476-1017 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 2217394013  476 KYFLVGAGAIGCELLKNFAMIGLGCGEGGEIIVTDMDTIEKSNLNRQFLFRPWDVTKLKSDTAAAAVRQMNPHIRVTSHQ 555
Cdd:cd01490      1 KVFLVGAGAIGCELLKNFALMGVGTGESGEITVTDMDNIEKSNLNRQFLFRPHDVGKPKSEVAAAAVKAMNPDLKITALQ 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  556 NRVGPDTERIYDDDFFQNLDGVANALDNVDARMYMDRRCVYYRKPLLESGTLGTKGNVQVVIPFLTESYSSSQDPPEKSI 635
Cdd:cd01490     81 NRVGPETEHIFNDEFWEKLDGVANALDNVDARMYVDRRCVYYRKPLLESGTLGTKGNTQVVIPHLTESYSSSRDPPEKSI 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  636 PICTLKNFPNAIEHTLQWARDEFEGLFKQPAENVNQYLtdpkfvertlrlagtqplevleavqrslvlqrpqtWADCVTW 715
Cdd:cd01490    161 PLCTLKNFPNAIEHTIQWARDEFEGLFKQPPENVNQYL-----------------------------------FEDCVRW 205

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  716 ACHHWHTQYSNNIRQLLHNFPPDQLTSSGAPFWSGPKRCPHPLTFDVNNPLHLDYVMAAANLFAQTYGLTGsqdraavat 795
Cdd:cd01490    206 ARLLFEKYFNNNIKQLLHNFPPDAVTSDGAPFWSGPKRCPTPLEFDVNNPLHLDFVLAAANLYAEVYGIPG--------- 276

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  796 flqsvqvpeftpksgvkihvsdqelqsanasvddsrleelkatlpspdklpgfkmypidFEKDDDSNFHMDFIVAASNLR 875
Cdd:cd01490    277 -----------------------------------------------------------FEKDDDTNFHMDFITAASNLR 297

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  876 AENYDIPSADRHKSKLIAGKIIPAIATTTAAVVGLVCLELYKVVQGHRQLDSYKNGFLNLALPFFGFSEPLAAPRHQY-Y 954
Cdd:cd01490    298 ARNYSIPPADRHKTKRIAGKIIPAIATTTAAVTGLVCLELYKVVDGKRPLEAYKNAFLNLALPFFAFSEPIPAPKVKYaY 377

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217394013  955 NQEWTLWDRFEVQGLQPNGEEMTlkqflDYFKTEHKLEITMLSQGVSMLYSFFMPAAKLKERL 1017
Cdd:cd01490    378 DEEWTIWDRFEVKGKQTLQELLI-----DYFKEKYGLEVTMLSQGVSMLYSSFMPPAKLKERL 435
UBA_E1_SCCH pfam10585
Ubiquitin-activating enzyme, SCCH domain; Ubiquitin-activating enzyme (E1 enzyme) activates ...
 644-890 1.18e-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: 445.91  E-value: 1.18e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  644 PNAIEHTLQWARDEFEGLFKQPAENVNQYLTDP-KFVERTLRLAGTQPLEVLEAVQRSLVLQRPQTWADCVTWACHHWHT 722
Cdd:pfam10585    1 PNAIEHTIQWARDEFEGLFVQPPEEVNKYLQPPqNFIESLLKQGGGQKLETLESVRKSLVTERPKTFEDCVAWARLKFEK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  723 QYSNNIRQLLHNFPPDQLTSSGAPFWSGPKRCPHPLTFDVNNPLHLDYVMAAANLFAQTYGLTGSQDRAAVATFLQSVQV 802
Cdd:pfam10585   81 LFNNDIKQLLYNFPPDHKTSSGAPFWSGPKRPPTPLEFDPNNPLHLDFVVAAANLRAQVYGIPGSRDREAIAKVLSKVKV 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  803 PEFTPKSGVKIHVSDQELQSANASV--DDSRLEELKATLP----SPDKLPGFKMYPIDFEKDDDSNFHMDFIVAASNLRA 876
Cdd:pfam10585  161 PEFKPKSGVKIQVNDEEAADPNAESedDEDELDELLEELPklavSPSSLAGFRLNPIEFEKDDDTNFHIDFITAASNLRA 240

                          250
                   ....*....|....
gi 2217394013  877 ENYDIPSADRHKSK 890
Cdd:pfam10585  241 RNYGIPPADRHKTK 254
UBA_e1_C smart00985
Ubiquitin-activating enzyme e1 C-terminal domain; This presumed domain found at the C terminus ...
 928-1059 3.94e-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: 226.76  E-value: 3.94e-69
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013   928 YKNGFLNLALPFFGFSEPLAAPRHQYYNQ-EWTLWDRFEVQGLqpngeEMTLKQFLDYFKTEHKLEITMLSQGVSMLYSF 1006
Cdd:smart00985    1 YKNAFLNLALPFFAFSEPIAAPKTKYRDKdKWTLWDRLEVPGG-----DITLKELLDYFEEKYGLEVTMLSQGVSLLYSS 75

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|...
gi 2217394013  1007 FMPAAKLKERLDQPMTEIVSRVSKRKLGRHVRALVLELCCNDESGEDVEVPYV 1059
Cdd:smart00985   76 FMPPKKHKERLDLPVTELVEQVTKKKLPPHVKYLVLEVSCEDEDDEDVEVPYI 128
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 456-618 1.20e-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: 1.20e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  456 RYDGQVAV--FGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGcgeggEIIVTDMDTIEKSNLNRQFLFRPWDVTKL 533
Cdd:COG0476      7 RYSRQILLpeIGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVG-----TLTLVDDDVVELSNLQRQILYTEADVGRP 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  534 KSDTAAAAVRQMNPHIRVTSHQNRVGPDTEriydDDFFQNLDGVANALDNVDARMYMDRRCVYYRKPLLESGTLGTKGNV 613
Cdd:COG0476     82 KVEAAAERLRALNPDVEVEAIPERLTEENA----LELLAGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIGFEGQV 157


                   ....*
gi 2217394013  614 QVVIP 618
Cdd:COG0476    158 TVFIP 162
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 456-601 6.77e-19

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 87.21  E-value: 6.77e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  456 RYDGQVAV--FGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGcgeggEIIVTDMDTIEKSNLNRQFLFRPWDVTKL 533
Cdd:PRK05690    12 RYNRQIILrgFDFDGQEKLKAARVLVVGLGGLGCAASQYLAAAGVG-----TLTLVDFDTVSLSNLQRQVLHDDATIGQP 86

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217394013  534 KSDTAAAAVRQMNPHIRVTSHQNRVGPDTEriydDDFFQNLDGVANALDNVDARMYMDRRCVYYRKPL 601
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 ...
 55-1061 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: 1324.90  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013   55 DIDEGLYSRQLYVLGHEAMKRLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREEDIGKNRA 134
Cdd:TIGR01408    1 EIDEALYSRQLYVLGDEAMQKMAKSNVLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLSSNFFLSEDDVGRNRA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  135 EVSQPRLAELNSYVPVTAYTGPLVEDFLSGFQVVVLTNTPLEDQLRVGEFCHNR--GIKLVVADTRGLFGQLFCDFGEEM 212
Cdd:TIGR01408   81 EAVVKKLAELNPYVHVSSSSVPFNEEFLDKFQCVVLTEMSLPLQKEINDFCHSQcpPIAFISADVRGLFGSLFCDFGDEF 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  213 ILTDSNGEQPLSAMVSMVTKDNPGVVTCLDEARHGFESGDFVSFSEVQGMVELNGNQPMEIKVLGPYTFSICDTSNFSDY 292
Cdd:TIGR01408  161 EVLDTDGEEPKTGFIASITQANPGIVTCLENHRHKLETGDFVTFREVNGMTGLNDGSPRKITVISPYSFSIGDTTELGPY 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  293 IRGGIVSQVKVPKKISFKSLVASLAEPDFVVTDFAKFSRPAQLHIGFQALHQFCAQHGRPPRPRNEEDAAELVALAQAVN 372
Cdd:TIGR01408  241 LHGGIATQVKTPKTVFFKSLREQLKDPKCLIVDFSKPERPPEIHTAFQALDQFQEKYSRKPNVGCQQDAEELLKLATSIS 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  373 ARALPAVQqnNLDEDLIRKLAYVAAGDLAPINAFIGGLAAQEVMKACSGKFMPIMQWLYFDALECLPEDKEVLTEDkCLQ 452
Cdd:TIGR01408  321 ETLEEKVP--DVDAKLVHWLSWTAQGFLSPMAAAVGGVVSQEVLKAVTGKFSPLCQWFYFDSAESLPSLGKPECEE-FLP 397

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  453 RQNRYDGQVAVFGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGCGEGGEIIVTDMDTIEKSNLNRQFLFRPWDVTK 532
Cdd:TIGR01408  398 RGDRYDAQIAVFGDTFQQKLQNLNIFLVGCGAIGCEMLKNFALMGVGTGKKGMITVTDPDLIEKSNLNRQFLFRPHHIGK 477

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  533 LKSDTAAAAVRQMNPHIRVTSHQNRVGPDTERIYDDDFFQNLDGVANALDNVDARMYMDRRCVYYRKPLLESGTLGTKGN 612
Cdd:TIGR01408  478 PKSYTAADATLKINPQIKIDAHQNRVGPETETIFNDEFYEKLDVVINALDNVEARRYVDSRCLAFLKPLLESGTLGTKGN 557

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  613 VQVVIPFLTESYSSSQDPPEKSIPICTLKNFPNAIEHTLQWARDEFEGLFKQPAENVNQYLTDP-KFVERTLRLAGTQPL 691
Cdd:TIGR01408  558 TQVVVPHLTESYGSSRDPPEKEIPFCTLKSFPAAIEHTIQWARDKFEGLFSHKPSLVNKYLSSPsSAEEVLQKIQSGHSR 637

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  692 EVLEAVQRSLVLQRPQTWADCVTWACHHWHTQYSNNIRQLLHNFPPDQLTSSGAPFWSGPKRCPHPLTFDVNNPLHLDYV 771
Cdd:TIGR01408  638 EGLEQIIKLLSKEKPRNFSQCVEWARLKFEKYFNNKALQLLHCFPLDIRTSTGSPFWSSPKRPPSPLKFDLNEPLHLSFI 717

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  772 MAAANLFAQTYGLTGSQ---DRAAVATFLQSVQVPEFTPKSGVKIHVSDQELQSANASVDDSR-LEELKATLPSPDKLPG 847
Cdd:TIGR01408  718 QAAAKLYATVYGIPFAEedlSADALLNILSEVKIPEFKPRSNKKIQTDETARKPDTAPIDDRNaIFQLEKAILSNEATKS 797

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  848 -FKMYPIDFEKDDDSNFHMDFIVAASNLRAENYDIPSADRHKSKLIAGKIIPAIATTTAAVVGLVCLELYKVVQGHRQLD 926
Cdd:TIGR01408  798 dFRMAPLSFEKDDDHNGHIDFITAASNLRAKNYSIEPADRFKTKFIAGKIIPAIATSTATVSGLVCLELIKVTDGGYKFE 877

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  927 SYKNGFLNLALPFFGFSEPLAAPRHQYYNQEW-TLWDRFEVQGlqpngeEMTLKQFLDYFKTEHKLEITMLSQGVSMLYS 1005
Cdd:TIGR01408  878 VYKNCFLNLAIPLFVFTEPTEVRKTKIRNGISfTIWDRWTLHG------DFTLLEFINAVKEKYGLEPTMVSQGVKLLYV 951

                          970       980       990      1000      1010
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217394013 1006 FFMPaaKLKERLDQPMTEIVSRVSKRKLGRHVRALVLELCCNDESGEDVEVPYVRY 1061
Cdd:TIGR01408  952 PVMP--GHAERLKLKMHKLVKPTTKKKLPPYRVHLTVSFACDDDGDEDVPGPPVRI 1005
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
 476-1017 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 2217394013  476 KYFLVGAGAIGCELLKNFAMIGLGCGEGGEIIVTDMDTIEKSNLNRQFLFRPWDVTKLKSDTAAAAVRQMNPHIRVTSHQ 555
Cdd:cd01490      1 KVFLVGAGAIGCELLKNFALMGVGTGESGEITVTDMDNIEKSNLNRQFLFRPHDVGKPKSEVAAAAVKAMNPDLKITALQ 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  556 NRVGPDTERIYDDDFFQNLDGVANALDNVDARMYMDRRCVYYRKPLLESGTLGTKGNVQVVIPFLTESYSSSQDPPEKSI 635
Cdd:cd01490     81 NRVGPETEHIFNDEFWEKLDGVANALDNVDARMYVDRRCVYYRKPLLESGTLGTKGNTQVVIPHLTESYSSSRDPPEKSI 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  636 PICTLKNFPNAIEHTLQWARDEFEGLFKQPAENVNQYLtdpkfvertlrlagtqplevleavqrslvlqrpqtWADCVTW 715
Cdd:cd01490    161 PLCTLKNFPNAIEHTIQWARDEFEGLFKQPPENVNQYL-----------------------------------FEDCVRW 205

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  716 ACHHWHTQYSNNIRQLLHNFPPDQLTSSGAPFWSGPKRCPHPLTFDVNNPLHLDYVMAAANLFAQTYGLTGsqdraavat 795
Cdd:cd01490    206 ARLLFEKYFNNNIKQLLHNFPPDAVTSDGAPFWSGPKRCPTPLEFDVNNPLHLDFVLAAANLYAEVYGIPG--------- 276

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  796 flqsvqvpeftpksgvkihvsdqelqsanasvddsrleelkatlpspdklpgfkmypidFEKDDDSNFHMDFIVAASNLR 875
Cdd:cd01490    277 -----------------------------------------------------------FEKDDDTNFHMDFITAASNLR 297

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  876 AENYDIPSADRHKSKLIAGKIIPAIATTTAAVVGLVCLELYKVVQGHRQLDSYKNGFLNLALPFFGFSEPLAAPRHQY-Y 954
Cdd:cd01490    298 ARNYSIPPADRHKTKRIAGKIIPAIATTTAAVTGLVCLELYKVVDGKRPLEAYKNAFLNLALPFFAFSEPIPAPKVKYaY 377

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217394013  955 NQEWTLWDRFEVQGLQPNGEEMTlkqflDYFKTEHKLEITMLSQGVSMLYSFFMPAAKLKERL 1017
Cdd:cd01490    378 DEEWTIWDRFEVKGKQTLQELLI-----DYFKEKYGLEVTMLSQGVSMLYSSFMPPAKLKERL 435
Ube1_repeat1 cd01491
Ubiquitin activating enzyme (E1), repeat 1. E1, a highly conserved small protein present ...
 60-442 2.72e-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: 526.45  E-value: 2.72e-180
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013   60 LYSRQLYVLGHEAMKRLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREEDIGKNRAEVSQP 139
Cdd:cd01491      1 LYSRQLYVLGHEAMKKLQKSNVLISGLGGLGVEIAKNLILAGVKSVTLHDTKPCSWSDLSSQFYLREEDIGKNRAEASQA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  140 RLAELNSYVPVTAYTGPLVEDFLSGFQVVVLTNTPLEDQLRVGEFCHNRGIKLVVADTRGLFGQLFCDFGEEMILTDSNG 219
Cdd:cd01491     81 RLAELNPYVPVTVSTGPLTTDELLKFQVVVLTDASLEDQLKINEFCHSPGIKFISADTRGLFGSIFCDFGDEFTVYDPNG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  220 EQPLSAMVSMVTKDNPGVVTCLDEARHGFESGDFVSFSEVQGMVELNGNQPMEIKVLGPYTFSICDTSNFSDYIRGGIVS 299
Cdd:cd01491    161 EEPKSGMISSISKDNPGVVTCLDETRHGFEDGDYVTFSEVEGMTELNGCEPRKIKVKGPYTFSIGDTSSFSEYIRGGIVT 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  300 QVKvpkkisfkslvaslaepdfvvtdfakfsrpaqlhigfqalhqfcaqhgrpprprneedaaelvalaqavnaralpav 379
Cdd:cd01491    241 QVK----------------------------------------------------------------------------- 243

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217394013  380 qqnnldedlirklayvaagdLAPINAFIGGLAAQEVMKACSGKFMPIMQWLYFDALECLPEDK 442
Cdd:cd01491    244 --------------------LSPMAAFFGGLAAQEVLKACSGKFTPLKQWLYFDALECLPEDE 286
UBA_E1_SCCH pfam10585
Ubiquitin-activating enzyme, SCCH domain; Ubiquitin-activating enzyme (E1 enzyme) activates ...
 644-890 1.18e-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: 445.91  E-value: 1.18e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  644 PNAIEHTLQWARDEFEGLFKQPAENVNQYLTDP-KFVERTLRLAGTQPLEVLEAVQRSLVLQRPQTWADCVTWACHHWHT 722
Cdd:pfam10585    1 PNAIEHTIQWARDEFEGLFVQPPEEVNKYLQPPqNFIESLLKQGGGQKLETLESVRKSLVTERPKTFEDCVAWARLKFEK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  723 QYSNNIRQLLHNFPPDQLTSSGAPFWSGPKRCPHPLTFDVNNPLHLDYVMAAANLFAQTYGLTGSQDRAAVATFLQSVQV 802
Cdd:pfam10585   81 LFNNDIKQLLYNFPPDHKTSSGAPFWSGPKRPPTPLEFDPNNPLHLDFVVAAANLRAQVYGIPGSRDREAIAKVLSKVKV 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  803 PEFTPKSGVKIHVSDQELQSANASV--DDSRLEELKATLP----SPDKLPGFKMYPIDFEKDDDSNFHMDFIVAASNLRA 876
Cdd:pfam10585  161 PEFKPKSGVKIQVNDEEAADPNAESedDEDELDELLEELPklavSPSSLAGFRLNPIEFEKDDDTNFHIDFITAASNLRA 240

                          250
                   ....*....|....
gi 2217394013  877 ENYDIPSADRHKSK 890
Cdd:pfam10585  241 RNYGIPPADRHKTK 254
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
 476-659 5.97e-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: 5.97e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  476 KYFLVGAGAIGCELLKNFAMIGLGcgeggEIIVTDMDTIEKSNLNRQFLFRPWDVTKLKSDTAAAAVRQMNPHIRVTSHQ 555
Cdd:cd01484      1 KVLLVGAGGIGCELLKNLALMGFG-----QIHVIDMDTIDVSNLNRQFLFRPKDIGRPKSEVAAEAVNDRNPNCKVVPYQ 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  556 NRVGPdtERIYDDDFFQNLDGVANALDNVDARMYMDRRCVYYRKPLLESGTLGTKGNVQVVIPFLTESYSSSQDPPEKSI 635
Cdd:cd01484     76 NKVGP--EQDFNDTFFEQFHIIVNALDNIIARRYVNGMLIFLIVPLIESGTEGFKGNAQVILPGMTECIECTLYPPQKNF 153

                          170       180
                   ....*....|....*....|....
gi 2217394013  636 PICTLKNFPNAIEHTLQWARDEFE 659
Cdd:cd01484    154 PMCTIASMPRLPEHCIEWARMLQW 177
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 457-643 2.44e-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: 2.44e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  457 YDGQVA--VFGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGcgeggEIIVTDMDTIEKSNLNRQFLFRPWDVTKLK 534
Cdd:pfam00899    1 YSRQLAlpLIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVG-----KITLVDFDTVELSNLNRQFLFREADIGKPK 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  535 SDTAAAAVRQMNPHIRVTSHQNRVGPDTeriyDDDFFQNLDGVANALDNVDARMYMDRRCVYYRKPLLESGTLGTKGNVQ 614
Cdd:pfam00899   76 AEVAAERLREINPDVEVEAYTERLTPEN----AEELIKSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVT 151

                          170       180       190
                   ....*....|....*....|....*....|.
gi 2217394013  615 VVIPFLTESYS--SSQDPPEKSIPICTLKNF 643
Cdd:pfam00899  152 VVIPGKTPCYRclFPEDPPPKLVPSCTVAGV 182
UBA_e1_C smart00985
Ubiquitin-activating enzyme e1 C-terminal domain; This presumed domain found at the C terminus ...
 928-1059 3.94e-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: 226.76  E-value: 3.94e-69
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013   928 YKNGFLNLALPFFGFSEPLAAPRHQYYNQ-EWTLWDRFEVQGLqpngeEMTLKQFLDYFKTEHKLEITMLSQGVSMLYSF 1006
Cdd:smart00985    1 YKNAFLNLALPFFAFSEPIAAPKTKYRDKdKWTLWDRLEVPGG-----DITLKELLDYFEEKYGLEVTMLSQGVSLLYSS 75

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|...
gi 2217394013  1007 FMPAAKLKERLDQPMTEIVSRVSKRKLGRHVRALVLELCCNDESGEDVEVPYV 1059
Cdd:smart00985   76 FMPPKKHKERLDLPVTELVEQVTKKKLPPHVKYLVLEVSCEDEDDEDVEVPYI 128
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 476-935 4.73e-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: 4.73e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  476 KYFLVGAGAIGCELLKNFAMIGLGcgeggEIIVTDMDTIEKSNLNRQFLFRPWDVTKLKSDTAAAAVRQMNPHIRVTSHQ 555
Cdd:cd01489      1 KVLVVGAGGIGCELLKNLVLTGFG-----EIHIIDLDTIDLSNLNRQFLFRKKHVGKSKAQVAKEAVLSFNPNVKIVAYH 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  556 NRVgpdTERIYDDDFFQNLDGVANALDNVDARMYMDRRCVYYRKPLLESGTLGTKGNVQVVIPFLTESYSSSQDPPEKSI 635
Cdd:cd01489     76 ANI---KDPDFNVEFFKQFDLVFNALDNLAARRHVNKMCLAADVPLIESGTTGFLGQVQVIKKGKTECYECQPKETPKTF 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  636 PICTLKNFPNAIEHTLQWARDE---FEGLFKQpaenvnqyltdpkfvertlrlagtqplevleavqrslvlqrpqtwadc 712
Cdd:cd01489    153 PVCTIRSTPSQPIHCIVWAKSLfflFNKVFKD------------------------------------------------ 184

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  713 vtwachhwhtqysnNIRQLLHNfppDQLtssgapfWSGPKRcPHPLTFDvnnplhldyvmaaanlfaqtygltgsqdraa 792
Cdd:cd01489    185 --------------DIERLLSM---EEL-------WKTRKP-PVPLSWK------------------------------- 208

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  793 vatflqsvqvpeftpksgvkihvsdqelqsanasvddsrleelkatlpspdklpgfkmyPIDFEKDDDSNfhMDFIVAAS 872
Cdd:cd01489    209 -----------------------------------------------------------ELTFDKDDQDA--LDFVAAAA 227

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217394013  873 NLRAENYDIPSADRHKSKLIAGKIIPAIATTTAAVVGLVCLELYKVVQGHrqLDSYKNGFLNL 935
Cdd:cd01489    228 NLRSHVFGIPMKSRFDIKQMAGNIIPAIATTNAIIAGLIVLEALKVLSGD--KEQCRTVFLNL 288
E1_UFD pfam09358
Ubiquitin fold domain; The ubiquitin fold domain is found at the C-terminus of ...
 961-1059 4.31e-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: 4.31e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  961 WDRFEVQGlqpngeEMTLKQFLDYFKTEHKLEITMLSQGVSMLYSFFMPAAKLKERLDQPMTEIVSRVSKRKLGRHVRAL 1040
Cdd:pfam09358    1 WDRFEVEG------DMTLQELLDYFKEKYGLEVTMLSYGVSLLYSSFMPPKKHKERLPMKISELVEEVSKKPIPPHQKYL 74

                           90
                   ....*....|....*....
gi 2217394013 1041 VLELCCNDESGEDVEVPYV 1059
Cdd:pfam09358   75 VLEVSCEDEDGEDVEVPYV 93
E1-1_like cd01485
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ...
 60-223 7.67e-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: 7.67e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013   60 LYSRQLYVLGHEAMKRLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREE--DIGKNRAEVS 137
Cdd:cd01485      1 LYDRQIRLWGDEAQNKLRSAKVLIIGAGALGAEIAKNLVLAGIDSITIVDHRLVSTEDLGSNFFLDAEvsNSGMNRAAAS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  138 QPRLAELNSYVPVTAYTGP------LVEDFLSGFQVVVLTNTPLEDQLRVGEFCHNRGIKLVVADTRGLFGQLFCDF--- 208
Cdd:cd01485     81 YEFLQELNPNVKLSIVEEDslsndsNIEEYLQKFTLVIATEENYERTAKVNDVCRKHHIPFISCATYGLIGYAFFDFpia 160

                          170       180
                   ....*....|....*....|..
gi 2217394013  209 -------GEEMILTDSNGEQPL 223
Cdd:cd01485    161 aflggvvAQEAIKSISGKFTPL 182
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 61-205 5.15e-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: 5.15e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013   61 YSRQLY--VLGHEAMKRLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREEDIGKNRAEVSQ 138
Cdd:pfam00899    1 YSRQLAlpLIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAA 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217394013  139 PRLAELNSYVPVTAYTGPL----VEDFLSGFQVVVLTNTPLEDQLRVGEFCHNRGIKLVVADTRGLFGQLF 205
Cdd:pfam00899   81 ERLREINPDVEVEAYTERLtpenAEELIKSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVT 151
E1_FCCH pfam16190
Ubiquitin-activating enzyme E1 FCCH domain; This domain is found in the ubiquitin-activating ...
 233-302 5.92e-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: 5.92e-43
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  233 DNPGVVTCLDEARHGFESGDFVSFSEVQGMVELNGNQPMEIKVLGPYTFSICDTSNFSDYIRGGIVSQVK 302
Cdd:pfam16190    1 DNPGVVTCLDDTRHGLEDGDYVTFSEVEGMTELNGCEPRKIKVLGPYTFSIGDTSSFSPYLRGGIVTQVK 70
Aos1_SUMO cd01492
Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating ...
 60-207 1.31e-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: 1.31e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013   60 LYSRQLYVLGHEAMKRLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREEDIGKNRAEVSQP 139
Cdd:cd01492      3 LYDRQIRLWGLEAQKRLRSARILLIGLKGLGAEIAKNLVLSGIGSLTILDDRTVTEEDLGAQFLIPAEDLGQNRAEASLE 82

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217394013  140 RLAELNSYVPVTAYTGPLVE---DFLSGFQVVVLTNTPLEDQLRVGEFCHNRGIKLVVADTRGLFGQLFCD 207
Cdd:cd01492     83 RLRALNPRVKVSVDTDDISEkpeEFFSQFDVVVATELSRAELVKINELCRKLGVKFYATGVHGLFGFVFAD 153
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 476-655 1.33e-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: 1.33e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  476 KYFLVGAGAIGCELLKNFAMIGLGcgeggEIIVTDMDTIEKSNLNRQFLFRPWDVTKLKSDTAAAAVRQMNPHIRVTSHQ 555
Cdd:cd01488      1 KILVIGAGGLGCELLKNLALSGFR-----NIHVIDMDTIDVSNLNRQFLFREKDIGKPKAEVAAKFVNDRVPGVNVTPHF 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  556 NRVgpdteRIYDDDFFQNLDGVANALDNVDARMYMDRRCVY--------YRKPLLESGTLGTKGNVQVVIPFLTESYSSS 627
Cdd:cd01488     76 GKI-----QDKDEEFYRQFNIIICGLDSIEARRWINGTLVSlllyedpeSIIPLIDGGTEGFKGHARVILPGITACIECS 150

                          170       180       190
                   ....*....|....*....|....*....|
gi 2217394013  628 QD--PPEKSIPICTLKNFPNAIEHTLQWAR 655
Cdd:cd01488    151 LDlfPPQVTFPLCTIANTPRLPEHCIEYAS 180
E1_4HB pfam16191
Ubiquitin-activating enzyme E1 four-helix bundle; This domain is found in the ...
 303-372 4.02e-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: 4.02e-38
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  303 VPKKISFKSLVASLAEPDFVVTDFAKFSRPAQLHIGFQALHQFCAQHGRPPRPRNEEDAAELVALAQAVN 372
Cdd:pfam16191    1 MPKTLSFKSLEESLKEPEFLISDFAKFDRPAQLHLAFQALHAFQEKHGRLPRPWNEEDAEEVVKLAKELN 70
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 456-638 1.01e-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: 1.01e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  456 RYDGQVAV--FGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGcgeggEIIVTDMDTIEKSNLNRQFLFRPWDVTKL 533
Cdd:cd00757      1 RYSRQILLpeIGEEGQEKLKNARVLVVGAGGLGSPAAEYLAAAGVG-----KLGLVDDDVVELSNLQRQILHTEADVGQP 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  534 KSDTAAAAVRQMNPHIRVTSHQNRVGPDTEriydDDFFQNLDGVANALDNVDARMYMDRRCVYYRKPLLESGTLGTKGNV 613
Cdd:cd00757     76 KAEAAAERLRAINPDVEIEAYNERLDAENA----EELIAGYDLVLDCTDNFATRYLINDACVKLGKPLVSGAVLGFEGQV 151

                          170       180
                   ....*....|....*....|....*.
gi 2217394013  614 QVVIPFLTESYSSS-QDPPEKSIPIC 638
Cdd:cd00757    152 TVFIPGEGPCYRCLfPEPPPPGVPSC 177
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 456-618 1.20e-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: 1.20e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  456 RYDGQVAV--FGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGcgeggEIIVTDMDTIEKSNLNRQFLFRPWDVTKL 533
Cdd:COG0476      7 RYSRQILLpeIGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVG-----TLTLVDDDVVELSNLQRQILYTEADVGRP 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  534 KSDTAAAAVRQMNPHIRVTSHQNRVGPDTEriydDDFFQNLDGVANALDNVDARMYMDRRCVYYRKPLLESGTLGTKGNV 613
Cdd:COG0476     82 KVEAAAERLRALNPDVEVEAIPERLTEENA----LELLAGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIGFEGQV 157


                   ....*
gi 2217394013  614 QVVIP 618
Cdd:COG0476    158 TVFIP 162
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 478-617 9.82e-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: 9.82e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  478 FLVGAGAIGCELLKNFAMIGLGcgeggEIIVTDMDTIEKSNLNRQFLFRPWDVTKLKSDTAAAAVRQMNPHIRVTSHQNR 557
Cdd:cd01483      3 LLVGLGGLGSEIALNLARSGVG-----KITLIDFDTVELSNLNRQFLARQADIGKPKAEVAARRLNELNPGVNVTAVPEG 77

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  558 VGPDTeriyDDDFFQNLDGVANALDNVDARMYMDRRCVYYRKPLLESGTLGTKGNVQVVI 617
Cdd:cd01483     78 ISEDN----LDDFLDGVDLVIDAIDNIAVRRALNRACKELGIPVIDAGGLGLGGDIQVID 133
APPBP1_RUB cd01493
Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric ...
 61-434 2.31e-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: 2.31e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013   61 YSRQLYVLGHEAMKRLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREEDIGKNRAEVSQPR 140
Cdd:cd01493      3 YDRQLRLWGEHGQAALESAHVCLLNATATGTEILKNLVLPGIGSFTIVDGSKVDEEDLGNNFFLDASSLGKSRAEATCEL 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  141 LAELNSYVPVTAYTGPLVE------DFLSGFQVVVLTNTPLEDQLRVGEFCHNRGIKLVVADTRGLFGQLFCDFGEEMIl 214
Cdd:cd01493     83 LQELNPDVNGSAVEESPEAlldndpSFFSQFTVVIATNLPESTLLRLADVLWSANIPLLYVRSYGLYGYIRIQLKEHTI- 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  215 TDSNGEQPLSAMvsmvTKDNPgvvtcldearhgfesgdfvsFSEVQGMVE---LNGNQPME----------IKVL----- 276
Cdd:cd01493    162 VESHPDNALEDL----RLDNP--------------------FPELREHADsidLDDMDPAEhshtpyivilIKYLekwrs 217

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  277 ---GPYTFSICDTSNFSDYIRGGIVSQvkvPKKISFKSLVASlaepdfVVTDFAKFSRPAQLHIGFQ------------- 340
Cdd:cd01493    218 ahnGQLPSTYKEKKEFRDLVRSLMRSN---EDEENFEEAIKA------VNKALNRTKIPSSVEEIFNddrcenltsqsss 288

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  341 ------ALHQFCA-QHGRPP----------------------RPRNEEDAAELVALAQAV-NARALPAvqqNNLDEDLI- 389
Cdd:cd01493    289 fwimarALKEFVAeENGLLPlpgtlpdmtadtekyiklqniyREKAEKDAAEVEKYVREIlKSLGRSP---DSISDKEIk 365

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2217394013  390 ---RKLAYVAA----GDLAPINAFIGGLAAQEVMKACSGKFMPIMQWLYFDA 434
Cdd:cd01493    366 lfcKNAAFLRVirgrSLEHNISAFMGGIAAQEVIKLITKQYVPIDNTFIFDG 417
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 81-204 3.16e-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: 3.16e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013   81 VLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREEDIGKNRAEVSQPRLAELNSYVPVTAYT----GP 156
Cdd:cd01483      2 VLLVGLGGLGSEIALNLARSGVGKITLIDFDTVELSNLNRQFLARQADIGKPKAEVAARRLNELNPGVNVTAVPegisED 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 2217394013  157 LVEDFLSGFQVVVLTNTPLEDQLRVGEFCHNRGIKLVVADTRGLFGQL 204
Cdd:cd01483     82 NLDDFLDGVDLVIDAIDNIAVRRALNRACKELGIPVIDAGGLGLGGDI 129
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 456-601 6.77e-19

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 87.21  E-value: 6.77e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  456 RYDGQVAV--FGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGcgeggEIIVTDMDTIEKSNLNRQFLFRPWDVTKL 533
Cdd:PRK05690    12 RYNRQIILrgFDFDGQEKLKAARVLVVGLGGLGCAASQYLAAAGVG-----TLTLVDFDTVSLSNLQRQVLHDDATIGQP 86

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217394013  534 KSDTAAAAVRQMNPHIRVTSHQNRVGPDTEriydDDFFQNLDGVANALDNVDARMYMDRRCVYYRKPL 601
Cdd:PRK05690    87 KVESARAALARINPHIAIETINARLDDDEL----AALIAGHDLVLDCTDNVATRNQLNRACFAAKKPL 150
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
465-618 1.78e-16

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 82.75  E-value: 1.78e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  465 GSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGcgeggEIIVTDMDTIEKSNLNRQFLFRPWDVTKLKSDTAAAAVRQ 544
Cdd:PRK08762   126 GEEGQRRLLEARVLLIGAGGLGSPAALYLAAAGVG-----TLGIVDHDVVDRSNLQRQILHTEDRVGQPKVDSAAQRLAA 200

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217394013  545 MNPHIRVTSHQNRVGPDTEriydDDFFQNLDGVANALDNVDARMYMDRRCVYYRKPLLESGTLGTKGNVQVVIP 618
Cdd:PRK08762   201 LNPDVQVEAVQERVTSDNV----EALLQDVDVVVDGADNFPTRYLLNDACVKLGKPLVYGAVFRFEGQVSVFDA 270
PRK08328 PRK08328
hypothetical protein; Provisional
 61-204 3.40e-16

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 79.07  E-value: 3.40e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013   61 YSRQLYVLGHEAMKRLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREEDIGKNRAEVSQP- 139
Cdd:PRK08328    10 YDRQIMIFGVEGQEKLKKAKVAVVGVGGLGSPVAYYLAAAGVGRILLIDEQTPELSNLNRQILHWEEDLGKNPKPLSAKw 89

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217394013  140 RLAELNSYVPVTAYTGPL----VEDFLSGFQVVVLTNTPLEDQLRVGEFCHNRGIKLVVADTRGLFGQL 204
Cdd:PRK08328    90 KLERFNSDIKIETFVGRLseenIDEVLKGVDVIVDCLDNFETRYLLDDYAHKKGIPLVHGAVEGTYGQV 158
PRK08328 PRK08328
hypothetical protein; Provisional
 456-623 2.44e-15

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 76.37  E-value: 2.44e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  456 RYDGQVAVFGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLgcgegGEIIVTDMDTIEKSNLNRQFLFRPWDVTK-LK 534
Cdd:PRK08328     9 RYDRQIMIFGVEGQEKLKKAKVAVVGVGGLGSPVAYYLAAAGV-----GRILLIDEQTPELSNLNRQILHWEEDLGKnPK 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  535 SDTAAAAVRQMNPHIRVTSHQNRVgpDTERIydDDFFQNLDGVANALDNVDARMYMDRRCVYYRKPLLESGTLGTKGNVQ 614
Cdd:PRK08328    84 PLSAKWKLERFNSDIKIETFVGRL--SEENI--DEVLKGVDVIVDCLDNFETRYLLDDYAHKKGIPLVHGAVEGTYGQVT 159


                   ....*....
gi 2217394013  615 VVIPFLTES 623
Cdd:PRK08328   160 TIVPGKTKR 168
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 61-230 3.93e-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: 3.93e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013   61 YSRQ--LYVLGHEAMKRLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREEDIGKNRAEVSQ 138
Cdd:COG0476      8 YSRQilLPEIGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADVGRPKVEAAA 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  139 PRLAELNSYVPVTAYTGPL----VEDFLSGFQVVV--LTNtpLEDQLRVGEFCHNRGIKLVVADTRGLFGQLF------- 205
Cdd:COG0476     88 ERLRALNPDVEVEAIPERLteenALELLAGADLVLdcTDN--FATRYLLNDACVKLGIPLVSGAVIGFEGQVTvfipgdt 165

                          170       180       190
                   ....*....|....*....|....*....|
gi 2217394013  206 ----CDFGEEMILTDSNGEQP-LSAMVSMV 230
Cdd:COG0476    166 pcyrCLFPEPPEPGPSCAEAGvLGPLVGVI 195
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 446-587 5.35e-15

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 78.00  E-value: 5.35e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  446 TEDKCLQRQNRYDGqvavFGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGcgeggEIIVTDMDTIEKSNLNRQFLF 525
Cdd:PRK05600    17 SELRRTARQLALPG----FGIEQQERLHNARVLVIGAGGLGCPAMQSLASAGVG-----TITLIDDDTVDVSNIHRQILF 87

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217394013  526 RPWDVTKLKSDTAAAAVRQMNPHIRVTSHQNRVGPDTERiyddDFFQNLDGVANALDNVDAR 587
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 ...
 61-204 1.56e-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: 1.56e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013   61 YSRQLYV--LGHEAMKRLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREEDIGKNRAEVSQ 138
Cdd:cd00757      2 YSRQILLpeIGEEGQEKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRQILHTEADVGQPKAEAAA 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217394013  139 PRLAELNSYVPVTAY----TGPLVEDFLSGFQVVV--LTNtpLEDQLRVGEFCHNRGIKLVVADTRGLFGQL 204
Cdd:cd00757     82 ERLRAINPDVEIEAYnerlDAENAEELIAGYDLVLdcTDN--FATRYLINDACVKLGKPLVSGAVLGFEGQV 151
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 455-618 7.32e-14

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 74.26  E-value: 7.32e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  455 NRYDGQV--AVFGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGcgeggEIIVTDMDTIEKSNLNRQFLFRPWDVTK 532
Cdd:PRK07688     3 ERYSRQElfSPIGEEGQQKLREKHVLIIGAGALGTANAEMLVRAGVG-----KVTIVDRDYVEWSNLQRQQLYTESDVKN 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  533 LKSDTAAAAVR--QMNPHIRVTSHQNRVGPdtERIydDDFFQNLDGVANALDNVDARMYMDRRCVYYRKPLLESGTLGTK 610
Cdd:PRK07688    78 NLPKAVAAKKRleEINSDVRVEAIVQDVTA--EEL--EELVTGVDLIIDATDNFETRFIVNDAAQKYGIPWIYGACVGSY 153


                   ....*...
gi 2217394013  611 GNVQVVIP 618
Cdd:PRK07688   154 GLSYTIIP 161
Aos1_SUMO cd01492
Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating ...
 457-611 1.96e-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: 1.96e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  457 YDGQVAVFGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLgcgegGEIIVTDMDTIEKSNLNRQFLFRPWDVTKLKSD 536
Cdd:cd01492      4 YDRQIRLWGLEAQKRLRSARILLIGLKGLGAEIAKNLVLSGI-----GSLTILDDRTVTEEDLGAQFLIPAEDLGQNRAE 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217394013  537 TAAAAVRQMNPHIRVTShqnrvgpDTERI--YDDDFFQNLDGV-ANALDNvDARMYMDRRCVYYRKPLLESGTLGTKG 611
Cdd:cd01492     79 ASLERLRALNPRVKVSV-------DTDDIseKPEEFFSQFDVVvATELSR-AELVKINELCRKLGVKFYATGVHGLFG 148
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
 464-610 4.24e-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: 4.24e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  464 FGSDLQEKLGKQKYFLVGAGAIGcellkNFAMIGL---GCGEggeIIVTDMDTIEKSNLNRQFLFRPWDVTKLKSDTAAA 540
Cdd:cd00755      1 YGEEGLEKLRNAHVAVVGLGGVG-----SWAAEALarsGVGK---LTLIDFDVVCVSNLNRQIHALLSTVGKPKVEVMAE 72

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  541 AVRQMNPHIRVTSHQNRVGPDTEriyDDDFFQNLDGVANALDNVDARMYMDRRCVYYRKPLLESGTLGTK 610
Cdd:cd00755     73 RIRDINPECEVDAVEEFLTPDNS---EDLLGGDPDFVVDAIDSIRAKVALIAYCRKRKIPVISSMGAGGK 139
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 465-600 5.29e-12

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 68.97  E-value: 5.29e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  465 GSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGcgeggEIIVTDMDTIEKSNLNRQFLFRPWDVTKLKSDTAAAAVRQ 544
Cdd:PRK07878    33 GVDGQKRLKNARVLVIGAGGLGSPTLLYLAAAGVG-----TLGIVEFDVVDESNLQRQVIHGQSDVGRSKAQSARDSIVE 107

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217394013  545 MNPHIRVTSHQNRVGPDTERiyddDFFQNLDGVANALDNVDARMYMDRRCVYYRKP 600
Cdd:PRK07878   108 INPLVNVRLHEFRLDPSNAV----ELFSQYDLILDGTDNFATRYLVNDAAVLAGKP 159
TcdA COG1179
tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ...
 479-605 1.71e-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: 1.71e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  479 LVGAGAIgcELLKN--FAMIGLG-----CGEG------GEIIVTDMDTIEKSNLNRQF--LfrpwDVT--KLKSDTAAAA 541
Cdd:COG1179     13 LYGEEGL--ERLANahVAVVGLGgvgswAAEAlarsgvGRLTLVDLDDVCESNINRQLhaL----DSTvgRPKVEVMAER 86

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217394013  542 VRQMNPHIRVTSHQNRVGPDTeriYDDDFFQNLDGVANALDNVDARMYMDRRCVYYRKPLLESG 605
Cdd:COG1179     87 IRDINPDCEVTAIDEFVTPEN---ADELLSEDYDYVIDAIDSVSAKAALIAWCRRRGIPIISSM 147
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 456-587 5.01e-11

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 65.66  E-value: 5.01e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  456 RYDGQVAV--FGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGcgeggEIIVTDMDTIEKSNLNRQFLFRPWDVTKL 533
Cdd:PRK05597     8 RYRRQIMLgeIGQQGQQSLFDAKVAVIGAGGLGSPALLYLAGAGVG-----HITIIDDDTVDLSNLHRQVIHSTAGVGQP 82

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2217394013  534 KSDTAAAAVRQMNPHIRVTSHQNRVGPDTERiyddDFFQNLDGVANALDNVDAR 587
Cdd:PRK05597    83 KAESAREAMLALNPDVKVTVSVRRLTWSNAL----DELRDADVILDGSDNFDTR 132
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
457-586 9.15e-11

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 62.57  E-value: 9.15e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  457 YDGQVAVFGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGcgeggEIIVTDMDTIEKSNLNRQFLFrPWDVTKLKSD 536
Cdd:PRK08644    11 EAMLASRHTPKLLEKLKKAKVGIAGAGGLGSNIAVALARSGVG-----NLKLVDFDVVEPSNLNRQQYF-ISQIGMPKVE 84

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2217394013  537 TAAAAVRQMNPHIRVTSHQNRVgpDTERIydDDFFQNLDGVANALDNVDA 586
Cdd:PRK08644    85 ALKENLLEINPFVEIEAHNEKI--DEDNI--EELFKDCDIVVEAFDNAET 130
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 80-170 1.66e-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: 1.66e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013   80 SVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREEDIGKNRAEVSQPRLAELNSYVPVTAYTGPLV- 158
Cdd:cd01488      1 KILVIGAGGLGCELLKNLALSGFRNIHVIDMDTIDVSNLNRQFLFREKDIGKPKAEVAAKFVNDRVPGVNVTPHFGKIQd 80

                           90
                   ....*....|....
gi 2217394013  159 --EDFLSGFQVVVL 170
Cdd:cd01488     81 kdEEFYRQFNIIIC 94
E1-1_like cd01485
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ...
 457-551 2.06e-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: 2.06e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  457 YDGQVAVFGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLgcgegGEIIVTDMDTIEKSNLNRQFLFRPWDVT--KLK 534
Cdd:cd01485      2 YDRQIRLWGDEAQNKLRSAKVLIIGAGALGAEIAKNLVLAGI-----DSITIVDHRLVSTEDLGSNFFLDAEVSNsgMNR 76

                           90
                   ....*....|....*..
gi 2217394013  535 SDTAAAAVRQMNPHIRV 551
Cdd:cd01485     77 AAASYEFLQELNPNVKL 93
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 454-644 2.72e-10

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 63.21  E-value: 2.72e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  454 QNRYDGQVAV--FGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGcgeggEIIVTDMDTIEKSNLNRQFLFRPWDVT 531
Cdd:PRK12475     2 QERYSRQILFsgIGEEGQRKIREKHVLIVGAGALGAANAEALVRAGIG-----KLTIADRDYVEWSNLQRQQLYTEEDAK 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  532 KLKSDTAAAA--VRQMNPHIRVTSHQNRVGPDTERiyddDFFQNLDGVANALDNVDARMYMDRRCVYYRKPLLESGTLGT 609
Cdd:PRK12475    77 QKKPKAIAAKehLRKINSEVEIVPVVTDVTVEELE----ELVKEVDLIIDATDNFDTRLLINDLSQKYNIPWIYGGCVGS 152

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 2217394013  610 KGNVQVVIPFLTESYSssqdppeksipiCTLKNFP 644
Cdd:PRK12475   153 YGVTYTIIPGKTPCLR------------CLMEHVP 175
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 81-204 1.18e-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: 1.18e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013   81 VLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREEDIGKNRAEVSQPRLAELNSYVPVTAYTGPLVE- 159
Cdd:cd01489      2 VLVVGAGGIGCELLKNLVLTGFGEIHIIDLDTIDLSNLNRQFLFRKKHVGKSKAQVAKEAVLSFNPNVKIVAYHANIKDp 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2217394013  160 ----DFLSGFQVVV--LTNtpLEDQLRVGEFCHNRGIKLVVADTRGLFGQL 204
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. ...
 479-587 4.16e-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: 4.16e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  479 LVGAGAIGCELLKNFAMIGLGcgeggEIIVTDMDTIEKSNLNRQFlFRPWDVTKLKSDTAAAAVRQMNPHIRVTSHQNRV 558
Cdd:cd01487      4 IAGAGGLGSNIAVLLARSGVG-----NLKLVDFDVVEPSNLNRQQ-YFLSQIGEPKVEALKENLREINPFVKIEAINIKI 77

                           90       100
                   ....*....|....*....|....*....
gi 2217394013  559 gpDTERIYddDFFQNLDGVANALDNVDAR 587
Cdd:cd01487     78 --DENNLE--GLFGDCDIVVEAFDNAETK 102
PTZ00245 PTZ00245
ubiquitin activating enzyme; Provisional
 61-177 1.88e-07

ubiquitin activating enzyme; Provisional


Pssm-ID: 140272  Cd Length: 287  Bit Score: 53.91  E-value: 1.88e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013   61 YSRQLYVLGHEAMKRLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQfYLREEDIGKNRAEVSQPR 140
Cdd:PTZ00245     9 YDRQIRLWGKSTQQQLMHTSVALHGVAGAAAEAAKNLVLAGVRAVAVADEGLVTDADVCTN-YLMQGEAGGTRGARALGA 87

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2217394013  141 LAELNSYvpVTAYTGPLVEDFLSGFQVVVLTNTPLED 177
Cdd:PTZ00245    88 LQRLNPH--VSVYDAVTKLDGSSGTRVTMAAVITEED 122
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
465-600 2.85e-07

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 53.97  E-value: 2.85e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  465 GSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGcgeggEIIVTDMDTIEKSNLNRQFLFRPWDVTKLKSDTAAAAVRQ 544
Cdd:PRK07411    29 GLEGQKRLKAASVLCIGTGGLGSPLLLYLAAAGIG-----RIGIVDFDVVDSSNLQRQVIHGTSWVGKPKIESAKNRILE 103

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217394013  545 MNPHIRVTSHQNRVGPDTERiyddDFFQNLDGVANALDNVDARMYMDRRCVYYRKP 600
Cdd:PRK07411   104 INPYCQVDLYETRLSSENAL----DILAPYDVVVDGTDNFPTRYLVNDACVLLNKP 155
PRK15116 PRK15116
sulfur acceptor protein CsdL; Provisional
 456-608 5.13e-07

sulfur acceptor protein CsdL; Provisional


Pssm-ID: 185071  Cd Length: 268  Bit Score: 52.50  E-value: 5.13e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  456 RYDGQVAVFGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGCgeggeIIVTDMDTIEKSNLNRQFLFRPWDVTKLKS 535
Cdd:PRK15116    12 RFGGTARLYGEKALQLFADAHICVVGIGGVGSWAAEALARTGIGA-----ITLIDMDDVCVTNTNRQIHALRDNVGLAKA 86

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217394013  536 DTAAAAVRQMNPHIRVTSHQNRVGPDTERIYDDdffQNLDGVANALDNVDARMYMDRRCVYYRKPLLESGTLG 608
Cdd:PRK15116    87 EVMAERIRQINPECRVTVVDDFITPDNVAEYMS---AGFSYVIDAIDSVRPKAALIAYCRRNKIPLVTTGGAG 156
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
 80-155 8.25e-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: 8.25e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217394013   80 SVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREEDIGKNRAEVSQPRLAELNSYVPVTAYTG 155
Cdd:cd01484      1 KVLLVGAGGIGCELLKNLALMGFGQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKSEVAAEAVNDRNPNCKVVPYQN 76
Ube1_repeat1 cd01491
Ubiquitin activating enzyme (E1), repeat 1. E1, a highly conserved small protein present ...
 457-556 1.47e-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: 1.47e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  457 YDGQVAVFGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGcgeggEIIVTDMDTIEKSNLNRQFLFRPWDVTKLKSD 536
Cdd:cd01491      2 YSRQLYVLGHEAMKKLQKSNVLISGLGGLGVEIAKNLILAGVK-----SVTLHDTKPCSWSDLSSQFYLREEDIGKNRAE 76

                           90       100
                   ....*....|....*....|
gi 2217394013  537 TAAAAVRQMNPHIRVTSHQN 556
Cdd:cd01491     77 ASQARLAELNPYVPVTVSTG 96
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 61-160 2.41e-06

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 50.76  E-value: 2.41e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013   61 YSRQLYV--LGHEAMKRLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREEDIGKN--RAEV 136
Cdd:PRK07688     5 YSRQELFspIGEEGQQKLREKHVLIIGAGALGTANAEMLVRAGVGKVTIVDRDYVEWSNLQRQQLYTESDVKNNlpKAVA 84

                           90       100
                   ....*....|....*....|....
gi 2217394013  137 SQPRLAELNSYVPVTAytgpLVED 160
Cdd:PRK07688    85 AKKRLEEINSDVRVEA----IVQD 104
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 61-169 2.42e-06

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 50.23  E-value: 2.42e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013   61 YSRQ--LYVLGHEAMKRLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREEDIGKNRAEVSQ 138
Cdd:PRK05690    13 YNRQiiLRGFDFDGQEKLKAARVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVSLSNLQRQVLHDDATIGQPKVESAR 92

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2217394013  139 PRLAELNSYVPVTAYTGPLVEDFL----SGFQVVV 169
Cdd:PRK05690    93 AALARINPHIAIETINARLDDDELaaliAGHDLVL 127
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 62-154 8.42e-06

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 49.49  E-value: 8.42e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013   62 SRQLYV--LGHEAMKRLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREEDIGKNRAEVSQP 139
Cdd:PRK05600    23 ARQLALpgFGIEQQERLHNARVLVIGAGGLGCPAMQSLASAGVGTITLIDDDTVDVSNIHRQILFGASDVGRPKVEVAAE 102

                           90
                   ....*....|....*
gi 2217394013  140 RLAELNSYVPVTAYT 154
Cdd:PRK05600   103 RLKEIQPDIRVNALR 117
APPBP1_RUB cd01493
Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric ...
 456-571 9.07e-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: 9.07e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  456 RYDGQVAVFGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLgcgegGEIIVTDMDTIEKSNLNRQFLFRPWDVTKLKS 535
Cdd:cd01493      2 KYDRQLRLWGEHGQAALESAHVCLLNATATGTEILKNLVLPGI-----GSFTIVDGSKVDEEDLGNNFFLDASSLGKSRA 76

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2217394013  536 DTAAAAVRQMNPHirVTSHQNRVGPDTERIYDDDFF 571
Cdd:cd01493     77 EATCELLQELNPD--VNGSAVEESPEALLDNDPSFF 110
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 900-955 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 2217394013  900 IATTTAAVVGLVCLELYKVVQGHRqLDSYKNGFLNLALPFFGFSEPLAAPRHQYYN 955
Cdd:pfam00899  183 LGPTTAVVAGLQALEALKLLLGKG-EPNLAGRLLQFDALTMTFRELRLALKNPNCP 237
PRK08223 PRK08223
hypothetical protein; Validated
 469-618 2.54e-05

hypothetical protein; Validated


Pssm-ID: 181302 [Multi-domain]  Cd Length: 287  Bit Score: 47.37  E-value: 2.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  469 QEKLGKQKYFLVGAGAIGCELLKNFAMIGLGCgeggeIIVTDMDTIEKSNLNRQF------LFRPwdvtklKSDTAAAAV 542
Cdd:PRK08223    22 QQRLRNSRVAIAGLGGVGGIHLLTLARLGIGK-----FTIADFDVFELRNFNRQAgammstLGRP------KAEVLAEMV 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  543 RQMNPHIRVTSHQNRVGPDTEriydDDFfqnLDGVANALDNVDARMYMDRRCVY---YRK--PLLESGTLGTKGNVQVVI 617
Cdd:PRK08223    91 RDINPELEIRAFPEGIGKENA----DAF---LDGVDVYVDGLDFFEFDARRLVFaacQQRgiPALTAAPLGMGTALLVFD 163


                   .
gi 2217394013  618 P 618
Cdd:PRK08223   164 P 164
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 61-153 4.83e-05

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 46.65  E-value: 4.83e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013   61 YSRQLYV--LGHEAMKRLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREEDIG--KNRAEV 136
Cdd:PRK12475     5 YSRQILFsgIGEEGQRKIREKHVLIVGAGALGAANAEALVRAGIGKLTIADRDYVEWSNLQRQQLYTEEDAKqkKPKAIA 84

                           90
                   ....*....|....*..
gi 2217394013  137 SQPRLAELNSYVPVTAY 153
Cdd:PRK12475    85 AKEHLRKINSEVEIVPV 101
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
61-169 9.10e-05

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 46.16  E-value: 9.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013   61 YSRQLYV--LGHEAMKRLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREEDIGKNRAEVSQ 138
Cdd:PRK08762   116 YSRHLRLpeVGEEGQRRLLEARVLLIGAGGLGSPAALYLAAAGVGTLGIVDHDVVDRSNLQRQILHTEDRVGQPKVDSAA 195

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2217394013  139 PRLAELNSYVPVTAY----TGPLVEDFLSGFQVVV 169
Cdd:PRK08762   196 QRLAALNPDVQVEAVqervTSDNVEALLQDVDVVV 230
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
 80-169 1.10e-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: 1.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013   80 SVLVSGLRGLGVEIAKNIILGGVKA-----VTLHDQGTAQWADLSSQFYLREEDIGKNRAEVSQPRLAELNSYVPVTAYT 154
Cdd:cd01490      1 KVFLVGAGAIGCELLKNFALMGVGTgesgeITVTDMDNIEKSNLNRQFLFRPHDVGKPKSEVAAAAVKAMNPDLKITALQ 80

                           90       100
                   ....*....|....*....|...
gi 2217394013  155 ---GPLVE-----DFLSGFQVVV 169
Cdd:cd01490     81 nrvGPETEhifndEFWEKLDGVA 103
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
55-169 3.65e-04

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 42.92  E-value: 3.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013   55 DIDEGLYSRqlyvLGHEAMKRLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYlREEDIGKNRA 134
Cdd:PRK08644     9 EFEAMLASR----HTPKLLEKLKKAKVGIAGAGGLGSNIAVALARSGVGNLKLVDFDVVEPSNLNRQQY-FISQIGMPKV 83

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2217394013  135 EVSQPRLAELNSYVPVTAY----TGPLVEDFLSGFQVVV 169
Cdd:PRK08644    84 EALKENLLEINPFVEIEAHnekiDEDNIEELFKDCDIVV 122
PRK14851 PRK14851
hypothetical protein; Provisional
 461-618 5.10e-04

hypothetical protein; Provisional


Pssm-ID: 184853 [Multi-domain]  Cd Length: 679  Bit Score: 44.08  E-value: 5.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  461 VAVFGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGcgeggEIIVTDMDTIEKSNLNRQFLFRPWDVTKLKSDTAAA 540
Cdd:PRK14851    30 IGLFTPGEQERLAEAKVAIPGMGGVGGVHLITMVRTGIG-----RFHIADFDQFEPVNVNRQFGARVPSFGRPKLAVMKE 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  541 AVRQMNPHIRVTshqnrvgPDTERIYDDDFFQNLDGVANALDNVDARMYMDRRCVYYRK-----PLLESGTLGTKGNVQV 615
Cdd:PRK14851   105 QALSINPFLEIT-------PFPAGINADNMDAFLDGVDVVLDGLDFFQFEIRRTLFNMArekgiPVITAGPLGYSSAMLV 177


                   ...
gi 2217394013  616 VIP 618
Cdd:PRK14851   178 FTP 180
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 61-150 5.75e-04

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 43.54  E-value: 5.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013   61 YSRQLYV--LGHEAMKRLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREEDIGKNRAEVSQ 138
Cdd:PRK07878    23 YSRHLIIpdVGVDGQKRLKNARVLVIGAGGLGSPTLLYLAAAGVGTLGIVEFDVVDESNLQRQVIHGQSDVGRSKAQSAR 102

                           90
                   ....*....|..
gi 2217394013  139 PRLAELNSYVPV 150
Cdd:PRK07878   103 DSIVEINPLVNV 114
E1_ThiF_like cd01487
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ...
 80-152 1.11e-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: 1.11e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217394013   80 SVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYlREEDIGKNRAEVSQPRLAELNSYVPVTA 152
Cdd:cd01487      1 KVGIAGAGGLGSNIAVLLARSGVGNLKLVDFDVVEPSNLNRQQY-FLSQIGEPKVEALKENLREINPFVKIEA 72
Apg7 cd01486
Apg7 is an E1-like protein, that activates two different ubiquitin-like proteins, Apg12 and ...
 476-554 1.29e-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: 1.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  476 KYFLVGAGAIGCellkNFAMIGLGCGEgGEIIVTDMDTIEKSNLNRQFLFRPWDVT--KLKSDTAAAAVRQMNPHIRVTS 553
Cdd:cd01486      1 KCLLLGAGTLGC----NVARNLLGWGV-RHITFVDSGKVSYSNPVRQSLFTFEDCKggKPKAEAAAERLKEIFPSIDATG 75


                   .
gi 2217394013  554 H 554
Cdd:cd01486     76 I 76
PRK14852 PRK14852
hypothetical protein; Provisional
 469-618 6.69e-03

hypothetical protein; Provisional


Pssm-ID: 184854 [Multi-domain]  Cd Length: 989  Bit Score: 40.45  E-value: 6.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217394013  469 QEKLGKQKYFLVGAGAIGCELLKNFAMIGLGcgeggEIIVTDMDTIEKSNLNRQFLFRPWDVTKLKSDTAAAAVRQMNPH 548
Cdd:PRK14852   327 QRRLLRSRVAIAGLGGVGGIHLMTLARTGIG-----NFNLADFDAYSPVNLNRQYGASIASFGRGKLDVMTERALSVNPF 401

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217394013  549 IRVTSHQNRVGPDTeriyDDDFFQNLDGVANALD--NVDARMYMDRRCVYYRKPLLESGTLGTKGNVQVVIP 618
Cdd:PRK14852   402 LDIRSFPEGVAAET----IDAFLKDVDLLVDGIDffALDIRRRLFNRALELGIPVITAGPLGYSCALLVFMP 469
PRK07877 PRK07877
Rv1355c family protein;
128-201 7.46e-03

Rv1355c family protein;


Pssm-ID: 236122 [Multi-domain]  Cd Length: 722  Bit Score: 40.36  E-value: 7.46e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217394013  128 DIGKNRAEVSQPRLAELNSYVPVTAYTGPL----VEDFLSGFQVVVLTNTPLEDQLRVGEFCHNRGIKLVVA-DTRGLF 201
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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