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Conserved domains on  [gi|19113852|ref|NP_592940|]
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NEDD8-activating enzyme uba3 [Schizosaccharomyces pombe]

Protein Classification

NEDD8-activating enzyme E1 catalytic subunit( domain architecture ID 10107293)

NEDD8-activating enzyme E1 catalytic subunit activates NEDD8 by first adenylating its C-terminal glycine residue with ATP, thereafter linking this residue to the side chain of the catalytic cysteine, yielding a NEDD8-UBA3 thioester and free AMP

CATH:  3.10.20.260|1.10.10.520|3.40.50.720
EC:  6.2.1.64
Gene Ontology:  GO:0005524|GO:0005515|GO:0019781|GO:0019788|GO:0006508|GO:0045116
SCOP:  4000345|4004110

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 46-354 0e+00

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: 538.87  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113852  46 KILIIGAGGLGCEILKDLALSGFRDLSVIDMDTIDITNLNRQFLFNESNIDEPKANVAASMIMKRIPSTVVTPFYGKIQD 125
Cdd:cd01488   1 KILVIGAGGLGCELLKNLALSGFRNIHVIDMDTIDVSNLNRQFLFREKDIGKPKAEVAAKFVNDRVPGVNVTPHFGKIQD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113852 126 KTIEFYKEFKLIICGLDSVEARRWINSTLVAIA---KTGDLIPLVDGGSEGLKGQARVIIPTITSCYECSLDMLTPKISY 202
Cdd:cd01488  81 KDEEFYRQFNIIICGLDSIEARRWINGTLVSLLlyeDPESIIPLIDGGTEGFKGHARVILPGITACIECSLDLFPPQVTF 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113852 203 PICTLANTPRLPEHCVEWAYLLEWPRVFLNAsvdsfskqevfepldgknsNFEPDNIRHIDWLVKRSIERANKFQIPSSS 282
Cdd:cd01488 161 PLCTIANTPRLPEHCIEYASLIQWPKEFPFV-------------------PLDGDDPEHIEWLYQKALERAAQFNISGVT 221

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19113852 283 InrFFVQGIVKRIIPAVASTNAIIAASCCNEALKILTESNPFLDNYMMYVGEDGAYTYTFNLEKRSDCPVCG 354
Cdd:cd01488 222 Y--SLTQGVVKRIIPAVASTNAIIAAACCLEALKIATDCYENLNNYLMYNGVDGCYTYTFEHERKEDCPVCS 291
E2_bind pfam08825
E2 binding domain; E1 and E2 enzymes play a central role in ubiquitin and ubiquitin-like ...
 365-442 1.39e-15

E2 binding domain; E1 and E2 enzymes play a central role in ubiquitin and ubiquitin-like protein transfer cascades. This is an E2 binding domain that is found on NEDD8 activating E1 enzyme. The domain resembles ubiquitin, and recruits the catalytic core of the E2 enzyme Ubc12 in a similar manner to that in which ubiquitin interacts with ubiquitin binding domains.


:

Pssm-ID: 462611  Cd Length: 81  Bit Score: 71.38  E-value: 1.39e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113852   365 SSTVTLKDILNHYSKS--YNLQNPSVSTAaGTPLYLASPPALQVATSKNLSQPILSITSVDVNLVITDKNLSTSLSVQLR 442
Cdd:pfam08825   2 SPSWTLQELIDSLAERpeLQLKKPSLSTE-GKTLYMQSPPSLEEATRPNLSKKLKELVEDGEEITVTDPTLPSTISLRLR 80
 
Name Accession Description Interval E-value
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 46-354 0e+00

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: 538.87  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113852  46 KILIIGAGGLGCEILKDLALSGFRDLSVIDMDTIDITNLNRQFLFNESNIDEPKANVAASMIMKRIPSTVVTPFYGKIQD 125
Cdd:cd01488   1 KILVIGAGGLGCELLKNLALSGFRNIHVIDMDTIDVSNLNRQFLFREKDIGKPKAEVAAKFVNDRVPGVNVTPHFGKIQD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113852 126 KTIEFYKEFKLIICGLDSVEARRWINSTLVAIA---KTGDLIPLVDGGSEGLKGQARVIIPTITSCYECSLDMLTPKISY 202
Cdd:cd01488  81 KDEEFYRQFNIIICGLDSIEARRWINGTLVSLLlyeDPESIIPLIDGGTEGFKGHARVILPGITACIECSLDLFPPQVTF 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113852 203 PICTLANTPRLPEHCVEWAYLLEWPRVFLNAsvdsfskqevfepldgknsNFEPDNIRHIDWLVKRSIERANKFQIPSSS 282
Cdd:cd01488 161 PLCTIANTPRLPEHCIEYASLIQWPKEFPFV-------------------PLDGDDPEHIEWLYQKALERAAQFNISGVT 221

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19113852 283 InrFFVQGIVKRIIPAVASTNAIIAASCCNEALKILTESNPFLDNYMMYVGEDGAYTYTFNLEKRSDCPVCG 354
Cdd:cd01488 222 Y--SLTQGVVKRIIPAVASTNAIIAAACCLEALKIATDCYENLNNYLMYNGVDGCYTYTFEHERKEDCPVCS 291
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 28-210 4.20e-53

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: 177.83  E-value: 4.20e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113852    28 NLDAPENPEETLKSAFSSKILIIGAGGLGCEILKDLALSGFRDLSVIDMDTIDITNLNRQFLFNESNIDEPKANVAASMI 107
Cdd:pfam00899   4 QLALPLIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAAERL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113852   108 MKRIPSTVVTPFYGKIQDKTI-EFYKEFKLIICGLDSVEARRWINstlVAIAKTGdlIPLVDGGSEGLKGQARVIIPTIT 186
Cdd:pfam00899  84 REINPDVEVEAYTERLTPENAeELIKSFDIVVDATDNFAARYLVN---DACVKLG--KPLIEAGVLGFKGQVTVVIPGKT 158

                         170       180
                  ....*....|....*....|....
gi 19113852   187 SCYECSLDMLTPKISYPICTLANT 210
Cdd:pfam00899 159 PCYRCLFPEDPPPKLVPSCTVAGV 182
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 44-354 1.47e-39

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: 142.19  E-value: 1.47e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113852  44 SSKILIIGAGGLGCEILKDLALSGFRDLSVIDMDTIDITNLNRQFLFNESNIDEPKANVAASMIMKRIPSTVVTPFYGKI 123
Cdd:COG0476  27 AARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADVGRPKVEAAAERLRALNPDVEVEAIPERL 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113852 124 QDKTI-EFYKEFKLIICGLDSVEARRWINStlvAIAKTGdlIPLVDGGSEGLKGQARVIIPTITSCYECsldmLTPkisy 202
Cdd:COG0476 107 TEENAlELLAGADLVLDCTDNFATRYLLND---ACVKLG--IPLVSGAVIGFEGQVTVFIPGDTPCYRC----LFP---- 173

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113852 203 pictlaNTPRLPEHCVEwayllewprvflnasvdsfskqevfepldgknsnfepdnirhidwlvkrsierankfqipsss 282
Cdd:COG0476 174 ------EPPEPGPSCAE--------------------------------------------------------------- 184

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19113852 283 inrffvqgivkriIPAVASTNAIIAASCCNEALKILTESNPFLDNYMMYVgeDGAY--TYTFNLEKRSDCPVCG 354
Cdd:COG0476 185 -------------AGVLGPLVGVIGSLQATEAIKLLTGIGEPLAGRLLLF--DALTmeFRTIKLPRDPDCPVCG 243
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 44-268 9.30e-37

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: 143.49  E-value: 9.30e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113852     44 SSKILIIGAGGLGCEILKDLALSGFR-----DLSVIDMDTIDITNLNRQFLFNESNIDEPKANVAASMIMKRIPSTVVTP 118
Cdd:TIGR01408  419 NLNIFLVGCGAIGCEMLKNFALMGVGtgkkgMITVTDPDLIEKSNLNRQFLFRPHHIGKPKSYTAADATLKINPQIKIDA 498

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113852    119 FYGKI--QDKTI---EFYKEFKLIICGLDSVEARRWINSTLVAIAKtgdliPLVDGGSEGLKGQARVIIPTITSCYECSL 193
Cdd:TIGR01408  499 HQNRVgpETETIfndEFYEKLDVVINALDNVEARRYVDSRCLAFLK-----PLLESGTLGTKGNTQVVVPHLTESYGSSR 573

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113852    194 DmlTPKISYPICTLANTPRLPEHCVEWAY-----LLEWPRVFLNASVDSFSK-QEVFEPLDGKNSNFEPDNIRhiDWLVK 267
Cdd:TIGR01408  574 D--PPEKEIPFCTLKSFPAAIEHTIQWARdkfegLFSHKPSLVNKYLSSPSSaEEVLQKIQSGHSREGLEQII--KLLSK 649


                   .
gi 19113852    268 R 268
Cdd:TIGR01408  650 E 650
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 37-191 1.16e-18

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 84.90  E-value: 1.16e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113852   37 ETLKSAfssKILIIGAGGLGCEILKDLALSGFRDLSVIDMDTIDITNLNRQFLFNESNIDEPKANVAASMIMKRIPSTVV 116
Cdd:PRK05690  28 EKLKAA---RVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVSLSNLQRQVLHDDATIGQPKVESARAALARINPHIAI 104

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19113852  117 TPFYGKIQDKTI-EFYKEFKLIICGLDSVEARRWINSTLVAiAKTgdliPLVDGGSEGLKGQARVIIPTITS-CYEC 191
Cdd:PRK05690 105 ETINARLDDDELaALIAGHDLVLDCTDNVATRNQLNRACFA-AKK----PLVSGAAIRMEGQVTVFTYQDDEpCYRC 176
E2_bind pfam08825
E2 binding domain; E1 and E2 enzymes play a central role in ubiquitin and ubiquitin-like ...
 365-442 1.39e-15

E2 binding domain; E1 and E2 enzymes play a central role in ubiquitin and ubiquitin-like protein transfer cascades. This is an E2 binding domain that is found on NEDD8 activating E1 enzyme. The domain resembles ubiquitin, and recruits the catalytic core of the E2 enzyme Ubc12 in a similar manner to that in which ubiquitin interacts with ubiquitin binding domains.


Pssm-ID: 462611  Cd Length: 81  Bit Score: 71.38  E-value: 1.39e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113852   365 SSTVTLKDILNHYSKS--YNLQNPSVSTAaGTPLYLASPPALQVATSKNLSQPILSITSVDVNLVITDKNLSTSLSVQLR 442
Cdd:pfam08825   2 SPSWTLQELIDSLAERpeLQLKKPSLSTE-GKTLYMQSPPSLEEATRPNLSKKLKELVEDGEEITVTDPTLPSTISLRLR 80
 
Name Accession Description Interval E-value
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 46-354 0e+00

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: 538.87  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113852  46 KILIIGAGGLGCEILKDLALSGFRDLSVIDMDTIDITNLNRQFLFNESNIDEPKANVAASMIMKRIPSTVVTPFYGKIQD 125
Cdd:cd01488   1 KILVIGAGGLGCELLKNLALSGFRNIHVIDMDTIDVSNLNRQFLFREKDIGKPKAEVAAKFVNDRVPGVNVTPHFGKIQD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113852 126 KTIEFYKEFKLIICGLDSVEARRWINSTLVAIA---KTGDLIPLVDGGSEGLKGQARVIIPTITSCYECSLDMLTPKISY 202
Cdd:cd01488  81 KDEEFYRQFNIIICGLDSIEARRWINGTLVSLLlyeDPESIIPLIDGGTEGFKGHARVILPGITACIECSLDLFPPQVTF 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113852 203 PICTLANTPRLPEHCVEWAYLLEWPRVFLNAsvdsfskqevfepldgknsNFEPDNIRHIDWLVKRSIERANKFQIPSSS 282
Cdd:cd01488 161 PLCTIANTPRLPEHCIEYASLIQWPKEFPFV-------------------PLDGDDPEHIEWLYQKALERAAQFNISGVT 221

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19113852 283 InrFFVQGIVKRIIPAVASTNAIIAASCCNEALKILTESNPFLDNYMMYVGEDGAYTYTFNLEKRSDCPVCG 354
Cdd:cd01488 222 Y--SLTQGVVKRIIPAVASTNAIIAAACCLEALKIATDCYENLNNYLMYNGVDGCYTYTFEHERKEDCPVCS 291
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
 46-315 4.73e-88

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: 267.91  E-value: 4.73e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113852  46 KILIIGAGGLGCEILKDLALSGFRDLSVIDMDTIDITNLNRQFLFNESNIDEPKANVAASMIMKRIPSTVVTPFYGKIQD 125
Cdd:cd01484   1 KVLLVGAGGIGCELLKNLALMGFGQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKSEVAAEAVNDRNPNCKVVPYQNKVGP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113852 126 KTI---EFYKEFKLIICGLDSVEARRWINSTLVAIAKtgdliPLVDGGSEGLKGQARVIIPTITSCYECSLDmlTPKISY 202
Cdd:cd01484  81 EQDfndTFFEQFHIIVNALDNIIARRYVNGMLIFLIV-----PLIESGTEGFKGNAQVILPGMTECIECTLY--PPQKNF 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113852 203 PICTLANTPRLPEHCVEWAYLLEWprvflnasvdsfskqevfepldgknsnfepDNIRHIDWLVKRSIERANKFQIPSSS 282
Cdd:cd01484 154 PMCTIASMPRLPEHCIEWARMLQW------------------------------DDPEHIQFIFQASNERASQYNIRGVT 203

                       250       260       270
                ....*....|....*....|....*....|...
gi 19113852 283 inRFFVQGIVKRIIPAVASTNAIIAASCCNEAL 315
Cdd:cd01484 204 --YFLTKGVAGRIIPAVATTNAVVAGVCALEVF 234
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 46-318 3.27e-73

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: 232.66  E-value: 3.27e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113852  46 KILIIGAGGLGCEILKDLALSGFRDLSVIDMDTIDITNLNRQFLFNESNIDEPKANVAASMIMKRIPSTVVTPFYGKIQD 125
Cdd:cd01489   1 KVLVVGAGGIGCELLKNLVLTGFGEIHIIDLDTIDLSNLNRQFLFRKKHVGKSKAQVAKEAVLSFNPNVKIVAYHANIKD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113852 126 KT--IEFYKEFKLIICGLDSVEARRWINSTLVAIAktgdlIPLVDGGSEGLKGQARVIIPTITSCYECSlDMLTPKiSYP 203
Cdd:cd01489  81 PDfnVEFFKQFDLVFNALDNLAARRHVNKMCLAAD-----VPLIESGTTGFLGQVQVIKKGKTECYECQ-PKETPK-TFP 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113852 204 ICTLANTPRLPEHCVEWA--YLLEWPRVF------LNASVDSFSKQEVFEPLDGKNSNFEPDNIRHIDWLVKRSIERANK 275
Cdd:cd01489 154 VCTIRSTPSQPIHCIVWAksLFFLFNKVFkddierLLSMEELWKTRKPPVPLSWKELTFDKDDQDALDFVAAAANLRSHV 233

                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 19113852 276 FQIPSSSinRFFVQGIVKRIIPAVASTNAIIAASCCNEALKIL 318
Cdd:cd01489 234 FGIPMKS--RFDIKQMAGNIIPAIATTNAIIAGLIVLEALKVL 274
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 28-210 4.20e-53

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: 177.83  E-value: 4.20e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113852    28 NLDAPENPEETLKSAFSSKILIIGAGGLGCEILKDLALSGFRDLSVIDMDTIDITNLNRQFLFNESNIDEPKANVAASMI 107
Cdd:pfam00899   4 QLALPLIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAAERL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113852   108 MKRIPSTVVTPFYGKIQDKTI-EFYKEFKLIICGLDSVEARRWINstlVAIAKTGdlIPLVDGGSEGLKGQARVIIPTIT 186
Cdd:pfam00899  84 REINPDVEVEAYTERLTPENAeELIKSFDIVVDATDNFAARYLVN---DACVKLG--KPLIEAGVLGFKGQVTVVIPGKT 158

                         170       180
                  ....*....|....*....|....
gi 19113852   187 SCYECSLDMLTPKISYPICTLANT 210
Cdd:pfam00899 159 PCYRCLFPEDPPPKLVPSCTVAGV 182
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
 46-324 6.52e-44

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: 158.99  E-value: 6.52e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113852  46 KILIIGAGGLGCEILKDLALSGFR-----DLSVIDMDTIDITNLNRQFLFNESNIDEPKANVAASMIMKRIPSTVVTPFY 120
Cdd:cd01490   1 KVFLVGAGAIGCELLKNFALMGVGtgesgEITVTDMDNIEKSNLNRQFLFRPHDVGKPKSEVAAAAVKAMNPDLKITALQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113852 121 GKIQDKT-----IEFYKEFKLIICGLDSVEARRWINSTLVAIAKtgdliPLVDGGSEGLKGQARVIIPTITSCYECSLDm 195
Cdd:cd01490  81 NRVGPETehifnDEFWEKLDGVANALDNVDARMYVDRRCVYYRK-----PLLESGTLGTKGNTQVVIPHLTESYSSSRD- 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113852 196 lTPKISYPICTLANTPRLPEHCVEWA-----------------YLLE----WPRVFLNasvDSFS---KQEVFE-PLDGK 250
Cdd:cd01490 155 -PPEKSIPLCTLKNFPNAIEHTIQWArdefeglfkqppenvnqYLFEdcvrWARLLFE---KYFNnniKQLLHNfPPDAV 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113852 251 NSN----------------FEPDNIRHIDWLVKRSIERANKFQIPS---------------------------SSINRFF 287
Cdd:cd01490 231 TSDgapfwsgpkrcptpleFDVNNPLHLDFVLAAANLYAEVYGIPGfekdddtnfhmdfitaasnlrarnysiPPADRHK 310

                       330       340       350
                ....*....|....*....|....*....|....*..
gi 19113852 288 VQGIVKRIIPAVASTNAIIAASCCNEALKILTESNPF 324
Cdd:cd01490 311 TKRIAGKIIPAIATTTAAVTGLVCLELYKVVDGKRPL 347
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 44-354 1.47e-39

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: 142.19  E-value: 1.47e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113852  44 SSKILIIGAGGLGCEILKDLALSGFRDLSVIDMDTIDITNLNRQFLFNESNIDEPKANVAASMIMKRIPSTVVTPFYGKI 123
Cdd:COG0476  27 AARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADVGRPKVEAAAERLRALNPDVEVEAIPERL 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113852 124 QDKTI-EFYKEFKLIICGLDSVEARRWINStlvAIAKTGdlIPLVDGGSEGLKGQARVIIPTITSCYECsldmLTPkisy 202
Cdd:COG0476 107 TEENAlELLAGADLVLDCTDNFATRYLLND---ACVKLG--IPLVSGAVIGFEGQVTVFIPGDTPCYRC----LFP---- 173

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113852 203 pictlaNTPRLPEHCVEwayllewprvflnasvdsfskqevfepldgknsnfepdnirhidwlvkrsierankfqipsss 282
Cdd:COG0476 174 ------EPPEPGPSCAE--------------------------------------------------------------- 184

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19113852 283 inrffvqgivkriIPAVASTNAIIAASCCNEALKILTESNPFLDNYMMYVgeDGAY--TYTFNLEKRSDCPVCG 354
Cdd:COG0476 185 -------------AGVLGPLVGVIGSLQATEAIKLLTGIGEPLAGRLLLF--DALTmeFRTIKLPRDPDCPVCG 243
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 46-191 9.79e-39

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: 136.63  E-value: 9.79e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113852  46 KILIIGAGGLGCEILKDLALSGFRDLSVIDMDTIDITNLNRQFLFNESNIDEPKANVAASMIMKRIPSTVVTPFYGKIQ- 124
Cdd:cd01483   1 RVLLVGLGGLGSEIALNLARSGVGKITLIDFDTVELSNLNRQFLARQADIGKPKAEVAARRLNELNPGVNVTAVPEGISe 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19113852 125 DKTIEFYKEFKLIICGLDSVEARRWINSTLVAIAktgdlIPLVDGGSEGLKGQARVIIPTITSCYEC 191
Cdd:cd01483  81 DNLDDFLDGVDLVIDAIDNIAVRRALNRACKELG-----IPVIDAGGLGLGGDIQVIDIGSLSAAEA 142
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 44-268 9.30e-37

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: 143.49  E-value: 9.30e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113852     44 SSKILIIGAGGLGCEILKDLALSGFR-----DLSVIDMDTIDITNLNRQFLFNESNIDEPKANVAASMIMKRIPSTVVTP 118
Cdd:TIGR01408  419 NLNIFLVGCGAIGCEMLKNFALMGVGtgkkgMITVTDPDLIEKSNLNRQFLFRPHHIGKPKSYTAADATLKINPQIKIDA 498

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113852    119 FYGKI--QDKTI---EFYKEFKLIICGLDSVEARRWINSTLVAIAKtgdliPLVDGGSEGLKGQARVIIPTITSCYECSL 193
Cdd:TIGR01408  499 HQNRVgpETETIfndEFYEKLDVVINALDNVEARRYVDSRCLAFLK-----PLLESGTLGTKGNTQVVVPHLTESYGSSR 573

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113852    194 DmlTPKISYPICTLANTPRLPEHCVEWAY-----LLEWPRVFLNASVDSFSK-QEVFEPLDGKNSNFEPDNIRhiDWLVK 267
Cdd:TIGR01408  574 D--PPEKEIPFCTLKSFPAAIEHTIQWARdkfegLFSHKPSLVNKYLSSPSSaEEVLQKIQSGHSREGLEQII--KLLSK 649


                   .
gi 19113852    268 R 268
Cdd:TIGR01408  650 E 650
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 44-191 5.62e-31

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


Pssm-ID: 238386 [Multi-domain]  Cd Length: 228  Bit Score: 118.73  E-value: 5.62e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113852  44 SSKILIIGAGGLGCEILKDLALSGFRDLSVIDMDTIDITNLNRQFLFNESNIDEPKANVAASMIMKRIPSTVVTPFYGKI 123
Cdd:cd00757  21 NARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRQILHTEADVGQPKAEAAAERLRAINPDVEIEAYNERL 100

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19113852 124 QDKTIE-FYKEFKLIICGLDSVEARRWINStlvAIAKTGdlIPLVDGGSEGLKGQARVIIPTITSCYEC 191
Cdd:cd00757 101 DAENAEeLIAGYDLVLDCTDNFATRYLIND---ACVKLG--KPLVSGAVLGFEGQVTVFIPGEGPCYRC 164
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 37-191 1.16e-18

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 84.90  E-value: 1.16e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113852   37 ETLKSAfssKILIIGAGGLGCEILKDLALSGFRDLSVIDMDTIDITNLNRQFLFNESNIDEPKANVAASMIMKRIPSTVV 116
Cdd:PRK05690  28 EKLKAA---RVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVSLSNLQRQVLHDDATIGQPKVESARAALARINPHIAI 104

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19113852  117 TPFYGKIQDKTI-EFYKEFKLIICGLDSVEARRWINSTLVAiAKTgdliPLVDGGSEGLKGQARVIIPTITS-CYEC 191
Cdd:PRK05690 105 ETINARLDDDELaALIAGHDLVLDCTDNVATRNQLNRACFA-AKK----PLVSGAAIRMEGQVTVFTYQDDEpCYRC 176
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 43-167 5.66e-16

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 79.15  E-value: 5.66e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113852   43 FSSKILIIGAGGLGCEILKDLALSGFRDLSVIDMDTIDITNLNRQFLFNESNIDEPKANVAASMIMKRIPSTVVTPFYGK 122
Cdd:PRK05600  40 HNARVLVIGAGGLGCPAMQSLASAGVGTITLIDDDTVDVSNIHRQILFGASDVGRPKVEVAAERLKEIQPDIRVNALRER 119

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 19113852  123 IQ-DKTIEFYKEFKLIICGLDSVEARrwinsTLVAIAKTGDLIPLV 167
Cdd:PRK05600 120 LTaENAVELLNGVDLVLDGSDSFATK-----FLVADAAEITGTPLV 160
E2_bind pfam08825
E2 binding domain; E1 and E2 enzymes play a central role in ubiquitin and ubiquitin-like ...
 365-442 1.39e-15

E2 binding domain; E1 and E2 enzymes play a central role in ubiquitin and ubiquitin-like protein transfer cascades. This is an E2 binding domain that is found on NEDD8 activating E1 enzyme. The domain resembles ubiquitin, and recruits the catalytic core of the E2 enzyme Ubc12 in a similar manner to that in which ubiquitin interacts with ubiquitin binding domains.


Pssm-ID: 462611  Cd Length: 81  Bit Score: 71.38  E-value: 1.39e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113852   365 SSTVTLKDILNHYSKS--YNLQNPSVSTAaGTPLYLASPPALQVATSKNLSQPILSITSVDVNLVITDKNLSTSLSVQLR 442
Cdd:pfam08825   2 SPSWTLQELIDSLAERpeLQLKKPSLSTE-GKTLYMQSPPSLEEATRPNLSKKLKELVEDGEEITVTDPTLPSTISLRLR 80
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 45-194 4.22e-15

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 76.18  E-value: 4.22e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113852   45 SKILIIGAGGLGCEILKDLALSGFRDLSVIDMDTIDITNLNRQFLFNESNIDE--PKAnVAASMIMKRIPSTV-VTPFyg 121
Cdd:PRK07688  25 KHVLIIGAGALGTANAEMLVRAGVGKVTIVDRDYVEWSNLQRQQLYTESDVKNnlPKA-VAAKKRLEEINSDVrVEAI-- 101

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19113852  122 kIQDKTIEFYKEF----KLIICGLDSVEARRWINStlvAIAKTGdlIPLVDGGSEGLKGQARVIIPTITSCYECSLD 194
Cdd:PRK07688 102 -VQDVTAEELEELvtgvDLIIDATDNFETRFIVND---AAQKYG--IPWIYGACVGSYGLSYTIIPGKTPCLRCLLQ 172
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
44-191 2.09e-14

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 74.28  E-value: 2.09e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113852   44 SSKILIIGAGGLGCEILKDLALSGFRDLSVIDMDTIDITNLNRQFLFNESNIDEPKANVAASMIMKRIPSTVVTPFYGKI 123
Cdd:PRK08762 135 EARVLLIGAGGLGSPAALYLAAAGVGTLGIVDHDVVDRSNLQRQILHTEDRVGQPKVDSAAQRLAALNPDVQVEAVQERV 214

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19113852  124 QDKTIE-FYKEFKLIICGLDSVEARRWINSTLVAIAKtgdliPLVDGGSEGLKGQARVIIPTITS----CYEC 191
Cdd:PRK08762 215 TSDNVEaLLQDVDVVVDGADNFPTRYLLNDACVKLGK-----PLVYGAVFRFEGQVSVFDAGRQRgqapCYRC 282
PRK08328 PRK08328
hypothetical protein; Provisional
 36-200 2.36e-14

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 72.14  E-value: 2.36e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113852   36 EETLKSAfssKILIIGAGGLGCEILKDLALSGFRDLSVIDMDTIDITNLNRQFLFNESNIDEPKANVAASMIMKRIPSTV 115
Cdd:PRK08328  22 QEKLKKA---KVAVVGVGGLGSPVAYYLAAAGVGRILLIDEQTPELSNLNRQILHWEEDLGKNPKPLSAKWKLERFNSDI 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113852  116 -VTPFYGKIQDKTI-EFYKEFKLIICGLDSVEARRWINSTlvaIAKTGdlIPLVDGGSEGLKGQARVIIPTITScyecSL 193
Cdd:PRK08328  99 kIETFVGRLSEENIdEVLKGVDVIVDCLDNFETRYLLDDY---AHKKG--IPLVHGAVEGTYGQVTTIVPGKTK----RL 169


                 ....*..
gi 19113852  194 DMLTPKI 200
Cdd:PRK08328 170 REIFPKV 176
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 44-194 6.97e-14

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 72.46  E-value: 6.97e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113852   44 SSKILIIGAGGLGCEILKDLALSGFRDLSVIDMDTIDITNLNRQFLFNESNIDE--PKAnVAASMIMKRIPSTV-VTPFY 120
Cdd:PRK12475  24 EKHVLIVGAGALGAANAEALVRAGIGKLTIADRDYVEWSNLQRQQLYTEEDAKQkkPKA-IAAKEHLRKINSEVeIVPVV 102

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19113852  121 GKIQDKTIE-FYKEFKLIICGLDSVEARRWINStlvaIA-KTGdlIPLVDGGSEGLKGQARVIIPTITSCYECSLD 194
Cdd:PRK12475 103 TDVTVEELEeLVKEVDLIIDATDNFDTRLLIND----LSqKYN--IPWIYGGCVGSYGVTYTIIPGKTPCLRCLME 172
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 39-180 8.15e-13

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 69.74  E-value: 8.15e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113852   39 LKSAfssKILIIGAGGLGCEILKDLALSGFRDLSVIDMDTIDITNLNRQFLFNESNIDEPKANVAASMIMKRIPSTVVTP 118
Cdd:PRK07878  40 LKNA---RVLVIGAGGLGSPTLLYLAAAGVGTLGIVEFDVVDESNLQRQVIHGQSDVGRSKAQSARDSIVEINPLVNVRL 116

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19113852  119 FYGKIQ-DKTIEFYKEFKLIICGLDSVEARRWINSTLVAIAKtgdliPLVDGGSEGLKGQARV 180
Cdd:PRK07878 117 HEFRLDpSNAVELFSQYDLILDGTDNFATRYLVNDAAVLAGK-----PYVWGSIYRFEGQASV 174
E1-1_like cd01485
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ...
 44-188 1.69e-12

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


Pssm-ID: 238762 [Multi-domain]  Cd Length: 198  Bit Score: 65.91  E-value: 1.69e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113852  44 SSKILIIGAGGLGCEILKDLALSGFRDLSVIDMDTIDITNLNRQFLF--NESNIDEPKANVAASMIMK---RIPSTVVTP 118
Cdd:cd01485  19 SAKVLIIGAGALGAEIAKNLVLAGIDSITIVDHRLVSTEDLGSNFFLdaEVSNSGMNRAAASYEFLQElnpNVKLSIVEE 98

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19113852 119 FYGKIQDKTIEFYKEFKLIICgLDSVEARrwinstlvaIAKTGDL-----IPLVDGGSEGLKGQARVIIPtITSC 188
Cdd:cd01485  99 DSLSNDSNIEEYLQKFTLVIA-TEENYER---------TAKVNDVcrkhhIPFISCATYGLIGYAFFDFP-IAAF 162
Aos1_SUMO cd01492
Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating ...
 44-176 2.32e-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: 65.77  E-value: 2.32e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113852  44 SSKILIIGAGGLGCEILKDLALSGFRDLSVIDMDTIDITNLNRQFLFNESNIDEPKANVAASMIMKRIPSTVVTPFYGKI 123
Cdd:cd01492  21 SARILLIGLKGLGAEIAKNLVLSGIGSLTILDDRTVTEEDLGAQFLIPAEDLGQNRAEASLERLRALNPRVKVSVDTDDI 100

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 19113852 124 QDKTIEFYKEFKLIICG-LDSVEARRwINSTlvaiakTGDL-IPLVDGGSEGLKG 176
Cdd:cd01492 101 SEKPEEFFSQFDVVVATeLSRAELVK-INEL------CRKLgVKFYATGVHGLFG 148
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
37-154 9.57e-12

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 64.11  E-value: 9.57e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113852   37 ETLKSAfssKILIIGAGGLGCEILKDLALSGFRDLSVIDMDTIDITNLNRQFLFnESNIDEPKANvAASMIMKRI-PSTV 115
Cdd:PRK08644  24 EKLKKA---KVGIAGAGGLGSNIAVALARSGVGNLKLVDFDVVEPSNLNRQQYF-ISQIGMPKVE-ALKENLLEInPFVE 98

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 19113852  116 VTPFYGKIQDKTI-EFYKEFKLIICGLDSVEARRWINSTL 154
Cdd:PRK08644  99 IEAHNEKIDEDNIeELFKDCDIVVEAFDNAETKAMLVETV 138
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 43-180 1.54e-11

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 65.28  E-value: 1.54e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113852   43 FSSKILIIGAGGLGCEILKDLALSGFRDLSVIDMDTIDITNLNRQFLFNESNIDEPKANVAASMIMKRIPSTVVTPFYGK 122
Cdd:PRK05597  27 FDAKVAVIGAGGLGSPALLYLAGAGVGHITIIDDDTVDLSNLHRQVIHSTAGVGQPKAESAREAMLALNPDVKVTVSVRR 106

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 19113852  123 IQ-DKTIEFYKEFKLIICGLDSVEArRWINSTlvAIAKTGdlIPLVDGGSEGLKGQARV 180
Cdd:PRK05597 107 LTwSNALDELRDADVILDGSDNFDT-RHLASW--AAARLG--IPHVWASILGFDAQLSV 160
E1_ThiF_like cd01487
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ...
 46-150 3.63e-11

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


Pssm-ID: 238764 [Multi-domain]  Cd Length: 174  Bit Score: 61.63  E-value: 3.63e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113852  46 KILIIGAGGLGCEILKDLALSGFRDLSVIDMDTIDITNLNRQFLFnESNIDEPKANVAASMIMKRIPSTVVTPFYGKIQD 125
Cdd:cd01487   1 KVGIAGAGGLGSNIAVLLARSGVGNLKLVDFDVVEPSNLNRQQYF-LSQIGEPKVEALKENLREINPFVKIEAINIKIDE 79

                        90       100
                ....*....|....*....|....*.
gi 19113852 126 KTI-EFYKEFKLIICGLDSVEARRWI 150
Cdd:cd01487  80 NNLeGLFGDCDIVVEAFDNAETKAML 105
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
 36-146 4.20e-11

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: 62.62  E-value: 4.20e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113852  36 EETLKSAFSSKILIIGAGGLGCEILKDLALSGFRDLSVIDMDTIDITNLNRQFLFNESNIDEPKANVAASMIMKRIPSTV 115
Cdd:cd00755   3 EEGLEKLRNAHVAVVGLGGVGSWAAEALARSGVGKLTLIDFDVVCVSNLNRQIHALLSTVGKPKVEVMAERIRDINPECE 82

                        90       100       110
                ....*....|....*....|....*....|...
gi 19113852 116 VTPFYGKIQDKTIEFY--KEFKLIICGLDSVEA 146
Cdd:cd00755  83 VDAVEEFLTPDNSEDLlgGDPDFVVDAIDSIRA 115
Ube1_repeat1 cd01491
Ubiquitin activating enzyme (E1), repeat 1. E1, a highly conserved small protein present ...
 36-151 6.61e-11

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


Pssm-ID: 238768 [Multi-domain]  Cd Length: 286  Bit Score: 62.67  E-value: 6.61e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113852  36 EETLKSAFSSKILIIGAGGLGCEILKDLALSGFRDLSVIDMDTIDITNLNRQFLFNESNIDEPKANVAASMIMKRIPSTV 115
Cdd:cd01491  11 HEAMKKLQKSNVLISGLGGLGVEIAKNLILAGVKSVTLHDTKPCSWSDLSSQFYLREEDIGKNRAEASQARLAELNPYVP 90

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 19113852 116 VTPFYGKIqdkTIEFYKEFKLIICGLDSVEARRWIN 151
Cdd:cd01491  91 VTVSTGPL---TTDELLKFQVVVLTDASLEDQLKIN 123
thiF_fam2 TIGR02354
thiamine biosynthesis protein ThiF, family 2; Members of the HesA/MoeB/ThiF family of proteins ...
 37-164 3.59e-10

thiamine biosynthesis protein ThiF, family 2; Members of the HesA/MoeB/ThiF family of proteins (pfam00899) include a number of members encoded in the midst of thiamine biosynthetic operons. This mix of known and putative ThiF proteins shows a deep split in phylogenetic trees, with one the E. coli ThiF and the E. coli MoeB proteins seemingly more closely related than E. coli ThiF and Campylobacter (for example) ThiF. This model represents the divergent clade of putative ThiF proteins such found in Campylobacter. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]


Pssm-ID: 162819  Cd Length: 200  Bit Score: 59.50  E-value: 3.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113852    37 ETLKSAfssKILIIGAGGLGCEILKDLALSGFRDLSVIDMDTIDITNLNRQFLFnESNIDEPKANVAASMIMKRIPSTVV 116
Cdd:TIGR02354  17 QKLEQA---TVAICGLGGLGSNVAINLARAGIGKLILVDFDVVEPSNLNRQQYK-ASQVGEPKTEALKENISEINPYTEI 92

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 19113852   117 TPFYGKIQDKTIE-FYKEFKLIICGLDSVEARRWINSTLVAIAKTGDLI 164
Cdd:TIGR02354  93 EAYDEKITEENIDkFFKDADIVCEAFDNAEAKAMLVNAVLEKYKDKYLI 141
TcdA COG1179
tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ...
 37-167 6.84e-10

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: 59.32  E-value: 6.84e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113852  37 ETLKSAfssKILIIGAGGLG---CEILkdlALSGFRDLSVIDMDTIDITNLNRQFLFNESNIDEPKANVAASMImKRI-P 112
Cdd:COG1179  20 ERLANA---HVAVVGLGGVGswaAEAL---ARSGVGRLTLVDLDDVCESNINRQLHALDSTVGRPKVEVMAERI-RDInP 92

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 19113852 113 STVVTPFYGKIQDKTIEFY--KEFKLIICGLDSVEARRwinsTLVAIAKTGDlIPLV 167
Cdd:COG1179  93 DCEVTAIDEFVTPENADELlsEDYDYVIDAIDSVSAKA----ALIAWCRRRG-IPII 144
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 36-151 1.92e-09

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: 59.90  E-value: 1.92e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113852     36 EETLKSAFSSKILIIGAGGLGCEILKDLALSGFRDLSVIDMDTIDITNLNRQFLFNESNIDEPKANVAASMIMKRIPSTV 115
Cdd:TIGR01408   16 DEAMQKMAKSNVLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLSSNFFLSEDDVGRNRAEAVVKKLAELNPYVH 95

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 19113852    116 VTpfygkIQDKTI--EFYKEFKLIICGLDSVEARRWIN 151
Cdd:TIGR01408   96 VS-----SSSVPFneEFLDKFQCVVLTEMSLPLQKEIN 128
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
32-180 2.42e-09

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 58.98  E-value: 2.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113852   32 PENPEETLKSAFSSKILIIGAGGLGCEILKDLALSGFRDLSVIDMDTIDITNLNRQFLFNESNIDEPKANVAASMIMKRI 111
Cdd:PRK07411  26 PEVGLEGQKRLKAASVLCIGTGGLGSPLLLYLAAAGIGRIGIVDFDVVDSSNLQRQVIHGTSWVGKPKIESAKNRILEIN 105

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113852  112 PSTVVTPFYGKIQ-DKTIEFYKEFKLIICGLDSVEARRWINSTLVAIAKtgdliPLVDGGSEGLKGQARV 180
Cdd:PRK07411 106 PYCQVDLYETRLSsENALDILAPYDVVVDGTDNFPTRYLVNDACVLLNK-----PNVYGSIFRFEGQATV 170
PRK15116 PRK15116
sulfur acceptor protein CsdL; Provisional
 36-184 3.75e-08

sulfur acceptor protein CsdL; Provisional


Pssm-ID: 185071  Cd Length: 268  Bit Score: 54.42  E-value: 3.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113852   36 EETLKSAFSSKILIIGAGGLGCEILKDLALSGFRDLSVIDMDTIDITNLNRQFLFNESNIDEPKANVAASMIMKRIPSTV 115
Cdd:PRK15116  22 EKALQLFADAHICVVGIGGVGSWAAEALARTGIGAITLIDMDDVCVTNTNRQIHALRDNVGLAKAEVMAERIRQINPECR 101

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19113852  116 VTPFYGKIQDKTIEFY--KEFKLIICGLDSVEARrwinSTLVAIAKTGDlIPLVDGGSEGlkGQarvIIPT 184
Cdd:PRK15116 102 VTVVDDFITPDNVAEYmsAGFSYVIDAIDSVRPK----AALIAYCRRNK-IPLVTTGGAG--GQ---IDPT 162
E1_like_apg7 TIGR01381
E1-like protein-activating enzyme Gsa7p/Apg7p; This model represents a family of eukaryotic ...
 35-159 5.50e-08

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


Pssm-ID: 273590 [Multi-domain]  Cd Length: 664  Bit Score: 54.95  E-value: 5.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113852    35 PEETLKSAFSSKILIIGAGGLGCEILKDLALSGFRDLSVIDMDTIDITNLNRQFLFNESNI---DEPKANVAASMIMKRI 111
Cdd:TIGR01381 329 PDLQLERYSQLKVLLLGAGTLGCNVARCLIGWGVRHITFVDNGKVSYSNPVRQSLSNFEDCllgGRGKAETAQKALKRIF 408

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19113852   112 PS--------TVVTP-----------FYGKIQdKTIEFYKEFKLIICGLDSVEArRWINSTLVAIAK 159
Cdd:TIGR01381 409 PSiqatghrlTVPMPghpidekdvpeLEKDIA-RLEQLIKDHDVVFLLLDSREA-RWLPTVLCSRHK 473
Apg7 cd01486
Apg7 is an E1-like protein, that activates two different ubiquitin-like proteins, Apg12 and ...
 46-159 2.37e-07

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


Pssm-ID: 238763 [Multi-domain]  Cd Length: 307  Bit Score: 52.38  E-value: 2.37e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113852  46 KILIIGAGGLGCEILKDLALSGFRDLSVIDMDTIDITNLNRQFLFN--ESNIDEPKANVAASMIMKRIPSTVVT------ 117
Cdd:cd01486   1 KCLLLGAGTLGCNVARNLLGWGVRHITFVDSGKVSYSNPVRQSLFTfeDCKGGKPKAEAAAERLKEIFPSIDATgivlsi 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 19113852 118 -----PFYGKIQDKTIEFYKEFK-------LIICGLDSVEArRWINSTLVAIAK 159
Cdd:cd01486  81 pmpghPISESEVPSTLKDVKRLEelikdhdVIFLLTDSRES-RWLPTLLSAAKN 133
PRK08223 PRK08223
hypothetical protein; Validated
 45-148 9.06e-07

hypothetical protein; Validated


Pssm-ID: 181302 [Multi-domain]  Cd Length: 287  Bit Score: 50.45  E-value: 9.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113852   45 SKILIIGAGGLGCEILKDLALSGFRDLSVIDMDTIDITNLNRQFLFNESNIDEPKANVAASMIMKRIPSTVVTPFYGKIQ 124
Cdd:PRK08223  28 SRVAIAGLGGVGGIHLLTLARLGIGKFTIADFDVFELRNFNRQAGAMMSTLGRPKAEVLAEMVRDINPELEIRAFPEGIG 107

                         90       100
                 ....*....|....*....|....*..
gi 19113852  125 DKTIE-FYKEFKLIICGLD--SVEARR 148
Cdd:PRK08223 108 KENADaFLDGVDVYVDGLDffEFDARR 134
APPBP1_RUB cd01493
Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric ...
 44-186 1.44e-05

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: 46.91  E-value: 1.44e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113852  44 SSKILIIGAGGLGCEILKDLALSGFRDLSVIDMDTIDITNLNRQFLFNESNIDEPKANVAASMIMKRIPS---TVVTPFY 120
Cdd:cd01493  20 SAHVCLLNATATGTEILKNLVLPGIGSFTIVDGSKVDEEDLGNNFFLDASSLGKSRAEATCELLQELNPDvngSAVEESP 99

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113852 121 GKIQDKTIEFYKEFKLIIcgldsveARRWINSTLVAIAKTgdL----IPLVDGGSEGLKGQARVIIPTIT 186
Cdd:cd01493 100 EALLDNDPSFFSQFTVVI-------ATNLPESTLLRLADV--LwsanIPLLYVRSYGLYGYIRIQLKEHT 160
PRK14852 PRK14852
hypothetical protein; Provisional
 45-183 9.45e-05

hypothetical protein; Provisional


Pssm-ID: 184854 [Multi-domain]  Cd Length: 989  Bit Score: 45.07  E-value: 9.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113852   45 SKILIIGAGGLGCEILKDLALSGFRDLSVIDMDTIDITNLNRQFLFNESNIDEPKANVAASMIMKRIPSTVVTPFYGKIQ 124
Cdd:PRK14852 333 SRVAIAGLGGVGGIHLMTLARTGIGNFNLADFDAYSPVNLNRQYGASIASFGRGKLDVMTERALSVNPFLDIRSFPEGVA 412

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19113852  125 DKTIE-FYKEFKLIICGLD--SVEARRWINSTLVAIAktgdlIPLVDGGSEGLKGQARVIIP 183
Cdd:PRK14852 413 AETIDaFLKDVDLLVDGIDffALDIRRRLFNRALELG-----IPVITAGPLGYSCALLVFMP 469
PRK14851 PRK14851
hypothetical protein; Provisional
 35-148 7.33e-03

hypothetical protein; Provisional


Pssm-ID: 184853 [Multi-domain]  Cd Length: 679  Bit Score: 38.69  E-value: 7.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113852   35 PEETLKSAfSSKILIIGAGGLGCEILKDLALSGFRDLSVIDMDTIDITNLNRQFLFNESNIDEPKANVAASMIMKRIPST 114
Cdd:PRK14851  35 PGEQERLA-EAKVAIPGMGGVGGVHLITMVRTGIGRFHIADFDQFEPVNVNRQFGARVPSFGRPKLAVMKEQALSINPFL 113

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 19113852  115 VVTPFYGKIQDKTIE-FYKEFKLIICGLD--SVEARR 148
Cdd:PRK14851 114 EITPFPAGINADNMDaFLDGVDVVLDGLDffQFEIRR 150
 
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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