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Conserved domains on  [gi|2750921205|gb|KAL0531068|]
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putative ThiF family [Leishmania shawi]

Protein Classification

ubiquitin-activating E1 family protein( domain architecture ID 320623)

ubiquitin-activating E1 family protein is an activating enzyme similar to Osphranter rufus ubiquitin-activating enzyme E1 Y that activates ubiquitin by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding a ubiquitin-E1 thioester and free AMP

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
E1_enzyme_family super family cl22428
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 44-394 1.30e-93

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.


The actual alignment was detected with superfamily member cd01488:

Pssm-ID: 451392 [Multi-domain]  Cd Length: 291  Bit Score: 287.71  E-value: 1.30e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921205  44 KPLVVGAGGIGCELLHLLALSGFAHLTVLDMDFVELSNLNRQFLFTRSDIGKAKSTAAAAAVQARCPGVSVTAIVGRLED 123
Cdd:cd01488     1 KILVIGAGGLGCELLKNLALSGFRNIHVIDMDTIDVSNLNRQFLFREKDIGKPKAEVAAKFVNDRVPGVNVTPHFGKIQD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921205 124 QPDDFYRDFDAVLLAVDSIQARRWMNqkvaaiatrvitpapasasppaarltAVPCDVPWASpapppasvqrvgDYviED 203
Cdd:cd01488    81 KDEEFYRQFNIIICGLDSIEARRWIN--------------------------GTLVSLLLYE------------DP--ES 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921205 204 AKLIIDAGTEGFEGHCRIVhmAHNRTPCIECEMYLYNSGVTrttVPLCTLVSVPRVPEHCVLYVQVKEWPEHHRHccrrs 283
Cdd:cd01488   121 IIPLIDGGTEGFKGHARVI--LPGITACIECSLDLFPPQVT---FPLCTIANTPRLPEHCIEYASLIQWPKEFPF----- 190

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921205 284 sqggdgavaaagereeegdgdEPLDPDNAEHVHWVAERARARQAAFGIGGAPIDdmFTLGVIKNVVPAVGFTNAYVAGQA 363
Cdd:cd01488   191 ---------------------VPLDGDDPEHIEWLYQKALERAAQFNISGVTYS--LTQGVVKRIIPAVASTNAIIAAAC 247

                         330       340       350
                  ....*....|....*....|....*....|.
gi 2750921205 364 VTELMKWLTGCAPELNNFAFYNGATeaGVYT 394
Cdd:cd01488   248 CLEALKIATDCYENLNNYLMYNGVD--GCYT 276
 
Name Accession Description Interval E-value
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 44-394 1.30e-93

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: 287.71  E-value: 1.30e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921205  44 KPLVVGAGGIGCELLHLLALSGFAHLTVLDMDFVELSNLNRQFLFTRSDIGKAKSTAAAAAVQARCPGVSVTAIVGRLED 123
Cdd:cd01488     1 KILVIGAGGLGCELLKNLALSGFRNIHVIDMDTIDVSNLNRQFLFREKDIGKPKAEVAAKFVNDRVPGVNVTPHFGKIQD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921205 124 QPDDFYRDFDAVLLAVDSIQARRWMNqkvaaiatrvitpapasasppaarltAVPCDVPWASpapppasvqrvgDYviED 203
Cdd:cd01488    81 KDEEFYRQFNIIICGLDSIEARRWIN--------------------------GTLVSLLLYE------------DP--ES 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921205 204 AKLIIDAGTEGFEGHCRIVhmAHNRTPCIECEMYLYNSGVTrttVPLCTLVSVPRVPEHCVLYVQVKEWPEHHRHccrrs 283
Cdd:cd01488   121 IIPLIDGGTEGFKGHARVI--LPGITACIECSLDLFPPQVT---FPLCTIANTPRLPEHCIEYASLIQWPKEFPF----- 190

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921205 284 sqggdgavaaagereeegdgdEPLDPDNAEHVHWVAERARARQAAFGIGGAPIDdmFTLGVIKNVVPAVGFTNAYVAGQA 363
Cdd:cd01488   191 ---------------------VPLDGDDPEHIEWLYQKALERAAQFNISGVTYS--LTQGVVKRIIPAVASTNAIIAAAC 247

                         330       340       350
                  ....*....|....*....|....*....|.
gi 2750921205 364 VTELMKWLTGCAPELNNFAFYNGATeaGVYT 394
Cdd:cd01488   248 CLEALKIATDCYENLNNYLMYNGVD--GCYT 276
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 23-256 4.35e-47

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: 164.35  E-value: 4.35e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921205  23 SPSTQFSIAGFDPQLKdWSFVKPLVVGAGGIGCELLHLLALSGFAHLTVLDMDFVELSNLNRQFLFTRSDIGKAKSTAAA 102
Cdd:pfam00899   2 SRQLALPLIGEDGQEK-LRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921205 103 AAVQARCPGVSVTAIVGRL-EDQPDDFYRDFDAVLLAVDSIQARRWMNQkvAAIATRvitpapasasppaarltavpcdv 181
Cdd:pfam00899  81 ERLREINPDVEVEAYTERLtPENAEELIKSFDIVVDATDNFAARYLVND--ACVKLG----------------------- 135

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2750921205 182 pwaspapppasvqrvgdyviedaKLIIDAGTEGFEGHCRIVHmaHNRTPCIECemyLYNSGVTRTTVPLCTLVSV 256
Cdd:pfam00899 136 -----------------------KPLIEAGVLGFKGQVTVVI--PGKTPCYRC---LFPEDPPPKLVPSCTVAGV 182
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 46-159 9.53e-27

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: 108.68  E-value: 9.53e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921205  46 LVVGAGGIGCELLHLLALSGFAHLTVLDMDFVELSNLNRQFLFTRSDIGKAKSTAAAAAVQARCPGVSVTAIVGRL-EDQ 124
Cdd:COG0476    31 LVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADVGRPKVEAAAERLRALNPDVEVEAIPERLtEEN 110

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2750921205 125 PDDFYRDFDAVLLAVDSIQARRWMNQkvAAIATRV 159
Cdd:COG0476   111 ALELLAGADLVLDCTDNFATRYLLND--ACVKLGI 143
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 43-264 1.51e-19

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: 92.64  E-value: 1.51e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921205   43 VKPLVVGAGGIGCELLHLLALSGFA-----HLTVLDMDFVELSNLNRQFLFTRSDIGKAKSTAAAAAVQARCPGVSVTAI 117
Cdd:TIGR01408  420 LNIFLVGCGAIGCEMLKNFALMGVGtgkkgMITVTDPDLIEKSNLNRQFLFRPHHIGKPKSYTAADATLKINPQIKIDAH 499

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921205  118 VGRLEDQP-----DDFYRDFDAVLLAVDSIQARRWMNQKVAAIatrvitpapasasppaarltavpcdvpwaspapppas 192
Cdd:TIGR01408  500 QNRVGPETetifnDEFYEKLDVVINALDNVEARRYVDSRCLAF------------------------------------- 542

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2750921205  193 vqrvgdyviedAKLIIDAGTEGFEGHCRIV--HMAHNrtpciecemylYNSG--VTRTTVPLCTLVSVPRVPEHCV 264
Cdd:TIGR01408  543 -----------LKPLLESGTLGTKGNTQVVvpHLTES-----------YGSSrdPPEKEIPFCTLKSFPAAIEHTI 596
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 32-159 9.94e-16

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 76.81  E-value: 9.94e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921205  32 GFDPQ--LKDwsfVKPLVVGAGGIGCELLHLLALSGFAHLTVLDMDFVELSNLNRQFLFTRSDIGKAKSTAAAAAVQARC 109
Cdd:PRK05690   23 DFDGQekLKA---ARVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVSLSNLQRQVLHDDATIGQPKVESARAALARIN 99

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2750921205 110 PGVSVTAIVGRL-EDQPDDFYRDFDAVLLAVDSIQARRWMNQkvAAIATRV 159
Cdd:PRK05690  100 PHIAIETINARLdDDELAALIAGHDLVLDCTDNVATRNQLNR--ACFAAKK 148
 
Name Accession Description Interval E-value
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 44-394 1.30e-93

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: 287.71  E-value: 1.30e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921205  44 KPLVVGAGGIGCELLHLLALSGFAHLTVLDMDFVELSNLNRQFLFTRSDIGKAKSTAAAAAVQARCPGVSVTAIVGRLED 123
Cdd:cd01488     1 KILVIGAGGLGCELLKNLALSGFRNIHVIDMDTIDVSNLNRQFLFREKDIGKPKAEVAAKFVNDRVPGVNVTPHFGKIQD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921205 124 QPDDFYRDFDAVLLAVDSIQARRWMNqkvaaiatrvitpapasasppaarltAVPCDVPWASpapppasvqrvgDYviED 203
Cdd:cd01488    81 KDEEFYRQFNIIICGLDSIEARRWIN--------------------------GTLVSLLLYE------------DP--ES 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921205 204 AKLIIDAGTEGFEGHCRIVhmAHNRTPCIECEMYLYNSGVTrttVPLCTLVSVPRVPEHCVLYVQVKEWPEHHRHccrrs 283
Cdd:cd01488   121 IIPLIDGGTEGFKGHARVI--LPGITACIECSLDLFPPQVT---FPLCTIANTPRLPEHCIEYASLIQWPKEFPF----- 190

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921205 284 sqggdgavaaagereeegdgdEPLDPDNAEHVHWVAERARARQAAFGIGGAPIDdmFTLGVIKNVVPAVGFTNAYVAGQA 363
Cdd:cd01488   191 ---------------------VPLDGDDPEHIEWLYQKALERAAQFNISGVTYS--LTQGVVKRIIPAVASTNAIIAAAC 247

                         330       340       350
                  ....*....|....*....|....*....|.
gi 2750921205 364 VTELMKWLTGCAPELNNFAFYNGATeaGVYT 394
Cdd:cd01488   248 CLEALKIATDCYENLNNYLMYNGVD--GCYT 276
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
 44-368 5.27e-49

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: 169.30  E-value: 5.27e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921205  44 KPLVVGAGGIGCELLHLLALSGFAHLTVLDMDFVELSNLNRQFLFTRSDIGKAKSTAAAAAVQARCPGVSVTAIVGRLED 123
Cdd:cd01484     1 KVLLVGAGGIGCELLKNLALMGFGQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKSEVAAEAVNDRNPNCKVVPYQNKVGP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921205 124 Q---PDDFYRDFDAVLLAVDSIQARRWMNQKVAAIatrvitpapasasppaarltAVPcdvpwaspapppasvqrvgdyv 200
Cdd:cd01484    81 EqdfNDTFFEQFHIIVNALDNIIARRYVNGMLIFL--------------------IVP---------------------- 118

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921205 201 iedaklIIDAGTEGFEGHCRIV--HMahnrTPCIECEMYlynsgVTRTTVPLCTLVSVPRVPEHCVLYVQVKEWpehhrh 278
Cdd:cd01484   119 ------LIESGTEGFKGNAQVIlpGM----TECIECTLY-----PPQKNFPMCTIASMPRLPEHCIEWARMLQW------ 177

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921205 279 ccrrssqggdgavaaagereeegdgdepldpDNAEHVHWVAERARARQAAFGIGGAPIDDmfTLGVIKNVVPAVGFTNAY 358
Cdd:cd01484   178 -------------------------------DDPEHIQFIFQASNERASQYNIRGVTYFL--TKGVAGRIIPAVATTNAV 224

                         330
                  ....*....|
gi 2750921205 359 VAGQAVTELM 368
Cdd:cd01484   225 VAGVCALEVF 234
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 23-256 4.35e-47

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: 164.35  E-value: 4.35e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921205  23 SPSTQFSIAGFDPQLKdWSFVKPLVVGAGGIGCELLHLLALSGFAHLTVLDMDFVELSNLNRQFLFTRSDIGKAKSTAAA 102
Cdd:pfam00899   2 SRQLALPLIGEDGQEK-LRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921205 103 AAVQARCPGVSVTAIVGRL-EDQPDDFYRDFDAVLLAVDSIQARRWMNQkvAAIATRvitpapasasppaarltavpcdv 181
Cdd:pfam00899  81 ERLREINPDVEVEAYTERLtPENAEELIKSFDIVVDATDNFAARYLVND--ACVKLG----------------------- 135

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2750921205 182 pwaspapppasvqrvgdyviedaKLIIDAGTEGFEGHCRIVHmaHNRTPCIECemyLYNSGVTRTTVPLCTLVSV 256
Cdd:pfam00899 136 -----------------------KPLIEAGVLGFKGQVTVVI--PGKTPCYRC---LFPEDPPPKLVPSCTVAGV 182
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 44-373 1.63e-36

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


Pssm-ID: 238766 [Multi-domain]  Cd Length: 312  Bit Score: 137.90  E-value: 1.63e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921205  44 KPLVVGAGGIGCELLHLLALSGFAHLTVLDMDFVELSNLNRQFLFTRSDIGKAKSTAAAAAVQARCPGVSVTAIVGRLED 123
Cdd:cd01489     1 KVLVVGAGGIGCELLKNLVLTGFGEIHIIDLDTIDLSNLNRQFLFRKKHVGKSKAQVAKEAVLSFNPNVKIVAYHANIKD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921205 124 Q--PDDFYRDFDAVLLAVDSIQARRWMNQKVAAiatrvitpapasasppaarlTAVPcdvpwaspapppasvqrvgdyvi 201
Cdd:cd01489    81 PdfNVEFFKQFDLVFNALDNLAARRHVNKMCLA--------------------ADVP----------------------- 117

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921205 202 edaklIIDAGTEGFEGHCRIVHmaHNRTPCIECemylyNSGVTRTTVPLCTLVSVPRVPEHCVLyvqvkeWPEHHRHCCR 281
Cdd:cd01489   118 -----LIESGTTGFLGQVQVIK--KGKTECYEC-----QPKETPKTFPVCTIRSTPSQPIHCIV------WAKSLFFLFN 179

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921205 282 RSSQGGDGAVAAAGEREEEGDGDEPL-------DPDNAEHVHWVAERARARQAAFGIggapidDMFTLGVIK----NVVP 350
Cdd:cd01489   180 KVFKDDIERLLSMEELWKTRKPPVPLswkeltfDKDDQDALDFVAAAANLRSHVFGI------PMKSRFDIKqmagNIIP 253

                         330       340
                  ....*....|....*....|...
gi 2750921205 351 AVGFTNAYVAGQAVTELMKWLTG 373
Cdd:cd01489   254 AIATTNAIIAGLIVLEALKVLSG 276
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 46-159 9.53e-27

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: 108.68  E-value: 9.53e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921205  46 LVVGAGGIGCELLHLLALSGFAHLTVLDMDFVELSNLNRQFLFTRSDIGKAKSTAAAAAVQARCPGVSVTAIVGRL-EDQ 124
Cdd:COG0476    31 LVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADVGRPKVEAAAERLRALNPDVEVEAIPERLtEEN 110

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2750921205 125 PDDFYRDFDAVLLAVDSIQARRWMNQkvAAIATRV 159
Cdd:COG0476   111 ALELLAGADLVLDCTDNFATRYLLND--ACVKLGI 143
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 46-151 2.21e-26

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: 104.66  E-value: 2.21e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921205  46 LVVGAGGIGCELLHLLALSGFAHLTVLDMDFVELSNLNRQFLFTRSDIGKAKSTAAAAAVQARCPGVSVTAIVGRLEDQ- 124
Cdd:cd01483     3 LLVGLGGLGSEIALNLARSGVGKITLIDFDTVELSNLNRQFLARQADIGKPKAEVAARRLNELNPGVNVTAVPEGISEDn 82

                          90       100
                  ....*....|....*....|....*..
gi 2750921205 125 PDDFYRDFDAVLLAVDSIQARRWMNQK 151
Cdd:cd01483    83 LDDFLDGVDLVIDAIDNIAVRRALNRA 109
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
 44-151 2.59e-24

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: 105.45  E-value: 2.59e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921205  44 KPLVVGAGGIGCELLHLLALSGFA-----HLTVLDMDFVELSNLNRQFLFTRSDIGKAKSTAAAAAVQARCPGVSVTAIV 118
Cdd:cd01490     1 KVFLVGAGAIGCELLKNFALMGVGtgesgEITVTDMDNIEKSNLNRQFLFRPHDVGKPKSEVAAAAVKAMNPDLKITALQ 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2750921205 119 GRL----ED-QPDDFYRDFDAVLLAVDSIQARRWMNQK 151
Cdd:cd01490    81 NRVgpetEHiFNDEFWEKLDGVANALDNVDARMYVDRR 118
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 46-160 2.49e-21

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: 92.93  E-value: 2.49e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921205  46 LVVGAGGIGCELLHLLALSGFAHLTVLDMDFVELSNLNRQFLFTRSDIGKAKSTAAAAAVQARCPGVSVTAIVGRL-EDQ 124
Cdd:cd00757    25 LVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRQILHTEADVGQPKAEAAAERLRAINPDVEIEAYNERLdAEN 104

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2750921205 125 PDDFYRDFDAVLLAVDSIQARRWMNQkvAAIATRVI 160
Cdd:cd00757   105 AEELIAGYDLVLDCTDNFATRYLIND--ACVKLGKP 138
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 43-264 1.51e-19

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: 92.64  E-value: 1.51e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921205   43 VKPLVVGAGGIGCELLHLLALSGFA-----HLTVLDMDFVELSNLNRQFLFTRSDIGKAKSTAAAAAVQARCPGVSVTAI 117
Cdd:TIGR01408  420 LNIFLVGCGAIGCEMLKNFALMGVGtgkkgMITVTDPDLIEKSNLNRQFLFRPHHIGKPKSYTAADATLKINPQIKIDAH 499

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921205  118 VGRLEDQP-----DDFYRDFDAVLLAVDSIQARRWMNQKVAAIatrvitpapasasppaarltavpcdvpwaspapppas 192
Cdd:TIGR01408  500 QNRVGPETetifnDEFYEKLDVVINALDNVEARRYVDSRCLAF------------------------------------- 542

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2750921205  193 vqrvgdyviedAKLIIDAGTEGFEGHCRIV--HMAHNrtpciecemylYNSG--VTRTTVPLCTLVSVPRVPEHCV 264
Cdd:TIGR01408  543 -----------LKPLLESGTLGTKGNTQVVvpHLTES-----------YGSSrdPPEKEIPFCTLKSFPAAIEHTI 596
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 32-159 9.94e-16

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 76.81  E-value: 9.94e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921205  32 GFDPQ--LKDwsfVKPLVVGAGGIGCELLHLLALSGFAHLTVLDMDFVELSNLNRQFLFTRSDIGKAKSTAAAAAVQARC 109
Cdd:PRK05690   23 DFDGQekLKA---ARVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVSLSNLQRQVLHDDATIGQPKVESARAALARIN 99

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2750921205 110 PGVSVTAIVGRL-EDQPDDFYRDFDAVLLAVDSIQARRWMNQkvAAIATRV 159
Cdd:PRK05690  100 PHIAIETINARLdDDELAALIAGHDLVLDCTDNVATRNQLNR--ACFAAKK 148
E1_ThiF_like cd01487
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ...
 44-153 1.57e-14

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: 71.64  E-value: 1.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921205  44 KPLVVGAGGIGCELLHLLALSGFAHLTVLDMDFVELSNLNRQFLFTrSDIGKAKSTAAAAAVQARCPGVSVTAIVGRLED 123
Cdd:cd01487     1 KVGIAGAGGLGSNIAVLLARSGVGNLKLVDFDVVEPSNLNRQQYFL-SQIGEPKVEALKENLREINPFVKIEAINIKIDE 79

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2750921205 124 QP-DDFYRDFDAVLLAVDSIQARRWMNQKVA 153
Cdd:cd01487    80 NNlEGLFGDCDIVVEAFDNAETKAMLAESLL 110
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
44-149 7.22e-14

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 73.12  E-value: 7.22e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921205  44 KPLVVGAGGIGCELLHLLALSGFAHLTVLDMDFVELSNLNRQFLFTRSDIGKAKSTAAAAAVQARCPGVSVTAIVGRLE- 122
Cdd:PRK08762  137 RVLLIGAGGLGSPAALYLAAAGVGTLGIVDHDVVDRSNLQRQILHTEDRVGQPKVDSAAQRLAALNPDVQVEAVQERVTs 216

                          90       100
                  ....*....|....*....|....*..
gi 2750921205 123 DQPDDFYRDFDAVLLAVDSIQARRWMN 149
Cdd:PRK08762  217 DNVEALLQDVDVVVDGADNFPTRYLLN 243
Aos1_SUMO cd01492
Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating ...
 30-137 2.27e-13

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: 68.86  E-value: 2.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921205  30 IAGFDPQLKDWSF--------VKPLVVGAGGIGCELLHLLALSGFAHLTVLDMDFVELSNLNRQFLFTRSDIGKAKSTAA 101
Cdd:cd01492     1 IALYDRQIRLWGLeaqkrlrsARILLIGLKGLGAEIAKNLVLSGIGSLTILDDRTVTEEDLGAQFLIPAEDLGQNRAEAS 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2750921205 102 AAAVQARCPGVSVTAIVGRLEDQPDDFYRDFDAVLL 137
Cdd:cd01492    81 LERLRALNPRVKVSVDTDDISEKPEEFFSQFDVVVA 116
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 27-140 2.93e-13

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 71.45  E-value: 2.93e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921205  27 QFSIAGFDPQLKDWSF-VKPLVVGAGGIGCELLHLLALSGFAHLTVLDMDFVELSNLNRQFLFTRSDIGKAKSTAAAAAV 105
Cdd:PRK05600   25 QLALPGFGIEQQERLHnARVLVIGAGGLGCPAMQSLASAGVGTITLIDDDTVDVSNIHRQILFGASDVGRPKVEVAAERL 104

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2750921205 106 QARCPGVSVTAIVGRLEdqPDDFYRDFDAVLLAVD 140
Cdd:PRK05600  105 KEIQPDIRVNALRERLT--AENAVELLNGVDLVLD 137
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
43-146 7.33e-13

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 67.57  E-value: 7.33e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921205  43 VKPLVVGAGGIGCELLHLLALSGFAHLTVLDMDFVELSNLNRQFLFTrSDIGKAKSTAAAAAVQARCPGVSVTAIVGRL- 121
Cdd:PRK08644   29 AKVGIAGAGGLGSNIAVALARSGVGNLKLVDFDVVEPSNLNRQQYFI-SQIGMPKVEALKENLLEINPFVEIEAHNEKId 107

                          90       100
                  ....*....|....*....|....*
gi 2750921205 122 EDQPDDFYRDFDAVLLAVDSIQARR 146
Cdd:PRK08644  108 EDNIEELFKDCDIVVEAFDNAETKA 132
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
 46-157 1.05e-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: 67.63  E-value: 1.05e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921205  46 LVVGAGGIGCELLHLLALSGFAHLTVLDMDFVELSNLNRQFLFTRSDIGKAKSTAAAAAVQARCPGVSVTAIVGRLEDQ- 124
Cdd:cd00755    15 AVVGLGGVGSWAAEALARSGVGKLTLIDFDVVCVSNLNRQIHALLSTVGKPKVEVMAERIRDINPECEVDAVEEFLTPDn 94

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2750921205 125 -PDDFYRDFDAVLLAVDSIQArrwmnqKVAAIAT 157
Cdd:cd00755    95 sEDLLGGDPDFVVDAIDSIRA------KVALIAY 122
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 47-145 7.70e-12

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 66.82  E-value: 7.70e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921205  47 VVGAGGIGCELLHLLALSGFAHLTVLDMDFVELSNLNRQFLFTRSDIGKAKSTAAAAAVQARCPGVSVTAIVGRLE-DQP 125
Cdd:PRK05597   33 VIGAGGLGSPALLYLAGAGVGHITIIDDDTVDLSNLHRQVIHSTAGVGQPKAESAREAMLALNPDVKVTVSVRRLTwSNA 112

                          90       100
                  ....*....|....*....|
gi 2750921205 126 DDFYRDFDAVLLAVDSIQAR 145
Cdd:PRK05597  113 LDELRDADVILDGSDNFDTR 132
TcdA COG1179
tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ...
 46-157 5.08e-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: 63.18  E-value: 5.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921205  46 LVVGAGGIG---CELLhllALSGFAHLTVLDMDFVELSNLNRQFLFTRSDIGKAKSTaaaaAVQARC----PGVSVTAIv 118
Cdd:COG1179    28 AVVGLGGVGswaAEAL---ARSGVGRLTLVDLDDVCESNINRQLHALDSTVGRPKVE----VMAERIrdinPDCEVTAI- 99

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2750921205 119 grledqpDDFY----------RDFDAVLLAVDSIQArrwmnqKVAAIAT 157
Cdd:COG1179   100 -------DEFVtpenadellsEDYDYVIDAIDSVSA------KAALIAW 135
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 44-149 6.93e-11

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 64.34  E-value: 6.93e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921205  44 KPLVVGAGGIGCELLHLLALSGFAHLTVLDMDFVELSNLNRQFLFTRSDIGKAKSTAAAAAVQARCPGVSVTAIVGRLE- 122
Cdd:PRK07878   44 RVLVIGAGGLGSPTLLYLAAAGVGTLGIVEFDVVDESNLQRQVIHGQSDVGRSKAQSARDSIVEINPLVNVRLHEFRLDp 123

                          90       100
                  ....*....|....*....|....*..
gi 2750921205 123 DQPDDFYRDFDAVLLAVDSIQARRWMN 149
Cdd:PRK07878  124 SNAVELFSQYDLILDGTDNFATRYLVN 150
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 46-149 3.56e-09

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 58.47  E-value: 3.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921205  46 LVVGAGGIGCELLHLLALSGFAHLTVLDMDFVELSNLNRQFLFTRSDIGKA--KSTAAAAAVQARCPGVSVTAIVGRLE- 122
Cdd:PRK07688   28 LIIGAGALGTANAEMLVRAGVGKVTIVDRDYVEWSNLQRQQLYTESDVKNNlpKAVAAKKRLEEINSDVRVEAIVQDVTa 107

                          90       100
                  ....*....|....*....|....*..
gi 2750921205 123 DQPDDFYRDFDAVLLAVDSIQARRWMN 149
Cdd:PRK07688  108 EELEELVTGVDLIIDATDNFETRFIVN 134
Apg7 cd01486
Apg7 is an E1-like protein, that activates two different ubiquitin-like proteins, Apg12 and ...
 44-148 1.86e-08

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: 56.23  E-value: 1.86e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921205  44 KPLVVGAGGIGCELLHLLALSGFAHLTVLDMDFVELSNLNRQFLFTRSDI--GKAKSTAAAAAVQARCPGVSVTAI---- 117
Cdd:cd01486     1 KCLLLGAGTLGCNVARNLLGWGVRHITFVDSGKVSYSNPVRQSLFTFEDCkgGKPKAEAAAERLKEIFPSIDATGIvlsi 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2750921205 118 ------------------VGRLEDQPDdfyrDFDAVLLAVDSIQArRWM 148
Cdd:cd01486    81 pmpghpisesevpstlkdVKRLEELIK----DHDVIFLLTDSRES-RWL 124
PRK08328 PRK08328
hypothetical protein; Provisional
 47-145 4.38e-08

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 54.03  E-value: 4.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921205  47 VVGAGGIGCELLHLLALSGFAHLTVLDMDFVELSNLNRQFLFTRSDIGK-AKSTAAAAAVQARCPGVSVTAIVGRL-EDQ 124
Cdd:PRK08328   32 VVGVGGLGSPVAYYLAAAGVGRILLIDEQTPELSNLNRQILHWEEDLGKnPKPLSAKWKLERFNSDIKIETFVGRLsEEN 111

                          90       100
                  ....*....|....*....|.
gi 2750921205 125 PDDFYRDFDAVLLAVDSIQAR 145
Cdd:PRK08328  112 IDEVLKGVDVIVDCLDNFETR 132
PRK15116 PRK15116
sulfur acceptor protein CsdL; Provisional
 47-145 4.95e-08

sulfur acceptor protein CsdL; Provisional


Pssm-ID: 185071  Cd Length: 268  Bit Score: 54.42  E-value: 4.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921205  47 VVGAGGIGCELLHLLALSGFAHLTVLDMDFVELSNLNRQFLFTRSDIGKAKSTAAAAAVQARCPGVSVTAIvgrledqpD 126
Cdd:PRK15116   35 VVGIGGVGSWAAEALARTGIGAITLIDMDDVCVTNTNRQIHALRDNVGLAKAEVMAERIRQINPECRVTVV--------D 106

                          90       100
                  ....*....|....*....|....*....
gi 2750921205 127 DFY----------RDFDAVLLAVDSIQAR 145
Cdd:PRK15116  107 DFItpdnvaeymsAGFSYVIDAIDSVRPK 135
Ube1_repeat1 cd01491
Ubiquitin activating enzyme (E1), repeat 1. E1, a highly conserved small protein present ...
 46-137 2.92e-07

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: 52.27  E-value: 2.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921205  46 LVVGAGGIGCELLHLLALSGFAHLTVLDMDFVELSNLNRQFLFTRSDIGKAKSTAAAAAVQARCPGVSVTAIVGRLEdqp 125
Cdd:cd01491    23 LISGLGGLGVEIAKNLILAGVKSVTLHDTKPCSWSDLSSQFYLREEDIGKNRAEASQARLAELNPYVPVTVSTGPLT--- 99

                          90
                  ....*....|..
gi 2750921205 126 DDFYRDFDAVLL 137
Cdd:cd01491   100 TDELLKFQVVVL 111
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 46-149 1.96e-06

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 50.11  E-value: 1.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921205  46 LVVGAGGIGCELLHLLALSGFAHLTVLDMDFVELSNLNRQFLFTRSDIG--KAKSTAAAAAVQARCPGVSVTAIVGRLED 123
Cdd:PRK12475   28 LIVGAGALGAANAEALVRAGIGKLTIADRDYVEWSNLQRQQLYTEEDAKqkKPKAIAAKEHLRKINSEVEIVPVVTDVTV 107

                          90       100
                  ....*....|....*....|....*..
gi 2750921205 124 QP-DDFYRDFDAVLLAVDSIQARRWMN 149
Cdd:PRK12475  108 EElEELVKEVDLIIDATDNFDTRLLIN 134
E1_like_apg7 TIGR01381
E1-like protein-activating enzyme Gsa7p/Apg7p; This model represents a family of eukaryotic ...
 34-159 7.71e-06

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: 48.78  E-value: 7.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921205  34 DPQLKDWSFVKPLVVGAGGIGCELLHLLALSGFAHLTVLDMDFVELSNLNRQFLFTRSDI---GKAKSTAAAAAVQARCP 110
Cdd:TIGR01381 330 DLQLERYSQLKVLLLGAGTLGCNVARCLIGWGVRHITFVDNGKVSYSNPVRQSLSNFEDCllgGRGKAETAQKALKRIFP 409

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2750921205 111 GVSVTAIVGRL--------EDQPDDFYRDF----------DAVLLAVDSIQArRWMNQKVAAIATRV 159
Cdd:TIGR01381 410 SIQATGHRLTVpmpghpidEKDVPELEKDIarleqlikdhDVVFLLLDSREA-RWLPTVLCSRHKKI 475
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
46-97 1.95e-05

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 47.04  E-value: 1.95e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2750921205  46 LVVGAGGIGCELLHLLALSGFAHLTVLDMDFVELSNLNRQFLFTRSDIGKAK 97
Cdd:PRK07411   42 LCIGTGGLGSPLLLYLAAAGIGRIGIVDFDVVDSSNLQRQVIHGTSWVGKPK 93
APPBP1_RUB cd01493
Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric ...
 46-136 3.76e-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: 46.14  E-value: 3.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921205  46 LVVGAGGIGCELLHLLALSGFAHLTVLDMDFVELSNLNRQFLFTRSDIGKAKSTAAAAAVQARCPGVSVTAIV---GRLE 122
Cdd:cd01493    24 CLLNATATGTEILKNLVLPGIGSFTIVDGSKVDEEDLGNNFFLDASSLGKSRAEATCELLQELNPDVNGSAVEespEALL 103

                          90
                  ....*....|....
gi 2750921205 123 DQPDDFYRDFDAVL 136
Cdd:cd01493   104 DNDPSFFSQFTVVI 117
PRK08223 PRK08223
hypothetical protein; Validated
 47-146 4.07e-04

hypothetical protein; Validated


Pssm-ID: 181302 [Multi-domain]  Cd Length: 287  Bit Score: 42.36  E-value: 4.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921205  47 VVGAGGIGCelLHLLALS--GFAHLTVLDMDFVELSNLNRQFLFTRSDIGKAKSTAAAAAVQARCPGVSVTAIV-GRLED 123
Cdd:PRK08223   32 IAGLGGVGG--IHLLTLArlGIGKFTIADFDVFELRNFNRQAGAMMSTLGRPKAEVLAEMVRDINPELEIRAFPeGIGKE 109

                          90       100
                  ....*....|....*....|....*...
gi 2750921205 124 QPDDFyrdFDAVLLAVDSI-----QARR 146
Cdd:PRK08223  110 NADAF---LDGVDVYVDGLdffefDARR 134
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 46-117 5.46e-04

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: 42.95  E-value: 5.46e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2750921205   46 LVVGAGGIGCELLHLLALSGFAHLTVLDMDFVELSNLNRQFLFTRSDIGKAKSTAAAAAVQARCPGVSVTAI 117
Cdd:TIGR01408   28 LISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLSSNFFLSEDDVGRNRAEAVVKKLAELNPYVHVSSS 99
E1-1_like cd01485
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ...
 44-137 9.69e-03

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: 37.40  E-value: 9.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921205  44 KPLVVGAGGIGCELLHLLALSGFAHLTVLDMDFVELSNLNRQFLFTR--SDIGKAKSTAAAAAVQ---ARCPGVSVTAIV 118
Cdd:cd01485    21 KVLIIGAGALGAEIAKNLVLAGIDSITIVDHRLVSTEDLGSNFFLDAevSNSGMNRAAASYEFLQelnPNVKLSIVEEDS 100

                          90
                  ....*....|....*....
gi 2750921205 119 GRLEDQPDDFYRDFDAVLL 137
Cdd:cd01485   101 LSNDSNIEEYLQKFTLVIA 119
 
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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