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Conserved domains on  [gi|19922550|ref|NP_611350|]
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Autophagy-related 7, isoform A [Drosophila melanogaster]

Protein Classification

ubiquitin-like modifier-activating enzyme ATG7( domain architecture ID 1002215)

ubiquitin-like modifier-activating enzyme ATG7 is an E1-like activating enzyme involved in the 2 ubiquitin-like systems required for cytoplasm to vacuole transport (Cvt) and autophagy

CATH:  3.40.50.720
Gene Ontology:  GO:0006497|GO:0061025|GO:0006914|GO:0008641|GO:0042803
TCDB:  9.A.15.2.1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
E1_like_apg7 super family cl36889
E1-like protein-activating enzyme Gsa7p/Apg7p; This model represents a family of eukaryotic ...
 11-682 0e+00

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.


The actual alignment was detected with superfamily member TIGR01381:

Pssm-ID: 273590 [Multi-domain]  Cd Length: 664  Bit Score: 629.28  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922550    11 FAPWESFVSPTFWHKLAELKLDHDRLSDSKRSITG----HYTNRNASGCLLEVDYTAYNRMAKPPKFSHSAIGTIYNKNT 86
Cdd:TIGR01381   1 FVPFVSCVDTGFWNEVSKLKLNKWKLDDTPKCISGqlslHQTEGFKCHLSLSYDSLSSLESTTGTHAQLSVSGILLNYNT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922550    87 IEEFKALDKLQLLADEGKELLADMCSGGALRDPSLLTRFFVLSFADLKCHSYYYWFAFPCPLTP------TLKLQGAVQK 160
Cdd:TIGR01381  81 VESFKKVDKSDLLRSEAEKIWESIQTRKWLQDPSLLSQFFIISFADLKKFKFYYWFCFPALVYPskvnklSGLTESIKQE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922550   161 LRDLPNSSSYIMALKALPTESQNFFILYANVEKNIFEARSLSSLDDKNVEFCyFGFADPSEYEH-PAWIMRNYAAFLLQQ 239
Cdd:TIGR01381 161 ITPLESLGADHKILFDFYRKNNFPFFLYSKQSSKMLELSELENNTNPDDELC-VGFADPSPVAYsAGWMLRNVLAAVAHL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922550   240 CPSFVgkplKFLGLRHNQQMNIDDSLVWKVIQTEA---CDLSQSENIKFVGWELNKNGKMGPRMVCMRDSMDPAKLAENS 316
Cdd:TIGR01381 240 HPTWK----HVHIFSLRSADSIGIKYLWTTLLPSAelsSDGAQNAVPKAVGWERNANGKLQPISVDLSKEFDPKRLAERS 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922550   317 VNLNLKLMKWRLVPDLNLEIISQTKCLLFGAGTLGCAVARNLLSWGFKHITLLDSGKVGFSNPVRQNLYTHADAVAGNRM 396
Cdd:TIGR01381 316 VDLNLKLMKWRLHPDLQLERYSQLKVLLLGAGTLGCNVARCLIGWGVRHITFVDNGKVSYSNPVRQSLSNFEDCLLGGRG 395

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922550   397 KATTAAQRLKEINPSAETAGYVLEIPMPGHTIGESLLAQTKEHLKVIEKLVQDHDVIFLLTDSRESRWLPTLLGAAKEKI 476
Cdd:TIGR01381 396 KAETAQKALKRIFPSIQATGHRLTVPMPGHPIDEKDVPELEKDIARLEQLIKDHDVVFLLLDSREARWLPTVLCSRHKKI 475

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922550   477 VINAALGFDSYLVMRHGTTRKEAGDDGQEiegLKCINGDQLGCYFCNDVTAPGNSLKDRTLDQQCTVTRPGVSNIAASYA 556
Cdd:TIGR01381 476 AISAALGFDSYVVMRHGIGRSESVSDVSS---SDSVPYSRLGCYFCNDVTAPGDSTTDRTLDQQCTVTRPGTAMIASGLA 552

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922550   557 VELLVALLQHPRKELAPAyyaqsgRGRSEETeekvpegLLGILPHSIRGMLCNYENILPATQKFAQCIACSAAVLNEYKK 636
Cdd:TIGR01381 553 VELLVSVLQHPLPSKTPA------SHDDNTT-------VLGALPHQIRGFLGRFQQILLSVKRFDQCVACSDAVAAEYQQ 619

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*.
gi 19922550   637 EGHAFLFKTFETAKFLEDLTGISEFKRlNSEIIDFDDEEFDMSDSD 682
Cdd:TIGR01381 620 RGWKFVRDAMNSPGYLEDLTGLTELKN-ESSVNAIDIQDFESDDDD 664
 
Name Accession Description Interval E-value
E1_like_apg7 TIGR01381
E1-like protein-activating enzyme Gsa7p/Apg7p; This model represents a family of eukaryotic ...
 11-682 0e+00

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: 629.28  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922550    11 FAPWESFVSPTFWHKLAELKLDHDRLSDSKRSITG----HYTNRNASGCLLEVDYTAYNRMAKPPKFSHSAIGTIYNKNT 86
Cdd:TIGR01381   1 FVPFVSCVDTGFWNEVSKLKLNKWKLDDTPKCISGqlslHQTEGFKCHLSLSYDSLSSLESTTGTHAQLSVSGILLNYNT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922550    87 IEEFKALDKLQLLADEGKELLADMCSGGALRDPSLLTRFFVLSFADLKCHSYYYWFAFPCPLTP------TLKLQGAVQK 160
Cdd:TIGR01381  81 VESFKKVDKSDLLRSEAEKIWESIQTRKWLQDPSLLSQFFIISFADLKKFKFYYWFCFPALVYPskvnklSGLTESIKQE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922550   161 LRDLPNSSSYIMALKALPTESQNFFILYANVEKNIFEARSLSSLDDKNVEFCyFGFADPSEYEH-PAWIMRNYAAFLLQQ 239
Cdd:TIGR01381 161 ITPLESLGADHKILFDFYRKNNFPFFLYSKQSSKMLELSELENNTNPDDELC-VGFADPSPVAYsAGWMLRNVLAAVAHL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922550   240 CPSFVgkplKFLGLRHNQQMNIDDSLVWKVIQTEA---CDLSQSENIKFVGWELNKNGKMGPRMVCMRDSMDPAKLAENS 316
Cdd:TIGR01381 240 HPTWK----HVHIFSLRSADSIGIKYLWTTLLPSAelsSDGAQNAVPKAVGWERNANGKLQPISVDLSKEFDPKRLAERS 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922550   317 VNLNLKLMKWRLVPDLNLEIISQTKCLLFGAGTLGCAVARNLLSWGFKHITLLDSGKVGFSNPVRQNLYTHADAVAGNRM 396
Cdd:TIGR01381 316 VDLNLKLMKWRLHPDLQLERYSQLKVLLLGAGTLGCNVARCLIGWGVRHITFVDNGKVSYSNPVRQSLSNFEDCLLGGRG 395

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922550   397 KATTAAQRLKEINPSAETAGYVLEIPMPGHTIGESLLAQTKEHLKVIEKLVQDHDVIFLLTDSRESRWLPTLLGAAKEKI 476
Cdd:TIGR01381 396 KAETAQKALKRIFPSIQATGHRLTVPMPGHPIDEKDVPELEKDIARLEQLIKDHDVVFLLLDSREARWLPTVLCSRHKKI 475

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922550   477 VINAALGFDSYLVMRHGTTRKEAGDDGQEiegLKCINGDQLGCYFCNDVTAPGNSLKDRTLDQQCTVTRPGVSNIAASYA 556
Cdd:TIGR01381 476 AISAALGFDSYVVMRHGIGRSESVSDVSS---SDSVPYSRLGCYFCNDVTAPGDSTTDRTLDQQCTVTRPGTAMIASGLA 552

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922550   557 VELLVALLQHPRKELAPAyyaqsgRGRSEETeekvpegLLGILPHSIRGMLCNYENILPATQKFAQCIACSAAVLNEYKK 636
Cdd:TIGR01381 553 VELLVSVLQHPLPSKTPA------SHDDNTT-------VLGALPHQIRGFLGRFQQILLSVKRFDQCVACSDAVAAEYQQ 619

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*.
gi 19922550   637 EGHAFLFKTFETAKFLEDLTGISEFKRlNSEIIDFDDEEFDMSDSD 682
Cdd:TIGR01381 620 RGWKFVRDAMNSPGYLEDLTGLTELKN-ESSVNAIDIQDFESDDDD 664
Apg7 cd01486
Apg7 is an E1-like protein, that activates two different ubiquitin-like proteins, Apg12 and ...
 341-658 0e+00

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: 546.59  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922550 341 KCLLFGAGTLGCAVARNLLSWGFKHITLLDSGKVGFSNPVRQNLYTHADAvAGNRMKATTAAQRLKEINPSAETAGYVLE 420
Cdd:cd01486   1 KCLLLGAGTLGCNVARNLLGWGVRHITFVDSGKVSYSNPVRQSLFTFEDC-KGGKPKAEAAAERLKEIFPSIDATGIVLS 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922550 421 IPMPGHTIGESLLAQTKEHLKVIEKLVQDHDVIFLLTDSRESRWLPTLLGAAKEKIVINAALGFDSYLVMRHGTTRKEAG 500
Cdd:cd01486  80 IPMPGHPISESEVPSTLKDVKRLEELIKDHDVIFLLTDSRESRWLPTLLSAAKNKLVINAALGFDSYLVMRHGAGPQSQS 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922550 501 DDGQeiEGLKCINGDQLGCYFCNDVTAPGNSLKDRTLDQQCTVTRPGVSNIAASYAVELLVALLQHPRKELAPAYyaqsg 580
Cdd:cd01486 160 GSGD--SSSDSIPGSRLGCYFCNDVVAPGDSLKDRTLDQQCTVTRPGLSMIASSIAVELLVSLLQHPLGGHAPAE----- 232

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19922550 581 rgrSEETEEKVPEGLLGILPHSIRGMLCNYENILPATQKFAQCIACSAAVLNEYKKEGHAFLFKTFETAKFLEDLTGI 658
Cdd:cd01486 233 ---SSSNEGDEPTTVLGILPHQIRGFLSNFSNLTLSGQAYDQCTACSDAVIDEYHREGWEFVLKAFNSPDYLEELTGL 307
ATG7_N pfam16420
Ubiquitin-like modifier-activating enzyme ATG7 N-terminus; This is the N-terminal domain of ...
 9-307 2.66e-120

Ubiquitin-like modifier-activating enzyme ATG7 N-terminus; This is the N-terminal domain of Ubiquitin-like modifier-activating enzyme ATG7. In Arabidopsis this domain binds the E2 enzymes ATG10 and ATG3.


Pssm-ID: 465114  Cd Length: 308  Bit Score: 361.19  E-value: 2.66e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922550     9 LQFAPWESFVSPTFWHKLAELKLDHDRLSDSKRSITGHYTNRNASG--CLLEVDYTAYNR-MAKPPKFSHSAIGTIYNKN 85
Cdd:pfam16420   1 LQFAPFSSFIDPSFWHELSSLKLDVLKLDDSPRPILGLYEPRDAPGlsCRLQLDGSSFNDtSDAVPPGSCRAEGTLKNFN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922550    86 TIEEFKALDKLQLLADEGKELLADMCSGGALRDPSLLTRFFVLSFADLKCHSYYYWFAFPCPLTPTLKLQGAVQKLRDLP 165
Cdd:pfam16420  81 TIEEFKNLDKQALLDDAGKKIWDAILSGTALEDPSLLSRFLLLSFADLKKYKFYYWFAFPALHSDPAWVLSWKPASEELS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922550   166 NS-----SSYIMALKALPTESQNFFiLYANVEKNIFEARSLSSL--DDKNVEFCYFGFADPSEY-EHPAWIMRNYAAFLL 237
Cdd:pfam16420 161 SEeteslVDAVQTWRYSVDARQHFF-LVKKSRGSDWEIASLSEYenFFADVEDVYFGFADPSTLpENPGWPLRNLLALLR 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19922550   238 QQCPSfvgKPLKFLGLRHNQQMNIDD--SLVWKVIQTEACDLSQSENIKFVGWELNKNGKMGPRMVCMRDSM 307
Cdd:pfam16420 240 ARWPL---KKVQVLCYRDNSRSGRRDerSLVLTLKLPEPSDENTSELPKAVGWERNANGKLGPRVVDLSSYM 308
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 337-465 2.59e-13

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 71.56  E-value: 2.59e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922550  337 ISQTKCLLFGAGTLGCAVARNLLSWGFKHITLLDSGKVGFSNPVRQNLYTHADAVagNRM-KATTAAQRLKEINPSAETA 415
Cdd:PRK07688  22 LREKHVLIIGAGALGTANAEMLVRAGVGKVTIVDRDYVEWSNLQRQQLYTESDVK--NNLpKAVAAKKRLEEINSDVRVE 99

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 19922550  416 GYVLEIpmpghTIGEsllaqtkehlkvIEKLVQDHDVIFLLTDSRESRWL 465
Cdd:PRK07688 100 AIVQDV-----TAEE------------LEELVTGVDLIIDATDNFETRFI 132
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 335-488 2.68e-13

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: 70.16  E-value: 2.68e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922550 335 EIISQTKCLLFGAGTLGCAVARNLLSWGFKHITLLDSGKVGFSNPVRQNLYTHADAvagNRMKATTAAQRLKEINPSaet 414
Cdd:COG0476  23 EKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADV---GRPKVEAAAERLRALNPD--- 96

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19922550 415 agyvLEIpmpgHTIGESLLAQTkehlkvIEKLVQDHDVIFLLTDSRESRwlpTLLGAA--KEKI--VINAALGFDSYL 488
Cdd:COG0476  97 ----VEV----EAIPERLTEEN------ALELLAGADLVLDCTDNFATR---YLLNDAcvKLGIplVSGAVIGFEGQV 157
 
Name Accession Description Interval E-value
E1_like_apg7 TIGR01381
E1-like protein-activating enzyme Gsa7p/Apg7p; This model represents a family of eukaryotic ...
 11-682 0e+00

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: 629.28  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922550    11 FAPWESFVSPTFWHKLAELKLDHDRLSDSKRSITG----HYTNRNASGCLLEVDYTAYNRMAKPPKFSHSAIGTIYNKNT 86
Cdd:TIGR01381   1 FVPFVSCVDTGFWNEVSKLKLNKWKLDDTPKCISGqlslHQTEGFKCHLSLSYDSLSSLESTTGTHAQLSVSGILLNYNT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922550    87 IEEFKALDKLQLLADEGKELLADMCSGGALRDPSLLTRFFVLSFADLKCHSYYYWFAFPCPLTP------TLKLQGAVQK 160
Cdd:TIGR01381  81 VESFKKVDKSDLLRSEAEKIWESIQTRKWLQDPSLLSQFFIISFADLKKFKFYYWFCFPALVYPskvnklSGLTESIKQE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922550   161 LRDLPNSSSYIMALKALPTESQNFFILYANVEKNIFEARSLSSLDDKNVEFCyFGFADPSEYEH-PAWIMRNYAAFLLQQ 239
Cdd:TIGR01381 161 ITPLESLGADHKILFDFYRKNNFPFFLYSKQSSKMLELSELENNTNPDDELC-VGFADPSPVAYsAGWMLRNVLAAVAHL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922550   240 CPSFVgkplKFLGLRHNQQMNIDDSLVWKVIQTEA---CDLSQSENIKFVGWELNKNGKMGPRMVCMRDSMDPAKLAENS 316
Cdd:TIGR01381 240 HPTWK----HVHIFSLRSADSIGIKYLWTTLLPSAelsSDGAQNAVPKAVGWERNANGKLQPISVDLSKEFDPKRLAERS 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922550   317 VNLNLKLMKWRLVPDLNLEIISQTKCLLFGAGTLGCAVARNLLSWGFKHITLLDSGKVGFSNPVRQNLYTHADAVAGNRM 396
Cdd:TIGR01381 316 VDLNLKLMKWRLHPDLQLERYSQLKVLLLGAGTLGCNVARCLIGWGVRHITFVDNGKVSYSNPVRQSLSNFEDCLLGGRG 395

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922550   397 KATTAAQRLKEINPSAETAGYVLEIPMPGHTIGESLLAQTKEHLKVIEKLVQDHDVIFLLTDSRESRWLPTLLGAAKEKI 476
Cdd:TIGR01381 396 KAETAQKALKRIFPSIQATGHRLTVPMPGHPIDEKDVPELEKDIARLEQLIKDHDVVFLLLDSREARWLPTVLCSRHKKI 475

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922550   477 VINAALGFDSYLVMRHGTTRKEAGDDGQEiegLKCINGDQLGCYFCNDVTAPGNSLKDRTLDQQCTVTRPGVSNIAASYA 556
Cdd:TIGR01381 476 AISAALGFDSYVVMRHGIGRSESVSDVSS---SDSVPYSRLGCYFCNDVTAPGDSTTDRTLDQQCTVTRPGTAMIASGLA 552

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922550   557 VELLVALLQHPRKELAPAyyaqsgRGRSEETeekvpegLLGILPHSIRGMLCNYENILPATQKFAQCIACSAAVLNEYKK 636
Cdd:TIGR01381 553 VELLVSVLQHPLPSKTPA------SHDDNTT-------VLGALPHQIRGFLGRFQQILLSVKRFDQCVACSDAVAAEYQQ 619

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*.
gi 19922550   637 EGHAFLFKTFETAKFLEDLTGISEFKRlNSEIIDFDDEEFDMSDSD 682
Cdd:TIGR01381 620 RGWKFVRDAMNSPGYLEDLTGLTELKN-ESSVNAIDIQDFESDDDD 664
Apg7 cd01486
Apg7 is an E1-like protein, that activates two different ubiquitin-like proteins, Apg12 and ...
 341-658 0e+00

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: 546.59  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922550 341 KCLLFGAGTLGCAVARNLLSWGFKHITLLDSGKVGFSNPVRQNLYTHADAvAGNRMKATTAAQRLKEINPSAETAGYVLE 420
Cdd:cd01486   1 KCLLLGAGTLGCNVARNLLGWGVRHITFVDSGKVSYSNPVRQSLFTFEDC-KGGKPKAEAAAERLKEIFPSIDATGIVLS 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922550 421 IPMPGHTIGESLLAQTKEHLKVIEKLVQDHDVIFLLTDSRESRWLPTLLGAAKEKIVINAALGFDSYLVMRHGTTRKEAG 500
Cdd:cd01486  80 IPMPGHPISESEVPSTLKDVKRLEELIKDHDVIFLLTDSRESRWLPTLLSAAKNKLVINAALGFDSYLVMRHGAGPQSQS 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922550 501 DDGQeiEGLKCINGDQLGCYFCNDVTAPGNSLKDRTLDQQCTVTRPGVSNIAASYAVELLVALLQHPRKELAPAYyaqsg 580
Cdd:cd01486 160 GSGD--SSSDSIPGSRLGCYFCNDVVAPGDSLKDRTLDQQCTVTRPGLSMIASSIAVELLVSLLQHPLGGHAPAE----- 232

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19922550 581 rgrSEETEEKVPEGLLGILPHSIRGMLCNYENILPATQKFAQCIACSAAVLNEYKKEGHAFLFKTFETAKFLEDLTGI 658
Cdd:cd01486 233 ---SSSNEGDEPTTVLGILPHQIRGFLSNFSNLTLSGQAYDQCTACSDAVIDEYHREGWEFVLKAFNSPDYLEELTGL 307
ATG7_N pfam16420
Ubiquitin-like modifier-activating enzyme ATG7 N-terminus; This is the N-terminal domain of ...
 9-307 2.66e-120

Ubiquitin-like modifier-activating enzyme ATG7 N-terminus; This is the N-terminal domain of Ubiquitin-like modifier-activating enzyme ATG7. In Arabidopsis this domain binds the E2 enzymes ATG10 and ATG3.


Pssm-ID: 465114  Cd Length: 308  Bit Score: 361.19  E-value: 2.66e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922550     9 LQFAPWESFVSPTFWHKLAELKLDHDRLSDSKRSITGHYTNRNASG--CLLEVDYTAYNR-MAKPPKFSHSAIGTIYNKN 85
Cdd:pfam16420   1 LQFAPFSSFIDPSFWHELSSLKLDVLKLDDSPRPILGLYEPRDAPGlsCRLQLDGSSFNDtSDAVPPGSCRAEGTLKNFN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922550    86 TIEEFKALDKLQLLADEGKELLADMCSGGALRDPSLLTRFFVLSFADLKCHSYYYWFAFPCPLTPTLKLQGAVQKLRDLP 165
Cdd:pfam16420  81 TIEEFKNLDKQALLDDAGKKIWDAILSGTALEDPSLLSRFLLLSFADLKKYKFYYWFAFPALHSDPAWVLSWKPASEELS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922550   166 NS-----SSYIMALKALPTESQNFFiLYANVEKNIFEARSLSSL--DDKNVEFCYFGFADPSEY-EHPAWIMRNYAAFLL 237
Cdd:pfam16420 161 SEeteslVDAVQTWRYSVDARQHFF-LVKKSRGSDWEIASLSEYenFFADVEDVYFGFADPSTLpENPGWPLRNLLALLR 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19922550   238 QQCPSfvgKPLKFLGLRHNQQMNIDD--SLVWKVIQTEACDLSQSENIKFVGWELNKNGKMGPRMVCMRDSM 307
Cdd:pfam16420 240 ARWPL---KKVQVLCYRDNSRSGRRDerSLVLTLKLPEPSDENTSELPKAVGWERNANGKLGPRVVDLSSYM 308
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 327-576 6.65e-39

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: 143.94  E-value: 6.65e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922550   327 RLVPDLNLEIISQTKCLLFGAGTLGCAVARNLLSWGFKHITLLDSGKVGFSNPVRQNLYTHADAvagNRMKATTAAQRLK 406
Cdd:pfam00899   8 PLIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADI---GKPKAEVAAERLR 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922550   407 EINPSAETAGYVLEIpmpghtigesllaqTKEhlkVIEKLVQDHDVIFLLTDSRESRWLPTLLGAAKEKIVINAA-LGFD 485
Cdd:pfam00899  85 EINPDVEVEAYTERL--------------TPE---NAEELIKSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGvLGFK 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922550   486 SYLVMrhgttrkeagddgqeieglkcINGDQLGCYFCNDVTAPgnslkDRTLDQQCTVT---RPGVSNIAASYAVELLVA 562
Cdd:pfam00899 148 GQVTV---------------------VIPGKTPCYRCLFPEDP-----PPKLVPSCTVAgvlGPTTAVVAGLQALEALKL 201

                         250
                  ....*....|....
gi 19922550   563 LLQHPRKELAPAYY 576
Cdd:pfam00899 202 LLGKGEPNLAGRLL 215
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 341-493 2.92e-17

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: 78.85  E-value: 2.92e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922550 341 KCLLFGAGTLGCAVARNLLSWGFKHITLLDSGKVGFSNPVRQNLYTHADAvagNRMKATTAAQRLKEINPSAETAGYVLE 420
Cdd:cd01483   1 RVLLVGLGGLGSEIALNLARSGVGKITLIDFDTVELSNLNRQFLARQADI---GKPKAEVAARRLNELNPGVNVTAVPEG 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19922550 421 IPMPGhtigesllaqtkehlkvIEKLVQDHDVIFLLTDSRESRWLptLLGAAKEKI--VINAALGFDSYLVMRHG 493
Cdd:cd01483  78 ISEDN-----------------LDDFLDGVDLVIDAIDNIAVRRA--LNRACKELGipVIDAGGLGLGGDIQVID 133
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 328-465 7.02e-14

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


Pssm-ID: 238386 [Multi-domain]  Cd Length: 228  Bit Score: 71.35  E-value: 7.02e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922550 328 LVPDLNLEI---ISQTKCLLFGAGTLGCAVARNLLSWGFKHITLLDSGKVGFSNPVRQNLYTHADAvagNRMKATTAAQR 404
Cdd:cd00757   7 LLPEIGEEGqekLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRQILHTEADV---GQPKAEAAAER 83

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19922550 405 LKEINPSAETAGYVLEIpmpghtigesllaqTKEHLkviEKLVQDHDVIFLLTDSRESRWL 465
Cdd:cd00757  84 LRAINPDVEIEAYNERL--------------DAENA---EELIAGYDLVLDCTDNFATRYL 127
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 337-465 2.59e-13

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 71.56  E-value: 2.59e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922550  337 ISQTKCLLFGAGTLGCAVARNLLSWGFKHITLLDSGKVGFSNPVRQNLYTHADAVagNRM-KATTAAQRLKEINPSAETA 415
Cdd:PRK07688  22 LREKHVLIIGAGALGTANAEMLVRAGVGKVTIVDRDYVEWSNLQRQQLYTESDVK--NNLpKAVAAKKRLEEINSDVRVE 99

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 19922550  416 GYVLEIpmpghTIGEsllaqtkehlkvIEKLVQDHDVIFLLTDSRESRWL 465
Cdd:PRK07688 100 AIVQDV-----TAEE------------LEELVTGVDLIIDATDNFETRFI 132
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 335-488 2.68e-13

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: 70.16  E-value: 2.68e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922550 335 EIISQTKCLLFGAGTLGCAVARNLLSWGFKHITLLDSGKVGFSNPVRQNLYTHADAvagNRMKATTAAQRLKEINPSaet 414
Cdd:COG0476  23 EKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADV---GRPKVEAAAERLRALNPD--- 96

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19922550 415 agyvLEIpmpgHTIGESLLAQTkehlkvIEKLVQDHDVIFLLTDSRESRwlpTLLGAA--KEKI--VINAALGFDSYL 488
Cdd:COG0476  97 ----VEV----EAIPERLTEEN------ALELLAGADLVLDCTDNFATR---YLLNDAcvKLGIplVSGAVIGFEGQV 157
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 337-465 1.08e-11

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 66.68  E-value: 1.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922550  337 ISQTKCLLFGAGTLGCAVARNLLSWGFKHITLLDSGKVGFSNPVRQNLYTHADavAGNRM-KATTAAQRLKEINPSAETA 415
Cdd:PRK12475  22 IREKHVLIVGAGALGAANAEALVRAGIGKLTIADRDYVEWSNLQRQQLYTEED--AKQKKpKAIAAKEHLRKINSEVEIV 99

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 19922550  416 GYVLEIPMpghtigesllaQTkehlkvIEKLVQDHDVIFLLTDSRESRWL 465
Cdd:PRK12475 100 PVVTDVTV-----------EE------LEELVKEVDLIIDATDNFDTRLL 132
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 339-481 6.20e-10

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 60.24  E-value: 6.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922550  339 QTKCLLFGAGTLGCAVARNLLSWGFKHITLLDSGKVGFSNPVRQNLytHADAVAGnRMKATTAAQRLKEINPSAETagyv 418
Cdd:PRK05690  32 AARVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVSLSNLQRQVL--HDDATIG-QPKVESARAALARINPHIAI---- 104

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19922550  419 leipmpgHTIGESLLAQTkehlkvIEKLVQDHDVIFLLTDSRESRWLPTLLGAAKEKIVINAA 481
Cdd:PRK05690 105 -------ETINARLDDDE------LAALIAGHDLVLDCTDNVATRNQLNRACFAAKKPLVSGA 154
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
 341-487 3.43e-08

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: 54.89  E-value: 3.43e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922550 341 KCLLFGAGTLGCAVARNLLSWGFKHITLLDSGKVGFSNPVRQNLYTHADAvagNRMKATTAAQRLKEINPSAETAGYVLE 420
Cdd:cd01484   1 KVLLVGAGGIGCELLKNLALMGFGQIHVIDMDTIDVSNLNRQFLFRPKDI---GRPKSEVAAEAVNDRNPNCKVVPYQNK 77

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19922550 421 IpMPGHTIGESLLAQtkehlkvieklvqdHDVIFLLTDSRESR-WLPTLLGAAKEKIVINAALGFDSY 487
Cdd:cd01484  78 V-GPEQDFNDTFFEQ--------------FHIIVNALDNIIARrYVNGMLIFLIVPLIESGTEGFKGN 130
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
322-453 6.16e-08

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 53.71  E-value: 6.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922550  322 KLMKWRLVPDLnLEIISQTKCLLFGAGTLGCAVARNLLSWGFKHITLLDSGKVGFSNPVRQNLYthADAVAgnrMKATTA 401
Cdd:PRK08644  12 AMLASRHTPKL-LEKLKKAKVGIAGAGGLGSNIAVALARSGVGNLKLVDFDVVEPSNLNRQQYF--ISQIG---MPKVEA 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 19922550  402 -AQRLKEINPSAETAGYVLEIpmpghtigesllaqTKEHlkvIEKLVQDHDVI 453
Cdd:PRK08644  86 lKENLLEINPFVEIEAHNEKI--------------DEDN---IEELFKDCDIV 121
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 343-410 1.09e-07

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 54.50  E-value: 1.09e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19922550  343 LLFGAGTLGCAVARNLLSWGFKHITLLDSGKVGFSNPVRQNLYTHADAvagNRMKATTAAQRLKEINP 410
Cdd:PRK05600  45 LVIGAGGLGCPAMQSLASAGVGTITLIDDDTVDVSNIHRQILFGASDV---GRPKVEVAAERLKEIQP 109
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 341-417 1.03e-06

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: 51.23  E-value: 1.03e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19922550 341 KCLLFGAGTLGCAVARNLLSWGFKHITLLDSGKVGFSNPVRQNLYTHADAvagNRMKATTAAQRLKEINPSAETAGY 417
Cdd:cd01489   1 KVLVVGAGGIGCELLKNLVLTGFGEIHIIDLDTIDLSNLNRQFLFRKKHV---GKSKAQVAKEAVLSFNPNVKIVAY 74
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 341-421 1.67e-06

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: 50.43  E-value: 1.67e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922550 341 KCLLFGAGTLGCAVARNLLSWGFKHITLLDSGKVGFSNPVRQNLYTHADAvagNRMKATTAAQRLKEINPSAETAGYVLE 420
Cdd:cd01488   1 KILVIGAGGLGCELLKNLALSGFRNIHVIDMDTIDVSNLNRQFLFREKDI---GKPKAEVAAKFVNDRVPGVNVTPHFGK 77


                .
gi 19922550 421 I 421
Cdd:cd01488  78 I 78
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
339-465 4.02e-06

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 49.62  E-value: 4.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922550  339 QTKCLLFGAGTLGCAVARNLLSWGFKHITLLDSGKVGFSNPVRQNLytHADAVAGnRMKATTAAQRLKEINPSAEtagyV 418
Cdd:PRK08762 135 EARVLLIGAGGLGSPAALYLAAAGVGTLGIVDHDVVDRSNLQRQIL--HTEDRVG-QPKVDSAAQRLAALNPDVQ----V 207

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 19922550  419 LEIPmpghtigESLLAQTkehlkvIEKLVQDHDVIFLLTDSRESRWL 465
Cdd:PRK08762 208 EAVQ-------ERVTSDN------VEALLQDVDVVVDGADNFPTRYL 241
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 335-492 4.49e-06

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 49.49  E-value: 4.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922550  335 EIISQTKCLLFGAGTLGCAVARNLLSWGFKHITLLDSGKVGFSNPVRQNLytHADAVAGnRMKATTAAQRLKEINPSAET 414
Cdd:PRK05597  24 QSLFDAKVAVIGAGGLGSPALLYLAGAGVGHITIIDDDTVDLSNLHRQVI--HSTAGVG-QPKAESAREAMLALNPDVKV 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922550  415 AGYVLEIPMPghtigeSLLAQTKehlkvieklvqDHDVIFLLTDSRESRWLPTlLGAAKEKI--VINAALGFDSYLVMRH 492
Cdd:PRK05597 101 TVSVRRLTWS------NALDELR-----------DADVILDGSDNFDTRHLAS-WAAARLGIphVWASILGFDAQLSVFH 162
E1_ThiF_like cd01487
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ...
 341-480 1.84e-05

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: 45.84  E-value: 1.84e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922550 341 KCLLFGAGTLGCAVARNLLSWGFKHITLLDSGKVGFSNPVRQNLYTHADavagNRMKATTAAQRLKEINPSAETAGYVLE 420
Cdd:cd01487   1 KVGIAGAGGLGSNIAVLLARSGVGNLKLVDFDVVEPSNLNRQQYFLSQI----GEPKVEALKENLREINPFVKIEAINIK 76

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19922550 421 IPMpghtigesllaqtkehlKVIEKLVQDHDVIFLLTDSRESRWL--PTLLGaAKEKIVINA 480
Cdd:cd01487  77 IDE-----------------NNLEGLFGDCDIVVEAFDNAETKAMlaESLLG-NKNKPVVCA 120
APPBP1_RUB cd01493
Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric ...
 342-422 2.72e-04

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: 43.83  E-value: 2.72e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922550 342 CLLfGAGTLGCAVARNLLSWGFKHITLLDSGKVGFSNpVRQNLYTHADAVAGNRMKATtaAQRLKEINPSAEtAGYVLEI 421
Cdd:cd01493  24 CLL-NATATGTEILKNLVLPGIGSFTIVDGSKVDEED-LGNNFFLDASSLGKSRAEAT--CELLQELNPDVN-GSAVEES 98


                .
gi 19922550 422 P 422
Cdd:cd01493  99 P 99
Aos1_SUMO cd01492
Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating ...
 339-460 5.14e-04

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: 41.89  E-value: 5.14e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922550 339 QTKCLLFGAGTLGCAVARNLLSWGFKHITLLDSGKVGFSNPVRQNLYthaDAVAGNRMKATTAAQRLKEINPSAETAGYV 418
Cdd:cd01492  21 SARILLIGLKGLGAEIAKNLVLSGIGSLTILDDRTVTEEDLGAQFLI---PAEDLGQNRAEASLERLRALNPRVKVSVDT 97

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 19922550 419 LEIPMpghtIGESLLAQ---------TKEHLKVIEKLVQDHDVIFLLTDSR 460
Cdd:cd01492  98 DDISE----KPEEFFSQfdvvvatelSRAELVKINELCRKLGVKFYATGVH 144
E1-1_like cd01485
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ...
 327-410 1.49e-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: 40.48  E-value: 1.49e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922550 327 RLVPDLNLEIISQTKCLLFGAGTLGCAVARNLLSWGFKHITLLDSGKVGFSNPVRQNLYTHADAVAGnRMKATTAAQRLK 406
Cdd:cd01485   7 RLWGDEAQNKLRSAKVLIIGAGALGAEIAKNLVLAGIDSITIVDHRLVSTEDLGSNFFLDAEVSNSG-MNRAAASYEFLQ 85


                ....
gi 19922550 407 EINP 410
Cdd:cd01485  86 ELNP 89
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
 333-413 3.12e-03

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: 39.90  E-value: 3.12e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922550 333 NLEIISQTKCLLFGAGTLGCAVARNLLSWGFKHITLLDSGKVGFSNPVRQnLYTHADAVAgnRMKATTAAQRLKEINPSA 412
Cdd:cd00755   5 GLEKLRNAHVAVVGLGGVGSWAAEALARSGVGKLTLIDFDVVCVSNLNRQ-IHALLSTVG--KPKVEVMAERIRDINPEC 81


                .
gi 19922550 413 E 413
Cdd:cd00755  82 E 82
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 337-410 4.30e-03

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: 40.26  E-value: 4.30e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19922550    337 ISQTKCLLFGAGTLGCAVARNLLSWGFKHITLLDSGKVGFSNpVRQNLYTHADAVAGNRMKATTaaQRLKEINP 410
Cdd:TIGR01408   22 MAKSNVLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWD-LSSNFFLSEDDVGRNRAEAVV--KKLAELNP 92
Ube1_repeat1 cd01491
Ubiquitin activating enzyme (E1), repeat 1. E1, a highly conserved small protein present ...
 337-460 5.00e-03

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: 39.56  E-value: 5.00e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922550 337 ISQTKCLLFGAGTLGCAVARNLLSWGFKHITLLDSGKVGFSNPVRQNLYTHADaVAGNRMKATTAaqRLKEINPsaetag 416
Cdd:cd01491  17 LQKSNVLISGLGGLGVEIAKNLILAGVKSVTLHDTKPCSWSDLSSQFYLREED-IGKNRAEASQA--RLAELNP------ 87

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 19922550 417 YVLEIPMPGHTIGESLL--------AQTKEHLKVIEKLVQDHDVIFLLTDSR 460
Cdd:cd01491  88 YVPVTVSTGPLTTDELLkfqvvvltDASLEDQLKINEFCHSPGIKFISADTR 139
 
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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