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Conserved domains on  [gi|1823752934|ref|NP_001366059|]
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ubiquitin-like modifier-activating enzyme ATG7 isoform 3 [Mus musculus]

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 ...
 27-713 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: 722.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823752934  27 FAPFNSALDVGFWHELTQKKLNEYRLDEAPKDIKGYYYNGDSAGL--PTRLTLEFSAFDMSASTPAHCCPAMGTLHNTNT 104
Cdd:TIGR01381   1 FVPFVSCVDTGFWNEVSKLKLNKWKLDDTPKCISGQLSLHQTEGFkcHLSLSYDSLSSLESTTGTHAQLSVSGILLNYNT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823752934 105 LEAFKTADKKLLLEQSANEIWEAIKSGAALENPMLLNKFLLLTFADLKKYHFYYWFCCPALCLPESIPLIRGPVSlDQRL 184
Cdd:TIGR01381  81 VESFKKVDKSDLLRSEAEKIWESIQTRKWLQDPSLLSQFFIISFADLKKFKFYYWFCFPALVYPSKVNKLSGLTE-SIKQ 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823752934 185 SPKQIQALEHAYDDLCRAEGVTALPYFLFKYDDDTVLVslLKHYSDFFQGQRtKITVGVYDPCNLAQYPGWPLRNFLVLA 264
Cdd:TIGR01381 160 EITPLESLGADHKILFDFYRKNNFPFFLYSKQSSKMLE--LSELENNTNPDD-ELCVGFADPSPVAYSAGWMLRNVLAAV 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823752934 265 AHRWsgsFQSVEVLCFRDRTMQGARDVTHSIifeVKLPEMAFSPD-----CPKAVGWEKNQKGGMGPRMVNLSGCMDPKR 339
Cdd:TIGR01381 237 AHLH---PTWKHVHIFSLRSADSIGIKYLWT---TLLPSAELSSDgaqnaVPKAVGWERNANGKLQPISVDLSKEFDPKR 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823752934 340 LAESSVDLNLKLMCWRLVPTLDLDKVVSVKCLLLGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQPLYEFEDCL 419
Cdd:TIGR01381 311 LAERSVDLNLKLMKWRLHPDLQLERYSQLKVLLLGAGTLGCNVARCLIGWGVRHITFVDNGKVSYSNPVRQSLSNFEDCL 390

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823752934 420 GGGKPKALAAAERLQKIFPGVNARGFNMSIPMPGHPVNFSDVtmEQARRDVEQLEQLIDNHDVIFLLMDTRESRWLPTVI 499
Cdd:TIGR01381 391 LGGRGKAETAQKALKRIFPSIQATGHRLTVPMPGHPIDEKDV--PELEKDIARLEQLIKDHDVVFLLLDSREARWLPTVL 468

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823752934 500 AASKRKLVINAALGFDTFVVMRHglkkpkqqGAGdlcPSHLVapADLGSSlfANIPGYKLGCYFCNDVVAPGDSTRDRTL 579
Cdd:TIGR01381 469 CSRHKKIAISAALGFDSYVVMRH--------GIG---RSESV--SDVSSS--DSVPYSRLGCYFCNDVTAPGDSTTDRTL 533

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823752934 580 DQQCTVSRPGLAVIAGALAVELMVSVLQHPEGGYAIASSSDDrmnepPTSLGLVPHQIRGFLSRFDNVLPVSLAFDKCTA 659
Cdd:TIGR01381 534 DQQCTVTRPGTAMIASGLAVELLVSVLQHPLPSKTPASHDDN-----TTVLGALPHQIRGFLGRFQQILLSVKRFDQCVA 608

                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1823752934 660 CSPKVLDQYEREGFTFLAKVFNSShSFLEDLTGLTLLHQETQAAEIwDMSDEET 713
Cdd:TIGR01381 609 CSDAVAAEYQQRGWKFVRDAMNSP-GYLEDLTGLTELKNESSVNAI-DIQDFES 660
 
Name Accession Description Interval E-value
E1_like_apg7 TIGR01381
E1-like protein-activating enzyme Gsa7p/Apg7p; This model represents a family of eukaryotic ...
 27-713 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: 722.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823752934  27 FAPFNSALDVGFWHELTQKKLNEYRLDEAPKDIKGYYYNGDSAGL--PTRLTLEFSAFDMSASTPAHCCPAMGTLHNTNT 104
Cdd:TIGR01381   1 FVPFVSCVDTGFWNEVSKLKLNKWKLDDTPKCISGQLSLHQTEGFkcHLSLSYDSLSSLESTTGTHAQLSVSGILLNYNT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823752934 105 LEAFKTADKKLLLEQSANEIWEAIKSGAALENPMLLNKFLLLTFADLKKYHFYYWFCCPALCLPESIPLIRGPVSlDQRL 184
Cdd:TIGR01381  81 VESFKKVDKSDLLRSEAEKIWESIQTRKWLQDPSLLSQFFIISFADLKKFKFYYWFCFPALVYPSKVNKLSGLTE-SIKQ 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823752934 185 SPKQIQALEHAYDDLCRAEGVTALPYFLFKYDDDTVLVslLKHYSDFFQGQRtKITVGVYDPCNLAQYPGWPLRNFLVLA 264
Cdd:TIGR01381 160 EITPLESLGADHKILFDFYRKNNFPFFLYSKQSSKMLE--LSELENNTNPDD-ELCVGFADPSPVAYSAGWMLRNVLAAV 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823752934 265 AHRWsgsFQSVEVLCFRDRTMQGARDVTHSIifeVKLPEMAFSPD-----CPKAVGWEKNQKGGMGPRMVNLSGCMDPKR 339
Cdd:TIGR01381 237 AHLH---PTWKHVHIFSLRSADSIGIKYLWT---TLLPSAELSSDgaqnaVPKAVGWERNANGKLQPISVDLSKEFDPKR 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823752934 340 LAESSVDLNLKLMCWRLVPTLDLDKVVSVKCLLLGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQPLYEFEDCL 419
Cdd:TIGR01381 311 LAERSVDLNLKLMKWRLHPDLQLERYSQLKVLLLGAGTLGCNVARCLIGWGVRHITFVDNGKVSYSNPVRQSLSNFEDCL 390

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823752934 420 GGGKPKALAAAERLQKIFPGVNARGFNMSIPMPGHPVNFSDVtmEQARRDVEQLEQLIDNHDVIFLLMDTRESRWLPTVI 499
Cdd:TIGR01381 391 LGGRGKAETAQKALKRIFPSIQATGHRLTVPMPGHPIDEKDV--PELEKDIARLEQLIKDHDVVFLLLDSREARWLPTVL 468

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823752934 500 AASKRKLVINAALGFDTFVVMRHglkkpkqqGAGdlcPSHLVapADLGSSlfANIPGYKLGCYFCNDVVAPGDSTRDRTL 579
Cdd:TIGR01381 469 CSRHKKIAISAALGFDSYVVMRH--------GIG---RSESV--SDVSSS--DSVPYSRLGCYFCNDVTAPGDSTTDRTL 533

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823752934 580 DQQCTVSRPGLAVIAGALAVELMVSVLQHPEGGYAIASSSDDrmnepPTSLGLVPHQIRGFLSRFDNVLPVSLAFDKCTA 659
Cdd:TIGR01381 534 DQQCTVTRPGTAMIASGLAVELLVSVLQHPLPSKTPASHDDN-----TTVLGALPHQIRGFLGRFQQILLSVKRFDQCVA 608

                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1823752934 660 CSPKVLDQYEREGFTFLAKVFNSShSFLEDLTGLTLLHQETQAAEIwDMSDEET 713
Cdd:TIGR01381 609 CSDAVAAEYQQRGWKFVRDAMNSP-GYLEDLTGLTELKNESSVNAI-DIQDFES 660
Apg7 cd01486
Apg7 is an E1-like protein, that activates two different ubiquitin-like proteins, Apg12 and ...
 369-693 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: 570.08  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823752934 369 KCLLLGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQPLYEFEDClGGGKPKALAAAERLQKIFPGVNARGFNMS 448
Cdd:cd01486     1 KCLLLGAGTLGCNVARNLLGWGVRHITFVDSGKVSYSNPVRQSLFTFEDC-KGGKPKAEAAAERLKEIFPSIDATGIVLS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823752934 449 IPMPGHPVNFSDVtmEQARRDVEQLEQLIDNHDVIFLLMDTRESRWLPTVIAASKRKLVINAALGFDTFVVMRHGLKKPK 528
Cdd:cd01486    80 IPMPGHPISESEV--PSTLKDVKRLEELIKDHDVIFLLTDSRESRWLPTLLSAAKNKLVINAALGFDSYLVMRHGAGPQS 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823752934 529 QQGAGDlcpshlvapadlgsSLFANIPGYKLGCYFCNDVVAPGDSTRDRTLDQQCTVSRPGLAVIAGALAVELMVSVLQH 608
Cdd:cd01486   158 QSGSGD--------------SSSDSIPGSRLGCYFCNDVVAPGDSLKDRTLDQQCTVTRPGLSMIASSIAVELLVSLLQH 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823752934 609 PEGGYAIASSSDDRMNEPPTSLGLVPHQIRGFLSRFDNVLPVSLAFDKCTACSPKVLDQYEREGFTFLAKVFNSSHsFLE 688
Cdd:cd01486   224 PLGGHAPAESSSNEGDEPTTVLGILPHQIRGFLSNFSNLTLSGQAYDQCTACSDAVIDEYHREGWEFVLKAFNSPD-YLE 302


                  ....*
gi 1823752934 689 DLTGL 693
Cdd:cd01486   303 ELTGL 307
ATG7_N pfam16420
Ubiquitin-like modifier-activating enzyme ATG7 N-terminus; This is the N-terminal domain of ...
 25-335 9.23e-143

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: 419.74  E-value: 9.23e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823752934  25 LQFAPFNSALDVGFWHELTQKKLNEYRLDEAPKDIKGYYYNGDSAGLPTRLTLEFSAFDM-SASTPAHCCPAMGTLHNTN 103
Cdd:pfam16420   1 LQFAPFSSFIDPSFWHELSSLKLDVLKLDDSPRPILGLYEPRDAPGLSCRLQLDGSSFNDtSDAVPPGSCRAEGTLKNFN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823752934 104 TLEAFKTADKKLLLEQSANEIWEAIKSGAALENPMLLNKFLLLTFADLKKYHFYYWFCCPALCLPesIPLIRGPVSLDQR 183
Cdd:pfam16420  81 TIEEFKNLDKQALLDDAGKKIWDAILSGTALEDPSLLSRFLLLSFADLKKYKFYYWFAFPALHSD--PAWVLSWKPASEE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823752934 184 LSPKQIQALEHAYDDLCRAEGVTALpYFLFKYDDDTVL-VSLLKHYSDFFQGqRTKITVGVYDPCNLAQYPGWPLRNFLV 262
Cdd:pfam16420 159 LSSEETESLVDAVQTWRYSVDARQH-FFLVKKSRGSDWeIASLSEYENFFAD-VEDVYFGFADPSTLPENPGWPLRNLLA 236

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1823752934 263 LAAHRWSGSfqSVEVLCFRDRTMQGARDvTHSIIFEVKLPE--MAFSPDCPKAVGWEKNQKGGMGPRMVNLSGCM 335
Cdd:pfam16420 237 LLRARWPLK--KVQVLCYRDNSRSGRRD-ERSLVLTLKLPEpsDENTSELPKAVGWERNANGKLGPRVVDLSSYM 308
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 371-515 5.96e-14

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: 72.08  E-value: 5.96e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823752934 371 LLLGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQPLYEFEDClggGKPKALAAAERLQKIFPGVNARGFNMSIp 450
Cdd:COG0476    31 LVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADV---GRPKVEAAAERLRALNPDVEVEAIPERL- 106

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1823752934 451 mpghpvnfsdvtmeqarrDVEQLEQLIDNHDVIFLLMDTRESR-WLPTVIAASKRKLVINAALGFD 515
Cdd:COG0476   107 ------------------TEENALELLAGADLVLDCTDNFATRyLLNDACVKLGIPLVSGAVIGFE 154
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 363-504 8.27e-13

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 70.02  E-value: 8.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823752934 363 DKVVSVKCLLLGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQPLYEFED---CLgggkPKALAAAERLQKIfpg 439
Cdd:PRK07688   20 QKLREKHVLIIGAGALGTANAEMLVRAGVGKVTIVDRDYVEWSNLQRQQLYTESDvknNL----PKAVAAKKRLEEI--- 92

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1823752934 440 vNargfnmsipmpghpvnfSDVTMEQARRDV--EQLEQLIDNHDVIFLLMDTRESRWLPTVIAASKR 504
Cdd:PRK07688   93 -N-----------------SDVRVEAIVQDVtaEELEELVTGVDLIIDATDNFETRFIVNDAAQKYG 141
 
Name Accession Description Interval E-value
E1_like_apg7 TIGR01381
E1-like protein-activating enzyme Gsa7p/Apg7p; This model represents a family of eukaryotic ...
 27-713 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: 722.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823752934  27 FAPFNSALDVGFWHELTQKKLNEYRLDEAPKDIKGYYYNGDSAGL--PTRLTLEFSAFDMSASTPAHCCPAMGTLHNTNT 104
Cdd:TIGR01381   1 FVPFVSCVDTGFWNEVSKLKLNKWKLDDTPKCISGQLSLHQTEGFkcHLSLSYDSLSSLESTTGTHAQLSVSGILLNYNT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823752934 105 LEAFKTADKKLLLEQSANEIWEAIKSGAALENPMLLNKFLLLTFADLKKYHFYYWFCCPALCLPESIPLIRGPVSlDQRL 184
Cdd:TIGR01381  81 VESFKKVDKSDLLRSEAEKIWESIQTRKWLQDPSLLSQFFIISFADLKKFKFYYWFCFPALVYPSKVNKLSGLTE-SIKQ 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823752934 185 SPKQIQALEHAYDDLCRAEGVTALPYFLFKYDDDTVLVslLKHYSDFFQGQRtKITVGVYDPCNLAQYPGWPLRNFLVLA 264
Cdd:TIGR01381 160 EITPLESLGADHKILFDFYRKNNFPFFLYSKQSSKMLE--LSELENNTNPDD-ELCVGFADPSPVAYSAGWMLRNVLAAV 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823752934 265 AHRWsgsFQSVEVLCFRDRTMQGARDVTHSIifeVKLPEMAFSPD-----CPKAVGWEKNQKGGMGPRMVNLSGCMDPKR 339
Cdd:TIGR01381 237 AHLH---PTWKHVHIFSLRSADSIGIKYLWT---TLLPSAELSSDgaqnaVPKAVGWERNANGKLQPISVDLSKEFDPKR 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823752934 340 LAESSVDLNLKLMCWRLVPTLDLDKVVSVKCLLLGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQPLYEFEDCL 419
Cdd:TIGR01381 311 LAERSVDLNLKLMKWRLHPDLQLERYSQLKVLLLGAGTLGCNVARCLIGWGVRHITFVDNGKVSYSNPVRQSLSNFEDCL 390

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823752934 420 GGGKPKALAAAERLQKIFPGVNARGFNMSIPMPGHPVNFSDVtmEQARRDVEQLEQLIDNHDVIFLLMDTRESRWLPTVI 499
Cdd:TIGR01381 391 LGGRGKAETAQKALKRIFPSIQATGHRLTVPMPGHPIDEKDV--PELEKDIARLEQLIKDHDVVFLLLDSREARWLPTVL 468

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823752934 500 AASKRKLVINAALGFDTFVVMRHglkkpkqqGAGdlcPSHLVapADLGSSlfANIPGYKLGCYFCNDVVAPGDSTRDRTL 579
Cdd:TIGR01381 469 CSRHKKIAISAALGFDSYVVMRH--------GIG---RSESV--SDVSSS--DSVPYSRLGCYFCNDVTAPGDSTTDRTL 533

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823752934 580 DQQCTVSRPGLAVIAGALAVELMVSVLQHPEGGYAIASSSDDrmnepPTSLGLVPHQIRGFLSRFDNVLPVSLAFDKCTA 659
Cdd:TIGR01381 534 DQQCTVTRPGTAMIASGLAVELLVSVLQHPLPSKTPASHDDN-----TTVLGALPHQIRGFLGRFQQILLSVKRFDQCVA 608

                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1823752934 660 CSPKVLDQYEREGFTFLAKVFNSShSFLEDLTGLTLLHQETQAAEIwDMSDEET 713
Cdd:TIGR01381 609 CSDAVAAEYQQRGWKFVRDAMNSP-GYLEDLTGLTELKNESSVNAI-DIQDFES 660
Apg7 cd01486
Apg7 is an E1-like protein, that activates two different ubiquitin-like proteins, Apg12 and ...
 369-693 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: 570.08  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823752934 369 KCLLLGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQPLYEFEDClGGGKPKALAAAERLQKIFPGVNARGFNMS 448
Cdd:cd01486     1 KCLLLGAGTLGCNVARNLLGWGVRHITFVDSGKVSYSNPVRQSLFTFEDC-KGGKPKAEAAAERLKEIFPSIDATGIVLS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823752934 449 IPMPGHPVNFSDVtmEQARRDVEQLEQLIDNHDVIFLLMDTRESRWLPTVIAASKRKLVINAALGFDTFVVMRHGLKKPK 528
Cdd:cd01486    80 IPMPGHPISESEV--PSTLKDVKRLEELIKDHDVIFLLTDSRESRWLPTLLSAAKNKLVINAALGFDSYLVMRHGAGPQS 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823752934 529 QQGAGDlcpshlvapadlgsSLFANIPGYKLGCYFCNDVVAPGDSTRDRTLDQQCTVSRPGLAVIAGALAVELMVSVLQH 608
Cdd:cd01486   158 QSGSGD--------------SSSDSIPGSRLGCYFCNDVVAPGDSLKDRTLDQQCTVTRPGLSMIASSIAVELLVSLLQH 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823752934 609 PEGGYAIASSSDDRMNEPPTSLGLVPHQIRGFLSRFDNVLPVSLAFDKCTACSPKVLDQYEREGFTFLAKVFNSSHsFLE 688
Cdd:cd01486   224 PLGGHAPAESSSNEGDEPTTVLGILPHQIRGFLSNFSNLTLSGQAYDQCTACSDAVIDEYHREGWEFVLKAFNSPD-YLE 302


                  ....*
gi 1823752934 689 DLTGL 693
Cdd:cd01486   303 ELTGL 307
ATG7_N pfam16420
Ubiquitin-like modifier-activating enzyme ATG7 N-terminus; This is the N-terminal domain of ...
 25-335 9.23e-143

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: 419.74  E-value: 9.23e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823752934  25 LQFAPFNSALDVGFWHELTQKKLNEYRLDEAPKDIKGYYYNGDSAGLPTRLTLEFSAFDM-SASTPAHCCPAMGTLHNTN 103
Cdd:pfam16420   1 LQFAPFSSFIDPSFWHELSSLKLDVLKLDDSPRPILGLYEPRDAPGLSCRLQLDGSSFNDtSDAVPPGSCRAEGTLKNFN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823752934 104 TLEAFKTADKKLLLEQSANEIWEAIKSGAALENPMLLNKFLLLTFADLKKYHFYYWFCCPALCLPesIPLIRGPVSLDQR 183
Cdd:pfam16420  81 TIEEFKNLDKQALLDDAGKKIWDAILSGTALEDPSLLSRFLLLSFADLKKYKFYYWFAFPALHSD--PAWVLSWKPASEE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823752934 184 LSPKQIQALEHAYDDLCRAEGVTALpYFLFKYDDDTVL-VSLLKHYSDFFQGqRTKITVGVYDPCNLAQYPGWPLRNFLV 262
Cdd:pfam16420 159 LSSEETESLVDAVQTWRYSVDARQH-FFLVKKSRGSDWeIASLSEYENFFAD-VEDVYFGFADPSTLPENPGWPLRNLLA 236

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1823752934 263 LAAHRWSGSfqSVEVLCFRDRTMQGARDvTHSIIFEVKLPE--MAFSPDCPKAVGWEKNQKGGMGPRMVNLSGCM 335
Cdd:pfam16420 237 LLRARWPLK--KVQVLCYRDNSRSGRRD-ERSLVLTLKLPEpsDENTSELPKAVGWERNANGKLGPRVVDLSSYM 308
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 347-614 3.83e-48

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: 169.74  E-value: 3.83e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823752934 347 LNLKLMCwRLVPTLDLDKVVSVKCLLLGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQPLYEFEDClggGKPKA 426
Cdd:pfam00899   1 YSRQLAL-PLIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADI---GKPKA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823752934 427 LAAAERLQKIFPGVNARGFNMSIpmpghpvnfsdvtmeqarrDVEQLEQLIDNHDVIFLLMDTRESRWLPTVIAASKRKL 506
Cdd:pfam00899  77 EVAAERLREINPDVEVEAYTERL-------------------TPENAEELIKSFDIVVDATDNFAARYLVNDACVKLGKP 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823752934 507 VINAA-LGFDTFVVMRhglkkpkqqgagdlcpshlvapadlgsslfanIPGyKLGCYFCNDVVAPgdstrDRTLDQQCTV 585
Cdd:pfam00899 138 LIEAGvLGFKGQVTVV--------------------------------IPG-KTPCYRCLFPEDP-----PPKLVPSCTV 179

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1823752934 586 S---RPGLAVIAGALAVELMVSVLQHPEGGYA 614
Cdd:pfam00899 180 AgvlGPTTAVVAGLQALEALKLLLGKGEPNLA 211
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 369-524 1.50e-23

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: 96.95  E-value: 1.50e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823752934 369 KCLLLGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQPLYEFEDClggGKPKALAAAERLQKIFPGVNARGFNMS 448
Cdd:cd01483     1 RVLLVGLGGLGSEIALNLARSGVGKITLIDFDTVELSNLNRQFLARQADI---GKPKAEVAARRLNELNPGVNVTAVPEG 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1823752934 449 IPMpghpvnfsdvtmeqarrdvEQLEQLIDNHDVIFLLMDTRESRWLPTVIAASKRKLVINAALGFDTFVVMRHGL 524
Cdd:cd01483    78 ISE-------------------DNLDDFLDGVDLVIDAIDNIAVRRALNRACKELGIPVIDAGGLGLGGDIQVIDI 134
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 371-515 5.96e-14

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: 72.08  E-value: 5.96e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823752934 371 LLLGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQPLYEFEDClggGKPKALAAAERLQKIFPGVNARGFNMSIp 450
Cdd:COG0476    31 LVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADV---GRPKVEAAAERLRALNPDVEVEAIPERL- 106

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1823752934 451 mpghpvnfsdvtmeqarrDVEQLEQLIDNHDVIFLLMDTRESR-WLPTVIAASKRKLVINAALGFD 515
Cdd:COG0476   107 ------------------TEENALELLAGADLVLDCTDNFATRyLLNDACVKLGIPLVSGAVIGFE 154
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 371-515 3.69e-13

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: 69.43  E-value: 3.69e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823752934 371 LLLGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQPLYEFEDClggGKPKALAAAERLQKIFPGVNARGFNMSIp 450
Cdd:cd00757    25 LVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRQILHTEADV---GQPKAEAAAERLRAINPDVEIEAYNERL- 100

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1823752934 451 mpghpvnfsdvtmeqarrDVEQLEQLIDNHDVIFLLMDTRESRWLPTVIAASKRK-LVINAALGFD 515
Cdd:cd00757   101 ------------------DAENAEELIAGYDLVLDCTDNFATRYLINDACVKLGKpLVSGAVLGFE 148
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 363-504 8.27e-13

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 70.02  E-value: 8.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823752934 363 DKVVSVKCLLLGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQPLYEFED---CLgggkPKALAAAERLQKIfpg 439
Cdd:PRK07688   20 QKLREKHVLIIGAGALGTANAEMLVRAGVGKVTIVDRDYVEWSNLQRQQLYTESDvknNL----PKAVAAKKRLEEI--- 92

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1823752934 440 vNargfnmsipmpghpvnfSDVTMEQARRDV--EQLEQLIDNHDVIFLLMDTRESRWLPTVIAASKR 504
Cdd:PRK07688   93 -N-----------------SDVRVEAIVQDVtaEELEELVTGVDLIIDATDNFETRFIVNDAAQKYG 141
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 371-495 1.74e-11

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 66.29  E-value: 1.74e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823752934 371 LLLGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQPLYEFEDClGGGKPKALAAAERLQKIFPGVNARGFNMsip 450
Cdd:PRK12475   28 LIVGAGALGAANAEALVRAGIGKLTIADRDYVEWSNLQRQQLYTEEDA-KQKKPKAIAAKEHLRKINSEVEIVPVVT--- 103

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1823752934 451 mpghpvnfsDVTMeqarrdvEQLEQLIDNHDVIFLLMDTRESRWL 495
Cdd:PRK12475  104 ---------DVTV-------EELEELVKEVDLIIDATDNFDTRLL 132
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
355-524 2.46e-10

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 60.64  E-value: 2.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823752934 355 RLVPTLdLDKVVSVKCLLLGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQpLYEFEDClggGKPKALAAAERLQ 434
Cdd:PRK08644   17 RHTPKL-LEKLKKAKVGIAGAGGLGSNIAVALARSGVGNLKLVDFDVVEPSNLNRQ-QYFISQI---GMPKVEALKENLL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823752934 435 KIFPGVNargfnmsipmpghpvnfsdVTMEQARRDVEQLEQLIDNHDVIFLLMDTresrwlptviAASKRKLViNAALG- 513
Cdd:PRK08644   92 EINPFVE-------------------IEAHNEKIDEDNIEELFKDCDIVVEAFDN----------AETKAMLV-ETVLEh 141

                         170
                  ....*....|.
gi 1823752934 514 FDTFVVMRHGL 524
Cdd:PRK08644  142 PGKKLVAASGM 152
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 371-498 2.64e-09

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 59.51  E-value: 2.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823752934 371 LLLGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQPLYEFEDClggGKPKALAAAERLQKIFPG--VNARGFNMs 448
Cdd:PRK05600   45 LVIGAGGLGCPAMQSLASAGVGTITLIDDDTVDVSNIHRQILFGASDV---GRPKVEVAAERLKEIQPDirVNALRERL- 120

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1823752934 449 ipmpghpvnfsdvTMEQARRDVEQLEQLIDNHDVI---FLLMDTRESRWLPTV 498
Cdd:PRK05600  121 -------------TAENAVELLNGVDLVLDGSDSFatkFLVADAAEITGTPLV 160
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 369-478 6.03e-09

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: 58.16  E-value: 6.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823752934 369 KCLLLGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQPLYEFEDClggGKPKALAAAERLQKIFPGVNARGFNMS 448
Cdd:cd01489     1 KVLVVGAGGIGCELLKNLVLTGFGEIHIIDLDTIDLSNLNRQFLFRKKHV---GKSKAQVAKEAVLSFNPNVKIVAYHAN 77

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1823752934 449 IPMPGHPVNF---SDVTME-----QARRDVEQLEQLID 478
Cdd:cd01489    78 IKDPDFNVEFfkqFDLVFNaldnlAARRHVNKMCLAAD 115
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 369-515 9.71e-09

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 56.78  E-value: 9.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823752934 369 KCLLLGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQPLYEFEDClggGKPKALAAAERLQKIFPGVNARGFNms 448
Cdd:PRK05690   34 RVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVSLSNLQRQVLHDDATI---GQPKVESARAALARINPHIAIETIN-- 108

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1823752934 449 ipmpghpvnfsdvtmeqARRDVEQLEQLIDNHDVIfllMD------TRESrwLPTVIAASKRKLVINAALGFD 515
Cdd:PRK05690  109 -----------------ARLDDDELAALIAGHDLV---LDctdnvaTRNQ--LNRACFAAKKPLVSGAAIRME 159
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 369-441 2.55e-08

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: 55.82  E-value: 2.55e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1823752934 369 KCLLLGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQPLYEFEDClggGKPKALAAAERLQKIFPGVN 441
Cdd:cd01488     1 KILVIGAGGLGCELLKNLALSGFRNIHVIDMDTIDVSNLNRQFLFREKDI---GKPKAEVAAKFVNDRVPGVN 70
E1_ThiF_like cd01487
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ...
 369-524 2.49e-07

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: 51.23  E-value: 2.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823752934 369 KCLLLGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQPlYEFEDClggGKPKALAAAERLQKIFPgvnargfnms 448
Cdd:cd01487     1 KVGIAGAGGLGSNIAVLLARSGVGNLKLVDFDVVEPSNLNRQQ-YFLSQI---GEPKVEALKENLREINP---------- 66

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1823752934 449 ipmpghpvnFSDVTMEQARRDVEQLEQLIDNHDVIFLLMDTresrwlptviAASKRkLVINAALGF-DTFVVMRHGL 524
Cdd:cd01487    67 ---------FVKIEAINIKIDENNLEGLFGDCDIVVEAFDN----------AETKA-MLAESLLGNkNKPVVCASGM 123
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
 369-441 1.06e-06

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: 50.27  E-value: 1.06e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1823752934 369 KCLLLGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQPLYEFEDClggGKPKALAAAERLQKIFPGVN 441
Cdd:cd01484     1 KVLLVGAGGIGCELLKNLALMGFGQIHVIDMDTIDVSNLNRQFLFRPKDI---GRPKSEVAAEAVNDRNPNCK 70
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
364-483 7.07e-06

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 48.85  E-value: 7.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823752934 364 KVVSVKCLLLGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQPLYEfEDCLggGKPKALAAAERLQKIFPGVnar 443
Cdd:PRK08762  132 RLLEARVLLIGAGGLGSPAALYLAAAGVGTLGIVDHDVVDRSNLQRQILHT-EDRV--GQPKVDSAAQRLAALNPDV--- 205

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1823752934 444 gfnmsipmpghpvnfsDVTMEQARRDVEQLEQLIDNHDVI 483
Cdd:PRK08762  206 ----------------QVEAVQERVTSDNVEALLQDVDVV 229
PRK08328 PRK08328
hypothetical protein; Provisional
 363-501 1.36e-05

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 47.10  E-value: 1.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823752934 363 DKVVSVKCLLLGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQPLYEFEDClgGGKPKALAAAERLQKifpgvna 442
Cdd:PRK08328   23 EKLKKAKVAVVGVGGLGSPVAYYLAAAGVGRILLIDEQTPELSNLNRQILHWEEDL--GKNPKPLSAKWKLER------- 93

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1823752934 443 rgFNMSIPMPGHPVNFSDVTMEQARRDVEQLEQLIDNHDVIFLLMDTRESRWLPTVIAA 501
Cdd:PRK08328   94 --FNSDIKIETFVGRLSEENIDEVLKGVDVIVDCLDNFETRYLLDDYAHKKGIPLVHGA 150
E1-1_like cd01485
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ...
 355-441 3.65e-05

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: 45.11  E-value: 3.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823752934 355 RLVPTLDLDKVVSVKCLLLGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQPLYEFEDClGGGKPKALAAAERLQ 434
Cdd:cd01485     7 RLWGDEAQNKLRSAKVLIIGAGALGAEIAKNLVLAGIDSITIVDHRLVSTEDLGSNFFLDAEVS-NSGMNRAAASYEFLQ 85


                  ....*..
gi 1823752934 435 KIFPGVN 441
Cdd:cd01485    86 ELNPNVK 92
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 373-515 8.90e-05

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 45.25  E-value: 8.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823752934 373 LGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQPLYEFEdclGGGKPKALAAAERLQKIFPGVnargfnmsipmp 452
Cdd:PRK05597   34 IGAGGLGSPALLYLAGAGVGHITIIDDDTVDLSNLHRQVIHSTA---GVGQPKAESAREAMLALNPDV------------ 98

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1823752934 453 ghpvnfsDVTMEQARRDVEQLEQLIDNHDVIFLLMDTRESRWLPTVIAAskrKLVI----NAALGFD 515
Cdd:PRK05597   99 -------KVTVSVRRLTWSNALDELRDADVILDGSDNFDTRHLASWAAA---RLGIphvwASILGFD 155
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
 369-441 3.56e-04

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


Pssm-ID: 238767 [Multi-domain]  Cd Length: 435  Bit Score: 43.43  E-value: 3.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823752934 369 KCLLLGAGTLGC----NVArtLMGWGVR---HVTFVDNAKISYSNPVRQPLYEFEDClggGKPKALAAAERLQKIFPGVN 441
Cdd:cd01490     1 KVFLVGAGAIGCellkNFA--LMGVGTGesgEITVTDMDNIEKSNLNRQFLFRPHDV---GKPKSEVAAAAVKAMNPDLK 75
 
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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