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Conserved domains on  [gi|2462586505|ref|XP_054200916|]
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ubiquitin-like modifier-activating enzyme ATG7 isoform X19 [Homo sapiens]

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 ...
 15-695 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: 725.19  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586505  15 FAPFSSALDVGFWHELTQKKLNEYRLDEAPKDIKGYYYNGDSAGLPARLTL--EFSAFDMSAPTPARCCPAIGTLYNTNT 92
Cdd:TIGR01381   1 FVPFVSCVDTGFWNEVSKLKLNKWKLDDTPKCISGQLSLHQTEGFKCHLSLsyDSLSSLESTTGTHAQLSVSGILLNYNT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586505  93 LESFKTADKKLLLEQAANEIWESIKSGTALENPVLLNKFLLLTFADLKKYHFYYWFCYPALCLPESLPLIQGPVGlDQRF 172
Cdd:TIGR01381  81 VESFKKVDKSDLLRSEAEKIWESIQTRKWLQDPSLLSQFFIISFADLKKFKFYYWFCFPALVYPSKVNKLSGLTE-SIKQ 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586505 173 SLKQIEALECAYDNLCQTEGVTALPYFLIKYDENMVLVslLKHYSDFFQGQRtKITIGVYDPCNLAQYPGWPLRNFLVLA 252
Cdd:TIGR01381 160 EITPLESLGADHKILFDFYRKNNFPFFLYSKQSSKMLE--LSELENNTNPDD-ELCVGFADPSPVAYSAGWMLRNVLAAV 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586505 253 AHRWSSsFQSVEVVCFRDrtmqgARDVAHSIIFEVKLPEMAFSPD-----CPKAVGWEKNQKGGMGPRMVNLSECMDPKR 327
Cdd:TIGR01381 237 AHLHPT-WKHVHIFSLRS-----ADSIGIKYLWTTLLPSAELSSDgaqnaVPKAVGWERNANGKLQPISVDLSKEFDPKR 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586505 328 LAESSVDLNLKLMCWRLVPTLDLDKVVSVKCLLLGAGTLGCNVARTLMGWGVRHITFVDNAKISYSNPVRQPLYEFEDCL 407
Cdd:TIGR01381 311 LAERSVDLNLKLMKWRLHPDLQLERYSQLKVLLLGAGTLGCNVARCLIGWGVRHITFVDNGKVSYSNPVRQSLSNFEDCL 390

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586505 408 GGGKPKALAAADRLQKIFPGVNARGFNMSIPMPGHPVnfSSVTLEQARRDVEQLEQLIESHDVVFLLMDTRESRWLPAVI 487
Cdd:TIGR01381 391 LGGRGKAETAQKALKRIFPSIQATGHRLTVPMPGHPI--DEKDVPELEKDIARLEQLIKDHDVVFLLLDSREARWLPTVL 468

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586505 488 AASKRKLVINAALGFDTFVVMRHGlkkpkqqgagdlcpNHPVASADLLGSSlfANIPGYKLGCYFCNDVVAPGDSTRDRT 567
Cdd:TIGR01381 469 CSRHKKIAISAALGFDSYVVMRHG--------------IGRSESVSDVSSS--DSVPYSRLGCYFCNDVTAPGDSTTDRT 532

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586505 568 LDQQCTVSRPGLAVIAGALAVELMVSVLQHPEGGYAIASSSDDrmnepPTSLGLVPHQIRGFLSRFDNVLPVSLAFDKCT 647
Cdd:TIGR01381 533 LDQQCTVTRPGTAMIASGLAVELLVSVLQHPLPSKTPASHDDN-----TTVLGALPHQIRGFLGRFQQILLSVKRFDQCV 607

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*...
gi 2462586505 648 ACSSKVLDQYEREGFNFLAKVFNSShSFLEDLTGLTLLHQETQAAEME 695
Cdd:TIGR01381 608 ACSDAVAAEYQQRGWKFVRDAMNSP-GYLEDLTGLTELKNESSVNAID 654
 
Name Accession Description Interval E-value
E1_like_apg7 TIGR01381
E1-like protein-activating enzyme Gsa7p/Apg7p; This model represents a family of eukaryotic ...
 15-695 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: 725.19  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586505  15 FAPFSSALDVGFWHELTQKKLNEYRLDEAPKDIKGYYYNGDSAGLPARLTL--EFSAFDMSAPTPARCCPAIGTLYNTNT 92
Cdd:TIGR01381   1 FVPFVSCVDTGFWNEVSKLKLNKWKLDDTPKCISGQLSLHQTEGFKCHLSLsyDSLSSLESTTGTHAQLSVSGILLNYNT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586505  93 LESFKTADKKLLLEQAANEIWESIKSGTALENPVLLNKFLLLTFADLKKYHFYYWFCYPALCLPESLPLIQGPVGlDQRF 172
Cdd:TIGR01381  81 VESFKKVDKSDLLRSEAEKIWESIQTRKWLQDPSLLSQFFIISFADLKKFKFYYWFCFPALVYPSKVNKLSGLTE-SIKQ 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586505 173 SLKQIEALECAYDNLCQTEGVTALPYFLIKYDENMVLVslLKHYSDFFQGQRtKITIGVYDPCNLAQYPGWPLRNFLVLA 252
Cdd:TIGR01381 160 EITPLESLGADHKILFDFYRKNNFPFFLYSKQSSKMLE--LSELENNTNPDD-ELCVGFADPSPVAYSAGWMLRNVLAAV 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586505 253 AHRWSSsFQSVEVVCFRDrtmqgARDVAHSIIFEVKLPEMAFSPD-----CPKAVGWEKNQKGGMGPRMVNLSECMDPKR 327
Cdd:TIGR01381 237 AHLHPT-WKHVHIFSLRS-----ADSIGIKYLWTTLLPSAELSSDgaqnaVPKAVGWERNANGKLQPISVDLSKEFDPKR 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586505 328 LAESSVDLNLKLMCWRLVPTLDLDKVVSVKCLLLGAGTLGCNVARTLMGWGVRHITFVDNAKISYSNPVRQPLYEFEDCL 407
Cdd:TIGR01381 311 LAERSVDLNLKLMKWRLHPDLQLERYSQLKVLLLGAGTLGCNVARCLIGWGVRHITFVDNGKVSYSNPVRQSLSNFEDCL 390

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586505 408 GGGKPKALAAADRLQKIFPGVNARGFNMSIPMPGHPVnfSSVTLEQARRDVEQLEQLIESHDVVFLLMDTRESRWLPAVI 487
Cdd:TIGR01381 391 LGGRGKAETAQKALKRIFPSIQATGHRLTVPMPGHPI--DEKDVPELEKDIARLEQLIKDHDVVFLLLDSREARWLPTVL 468

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586505 488 AASKRKLVINAALGFDTFVVMRHGlkkpkqqgagdlcpNHPVASADLLGSSlfANIPGYKLGCYFCNDVVAPGDSTRDRT 567
Cdd:TIGR01381 469 CSRHKKIAISAALGFDSYVVMRHG--------------IGRSESVSDVSSS--DSVPYSRLGCYFCNDVTAPGDSTTDRT 532

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586505 568 LDQQCTVSRPGLAVIAGALAVELMVSVLQHPEGGYAIASSSDDrmnepPTSLGLVPHQIRGFLSRFDNVLPVSLAFDKCT 647
Cdd:TIGR01381 533 LDQQCTVTRPGTAMIASGLAVELLVSVLQHPLPSKTPASHDDN-----TTVLGALPHQIRGFLGRFQQILLSVKRFDQCV 607

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*...
gi 2462586505 648 ACSSKVLDQYEREGFNFLAKVFNSShSFLEDLTGLTLLHQETQAAEME 695
Cdd:TIGR01381 608 ACSDAVAAEYQQRGWKFVRDAMNSP-GYLEDLTGLTELKNESSVNAID 654
Apg7 cd01486
Apg7 is an E1-like protein, that activates two different ubiquitin-like proteins, Apg12 and ...
 357-682 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: 571.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586505 357 KCLLLGAGTLGCNVARTLMGWGVRHITFVDNAKISYSNPVRQPLYEFEDClGGGKPKALAAADRLQKIFPGVNARGFNMS 436
Cdd:cd01486     1 KCLLLGAGTLGCNVARNLLGWGVRHITFVDSGKVSYSNPVRQSLFTFEDC-KGGKPKAEAAAERLKEIFPSIDATGIVLS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586505 437 IPMPGHPVNFSSVtlEQARRDVEQLEQLIESHDVVFLLMDTRESRWLPAVIAASKRKLVINAALGFDTFVVMRHGLKKPK 516
Cdd:cd01486    80 IPMPGHPISESEV--PSTLKDVKRLEELIKDHDVIFLLTDSRESRWLPTLLSAAKNKLVINAALGFDSYLVMRHGAGPQS 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586505 517 QQGAGDlcpnhpvasadllgsSLFANIPGYKLGCYFCNDVVAPGDSTRDRTLDQQCTVSRPGLAVIAGALAVELMVSVLQ 596
Cdd:cd01486   158 QSGSGD---------------SSSDSIPGSRLGCYFCNDVVAPGDSLKDRTLDQQCTVTRPGLSMIASSIAVELLVSLLQ 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586505 597 HPEGGYAIASSSDDRMNEPPTSLGLVPHQIRGFLSRFDNVLPVSLAFDKCTACSSKVLDQYEREGFNFLAKVFNSSHsFL 676
Cdd:cd01486   223 HPLGGHAPAESSSNEGDEPTTVLGILPHQIRGFLSNFSNLTLSGQAYDQCTACSDAVIDEYHREGWEFVLKAFNSPD-YL 301


                  ....*.
gi 2462586505 677 EDLTGL 682
Cdd:cd01486   302 EELTGL 307
ATG7_N pfam16420
Ubiquitin-like modifier-activating enzyme ATG7 N-terminus; This is the N-terminal domain of ...
 13-323 2.45e-144

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: 425.51  E-value: 2.45e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586505  13 LQFAPFSSALDVGFWHELTQKKLNEYRLDEAPKDIKGYYYNGDSAGLPARLTLEFSAFDM-SAPTPARCCPAIGTLYNTN 91
Cdd:pfam16420   1 LQFAPFSSFIDPSFWHELSSLKLDVLKLDDSPRPILGLYEPRDAPGLSCRLQLDGSSFNDtSDAVPPGSCRAEGTLKNFN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586505  92 TLESFKTADKKLLLEQAANEIWESIKSGTALENPVLLNKFLLLTFADLKKYHFYYWFCYPALCLPEslPLIQGPVGLDQR 171
Cdd:pfam16420  81 TIEEFKNLDKQALLDDAGKKIWDAILSGTALEDPSLLSRFLLLSFADLKKYKFYYWFAFPALHSDP--AWVLSWKPASEE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586505 172 FSLKQIEALECAYDNLCQTEGVTALpYFLIKYDENMVL-VSLLKHYSDFFQGqRTKITIGVYDPCNLAQYPGWPLRNFLV 250
Cdd:pfam16420 159 LSSEETESLVDAVQTWRYSVDARQH-FFLVKKSRGSDWeIASLSEYENFFAD-VEDVYFGFADPSTLPENPGWPLRNLLA 236

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462586505 251 LAAHRWSSSfqSVEVVCFRDRTMQGARDvAHSIIFEVKLPE--MAFSPDCPKAVGWEKNQKGGMGPRMVNLSECM 323
Cdd:pfam16420 237 LLRARWPLK--KVQVLCYRDNSRSGRRD-ERSLVLTLKLPEpsDENTSELPKAVGWERNANGKLGPRVVDLSSYM 308
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 359-503 1.26e-15

Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; Molybdopterin or thiamine biosynthesis adenylyltransferase is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 440244 [Multi-domain]  Cd Length: 244  Bit Score: 77.09  E-value: 1.26e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586505 359 LLLGAGTLGCNVARTLMGWGVRHITFVDNAKISYSNPVRQPLYEFEDClggGKPKALAAADRLQKIFPGVNARGFNMSIp 438
Cdd:COG0476    31 LVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADV---GRPKVEAAAERLRALNPDVEVEAIPERL- 106

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462586505 439 mpghpvnfssvtleqarrDVEQLEQLIESHDVVFLLMDTRESR-WLPAVIAASKRKLVINAALGFD 503
Cdd:COG0476   107 ------------------TEENALELLAGADLVLDCTDNFATRyLLNDACVKLGIPLVSGAVIGFE 154
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 359-538 5.26e-11

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 65.29  E-value: 5.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586505 359 LLLGAGTLGCNVARTLMGWGVRHITFVDNAKISYSNPVRQPLYEFEDClggGKPKALAAADRLQKIFPGVnargfnmsip 438
Cdd:PRK05600   45 LVIGAGGLGCPAMQSLASAGVGTITLIDDDTVDVSNIHRQILFGASDV---GRPKVEVAAERLKEIQPDI---------- 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586505 439 mpghpvnfsSVTLEQARRDVEQLEQLIESHDVVFLLMDTRESRWLPAVIAA-SKRKLVINAALGFDTFVVMRHGLKKPKQ 517
Cdd:PRK05600  112 ---------RVNALRERLTAENAVELLNGVDLVLDGSDSFATKFLVADAAEiTGTPLVWGTVLRFHGELAVFNSGPDHRG 182

                         170       180
                  ....*....|....*....|....*...
gi 2462586505 518 QGAGDLCPNHPV-------ASADLLGSS 538
Cdd:PRK05600  183 VGLRDLFPEQPSgdsipdcATAGVLGAT 210
 
Name Accession Description Interval E-value
E1_like_apg7 TIGR01381
E1-like protein-activating enzyme Gsa7p/Apg7p; This model represents a family of eukaryotic ...
 15-695 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: 725.19  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586505  15 FAPFSSALDVGFWHELTQKKLNEYRLDEAPKDIKGYYYNGDSAGLPARLTL--EFSAFDMSAPTPARCCPAIGTLYNTNT 92
Cdd:TIGR01381   1 FVPFVSCVDTGFWNEVSKLKLNKWKLDDTPKCISGQLSLHQTEGFKCHLSLsyDSLSSLESTTGTHAQLSVSGILLNYNT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586505  93 LESFKTADKKLLLEQAANEIWESIKSGTALENPVLLNKFLLLTFADLKKYHFYYWFCYPALCLPESLPLIQGPVGlDQRF 172
Cdd:TIGR01381  81 VESFKKVDKSDLLRSEAEKIWESIQTRKWLQDPSLLSQFFIISFADLKKFKFYYWFCFPALVYPSKVNKLSGLTE-SIKQ 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586505 173 SLKQIEALECAYDNLCQTEGVTALPYFLIKYDENMVLVslLKHYSDFFQGQRtKITIGVYDPCNLAQYPGWPLRNFLVLA 252
Cdd:TIGR01381 160 EITPLESLGADHKILFDFYRKNNFPFFLYSKQSSKMLE--LSELENNTNPDD-ELCVGFADPSPVAYSAGWMLRNVLAAV 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586505 253 AHRWSSsFQSVEVVCFRDrtmqgARDVAHSIIFEVKLPEMAFSPD-----CPKAVGWEKNQKGGMGPRMVNLSECMDPKR 327
Cdd:TIGR01381 237 AHLHPT-WKHVHIFSLRS-----ADSIGIKYLWTTLLPSAELSSDgaqnaVPKAVGWERNANGKLQPISVDLSKEFDPKR 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586505 328 LAESSVDLNLKLMCWRLVPTLDLDKVVSVKCLLLGAGTLGCNVARTLMGWGVRHITFVDNAKISYSNPVRQPLYEFEDCL 407
Cdd:TIGR01381 311 LAERSVDLNLKLMKWRLHPDLQLERYSQLKVLLLGAGTLGCNVARCLIGWGVRHITFVDNGKVSYSNPVRQSLSNFEDCL 390

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586505 408 GGGKPKALAAADRLQKIFPGVNARGFNMSIPMPGHPVnfSSVTLEQARRDVEQLEQLIESHDVVFLLMDTRESRWLPAVI 487
Cdd:TIGR01381 391 LGGRGKAETAQKALKRIFPSIQATGHRLTVPMPGHPI--DEKDVPELEKDIARLEQLIKDHDVVFLLLDSREARWLPTVL 468

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586505 488 AASKRKLVINAALGFDTFVVMRHGlkkpkqqgagdlcpNHPVASADLLGSSlfANIPGYKLGCYFCNDVVAPGDSTRDRT 567
Cdd:TIGR01381 469 CSRHKKIAISAALGFDSYVVMRHG--------------IGRSESVSDVSSS--DSVPYSRLGCYFCNDVTAPGDSTTDRT 532

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586505 568 LDQQCTVSRPGLAVIAGALAVELMVSVLQHPEGGYAIASSSDDrmnepPTSLGLVPHQIRGFLSRFDNVLPVSLAFDKCT 647
Cdd:TIGR01381 533 LDQQCTVTRPGTAMIASGLAVELLVSVLQHPLPSKTPASHDDN-----TTVLGALPHQIRGFLGRFQQILLSVKRFDQCV 607

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*...
gi 2462586505 648 ACSSKVLDQYEREGFNFLAKVFNSShSFLEDLTGLTLLHQETQAAEME 695
Cdd:TIGR01381 608 ACSDAVAAEYQQRGWKFVRDAMNSP-GYLEDLTGLTELKNESSVNAID 654
Apg7 cd01486
Apg7 is an E1-like protein, that activates two different ubiquitin-like proteins, Apg12 and ...
 357-682 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: 571.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586505 357 KCLLLGAGTLGCNVARTLMGWGVRHITFVDNAKISYSNPVRQPLYEFEDClGGGKPKALAAADRLQKIFPGVNARGFNMS 436
Cdd:cd01486     1 KCLLLGAGTLGCNVARNLLGWGVRHITFVDSGKVSYSNPVRQSLFTFEDC-KGGKPKAEAAAERLKEIFPSIDATGIVLS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586505 437 IPMPGHPVNFSSVtlEQARRDVEQLEQLIESHDVVFLLMDTRESRWLPAVIAASKRKLVINAALGFDTFVVMRHGLKKPK 516
Cdd:cd01486    80 IPMPGHPISESEV--PSTLKDVKRLEELIKDHDVIFLLTDSRESRWLPTLLSAAKNKLVINAALGFDSYLVMRHGAGPQS 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586505 517 QQGAGDlcpnhpvasadllgsSLFANIPGYKLGCYFCNDVVAPGDSTRDRTLDQQCTVSRPGLAVIAGALAVELMVSVLQ 596
Cdd:cd01486   158 QSGSGD---------------SSSDSIPGSRLGCYFCNDVVAPGDSLKDRTLDQQCTVTRPGLSMIASSIAVELLVSLLQ 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586505 597 HPEGGYAIASSSDDRMNEPPTSLGLVPHQIRGFLSRFDNVLPVSLAFDKCTACSSKVLDQYEREGFNFLAKVFNSSHsFL 676
Cdd:cd01486   223 HPLGGHAPAESSSNEGDEPTTVLGILPHQIRGFLSNFSNLTLSGQAYDQCTACSDAVIDEYHREGWEFVLKAFNSPD-YL 301


                  ....*.
gi 2462586505 677 EDLTGL 682
Cdd:cd01486   302 EELTGL 307
ATG7_N pfam16420
Ubiquitin-like modifier-activating enzyme ATG7 N-terminus; This is the N-terminal domain of ...
 13-323 2.45e-144

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: 425.51  E-value: 2.45e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586505  13 LQFAPFSSALDVGFWHELTQKKLNEYRLDEAPKDIKGYYYNGDSAGLPARLTLEFSAFDM-SAPTPARCCPAIGTLYNTN 91
Cdd:pfam16420   1 LQFAPFSSFIDPSFWHELSSLKLDVLKLDDSPRPILGLYEPRDAPGLSCRLQLDGSSFNDtSDAVPPGSCRAEGTLKNFN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586505  92 TLESFKTADKKLLLEQAANEIWESIKSGTALENPVLLNKFLLLTFADLKKYHFYYWFCYPALCLPEslPLIQGPVGLDQR 171
Cdd:pfam16420  81 TIEEFKNLDKQALLDDAGKKIWDAILSGTALEDPSLLSRFLLLSFADLKKYKFYYWFAFPALHSDP--AWVLSWKPASEE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586505 172 FSLKQIEALECAYDNLCQTEGVTALpYFLIKYDENMVL-VSLLKHYSDFFQGqRTKITIGVYDPCNLAQYPGWPLRNFLV 250
Cdd:pfam16420 159 LSSEETESLVDAVQTWRYSVDARQH-FFLVKKSRGSDWeIASLSEYENFFAD-VEDVYFGFADPSTLPENPGWPLRNLLA 236

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462586505 251 LAAHRWSSSfqSVEVVCFRDRTMQGARDvAHSIIFEVKLPE--MAFSPDCPKAVGWEKNQKGGMGPRMVNLSECM 323
Cdd:pfam16420 237 LLRARWPLK--KVQVLCYRDNSRSGRRD-ERSLVLTLKLPEpsDENTSELPKAVGWERNANGKLGPRVVDLSSYM 308
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 335-603 3.42e-49

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: 173.21  E-value: 3.42e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586505 335 LNLKLMCwRLVPTLDLDKVVSVKCLLLGAGTLGCNVARTLMGWGVRHITFVDNAKISYSNPVRQPLYEFEDClggGKPKA 414
Cdd:pfam00899   1 YSRQLAL-PLIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADI---GKPKA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586505 415 LAAADRLQKIFPGVNARGFNMSIpmpghpvnfssvtleqarrDVEQLEQLIESHDVVFLLMDTRESRWLPAVIAASKRKL 494
Cdd:pfam00899  77 EVAAERLREINPDVEVEAYTERL-------------------TPENAEELIKSFDIVVDATDNFAARYLVNDACVKLGKP 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586505 495 VINAA-LGFDTFVVMRhglkkpkqqgagdlcpnhpvasadllgsslfanIPGyKLGCYFCNDVVAPgdstrDRTLDQQCT 573
Cdd:pfam00899 138 LIEAGvLGFKGQVTVV---------------------------------IPG-KTPCYRCLFPEDP-----PPKLVPSCT 178

                         250       260       270
                  ....*....|....*....|....*....|...
gi 2462586505 574 VS---RPGLAVIAGALAVELMVSVLQHPEGGYA 603
Cdd:pfam00899 179 VAgvlGPTTAVVAGLQALEALKLLLGKGEPNLA 211
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 357-512 1.31e-24

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: 100.04  E-value: 1.31e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586505 357 KCLLLGAGTLGCNVARTLMGWGVRHITFVDNAKISYSNPVRQPLYEFEDClggGKPKALAAADRLQKIFPGVNARGFNMS 436
Cdd:cd01483     1 RVLLVGLGGLGSEIALNLARSGVGKITLIDFDTVELSNLNRQFLARQADI---GKPKAEVAARRLNELNPGVNVTAVPEG 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462586505 437 IPMpghpvnfssvtleqarrdvEQLEQLIESHDVVFLLMDTRESRWLPAVIAASKRKLVINAALGFDTFVVMRHGL 512
Cdd:cd01483    78 ISE-------------------DNLDDFLDGVDLVIDAIDNIAVRRALNRACKELGIPVIDAGGLGLGGDIQVIDI 134
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 359-503 1.26e-15

Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; Molybdopterin or thiamine biosynthesis adenylyltransferase is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 440244 [Multi-domain]  Cd Length: 244  Bit Score: 77.09  E-value: 1.26e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586505 359 LLLGAGTLGCNVARTLMGWGVRHITFVDNAKISYSNPVRQPLYEFEDClggGKPKALAAADRLQKIFPGVNARGFNMSIp 438
Cdd:COG0476    31 LVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADV---GRPKVEAAAERLRALNPDVEVEAIPERL- 106

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462586505 439 mpghpvnfssvtleqarrDVEQLEQLIESHDVVFLLMDTRESR-WLPAVIAASKRKLVINAALGFD 503
Cdd:COG0476   107 ------------------TEENALELLAGADLVLDCTDNFATRyLLNDACVKLGIPLVSGAVIGFE 154
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 359-503 2.42e-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: 72.90  E-value: 2.42e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586505 359 LLLGAGTLGCNVARTLMGWGVRHITFVDNAKISYSNPVRQPLYEFEDClggGKPKALAAADRLQKIFPGVNARGFNMSIp 438
Cdd:cd00757    25 LVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRQILHTEADV---GQPKAEAAAERLRAINPDVEIEAYNERL- 100

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462586505 439 mpghpvnfssvtleqarrDVEQLEQLIESHDVVFLLMDTRESRWLPAVIAASKRK-LVINAALGFD 503
Cdd:cd00757   101 ------------------DAENAEELIAGYDLVLDCTDNFATRYLINDACVKLGKpLVSGAVLGFE 148
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 359-538 5.26e-11

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 65.29  E-value: 5.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586505 359 LLLGAGTLGCNVARTLMGWGVRHITFVDNAKISYSNPVRQPLYEFEDClggGKPKALAAADRLQKIFPGVnargfnmsip 438
Cdd:PRK05600   45 LVIGAGGLGCPAMQSLASAGVGTITLIDDDTVDVSNIHRQILFGASDV---GRPKVEVAAERLKEIQPDI---------- 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586505 439 mpghpvnfsSVTLEQARRDVEQLEQLIESHDVVFLLMDTRESRWLPAVIAA-SKRKLVINAALGFDTFVVMRHGLKKPKQ 517
Cdd:PRK05600  112 ---------RVNALRERLTAENAVELLNGVDLVLDGSDSFATKFLVADAAEiTGTPLVWGTVLRFHGELAVFNSGPDHRG 182

                         170       180
                  ....*....|....*....|....*...
gi 2462586505 518 QGAGDLCPNHPV-------ASADLLGSS 538
Cdd:PRK05600  183 VGLRDLFPEQPSgdsipdcATAGVLGAT 210
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 351-483 7.07e-11

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 64.24  E-value: 7.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586505 351 DKVVSVKCLLLGAGTLGCNVARTLMGWGVRHITFVDNAKISYSNPVRQPLYEFED---CLgggkPKALAAADRLQKIfpg 427
Cdd:PRK07688   20 QKLREKHVLIIGAGALGTANAEMLVRAGVGKVTIVDRDYVEWSNLQRQQLYTESDvknNL----PKAVAAKKRLEEI--- 92

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462586505 428 vNargfnmsipmpghpvnfSSVTLEQARRDV--EQLEQLIESHDVVFLLMDTRESRWL 483
Cdd:PRK07688   93 -N-----------------SDVRVEAIVQDVtaEELEELVTGVDLIIDATDNFETRFI 132
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 357-503 1.94e-10

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 61.78  E-value: 1.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586505 357 KCLLLGAGTLGCNVARTLMGWGVRHITFVDNAKISYSNPVRQPLYEFEDClggGKPKALAAADRLQKIFPGVNARGFNms 436
Cdd:PRK05690   34 RVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVSLSNLQRQVLHDDATI---GQPKVESARAALARINPHIAIETIN-- 108

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462586505 437 ipmpghpvnfssvtleqARRDVEQLEQLIESHDVVfllMD------TRESrwLPAVIAASKRKLVINAALGFD 503
Cdd:PRK05690  109 -----------------ARLDDDELAALIAGHDLV---LDctdnvaTRNQ--LNRACFAAKKPLVSGAAIRME 159
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
343-512 3.25e-10

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 60.64  E-value: 3.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586505 343 RLVPTLdLDKVVSVKCLLLGAGTLGCNVARTLMGWGVRHITFVDNAKISYSNPVRQpLYEFEDClggGKPKALAAADRLQ 422
Cdd:PRK08644   17 RHTPKL-LEKLKKAKVGIAGAGGLGSNIAVALARSGVGNLKLVDFDVVEPSNLNRQ-QYFISQI---GMPKVEALKENLL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586505 423 KIFPGVNargfnmsipmpghpvnfssVTLEQARRDVEQLEQLIESHDVVFLLMDTresrwlpaviAASKRKLViNAALG- 501
Cdd:PRK08644   92 EINPFVE-------------------IEAHNEKIDEDNIEELFKDCDIVVEAFDN----------AETKAMLV-ETVLEh 141

                         170
                  ....*....|.
gi 2462586505 502 FDTFVVMRHGL 512
Cdd:PRK08644  142 PGKKLVAASGM 152
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 359-483 1.08e-09

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 60.90  E-value: 1.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586505 359 LLLGAGTLGCNVARTLMGWGVRHITFVDNAKISYSNPVRQPLYEFEDClGGGKPKALAAADRLQKIFPGVNARGFNMSIP 438
Cdd:PRK12475   28 LIVGAGALGAANAEALVRAGIGKLTIADRDYVEWSNLQRQQLYTEEDA-KQKKPKAIAAKEHLRKINSEVEIVPVVTDVT 106

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2462586505 439 MpghpvnfssvtleqarrdvEQLEQLIESHDVVFLLMDTRESRWL 483
Cdd:PRK12475  107 V-------------------EELEELVKEVDLIIDATDNFDTRLL 132
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 357-481 3.50e-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: 58.93  E-value: 3.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586505 357 KCLLLGAGTLGCNVARTLMGWGVRHITFVDNAKISYSNPVRQPLYEFEDClggGKPKALAAADRLQKIFPGVNARGFNMS 436
Cdd:cd01489     1 KVLVVGAGGIGCELLKNLVLTGFGEIHIIDLDTIDLSNLNRQFLFRKKHV---GKSKAQVAKEAVLSFNPNVKIVAYHAN 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2462586505 437 IPMPGHPVNFssvtleqarrdveqleqlIESHDVVFLLMDTRESR 481
Cdd:cd01489    78 IKDPDFNVEF------------------FKQFDLVFNALDNLAAR 104
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 357-429 1.80e-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: 56.60  E-value: 1.80e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462586505 357 KCLLLGAGTLGCNVARTLMGWGVRHITFVDNAKISYSNPVRQPLYEFEDClggGKPKALAAADRLQKIFPGVN 429
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. ...
 357-512 4.78e-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: 50.46  E-value: 4.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586505 357 KCLLLGAGTLGCNVARTLMGWGVRHITFVDNAKISYSNPVRQPlYEFEDClggGKPKALAAADRLQKIFPgvnargfnms 436
Cdd:cd01487     1 KVGIAGAGGLGSNIAVLLARSGVGNLKLVDFDVVEPSNLNRQQ-YFLSQI---GEPKVEALKENLREINP---------- 66

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462586505 437 ipmpghpvnFSSVTLEQARRDVEQLEQLIESHDVVFLLMDTresrwlpaviAASKRkLVINAALGF-DTFVVMRHGL 512
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 ...
 357-429 1.23e-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: 1.23e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462586505 357 KCLLLGAGTLGCNVARTLMGWGVRHITFVDNAKISYSNPVRQPLYEFEDClggGKPKALAAADRLQKIFPGVN 429
Cdd:cd01484     1 KVLLVGAGGIGCELLKNLALMGFGQIHVIDMDTIDVSNLNRQFLFRPKDI---GRPKSEVAAEAVNDRNPNCK 70
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
352-471 4.33e-06

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 49.62  E-value: 4.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586505 352 KVVSVKCLLLGAGTLGCNVARTLMGWGVRHITFVDNAKISYSNPVRQPLYEfEDCLggGKPKALAAADRLQKIFPGVnar 431
Cdd:PRK08762  132 RLLEARVLLIGAGGLGSPAALYLAAAGVGTLGIVDHDVVDRSNLQRQILHT-EDRV--GQPKVDSAAQRLAALNPDV--- 205

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2462586505 432 gfnmsipmpghpvnfsSVTLEQARRDVEQLEQLIESHDVV 471
Cdd:PRK08762  206 ----------------QVEAVQERVTSDNVEALLQDVDVV 229
E1-1_like cd01485
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ...
 343-429 3.86e-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: 45.49  E-value: 3.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586505 343 RLVPTLDLDKVVSVKCLLLGAGTLGCNVARTLMGWGVRHITFVDNAKISYSNPVRQPLYEFEDClGGGKPKALAAADRLQ 422
Cdd:cd01485     7 RLWGDEAQNKLRSAKVLIIGAGALGAEIAKNLVLAGIDSITIVDHRLVSTEDLGSNFFLDAEVS-NSGMNRAAASYEFLQ 85


                  ....*..
gi 2462586505 423 KIFPGVN 429
Cdd:cd01485    86 ELNPNVK 92
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 361-532 1.71e-04

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 44.48  E-value: 1.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586505 361 LGAGTLGCNVARTLMGWGVRHITFVDNAKISYSNPVRQPLYEFEdclGGGKPKALAAADRLQKIFPGVNargfnmsipmp 440
Cdd:PRK05597   34 IGAGGLGSPALLYLAGAGVGHITIIDDDTVDLSNLHRQVIHSTA---GVGQPKAESAREAMLALNPDVK----------- 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586505 441 ghpvnfssVTLEQARRDVEQLEQLIESHDVVFLLMDTRESRWLPAVIAAskrKLVI----NAALGFDTFVVMRHGLKKPK 516
Cdd:PRK05597  100 --------VTVSVRRLTWSNALDELRDADVILDGSDNFDTRHLASWAAA---RLGIphvwASILGFDAQLSVFHAGHGPI 168

                         170
                  ....*....|....*.
gi 2462586505 517 QQgagDLCPNHPVASA 532
Cdd:PRK05597  169 YE---DLFPTPPPPGS 181
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
 357-429 3.77e-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: 43.82  E-value: 3.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586505 357 KCLLLGAGTLGC----NVArtLMGWGVR---HITFVDNAKISYSNPVRQPLYEFEDClggGKPKALAAADRLQKIFPGVN 429
Cdd:cd01490     1 KVFLVGAGAIGCellkNFA--LMGVGTGesgEITVTDMDNIEKSNLNRQFLFRPHDV---GKPKSEVAAAAVKAMNPDLK 75
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 352-429 8.25e-04

ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino acids, of a multicopy family of eukaryotic proteins, many of which are designated ubiquitin-activating enzyme E1. Members have two copies of the ThiF family domain (pfam00899), a repeat found in ubiquitin-activating proteins (pfam02134), and other regions.


Pssm-ID: 273603 [Multi-domain]  Cd Length: 1006  Bit Score: 42.95  E-value: 8.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586505  352 KVVSVKCLLLGAGTLGCNVARTLMGWGVR-----HITFVDNAKISYSNPVRQPLYEFEDClggGKPKALAAADRLQKIFP 426
Cdd:TIGR01408  416 KLQNLNIFLVGCGAIGCEMLKNFALMGVGtgkkgMITVTDPDLIEKSNLNRQFLFRPHHI---GKPKSYTAADATLKINP 492


                   ...
gi 2462586505  427 GVN 429
Cdd:TIGR01408  493 QIK 495
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
 362-426 5.42e-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: 39.13  E-value: 5.42e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462586505 362 GAGTLGCNVARTLMGWGVRHITFVDNAKISYSNPVRQpLYEFEDCLGggKPKALAAADRLQKIFP 426
Cdd:cd00755    18 GLGGVGSWAAEALARSGVGKLTLIDFDVVCVSNLNRQ-IHALLSTVG--KPKVEVMAERIRDINP 79
 
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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