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Conserved domains on  [gi|222144229|ref|NP_001138384|]
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ubiquitin-like modifier-activating enzyme ATG7 isoform c [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 ...
 15-614 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: 637.75  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222144229   15 FAPFSSALDVGFWHELTQKKLNEYRLDEAPKDIKGYYYNGDSAGLPARLTL--EFSAFDMSAPTPARCCPAIGTLYNTNT 92
Cdd:TIGR01381   1 FVPFVSCVDTGFWNEVSKLKLNKWKLDDTPKCISGQLSLHQTEGFKCHLSLsyDSLSSLESTTGTHAQLSVSGILLNYNT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222144229   93 LESFKTADKKLLLEQAANEIWESIKSGTALENPVLLNKFLLLTFA------------------------IEAL-ECAYDN 147
Cdd:TIGR01381  81 VESFKKVDKSDLLRSEAEKIWESIQTRKWLQDPSLLSQFFIISFAdlkkfkfyywfcfpalvypskvnkLSGLtESIKQE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222144229  148 LCQTEGVTA----LPYFLIKYDENMVLVSL-------LKHYSDFFQGQRtKITIGVYDPCNLAQYPGWPLRNFLVLAAHR 216
Cdd:TIGR01381 161 ITPLESLGAdhkiLFDFYRKNNFPFFLYSKqsskmleLSELENNTNPDD-ELCVGFADPSPVAYSAGWMLRNVLAAVAHL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222144229  217 WSSsFQSVEVVCFRDrtmqgARDVAHSIIFEVKLPEMAFSPD-----CPKAVGWEKNQKGGMGPRMVNLSECMDPKRLAE 291
Cdd:TIGR01381 240 HPT-WKHVHIFSLRS-----ADSIGIKYLWTTLLPSAELSSDgaqnaVPKAVGWERNANGKLQPISVDLSKEFDPKRLAE 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222144229  292 SSVDLNLKLMCWRLVPTLDLDKVVSVKCLLLGAGTLGCNVARTLMGWGVRHITFVDNAKISYSNPVRQPLYEFEDCLGGG 371
Cdd:TIGR01381 314 RSVDLNLKLMKWRLHPDLQLERYSQLKVLLLGAGTLGCNVARCLIGWGVRHITFVDNGKVSYSNPVRQSLSNFEDCLLGG 393

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222144229  372 KPKALAAADRLQKIFPGVNARGFNMSIPMPGHPVnfSSVTLEQARRDVEQLEQLIESHDVVFLLMDTRESRWLPAVIAAS 451
Cdd:TIGR01381 394 RGKAETAQKALKRIFPSIQATGHRLTVPMPGHPI--DEKDVPELEKDIARLEQLIKDHDVVFLLLDSREARWLPTVLCSR 471

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222144229  452 KRKLVINAALGFDTFVVMRHGlkkpkqqgagdlcpNHPVASADLLGSSlfANIPGYKLGCYFCNDVVAPGDSTRDRTLDQ 531
Cdd:TIGR01381 472 HKKIAISAALGFDSYVVMRHG--------------IGRSESVSDVSSS--DSVPYSRLGCYFCNDVTAPGDSTTDRTLDQ 535

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222144229  532 QCTVSRPGLAVIAGALAVELMVSVLQHPEGGYAIASSSDDrmnepPTSLGLVPHQIRGFLSRFDNVLPVSLAFDKCTACS 611
Cdd:TIGR01381 536 QCTVTRPGTAMIASGLAVELLVSVLQHPLPSKTPASHDDN-----TTVLGALPHQIRGFLGRFQQILLSVKRFDQCVACS 610


                  ...
gi 222144229  612 SKI 614
Cdd:TIGR01381 611 DAV 613
 
Name Accession Description Interval E-value
E1_like_apg7 TIGR01381
E1-like protein-activating enzyme Gsa7p/Apg7p; This model represents a family of eukaryotic ...
 15-614 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: 637.75  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222144229   15 FAPFSSALDVGFWHELTQKKLNEYRLDEAPKDIKGYYYNGDSAGLPARLTL--EFSAFDMSAPTPARCCPAIGTLYNTNT 92
Cdd:TIGR01381   1 FVPFVSCVDTGFWNEVSKLKLNKWKLDDTPKCISGQLSLHQTEGFKCHLSLsyDSLSSLESTTGTHAQLSVSGILLNYNT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222144229   93 LESFKTADKKLLLEQAANEIWESIKSGTALENPVLLNKFLLLTFA------------------------IEAL-ECAYDN 147
Cdd:TIGR01381  81 VESFKKVDKSDLLRSEAEKIWESIQTRKWLQDPSLLSQFFIISFAdlkkfkfyywfcfpalvypskvnkLSGLtESIKQE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222144229  148 LCQTEGVTA----LPYFLIKYDENMVLVSL-------LKHYSDFFQGQRtKITIGVYDPCNLAQYPGWPLRNFLVLAAHR 216
Cdd:TIGR01381 161 ITPLESLGAdhkiLFDFYRKNNFPFFLYSKqsskmleLSELENNTNPDD-ELCVGFADPSPVAYSAGWMLRNVLAAVAHL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222144229  217 WSSsFQSVEVVCFRDrtmqgARDVAHSIIFEVKLPEMAFSPD-----CPKAVGWEKNQKGGMGPRMVNLSECMDPKRLAE 291
Cdd:TIGR01381 240 HPT-WKHVHIFSLRS-----ADSIGIKYLWTTLLPSAELSSDgaqnaVPKAVGWERNANGKLQPISVDLSKEFDPKRLAE 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222144229  292 SSVDLNLKLMCWRLVPTLDLDKVVSVKCLLLGAGTLGCNVARTLMGWGVRHITFVDNAKISYSNPVRQPLYEFEDCLGGG 371
Cdd:TIGR01381 314 RSVDLNLKLMKWRLHPDLQLERYSQLKVLLLGAGTLGCNVARCLIGWGVRHITFVDNGKVSYSNPVRQSLSNFEDCLLGG 393

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222144229  372 KPKALAAADRLQKIFPGVNARGFNMSIPMPGHPVnfSSVTLEQARRDVEQLEQLIESHDVVFLLMDTRESRWLPAVIAAS 451
Cdd:TIGR01381 394 RGKAETAQKALKRIFPSIQATGHRLTVPMPGHPI--DEKDVPELEKDIARLEQLIKDHDVVFLLLDSREARWLPTVLCSR 471

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222144229  452 KRKLVINAALGFDTFVVMRHGlkkpkqqgagdlcpNHPVASADLLGSSlfANIPGYKLGCYFCNDVVAPGDSTRDRTLDQ 531
Cdd:TIGR01381 472 HKKIAISAALGFDSYVVMRHG--------------IGRSESVSDVSSS--DSVPYSRLGCYFCNDVTAPGDSTTDRTLDQ 535

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222144229  532 QCTVSRPGLAVIAGALAVELMVSVLQHPEGGYAIASSSDDrmnepPTSLGLVPHQIRGFLSRFDNVLPVSLAFDKCTACS 611
Cdd:TIGR01381 536 QCTVTRPGTAMIASGLAVELLVSVLQHPLPSKTPASHDDN-----TTVLGALPHQIRGFLGRFQQILLSVKRFDQCVACS 610


                  ...
gi 222144229  612 SKI 614
Cdd:TIGR01381 611 DAV 613
Apg7 cd01486
Apg7 is an E1-like protein, that activates two different ubiquitin-like proteins, Apg12 and ...
 318-616 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: 528.87  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222144229 318 KCLLLGAGTLGCNVARTLMGWGVRHITFVDNAKISYSNPVRQPLYEFEDClGGGKPKALAAADRLQKIFPGVNARGFNMS 397
Cdd:cd01486    1 KCLLLGAGTLGCNVARNLLGWGVRHITFVDSGKVSYSNPVRQSLFTFEDC-KGGKPKAEAAAERLKEIFPSIDATGIVLS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222144229 398 IPMPGHPVNFSSVtlEQARRDVEQLEQLIESHDVVFLLMDTRESRWLPAVIAASKRKLVINAALGFDTFVVMRHGLKKPK 477
Cdd:cd01486   80 IPMPGHPISESEV--PSTLKDVKRLEELIKDHDVIFLLTDSRESRWLPTLLSAAKNKLVINAALGFDSYLVMRHGAGPQS 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222144229 478 QQGAGDlcpnhpvasadllgsSLFANIPGYKLGCYFCNDVVAPGDSTRDRTLDQQCTVSRPGLAVIAGALAVELMVSVLQ 557
Cdd:cd01486  158 QSGSGD---------------SSSDSIPGSRLGCYFCNDVVAPGDSLKDRTLDQQCTVTRPGLSMIASSIAVELLVSLLQ 222

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 222144229 558 HPEGGYAIASSSDDRMNEPPTSLGLVPHQIRGFLSRFDNVLPVSLAFDKCTACSSKIWD 616
Cdd:cd01486  223 HPLGGHAPAESSSNEGDEPTTVLGILPHQIRGFLSNFSNLTLSGQAYDQCTACSDAVID 281
ATG7_N pfam16420
Ubiquitin-like modifier-activating enzyme ATG7 N-terminus; This is the N-terminal domain of ...
 13-284 5.85e-120

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


Pssm-ID: 465114  Cd Length: 308  Bit Score: 358.49  E-value: 5.85e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222144229   13 LQFAPFSSALDVGFWHELTQKKLNEYRLDEAPKDIKGYYYNGDSAGLPARLTLEFSAFDM-SAPTPARCCPAIGTLYNTN 91
Cdd:pfam16420   1 LQFAPFSSFIDPSFWHELSSLKLDVLKLDDSPRPILGLYEPRDAPGLSCRLQLDGSSFNDtSDAVPPGSCRAEGTLKNFN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222144229   92 TLESFKTADKKLLLEQAANEIWESIKSGTALENPVLLNKFLLLTFA---------------------------------- 137
Cdd:pfam16420  81 TIEEFKNLDKQALLDDAGKKIWDAILSGTALEDPSLLSRFLLLSFAdlkkykfyywfafpalhsdpawvlswkpaseels 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222144229  138 ---IEALECAYDNLCQTEGVTALpYFLIKYDENMVL-VSLLKHYSDFFQGqRTKITIGVYDPCNLAQYPGWPLRNFLVLA 213
Cdd:pfam16420 161 seeTESLVDAVQTWRYSVDARQH-FFLVKKSRGSDWeIASLSEYENFFAD-VEDVYFGFADPSTLPENPGWPLRNLLALL 238

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 222144229  214 AHRWSSSfqSVEVVCFRDRTMQGARDvAHSIIFEVKLPE--MAFSPDCPKAVGWEKNQKGGMGPRMVNLSECM 284
Cdd:pfam16420 239 RARWPLK--KVQVLCYRDNSRSGRRD-ERSLVLTLKLPEpsDENTSELPKAVGWERNANGKLGPRVVDLSSYM 308
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 320-464 1.51e-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: 76.71  E-value: 1.51e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222144229 320 LLLGAGTLGCNVARTLMGWGVRHITFVDNAKISYSNPVRQPLYEFEDClggGKPKALAAADRLQKIFPGVNARGFNMSIp 399
Cdd:COG0476   31 LVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADV---GRPKVEAAAERLRALNPDVEVEAIPERL- 106

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 222144229 400 mpghpvnfssvtleqarrDVEQLEQLIESHDVVFLLMDTRESR-WLPAVIAASKRKLVINAALGFD 464
Cdd:COG0476  107 ------------------TEENALELLAGADLVLDCTDNFATRyLLNDACVKLGIPLVSGAVIGFE 154
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 320-499 4.54e-11

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 64.90  E-value: 4.54e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222144229 320 LLLGAGTLGCNVARTLMGWGVRHITFVDNAKISYSNPVRQPLYEFEDClggGKPKALAAADRLQKIFPGVnargfnmsip 399
Cdd:PRK05600  45 LVIGAGGLGCPAMQSLASAGVGTITLIDDDTVDVSNIHRQILFGASDV---GRPKVEVAAERLKEIQPDI---------- 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222144229 400 mpghpvnfsSVTLEQARRDVEQLEQLIESHDVVFLLMDTRESRWLPAVIAA-SKRKLVINAALGFDTFVVMRHGLKKPKQ 478
Cdd:PRK05600 112 ---------RVNALRERLTAENAVELLNGVDLVLDGSDSFATKFLVADAAEiTGTPLVWGTVLRFHGELAVFNSGPDHRG 182

                        170       180
                 ....*....|....*....|....*...
gi 222144229 479 QGAGDLCPNHPV-------ASADLLGSS 499
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 ...
 15-614 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: 637.75  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222144229   15 FAPFSSALDVGFWHELTQKKLNEYRLDEAPKDIKGYYYNGDSAGLPARLTL--EFSAFDMSAPTPARCCPAIGTLYNTNT 92
Cdd:TIGR01381   1 FVPFVSCVDTGFWNEVSKLKLNKWKLDDTPKCISGQLSLHQTEGFKCHLSLsyDSLSSLESTTGTHAQLSVSGILLNYNT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222144229   93 LESFKTADKKLLLEQAANEIWESIKSGTALENPVLLNKFLLLTFA------------------------IEAL-ECAYDN 147
Cdd:TIGR01381  81 VESFKKVDKSDLLRSEAEKIWESIQTRKWLQDPSLLSQFFIISFAdlkkfkfyywfcfpalvypskvnkLSGLtESIKQE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222144229  148 LCQTEGVTA----LPYFLIKYDENMVLVSL-------LKHYSDFFQGQRtKITIGVYDPCNLAQYPGWPLRNFLVLAAHR 216
Cdd:TIGR01381 161 ITPLESLGAdhkiLFDFYRKNNFPFFLYSKqsskmleLSELENNTNPDD-ELCVGFADPSPVAYSAGWMLRNVLAAVAHL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222144229  217 WSSsFQSVEVVCFRDrtmqgARDVAHSIIFEVKLPEMAFSPD-----CPKAVGWEKNQKGGMGPRMVNLSECMDPKRLAE 291
Cdd:TIGR01381 240 HPT-WKHVHIFSLRS-----ADSIGIKYLWTTLLPSAELSSDgaqnaVPKAVGWERNANGKLQPISVDLSKEFDPKRLAE 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222144229  292 SSVDLNLKLMCWRLVPTLDLDKVVSVKCLLLGAGTLGCNVARTLMGWGVRHITFVDNAKISYSNPVRQPLYEFEDCLGGG 371
Cdd:TIGR01381 314 RSVDLNLKLMKWRLHPDLQLERYSQLKVLLLGAGTLGCNVARCLIGWGVRHITFVDNGKVSYSNPVRQSLSNFEDCLLGG 393

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222144229  372 KPKALAAADRLQKIFPGVNARGFNMSIPMPGHPVnfSSVTLEQARRDVEQLEQLIESHDVVFLLMDTRESRWLPAVIAAS 451
Cdd:TIGR01381 394 RGKAETAQKALKRIFPSIQATGHRLTVPMPGHPI--DEKDVPELEKDIARLEQLIKDHDVVFLLLDSREARWLPTVLCSR 471

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222144229  452 KRKLVINAALGFDTFVVMRHGlkkpkqqgagdlcpNHPVASADLLGSSlfANIPGYKLGCYFCNDVVAPGDSTRDRTLDQ 531
Cdd:TIGR01381 472 HKKIAISAALGFDSYVVMRHG--------------IGRSESVSDVSSS--DSVPYSRLGCYFCNDVTAPGDSTTDRTLDQ 535

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222144229  532 QCTVSRPGLAVIAGALAVELMVSVLQHPEGGYAIASSSDDrmnepPTSLGLVPHQIRGFLSRFDNVLPVSLAFDKCTACS 611
Cdd:TIGR01381 536 QCTVTRPGTAMIASGLAVELLVSVLQHPLPSKTPASHDDN-----TTVLGALPHQIRGFLGRFQQILLSVKRFDQCVACS 610


                  ...
gi 222144229  612 SKI 614
Cdd:TIGR01381 611 DAV 613
Apg7 cd01486
Apg7 is an E1-like protein, that activates two different ubiquitin-like proteins, Apg12 and ...
 318-616 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: 528.87  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222144229 318 KCLLLGAGTLGCNVARTLMGWGVRHITFVDNAKISYSNPVRQPLYEFEDClGGGKPKALAAADRLQKIFPGVNARGFNMS 397
Cdd:cd01486    1 KCLLLGAGTLGCNVARNLLGWGVRHITFVDSGKVSYSNPVRQSLFTFEDC-KGGKPKAEAAAERLKEIFPSIDATGIVLS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222144229 398 IPMPGHPVNFSSVtlEQARRDVEQLEQLIESHDVVFLLMDTRESRWLPAVIAASKRKLVINAALGFDTFVVMRHGLKKPK 477
Cdd:cd01486   80 IPMPGHPISESEV--PSTLKDVKRLEELIKDHDVIFLLTDSRESRWLPTLLSAAKNKLVINAALGFDSYLVMRHGAGPQS 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222144229 478 QQGAGDlcpnhpvasadllgsSLFANIPGYKLGCYFCNDVVAPGDSTRDRTLDQQCTVSRPGLAVIAGALAVELMVSVLQ 557
Cdd:cd01486  158 QSGSGD---------------SSSDSIPGSRLGCYFCNDVVAPGDSLKDRTLDQQCTVTRPGLSMIASSIAVELLVSLLQ 222

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 222144229 558 HPEGGYAIASSSDDRMNEPPTSLGLVPHQIRGFLSRFDNVLPVSLAFDKCTACSSKIWD 616
Cdd:cd01486  223 HPLGGHAPAESSSNEGDEPTTVLGILPHQIRGFLSNFSNLTLSGQAYDQCTACSDAVID 281
ATG7_N pfam16420
Ubiquitin-like modifier-activating enzyme ATG7 N-terminus; This is the N-terminal domain of ...
 13-284 5.85e-120

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


Pssm-ID: 465114  Cd Length: 308  Bit Score: 358.49  E-value: 5.85e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222144229   13 LQFAPFSSALDVGFWHELTQKKLNEYRLDEAPKDIKGYYYNGDSAGLPARLTLEFSAFDM-SAPTPARCCPAIGTLYNTN 91
Cdd:pfam16420   1 LQFAPFSSFIDPSFWHELSSLKLDVLKLDDSPRPILGLYEPRDAPGLSCRLQLDGSSFNDtSDAVPPGSCRAEGTLKNFN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222144229   92 TLESFKTADKKLLLEQAANEIWESIKSGTALENPVLLNKFLLLTFA---------------------------------- 137
Cdd:pfam16420  81 TIEEFKNLDKQALLDDAGKKIWDAILSGTALEDPSLLSRFLLLSFAdlkkykfyywfafpalhsdpawvlswkpaseels 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222144229  138 ---IEALECAYDNLCQTEGVTALpYFLIKYDENMVL-VSLLKHYSDFFQGqRTKITIGVYDPCNLAQYPGWPLRNFLVLA 213
Cdd:pfam16420 161 seeTESLVDAVQTWRYSVDARQH-FFLVKKSRGSDWeIASLSEYENFFAD-VEDVYFGFADPSTLPENPGWPLRNLLALL 238

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 222144229  214 AHRWSSSfqSVEVVCFRDRTMQGARDvAHSIIFEVKLPE--MAFSPDCPKAVGWEKNQKGGMGPRMVNLSECM 284
Cdd:pfam16420 239 RARWPLK--KVQVLCYRDNSRSGRRD-ERSLVLTLKLPEpsDENTSELPKAVGWERNANGKLGPRVVDLSSYM 308
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 296-564 1.01e-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: 172.83  E-value: 1.01e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222144229  296 LNLKLMCwRLVPTLDLDKVVSVKCLLLGAGTLGCNVARTLMGWGVRHITFVDNAKISYSNPVRQPLYEFEDClggGKPKA 375
Cdd:pfam00899   1 YSRQLAL-PLIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADI---GKPKA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222144229  376 LAAADRLQKIFPGVNARGFNMSIpmpghpvnfssvtleqarrDVEQLEQLIESHDVVFLLMDTRESRWLPAVIAASKRKL 455
Cdd:pfam00899  77 EVAAERLREINPDVEVEAYTERL-------------------TPENAEELIKSFDIVVDATDNFAARYLVNDACVKLGKP 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222144229  456 VINAA-LGFDTFVVMRhglkkpkqqgagdlcpnhpvasadllgsslfanIPGyKLGCYFCNDVVAPgdstrDRTLDQQCT 534
Cdd:pfam00899 138 LIEAGvLGFKGQVTVV---------------------------------IPG-KTPCYRCLFPEDP-----PPKLVPSCT 178

                         250       260       270
                  ....*....|....*....|....*....|...
gi 222144229  535 VS---RPGLAVIAGALAVELMVSVLQHPEGGYA 564
Cdd:pfam00899 179 VAgvlGPTTAVVAGLQALEALKLLLGKGEPNLA 211
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 318-473 1.01e-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: 1.01e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222144229 318 KCLLLGAGTLGCNVARTLMGWGVRHITFVDNAKISYSNPVRQPLYEFEDClggGKPKALAAADRLQKIFPGVNARGFNMS 397
Cdd:cd01483    1 RVLLVGLGGLGSEIALNLARSGVGKITLIDFDTVELSNLNRQFLARQADI---GKPKAEVAARRLNELNPGVNVTAVPEG 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 222144229 398 IPMpghpvnfssvtleqarrdvEQLEQLIESHDVVFLLMDTRESRWLPAVIAASKRKLVINAALGFDTFVVMRHGL 473
Cdd:cd01483   78 ISE-------------------DNLDDFLDGVDLVIDAIDNIAVRRALNRACKELGIPVIDAGGLGLGGDIQVIDI 134
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 320-464 1.51e-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: 76.71  E-value: 1.51e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222144229 320 LLLGAGTLGCNVARTLMGWGVRHITFVDNAKISYSNPVRQPLYEFEDClggGKPKALAAADRLQKIFPGVNARGFNMSIp 399
Cdd:COG0476   31 LVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADV---GRPKVEAAAERLRALNPDVEVEAIPERL- 106

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 222144229 400 mpghpvnfssvtleqarrDVEQLEQLIESHDVVFLLMDTRESR-WLPAVIAASKRKLVINAALGFD 464
Cdd:COG0476  107 ------------------TEENALELLAGADLVLDCTDNFATRyLLNDACVKLGIPLVSGAVIGFE 154
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 320-464 2.24e-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: 2.24e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222144229 320 LLLGAGTLGCNVARTLMGWGVRHITFVDNAKISYSNPVRQPLYEFEDClggGKPKALAAADRLQKIFPGVNARGFNMSIp 399
Cdd:cd00757   25 LVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRQILHTEADV---GQPKAEAAAERLRAINPDVEIEAYNERL- 100

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 222144229 400 mpghpvnfssvtleqarrDVEQLEQLIESHDVVFLLMDTRESRWLPAVIAASKRK-LVINAALGFD 464
Cdd:cd00757  101 ------------------DAENAEELIAGYDLVLDCTDNFATRYLINDACVKLGKpLVSGAVLGFE 148
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 320-499 4.54e-11

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 64.90  E-value: 4.54e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222144229 320 LLLGAGTLGCNVARTLMGWGVRHITFVDNAKISYSNPVRQPLYEFEDClggGKPKALAAADRLQKIFPGVnargfnmsip 399
Cdd:PRK05600  45 LVIGAGGLGCPAMQSLASAGVGTITLIDDDTVDVSNIHRQILFGASDV---GRPKVEVAAERLKEIQPDI---------- 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222144229 400 mpghpvnfsSVTLEQARRDVEQLEQLIESHDVVFLLMDTRESRWLPAVIAA-SKRKLVINAALGFDTFVVMRHGLKKPKQ 478
Cdd:PRK05600 112 ---------RVNALRERLTAENAVELLNGVDLVLDGSDSFATKFLVADAAEiTGTPLVWGTVLRFHGELAVFNSGPDHRG 182

                        170       180
                 ....*....|....*....|....*...
gi 222144229 479 QGAGDLCPNHPV-------ASADLLGSS 499
Cdd:PRK05600 183 VGLRDLFPEQPSgdsipdcATAGVLGAT 210
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 312-444 5.24e-11

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 64.24  E-value: 5.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222144229 312 DKVVSVKCLLLGAGTLGCNVARTLMGWGVRHITFVDNAKISYSNPVRQPLYEFED---CLgggkPKALAAADRLQKIfpg 388
Cdd:PRK07688  20 QKLREKHVLIIGAGALGTANAEMLVRAGVGKVTIVDRDYVEWSNLQRQQLYTESDvknNL----PKAVAAKKRLEEI--- 92

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 222144229 389 vNargfnmsipmpghpvnfSSVTLEQARRDV--EQLEQLIESHDVVFLLMDTRESRWL 444
Cdd:PRK07688  93 -N-----------------SDVRVEAIVQDVtaEELEELVTGVDLIIDATDNFETRFI 132
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 318-464 1.97e-10

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 61.40  E-value: 1.97e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222144229 318 KCLLLGAGTLGCNVARTLMGWGVRHITFVDNAKISYSNPVRQPLYEFEDClggGKPKALAAADRLQKIFPGVNARGFNms 397
Cdd:PRK05690  34 RVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVSLSNLQRQVLHDDATI---GQPKVESARAALARINPHIAIETIN-- 108

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 222144229 398 ipmpghpvnfssvtleqARRDVEQLEQLIESHDVVfllMD------TRESrwLPAVIAASKRKLVINAALGFD 464
Cdd:PRK05690 109 -----------------ARLDDDELAALIAGHDLV---LDctdnvaTRNQ--LNRACFAAKKPLVSGAAIRME 159
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
304-473 2.50e-10

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 60.64  E-value: 2.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222144229 304 RLVPTLdLDKVVSVKCLLLGAGTLGCNVARTLMGWGVRHITFVDNAKISYSNPVRQpLYEFEDClggGKPKALAAADRLQ 383
Cdd:PRK08644  17 RHTPKL-LEKLKKAKVGIAGAGGLGSNIAVALARSGVGNLKLVDFDVVEPSNLNRQ-QYFISQI---GMPKVEALKENLL 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222144229 384 KIFPGVNargfnmsipmpghpvnfssVTLEQARRDVEQLEQLIESHDVVFLLMDTresrwlpaviAASKRKLViNAALG- 462
Cdd:PRK08644  92 EINPFVE-------------------IEAHNEKIDEDNIEELFKDCDIVVEAFDN----------AETKAMLV-ETVLEh 141

                        170
                 ....*....|.
gi 222144229 463 FDTFVVMRHGL 473
Cdd:PRK08644 142 PGKKLVAASGM 152
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 320-444 8.05e-10

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 60.90  E-value: 8.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222144229 320 LLLGAGTLGCNVARTLMGWGVRHITFVDNAKISYSNPVRQPLYEFEDClGGGKPKALAAADRLQKIFPGVNARGFNMSIP 399
Cdd:PRK12475  28 LIVGAGALGAANAEALVRAGIGKLTIADRDYVEWSNLQRQQLYTEEDA-KQKKPKAIAAKEHLRKINSEVEIVPVVTDVT 106

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 222144229 400 MpghpvnfssvtleqarrdvEQLEQLIESHDVVFLLMDTRESRWL 444
Cdd:PRK12475 107 V-------------------EELEELVKEVDLIIDATDNFDTRLL 132
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 318-442 2.65e-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: 2.65e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222144229 318 KCLLLGAGTLGCNVARTLMGWGVRHITFVDNAKISYSNPVRQPLYEFEDClggGKPKALAAADRLQKIFPGVNARGFNMS 397
Cdd:cd01489    1 KVLVVGAGGIGCELLKNLVLTGFGEIHIIDLDTIDLSNLNRQFLFRKKHV---GKSKAQVAKEAVLSFNPNVKIVAYHAN 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 222144229 398 IPMPGHPVNFssvtleqarrdveqleqlIESHDVVFLLMDTRESR 442
Cdd:cd01489   78 IKDPDFNVEF------------------FKQFDLVFNALDNLAAR 104
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 318-390 1.36e-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: 1.36e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 222144229 318 KCLLLGAGTLGCNVARTLMGWGVRHITFVDNAKISYSNPVRQPLYEFEDClggGKPKALAAADRLQKIFPGVN 390
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. ...
 318-473 3.74e-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: 3.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222144229 318 KCLLLGAGTLGCNVARTLMGWGVRHITFVDNAKISYSNPVRQPlYEFEDClggGKPKALAAADRLQKIFPgvnargfnms 397
Cdd:cd01487    1 KVGIAGAGGLGSNIAVLLARSGVGNLKLVDFDVVEPSNLNRQQ-YFLSQI---GEPKVEALKENLREINP---------- 66

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 222144229 398 ipmpghpvnFSSVTLEQARRDVEQLEQLIESHDVVFLLMDTresrwlpaviAASKRkLVINAALGF-DTFVVMRHGL 473
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 ...
 318-390 9.47e-07

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: 9.47e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 222144229 318 KCLLLGAGTLGCNVARTLMGWGVRHITFVDNAKISYSNPVRQPLYEFEDClggGKPKALAAADRLQKIFPGVN 390
Cdd:cd01484    1 KVLLVGAGGIGCELLKNLALMGFGQIHVIDMDTIDVSNLNRQFLFRPKDI---GRPKSEVAAEAVNDRNPNCK 70
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
313-432 3.57e-06

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 49.62  E-value: 3.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222144229 313 KVVSVKCLLLGAGTLGCNVARTLMGWGVRHITFVDNAKISYSNPVRQPLYEfEDCLggGKPKALAAADRLQKIFPGVnar 392
Cdd:PRK08762 132 RLLEARVLLIGAGGLGSPAALYLAAAGVGTLGIVDHDVVDRSNLQRQILHT-EDRV--GQPKVDSAAQRLAALNPDV--- 205

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 222144229 393 gfnmsipmpghpvnfsSVTLEQARRDVEQLEQLIESHDVV 432
Cdd:PRK08762 206 ----------------QVEAVQERVTSDNVEALLQDVDVV 229
E1-1_like cd01485
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ...
 304-390 3.01e-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: 3.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222144229 304 RLVPTLDLDKVVSVKCLLLGAGTLGCNVARTLMGWGVRHITFVDNAKISYSNPVRQPLYEFEDClGGGKPKALAAADRLQ 383
Cdd:cd01485    7 RLWGDEAQNKLRSAKVLIIGAGALGAEIAKNLVLAGIDSITIVDHRLVSTEDLGSNFFLDAEVS-NSGMNRAAASYEFLQ 85


                 ....*..
gi 222144229 384 KIFPGVN 390
Cdd:cd01485   86 ELNPNVK 92
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 322-493 1.31e-04

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 44.48  E-value: 1.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222144229 322 LGAGTLGCNVARTLMGWGVRHITFVDNAKISYSNPVRQPLYEFEdclGGGKPKALAAADRLQKIFPGVNargfnmsipmp 401
Cdd:PRK05597  34 IGAGGLGSPALLYLAGAGVGHITIIDDDTVDLSNLHRQVIHSTA---GVGQPKAESAREAMLALNPDVK----------- 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222144229 402 ghpvnfssVTLEQARRDVEQLEQLIESHDVVFLLMDTRESRWLPAVIAAskrKLVI----NAALGFDTFVVMRHGLKKPK 477
Cdd:PRK05597 100 --------VTVSVRRLTWSNALDELRDADVILDGSDNFDTRHLASWAAA---RLGIphvwASILGFDAQLSVFHAGHGPI 168

                        170
                 ....*....|....*.
gi 222144229 478 QQgagDLCPNHPVASA 493
Cdd:PRK05597 169 YE---DLFPTPPPPGS 181
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
 318-390 2.88e-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: 2.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222144229 318 KCLLLGAGTLGC----NVArtLMGWGVR---HITFVDNAKISYSNPVRQPLYEFEDClggGKPKALAAADRLQKIFPGVN 390
Cdd:cd01490    1 KVFLVGAGAIGCellkNFA--LMGVGTGesgEITVTDMDNIEKSNLNRQFLFRPHDV---GKPKSEVAAAAVKAMNPDLK 75
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 313-390 6.28e-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: 6.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222144229   313 KVVSVKCLLLGAGTLGCNVARTLMGWGVR-----HITFVDNAKISYSNPVRQPLYEFEDClggGKPKALAAADRLQKIFP 387
Cdd:TIGR01408  416 KLQNLNIFLVGCGAIGCEMLKNFALMGVGtgkkgMITVTDPDLIEKSNLNRQFLFRPHHI---GKPKSYTAADATLKINP 492


                   ...
gi 222144229   388 GVN 390
Cdd:TIGR01408  493 QIK 495
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
 323-387 4.57e-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: 4.57e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 222144229 323 GAGTLGCNVARTLMGWGVRHITFVDNAKISYSNPVRQpLYEFEDCLGggKPKALAAADRLQKIFP 387
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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