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Conserved domains on  [gi|1907173742|ref|XP_036008262|]
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ubiquitin-like modifier-activating enzyme ATG7 isoform X1 [Mus musculus]

Protein Classification

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

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
E1_like_apg7 super family cl36889
E1-like protein-activating enzyme Gsa7p/Apg7p; This model represents a family of eukaryotic ...
11-697 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: 721.73  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173742  11 FAPFNSALDVGFWHELTQKKLNEYRLDEAPKDIKGYYYNGDSAGL--PTRLTLEFSAFDMSASTPAHCCPAMGTLHNTNT 88
Cdd:TIGR01381   1 FVPFVSCVDTGFWNEVSKLKLNKWKLDDTPKCISGQLSLHQTEGFkcHLSLSYDSLSSLESTTGTHAQLSVSGILLNYNT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173742  89 LEAFKTADKKLLLEQSANEIWEAIKSGAALENPMLLNKFLLLTFADLKKYHFYYWFCCPALCLPESIPLIRGPVSlDQRL 168
Cdd:TIGR01381  81 VESFKKVDKSDLLRSEAEKIWESIQTRKWLQDPSLLSQFFIISFADLKKFKFYYWFCFPALVYPSKVNKLSGLTE-SIKQ 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173742 169 SPKQIQALEHAYDDLCRAEGVTALPYFLFKYDDDTVLVslLKHYSDFFQGQRtKITVGVYDPCNLAQYPGWPLRNFLVLA 248
Cdd:TIGR01381 160 EITPLESLGADHKILFDFYRKNNFPFFLYSKQSSKMLE--LSELENNTNPDD-ELCVGFADPSPVAYSAGWMLRNVLAAV 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173742 249 AHRWsgsFQSVEVLCFRDRTMQGARDVTHSIifeVKLPEMAFSPD-----CPKAVGWEKNQKGGMGPRMVNLSGCMDPKR 323
Cdd:TIGR01381 237 AHLH---PTWKHVHIFSLRSADSIGIKYLWT---TLLPSAELSSDgaqnaVPKAVGWERNANGKLQPISVDLSKEFDPKR 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173742 324 LAESSVDLNLKLMCWRLVPTLDLDKVVSVKCLLLGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQPLYEFEDCL 403
Cdd:TIGR01381 311 LAERSVDLNLKLMKWRLHPDLQLERYSQLKVLLLGAGTLGCNVARCLIGWGVRHITFVDNGKVSYSNPVRQSLSNFEDCL 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173742 404 GGGKPKALAAAERLQKIFPGVNARGFNMSIPMPGHPVNFSDVtmEQARRDVEQLEQLIDNHDVIFLLMDTRESRWLPTVI 483
Cdd:TIGR01381 391 LGGRGKAETAQKALKRIFPSIQATGHRLTVPMPGHPIDEKDV--PELEKDIARLEQLIKDHDVVFLLLDSREARWLPTVL 468
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173742 484 AASKRKLVINAALGFDTFVVMRHglkkpkqqGAGdlcPSHLVapADLGSSlfANIPGYKLGCYFCNDVVAPGDSTRDRTL 563
Cdd:TIGR01381 469 CSRHKKIAISAALGFDSYVVMRH--------GIG---RSESV--SDVSSS--DSVPYSRLGCYFCNDVTAPGDSTTDRTL 533
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173742 564 DQQCTVSRPGLAVIAGALAVELMVSVLQHPEGGYAIASSSDDrmnepPTSLGLVPHQIRGFLSRFDNVLPVSLAFDKCTA 643
Cdd:TIGR01381 534 DQQCTVTRPGTAMIASGLAVELLVSVLQHPLPSKTPASHDDN-----TTVLGALPHQIRGFLGRFQQILLSVKRFDQCVA 608
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907173742 644 CSPKVLDQYEREGFTFLAKVFNSShSFLEDLTGLTLLHQETQAAEIwDMSDEET 697
Cdd:TIGR01381 609 CSDAVAAEYQQRGWKFVRDAMNSP-GYLEDLTGLTELKNESSVNAI-DIQDFES 660
 
Name Accession Description Interval E-value
E1_like_apg7 TIGR01381
E1-like protein-activating enzyme Gsa7p/Apg7p; This model represents a family of eukaryotic ...
11-697 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: 721.73  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173742  11 FAPFNSALDVGFWHELTQKKLNEYRLDEAPKDIKGYYYNGDSAGL--PTRLTLEFSAFDMSASTPAHCCPAMGTLHNTNT 88
Cdd:TIGR01381   1 FVPFVSCVDTGFWNEVSKLKLNKWKLDDTPKCISGQLSLHQTEGFkcHLSLSYDSLSSLESTTGTHAQLSVSGILLNYNT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173742  89 LEAFKTADKKLLLEQSANEIWEAIKSGAALENPMLLNKFLLLTFADLKKYHFYYWFCCPALCLPESIPLIRGPVSlDQRL 168
Cdd:TIGR01381  81 VESFKKVDKSDLLRSEAEKIWESIQTRKWLQDPSLLSQFFIISFADLKKFKFYYWFCFPALVYPSKVNKLSGLTE-SIKQ 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173742 169 SPKQIQALEHAYDDLCRAEGVTALPYFLFKYDDDTVLVslLKHYSDFFQGQRtKITVGVYDPCNLAQYPGWPLRNFLVLA 248
Cdd:TIGR01381 160 EITPLESLGADHKILFDFYRKNNFPFFLYSKQSSKMLE--LSELENNTNPDD-ELCVGFADPSPVAYSAGWMLRNVLAAV 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173742 249 AHRWsgsFQSVEVLCFRDRTMQGARDVTHSIifeVKLPEMAFSPD-----CPKAVGWEKNQKGGMGPRMVNLSGCMDPKR 323
Cdd:TIGR01381 237 AHLH---PTWKHVHIFSLRSADSIGIKYLWT---TLLPSAELSSDgaqnaVPKAVGWERNANGKLQPISVDLSKEFDPKR 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173742 324 LAESSVDLNLKLMCWRLVPTLDLDKVVSVKCLLLGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQPLYEFEDCL 403
Cdd:TIGR01381 311 LAERSVDLNLKLMKWRLHPDLQLERYSQLKVLLLGAGTLGCNVARCLIGWGVRHITFVDNGKVSYSNPVRQSLSNFEDCL 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173742 404 GGGKPKALAAAERLQKIFPGVNARGFNMSIPMPGHPVNFSDVtmEQARRDVEQLEQLIDNHDVIFLLMDTRESRWLPTVI 483
Cdd:TIGR01381 391 LGGRGKAETAQKALKRIFPSIQATGHRLTVPMPGHPIDEKDV--PELEKDIARLEQLIKDHDVVFLLLDSREARWLPTVL 468
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173742 484 AASKRKLVINAALGFDTFVVMRHglkkpkqqGAGdlcPSHLVapADLGSSlfANIPGYKLGCYFCNDVVAPGDSTRDRTL 563
Cdd:TIGR01381 469 CSRHKKIAISAALGFDSYVVMRH--------GIG---RSESV--SDVSSS--DSVPYSRLGCYFCNDVTAPGDSTTDRTL 533
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173742 564 DQQCTVSRPGLAVIAGALAVELMVSVLQHPEGGYAIASSSDDrmnepPTSLGLVPHQIRGFLSRFDNVLPVSLAFDKCTA 643
Cdd:TIGR01381 534 DQQCTVTRPGTAMIASGLAVELLVSVLQHPLPSKTPASHDDN-----TTVLGALPHQIRGFLGRFQQILLSVKRFDQCVA 608
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907173742 644 CSPKVLDQYEREGFTFLAKVFNSShSFLEDLTGLTLLHQETQAAEIwDMSDEET 697
Cdd:TIGR01381 609 CSDAVAAEYQQRGWKFVRDAMNSP-GYLEDLTGLTELKNESSVNAI-DIQDFES 660
Apg7 cd01486
Apg7 is an E1-like protein, that activates two different ubiquitin-like proteins, Apg12 and ...
353-677 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  Cd Length: 307  Bit Score: 570.08  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173742 353 KCLLLGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQPLYEFEDClGGGKPKALAAAERLQKIFPGVNARGFNMS 432
Cdd:cd01486     1 KCLLLGAGTLGCNVARNLLGWGVRHITFVDSGKVSYSNPVRQSLFTFEDC-KGGKPKAEAAAERLKEIFPSIDATGIVLS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173742 433 IPMPGHPVNFSDVtmEQARRDVEQLEQLIDNHDVIFLLMDTRESRWLPTVIAASKRKLVINAALGFDTFVVMRHGLKKPK 512
Cdd:cd01486    80 IPMPGHPISESEV--PSTLKDVKRLEELIKDHDVIFLLTDSRESRWLPTLLSAAKNKLVINAALGFDSYLVMRHGAGPQS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173742 513 QQGAGDlcpshlvapadlgsSLFANIPGYKLGCYFCNDVVAPGDSTRDRTLDQQCTVSRPGLAVIAGALAVELMVSVLQH 592
Cdd:cd01486   158 QSGSGD--------------SSSDSIPGSRLGCYFCNDVVAPGDSLKDRTLDQQCTVTRPGLSMIASSIAVELLVSLLQH 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173742 593 PEGGYAIASSSDDRMNEPPTSLGLVPHQIRGFLSRFDNVLPVSLAFDKCTACSPKVLDQYEREGFTFLAKVFNSSHsFLE 672
Cdd:cd01486   224 PLGGHAPAESSSNEGDEPTTVLGILPHQIRGFLSNFSNLTLSGQAYDQCTACSDAVIDEYHREGWEFVLKAFNSPD-YLE 302

                  ....*
gi 1907173742 673 DLTGL 677
Cdd:cd01486   303 ELTGL 307
ATG7_N pfam16420
Ubiquitin-like modifier-activating enzyme ATG7 N-terminus; This is the N-terminal domain of ...
9-319 8.11e-145

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: 435331  Cd Length: 309  Bit Score: 424.36  E-value: 8.11e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173742   9 LQFAPFNSALDVGFWHELTQKKLNEYRLDEAPKDIKGYYYNGDSAGLPTRLTLEFSAFDM-SASTPAHCCPAMGTLHNTN 87
Cdd:pfam16420   1 LQFAPFSSFIDPSFWHELSSLKLDVLKLDDSPRPILGLYEPRDAPGLSCRLQLDGSSFNDtSDDVPAGSCRAEGTLKNFN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173742  88 TLEAFKTADKKLLLEQSANEIWEAIKSGAALENPMLLNKFLLLTFADLKKYHFYYWFCCPALCLPesIPLIRGPVSLDQR 167
Cdd:pfam16420  81 TIEEFKNLDKQALLDDAGKKIWDAILSGTALEDPSLLSRFLLLSFADLKKYKFYYWFAFPALHSD--PAWVLSWKPASSA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173742 168 LSPKQIQALEHAYDDLCRAEGVTALPYFLFKYDDDTVL-VSLLKHYSDFFQGqRTKITVGVYDPCNLAQYPGWPLRNFLV 246
Cdd:pfam16420 159 LSSEETESLVDAVQTWRYSVDARQHGFFLVKKSRGSDWeIASLSEYENFFAD-VEDVYFGFADPSTLPENPGWPLRNLLA 237
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907173742 247 LAAHRWSGSfqSVEVLCFRDRTMQGARDvTHSIIFEVKLPE--MAFSPDCPKAVGWEKNQKGGMGPRMVNLSGCM 319
Cdd:pfam16420 238 LLRARWPLK--KVQVLCYRDTSRSGRRD-ERSLVLTLKLPEpsDENTSELPKAVGWERNAKGKLGPRVVDLSSYM 309
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
347-488 7.67e-13

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 70.02  E-value: 7.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173742 347 DKVVSVKCLLLGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQPLYEFED---CLgggkPKALAAAERLQKIfpg 423
Cdd:PRK07688   20 QKLREKHVLIIGAGALGTANAEMLVRAGVGKVTIVDRDYVEWSNLQRQQLYTESDvknNL----PKAVAAKKRLEEI--- 92
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907173742 424 vNargfnmsipmpghpvnfSDVTMEQARRDV--EQLEQLIDNHDVIFLLMDTRESRWLPTVIAASKR 488
Cdd:PRK07688   93 -N-----------------SDVRVEAIVQDVtaEELEELVTGVDLIIDATDNFETRFIVNDAAQKYG 141
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
347-646 1.86e-12

Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism];


Pssm-ID: 223552 [Multi-domain]  Cd Length: 254  Bit Score: 67.81  E-value: 1.86e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173742 347 DKVVSVKCLLLGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQPLYEFEDClggGKPKALAAAERLQKIFPGVNA 426
Cdd:COG0476    26 QKLKDSRVLVVGAGGLGSPAAKYLALAGVGKLTIVDFDTVELSNLQRQFLFTEADV---GKPKAEVAAKALRKLNPLVEV 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173742 427 RGFNMSIpmpghpvnfsdvtmeqarrDVEQLEQLIDNHDVIFLLMDTRESRWLptviaaskrklvINAAlgfdtfvvmRH 506
Cdd:COG0476   103 VAYLERL-------------------DEENAEELIAQFDVVLDCTDNFETRYL------------INDA---------CV 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173742 507 GLKKPkqqgagdlcpshLVAPADLGS--SLFANIPGYKLGCYFCNDVVAPGDSTRDRTLDQQCTVSRpgLAVIAGALAVE 584
Cdd:COG0476   143 KLGIP------------LVHGGAIGFegQVTVIIPGDKTPCYRCLFPEKPPPGLVPTSCDEAGVLGP--LVGVVGSLQAL 208
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907173742 585 LMVSVLqhpeggyaiasssddRMNEPPTSLGLVPHQIRGFLSRFDNVlPVSLAFDKCTACSP 646
Cdd:COG0476   209 EAIKLL---------------TGIGLEPLIGRLLLYDALDMERFRTL-KLRRRPISCPVCGV 254
 
Name Accession Description Interval E-value
E1_like_apg7 TIGR01381
E1-like protein-activating enzyme Gsa7p/Apg7p; This model represents a family of eukaryotic ...
11-697 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: 721.73  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173742  11 FAPFNSALDVGFWHELTQKKLNEYRLDEAPKDIKGYYYNGDSAGL--PTRLTLEFSAFDMSASTPAHCCPAMGTLHNTNT 88
Cdd:TIGR01381   1 FVPFVSCVDTGFWNEVSKLKLNKWKLDDTPKCISGQLSLHQTEGFkcHLSLSYDSLSSLESTTGTHAQLSVSGILLNYNT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173742  89 LEAFKTADKKLLLEQSANEIWEAIKSGAALENPMLLNKFLLLTFADLKKYHFYYWFCCPALCLPESIPLIRGPVSlDQRL 168
Cdd:TIGR01381  81 VESFKKVDKSDLLRSEAEKIWESIQTRKWLQDPSLLSQFFIISFADLKKFKFYYWFCFPALVYPSKVNKLSGLTE-SIKQ 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173742 169 SPKQIQALEHAYDDLCRAEGVTALPYFLFKYDDDTVLVslLKHYSDFFQGQRtKITVGVYDPCNLAQYPGWPLRNFLVLA 248
Cdd:TIGR01381 160 EITPLESLGADHKILFDFYRKNNFPFFLYSKQSSKMLE--LSELENNTNPDD-ELCVGFADPSPVAYSAGWMLRNVLAAV 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173742 249 AHRWsgsFQSVEVLCFRDRTMQGARDVTHSIifeVKLPEMAFSPD-----CPKAVGWEKNQKGGMGPRMVNLSGCMDPKR 323
Cdd:TIGR01381 237 AHLH---PTWKHVHIFSLRSADSIGIKYLWT---TLLPSAELSSDgaqnaVPKAVGWERNANGKLQPISVDLSKEFDPKR 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173742 324 LAESSVDLNLKLMCWRLVPTLDLDKVVSVKCLLLGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQPLYEFEDCL 403
Cdd:TIGR01381 311 LAERSVDLNLKLMKWRLHPDLQLERYSQLKVLLLGAGTLGCNVARCLIGWGVRHITFVDNGKVSYSNPVRQSLSNFEDCL 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173742 404 GGGKPKALAAAERLQKIFPGVNARGFNMSIPMPGHPVNFSDVtmEQARRDVEQLEQLIDNHDVIFLLMDTRESRWLPTVI 483
Cdd:TIGR01381 391 LGGRGKAETAQKALKRIFPSIQATGHRLTVPMPGHPIDEKDV--PELEKDIARLEQLIKDHDVVFLLLDSREARWLPTVL 468
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173742 484 AASKRKLVINAALGFDTFVVMRHglkkpkqqGAGdlcPSHLVapADLGSSlfANIPGYKLGCYFCNDVVAPGDSTRDRTL 563
Cdd:TIGR01381 469 CSRHKKIAISAALGFDSYVVMRH--------GIG---RSESV--SDVSSS--DSVPYSRLGCYFCNDVTAPGDSTTDRTL 533
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173742 564 DQQCTVSRPGLAVIAGALAVELMVSVLQHPEGGYAIASSSDDrmnepPTSLGLVPHQIRGFLSRFDNVLPVSLAFDKCTA 643
Cdd:TIGR01381 534 DQQCTVTRPGTAMIASGLAVELLVSVLQHPLPSKTPASHDDN-----TTVLGALPHQIRGFLGRFQQILLSVKRFDQCVA 608
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907173742 644 CSPKVLDQYEREGFTFLAKVFNSShSFLEDLTGLTLLHQETQAAEIwDMSDEET 697
Cdd:TIGR01381 609 CSDAVAAEYQQRGWKFVRDAMNSP-GYLEDLTGLTELKNESSVNAI-DIQDFES 660
Apg7 cd01486
Apg7 is an E1-like protein, that activates two different ubiquitin-like proteins, Apg12 and ...
353-677 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  Cd Length: 307  Bit Score: 570.08  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173742 353 KCLLLGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQPLYEFEDClGGGKPKALAAAERLQKIFPGVNARGFNMS 432
Cdd:cd01486     1 KCLLLGAGTLGCNVARNLLGWGVRHITFVDSGKVSYSNPVRQSLFTFEDC-KGGKPKAEAAAERLKEIFPSIDATGIVLS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173742 433 IPMPGHPVNFSDVtmEQARRDVEQLEQLIDNHDVIFLLMDTRESRWLPTVIAASKRKLVINAALGFDTFVVMRHGLKKPK 512
Cdd:cd01486    80 IPMPGHPISESEV--PSTLKDVKRLEELIKDHDVIFLLTDSRESRWLPTLLSAAKNKLVINAALGFDSYLVMRHGAGPQS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173742 513 QQGAGDlcpshlvapadlgsSLFANIPGYKLGCYFCNDVVAPGDSTRDRTLDQQCTVSRPGLAVIAGALAVELMVSVLQH 592
Cdd:cd01486   158 QSGSGD--------------SSSDSIPGSRLGCYFCNDVVAPGDSLKDRTLDQQCTVTRPGLSMIASSIAVELLVSLLQH 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173742 593 PEGGYAIASSSDDRMNEPPTSLGLVPHQIRGFLSRFDNVLPVSLAFDKCTACSPKVLDQYEREGFTFLAKVFNSSHsFLE 672
Cdd:cd01486   224 PLGGHAPAESSSNEGDEPTTVLGILPHQIRGFLSNFSNLTLSGQAYDQCTACSDAVIDEYHREGWEFVLKAFNSPD-YLE 302

                  ....*
gi 1907173742 673 DLTGL 677
Cdd:cd01486   303 ELTGL 307
ATG7_N pfam16420
Ubiquitin-like modifier-activating enzyme ATG7 N-terminus; This is the N-terminal domain of ...
9-319 8.11e-145

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: 435331  Cd Length: 309  Bit Score: 424.36  E-value: 8.11e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173742   9 LQFAPFNSALDVGFWHELTQKKLNEYRLDEAPKDIKGYYYNGDSAGLPTRLTLEFSAFDM-SASTPAHCCPAMGTLHNTN 87
Cdd:pfam16420   1 LQFAPFSSFIDPSFWHELSSLKLDVLKLDDSPRPILGLYEPRDAPGLSCRLQLDGSSFNDtSDDVPAGSCRAEGTLKNFN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173742  88 TLEAFKTADKKLLLEQSANEIWEAIKSGAALENPMLLNKFLLLTFADLKKYHFYYWFCCPALCLPesIPLIRGPVSLDQR 167
Cdd:pfam16420  81 TIEEFKNLDKQALLDDAGKKIWDAILSGTALEDPSLLSRFLLLSFADLKKYKFYYWFAFPALHSD--PAWVLSWKPASSA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173742 168 LSPKQIQALEHAYDDLCRAEGVTALPYFLFKYDDDTVL-VSLLKHYSDFFQGqRTKITVGVYDPCNLAQYPGWPLRNFLV 246
Cdd:pfam16420 159 LSSEETESLVDAVQTWRYSVDARQHGFFLVKKSRGSDWeIASLSEYENFFAD-VEDVYFGFADPSTLPENPGWPLRNLLA 237
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907173742 247 LAAHRWSGSfqSVEVLCFRDRTMQGARDvTHSIIFEVKLPE--MAFSPDCPKAVGWEKNQKGGMGPRMVNLSGCM 319
Cdd:pfam16420 238 LLRARWPLK--KVQVLCYRDTSRSGRRD-ERSLVLTLKLPEpsDENTSELPKAVGWERNAKGKLGPRVVDLSSYM 309
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
339-598 6.97e-48

ThiF family; This domain is found in ubiquitin activating E1 family and members of the bacterial ThiF/MoeB/HesA family. It is repeated in Ubiquitin-activating enzyme E1.


Pssm-ID: 425935 [Multi-domain]  Cd Length: 238  Bit Score: 168.59  E-value: 6.97e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173742 339 RLVPTLDLDKVVSVKCLLLGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQPLYEFEDClggGKPKALAAAERLQ 418
Cdd:pfam00899   8 PLIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREEDI---GKPKAEVAAERLR 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173742 419 KIFPGVNARGFNMSIpmpghpvnfsdvtmeqarrDVEQLEQLIDNHDVIFLLMDTRESRWLPTVIAASKRKLVINAA-LG 497
Cdd:pfam00899  85 EINPDVEVEAYTERL-------------------TPENAEELIESVDIVVDATDNFAARYLVNDACVKLGIPLIEAGvLG 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173742 498 FDTFVVMRhglkkpkqqgagdlcpshlvapadlgsslfanIPGyKLGCYFCNDVVAPgdstrDRTLDQQCTVS---RPGL 574
Cdd:pfam00899 146 FKGQVTVV--------------------------------IPG-KTPCYRCLFPEDP-----PRKLVPSCTVAgilGPTT 187
                         250       260
                  ....*....|....*....|....
gi 1907173742 575 AVIAGALAVELMVSVLQHPEGGYA 598
Cdd:pfam00899 188 AVVGGLQALEALKLLLGKGEPALA 211
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
353-508 1.40e-23

Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes classical ubiquitin-activating enzymes E1, ubiquitin-like (ubl) activating enzymes and other mechanistic homologes, like MoeB, Thif1 and others. The common reaction mechanism catalyzed by MoeB, ThiF and the E1 enzymes begins with a nucleophilic attack of the C-terminal carboxylate of MoaD, ThiS and ubiquitin, respectively, on the alpha-phosphate of an ATP molecule bound at the active site of the activating enzymes, leading to the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of MoaD and ThiS.


Pssm-ID: 238760 [Multi-domain]  Cd Length: 143  Bit Score: 96.95  E-value: 1.40e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173742 353 KCLLLGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQPLYEFEDClggGKPKALAAAERLQKIFPGVNARGFNMS 432
Cdd:cd01483     1 RVLLVGLGGLGSEIALNLARSGVGKITLIDFDTVELSNLNRQFLARQADI---GKPKAEVAARRLNELNPGVNVTAVPEG 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907173742 433 IPMpghpvnfsdvtmeqarrdvEQLEQLIDNHDVIFLLMDTRESRWLPTVIAASKRKLVINAALGFDTFVVMRHGL 508
Cdd:cd01483    78 ISE-------------------DNLDDFLDGVDLVIDAIDNIAVRRALNRACKELGIPVIDAGGLGLGGDIQVIDI 134
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
355-499 3.28e-13

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


Pssm-ID: 238386 [Multi-domain]  Cd Length: 228  Bit Score: 69.43  E-value: 3.28e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173742 355 LLLGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQPLYEFEDClggGKPKALAAAERLQKIFPGVNARGFNMSIp 434
Cdd:cd00757    25 LVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRQILHTEADV---GQPKAEAAAERLRAINPDVEIEAYNERL- 100
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907173742 435 mpghpvnfsdvtmeqarrDVEQLEQLIDNHDVIFLLMDTRESRWLPTVIAASKRK-LVINAALGFD 499
Cdd:cd00757   101 ------------------DAENAEELIAGYDLVLDCTDNFATRYLINDACVKLGKpLVSGAVLGFE 148
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
347-488 7.67e-13

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 70.02  E-value: 7.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173742 347 DKVVSVKCLLLGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQPLYEFED---CLgggkPKALAAAERLQKIfpg 423
Cdd:PRK07688   20 QKLREKHVLIIGAGALGTANAEMLVRAGVGKVTIVDRDYVEWSNLQRQQLYTESDvknNL----PKAVAAKKRLEEI--- 92
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907173742 424 vNargfnmsipmpghpvnfSDVTMEQARRDV--EQLEQLIDNHDVIFLLMDTRESRWLPTVIAASKR 488
Cdd:PRK07688   93 -N-----------------SDVRVEAIVQDVtaEELEELVTGVDLIIDATDNFETRFIVNDAAQKYG 141
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
347-646 1.86e-12

Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism];


Pssm-ID: 223552 [Multi-domain]  Cd Length: 254  Bit Score: 67.81  E-value: 1.86e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173742 347 DKVVSVKCLLLGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQPLYEFEDClggGKPKALAAAERLQKIFPGVNA 426
Cdd:COG0476    26 QKLKDSRVLVVGAGGLGSPAAKYLALAGVGKLTIVDFDTVELSNLQRQFLFTEADV---GKPKAEVAAKALRKLNPLVEV 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173742 427 RGFNMSIpmpghpvnfsdvtmeqarrDVEQLEQLIDNHDVIFLLMDTRESRWLptviaaskrklvINAAlgfdtfvvmRH 506
Cdd:COG0476   103 VAYLERL-------------------DEENAEELIAQFDVVLDCTDNFETRYL------------INDA---------CV 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173742 507 GLKKPkqqgagdlcpshLVAPADLGS--SLFANIPGYKLGCYFCNDVVAPGDSTRDRTLDQQCTVSRpgLAVIAGALAVE 584
Cdd:COG0476   143 KLGIP------------LVHGGAIGFegQVTVIIPGDKTPCYRCLFPEKPPPGLVPTSCDEAGVLGP--LVGVVGSLQAL 208
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907173742 585 LMVSVLqhpeggyaiasssddRMNEPPTSLGLVPHQIRGFLSRFDNVlPVSLAFDKCTACSP 646
Cdd:COG0476   209 EAIKLL---------------TGIGLEPLIGRLLLYDALDMERFRTL-KLRRRPISCPVCGV 254
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
355-479 1.62e-11

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 66.29  E-value: 1.62e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173742 355 LLLGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQPLYEFEDClGGGKPKALAAAERLQKIFPGVNARGFNMsip 434
Cdd:PRK12475   28 LIVGAGALGAANAEALVRAGIGKLTIADRDYVEWSNLQRQQLYTEEDA-KQKKPKAIAAKEHLRKINSEVEIVPVVT--- 103
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1907173742 435 mpghpvnfsDVTMeqarrdvEQLEQLIDNHDVIFLLMDTRESRWL 479
Cdd:PRK12475  104 ---------DVTV-------EELEELVKEVDLIIDATDNFDTRLL 132
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
339-508 2.29e-10

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320  Cd Length: 212  Bit Score: 60.64  E-value: 2.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173742 339 RLVPTLdLDKVVSVKCLLLGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQpLYEFEDClggGKPKALAAAERLQ 418
Cdd:PRK08644   17 RHTPKL-LEKLKKAKVGIAGAGGLGSNIAVALARSGVGNLKLVDFDVVEPSNLNRQ-QYFISQI---GMPKVEALKENLL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173742 419 KIFPGVNargfnmsipmpghpvnfsdVTMEQARRDVEQLEQLIDNHDVIFLLMDTresrwlptviAASKRKLViNAALG- 497
Cdd:PRK08644   92 EINPFVE-------------------IEAHNEKIDEDNIEELFKDCDIVVEAFDN----------AETKAMLV-ETVLEh 141
                         170
                  ....*....|.
gi 1907173742 498 FDTFVVMRHGL 508
Cdd:PRK08644  142 PGKKLVAASGM 152
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
355-482 2.35e-09

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 59.89  E-value: 2.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173742 355 LLLGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQPLYEFEDClggGKPKALAAAERLQKIFPG--VNARGFNMs 432
Cdd:PRK05600   45 LVIGAGGLGCPAMQSLASAGVGTITLIDDDTVDVSNIHRQILFGASDV---GRPKVEVAAERLKEIQPDirVNALRERL- 120
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907173742 433 ipmpghpvnfsdvTMEQARRDVEQLEQLIDNHDVI---FLLMDTRESRWLPTV 482
Cdd:PRK05600  121 -------------TAENAVELLNGVDLVLDGSDSFatkFLVADAAEITGTPLV 160
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
353-462 5.71e-09

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


Pssm-ID: 238766 [Multi-domain]  Cd Length: 312  Bit Score: 58.16  E-value: 5.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173742 353 KCLLLGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQPLYEFEDClggGKPKALAAAERLQKIFPGVNARGFNMS 432
Cdd:cd01489     1 KVLVVGAGGIGCELLKNLVLTGFGEIHIIDLDTIDLSNLNRQFLFRKKHV---GKSKAQVAKEAVLSFNPNVKIVAYHAN 77
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1907173742 433 IPMPGHPVNF---SDVTME-----QARRDVEQLEQLID 462
Cdd:cd01489    78 IKDPDFNVEFfkqFDLVFNaldnlAARRHVNKMCLAAD 115
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
353-499 8.56e-09

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 56.78  E-value: 8.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173742 353 KCLLLGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQPLYEFEDClggGKPKALAAAERLQKIFPGVNARGFNms 432
Cdd:PRK05690   34 RVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVSLSNLQRQVLHDDATI---GQPKVESARAALARINPHIAIETIN-- 108
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907173742 433 ipmpghpvnfsdvtmeqARRDVEQLEQLIDNHDVIfllMD------TRESrwLPTVIAASKRKLVINAALGFD 499
Cdd:PRK05690  109 -----------------ARLDDDELAALIAGHDLV---LDctdnvaTRNQ--LNRACFAAKKPLVSGAAIRME 159
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
353-425 2.37e-08

Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating enzyme (E1), specific for the Rub family of ubiquitin-like proteins (Ubls). E1 enzymes are part of a conjugation cascade to attach Ub or Ubls, covalently to substrate proteins. consisting of activating (E1), conjugating (E2), and/or ligating (E3) enzymes. E1 activates ubiquitin(-like) by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and Ubls C-terminus. E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. Post-translational modification by Rub family of ubiquitin-like proteins (Ublps) activates SCF ubiquitin ligases and is involved in cell cycle control, signaling and embryogenesis. UBA3 contains both the nucleotide-binding motif involved in adenylation and the catalytic cysteine involved in the thioester intermediate and Ublp transfer to E2.


Pssm-ID: 238765 [Multi-domain]  Cd Length: 291  Bit Score: 55.82  E-value: 2.37e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907173742 353 KCLLLGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQPLYEFEDClggGKPKALAAAERLQKIFPGVN 425
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. ...
353-508 2.32e-07

E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. The common reaction mechanism catalyzed by E1-like enzymes begins with a nucleophilic attack of the C-terminal carboxylate of the ubiquitin-like substrate, on the alpha-phosphate of an ATP molecule bound at the active site of the activating enzymes, leading to the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of the substrate. The exact function of this family is unknown.


Pssm-ID: 238764 [Multi-domain]  Cd Length: 174  Bit Score: 51.23  E-value: 2.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173742 353 KCLLLGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQPlYEFEDClggGKPKALAAAERLQKIFPgvnargfnms 432
Cdd:cd01487     1 KVGIAGAGGLGSNIAVLLARSGVGNLKLVDFDVVEPSNLNRQQ-YFLSQI---GEPKVEALKENLREINP---------- 66
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907173742 433 ipmpghpvnFSDVTMEQARRDVEQLEQLIDNHDVIFLLMDTresrwlptviAASKRkLVINAALGF-DTFVVMRHGL 508
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 ...
353-425 9.91e-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  Cd Length: 234  Bit Score: 50.27  E-value: 9.91e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907173742 353 KCLLLGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQPLYEFEDClggGKPKALAAAERLQKIFPGVN 425
Cdd:cd01484     1 KVLLVGAGGIGCELLKNLALMGFGQIHVIDMDTIDVSNLNRQFLFRPKDI---GRPKSEVAAEAVNDRNPNCK 70
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
348-467 6.58e-06

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 48.85  E-value: 6.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173742 348 KVVSVKCLLLGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQPLYEfEDCLggGKPKALAAAERLQKIFPGVnar 427
Cdd:PRK08762  132 RLLEARVLLIGAGGLGSPAALYLAAAGVGTLGIVDHDVVDRSNLQRQILHT-EDRV--GQPKVDSAAQRLAALNPDV--- 205
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1907173742 428 gfnmsipmpghpvnfsDVTMEQARRDVEQLEQLIDNHDVI 467
Cdd:PRK08762  206 ----------------QVEAVQERVTSDNVEALLQDVDVV 229
PRK08328 PRK08328
hypothetical protein; Provisional
347-485 1.22e-05

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 47.10  E-value: 1.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173742 347 DKVVSVKCLLLGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQPLYEFEDClgGGKPKALAAAERLQKifpgvna 426
Cdd:PRK08328   23 EKLKKAKVAVVGVGGLGSPVAYYLAAAGVGRILLIDEQTPELSNLNRQILHWEEDL--GKNPKPLSAKWKLER------- 93
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907173742 427 rgFNMSIPMPGHPVNFSDVTMEQARRDVEQLEQLIDNHDVIFLLMDTRESRWLPTVIAA 485
Cdd:PRK08328   94 --FNSDIKIETFVGRLSEENIDEVLKGVDVIVDCLDNFETRYLLDDYAHKKGIPLVHGA 150
E1-1_like cd01485
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ...
339-425 3.40e-05

Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present universally in eukaryotic cells, is part of cascade to attach ubiquitin (Ub) covalently to substrate proteins. This cascade consists of activating (E1), conjugating (E2), and/or ligating (E3) enzymes and then targets them for degradation by the 26S proteasome. E1 activates ubiquitin by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and ubiquitin's C-terminus. The E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. A set of novel molecules with a structural similarity to Ub, called Ub-like proteins (Ubls), have similar conjugation cascades. In contrast to ubiquitin-E1, which is a single-chain protein with a weakly conserved two-fold repeat, many of the Ubls-E1are a heterodimer where each subunit corresponds to one half of a single-chain E1. This CD represents the family homologous to the first repeat of Ub-E1.


Pssm-ID: 238762 [Multi-domain]  Cd Length: 198  Bit Score: 45.11  E-value: 3.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173742 339 RLVPTLDLDKVVSVKCLLLGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQPLYEFEDClGGGKPKALAAAERLQ 418
Cdd:cd01485     7 RLWGDEAQNKLRSAKVLIIGAGALGAEIAKNLVLAGIDSITIVDHRLVSTEDLGSNFFLDAEVS-NSGMNRAAASYEFLQ 85

                  ....*..
gi 1907173742 419 KIFPGVN 425
Cdd:cd01485    86 ELNPNVK 92
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
357-499 8.29e-05

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 45.25  E-value: 8.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173742 357 LGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQPLYEFEdclGGGKPKALAAAERLQKIFPGVnargfnmsipmp 436
Cdd:PRK05597   34 IGAGGLGSPALLYLAGAGVGHITIIDDDTVDLSNLHRQVIHSTA---GVGQPKAESAREAMLALNPDV------------ 98
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907173742 437 ghpvnfsDVTMEQARRDVEQLEQLIDNHDVIFLLMDTRESRWLPTVIAAskrKLVI----NAALGFD 499
Cdd:PRK05597   99 -------KVTVSVRRLTWSNALDELRDADVILDGSDNFDTRHLASWAAA---RLGIphvwASILGFD 155
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
353-425 3.32e-04

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


Pssm-ID: 238767 [Multi-domain]  Cd Length: 435  Bit Score: 43.43  E-value: 3.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173742 353 KCLLLGAGTLGC----NVArtLMGWGVR---HVTFVDNAKISYSNPVRQPLYEFEDClggGKPKALAAAERLQKIFPGVN 425
Cdd:cd01490     1 KVFLVGAGAIGCellkNFA--LMGVGTGesgEITVTDMDNIEKSNLNRQFLFRPHDV---GKPKSEVAAAAVKAMNPDLK 75
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
348-425 5.23e-03

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


Pssm-ID: 273603 [Multi-domain]  Cd Length: 1006  Bit Score: 40.26  E-value: 5.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173742  348 KVVSVKCLLLGAGTLGCNVARTLMGWGVR-----HVTFVDNAKISYSNPVRQPLYEFEDClggGKPKALAAAERLQKIFP 422
Cdd:TIGR01408  416 KLQNLNIFLVGCGAIGCEMLKNFALMGVGtgkkgMITVTDPDLIEKSNLNRQFLFRPHHI---GKPKSYTAADATLKINP 492

                   ...
gi 1907173742  423 GVN 425
Cdd:TIGR01408  493 QIK 495
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
358-422 9.81e-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: 38.35  E-value: 9.81e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907173742 358 GAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQpLYEFEDCLGggKPKALAAAERLQKIFP 422
Cdd:cd00755    18 GLGGVGSWAAEALARSGVGKLTLIDFDVVCVSNLNRQ-IHALLSTVG--KPKVEVMAERIRDINP 79
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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