|
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 22550098 11 FAPFNSALDVGFWHELTQKKLNEYRLDEAPKDIKGYYYNGDSAGL--PTRLTLEFSAFDMSASTPAHCCPAMGTLHNTNT 88
Cdd:TIGR01381 1 FVPFVSCVDTGFWNEVSKLKLNKWKLDDTPKCISGQLSLHQTEGFkcHLSLSYDSLSSLESTTGTHAQLSVSGILLNYNT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550098 89 LEAFKTADKKLLLEQSANEIWEAIKSGAALENPMLLNKFLLLTFADLKKYHFYYWFCCPALCLPESIPLIRGPVSlDQRL 168
Cdd:TIGR01381 81 VESFKKVDKSDLLRSEAEKIWESIQTRKWLQDPSLLSQFFIISFADLKKFKFYYWFCFPALVYPSKVNKLSGLTE-SIKQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550098 169 SPKQIQALEHAYDDLCRAEGVTALPYFLFKYDDDTVLVslLKHYSDFFQGQRtKITVGVYDPCNLAQYPGWPLRNFLVLA 248
Cdd:TIGR01381 160 EITPLESLGADHKILFDFYRKNNFPFFLYSKQSSKMLE--LSELENNTNPDD-ELCVGFADPSPVAYSAGWMLRNVLAAV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550098 249 AHRWsgsFQSVEVLCFRDRTMQGARDVTHSIifeVKLPEMAFSPD-----CPKAVGWEKNQKGGMGPRMVNLSGCMDPKR 323
Cdd:TIGR01381 237 AHLH---PTWKHVHIFSLRSADSIGIKYLWT---TLLPSAELSSDgaqnaVPKAVGWERNANGKLQPISVDLSKEFDPKR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550098 324 LAESSVDLNLKLMCWRLVPTLDLDKVVSVKCLLLGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQPLYEFEDCL 403
Cdd:TIGR01381 311 LAERSVDLNLKLMKWRLHPDLQLERYSQLKVLLLGAGTLGCNVARCLIGWGVRHITFVDNGKVSYSNPVRQSLSNFEDCL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550098 404 GGGKPKALAAAERLQKIFPGVNARGFNMSIPMPGHPVNFSDVtmEQARRDVEQLEQLIDNHDVIFLLMDTRESRWLPTVI 483
Cdd:TIGR01381 391 LGGRGKAETAQKALKRIFPSIQATGHRLTVPMPGHPIDEKDV--PELEKDIARLEQLIKDHDVVFLLLDSREARWLPTVL 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550098 484 AASKRKLVINAALGFDTFVVMRHglkkpkqqGAGdlcPSHLVapADLGSSlfANIPGYKLGCYFCNDVVAPGDSTRDRTL 563
Cdd:TIGR01381 469 CSRHKKIAISAALGFDSYVVMRH--------GIG---RSESV--SDVSSS--DSVPYSRLGCYFCNDVTAPGDSTTDRTL 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550098 564 DQQCTVSRPGLAVIAGALAVELMVSVLQHPEGGYAIASSSDDrmnepPTSLGLVPHQIRGFLSRFDNVLPVSLAFDKCTA 643
Cdd:TIGR01381 534 DQQCTVTRPGTAMIASGLAVELLVSVLQHPLPSKTPASHDDN-----TTVLGALPHQIRGFLGRFQQILLSVKRFDQCVA 608
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 22550098 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 [Multi-domain] Cd Length: 307 Bit Score: 570.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550098 353 KCLLLGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQPLYEFEDClGGGKPKALAAAERLQKIFPGVNARGFNMS 432
Cdd:cd01486 1 KCLLLGAGTLGCNVARNLLGWGVRHITFVDSGKVSYSNPVRQSLFTFEDC-KGGKPKAEAAAERLKEIFPSIDATGIVLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550098 433 IPMPGHPVNFSDVtmEQARRDVEQLEQLIDNHDVIFLLMDTRESRWLPTVIAASKRKLVINAALGFDTFVVMRHGLKKPK 512
Cdd:cd01486 80 IPMPGHPISESEV--PSTLKDVKRLEELIKDHDVIFLLTDSRESRWLPTLLSAAKNKLVINAALGFDSYLVMRHGAGPQS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550098 513 QQGAGDlcpshlvapadlgsSLFANIPGYKLGCYFCNDVVAPGDSTRDRTLDQQCTVSRPGLAVIAGALAVELMVSVLQH 592
Cdd:cd01486 158 QSGSGD--------------SSSDSIPGSRLGCYFCNDVVAPGDSLKDRTLDQQCTVTRPGLSMIASSIAVELLVSLLQH 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550098 593 PEGGYAIASSSDDRMNEPPTSLGLVPHQIRGFLSRFDNVLPVSLAFDKCTACSPKVLDQYEREGFTFLAKVFNSSHsFLE 672
Cdd:cd01486 224 PLGGHAPAESSSNEGDEPTTVLGILPHQIRGFLSNFSNLTLSGQAYDQCTACSDAVIDEYHREGWEFVLKAFNSPD-YLE 302
|
....*
gi 22550098 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 |
1.33e-142 |
|
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: 418.97 E-value: 1.33e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550098 9 LQFAPFNSALDVGFWHELTQKKLNEYRLDEAPKDIKGYYYNGDSAGLPTRLTLEFSAFDM-SASTPAHCCPAMGTLHNTN 87
Cdd:pfam16420 1 LQFAPFSSFIDPSFWHELSSLKLDVLKLDDSPRPILGLYEPRDAPGLSCRLQLDGSSFNDtSDAVPPGSCRAEGTLKNFN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550098 88 TLEAFKTADKKLLLEQSANEIWEAIKSGAALENPMLLNKFLLLTFADLKKYHFYYWFCCPALCLPesIPLIRGPVSLDQR 167
Cdd:pfam16420 81 TIEEFKNLDKQALLDDAGKKIWDAILSGTALEDPSLLSRFLLLSFADLKKYKFYYWFAFPALHSD--PAWVLSWKPASEE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550098 168 LSPKQIQALEHAYDDLCRAEGVTALpYFLFKYDDDTVL-VSLLKHYSDFFQGqRTKITVGVYDPCNLAQYPGWPLRNFLV 246
Cdd:pfam16420 159 LSSEETESLVDAVQTWRYSVDARQH-FFLVKKSRGSDWeIASLSEYENFFAD-VEDVYFGFADPSTLPENPGWPLRNLLA 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22550098 247 LAAHRWSGSfqSVEVLCFRDRTMQGARDvTHSIIFEVKLPE--MAFSPDCPKAVGWEKNQKGGMGPRMVNLSGCM 319
Cdd:pfam16420 237 LLRARWPLK--KVQVLCYRDNSRSGRRD-ERSLVLTLKLPEpsDENTSELPKAVGWERNANGKLGPRVVDLSSYM 308
|
|
| ThiF |
COG0476 |
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ... |
355-499 |
5.17e-14 |
|
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; Molybdopterin or thiamine biosynthesis adenylyltransferase is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 440244 [Multi-domain] Cd Length: 244 Bit Score: 72.08 E-value: 5.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550098 355 LLLGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQPLYEFEDClggGKPKALAAAERLQKIFPGVNARGFNMSIp 434
Cdd:COG0476 31 LVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADV---GRPKVEAAAERLRALNPDVEVEAIPERL- 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22550098 435 mpghpvnfsdvtmeqarrDVEQLEQLIDNHDVIFLLMDTRESR-WLPTVIAASKRKLVINAALGFD 499
Cdd:COG0476 107 ------------------TEENALELLAGADLVLDCTDNFATRyLLNDACVKLGIPLVSGAVIGFE 154
|
|
| PRK07688 |
PRK07688 |
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated |
347-488 |
8.00e-13 |
|
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
Pssm-ID: 181084 [Multi-domain] Cd Length: 339 Bit Score: 70.02 E-value: 8.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550098 347 DKVVSVKCLLLGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQPLYEFED---CLgggkPKALAAAERLQKIfpg 423
Cdd:PRK07688 20 QKLREKHVLIIGAGALGTANAEMLVRAGVGKVTIVDRDYVEWSNLQRQQLYTESDvknNL----PKAVAAKKRLEEI--- 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22550098 424 vNargfnmsipmpghpvnfSDVTMEQARRDV--EQLEQLIDNHDVIFLLMDTRESRWLPTVIAASKR 488
Cdd:PRK07688 93 -N-----------------SDVRVEAIVQDVtaEELEELVTGVDLIIDATDNFETRFIVNDAAQKYG 141
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| E1_like_apg7 |
TIGR01381 |
E1-like protein-activating enzyme Gsa7p/Apg7p; This model represents a family of eukaryotic ... |
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 22550098 11 FAPFNSALDVGFWHELTQKKLNEYRLDEAPKDIKGYYYNGDSAGL--PTRLTLEFSAFDMSASTPAHCCPAMGTLHNTNT 88
Cdd:TIGR01381 1 FVPFVSCVDTGFWNEVSKLKLNKWKLDDTPKCISGQLSLHQTEGFkcHLSLSYDSLSSLESTTGTHAQLSVSGILLNYNT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550098 89 LEAFKTADKKLLLEQSANEIWEAIKSGAALENPMLLNKFLLLTFADLKKYHFYYWFCCPALCLPESIPLIRGPVSlDQRL 168
Cdd:TIGR01381 81 VESFKKVDKSDLLRSEAEKIWESIQTRKWLQDPSLLSQFFIISFADLKKFKFYYWFCFPALVYPSKVNKLSGLTE-SIKQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550098 169 SPKQIQALEHAYDDLCRAEGVTALPYFLFKYDDDTVLVslLKHYSDFFQGQRtKITVGVYDPCNLAQYPGWPLRNFLVLA 248
Cdd:TIGR01381 160 EITPLESLGADHKILFDFYRKNNFPFFLYSKQSSKMLE--LSELENNTNPDD-ELCVGFADPSPVAYSAGWMLRNVLAAV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550098 249 AHRWsgsFQSVEVLCFRDRTMQGARDVTHSIifeVKLPEMAFSPD-----CPKAVGWEKNQKGGMGPRMVNLSGCMDPKR 323
Cdd:TIGR01381 237 AHLH---PTWKHVHIFSLRSADSIGIKYLWT---TLLPSAELSSDgaqnaVPKAVGWERNANGKLQPISVDLSKEFDPKR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550098 324 LAESSVDLNLKLMCWRLVPTLDLDKVVSVKCLLLGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQPLYEFEDCL 403
Cdd:TIGR01381 311 LAERSVDLNLKLMKWRLHPDLQLERYSQLKVLLLGAGTLGCNVARCLIGWGVRHITFVDNGKVSYSNPVRQSLSNFEDCL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550098 404 GGGKPKALAAAERLQKIFPGVNARGFNMSIPMPGHPVNFSDVtmEQARRDVEQLEQLIDNHDVIFLLMDTRESRWLPTVI 483
Cdd:TIGR01381 391 LGGRGKAETAQKALKRIFPSIQATGHRLTVPMPGHPIDEKDV--PELEKDIARLEQLIKDHDVVFLLLDSREARWLPTVL 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550098 484 AASKRKLVINAALGFDTFVVMRHglkkpkqqGAGdlcPSHLVapADLGSSlfANIPGYKLGCYFCNDVVAPGDSTRDRTL 563
Cdd:TIGR01381 469 CSRHKKIAISAALGFDSYVVMRH--------GIG---RSESV--SDVSSS--DSVPYSRLGCYFCNDVTAPGDSTTDRTL 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550098 564 DQQCTVSRPGLAVIAGALAVELMVSVLQHPEGGYAIASSSDDrmnepPTSLGLVPHQIRGFLSRFDNVLPVSLAFDKCTA 643
Cdd:TIGR01381 534 DQQCTVTRPGTAMIASGLAVELLVSVLQHPLPSKTPASHDDN-----TTVLGALPHQIRGFLGRFQQILLSVKRFDQCVA 608
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 22550098 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 [Multi-domain] Cd Length: 307 Bit Score: 570.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550098 353 KCLLLGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQPLYEFEDClGGGKPKALAAAERLQKIFPGVNARGFNMS 432
Cdd:cd01486 1 KCLLLGAGTLGCNVARNLLGWGVRHITFVDSGKVSYSNPVRQSLFTFEDC-KGGKPKAEAAAERLKEIFPSIDATGIVLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550098 433 IPMPGHPVNFSDVtmEQARRDVEQLEQLIDNHDVIFLLMDTRESRWLPTVIAASKRKLVINAALGFDTFVVMRHGLKKPK 512
Cdd:cd01486 80 IPMPGHPISESEV--PSTLKDVKRLEELIKDHDVIFLLTDSRESRWLPTLLSAAKNKLVINAALGFDSYLVMRHGAGPQS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550098 513 QQGAGDlcpshlvapadlgsSLFANIPGYKLGCYFCNDVVAPGDSTRDRTLDQQCTVSRPGLAVIAGALAVELMVSVLQH 592
Cdd:cd01486 158 QSGSGD--------------SSSDSIPGSRLGCYFCNDVVAPGDSLKDRTLDQQCTVTRPGLSMIASSIAVELLVSLLQH 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550098 593 PEGGYAIASSSDDRMNEPPTSLGLVPHQIRGFLSRFDNVLPVSLAFDKCTACSPKVLDQYEREGFTFLAKVFNSSHsFLE 672
Cdd:cd01486 224 PLGGHAPAESSSNEGDEPTTVLGILPHQIRGFLSNFSNLTLSGQAYDQCTACSDAVIDEYHREGWEFVLKAFNSPD-YLE 302
|
....*
gi 22550098 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 |
1.33e-142 |
|
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: 418.97 E-value: 1.33e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550098 9 LQFAPFNSALDVGFWHELTQKKLNEYRLDEAPKDIKGYYYNGDSAGLPTRLTLEFSAFDM-SASTPAHCCPAMGTLHNTN 87
Cdd:pfam16420 1 LQFAPFSSFIDPSFWHELSSLKLDVLKLDDSPRPILGLYEPRDAPGLSCRLQLDGSSFNDtSDAVPPGSCRAEGTLKNFN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550098 88 TLEAFKTADKKLLLEQSANEIWEAIKSGAALENPMLLNKFLLLTFADLKKYHFYYWFCCPALCLPesIPLIRGPVSLDQR 167
Cdd:pfam16420 81 TIEEFKNLDKQALLDDAGKKIWDAILSGTALEDPSLLSRFLLLSFADLKKYKFYYWFAFPALHSD--PAWVLSWKPASEE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550098 168 LSPKQIQALEHAYDDLCRAEGVTALpYFLFKYDDDTVL-VSLLKHYSDFFQGqRTKITVGVYDPCNLAQYPGWPLRNFLV 246
Cdd:pfam16420 159 LSSEETESLVDAVQTWRYSVDARQH-FFLVKKSRGSDWeIASLSEYENFFAD-VEDVYFGFADPSTLPENPGWPLRNLLA 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22550098 247 LAAHRWSGSfqSVEVLCFRDRTMQGARDvTHSIIFEVKLPE--MAFSPDCPKAVGWEKNQKGGMGPRMVNLSGCM 319
Cdd:pfam16420 237 LLRARWPLK--KVQVLCYRDNSRSGRRD-ERSLVLTLKLPEpsDENTSELPKAVGWERNANGKLGPRVVDLSSYM 308
|
|
| ThiF |
pfam00899 |
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ... |
331-598 |
3.27e-48 |
|
ThiF family; This domain is found in ubiquitin activating E1 family and members of the bacterial ThiF/MoeB/HesA family. It is repeated in Ubiquitin-activating enzyme E1.
Pssm-ID: 459987 [Multi-domain] Cd Length: 238 Bit Score: 169.74 E-value: 3.27e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550098 331 LNLKLMCwRLVPTLDLDKVVSVKCLLLGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQPLYEFEDClggGKPKA 410
Cdd:pfam00899 1 YSRQLAL-PLIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADI---GKPKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550098 411 LAAAERLQKIFPGVNARGFNMSIpmpghpvnfsdvtmeqarrDVEQLEQLIDNHDVIFLLMDTRESRWLPTVIAASKRKL 490
Cdd:pfam00899 77 EVAAERLREINPDVEVEAYTERL-------------------TPENAEELIKSFDIVVDATDNFAARYLVNDACVKLGKP 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550098 491 VINAA-LGFDTFVVMRhglkkpkqqgagdlcpshlvapadlgsslfanIPGyKLGCYFCNDVVAPgdstrDRTLDQQCTV 569
Cdd:pfam00899 138 LIEAGvLGFKGQVTVV--------------------------------IPG-KTPCYRCLFPEDP-----PPKLVPSCTV 179
|
250 260 270
....*....|....*....|....*....|..
gi 22550098 570 S---RPGLAVIAGALAVELMVSVLQHPEGGYA 598
Cdd:pfam00899 180 AgvlGPTTAVVAGLQALEALKLLLGKGEPNLA 211
|
|
| E1_enzyme_family |
cd01483 |
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ... |
353-508 |
1.46e-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: 1.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550098 353 KCLLLGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQPLYEFEDClggGKPKALAAAERLQKIFPGVNARGFNMS 432
Cdd:cd01483 1 RVLLVGLGGLGSEIALNLARSGVGKITLIDFDTVELSNLNRQFLARQADI---GKPKAEVAARRLNELNPGVNVTAVPEG 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22550098 433 IPMpghpvnfsdvtmeqarrdvEQLEQLIDNHDVIFLLMDTRESRWLPTVIAASKRKLVINAALGFDTFVVMRHGL 508
Cdd:cd01483 78 ISE-------------------DNLDDFLDGVDLVIDAIDNIAVRRALNRACKELGIPVIDAGGLGLGGDIQVIDI 134
|
|
| ThiF |
COG0476 |
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ... |
355-499 |
5.17e-14 |
|
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; Molybdopterin or thiamine biosynthesis adenylyltransferase is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 440244 [Multi-domain] Cd Length: 244 Bit Score: 72.08 E-value: 5.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550098 355 LLLGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQPLYEFEDClggGKPKALAAAERLQKIFPGVNARGFNMSIp 434
Cdd:COG0476 31 LVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADV---GRPKVEAAAERLRALNPDVEVEAIPERL- 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22550098 435 mpghpvnfsdvtmeqarrDVEQLEQLIDNHDVIFLLMDTRESR-WLPTVIAASKRKLVINAALGFD 499
Cdd:COG0476 107 ------------------TEENALELLAGADLVLDCTDNFATRyLLNDACVKLGIPLVSGAVIGFE 154
|
|
| ThiF_MoeB_HesA_family |
cd00757 |
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ... |
355-499 |
3.42e-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: 3.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550098 355 LLLGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQPLYEFEDClggGKPKALAAAERLQKIFPGVNARGFNMSIp 434
Cdd:cd00757 25 LVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRQILHTEADV---GQPKAEAAAERLRAINPDVEIEAYNERL- 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22550098 435 mpghpvnfsdvtmeqarrDVEQLEQLIDNHDVIFLLMDTRESRWLPTVIAASKRK-LVINAALGFD 499
Cdd:cd00757 101 ------------------DAENAEELIAGYDLVLDCTDNFATRYLINDACVKLGKpLVSGAVLGFE 148
|
|
| PRK07688 |
PRK07688 |
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated |
347-488 |
8.00e-13 |
|
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
Pssm-ID: 181084 [Multi-domain] Cd Length: 339 Bit Score: 70.02 E-value: 8.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550098 347 DKVVSVKCLLLGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQPLYEFED---CLgggkPKALAAAERLQKIfpg 423
Cdd:PRK07688 20 QKLREKHVLIIGAGALGTANAEMLVRAGVGKVTIVDRDYVEWSNLQRQQLYTESDvknNL----PKAVAAKKRLEEI--- 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22550098 424 vNargfnmsipmpghpvnfSDVTMEQARRDV--EQLEQLIDNHDVIFLLMDTRESRWLPTVIAASKR 488
Cdd:PRK07688 93 -N-----------------SDVRVEAIVQDVtaEELEELVTGVDLIIDATDNFETRFIVNDAAQKYG 141
|
|
| PRK12475 |
PRK12475 |
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional |
355-479 |
1.69e-11 |
|
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
Pssm-ID: 183547 [Multi-domain] Cd Length: 338 Bit Score: 66.29 E-value: 1.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550098 355 LLLGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQPLYEFEDClGGGKPKALAAAERLQKIFPGVNARGFNMsip 434
Cdd:PRK12475 28 LIVGAGALGAANAEALVRAGIGKLTIADRDYVEWSNLQRQQLYTEEDA-KQKKPKAIAAKEHLRKINSEVEIVPVVT--- 103
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 22550098 435 mpghpvnfsDVTMeqarrdvEQLEQLIDNHDVIFLLMDTRESRWL 479
Cdd:PRK12475 104 ---------DVTV-------EELEELVKEVDLIIDATDNFDTRLL 132
|
|
| PRK08644 |
PRK08644 |
sulfur carrier protein ThiS adenylyltransferase ThiF; |
339-508 |
2.39e-10 |
|
sulfur carrier protein ThiS adenylyltransferase ThiF;
Pssm-ID: 236320 [Multi-domain] Cd Length: 212 Bit Score: 60.64 E-value: 2.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550098 339 RLVPTLdLDKVVSVKCLLLGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQpLYEFEDClggGKPKALAAAERLQ 418
Cdd:PRK08644 17 RHTPKL-LEKLKKAKVGIAGAGGLGSNIAVALARSGVGNLKLVDFDVVEPSNLNRQ-QYFISQI---GMPKVEALKENLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550098 419 KIFPGVNargfnmsipmpghpvnfsdVTMEQARRDVEQLEQLIDNHDVIFLLMDTresrwlptviAASKRKLViNAALG- 497
Cdd:PRK08644 92 EINPFVE-------------------IEAHNEKIDEDNIEELFKDCDIVVEAFDN----------AETKAMLV-ETVLEh 141
|
170
....*....|.
gi 22550098 498 FDTFVVMRHGL 508
Cdd:PRK08644 142 PGKKLVAASGM 152
|
|
| PRK05600 |
PRK05600 |
thiamine biosynthesis protein ThiF; Validated |
355-482 |
2.45e-09 |
|
thiamine biosynthesis protein ThiF; Validated
Pssm-ID: 235528 [Multi-domain] Cd Length: 370 Bit Score: 59.89 E-value: 2.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550098 355 LLLGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQPLYEFEDClggGKPKALAAAERLQKIFPG--VNARGFNMs 432
Cdd:PRK05600 45 LVIGAGGLGCPAMQSLASAGVGTITLIDDDTVDVSNIHRQILFGASDV---GRPKVEVAAERLKEIQPDirVNALRERL- 120
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 22550098 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 |
5.95e-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: 5.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550098 353 KCLLLGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQPLYEFEDClggGKPKALAAAERLQKIFPGVNARGFNMS 432
Cdd:cd01489 1 KVLVVGAGGIGCELLKNLVLTGFGEIHIIDLDTIDLSNLNRQFLFRKKHV---GKSKAQVAKEAVLSFNPNVKIVAYHAN 77
|
90 100 110
....*....|....*....|....*....|....*...
gi 22550098 433 IPMPGHPVNF---SDVTME-----QARRDVEQLEQLID 462
Cdd:cd01489 78 IKDPDFNVEFfkqFDLVFNaldnlAARRHVNKMCLAAD 115
|
|
| PRK05690 |
PRK05690 |
molybdopterin biosynthesis protein MoeB; Provisional |
353-499 |
8.93e-09 |
|
molybdopterin biosynthesis protein MoeB; Provisional
Pssm-ID: 180204 [Multi-domain] Cd Length: 245 Bit Score: 56.78 E-value: 8.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550098 353 KCLLLGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQPLYEFEDClggGKPKALAAAERLQKIFPGVNARGFNms 432
Cdd:PRK05690 34 RVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVSLSNLQRQVLHDDATI---GQPKVESARAALARINPHIAIETIN-- 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22550098 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 |
2.48e-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: 2.48e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22550098 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 |
2.42e-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: 2.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550098 353 KCLLLGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQPlYEFEDClggGKPKALAAAERLQKIFPgvnargfnms 432
Cdd:cd01487 1 KVGIAGAGGLGSNIAVLLARSGVGNLKLVDFDVVEPSNLNRQQ-YFLSQI---GEPKVEALKENLREINP---------- 66
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22550098 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 |
1.03e-06 |
|
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present universally in eukaryotic cells, is part of cascade to attach ubiquitin (Ub) covalently to substrate proteins. This cascade consists of activating (E1), conjugating (E2), and/or ligating (E3) enzymes and then targets them for degradation by the 26S proteasome. E1 activates ubiquitin by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and ubiquitin's C-terminus. E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. A set of novel molecules with a structural similarity to Ub, called Ub-like proteins (Ubls), have similar conjugation cascades. In contrast to ubiquitin-E1, which is a single-chain protein with a weakly conserved two-fold repeat, many of the Ubls-E1are a heterodimer where each subunit corresponds to one half of a single-chain E1. This CD represents the family homologous to the second repeat of Ub-E1.
Pssm-ID: 238761 [Multi-domain] Cd Length: 234 Bit Score: 50.27 E-value: 1.03e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22550098 353 KCLLLGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQPLYEFEDClggGKPKALAAAERLQKIFPGVN 425
Cdd:cd01484 1 KVLLVGAGGIGCELLKNLALMGFGQIHVIDMDTIDVSNLNRQFLFRPKDI---GRPKSEVAAEAVNDRNPNCK 70
|
|
| PRK08762 |
PRK08762 |
molybdopterin-synthase adenylyltransferase MoeB; |
348-467 |
6.86e-06 |
|
molybdopterin-synthase adenylyltransferase MoeB;
Pssm-ID: 236337 [Multi-domain] Cd Length: 376 Bit Score: 48.85 E-value: 6.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550098 348 KVVSVKCLLLGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQPLYEfEDCLggGKPKALAAAERLQKIFPGVnar 427
Cdd:PRK08762 132 RLLEARVLLIGAGGLGSPAALYLAAAGVGTLGIVDHDVVDRSNLQRQILHT-EDRV--GQPKVDSAAQRLAALNPDV--- 205
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 22550098 428 gfnmsipmpghpvnfsDVTMEQARRDVEQLEQLIDNHDVI 467
Cdd:PRK08762 206 ----------------QVEAVQERVTSDNVEALLQDVDVV 229
|
|
| PRK08328 |
PRK08328 |
hypothetical protein; Provisional |
347-485 |
1.28e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 169382 [Multi-domain] Cd Length: 231 Bit Score: 47.10 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550098 347 DKVVSVKCLLLGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQPLYEFEDClgGGKPKALAAAERLQKifpgvna 426
Cdd:PRK08328 23 EKLKKAKVAVVGVGGLGSPVAYYLAAAGVGRILLIDEQTPELSNLNRQILHWEEDL--GKNPKPLSAKWKLER------- 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 22550098 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 |
3.55e-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: 3.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550098 339 RLVPTLDLDKVVSVKCLLLGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQPLYEFEDClGGGKPKALAAAERLQ 418
Cdd:cd01485 7 RLWGDEAQNKLRSAKVLIIGAGALGAEIAKNLVLAGIDSITIVDHRLVSTEDLGSNFFLDAEVS-NSGMNRAAASYEFLQ 85
|
....*..
gi 22550098 419 KIFPGVN 425
Cdd:cd01485 86 ELNPNVK 92
|
|
| PRK05597 |
PRK05597 |
molybdopterin biosynthesis protein MoeB; Validated |
357-499 |
8.64e-05 |
|
molybdopterin biosynthesis protein MoeB; Validated
Pssm-ID: 235526 [Multi-domain] Cd Length: 355 Bit Score: 45.25 E-value: 8.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550098 357 LGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQPLYEFEdclGGGKPKALAAAERLQKIFPGVnargfnmsipmp 436
Cdd:PRK05597 34 IGAGGLGSPALLYLAGAGVGHITIIDDDTVDLSNLHRQVIHSTA---GVGQPKAESAREAMLALNPDV------------ 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22550098 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 |
3.46e-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: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550098 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 |
5.45e-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: 5.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550098 348 KVVSVKCLLLGAGTLGCNVARTLMGWGVR-----HVTFVDNAKISYSNPVRQPLYEFEDClggGKPKALAAAERLQKIFP 422
Cdd:TIGR01408 416 KLQNLNIFLVGCGAIGCEMLKNFALMGVGtgkkgMITVTDPDLIEKSNLNRQFLFRPHHI---GKPKSYTAADATLKINP 492
|
...
gi 22550098 423 GVN 425
Cdd:TIGR01408 493 QIK 495
|
|
| |
