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Conserved domains on  [gi|1972267130|ref|NP_001379450|]
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E1 ubiquitin-activating enzyme [Caenorhabditis elegans]

Protein Classification

ubiquitin-activating E1 family protein( domain architecture ID 1000537)

Ube1 (ubiquitin-activating E1) family protein similar to ubiquitin-activating enzyme E1 (UBA1) that catalyzes the first step in ubiquitin conjugation to mark cellular proteins for degradation through the ubiquitin-proteasome system

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Ube1 super family cl36897
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
18-1026 0e+00

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.


The actual alignment was detected with superfamily member TIGR01408:

Pssm-ID: 273603 [Multi-domain]  Cd Length: 1006  Bit Score: 1003.64  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130   18 LDKNLYSRQIYTLGESAMVNLRTASVLISGLGSVGVEIAKNLILGGVRHVTIHDTKLAKWSDLSAQYYLRDADVGHNRAT 97
Cdd:TIGR01408    2 IDEALYSRQLYVLGDEAMQKMAKSNVLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLSSNFFLSEDDVGRNRAE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130   98 SCYERLAELNDSVNVQVSTDELTEEFVKTFDLVVLTDAARTAQRQIAAWTRAHNRRI--LITDARGVFSYIFNDFGDNFR 175
Cdd:TIGR01408   82 AVVKKLAELNPYVHVSSSSVPFNEEFLDKFQCVVLTEMSLPLQKEINDFCHSQCPPIafISADVRGLFGSLFCDFGDEFE 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  176 IDDATGEQVREFFIEHI-DKTTGEVTTLENLFHGLEDGDHVTFSEVKGLTEINGCEPLKITVKNASKFNIGDfAVSFSDY 254
Cdd:TIGR01408  162 VLDTDGEEPKTGFIASItQANPGIVTCLENHRHKLETGDFVTFREVNGMTGLNDGSPRKITVISPYSFSIGD-TTELGPY 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  255 KEGGRCRQVKVPTSVSHVPFEKSLVEPEFGIWDYAKFEYPSQLHALWTALYAFEEKYGRSPAPRSTQDAALLKEL---IP 331
Cdd:TIGR01408  241 LHGGIATQVKTPKTVFFKSLREQLKDPKCLIVDFSKPERPPEIHTAFQALDQFQEKYSRKPNVGCQQDAEELLKLatsIS 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  332 SGTE----EIPEKLIELFSFSASGNLVTVSSVVGGIAAQEAMKGVTHHMTPLKQWLHLDHVEVLPGDwtsfdnSKLSETD 407
Cdd:TIGR01408  321 ETLEekvpDVDAKLVHWLSWTAQGFLSPMAAAVGGVVSQEVLKAVTGKFSPLCQWFYFDSAESLPSL------GKPECEE 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  408 CQPRQSRYDGQAAVFGWPYQECLFRQRWFVVGAGAIGCELLKNLSMMGVACGEGGLIKITDMDQIEISNLNRQFLFRRRD 487
Cdd:TIGR01408  395 FLPRGDRYDAQIAVFGDTFQQKLQNLNIFLVGCGAIGCEMLKNFALMGVGTGKKGMITVTDPDLIEKSNLNRQFLFRPHH 474
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  488 VGGKKSECAARAVTAFNSDVRIEALAERVGLETEHIFNDEFFGELNGVANALDNVDARRYMDRRCVYYRLPLLESGTMGT 567
Cdd:TIGR01408  475 IGKPKSYTAADATLKINPQIKIDAHQNRVGPETETIFNDEFYEKLDVVINALDNVEARRYVDSRCLAFLKPLLESGTLGT 554
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  568 KGNTQVVYPYLTESYSSSVDPPEKEIPVCTLKNFPNEIQHTIQWAREQFETFFAQPGEMANKFLSDERGFNEHVDKLISG 647
Cdd:TIGR01408  555 KGNTQVVVPHLTESYGSSRDPPEKEIPFCTLKSFPAAIEHTIQWARDKFEGLFSHKPSLVNKYLSSPSSAEEVLQKIQSG 634
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  648 QQIDILQKVKDALIDARPSSAEDCIRWARNQFQELYHNNIAQMLHSFPPDQLTDSGAKFWSGAKRCPHVLNFDPSKEEHF 727
Cdd:TIGR01408  635 HSREGLEQIIKLLSKEKPRNFSQCVEWARLKFEKYFNNKALQLLHCFPLDIRTSTGSPFWSSPKRPPSPLKFDLNEPLHL 714
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  728 NFVFAASILIAELYGVqPI----LDREEVIRVALSVNPEPFEPKSGVKIaVTDaeakeQNERGASSMIVDDDAAIEALKL 803
Cdd:TIGR01408  715 SFIQAAAKLYATVYGI-PFaeedLSADALLNILSEVKIPEFKPRSNKKI-QTD-----ETARKPDTAPIDDRNAIFQLEK 787
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  804 KL-ATLNVKSTSKLNCVDFEKDDDSNHHMEFITAASNLRAENYDILPADRMRTKQIAGKIIPAIATTTAAVAGLVCIELY 882
Cdd:TIGR01408  788 AIlSNEATKSDFRMAPLSFEKDDDHNGHIDFITAASNLRAKNYSIEPADRFKTKFIAGKIIPAIATSTATVSGLVCLELI 867
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  883 KVVDAngipKTPMERFKNTFLNLSMPFFSSAEPIGAPKKTYMDRE-FTLWDRIDVQGPLTLQEFIDNVQNQTgGCEVSML 961
Cdd:TIGR01408  868 KVTDG----GYKFEVYKNCFLNLAIPLFVFTEPTEVRKTKIRNGIsFTIWDRWTLHGDFTLLEFINAVKEKY-GLEPTMV 942
                          970       980       990      1000      1010      1020
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1972267130  962 SAGACLLFSFFMNagKKQERLKTEVKAVYEELLKKSLHPSVHALVLEPMMSDPDGEDVEVPYIRY 1026
Cdd:TIGR01408  943 SQGVKLLYVPVMP--GHAERLKLKMHKLVKPTTKKKLPPYRVHLTVSFACDDDGDEDVPGPPVRI 1005
 
Name Accession Description Interval E-value
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
18-1026 0e+00

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: 1003.64  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130   18 LDKNLYSRQIYTLGESAMVNLRTASVLISGLGSVGVEIAKNLILGGVRHVTIHDTKLAKWSDLSAQYYLRDADVGHNRAT 97
Cdd:TIGR01408    2 IDEALYSRQLYVLGDEAMQKMAKSNVLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLSSNFFLSEDDVGRNRAE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130   98 SCYERLAELNDSVNVQVSTDELTEEFVKTFDLVVLTDAARTAQRQIAAWTRAHNRRI--LITDARGVFSYIFNDFGDNFR 175
Cdd:TIGR01408   82 AVVKKLAELNPYVHVSSSSVPFNEEFLDKFQCVVLTEMSLPLQKEINDFCHSQCPPIafISADVRGLFGSLFCDFGDEFE 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  176 IDDATGEQVREFFIEHI-DKTTGEVTTLENLFHGLEDGDHVTFSEVKGLTEINGCEPLKITVKNASKFNIGDfAVSFSDY 254
Cdd:TIGR01408  162 VLDTDGEEPKTGFIASItQANPGIVTCLENHRHKLETGDFVTFREVNGMTGLNDGSPRKITVISPYSFSIGD-TTELGPY 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  255 KEGGRCRQVKVPTSVSHVPFEKSLVEPEFGIWDYAKFEYPSQLHALWTALYAFEEKYGRSPAPRSTQDAALLKEL---IP 331
Cdd:TIGR01408  241 LHGGIATQVKTPKTVFFKSLREQLKDPKCLIVDFSKPERPPEIHTAFQALDQFQEKYSRKPNVGCQQDAEELLKLatsIS 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  332 SGTE----EIPEKLIELFSFSASGNLVTVSSVVGGIAAQEAMKGVTHHMTPLKQWLHLDHVEVLPGDwtsfdnSKLSETD 407
Cdd:TIGR01408  321 ETLEekvpDVDAKLVHWLSWTAQGFLSPMAAAVGGVVSQEVLKAVTGKFSPLCQWFYFDSAESLPSL------GKPECEE 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  408 CQPRQSRYDGQAAVFGWPYQECLFRQRWFVVGAGAIGCELLKNLSMMGVACGEGGLIKITDMDQIEISNLNRQFLFRRRD 487
Cdd:TIGR01408  395 FLPRGDRYDAQIAVFGDTFQQKLQNLNIFLVGCGAIGCEMLKNFALMGVGTGKKGMITVTDPDLIEKSNLNRQFLFRPHH 474
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  488 VGGKKSECAARAVTAFNSDVRIEALAERVGLETEHIFNDEFFGELNGVANALDNVDARRYMDRRCVYYRLPLLESGTMGT 567
Cdd:TIGR01408  475 IGKPKSYTAADATLKINPQIKIDAHQNRVGPETETIFNDEFYEKLDVVINALDNVEARRYVDSRCLAFLKPLLESGTLGT 554
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  568 KGNTQVVYPYLTESYSSSVDPPEKEIPVCTLKNFPNEIQHTIQWAREQFETFFAQPGEMANKFLSDERGFNEHVDKLISG 647
Cdd:TIGR01408  555 KGNTQVVVPHLTESYGSSRDPPEKEIPFCTLKSFPAAIEHTIQWARDKFEGLFSHKPSLVNKYLSSPSSAEEVLQKIQSG 634
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  648 QQIDILQKVKDALIDARPSSAEDCIRWARNQFQELYHNNIAQMLHSFPPDQLTDSGAKFWSGAKRCPHVLNFDPSKEEHF 727
Cdd:TIGR01408  635 HSREGLEQIIKLLSKEKPRNFSQCVEWARLKFEKYFNNKALQLLHCFPLDIRTSTGSPFWSSPKRPPSPLKFDLNEPLHL 714
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  728 NFVFAASILIAELYGVqPI----LDREEVIRVALSVNPEPFEPKSGVKIaVTDaeakeQNERGASSMIVDDDAAIEALKL 803
Cdd:TIGR01408  715 SFIQAAAKLYATVYGI-PFaeedLSADALLNILSEVKIPEFKPRSNKKI-QTD-----ETARKPDTAPIDDRNAIFQLEK 787
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  804 KL-ATLNVKSTSKLNCVDFEKDDDSNHHMEFITAASNLRAENYDILPADRMRTKQIAGKIIPAIATTTAAVAGLVCIELY 882
Cdd:TIGR01408  788 AIlSNEATKSDFRMAPLSFEKDDDHNGHIDFITAASNLRAKNYSIEPADRFKTKFIAGKIIPAIATSTATVSGLVCLELI 867
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  883 KVVDAngipKTPMERFKNTFLNLSMPFFSSAEPIGAPKKTYMDRE-FTLWDRIDVQGPLTLQEFIDNVQNQTgGCEVSML 961
Cdd:TIGR01408  868 KVTDG----GYKFEVYKNCFLNLAIPLFVFTEPTEVRKTKIRNGIsFTIWDRWTLHGDFTLLEFINAVKEKY-GLEPTMV 942
                          970       980       990      1000      1010      1020
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1972267130  962 SAGACLLFSFFMNagKKQERLKTEVKAVYEELLKKSLHPSVHALVLEPMMSDPDGEDVEVPYIRY 1026
Cdd:TIGR01408  943 SQGVKLLYVPVMP--GHAERLKLKMHKLVKPTTKKKLPPYRVHLTVSFACDDDGDEDVPGPPVRI 1005
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
434-982 0e+00

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: 734.48  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  434 RWFVVGAGAIGCELLKNLSMMGVACGEGGLIKITDMDQIEISNLNRQFLFRRRDVGGKKSECAARAVTAFNSDVRIEALA 513
Cdd:cd01490      1 KVFLVGAGAIGCELLKNFALMGVGTGESGEITVTDMDNIEKSNLNRQFLFRPHDVGKPKSEVAAAAVKAMNPDLKITALQ 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  514 ERVGLETEHIFNDEFFGELNGVANALDNVDARRYMDRRCVYYRLPLLESGTMGTKGNTQVVYPYLTESYSSSVDPPEKEI 593
Cdd:cd01490     81 NRVGPETEHIFNDEFWEKLDGVANALDNVDARMYVDRRCVYYRKPLLESGTLGTKGNTQVVIPHLTESYSSSRDPPEKSI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  594 PVCTLKNFPNEIQHTIQWAREQFETFFAQPGEMANKFLsdergfnehvdklisgqqidilqkvkdalidarpssAEDCIR 673
Cdd:cd01490    161 PLCTLKNFPNAIEHTIQWARDEFEGLFKQPPENVNQYL------------------------------------FEDCVR 204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  674 WARNQFQELYHNNIAQMLHSFPPDQLTDSGAKFWSGAKRCPHVLNFDPSKEEHFNFVFAASILIAELYGVQPildreevi 753
Cdd:cd01490    205 WARLLFEKYFNNNIKQLLHNFPPDAVTSDGAPFWSGPKRCPTPLEFDVNNPLHLDFVLAAANLYAEVYGIPG-------- 276
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  754 rvalsvnpepfepksgvkiavtdaeakeqnergassmivdddaaiealklklatlnvkstsklncvdFEKDDDSNHHMEF 833
Cdd:cd01490    277 -------------------------------------------------------------------FEKDDDTNFHMDF 289
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  834 ITAASNLRAENYDILPADRMRTKQIAGKIIPAIATTTAAVAGLVCIELYKVVDANgipkTPMERFKNTFLNLSMPFFSSA 913
Cdd:cd01490    290 ITAASNLRARNYSIPPADRHKTKRIAGKIIPAIATTTAAVTGLVCLELYKVVDGK----RPLEAYKNAFLNLALPFFAFS 365
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  914 EPIGAPKKTY-MDREFTLWDRIDVQGPLTLQEFIDNVQNQTGGCEVSMLSAGACLLFSFFMNAGKKQERL 982
Cdd:cd01490    366 EPIPAPKVKYaYDEEWTIWDRFEVKGKQTLQELLIDYFKEKYGLEVTMLSQGVSMLYSSFMPPAKLKERL 435
UBA_E1_SCCH pfam10585
Ubiquitin-activating enzyme, SCCH domain; Ubiquitin-activating enzyme (E1 enzyme) activates ...
602-856 8.16e-121

Ubiquitin-activating enzyme, SCCH domain; Ubiquitin-activating enzyme (E1 enzyme) activates ubiquitin by first adenylating with ATP its C-terminal glycine residue and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding an ubiquitin-E1 thiolester and free AMP. Later the ubiquitin moiety is transferred to a cysteine residue on one of the many forms of ubiquitin-conjugating enzymes (E2). This domain carries the last of five conserved cysteines that is part of the active site of the enzyme, responsible for ubiquitin thiolester complex formation, the active site being represented by the sequence motif PICTLKNFP. The catalytic cysteine domain contains the E1 active site cysteine, and is divided in two half-domains, FCCH and SCCH, for 'first' and 'second' catalytic cysteine half-domain, respectively. This is the SCCH domain in which resides the catalytic cysteine.


Pssm-ID: 463157  Cd Length: 254  Bit Score: 369.64  E-value: 8.16e-121
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  602 PNEIQHTIQWAREQFETFFAQPGEMANKFLSDERGFNEHVDKLISGQQIDILQKVKDALIDARPSSAEDCIRWARNQFQE 681
Cdd:pfam10585    1 PNAIEHTIQWARDEFEGLFVQPPEEVNKYLQPPQNFIESLLKQGGGQKLETLESVRKSLVTERPKTFEDCVAWARLKFEK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  682 LYHNNIAQMLHSFPPDQLTDSGAKFWSGAKRCPHVLNFDPSKEEHFNFVFAASILIAELYGVQPILDREEVIRVALSVNP 761
Cdd:pfam10585   81 LFNNDIKQLLYNFPPDHKTSSGAPFWSGPKRPPTPLEFDPNNPLHLDFVVAAANLRAQVYGIPGSRDREAIAKVLSKVKV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  762 EPFEPKSGVKIAVTDAEAKEQNERGAssmivDDDAAIEALKLKLATLNVKSTS----KLNCVDFEKDDDSNHHMEFITAA 837
Cdd:pfam10585  161 PEFKPKSGVKIQVNDEEAADPNAESE-----DDEDELDELLEELPKLAVSPSSlagfRLNPIEFEKDDDTNFHIDFITAA 235
                          250
                   ....*....|....*....
gi 1972267130  838 SNLRAENYDILPADRMRTK 856
Cdd:pfam10585  236 SNLRARNYGIPPADRHKTK 254
UBA_e1_C smart00985
Ubiquitin-activating enzyme e1 C-terminal domain; This presumed domain found at the C terminus ...
898-1024 2.55e-52

Ubiquitin-activating enzyme e1 C-terminal domain; This presumed domain found at the C terminus of Ubiquitin-activating enzyme e1 proteins is functionally uncharacterised.


Pssm-ID: 214955  Cd Length: 128  Bit Score: 178.99  E-value: 2.55e-52
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130   898 FKNTFLNLSMPFFSSAEPIGAPKKTYMDR-EFTLWDRIDVQGP-LTLQEFIDNVQNQTGgCEVSMLSAGACLLFSFFMNA 975
Cdd:smart00985    1 YKNAFLNLALPFFAFSEPIAAPKTKYRDKdKWTLWDRLEVPGGdITLKELLDYFEEKYG-LEVTMLSQGVSLLYSSFMPP 79
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*....
gi 1972267130   976 GKKQERLKTEVKAVYEELLKKSLHPSVHALVLEPMMSDPDGEDVEVPYI 1024
Cdd:smart00985   80 KKHKERLDLPVTELVEQVTKKKLPPHVKYLVLEVSCEDEDDEDVEVPYI 128
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
414-596 3.49e-30

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: 119.85  E-value: 3.49e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  414 RYDGQAAV--FGWPYQECLFRQRWFVVGAGAIGCELLKNLSMMGVacgegGLIKITDMDQIEISNLNRQFLFRRRDVGGK 491
Cdd:COG0476      7 RYSRQILLpeIGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGV-----GTLTLVDDDVVELSNLQRQILYTEADVGRP 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  492 KSECAARAVTAFNSDVRIEALAERVgleTEHIFnDEFFGELNGVANALDNVDARRYMDRRCVYYRLPLLESGTMGTKGNT 571
Cdd:COG0476     82 KVEAAAERLRALNPDVEVEAIPERL---TEENA-LELLAGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIGFEGQV 157
                          170       180
                   ....*....|....*....|....*
gi 1972267130  572 QVVYPYLTESYSSSVDPPEKEIPVC 596
Cdd:COG0476    158 TVFIPGDTPCYRCLFPEPPEPGPSC 182
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
396-545 4.01e-17

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 84.55  E-value: 4.01e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  396 TSFDNSKLSETDCQ--PRQSRYDGqaavFGWPYQECLFRQRWFVVGAGAIGCELLKNLSMMGVacgegGLIKITDMDQIE 473
Cdd:PRK05600     7 TLSPFMQLPTSELRrtARQLALPG----FGIEQQERLHNARVLVIGAGGLGCPAMQSLASAGV-----GTITLIDDDTVD 77
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1972267130  474 ISNLNRQFLFRRRDVGGKKSECAARAVTAFNSDVRIEALAERVGLETEHifndEFFGELNGVANALDNVDAR 545
Cdd:PRK05600    78 VSNIHRQILFGASDVGRPKVEVAAERLKEIQPDIRVNALRERLTAENAV----ELLNGVDLVLDGSDSFATK 145
 
Name Accession Description Interval E-value
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
18-1026 0e+00

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: 1003.64  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130   18 LDKNLYSRQIYTLGESAMVNLRTASVLISGLGSVGVEIAKNLILGGVRHVTIHDTKLAKWSDLSAQYYLRDADVGHNRAT 97
Cdd:TIGR01408    2 IDEALYSRQLYVLGDEAMQKMAKSNVLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLSSNFFLSEDDVGRNRAE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130   98 SCYERLAELNDSVNVQVSTDELTEEFVKTFDLVVLTDAARTAQRQIAAWTRAHNRRI--LITDARGVFSYIFNDFGDNFR 175
Cdd:TIGR01408   82 AVVKKLAELNPYVHVSSSSVPFNEEFLDKFQCVVLTEMSLPLQKEINDFCHSQCPPIafISADVRGLFGSLFCDFGDEFE 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  176 IDDATGEQVREFFIEHI-DKTTGEVTTLENLFHGLEDGDHVTFSEVKGLTEINGCEPLKITVKNASKFNIGDfAVSFSDY 254
Cdd:TIGR01408  162 VLDTDGEEPKTGFIASItQANPGIVTCLENHRHKLETGDFVTFREVNGMTGLNDGSPRKITVISPYSFSIGD-TTELGPY 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  255 KEGGRCRQVKVPTSVSHVPFEKSLVEPEFGIWDYAKFEYPSQLHALWTALYAFEEKYGRSPAPRSTQDAALLKEL---IP 331
Cdd:TIGR01408  241 LHGGIATQVKTPKTVFFKSLREQLKDPKCLIVDFSKPERPPEIHTAFQALDQFQEKYSRKPNVGCQQDAEELLKLatsIS 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  332 SGTE----EIPEKLIELFSFSASGNLVTVSSVVGGIAAQEAMKGVTHHMTPLKQWLHLDHVEVLPGDwtsfdnSKLSETD 407
Cdd:TIGR01408  321 ETLEekvpDVDAKLVHWLSWTAQGFLSPMAAAVGGVVSQEVLKAVTGKFSPLCQWFYFDSAESLPSL------GKPECEE 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  408 CQPRQSRYDGQAAVFGWPYQECLFRQRWFVVGAGAIGCELLKNLSMMGVACGEGGLIKITDMDQIEISNLNRQFLFRRRD 487
Cdd:TIGR01408  395 FLPRGDRYDAQIAVFGDTFQQKLQNLNIFLVGCGAIGCEMLKNFALMGVGTGKKGMITVTDPDLIEKSNLNRQFLFRPHH 474
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  488 VGGKKSECAARAVTAFNSDVRIEALAERVGLETEHIFNDEFFGELNGVANALDNVDARRYMDRRCVYYRLPLLESGTMGT 567
Cdd:TIGR01408  475 IGKPKSYTAADATLKINPQIKIDAHQNRVGPETETIFNDEFYEKLDVVINALDNVEARRYVDSRCLAFLKPLLESGTLGT 554
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  568 KGNTQVVYPYLTESYSSSVDPPEKEIPVCTLKNFPNEIQHTIQWAREQFETFFAQPGEMANKFLSDERGFNEHVDKLISG 647
Cdd:TIGR01408  555 KGNTQVVVPHLTESYGSSRDPPEKEIPFCTLKSFPAAIEHTIQWARDKFEGLFSHKPSLVNKYLSSPSSAEEVLQKIQSG 634
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  648 QQIDILQKVKDALIDARPSSAEDCIRWARNQFQELYHNNIAQMLHSFPPDQLTDSGAKFWSGAKRCPHVLNFDPSKEEHF 727
Cdd:TIGR01408  635 HSREGLEQIIKLLSKEKPRNFSQCVEWARLKFEKYFNNKALQLLHCFPLDIRTSTGSPFWSSPKRPPSPLKFDLNEPLHL 714
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  728 NFVFAASILIAELYGVqPI----LDREEVIRVALSVNPEPFEPKSGVKIaVTDaeakeQNERGASSMIVDDDAAIEALKL 803
Cdd:TIGR01408  715 SFIQAAAKLYATVYGI-PFaeedLSADALLNILSEVKIPEFKPRSNKKI-QTD-----ETARKPDTAPIDDRNAIFQLEK 787
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  804 KL-ATLNVKSTSKLNCVDFEKDDDSNHHMEFITAASNLRAENYDILPADRMRTKQIAGKIIPAIATTTAAVAGLVCIELY 882
Cdd:TIGR01408  788 AIlSNEATKSDFRMAPLSFEKDDDHNGHIDFITAASNLRAKNYSIEPADRFKTKFIAGKIIPAIATSTATVSGLVCLELI 867
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  883 KVVDAngipKTPMERFKNTFLNLSMPFFSSAEPIGAPKKTYMDRE-FTLWDRIDVQGPLTLQEFIDNVQNQTgGCEVSML 961
Cdd:TIGR01408  868 KVTDG----GYKFEVYKNCFLNLAIPLFVFTEPTEVRKTKIRNGIsFTIWDRWTLHGDFTLLEFINAVKEKY-GLEPTMV 942
                          970       980       990      1000      1010      1020
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1972267130  962 SAGACLLFSFFMNagKKQERLKTEVKAVYEELLKKSLHPSVHALVLEPMMSDPDGEDVEVPYIRY 1026
Cdd:TIGR01408  943 SQGVKLLYVPVMP--GHAERLKLKMHKLVKPTTKKKLPPYRVHLTVSFACDDDGDEDVPGPPVRI 1005
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
434-982 0e+00

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: 734.48  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  434 RWFVVGAGAIGCELLKNLSMMGVACGEGGLIKITDMDQIEISNLNRQFLFRRRDVGGKKSECAARAVTAFNSDVRIEALA 513
Cdd:cd01490      1 KVFLVGAGAIGCELLKNFALMGVGTGESGEITVTDMDNIEKSNLNRQFLFRPHDVGKPKSEVAAAAVKAMNPDLKITALQ 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  514 ERVGLETEHIFNDEFFGELNGVANALDNVDARRYMDRRCVYYRLPLLESGTMGTKGNTQVVYPYLTESYSSSVDPPEKEI 593
Cdd:cd01490     81 NRVGPETEHIFNDEFWEKLDGVANALDNVDARMYVDRRCVYYRKPLLESGTLGTKGNTQVVIPHLTESYSSSRDPPEKSI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  594 PVCTLKNFPNEIQHTIQWAREQFETFFAQPGEMANKFLsdergfnehvdklisgqqidilqkvkdalidarpssAEDCIR 673
Cdd:cd01490    161 PLCTLKNFPNAIEHTIQWARDEFEGLFKQPPENVNQYL------------------------------------FEDCVR 204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  674 WARNQFQELYHNNIAQMLHSFPPDQLTDSGAKFWSGAKRCPHVLNFDPSKEEHFNFVFAASILIAELYGVQPildreevi 753
Cdd:cd01490    205 WARLLFEKYFNNNIKQLLHNFPPDAVTSDGAPFWSGPKRCPTPLEFDVNNPLHLDFVLAAANLYAEVYGIPG-------- 276
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  754 rvalsvnpepfepksgvkiavtdaeakeqnergassmivdddaaiealklklatlnvkstsklncvdFEKDDDSNHHMEF 833
Cdd:cd01490    277 -------------------------------------------------------------------FEKDDDTNFHMDF 289
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  834 ITAASNLRAENYDILPADRMRTKQIAGKIIPAIATTTAAVAGLVCIELYKVVDANgipkTPMERFKNTFLNLSMPFFSSA 913
Cdd:cd01490    290 ITAASNLRARNYSIPPADRHKTKRIAGKIIPAIATTTAAVTGLVCLELYKVVDGK----RPLEAYKNAFLNLALPFFAFS 365
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  914 EPIGAPKKTY-MDREFTLWDRIDVQGPLTLQEFIDNVQNQTGGCEVSMLSAGACLLFSFFMNAGKKQERL 982
Cdd:cd01490    366 EPIPAPKVKYaYDEEWTIWDRFEVKGKQTLQELLIDYFKEKYGLEVTMLSQGVSMLYSSFMPPAKLKERL 435
Ube1_repeat1 cd01491
Ubiquitin activating enzyme (E1), repeat 1. E1, a highly conserved small protein present ...
22-395 4.53e-138

Ubiquitin activating enzyme (E1), repeat 1. 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 first repeat of Ub-E1.


Pssm-ID: 238768 [Multi-domain]  Cd Length: 286  Bit Score: 416.28  E-value: 4.53e-138
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130   22 LYSRQIYTLGESAMVNLRTASVLISGLGSVGVEIAKNLILGGVRHVTIHDTKLAKWSDLSAQYYLRDADVGHNRATSCYE 101
Cdd:cd01491      1 LYSRQLYVLGHEAMKKLQKSNVLISGLGGLGVEIAKNLILAGVKSVTLHDTKPCSWSDLSSQFYLREEDIGKNRAEASQA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  102 RLAELNDSVNVQVSTDELTEEFVKTFDLVVLTDAARTAQRQIAAWTRAHNRRILITDARGVFSYIFNDFGDNFRIDDATG 181
Cdd:cd01491     81 RLAELNPYVPVTVSTGPLTTDELLKFQVVVLTDASLEDQLKINEFCHSPGIKFISADTRGLFGSIFCDFGDEFTVYDPNG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  182 EQVREFFIEHIDK-TTGEVTTLENLFHGLEDGDHVTFSEVKGLTEINGCEPLKITVKNASKFNIGDfAVSFSDYKEGGRC 260
Cdd:cd01491    161 EEPKSGMISSISKdNPGVVTCLDETRHGFEDGDYVTFSEVEGMTELNGCEPRKIKVKGPYTFSIGD-TSSFSEYIRGGIV 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  261 RQVKvptsvshvpfekslvepefgiwdyakfeypsqlhalwtalyafeekygrspaprstqdaallkelipsgteeipek 340
Cdd:cd01491    240 TQVK---------------------------------------------------------------------------- 243
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1972267130  341 lielfsfsasgnLVTVSSVVGGIAAQEAMKGVTHHMTPLKQWLHLDHVEVLPGDW 395
Cdd:cd01491    244 ------------LSPMAAFFGGLAAQEVLKACSGKFTPLKQWLYFDALECLPEDE 286
UBA_E1_SCCH pfam10585
Ubiquitin-activating enzyme, SCCH domain; Ubiquitin-activating enzyme (E1 enzyme) activates ...
602-856 8.16e-121

Ubiquitin-activating enzyme, SCCH domain; Ubiquitin-activating enzyme (E1 enzyme) activates ubiquitin by first adenylating with ATP its C-terminal glycine residue and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding an ubiquitin-E1 thiolester and free AMP. Later the ubiquitin moiety is transferred to a cysteine residue on one of the many forms of ubiquitin-conjugating enzymes (E2). This domain carries the last of five conserved cysteines that is part of the active site of the enzyme, responsible for ubiquitin thiolester complex formation, the active site being represented by the sequence motif PICTLKNFP. The catalytic cysteine domain contains the E1 active site cysteine, and is divided in two half-domains, FCCH and SCCH, for 'first' and 'second' catalytic cysteine half-domain, respectively. This is the SCCH domain in which resides the catalytic cysteine.


Pssm-ID: 463157  Cd Length: 254  Bit Score: 369.64  E-value: 8.16e-121
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  602 PNEIQHTIQWAREQFETFFAQPGEMANKFLSDERGFNEHVDKLISGQQIDILQKVKDALIDARPSSAEDCIRWARNQFQE 681
Cdd:pfam10585    1 PNAIEHTIQWARDEFEGLFVQPPEEVNKYLQPPQNFIESLLKQGGGQKLETLESVRKSLVTERPKTFEDCVAWARLKFEK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  682 LYHNNIAQMLHSFPPDQLTDSGAKFWSGAKRCPHVLNFDPSKEEHFNFVFAASILIAELYGVQPILDREEVIRVALSVNP 761
Cdd:pfam10585   81 LFNNDIKQLLYNFPPDHKTSSGAPFWSGPKRPPTPLEFDPNNPLHLDFVVAAANLRAQVYGIPGSRDREAIAKVLSKVKV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  762 EPFEPKSGVKIAVTDAEAKEQNERGAssmivDDDAAIEALKLKLATLNVKSTS----KLNCVDFEKDDDSNHHMEFITAA 837
Cdd:pfam10585  161 PEFKPKSGVKIQVNDEEAADPNAESE-----DDEDELDELLEELPKLAVSPSSlagfRLNPIEFEKDDDTNFHIDFITAA 235
                          250
                   ....*....|....*....
gi 1972267130  838 SNLRAENYDILPADRMRTK 856
Cdd:pfam10585  236 SNLRARNYGIPPADRHKTK 254
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
434-617 1.70e-72

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: 239.79  E-value: 1.70e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  434 RWFVVGAGAIGCELLKNLSMMGVacgegGLIKITDMDQIEISNLNRQFLFRRRDVGGKKSECAARAVTAFNSDVRIEALA 513
Cdd:cd01484      1 KVLLVGAGGIGCELLKNLALMGF-----GQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKSEVAAEAVNDRNPNCKVVPYQ 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  514 ERVGleTEHIFNDEFFGELNGVANALDNVDARRYMDRRCVYYRLPLLESGTMGTKGNTQVVYPYLTESYSSSVDPPEKEI 593
Cdd:cd01484     76 NKVG--PEQDFNDTFFEQFHIIVNALDNIIARRYVNGMLIFLIVPLIESGTEGFKGNAQVILPGMTECIECTLYPPQKNF 153
                          170       180
                   ....*....|....*....|....
gi 1972267130  594 PVCTLKNFPNEIQHTIQWAREQFE 617
Cdd:cd01484    154 PMCTIASMPRLPEHCIEWARMLQW 177
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
415-601 3.66e-60

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: 205.57  E-value: 3.66e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  415 YDGQAAVFGWPY--QECLFRQRWFVVGAGAIGCELLKNLSMMGVacgegGLIKITDMDQIEISNLNRQFLFRRRDVGGKK 492
Cdd:pfam00899    1 YSRQLALPLIGEdgQEKLRNSRVLIVGAGGLGSEAAKYLARAGV-----GKITLVDFDTVELSNLNRQFLFREADIGKPK 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  493 SECAARAVTAFNSDVRIEALAERVGLETehifNDEFFGELNGVANALDNVDARRYMDRRCVYYRLPLLESGTMGTKGNTQ 572
Cdd:pfam00899   76 AEVAAERLREINPDVEVEAYTERLTPEN----AEELIKSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVT 151
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1972267130  573 VVYPYLTESYS--SSVDPPEKEIPVCTLKNF 601
Cdd:pfam00899  152 VVIPGKTPCYRclFPEDPPPKLVPSCTVAGV 182
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
434-619 1.14e-55

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: 195.68  E-value: 1.14e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  434 RWFVVGAGAIGCELLKNLSMMGVacgegGLIKITDMDQIEISNLNRQFLFRRRDVGGKKSECAARAVTAFNSDVRIEALA 513
Cdd:cd01489      1 KVLVVGAGGIGCELLKNLVLTGF-----GEIHIIDLDTIDLSNLNRQFLFRKKHVGKSKAQVAKEAVLSFNPNVKIVAYH 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  514 ERVgleTEHIFNDEFFGELNGVANALDNVDARRYMDRRCVYYRLPLLESGTMGTKGNTQVVYPYLTESYSSSVDPPEKEI 593
Cdd:cd01489     76 ANI---KDPDFNVEFFKQFDLVFNALDNLAARRHVNKMCLAADVPLIESGTTGFLGQVQVIKKGKTECYECQPKETPKTF 152
                          170       180
                   ....*....|....*....|....*.
gi 1972267130  594 PVCTLKNFPNEIQHTIQWAREQFETF 619
Cdd:cd01489    153 PVCTIRSTPSQPIHCIVWAKSLFFLF 178
UBA_e1_C smart00985
Ubiquitin-activating enzyme e1 C-terminal domain; This presumed domain found at the C terminus ...
898-1024 2.55e-52

Ubiquitin-activating enzyme e1 C-terminal domain; This presumed domain found at the C terminus of Ubiquitin-activating enzyme e1 proteins is functionally uncharacterised.


Pssm-ID: 214955  Cd Length: 128  Bit Score: 178.99  E-value: 2.55e-52
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130   898 FKNTFLNLSMPFFSSAEPIGAPKKTYMDR-EFTLWDRIDVQGP-LTLQEFIDNVQNQTGgCEVSMLSAGACLLFSFFMNA 975
Cdd:smart00985    1 YKNAFLNLALPFFAFSEPIAAPKTKYRDKdKWTLWDRLEVPGGdITLKELLDYFEEKYG-LEVTMLSQGVSLLYSSFMPP 79
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*....
gi 1972267130   976 GKKQERLKTEVKAVYEELLKKSLHPSVHALVLEPMMSDPDGEDVEVPYI 1024
Cdd:smart00985   80 KKHKERLDLPVTELVEQVTKKKLPPHVKYLVLEVSCEDEDDEDVEVPYI 128
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
437-613 5.84e-41

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: 152.51  E-value: 5.84e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  437 VVGAGAIGCELLKNLSMMGVacgegGLIKITDMDQIEISNLNRQFLFRRRDVGGKKSECAARAVTAFNSDVRIEALAERv 516
Cdd:cd01488      4 VIGAGGLGCELLKNLALSGF-----RNIHVIDMDTIDVSNLNRQFLFREKDIGKPKAEVAAKFVNDRVPGVNVTPHFGK- 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  517 gLETehiFNDEFFGELNGVANALDNVDARRYMDRRCVYYRL--------PLLESGTMGTKGNTQVVYPYLTESYSSSVD- 587
Cdd:cd01488     78 -IQD---KDEEFYRQFNIIICGLDSIEARRWINGTLVSLLLyedpesiiPLIDGGTEGFKGHARVILPGITACIECSLDl 153
                          170       180
                   ....*....|....*....|....*..
gi 1972267130  588 -PPEKEIPVCTLKNFPNEIQHTIQWAR 613
Cdd:cd01488    154 fPPQVTFPLCTIANTPRLPEHCIEYAS 180
E1-1_like cd01485
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ...
22-170 5.33e-38

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: 141.02  E-value: 5.33e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130   22 LYSRQIYTLGESAMVNLRTASVLISGLGSVGVEIAKNLILGGVRHVTIHDTKLAKWSDLSAQYYLR--DADVGHNRATSC 99
Cdd:cd01485      1 LYDRQIRLWGDEAQNKLRSAKVLIIGAGALGAEIAKNLVLAGIDSITIVDHRLVSTEDLGSNFFLDaeVSNSGMNRAAAS 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1972267130  100 YERLAELNDSVNVQV------STDELTEEFVKTFDLVVLTDAARTAQRQIAAWTRAHNRRILITDARGVFSYIFNDF 170
Cdd:cd01485     81 YEFLQELNPNVKLSIveedslSNDSNIEEYLQKFTLVIATEENYERTAKVNDVCRKHHIPFISCATYGLIGYAFFDF 157
Aos1_SUMO cd01492
Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating ...
22-169 1.45e-36

Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 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. Aos1 contains part of the adenylation domain.


Pssm-ID: 238769 [Multi-domain]  Cd Length: 197  Bit Score: 136.65  E-value: 1.45e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130   22 LYSRQIYTLGESAMVNLRTASVLISGLGSVGVEIAKNLILGGVRHVTIHDTKLAKWSDLSAQYYLRDADVGHNRATSCYE 101
Cdd:cd01492      3 LYDRQIRLWGLEAQKRLRSARILLIGLKGLGAEIAKNLVLSGIGSLTILDDRTVTEEDLGAQFLIPAEDLGQNRAEASLE 82
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1972267130  102 RLAELNDSVNVQVSTD---ELTEEFVKTFDLVVLTDAARTAQRQIAAWTRAHNRRILITDARGVFSYIFND 169
Cdd:cd01492     83 RLRALNPRVKVSVDTDdisEKPEEFFSQFDVVVATELSRAELVKINELCRKLGVKFYATGVHGLFGFVFAD 153
E1_UFD pfam09358
Ubiquitin fold domain; The ubiquitin fold domain is found at the C-terminus of ...
931-1024 8.76e-36

Ubiquitin fold domain; The ubiquitin fold domain is found at the C-terminus of ubiquitin-activating E1 family enzymes. This domain binds to E2 enzymes.


Pssm-ID: 462768  Cd Length: 93  Bit Score: 130.74  E-value: 8.76e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  931 WDRIDVQGPLTLQEFIDNVQNQTGgCEVSMLSAGACLLFSFFMNAGKKQERLKTEVKAVYEELLKKSLHPSVHALVLEPM 1010
Cdd:pfam09358    1 WDRFEVEGDMTLQELLDYFKEKYG-LEVTMLSYGVSLLYSSFMPPKKHKERLPMKISELVEEVSKKPIPPHQKYLVLEVS 79
                           90
                   ....*....|....
gi 1972267130 1011 MSDPDGEDVEVPYI 1024
Cdd:pfam09358   80 CEDEDGEDVEVPYV 93
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
436-574 3.35e-32

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: 122.38  E-value: 3.35e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  436 FVVGAGAIGCELLKNLSMMGVacgegGLIKITDMDQIEISNLNRQFLFRRRDVGGKKSECAARAVTAFNSDVRIEALAER 515
Cdd:cd01483      3 LLVGLGGLGSEIALNLARSGV-----GKITLIDFDTVELSNLNRQFLARQADIGKPKAEVAARRLNELNPGVNVTAVPEG 77
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1972267130  516 VGLETEhifnDEFFGELNGVANALDNVDARRYMDRRCVYYRLPLLESGTMGTKGNTQVV 574
Cdd:cd01483     78 ISEDNL----DDFLDGVDLVIDAIDNIAVRRALNRACKELGIPVIDAGGLGLGGDIQVI 132
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
414-596 6.73e-32

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: 124.51  E-value: 6.73e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  414 RYDGQAAV--FGWPYQECLFRQRWFVVGAGAIGCELLKNLSMMGVacgegGLIKITDMDQIEISNLNRQFLFRRRDVGGK 491
Cdd:cd00757      1 RYSRQILLpeIGEEGQEKLKNARVLVVGAGGLGSPAAEYLAAAGV-----GKLGLVDDDVVELSNLQRQILHTEADVGQP 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  492 KSECAARAVTAFNSDVRIEALAERVGLETEHifndEFFGELNGVANALDNVDARRYMDRRCVYYRLPLLESGTMGTKGNT 571
Cdd:cd00757     76 KAEAAAERLRAINPDVEIEAYNERLDAENAE----ELIAGYDLVLDCTDNFATRYLINDACVKLGKPLVSGAVLGFEGQV 151
                          170       180
                   ....*....|....*....|....*.
gi 1972267130  572 QVVYPYLTESYSSSV-DPPEKEIPVC 596
Cdd:cd00757    152 TVFIPGEGPCYRCLFpEPPPPGVPSC 177
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
414-596 3.49e-30

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: 119.85  E-value: 3.49e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  414 RYDGQAAV--FGWPYQECLFRQRWFVVGAGAIGCELLKNLSMMGVacgegGLIKITDMDQIEISNLNRQFLFRRRDVGGK 491
Cdd:COG0476      7 RYSRQILLpeIGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGV-----GTLTLVDDDVVELSNLQRQILYTEADVGRP 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  492 KSECAARAVTAFNSDVRIEALAERVgleTEHIFnDEFFGELNGVANALDNVDARRYMDRRCVYYRLPLLESGTMGTKGNT 571
Cdd:COG0476     82 KVEAAAERLRALNPDVEVEAIPERL---TEENA-LELLAGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIGFEGQV 157
                          170       180
                   ....*....|....*....|....*
gi 1972267130  572 QVVYPYLTESYSSSVDPPEKEIPVC 596
Cdd:COG0476    158 TVFIPGDTPCYRCLFPEPPEPGPSC 182
E1_FCCH pfam16190
Ubiquitin-activating enzyme E1 FCCH domain; This domain is found in the ubiquitin-activating ...
197-264 5.91e-29

Ubiquitin-activating enzyme E1 FCCH domain; This domain is found in the ubiquitin-activating E1 family enzymes.


Pssm-ID: 465054 [Multi-domain]  Cd Length: 70  Bit Score: 110.27  E-value: 5.91e-29
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1972267130  197 GEVTTLENLFHGLEDGDHVTFSEVKGLTEINGCEPLKITVKNASKFNIGDFAvSFSDYKEGGRCRQVK 264
Cdd:pfam16190    4 GVVTCLDDTRHGLEDGDYVTFSEVEGMTELNGCEPRKIKVLGPYTFSIGDTS-SFSPYLRGGIVTQVK 70
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
23-154 7.94e-26

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: 107.34  E-value: 7.94e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130   23 YSRQIY--TLGESAMVNLRTASVLISGLGSVGVEIAKNLILGGVRHVTIHDTKLAKWSDLSAQYYLRDADVGHNRATSCY 100
Cdd:pfam00899    1 YSRQLAlpLIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAA 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1972267130  101 ERLAELNDSVNVQVSTDELT----EEFVKTFDLVVLTDAARTAQRQIAAwtRAHNRRI 154
Cdd:pfam00899   81 ERLREINPDVEVEAYTERLTpenaEELIKSFDIVVDATDNFAARYLVND--ACVKLGK 136
APPBP1_RUB cd01493
Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric ...
23-379 1.76e-23

Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 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. ABPP1 contains part of the adenylation domain.


Pssm-ID: 238770 [Multi-domain]  Cd Length: 425  Bit Score: 104.69  E-value: 1.76e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130   23 YSRQIYTLGESAMVNLRTASVLISGLGSVGVEIAKNLILGGVRHVTIHDTKLAKWSDLSAQYYLRDADVGHNRATSCYER 102
Cdd:cd01493      3 YDRQLRLWGEHGQAALESAHVCLLNATATGTEILKNLVLPGIGSFTIVDGSKVDEEDLGNNFFLDASSLGKSRAEATCEL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  103 LAELNDSVN---VQVSTDELTE---EFVKTFDLVVLTDAARTAQRQIAAWTRAHNRRILITDARGVFSYI---FNDFG-- 171
Cdd:cd01493     83 LQELNPDVNgsaVEESPEALLDndpSFFSQFTVVIATNLPESTLLRLADVLWSANIPLLYVRSYGLYGYIriqLKEHTiv 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  172 ----DNFRID---DATGEQVREfFIEHID------KTTGEVTTLENLFHGLEdgdhvtfsevKGLTEINGCEPLKITVKN 238
Cdd:cd01493    163 eshpDNALEDlrlDNPFPELRE-HADSIDlddmdpAEHSHTPYIVILIKYLE----------KWRSAHNGQLPSTYKEKK 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  239 ASKFNIGDFAVSFSD---YKEGGR-CRQVKVPTSVShvpfeKSLvepefgiwdYAKFEYP------SQLHALWTALYAFE 308
Cdd:cd01493    232 EFRDLVRSLMRSNEDeenFEEAIKaVNKALNRTKIP-----SSV---------EEIFNDDrcenltSQSSSFWIMARALK 297
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  309 EKY----GRSPAP----------------------RSTQDAA--------LLKELIPSGtEEIPEKLIELFSFSASGNLV 354
Cdd:cd01493    298 EFVaeenGLLPLPgtlpdmtadtekyiklqniyreKAEKDAAevekyvreILKSLGRSP-DSISDKEIKLFCKNAAFLRV 376
                          410       420       430
                   ....*....|....*....|....*....|...
gi 1972267130  355 --------TVSSVVGGIAAQEAMKGVTHHMTPL 379
Cdd:cd01493    377 irgrslehNISAFMGGIAAQEVIKLITKQYVPI 409
E1_4HB pfam16191
Ubiquitin-activating enzyme E1 four-helix bundle; This domain is found in the ...
265-329 1.59e-21

Ubiquitin-activating enzyme E1 four-helix bundle; This domain is found in the ubiquitin-activating E1 family enzymes.


Pssm-ID: 465055  Cd Length: 70  Bit Score: 89.05  E-value: 1.59e-21
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1972267130  265 VPTSVSHVPFEKSLVEPEFGIWDYAKFEYPSQLHALWTALYAFEEKYGRSPAPRSTQDAALLKEL 329
Cdd:pfam16191    1 MPKTLSFKSLEESLKEPEFLISDFAKFDRPAQLHLAFQALHAFQEKHGRLPRPWNEEDAEEVVKL 65
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
43-170 1.81e-17

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: 80.00  E-value: 1.81e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130   43 VLISGLGSVGVEIAKNLILGGVRHVTIHDTKLAKWSDLSAQYYLRDADVGHNRATSCYERLAELNDSVNVQV----STDE 118
Cdd:cd01483      2 VLLVGLGGLGSEIALNLARSGVGKITLIDFDTVELSNLNRQFLARQADIGKPKAEVAARRLNELNPGVNVTAvpegISED 81
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1972267130  119 LTEEFVKTFDLVVLTDAARTAQRQIAAWTRAHNRRILITDARGVFSYIFNDF 170
Cdd:cd01483     82 NLDDFLDGVDLVIDAIDNIAVRRALNRACKELGIPVIDAGGLGLGGDIQVID 133
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
396-545 4.01e-17

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 84.55  E-value: 4.01e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  396 TSFDNSKLSETDCQ--PRQSRYDGqaavFGWPYQECLFRQRWFVVGAGAIGCELLKNLSMMGVacgegGLIKITDMDQIE 473
Cdd:PRK05600     7 TLSPFMQLPTSELRrtARQLALPG----FGIEQQERLHNARVLVIGAGGLGCPAMQSLASAGV-----GTITLIDDDTVD 77
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1972267130  474 ISNLNRQFLFRRRDVGGKKSECAARAVTAFNSDVRIEALAERVGLETEHifndEFFGELNGVANALDNVDAR 545
Cdd:PRK05600    78 VSNIHRQILFGASDVGRPKVEVAAERLKEIQPDIRVNALRERLTAENAV----ELLNGVDLVLDGSDSFATK 145
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
422-566 5.08e-15

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 76.04  E-value: 5.08e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  422 FGWPYQECLFRQRWFVVGAGAIGCELLKNLSMMGVacgegGLIKITDMDQIEISNLNRQFLFRRRDVGGKKSECAARAVT 501
Cdd:PRK05690    22 FDFDGQEKLKAARVLVVGLGGLGCAASQYLAAAGV-----GTLTLVDFDTVSLSNLQRQVLHDDATIGQPKVESARAALA 96
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1972267130  502 AFNSDVRIEALAERvgLETEHIfnDEFFGELNGVANALDNVDARRYMDRRCVYYRLPLLeSGTMG 566
Cdd:PRK05690    97 RINPHIAIETINAR--LDDDEL--AALIAGHDLVLDCTDNVATRNQLNRACFAAKKPLV-SGAAI 156
PRK08328 PRK08328
hypothetical protein; Provisional
414-581 7.72e-15

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 75.22  E-value: 7.72e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  414 RYDGQAAVFGWPYQECLFRQRWFVVGAGAIGCELLKNLSMMGVacgegGLIKITDMDQIEISNLNRQFLFRRRDVGGK-K 492
Cdd:PRK08328     9 RYDRQIMIFGVEGQEKLKKAKVAVVGVGGLGSPVAYYLAAAGV-----GRILLIDEQTPELSNLNRQILHWEEDLGKNpK 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  493 SECAARAVTAFNSDVRIEALAERvgLETEHIfnDEFFGELNGVANALDNVDARRYMDRRCVYYRLPLLESGTMGTKGNTQ 572
Cdd:PRK08328    84 PLSAKWKLERFNSDIKIETFVGR--LSEENI--DEVLKGVDVIVDCLDNFETRYLLDDYAHKKGIPLVHGAVEGTYGQVT 159

                   ....*....
gi 1972267130  573 VVYPYLTES 581
Cdd:PRK08328   160 TIVPGKTKR 168
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
427-576 9.86e-15

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 76.57  E-value: 9.86e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  427 QECLFRQRWFVVGAGAIGCELLKNLSMMGVacgegGLIKITDMDQIEISNLNRQFLFRRRDVggkkSECAARAVTA---- 502
Cdd:PRK07688    19 QQKLREKHVLIIGAGALGTANAEMLVRAGV-----GKVTIVDRDYVEWSNLQRQQLYTESDV----KNNLPKAVAAkkrl 89
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1972267130  503 --FNSDVRIEALAERVGleTEHIfnDEFFGELNGVANALDNVDARRYMDRRCVYYRLPLLESGTMGTKGNTQVVYP 576
Cdd:PRK07688    90 eeINSDVRVEAIVQDVT--AEEL--EELVTGVDLIIDATDNFETRFIVNDAAQKYGIPWIYGACVGSYGLSYTIIP 161
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
427-559 3.43e-13

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 72.35  E-value: 3.43e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  427 QECLFRQRWFVVGAGAIGCELLKNLSMMGVacgegGLIKITDMDQIEISNLNRQFLFRRRDVGGKKSECAARAVTAFNSD 506
Cdd:PRK08762   130 QRRLLEARVLLIGAGGLGSPAALYLAAAGV-----GTLGIVDHDVVDRSNLQRQILHTEDRVGQPKVDSAAQRLAALNPD 204
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1972267130  507 VRIEALAERvgLETEHIfnDEFFGELNGVANALDNVDARRYMDRRCVYYRLPL 559
Cdd:PRK08762   205 VQVEAVQER--VTSDNV--EALLQDVDVVVDGADNFPTRYLLNDACVKLGKPL 253
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
23-136 7.96e-13

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: 69.39  E-value: 7.96e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130   23 YSRQI--YTLGESAMVNLRTASVLISGLGSVGVEIAKNLILGGVRHVTI--HDTklAKWSDLSAQYYLRDADVGHNRATS 98
Cdd:COG0476      8 YSRQIllPEIGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLvdDDV--VELSNLQRQILYTEADVGRPKVEA 85
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1972267130   99 CYERLAELNDSVNVQVSTDELTE----EFVKTFDLVVltDAA 136
Cdd:COG0476     86 AAERLRALNPDVEVEAIPERLTEenalELLAGADLVL--DCT 125
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
430-573 2.09e-12

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: 68.02  E-value: 2.09e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  430 LFRQRWFVVGAGAIGCELLKNLSMMGVacgegGLIKITDMDQIEISNLNRQFLFRRRDVGGKKSECAARAVTAFNSDVRI 509
Cdd:cd00755      9 LRNAHVAVVGLGGVGSWAAEALARSGV-----GKLTLIDFDVVCVSNLNRQIHALLSTVGKPKVEVMAERIRDINPECEV 83
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1972267130  510 EALAERVGLETEHifnDEFFGELNGVANALDNVDARRYMDRRCVYYRLPLLESGTMGTKGN-TQV 573
Cdd:cd00755     84 DAVEEFLTPDNSE---DLLGGDPDFVVDAIDSIRAKVALIAYCRKRKIPVISSMGAGGKLDpTRI 145
E1_ThiF_like cd01487
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ...
437-548 4.48e-12

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: 65.48  E-value: 4.48e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  437 VVGAGAIGCELLKNLSMMGVacgegGLIKITDMDQIEISNLNRQFlFRRRDVGGKKSECAARAVTAFNSDVRIEALAERV 516
Cdd:cd01487      4 IAGAGGLGSNIAVLLARSGV-----GNLKLVDFDVVEPSNLNRQQ-YFLSQIGEPKVEALKENLREINPFVKIEAINIKI 77
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1972267130  517 GLETehifNDEFFGELNGVANALDNVDARRYM 548
Cdd:cd01487     78 DENN----LEGLFGDCDIVVEAFDNAETKAML 105
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
413-515 2.45e-11

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 66.43  E-value: 2.45e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  413 SRYDGQAAVFGW--PYQECLFRQRWFVVGAGAIGCELLKNLSMMGVacgegGLIKITDMDQIEISNLNRQFLFRRRDVGG 490
Cdd:PRK05597     7 ARYRRQIMLGEIgqQGQQSLFDAKVAVIGAGGLGSPALLYLAGAGV-----GHITIIDDDTVDLSNLHRQVIHSTAGVGQ 81
                           90       100
                   ....*....|....*....|....*
gi 1972267130  491 KKSECAARAVTAFNSDVRIEALAER 515
Cdd:PRK05597    82 PKAESAREAMLALNPDVKVTVSVRR 106
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
411-602 4.15e-10

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 62.44  E-value: 4.15e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  411 RQSRYDGqaavFGWPYQECLFRQRWFVVGAGAIGCELLKNLSMMGVacgegGLIKITDMDQIEISNLNRQFLFRRRDVGG 490
Cdd:PRK12475     7 RQILFSG----IGEEGQRKIREKHVLIVGAGALGAANAEALVRAGI-----GKLTIADRDYVEWSNLQRQQLYTEEDAKQ 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  491 KKSECAARA--VTAFNSDVRIEALAERVGLETEhifnDEFFGELNGVANALDNVDARRYMDRRCVYYRLPLLESGTMGTK 568
Cdd:PRK12475    78 KKPKAIAAKehLRKINSEVEIVPVVTDVTVEEL----EELVKEVDLIIDATDNFDTRLLINDLSQKYNIPWIYGGCVGSY 153
                          170       180       190
                   ....*....|....*....|....*....|....
gi 1972267130  569 GNTQVVYPYLTESYSssvdppekeipvCTLKNFP 602
Cdd:PRK12475   154 GVTYTIIPGKTPCLR------------CLMEHVP 175
Aos1_SUMO cd01492
Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating ...
415-569 4.30e-10

Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 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. Aos1 contains part of the adenylation domain.


Pssm-ID: 238769 [Multi-domain]  Cd Length: 197  Bit Score: 60.38  E-value: 4.30e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  415 YDGQAAVFGWPYQECLFRQRWFVVGAGAIGCELLKNLSMMGVacgegGLIKITDMDQIEISNLNRQFLFRRRDVGGKKSE 494
Cdd:cd01492      4 YDRQIRLWGLEAQKRLRSARILLIGLKGLGAEIAKNLVLSGI-----GSLTILDDRTVTEEDLGAQFLIPAEDLGQNRAE 78
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1972267130  495 CAARAVTAFNSDVRIEALAErvGLETEHifnDEFFGELNGV-ANALDNVDARRyMDRRCVYYRLPLLESGTMGTKG 569
Cdd:cd01492     79 ASLERLRALNPRVKVSVDTD--DISEKP---EEFFSQFDVVvATELSRAELVK-INELCRKLGVKFYATGVHGLFG 148
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
23-136 2.56e-09

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 60.01  E-value: 2.56e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130   23 YSRQIY--TLGESAMVNLRTASVLISGLGSVGVEIAKNLILGGVRHVTIHDTKLAKWSDLSAQYYLRDADVGHN--RATS 98
Cdd:PRK07688     5 YSRQELfsPIGEEGQQKLREKHVLIIGAGALGTANAEMLVRAGVGKVTIVDRDYVEWSNLQRQQLYTESDVKNNlpKAVA 84
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1972267130   99 CYERLAELNDSVNVQV----STDELTEEFVKTFDLVVltDAA 136
Cdd:PRK07688    85 AKKRLEEINSDVRVEAivqdVTAEELEELVTGVDLII--DAT 124
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
23-149 2.87e-09

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 60.27  E-value: 2.87e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130   23 YSRQIyTLGE---SAMVNLRTASVLISGLGSVGVEIAKNLILGGVRHVTIHDTKLAKWSDLSAQYYLRDADVGHNRATSC 99
Cdd:PRK05597     9 YRRQI-MLGEigqQGQQSLFDAKVAVIGAGGLGSPALLYLAGAGVGHITIIDDDTVDLSNLHRQVIHSTAGVGQPKAESA 87
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1972267130  100 YERLAELNDSVNVQVSTDELTEE----FVKTFDLVVL-TDAARTaqRQIAAWTRA 149
Cdd:PRK05597    88 REAMLALNPDVKVTVSVRRLTWSnaldELRDADVILDgSDNFDT--RHLASWAAA 140
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
439-546 9.08e-09

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 56.79  E-value: 9.08e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  439 GAGAIGcellKNLSMMGVACGEGGLiKITDMDQIEISNLNRQFLFrRRDVGGKKSECAARAVTAFNSDVRIEALAERVgl 518
Cdd:PRK08644    35 GAGGLG----SNIAVALARSGVGNL-KLVDFDVVEPSNLNRQQYF-ISQIGMPKVEALKENLLEINPFVEIEAHNEKI-- 106
                           90       100
                   ....*....|....*....|....*...
gi 1972267130  519 ETEHIfnDEFFGELNGVANALDNVDARR 546
Cdd:PRK08644   107 DEDNI--EELFKDCDIVVEAFDNAETKA 132
PRK15116 PRK15116
sulfur acceptor protein CsdL; Provisional
412-566 1.18e-08

sulfur acceptor protein CsdL; Provisional


Pssm-ID: 185071  Cd Length: 268  Bit Score: 57.51  E-value: 1.18e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  412 QSRYDGQAAVFGWPYQECLFRQRWFVVGAGAIGCELLKNLSMMGVacgegGLIKITDMDQIEISNLNRQFLFRRRDVGGK 491
Cdd:PRK15116    10 RQRFGGTARLYGEKALQLFADAHICVVGIGGVGSWAAEALARTGI-----GAITLIDMDDVCVTNTNRQIHALRDNVGLA 84
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1972267130  492 KSECAARAVTAFNSDVRIEALAERVGLE-TEHIFNDEFfgelNGVANALDNVDARRYMDRRCVYYRLPLLESGTMG 566
Cdd:PRK15116    85 KAEVMAERIRQINPECRVTVVDDFITPDnVAEYMSAGF----SYVIDAIDSVRPKAALIAYCRRNKIPLVTTGGAG 156
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
23-135 3.90e-08

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 56.28  E-value: 3.90e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130   23 YSRQIY--TLGESAMVNLRTASVLISGLGSVGVEIAKNLILGGVRHVTIHDTKLAKWSDLSAQ--YYLRDADVGHNRATS 98
Cdd:PRK12475     5 YSRQILfsGIGEEGQRKIREKHVLIVGAGALGAANAEALVRAGIGKLTIADRDYVEWSNLQRQqlYTEEDAKQKKPKAIA 84
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1972267130   99 CYERLAELNDSVNVQ-VSTD---ELTEEFVKTFDLVVltDA 135
Cdd:PRK12475    85 AKEHLRKINSEVEIVpVVTDvtvEELEELVKEVDLII--DA 123
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
427-548 4.54e-08

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 56.64  E-value: 4.54e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  427 QECLFRQRWFVVGAGAIGCELLKNLSMMGVacgegGLIKITDMDQIEISNLNRQFLFRRRDVGGKKSECAARAVTAFNSD 506
Cdd:PRK07878    37 QKRLKNARVLVIGAGGLGSPTLLYLAAAGV-----GTLGIVEFDVVDESNLQRQVIHGQSDVGRSKAQSARDSIVEINPL 111
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1972267130  507 VRIEALAERvgLETEHIFndEFFGELNGVANALDNVdARRYM 548
Cdd:PRK07878   112 VNVRLHEFR--LDPSNAV--ELFSQYDLILDGTDNF-ATRYL 148
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
42-145 1.75e-07

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: 53.90  E-value: 1.75e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130   42 SVLISGLGSVGVEIAKNLILGGVRHVTIHDTKLAKWSDLSAQYYLRDADVGHNRATSCYERLAELNDSVNVQVSTDELT- 120
Cdd:cd01488      1 KILVIGAGGLGCELLKNLALSGFRNIHVIDMDTIDVSNLNRQFLFREKDIGKPKAEVAAKFVNDRVPGVNVTPHFGKIQd 80
                           90       100
                   ....*....|....*....|....*..
gi 1972267130  121 --EEFVKTFDLVVLTDAARTAQRQIAA 145
Cdd:cd01488     81 kdEEFYRQFNIIICGLDSIEARRWING 107
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
15-131 4.91e-07

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 52.15  E-value: 4.91e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130   15 DELLDKNL--YSRQIyTL------GESAmvnLRTASVLISGLGSVGVEIAKNLILGGVRHVTIHDTKLAKWSDLSAQYYL 86
Cdd:PRK05690     3 AELSDEEMlrYNRQI-ILrgfdfdGQEK---LKAARVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVSLSNLQRQVLH 78
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1972267130   87 RDADVGHNRATSCYERLAELN-----DSVNVQVSTDELtEEFVKTFDLVV 131
Cdd:PRK05690    79 DDATIGQPKVESARAALARINphiaiETINARLDDDEL-AALIAGHDLVL 127
E1-1_like cd01485
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ...
415-514 1.14e-06

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: 50.11  E-value: 1.14e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  415 YDGQAAVFGWPYQECLFRQRWFVVGAGAIGCELLKNLSMMGVacgegGLIKITDMDQIEISNLNRQFLFRRRDV--GGKK 492
Cdd:cd01485      2 YDRQIRLWGDEAQNKLRSAKVLIIGAGALGAEIAKNLVLAGI-----DSITIVDHRLVSTEDLGSNFFLDAEVSnsGMNR 76
                           90       100
                   ....*....|....*....|..
gi 1972267130  493 SECAARAVTAFNSDVRIEALAE 514
Cdd:cd01485     77 AAASYEFLQELNPNVKLSIVEE 98
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
42-131 2.48e-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: 49.88  E-value: 2.48e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130   42 SVLISGLGSVGVEIAKNLILGGVRHVTIHDTKLAKWSDLSAQYYLRDADVGHNRATSCYERLAELNDSVNVQ------VS 115
Cdd:cd01484      1 KVLLVGAGGIGCELLKNLALMGFGQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKSEVAAEAVNDRNPNCKVVpyqnkvGP 80
                           90
                   ....*....|....*.
gi 1972267130  116 TDELTEEFVKTFDLVV 131
Cdd:cd01484     81 EQDFNDTFFEQFHIIV 96
PRK08223 PRK08223
hypothetical protein; Validated
424-554 2.18e-05

hypothetical protein; Validated


Pssm-ID: 181302 [Multi-domain]  Cd Length: 287  Bit Score: 47.37  E-value: 2.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  424 WPYQECLFRQRWFVVGAGAIGCELLKNLSMMGVACgegglIKITDMDQIEISNLNRQFLFRRRDVGGKKSECAARAVTAF 503
Cdd:PRK08223    19 PTEQQRLRNSRVAIAGLGGVGGIHLLTLARLGIGK-----FTIADFDVFELRNFNRQAGAMMSTLGRPKAEVLAEMVRDI 93
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1972267130  504 NSDVRIEALAErvGLETEHIfnDEFfgeLNGVANALDNVDARRYMDRRCVY 554
Cdd:PRK08223    94 NPELEIRAFPE--GIGKENA--DAF---LDGVDVYVDGLDFFEFDARRLVF 137
APPBP1_RUB cd01493
Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric ...
414-514 2.31e-05

Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 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. ABPP1 contains part of the adenylation domain.


Pssm-ID: 238770 [Multi-domain]  Cd Length: 425  Bit Score: 48.07  E-value: 2.31e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  414 RYDGQAAVFGWPYQECLFRQRWFVVGAGAIGCELLKNLSMMGVacgegGLIKITDMDQIEISNLNRQFLFRRRDVGGKKS 493
Cdd:cd01493      2 KYDRQLRLWGEHGQAALESAHVCLLNATATGTEILKNLVLPGI-----GSFTIVDGSKVDEEDLGNNFFLDASSLGKSRA 76
                           90       100
                   ....*....|....*....|.
gi 1972267130  494 ECAARAVTAFNSDVRIEALAE 514
Cdd:cd01493     77 EATCELLQELNPDVNGSAVEE 97
PTZ00245 PTZ00245
ubiquitin activating enzyme; Provisional
23-112 2.65e-05

ubiquitin activating enzyme; Provisional


Pssm-ID: 140272  Cd Length: 287  Bit Score: 47.36  E-value: 2.65e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130   23 YSRQIYTLGESAMVNLRTASVLISGLGSVGVEIAKNLILGGVRHVTIHDTKLAKWSDLSAQyYLRDADVGHNRATSCYER 102
Cdd:PTZ00245     9 YDRQIRLWGKSTQQQLMHTSVALHGVAGAAAEAAKNLVLAGVRAVAVADEGLVTDADVCTN-YLMQGEAGGTRGARALGA 87
                           90
                   ....*....|
gi 1972267130  103 LAELNDSVNV 112
Cdd:PTZ00245    88 LQRLNPHVSV 97
E1_ThiF_like cd01487
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ...
42-131 3.17e-05

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: 45.45  E-value: 3.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130   42 SVLISGLGSVGVEIAKNLILGGVRHVTIHDTKLAKWSDLSAQYYlRDADVGHNRATSCYERLAELNDSVNVQVSTDELTE 121
Cdd:cd01487      1 KVGIAGAGGLGSNIAVLLARSGVGNLKLVDFDVVEPSNLNRQQY-FLSQIGEPKVEALKENLREINPFVKIEAINIKIDE 79
                           90
                   ....*....|....
gi 1972267130  122 ----EFVKTFDLVV 131
Cdd:cd01487     80 nnleGLFGDCDIVV 93
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
16-131 4.22e-05

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 45.62  E-value: 4.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130   16 ELLDKNLYSRqiytLGESAMVNLRTASVLISGLGSVGVEIAKNLILGGVRHVTIHDTKLAKWSDLSAQYYLRDaDVGHNR 95
Cdd:PRK08644     8 EEFEAMLASR----HTPKLLEKLKKAKVGIAGAGGLGSNIAVALARSGVGNLKLVDFDVVEPSNLNRQQYFIS-QIGMPK 82
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1972267130   96 ATSCYERLAELNDSVNVQVSTDELTEEFVKTF----DLVV 131
Cdd:PRK08644    83 VEALKENLLEINPFVEIEAHNEKIDEDNIEELfkdcDIVV 122
TcdA COG1179
tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ...
433-570 6.96e-05

tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and biogenesis]; tRNA A37 threonylcarbamoyladenosine dehydratase is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440792  Cd Length: 247  Bit Score: 45.46  E-value: 6.96e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  433 QRWF-----VVGAGAIgcELLKNLSMM-----GV--ACGEG------GLIKITDMDQIEISNLNRQFLFRRRDVGGKKSE 494
Cdd:COG1179      4 ERRFsrterLYGEEGL--ERLANAHVAvvglgGVgsWAAEAlarsgvGRLTLVDLDDVCESNINRQLHALDSTVGRPKVE 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1972267130  495 CAARAVTAFNSDVRIEALAERVGLETEhifnDEFFGE-LNGVANALDNVDARRYMDRRCVYYRLPLLESgtMGTkGN 570
Cdd:COG1179     82 VMAERIRDINPDCEVTAIDEFVTPENA----DELLSEdYDYVIDAIDSVSAKAALIAWCRRRGIPIISS--MGA-GG 151
Apg7 cd01486
Apg7 is an E1-like protein, that activates two different ubiquitin-like proteins, Apg12 and ...
42-166 1.14e-04

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: 45.44  E-value: 1.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130   42 SVLISGLGSVGVEIAKNLILGGVRHVTIHDTKLAKWSDLSAQ--YYLRDADVGHNRATSCYERLAELNDSVN-------- 111
Cdd:cd01486      1 KCLLLGAGTLGCNVARNLLGWGVRHITFVDSGKVSYSNPVRQslFTFEDCKGGKPKAEAAAERLKEIFPSIDatgivlsi 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1972267130  112 ------------VQVSTD-ELTEEFVKTFDLVVLTDAARTAQRQIAAWTRAHNrRILITDARGVFSYI 166
Cdd:cd01486     81 pmpghpisesevPSTLKDvKRLEELIKDHDVIFLLTDSRESRWLPTLLSAAKN-KLVINAALGFDSYL 147
PRK07877 PRK07877
Rv1355c family protein;
427-560 3.90e-04

Rv1355c family protein;


Pssm-ID: 236122 [Multi-domain]  Cd Length: 722  Bit Score: 44.60  E-value: 3.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  427 QECLFRQRWFVVGAgAIGCELLKNLSMMGvACGEgglIKITDMDQIEISNLNR--QFLFrrrDVGGKKSECAARAVTAFN 504
Cdd:PRK07877   102 QERLGRLRIGVVGL-SVGHAIAHTLAAEG-LCGE---LRLADFDTLELSNLNRvpAGVF---DLGVNKAVVAARRIAELD 173
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1972267130  505 SDVRIEALAErvGLETEHIfnDEFFGELNGVANALDNVDAR---RYMDRRcvyYRLPLL 560
Cdd:PRK07877   174 PYLPVEVFTD--GLTEDNV--DAFLDGLDVVVEECDSLDVKvllREAARA---RRIPVL 225
PRK14852 PRK14852
hypothetical protein; Provisional
427-576 1.16e-03

hypothetical protein; Provisional


Pssm-ID: 184854 [Multi-domain]  Cd Length: 989  Bit Score: 43.15  E-value: 1.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  427 QECLFRQRWFVVGAGAIGCELLKNLSMMGVacgegGLIKITDMDQIEISNLNRQFLFRRRDVGGKKSECAARAVTAFNSD 506
Cdd:PRK14852   327 QRRLLRSRVAIAGLGGVGGIHLMTLARTGI-----GNFNLADFDAYSPVNLNRQYGASIASFGRGKLDVMTERALSVNPF 401
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1972267130  507 VRIEALAERVGLETEhifnDEFFGELNGVANALD--NVDARRYMDRRCVYYRLPLLESGTMGTKGNTQVVYP 576
Cdd:PRK14852   402 LDIRSFPEGVAAETI----DAFLKDVDLLVDGIDffALDIRRRLFNRALELGIPVITAGPLGYSCALLVFMP 469
PRK14851 PRK14851
hypothetical protein; Provisional
427-566 1.98e-03

hypothetical protein; Provisional


Pssm-ID: 184853 [Multi-domain]  Cd Length: 679  Bit Score: 42.15  E-value: 1.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  427 QECLFRQRWFVVGAGAIGCELLKNLSMMGVacgegGLIKITDMDQIEISNLNRQFLFRRRDVGGKKSECAARAVTAFNSD 506
Cdd:PRK14851    38 QERLAEAKVAIPGMGGVGGVHLITMVRTGI-----GRFHIADFDQFEPVNVNRQFGARVPSFGRPKLAVMKEQALSINPF 112
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1972267130  507 VRIEALAErvGLETEHIfnDEFfgeLNGVANALDNVDARRYMDRRCVYYR-----LPLLESGTMG 566
Cdd:PRK14851   113 LEITPFPA--GINADNM--DAF---LDGVDVVLDGLDFFQFEIRRTLFNMarekgIPVITAGPLG 170
Ube1_repeat1 cd01491
Ubiquitin activating enzyme (E1), repeat 1. E1, a highly conserved small protein present ...
415-498 2.06e-03

Ubiquitin activating enzyme (E1), repeat 1. 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 first repeat of Ub-E1.


Pssm-ID: 238768 [Multi-domain]  Cd Length: 286  Bit Score: 41.48  E-value: 2.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130  415 YDGQAAVFGWPYQECLFRQRWFVVGAGAIGCELLKNLSMMGVacgegGLIKITDMDQIEISNLNRQFLFRRRDVGGKKSE 494
Cdd:cd01491      2 YSRQLYVLGHEAMKKLQKSNVLISGLGGLGVEIAKNLILAGV-----KSVTLHDTKPCSWSDLSSQFYLREEDIGKNRAE 76

                   ....*
gi 1972267130  495 -CAAR 498
Cdd:cd01491     77 aSQAR 81
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
23-131 3.49e-03

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 40.85  E-value: 3.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130   23 YSRQ--IYTLGESAMVNLRTASVLISGLGSVGVEIAKNLILGGVRHVTIHDTKLAKWSDLSAQYYLRDADVGHNRATSCY 100
Cdd:PRK07878    23 YSRHliIPDVGVDGQKRLKNARVLVIGAGGLGSPTLLYLAAAGVGTLGIVEFDVVDESNLQRQVIHGQSDVGRSKAQSAR 102
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1972267130  101 ERLAELNDSVNVQVSTDELTEEFV----KTFDLVV 131
Cdd:PRK07878   103 DSIVEINPLVNVRLHEFRLDPSNAvelfSQYDLIL 137
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
38-131 4.64e-03

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 40.63  E-value: 4.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267130   38 LRTASVLISGLGSVGVEIAKNLILGGVRHVTIHDTKLAKWSDLSAQYYLRDADVGHNRATSCYERLAELNDSVNVQVSTD 117
Cdd:PRK05600    39 LHNARVLVIGAGGLGCPAMQSLASAGVGTITLIDDDTVDVSNIHRQILFGASDVGRPKVEVAAERLKEIQPDIRVNALRE 118
                           90
                   ....*....|....*...
gi 1972267130  118 ELTE----EFVKTFDLVV 131
Cdd:PRK05600   119 RLTAenavELLNGVDLVL 136
Apg7 cd01486
Apg7 is an E1-like protein, that activates two different ubiquitin-like proteins, Apg12 and ...
437-499 8.18e-03

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: 39.66  E-value: 8.18e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1972267130  437 VVGAGAIGCELLKNLSMMGVAcgeggliKITDMD--QIEISNLNRQFLFRRRDVGGK--KSECAARA 499
Cdd:cd01486      4 LLGAGTLGCNVARNLLGWGVR-------HITFVDsgKVSYSNPVRQSLFTFEDCKGGkpKAEAAAER 63
 
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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