|
Name |
Accession |
Description |
Interval |
E-value |
| Uba2_SUMO |
cd01489 |
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ... |
19-444 |
0e+00 |
|
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: 615.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 19 RVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQKKHVGRSKAQVAKESVLQFYPKANIVAYHDSIMN 98
Cdd:cd01489 1 KVLVVGAGGIGCELLKNLVLTGFGEIHIIDLDTIDLSNLNRQFLFRKKHVGKSKAQVAKEAVLSFNPNVKIVAYHANIKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 99 PDYNVEFFRQFILVMNALDNRAARNHVNRMCLAADVPLIESGTAGYLGQVTTIKKGVTECYECHPKPTQRTFPGCTIRNT 178
Cdd:cd01489 81 PDFNVEFFKQFDLVFNALDNLAARRHVNKMCLAADVPLIESGTTGFLGQVQVIKKGKTECYECQPKETPKTFPVCTIRST 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 179 PSEPIHCIVWAKYLFNqlfgeedadqevspdradpeaawepteaeararasnedgdikristkewakstgydpvkLFTKL 258
Cdd:cd01489 161 PSQPIHCIVWAKSLFF-----------------------------------------------------------LFNKV 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 259 FKDDIRYLLTMDKLWRKRKPPVPLDWaevqsqgeetnasdqqnepqlglkdqqvldvksyarlfsksietlrvhlaekgd 338
Cdd:cd01489 182 FKDDIERLLSMEELWKTRKPPVPLSW------------------------------------------------------ 207
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 339 gAELIWDKDDPSAMDFVTSAANLRMHIFSMNMKSRFDIKSMAGNIIPAIATTNAVIAGLIVLEGLKILSGKIDQCRTIFL 418
Cdd:cd01489 208 -KELTFDKDDQDALDFVAAAANLRSHVFGIPMKSRFDIKQMAGNIIPAIATTNAIIAGLIVLEALKVLSGDKEQCRTVFL 286
|
410 420
....*....|....*....|....*.
gi 42559898 419 NKQPNPRKKLLVPCALDPPNPNCYVC 444
Cdd:cd01489 287 NLQPNRRKRLLVPCKLDPPNPNCYVC 312
|
|
| ThiF |
pfam00899 |
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ... |
3-178 |
1.09e-66 |
|
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: 218.28 E-value: 1.09e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 3 LSRGLPRELAEAVAGGRVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQKKHVGRSKAQVAKESVLQ 82
Cdd:pfam00899 6 ALPLIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAAERLRE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 83 FYPKANIVAYHDSIMNPDyNVEFFRQFILVMNALDNRAARNHVNRMCLAADVPLIESGTAGYLGQVTTIKKGVTECYECH 162
Cdd:pfam00899 86 INPDVEVEAYTERLTPEN-AEELIKSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVTVVIPGKTPCYRCL 164
|
170
....*....|....*...
gi 42559898 163 P--KPTQRTFPGCTIRNT 178
Cdd:pfam00899 165 FpeDPPPKLVPSCTVAGV 182
|
|
| Ube1 |
TIGR01408 |
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ... |
10-419 |
1.72e-56 |
|
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: 206.66 E-value: 1.72e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 10 ELAEAVAGGRVLVVGAGGIGCELLKNLVLTGFS-----HIDLIDLDTIDVSNLNRQFLFQKKHVGRSKAQVAKESVLQFY 84
Cdd:TIGR01408 412 TFQQKLQNLNIFLVGCGAIGCEMLKNFALMGVGtgkkgMITVTDPDLIEKSNLNRQFLFRPHHIGKPKSYTAADATLKIN 491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 85 PKANIVAYHDSImNPD----YNVEFFRQFILVMNALDNRAARNHVNRMCLAADVPLIESGTAGYLGQVTTIKKGVTECYE 160
Cdd:TIGR01408 492 PQIKIDAHQNRV-GPEtetiFNDEFYEKLDVVINALDNVEARRYVDSRCLAFLKPLLESGTLGTKGNTQVVVPHLTESYG 570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 161 CHPKPTQRTFPGCTIRNTPSEPIHCIVWAKYLFNQLFGEEDAdqEVSPDRADPEAAWEPTEAEARARASNEDGDIKRIST 240
Cdd:TIGR01408 571 SSRDPPEKEIPFCTLKSFPAAIEHTIQWARDKFEGLFSHKPS--LVNKYLSSPSSAEEVLQKIQSGHSREGLEQIIKLLS 648
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 241 KE----WAKSTGYDPVKlFTKLFKDDIRYLL----------TMDKLWRK-RKPPVPLDW------------------AEV 287
Cdd:TIGR01408 649 KEkprnFSQCVEWARLK-FEKYFNNKALQLLhcfpldirtsTGSPFWSSpKRPPSPLKFdlneplhlsfiqaaaklyATV 727
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 288 QS--QGEETNASD-----------QQNEPQLGLKDQ--------QVLDVKSYARLFS--KSIETLRvHLAEKGDGAELIW 344
Cdd:TIGR01408 728 YGipFAEEDLSADallnilsevkiPEFKPRSNKKIQtdetarkpDTAPIDDRNAIFQleKAILSNE-ATKSDFRMAPLSF 806
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42559898 345 DKDDPSA--MDFVTSAANLRMHIFSMNMKSRFDIKSMAGNIIPAIATTNAVIAGLIVLEGLKILSG--KIDQCRTIFLN 419
Cdd:TIGR01408 807 EKDDDHNghIDFITAASNLRAKNYSIEPADRFKTKFIAGKIIPAIATSTATVSGLVCLELIKVTDGgyKFEVYKNCFLN 885
|
|
| ThiF |
COG0476 |
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ... |
13-161 |
2.41e-39 |
|
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: 144.89 E-value: 2.41e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 13 EAVAGGRVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQKKHVGRSKAQVAKESVLQFYPKANIVAY 92
Cdd:COG0476 23 EKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADVGRPKVEAAAERLRALNPDVEVEAI 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 93 HDSImNPDyNV-EFFRQFILVMNALDNRAARNHVNRMCLAADVPLIESGTAGYLGQVTTIKKGVTECYEC 161
Cdd:COG0476 103 PERL-TEE-NAlELLAGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIGFEGQVTVFIPGDTPCYRC 170
|
|
| UBA2_C |
pfam16195 |
SUMO-activating enzyme subunit 2 C-terminus; |
549-635 |
3.49e-33 |
|
SUMO-activating enzyme subunit 2 C-terminus;
Pssm-ID: 465058 Cd Length: 93 Bit Score: 122.33 E-value: 3.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 549 DAPEKVGPKQA-EDAAKSITNGSDDGAQPSTST--AQEQDDVLIVDSDEEDSSNNADVSEEERSRKRKLD-EKENLSAKR 624
Cdd:pfam16195 1 DAPEKAPPKQAnPEEVNSIANGNKDSAQPSTSTkaAPEQDDVLIVDSDEEGPSSSADVATEGSGRKRKLDaDTEEASTKR 80
|
90
....*....|.
gi 42559898 625 SRIEQKEELDD 635
Cdd:pfam16195 81 SRTEQSAADDD 91
|
|
| UAE_UbL |
pfam14732 |
Ubiquitin/SUMO-activating enzyme ubiquitin-like domain; This is the C-terminal domain of ... |
452-538 |
2.59e-31 |
|
Ubiquitin/SUMO-activating enzyme ubiquitin-like domain; This is the C-terminal domain of ubiquitin-activating enzyme and SUMO-activating enzyme 2. It is structurally similar to ubiquitin. This domain is involved in E1-SUMO-thioester transfer to the SUMO E2 conjugating protein.
Pssm-ID: 464286 Cd Length: 88 Bit Score: 116.91 E-value: 2.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 452 VRLNVHKVTVLTLQDKIVKEKFAMVAPDVQIEDGKGTILISSEEGETEA-NNHKKLSEFGIRNGSRLQADDFLQDYTLLI 530
Cdd:pfam14732 1 LKVDTEKATLGDLVEDVLKKKLGMVAPDVSLSGGGTILYLSSEEDETEDdNLPKKLSELGIKNGSILTVDDFLQDFEVNL 80
|
....*...
gi 42559898 531 NILHSEDL 538
Cdd:pfam14732 81 VILHREEL 88
|
|
| PRK05690 |
PRK05690 |
molybdopterin biosynthesis protein MoeB; Provisional |
13-161 |
8.93e-25 |
|
molybdopterin biosynthesis protein MoeB; Provisional
Pssm-ID: 180204 [Multi-domain] Cd Length: 245 Bit Score: 103.39 E-value: 8.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 13 EAVAGGRVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQKKHVGRSKAQVAKESVLQFYPKANIVAy 92
Cdd:PRK05690 28 EKLKAARVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVSLSNLQRQVLHDDATIGQPKVESARAALARINPHIAIET- 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42559898 93 HDSIMNPDYNVEFFRQFILVMNALDNRAARNHVNRMCLAADVPLIeSGTAGYL-GQVTTIKKGVTE-CYEC 161
Cdd:PRK05690 107 INARLDDDELAALIAGHDLVLDCTDNVATRNQLNRACFAAKKPLV-SGAAIRMeGQVTVFTYQDDEpCYRC 176
|
|
| UBA_E1_SCCH |
pfam10585 |
Ubiquitin-activating enzyme, SCCH domain; Ubiquitin-activating enzyme (E1 enzyme) activates ... |
179-362 |
4.09e-05 |
|
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: 45.68 E-value: 4.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 179 PSEPIHCIVWAKYLFNQLFGE--EDADQEVSPdradPEAAWEPTEAEararASNEDGDI----------KRISTKE---- 242
Cdd:pfam10585 1 PNAIEHTIQWARDEFEGLFVQppEEVNKYLQP----PQNFIESLLKQ----GGGQKLETlesvrkslvtERPKTFEdcva 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 243 WAkstgydpVKLFTKLFKDDIRYLLT---MDKL-------WR--KRkPPVPLDW------------------AEVQSQGE 292
Cdd:pfam10585 73 WA-------RLKFEKLFNNDIKQLLYnfpPDHKtssgapfWSgpKR-PPTPLEFdpnnplhldfvvaaanlrAQVYGIPG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 293 ETNASDQQN----------EPQLGLK----DQQVLDVKSYARLFSKSIETLRVHLAEKGDGAE---------LIWDKDDP 349
Cdd:pfam10585 145 SRDREAIAKvlskvkvpefKPKSGVKiqvnDEEAADPNAESEDDEDELDELLEELPKLAVSPSslagfrlnpIEFEKDDD 224
|
250
....*....|....*
gi 42559898 350 SA--MDFVTSAANLR 362
Cdd:pfam10585 225 TNfhIDFITAASNLR 239
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| Uba2_SUMO |
cd01489 |
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ... |
19-444 |
0e+00 |
|
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: 615.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 19 RVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQKKHVGRSKAQVAKESVLQFYPKANIVAYHDSIMN 98
Cdd:cd01489 1 KVLVVGAGGIGCELLKNLVLTGFGEIHIIDLDTIDLSNLNRQFLFRKKHVGKSKAQVAKEAVLSFNPNVKIVAYHANIKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 99 PDYNVEFFRQFILVMNALDNRAARNHVNRMCLAADVPLIESGTAGYLGQVTTIKKGVTECYECHPKPTQRTFPGCTIRNT 178
Cdd:cd01489 81 PDFNVEFFKQFDLVFNALDNLAARRHVNKMCLAADVPLIESGTTGFLGQVQVIKKGKTECYECQPKETPKTFPVCTIRST 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 179 PSEPIHCIVWAKYLFNqlfgeedadqevspdradpeaawepteaeararasnedgdikristkewakstgydpvkLFTKL 258
Cdd:cd01489 161 PSQPIHCIVWAKSLFF-----------------------------------------------------------LFNKV 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 259 FKDDIRYLLTMDKLWRKRKPPVPLDWaevqsqgeetnasdqqnepqlglkdqqvldvksyarlfsksietlrvhlaekgd 338
Cdd:cd01489 182 FKDDIERLLSMEELWKTRKPPVPLSW------------------------------------------------------ 207
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 339 gAELIWDKDDPSAMDFVTSAANLRMHIFSMNMKSRFDIKSMAGNIIPAIATTNAVIAGLIVLEGLKILSGKIDQCRTIFL 418
Cdd:cd01489 208 -KELTFDKDDQDALDFVAAAANLRSHVFGIPMKSRFDIKQMAGNIIPAIATTNAIIAGLIVLEALKVLSGDKEQCRTVFL 286
|
410 420
....*....|....*....|....*.
gi 42559898 419 NKQPNPRKKLLVPCALDPPNPNCYVC 444
Cdd:cd01489 287 NLQPNRRKRLLVPCKLDPPNPNCYVC 312
|
|
| E1-2_like |
cd01484 |
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ... |
19-401 |
1.56e-78 |
|
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: 249.03 E-value: 1.56e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 19 RVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQKKHVGRSKAQVAKESVLQFYPKANIVAYHDSIMN 98
Cdd:cd01484 1 KVLLVGAGGIGCELLKNLALMGFGQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKSEVAAEAVNDRNPNCKVVPYQNKVGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 99 P-DYNVEFFRQFILVMNALDNRAARNHVNRMCLAADVPLIESGTAGYLGQVTTIKKGVTECYECHPKPTQRTFPGCTIRN 177
Cdd:cd01484 81 EqDFNDTFFEQFHIIVNALDNIIARRYVNGMLIFLIVPLIESGTEGFKGNAQVILPGMTECIECTLYPPQKNFPMCTIAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 178 TPSEPIHCIVWAKYLFnqlfgeedadqevspdradpeaawepteaeararasnedgdikristkewakstgydpvklftk 257
Cdd:cd01484 161 MPRLPEHCIEWARMLQ---------------------------------------------------------------- 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 258 lfkddirylltmdklwrkrkppvpldwaevqsqgeetnasdqqnepqlglkdqqvldvksyarlfsksietlrvhlaekg 337
Cdd:cd01484 --------------------------------------------------------------------------------
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42559898 338 dgaeliwdKDDPSAMDFVTSAANLRMHIFSMNMKSRFDIKSMAGNIIPAIATTNAVIAGLIVLE 401
Cdd:cd01484 177 --------WDDPEHIQFIFQASNERASQYNIRGVTYFLTKGVAGRIIPAVATTNAVVAGVCALE 232
|
|
| Ube1_repeat2 |
cd01490 |
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ... |
19-419 |
6.83e-71 |
|
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: 236.03 E-value: 6.83e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 19 RVLVVGAGGIGCELLKNLVLTGFS-----HIDLIDLDTIDVSNLNRQFLFQKKHVGRSKAQVAKESVLQFYPKANIVAYH 93
Cdd:cd01490 1 KVFLVGAGAIGCELLKNFALMGVGtgesgEITVTDMDNIEKSNLNRQFLFRPHDVGKPKSEVAAAAVKAMNPDLKITALQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 94 DSiMNPD----YNVEFFRQFILVMNALDNRAARNHVNRMCLAADVPLIESGTAGYLGQVTTIKKGVTECYECHPKPTQRT 169
Cdd:cd01490 81 NR-VGPEtehiFNDEFWEKLDGVANALDNVDARMYVDRRCVYYRKPLLESGTLGTKGNTQVVIPHLTESYSSSRDPPEKS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 170 FPGCTIRNTPSEPIHCIVWAKYLFNQLFgeedadqevspdRADPEAA----WEPTEAEARArasnedgdikristkewak 245
Cdd:cd01490 160 IPLCTLKNFPNAIEHTIQWARDEFEGLF------------KQPPENVnqylFEDCVRWARL------------------- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 246 stgydpvkLFTKLFKDDIRYLLT---MDKL-------WR--KRkPPVPLdwaevqsqgeetnasdqqnepQLGLKDQQVL 313
Cdd:cd01490 209 --------LFEKYFNNNIKQLLHnfpPDAVtsdgapfWSgpKR-CPTPL---------------------EFDVNNPLHL 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 314 D-VKSYARLFSKS--IEtlrvhlaekgdgaelIWDKDDPSA--MDFVTSAANLRMHIFSMNMKSRFDIKSMAGNIIPAIA 388
Cdd:cd01490 259 DfVLAAANLYAEVygIP---------------GFEKDDDTNfhMDFITAASNLRARNYSIPPADRHKTKRIAGKIIPAIA 323
|
410 420 430
....*....|....*....|....*....|...
gi 42559898 389 TTNAVIAGLIVLEGLKILSGK--IDQCRTIFLN 419
Cdd:cd01490 324 TTTAAVTGLVCLELYKVVDGKrpLEAYKNAFLN 356
|
|
| ThiF |
pfam00899 |
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ... |
3-178 |
1.09e-66 |
|
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: 218.28 E-value: 1.09e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 3 LSRGLPRELAEAVAGGRVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQKKHVGRSKAQVAKESVLQ 82
Cdd:pfam00899 6 ALPLIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAAERLRE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 83 FYPKANIVAYHDSIMNPDyNVEFFRQFILVMNALDNRAARNHVNRMCLAADVPLIESGTAGYLGQVTTIKKGVTECYECH 162
Cdd:pfam00899 86 INPDVEVEAYTERLTPEN-AEELIKSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVTVVIPGKTPCYRCL 164
|
170
....*....|....*...
gi 42559898 163 P--KPTQRTFPGCTIRNT 178
Cdd:pfam00899 165 FpeDPPPKLVPSCTVAGV 182
|
|
| Uba3_RUB |
cd01488 |
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ... |
19-408 |
4.48e-62 |
|
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: 207.98 E-value: 4.48e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 19 RVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQKKHVGRSKAQVAKESVLQFYPKANIVAYHDSIMn 98
Cdd:cd01488 1 KILVIGAGGLGCELLKNLALSGFRNIHVIDMDTIDVSNLNRQFLFREKDIGKPKAEVAAKFVNDRVPGVNVTPHFGKIQ- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 99 pDYNVEFFRQFILVMNALDNRAARNHVN----RMCLAAD----VPLIESGTAGYLGQVTTIKKGVTECYECHPK--PTQR 168
Cdd:cd01488 80 -DKDEEFYRQFNIIICGLDSIEARRWINgtlvSLLLYEDpesiIPLIDGGTEGFKGHARVILPGITACIECSLDlfPPQV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 169 TFPGCTIRNTPSEPIHCIVWAKYLfnqlfgeedadqevspdradpeaawepteaeararasnedgdikristkewakstg 248
Cdd:cd01488 159 TFPLCTIANTPRLPEHCIEYASLI-------------------------------------------------------- 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 249 ydpvklftklfkddirylltmdkLWRKRKPPVPLdwaevqsqgeetnasdqqnepqlglkdqqvldvksyarlfsksiet 328
Cdd:cd01488 183 -----------------------QWPKEFPFVPL---------------------------------------------- 193
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 329 lrvhlaekgdgaeliwDKDDPSAMDFVTSAANLRMHIFSMNMKSRFDIKSMAGNIIPAIATTNAVIAGLIVLEGLKILSG 408
Cdd:cd01488 194 ----------------DGDDPEHIEWLYQKALERAAQFNISGVTYSLTQGVVKRIIPAVASTNAIIAAACCLEALKIATD 257
|
|
| Ube1 |
TIGR01408 |
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ... |
10-419 |
1.72e-56 |
|
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: 206.66 E-value: 1.72e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 10 ELAEAVAGGRVLVVGAGGIGCELLKNLVLTGFS-----HIDLIDLDTIDVSNLNRQFLFQKKHVGRSKAQVAKESVLQFY 84
Cdd:TIGR01408 412 TFQQKLQNLNIFLVGCGAIGCEMLKNFALMGVGtgkkgMITVTDPDLIEKSNLNRQFLFRPHHIGKPKSYTAADATLKIN 491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 85 PKANIVAYHDSImNPD----YNVEFFRQFILVMNALDNRAARNHVNRMCLAADVPLIESGTAGYLGQVTTIKKGVTECYE 160
Cdd:TIGR01408 492 PQIKIDAHQNRV-GPEtetiFNDEFYEKLDVVINALDNVEARRYVDSRCLAFLKPLLESGTLGTKGNTQVVVPHLTESYG 570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 161 CHPKPTQRTFPGCTIRNTPSEPIHCIVWAKYLFNQLFGEEDAdqEVSPDRADPEAAWEPTEAEARARASNEDGDIKRIST 240
Cdd:TIGR01408 571 SSRDPPEKEIPFCTLKSFPAAIEHTIQWARDKFEGLFSHKPS--LVNKYLSSPSSAEEVLQKIQSGHSREGLEQIIKLLS 648
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 241 KE----WAKSTGYDPVKlFTKLFKDDIRYLL----------TMDKLWRK-RKPPVPLDW------------------AEV 287
Cdd:TIGR01408 649 KEkprnFSQCVEWARLK-FEKYFNNKALQLLhcfpldirtsTGSPFWSSpKRPPSPLKFdlneplhlsfiqaaaklyATV 727
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 288 QS--QGEETNASD-----------QQNEPQLGLKDQ--------QVLDVKSYARLFS--KSIETLRvHLAEKGDGAELIW 344
Cdd:TIGR01408 728 YGipFAEEDLSADallnilsevkiPEFKPRSNKKIQtdetarkpDTAPIDDRNAIFQleKAILSNE-ATKSDFRMAPLSF 806
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42559898 345 DKDDPSA--MDFVTSAANLRMHIFSMNMKSRFDIKSMAGNIIPAIATTNAVIAGLIVLEGLKILSG--KIDQCRTIFLN 419
Cdd:TIGR01408 807 EKDDDHNghIDFITAASNLRAKNYSIEPADRFKTKFIAGKIIPAIATSTATVSGLVCLELIKVTDGgyKFEVYKNCFLN 885
|
|
| ThiF |
COG0476 |
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ... |
13-161 |
2.41e-39 |
|
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: 144.89 E-value: 2.41e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 13 EAVAGGRVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQKKHVGRSKAQVAKESVLQFYPKANIVAY 92
Cdd:COG0476 23 EKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADVGRPKVEAAAERLRALNPDVEVEAI 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 93 HDSImNPDyNV-EFFRQFILVMNALDNRAARNHVNRMCLAADVPLIESGTAGYLGQVTTIKKGVTECYEC 161
Cdd:COG0476 103 PERL-TEE-NAlELLAGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIGFEGQVTVFIPGDTPCYRC 170
|
|
| ThiF_MoeB_HesA_family |
cd00757 |
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ... |
19-173 |
4.88e-38 |
|
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: 140.69 E-value: 4.88e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 19 RVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQKKHVGRSKAQVAKESVLQFYPKANIVAYHDSImN 98
Cdd:cd00757 23 RVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRQILHTEADVGQPKAEAAAERLRAINPDVEIEAYNERL-D 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42559898 99 PDYNVEFFRQFILVMNALDNRAARNHVNRMCLAADVPLIESGTAGYLGQVTTIKKGVTECYEC-HPKPTQRTFPGC 173
Cdd:cd00757 102 AENAEELIAGYDLVLDCTDNFATRYLINDACVKLGKPLVSGAVLGFEGQVTVFIPGEGPCYRClFPEPPPPGVPSC 177
|
|
| E1_enzyme_family |
cd01483 |
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ... |
19-151 |
2.70e-36 |
|
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: 132.78 E-value: 2.70e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 19 RVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQKKHVGRSKAQVAKESVLQFYPKANIVAYHDSIMN 98
Cdd:cd01483 1 RVLLVGLGGLGSEIALNLARSGVGKITLIDFDTVELSNLNRQFLARQADIGKPKAEVAARRLNELNPGVNVTAVPEGISE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 42559898 99 PDYNvEFFRQFILVMNALDNRAARNHVNRMCLAADVPLIESGTAGYLGQVTTI 151
Cdd:cd01483 81 DNLD-DFLDGVDLVIDAIDNIAVRRALNRACKELGIPVIDAGGLGLGGDIQVI 132
|
|
| UBA2_C |
pfam16195 |
SUMO-activating enzyme subunit 2 C-terminus; |
549-635 |
3.49e-33 |
|
SUMO-activating enzyme subunit 2 C-terminus;
Pssm-ID: 465058 Cd Length: 93 Bit Score: 122.33 E-value: 3.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 549 DAPEKVGPKQA-EDAAKSITNGSDDGAQPSTST--AQEQDDVLIVDSDEEDSSNNADVSEEERSRKRKLD-EKENLSAKR 624
Cdd:pfam16195 1 DAPEKAPPKQAnPEEVNSIANGNKDSAQPSTSTkaAPEQDDVLIVDSDEEGPSSSADVATEGSGRKRKLDaDTEEASTKR 80
|
90
....*....|.
gi 42559898 625 SRIEQKEELDD 635
Cdd:pfam16195 81 SRTEQSAADDD 91
|
|
| UAE_UbL |
pfam14732 |
Ubiquitin/SUMO-activating enzyme ubiquitin-like domain; This is the C-terminal domain of ... |
452-538 |
2.59e-31 |
|
Ubiquitin/SUMO-activating enzyme ubiquitin-like domain; This is the C-terminal domain of ubiquitin-activating enzyme and SUMO-activating enzyme 2. It is structurally similar to ubiquitin. This domain is involved in E1-SUMO-thioester transfer to the SUMO E2 conjugating protein.
Pssm-ID: 464286 Cd Length: 88 Bit Score: 116.91 E-value: 2.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 452 VRLNVHKVTVLTLQDKIVKEKFAMVAPDVQIEDGKGTILISSEEGETEA-NNHKKLSEFGIRNGSRLQADDFLQDYTLLI 530
Cdd:pfam14732 1 LKVDTEKATLGDLVEDVLKKKLGMVAPDVSLSGGGTILYLSSEEDETEDdNLPKKLSELGIKNGSILTVDDFLQDFEVNL 80
|
....*...
gi 42559898 531 NILHSEDL 538
Cdd:pfam14732 81 VILHREEL 88
|
|
| PRK05690 |
PRK05690 |
molybdopterin biosynthesis protein MoeB; Provisional |
13-161 |
8.93e-25 |
|
molybdopterin biosynthesis protein MoeB; Provisional
Pssm-ID: 180204 [Multi-domain] Cd Length: 245 Bit Score: 103.39 E-value: 8.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 13 EAVAGGRVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQKKHVGRSKAQVAKESVLQFYPKANIVAy 92
Cdd:PRK05690 28 EKLKAARVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVSLSNLQRQVLHDDATIGQPKVESARAALARINPHIAIET- 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42559898 93 HDSIMNPDYNVEFFRQFILVMNALDNRAARNHVNRMCLAADVPLIeSGTAGYL-GQVTTIKKGVTE-CYEC 161
Cdd:PRK05690 107 INARLDDDELAALIAGHDLVLDCTDNVATRNQLNRACFAAKKPLV-SGAAIRMeGQVTVFTYQDDEpCYRC 176
|
|
| PRK05600 |
PRK05600 |
thiamine biosynthesis protein ThiF; Validated |
10-173 |
5.63e-21 |
|
thiamine biosynthesis protein ThiF; Validated
Pssm-ID: 235528 [Multi-domain] Cd Length: 370 Bit Score: 95.33 E-value: 5.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 10 ELAEAVAGGRVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQKKHVGRSKAQVAKESVLQFYPKANI 89
Cdd:PRK05600 34 EQQERLHNARVLVIGAGGLGCPAMQSLASAGVGTITLIDDDTVDVSNIHRQILFGASDVGRPKVEVAAERLKEIQPDIRV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 90 VAYHDSImNPDYNVEFFRQFILVMNALDNRAARNHVNRMCLAADVPLIESGTAGYLGQVTTIKKGVTEC----YECHP-K 164
Cdd:PRK05600 114 NALRERL-TAENAVELLNGVDLVLDGSDSFATKFLVADAAEITGTPLVWGTVLRFHGELAVFNSGPDHRgvglRDLFPeQ 192
|
....*....
gi 42559898 165 PTQRTFPGC 173
Cdd:PRK05600 193 PSGDSIPDC 201
|
|
| PRK07878 |
PRK07878 |
molybdopterin biosynthesis-like protein MoeZ; Validated |
19-165 |
1.06e-20 |
|
molybdopterin biosynthesis-like protein MoeZ; Validated
Pssm-ID: 181156 [Multi-domain] Cd Length: 392 Bit Score: 94.77 E-value: 1.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 19 RVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQKKHVGRSKAQVAKESVLQFYPKANIVaYHDSIMN 98
Cdd:PRK07878 44 RVLVIGAGGLGSPTLLYLAAAGVGTLGIVEFDVVDESNLQRQVIHGQSDVGRSKAQSARDSIVEINPLVNVR-LHEFRLD 122
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42559898 99 PDYNVEFFRQFILVMNALDNRAARNHVNRMCLAADVPLIESGTAGYLGQVTTI----KKGVTECYEC-HPKP 165
Cdd:PRK07878 123 PSNAVELFSQYDLILDGTDNFATRYLVNDAAVLAGKPYVWGSIYRFEGQASVFwedaPDGLGLNYRDlYPEP 194
|
|
| PRK08762 |
PRK08762 |
molybdopterin-synthase adenylyltransferase MoeB; |
9-174 |
6.27e-20 |
|
molybdopterin-synthase adenylyltransferase MoeB;
Pssm-ID: 236337 [Multi-domain] Cd Length: 376 Bit Score: 92.00 E-value: 6.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 9 RELAEAvaggRVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQKKHVGRSKAQVAKESVLQFYPKAN 88
Cdd:PRK08762 131 RRLLEA----RVLLIGAGGLGSPAALYLAAAGVGTLGIVDHDVVDRSNLQRQILHTEDRVGQPKVDSAAQRLAALNPDVQ 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 89 IVAyHDSIMNPDyNVE-FFRQFILVMNALDNRAARNHVNRMCLAADVPLIESGTAGYLGQVTTIKKGVTE----CYEC-H 162
Cdd:PRK08762 207 VEA-VQERVTSD-NVEaLLQDVDVVVDGADNFPTRYLLNDACVKLGKPLVYGAVFRFEGQVSVFDAGRQRgqapCYRClF 284
|
170
....*....|...
gi 42559898 163 PKPTQRTF-PGCT 174
Cdd:PRK08762 285 PEPPPPELaPSCA 297
|
|
| YgdL_like |
cd00755 |
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ... |
10-143 |
6.64e-19 |
|
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: 86.12 E-value: 6.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 10 ELAEAVAGGRVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQKKHVGRSKAQVAKESVLQFYPKANI 89
Cdd:cd00755 4 EGLEKLRNAHVAVVGLGGVGSWAAEALARSGVGKLTLIDFDVVCVSNLNRQIHALLSTVGKPKVEVMAERIRDINPECEV 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 42559898 90 VAYHDSImNPDyNVE--FFRQFILVMNALDNRAARNHVNRMCLAADVPLIESGTAG 143
Cdd:cd00755 84 DAVEEFL-TPD-NSEdlLGGDPDFVVDAIDSIRAKVALIAYCRKRKIPVISSMGAG 137
|
|
| TcdA |
COG1179 |
tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ... |
19-143 |
8.42e-19 |
|
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: 86.29 E-value: 8.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 19 RVLVVGAGGIG---CEllkNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQKKHVGRSKAQVAKESVLQFYPKANIVAYHDS 95
Cdd:COG1179 26 HVAVVGLGGVGswaAE---ALARSGVGRLTLVDLDDVCESNINRQLHALDSTVGRPKVEVMAERIRDINPDCEVTAIDEF 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 42559898 96 ImNPDyNVE--FFRQFILVMNALDNRAARNHVNRMCLAADVPLIESGTAG 143
Cdd:COG1179 103 V-TPE-NADelLSEDYDYVIDAIDSVSAKAALIAWCRRRGIPIISSMGAG 150
|
|
| Aos1_SUMO |
cd01492 |
Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating ... |
19-148 |
1.78e-18 |
|
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: 83.88 E-value: 1.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 19 RVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQKKHVGRSKAQVAKESVLQFYPKANIVAyhDSIMN 98
Cdd:cd01492 23 RILLIGLKGLGAEIAKNLVLSGIGSLTILDDRTVTEEDLGAQFLIPAEDLGQNRAEASLERLRALNPRVKVSV--DTDDI 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 42559898 99 PDYNVEFFRQFILVMNALDNRAARNHVNRMCLAADVPLIESGTAGYLGQV 148
Cdd:cd01492 101 SEKPEEFFSQFDVVVATELSRAELVKINELCRKLGVKFYATGVHGLFGFV 150
|
|
| PRK08644 |
PRK08644 |
sulfur carrier protein ThiS adenylyltransferase ThiF; |
2-144 |
3.00e-17 |
|
sulfur carrier protein ThiS adenylyltransferase ThiF;
Pssm-ID: 236320 [Multi-domain] Cd Length: 212 Bit Score: 80.67 E-value: 3.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 2 ALSRGLPRELAEAVAGGRVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFqKKHVGRSKAQVAKESVL 81
Cdd:PRK08644 13 MLASRHTPKLLEKLKKAKVGIAGAGGLGSNIAVALARSGVGNLKLVDFDVVEPSNLNRQQYF-ISQIGMPKVEALKENLL 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42559898 82 QFYPKANIVAyHDSIMNPDyNV-EFFRQFILVMNALDN--------RAARNHVNRMCLAAdvplieSGTAGY 144
Cdd:PRK08644 92 EINPFVEIEA-HNEKIDED-NIeELFKDCDIVVEAFDNaetkamlvETVLEHPGKKLVAA------SGMAGY 155
|
|
| E1-1_like |
cd01485 |
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ... |
13-151 |
2.22e-15 |
|
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: 75.15 E-value: 2.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 13 EAVAGGRVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQKKHV--GRSKAQVAKESVLQFYPKANIV 90
Cdd:cd01485 15 NKLRSAKVLIIGAGALGAEIAKNLVLAGIDSITIVDHRLVSTEDLGSNFFLDAEVSnsGMNRAAASYEFLQELNPNVKLS 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42559898 91 AYHDSIMNPDYNV-EFFRQFILVMNALDNRAARNHVNRMCLAADVPLIESGTAGYLGQVTTI 151
Cdd:cd01485 95 IVEEDSLSNDSNIeEYLQKFTLVIATEENYERTAKVNDVCRKHHIPFISCATYGLIGYAFFD 156
|
|
| PRK05597 |
PRK05597 |
molybdopterin biosynthesis protein MoeB; Validated |
13-174 |
1.17e-14 |
|
molybdopterin biosynthesis protein MoeB; Validated
Pssm-ID: 235526 [Multi-domain] Cd Length: 355 Bit Score: 75.68 E-value: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 13 EAVAGGRVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQKKHVGRSKAQVAKESVLQFYPKANIVAY 92
Cdd:PRK05597 24 QSLFDAKVAVIGAGGLGSPALLYLAGAGVGHITIIDDDTVDLSNLHRQVIHSTAGVGQPKAESAREAMLALNPDVKVTVS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 93 HDSiMNPDYNVEFFRQFILVMNALDNRAARNHVNRMCLAADVPLIESGTAGYLGQVTTIKKGVTECYE-CHPK-PTQRTF 170
Cdd:PRK05597 104 VRR-LTWSNALDELRDADVILDGSDNFDTRHLASWAAARLGIPHVWASILGFDAQLSVFHAGHGPIYEdLFPTpPPPGSV 182
|
....
gi 42559898 171 PGCT 174
Cdd:PRK05597 183 PSCS 186
|
|
| PRK15116 |
PRK15116 |
sulfur acceptor protein CsdL; Provisional |
16-148 |
1.45e-14 |
|
sulfur acceptor protein CsdL; Provisional
Pssm-ID: 185071 Cd Length: 268 Bit Score: 74.07 E-value: 1.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 16 AGGRVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQKKHVGRSKAQVAKESVLQFYPKANIVAYHDS 95
Cdd:PRK15116 29 ADAHICVVGIGGVGSWAAEALARTGIGAITLIDMDDVCVTNTNRQIHALRDNVGLAKAEVMAERIRQINPECRVTVVDDF 108
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 42559898 96 ImNPDYNVEFFRQ-FILVMNALDNRAARNHVNRMCLAADVPLIESGTAGylGQV 148
Cdd:PRK15116 109 I-TPDNVAEYMSAgFSYVIDAIDSVRPKAALIAYCRRNKIPLVTTGGAG--GQI 159
|
|
| E1_ThiF_like |
cd01487 |
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ... |
19-144 |
5.44e-14 |
|
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: 70.49 E-value: 5.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 19 RVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQkKHVGRSKAQVAKESVLQFYPKANIVAyHDSIMN 98
Cdd:cd01487 1 KVGIAGAGGLGSNIAVLLARSGVGNLKLVDFDVVEPSNLNRQQYFL-SQIGEPKVEALKENLREINPFVKIEA-INIKID 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 42559898 99 PDYNVEFFRQFILVMNALDN--------RAARNHVNRMCLAAdvplieSGTAGY 144
Cdd:cd01487 79 ENNLEGLFGDCDIVVEAFDNaetkamlaESLLGNKNKPVVCA------SGMAGF 126
|
|
| PRK08328 |
PRK08328 |
hypothetical protein; Provisional |
10-171 |
1.13e-11 |
|
hypothetical protein; Provisional
Pssm-ID: 169382 [Multi-domain] Cd Length: 231 Bit Score: 64.82 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 10 ELAEAVAGGRVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQKKHVGR-SKAQVAKESVLQFYPKAN 88
Cdd:PRK08328 20 EGQEKLKKAKVAVVGVGGLGSPVAYYLAAAGVGRILLIDEQTPELSNLNRQILHWEEDLGKnPKPLSAKWKLERFNSDIK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 89 IVAYHDSIMNPDYNvEFFRQFILVMNALDNRAARNHVNRMCLAADVPLIESGTAGYLGQVTTIKKGVTECY-ECHPKPTQ 167
Cdd:PRK08328 100 IETFVGRLSEENID-EVLKGVDVIVDCLDNFETRYLLDDYAHKKGIPLVHGAVEGTYGQVTTIVPGKTKRLrEIFPKVKK 178
|
....*.
gi 42559898 168 RT--FP 171
Cdd:PRK08328 179 KKgkFP 184
|
|
| PRK07411 |
PRK07411 |
molybdopterin-synthase adenylyltransferase MoeB; |
18-165 |
1.25e-11 |
|
molybdopterin-synthase adenylyltransferase MoeB;
Pssm-ID: 180967 [Multi-domain] Cd Length: 390 Bit Score: 66.68 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 18 GRVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQKKHVGRSKAQVAKESVLQFYPKANIVAYhDSIM 97
Cdd:PRK07411 39 ASVLCIGTGGLGSPLLLYLAAAGIGRIGIVDFDVVDSSNLQRQVIHGTSWVGKPKIESAKNRILEINPYCQVDLY-ETRL 117
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42559898 98 NPDYNVEFFRQFILVMNALDNRAARNHVNRMCLAADVPLIESGTAGYLGQVTTIKKGVTECYEC-HPKP 165
Cdd:PRK07411 118 SSENALDILAPYDVVVDGTDNFPTRYLVNDACVLLNKPNVYGSIFRFEGQATVFNYEGGPNYRDlYPEP 186
|
|
| Ube1_repeat1 |
cd01491 |
Ubiquitin activating enzyme (E1), repeat 1. E1, a highly conserved small protein present ... |
16-148 |
1.84e-11 |
|
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: 65.37 E-value: 1.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 16 AGGRVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQKKHVGRSKAQVAKESVLQFYPKANIVAYHDS 95
Cdd:cd01491 18 QKSNVLISGLGGLGVEIAKNLILAGVKSVTLHDTKPCSWSDLSSQFYLREEDIGKNRAEASQARLAELNPYVPVTVSTGP 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 42559898 96 ImnpdyNVEFFRQFILVMNALDNRAARNHVNRMCLAADVPLIESGTAGYLGQV 148
Cdd:cd01491 98 L-----TTDELLKFQVVVLTDASLEDQLKINEFCHSPGIKFISADTRGLFGSI 145
|
|
| APPBP1_RUB |
cd01493 |
Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric ... |
13-167 |
4.63e-11 |
|
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: 65.40 E-value: 4.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 13 EAVAGGRVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQKKHVGRSKAQVAKESVLQFYPKaniVAY 92
Cdd:cd01493 16 AALESAHVCLLNATATGTEILKNLVLPGIGSFTIVDGSKVDEEDLGNNFFLDASSLGKSRAEATCELLQELNPD---VNG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 93 HDSIMNP----DYNVEFFRQFILVMNaldnrAARNHVNRMCLA-----ADVPLIESGTAGYLGQVTTIKK--GVTecyEC 161
Cdd:cd01493 93 SAVEESPeallDNDPSFFSQFTVVIA-----TNLPESTLLRLAdvlwsANIPLLYVRSYGLYGYIRIQLKehTIV---ES 164
|
....*.
gi 42559898 162 HPKPTQ 167
Cdd:cd01493 165 HPDNAL 170
|
|
| PRK12475 |
PRK12475 |
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional |
13-161 |
6.94e-11 |
|
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
Pssm-ID: 183547 [Multi-domain] Cd Length: 338 Bit Score: 63.98 E-value: 6.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 13 EAVAGGRVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLF------QKKhvgrSKAQVAKESVLQFYPK 86
Cdd:PRK12475 20 RKIREKHVLIVGAGALGAANAEALVRAGIGKLTIADRDYVEWSNLQRQQLYteedakQKK----PKAIAAKEHLRKINSE 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42559898 87 ANIVAYhdsIMnpDYNVEFFRQFI----LVMNALDNRAARNHVNRMCLAADVPLIESGTAGYLGQVTTIKKGVTECYEC 161
Cdd:PRK12475 96 VEIVPV---VT--DVTVEELEELVkevdLIIDATDNFDTRLLINDLSQKYNIPWIYGGCVGSYGVTYTIIPGKTPCLRC 169
|
|
| PRK07688 |
PRK07688 |
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated |
13-161 |
4.72e-09 |
|
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
Pssm-ID: 181084 [Multi-domain] Cd Length: 339 Bit Score: 58.47 E-value: 4.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 13 EAVAGGRVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQ----KKHVgrSKAqVAKESVLQfypKAN 88
Cdd:PRK07688 20 QKLREKHVLIIGAGALGTANAEMLVRAGVGKVTIVDRDYVEWSNLQRQQLYTesdvKNNL--PKA-VAAKKRLE---EIN 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42559898 89 -IVAYHDSIMnpDYNVEFFRQFI----LVMNALDNRAARNHVNRMCLAADVPLIESGTAGYLGQVTTIKKGVTECYEC 161
Cdd:PRK07688 94 sDVRVEAIVQ--DVTAEELEELVtgvdLIIDATDNFETRFIVNDAAQKYGIPWIYGACVGSYGLSYTIIPGKTPCLRC 169
|
|
| PRK14851 |
PRK14851 |
hypothetical protein; Provisional |
2-144 |
2.91e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 184853 [Multi-domain] Cd Length: 679 Bit Score: 56.79 E-value: 2.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 2 ALSR--GL--PRElAEAVAGGRVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQKKHVGRSKAQVAK 77
Cdd:PRK14851 25 AFSRniGLftPGE-QERLAEAKVAIPGMGGVGGVHLITMVRTGIGRFHIADFDQFEPVNVNRQFGARVPSFGRPKLAVMK 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42559898 78 ESVLQFYPKANIVAYHDSImNPDYNVEFFRQFILVMNALDNRA--ARNHVNRMCLAADVPLIESGTAGY 144
Cdd:PRK14851 104 EQALSINPFLEITPFPAGI-NADNMDAFLDGVDVVLDGLDFFQfeIRRTLFNMAREKGIPVITAGPLGY 171
|
|
| Apg7 |
cd01486 |
Apg7 is an E1-like protein, that activates two different ubiquitin-like proteins, Apg12 and ... |
19-103 |
6.80e-08 |
|
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: 54.69 E-value: 6.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 19 RVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQKKHV--GRSKAQVAKESVLQFYPKANIVAYHDSI 96
Cdd:cd01486 1 KCLLLGAGTLGCNVARNLLGWGVRHITFVDSGKVSYSNPVRQSLFTFEDCkgGKPKAEAAAERLKEIFPSIDATGIVLSI 80
|
....*..
gi 42559898 97 MNPDYNV 103
Cdd:cd01486 81 PMPGHPI 87
|
|
| PRK14852 |
PRK14852 |
hypothetical protein; Provisional |
19-144 |
3.30e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 184854 [Multi-domain] Cd Length: 989 Bit Score: 53.55 E-value: 3.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 19 RVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQKKHVGRSKAQVAKESVLQFYPKANIVAYHDSIMN 98
Cdd:PRK14852 334 RVAIAGLGGVGGIHLMTLARTGIGNFNLADFDAYSPVNLNRQYGASIASFGRGKLDVMTERALSVNPFLDIRSFPEGVAA 413
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 42559898 99 PDYNVeFFRQFILVMNALDNRA--ARNHVNRMCLAADVPLIESGTAGY 144
Cdd:PRK14852 414 ETIDA-FLKDVDLLVDGIDFFAldIRRRLFNRALELGIPVITAGPLGY 460
|
|
| PRK08223 |
PRK08223 |
hypothetical protein; Validated |
17-151 |
2.41e-06 |
|
hypothetical protein; Validated
Pssm-ID: 181302 [Multi-domain] Cd Length: 287 Bit Score: 49.68 E-value: 2.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 17 GGRVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQKKHVGRSKAQVAKESVLQFYPKANIVAYHDSI 96
Cdd:PRK08223 27 NSRVAIAGLGGVGGIHLLTLARLGIGKFTIADFDVFELRNFNRQAGAMMSTLGRPKAEVLAEMVRDINPELEIRAFPEGI 106
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 42559898 97 mnPDYNVEFFRQFI-LVMNALDNRA--ARNHVNRMCLAADVPLIesgTAGYLGQVTTI 151
Cdd:PRK08223 107 --GKENADAFLDGVdVYVDGLDFFEfdARRLVFAACQQRGIPAL---TAAPLGMGTAL 159
|
|
| Ube1 |
TIGR01408 |
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ... |
7-113 |
4.44e-06 |
|
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: 49.89 E-value: 4.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 7 LPRELAEAVAGGRVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQKKHVGRSKAQVAKESVLQFYPk 86
Cdd:TIGR01408 14 LGDEAMQKMAKSNVLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLSSNFFLSEDDVGRNRAEAVVKKLAELNP- 92
|
90 100
....*....|....*....|....*..
gi 42559898 87 anivAYHDSIMNPDYNVEFFRQFILVM 113
Cdd:TIGR01408 93 ----YVHVSSSSVPFNEEFLDKFQCVV 115
|
|
| E1_like_apg7 |
TIGR01381 |
E1-like protein-activating enzyme Gsa7p/Apg7p; This model represents a family of eukaryotic ... |
5-132 |
1.64e-05 |
|
E1-like protein-activating enzyme Gsa7p/Apg7p; This model represents a family of eukaryotic proteins found in animals, plants, and yeasts, including Apg7p (YHR171W) from Saccharomyces cerevisiae and GSA7 from Pichia pastoris. Members are about 650 to 700 residues in length and include a central domain of about 150 residues shared with the ThiF/MoeB/HesA family of proteins. A low level of similarity to ubiquitin-activating enzyme E1 is described in a paper on peroxisome autophagy mediated by GSA7, and is the basis of the name ubiquitin activating enzyme E1-like protein. Members of the family appear to be involved in protein lipidation events analogous to ubiquitination and required for membrane fusion events during autophagy.
Pssm-ID: 273590 [Multi-domain] Cd Length: 664 Bit Score: 48.01 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 5 RGLPRELAEAVAGGRVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQKKHV---GRSKAQVAKESVL 81
Cdd:TIGR01381 326 RLHPDLQLERYSQLKVLLLGAGTLGCNVARCLIGWGVRHITFVDNGKVSYSNPVRQSLSNFEDCllgGRGKAETAQKALK 405
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42559898 82 QFYPKANIVAYHDSIMNP--------------DYN--VEFFRQFILVMNALDNRAAR-------NHVNRMCLAA 132
Cdd:TIGR01381 406 RIFPSIQATGHRLTVPMPghpidekdvpelekDIArlEQLIKDHDVVFLLLDSREARwlptvlcSRHKKIAISA 479
|
|
| UBA_E1_SCCH |
pfam10585 |
Ubiquitin-activating enzyme, SCCH domain; Ubiquitin-activating enzyme (E1 enzyme) activates ... |
179-362 |
4.09e-05 |
|
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: 45.68 E-value: 4.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 179 PSEPIHCIVWAKYLFNQLFGE--EDADQEVSPdradPEAAWEPTEAEararASNEDGDI----------KRISTKE---- 242
Cdd:pfam10585 1 PNAIEHTIQWARDEFEGLFVQppEEVNKYLQP----PQNFIESLLKQ----GGGQKLETlesvrkslvtERPKTFEdcva 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 243 WAkstgydpVKLFTKLFKDDIRYLLT---MDKL-------WR--KRkPPVPLDW------------------AEVQSQGE 292
Cdd:pfam10585 73 WA-------RLKFEKLFNNDIKQLLYnfpPDHKtssgapfWSgpKR-PPTPLEFdpnnplhldfvvaaanlrAQVYGIPG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559898 293 ETNASDQQN----------EPQLGLK----DQQVLDVKSYARLFSKSIETLRVHLAEKGDGAE---------LIWDKDDP 349
Cdd:pfam10585 145 SRDREAIAKvlskvkvpefKPKSGVKiqvnDEEAADPNAESEDDEDELDELLEELPKLAVSPSslagfrlnpIEFEKDDD 224
|
250
....*....|....*
gi 42559898 350 SA--MDFVTSAANLR 362
Cdd:pfam10585 225 TNfhIDFITAASNLR 239
|
|
|