|
Name |
Accession |
Description |
Interval |
E-value |
| HECTc |
smart00119 |
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ... |
918-1244 |
2.60e-139 |
|
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to E2 enzymes.
:
Pssm-ID: 214523 Cd Length: 328 Bit Score: 426.26 E-value: 2.60e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385183 918 LKKSRLHIRFEGELALDYGGLSREFFILLSRELFHPKNGYFEYEGNDYHLQLRPRGCETEKEK-KWLILCGRVLALAVIH 996
Cdd:smart00119 2 LKKRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNPRSGFANEEHlSYFRFIGRVLGKALYD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385183 997 RCYIDVFFTNVFYKSLQKRPVTLMDFKESDAEFYKSMNWL-LENDVVD-LEMSFVYSSM-VNGKLAEQELVPGGESQMVT 1073
Cdd:smart00119 82 NRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEeLDLTFSIVLTsEFGQVKVVELKPGGSNIPVT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385183 1074 EANKAEFIDLMCQKKAIRGVEKPLEILLTSFNQILNDNLLNSLESSDLKRILSGSLELDLNDWRTNTIYKGGYSDCHIVV 1153
Cdd:smart00119 162 EENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGGYSANSQTI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385183 1154 EWFWEVIETMTNQERFDLLLFVTGSSSVPFEGFSALRGneeisKFCIEKWG-DATSFPRAHTCFNRLQLPSYNTKQQLKS 1232
Cdd:smart00119 242 KWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSP-----KFTIRKAGsDDERLPTAHTCFNRLKLPPYSSKEILRE 316
|
330
....*....|..
gi 1061385183 1233 KLQQAIVNGMSY 1244
Cdd:smart00119 317 KLLLAINEGKGF 328
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
603-634 |
7.25e-08 |
|
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.
:
Pssm-ID: 197736 [Multi-domain] Cd Length: 33 Bit Score: 49.52 E-value: 7.25e-08
10 20 30
....*....|....*....|....*....|..
gi 1061385183 603 PPESHWKTYLDAKKRKFYVNHVTKETRWTKPD 634
Cdd:smart00456 1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPR 32
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
746-777 |
1.26e-05 |
|
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.
:
Pssm-ID: 197736 [Multi-domain] Cd Length: 33 Bit Score: 42.97 E-value: 1.26e-05
10 20 30
....*....|....*....|....*....|...
gi 1061385183 746 PLPSGWECITM-NNRTVFLNHANKETSFYDPRI 777
Cdd:smart00456 1 PLPPGWEERKDpDGRPYYYNHETKETQWEKPRE 33
|
|
| FBA_2 |
pfam07735 |
F-box associated; Most of these proteins contain pfam00646 at the N terminus, suggesting that ... |
230-285 |
3.51e-05 |
|
F-box associated; Most of these proteins contain pfam00646 at the N terminus, suggesting that they are effectors linked with ubiquitination.
:
Pssm-ID: 429626 Cd Length: 67 Bit Score: 42.94 E-value: 3.51e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1061385183 230 DHIYLQH-ADWITSEDLLNLDVQTAMLIENNLTEQDLNAFIKQWLRSDSDKLWWLEV 285
Cdd:pfam07735 11 DELTIGDsSVWITLDDLLLINSKKIELDNSRLSLKDLNRFLKHWIKGSNPRLEYLEI 67
|
|
| HECW1_helix super family |
cl39772 |
Helical box domain of E3 ubiquitin-protein ligase HECW1; This is a region of 109 amino acids ... |
679-741 |
5.62e-04 |
|
Helical box domain of E3 ubiquitin-protein ligase HECW1; This is a region of 109 amino acids found in HECW1 proteins in Eukaryotes.Polymorphisms in the same region in the C.elegans homolog affects C. elegans behavioural avoidance of a lawn of Pseudomonas aeruginosa.
The actual alignment was detected with superfamily member pfam18436:
Pssm-ID: 465766 Cd Length: 67 Bit Score: 39.40 E-value: 5.62e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1061385183 679 SDLIQFFQRDEFKTALYENQDAMQIYNECSVVRHAIHRIQKDLDPPSKFENQPLFVRFVNLFA 741
Cdd:pfam18436 5 SPAVKFITRPDFFSVLHNNYSAYRMFTNNTCLKHMISKVRRDPRHFERYQHNRDLVNFLNLFA 67
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| HECTc |
smart00119 |
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ... |
918-1244 |
2.60e-139 |
|
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to E2 enzymes.
Pssm-ID: 214523 Cd Length: 328 Bit Score: 426.26 E-value: 2.60e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385183 918 LKKSRLHIRFEGELALDYGGLSREFFILLSRELFHPKNGYFEYEGNDYHLQLRPRGCETEKEK-KWLILCGRVLALAVIH 996
Cdd:smart00119 2 LKKRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNPRSGFANEEHlSYFRFIGRVLGKALYD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385183 997 RCYIDVFFTNVFYKSLQKRPVTLMDFKESDAEFYKSMNWL-LENDVVD-LEMSFVYSSM-VNGKLAEQELVPGGESQMVT 1073
Cdd:smart00119 82 NRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEeLDLTFSIVLTsEFGQVKVVELKPGGSNIPVT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385183 1074 EANKAEFIDLMCQKKAIRGVEKPLEILLTSFNQILNDNLLNSLESSDLKRILSGSLELDLNDWRTNTIYKGGYSDCHIVV 1153
Cdd:smart00119 162 EENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGGYSANSQTI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385183 1154 EWFWEVIETMTNQERFDLLLFVTGSSSVPFEGFSALRGneeisKFCIEKWG-DATSFPRAHTCFNRLQLPSYNTKQQLKS 1232
Cdd:smart00119 242 KWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSP-----KFTIRKAGsDDERLPTAHTCFNRLKLPPYSSKEILRE 316
|
330
....*....|..
gi 1061385183 1233 KLQQAIVNGMSY 1244
Cdd:smart00119 317 KLLLAINEGKGF 328
|
|
| HECTc |
cd00078 |
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ... |
893-1245 |
4.55e-133 |
|
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It binds specific ubiquitin-conjugating enzymes (E2), accepts ubiquitin from E2, transfers ubiquitin to substrate lysine side chains, and transfers additional ubiquitin molecules to the end of growing ubiquitin chains.
Pssm-ID: 238033 [Multi-domain] Cd Length: 352 Bit Score: 410.80 E-value: 4.55e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385183 893 LCWKVSRDRLLDDAFRIILNVDPFVLKKsRLHIRFEGELALDYGGLSREFFILLSRELFHPKNGYFEY-EGNDYHLQLRP 971
Cdd:cd00078 1 LKITVRRDRILEDALRQLSKVSSSDLKK-VLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYtPDDSGLLYPNP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385183 972 RGCETEKEKKWLILCGRVLALAVIHRCYIDVFFTNVFYKSLQKRPVTLMDFKESDAEFYKSMNWLLENDVVDLEMSFVYS 1051
Cdd:cd00078 80 SSFADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385183 1052 SMVN---GKLAEQELVPGGESQMVTEANKAEFIDLMCQKKAIRGVEKPLEILLTSFNQILNDNLLNSLESSDLKRILSGS 1128
Cdd:cd00078 160 IELDssfGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385183 1129 LELDLNDWRTNTIYKGGYSDCHIVVEWFWEVIETMTNQERFDLLLFVTGSSSVPFEGFSALRgneeiSKFCIEKWGDATS 1208
Cdd:cd00078 240 EDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRVGSPDD 314
|
330 340 350
....*....|....*....|....*....|....*...
gi 1061385183 1209 F-PRAHTCFNRLQLPSYNTKQQLKSKLQQAIVNGMSYS 1245
Cdd:cd00078 315 RlPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
|
|
| HECT |
pfam00632 |
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ... |
945-1241 |
3.19e-87 |
|
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl Terminus.
Pssm-ID: 459880 Cd Length: 304 Bit Score: 285.27 E-value: 3.19e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385183 945 LLSRELFHPKNGYFEYE-GNDYHLQLRPRGCETEKEKKWLILC--GRVLALAVIHRCYIDVFFTNVFYKSLQKRPVTLMD 1021
Cdd:pfam00632 2 LLSKELFDPNYGLFEYEtEDDRTYWFNPSSSESPDLELLDYFKflGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLED 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385183 1022 FKESDAEFYKSMNWLL---ENDVVDLEMSFVYSsmVNGKLAEQELVPGGESQMVTEANKAEFIDLMCQKKAIRGVEKPLE 1098
Cdd:pfam00632 82 LESIDPELYKSLKSLLnmdNDDDEDLGLTFTIP--VFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385183 1099 ILLTSFNQILNDNLLNSLESSDLKRILSGSLELDLNDWRTNTIYKGGYSDCHIVVEWFWEVIETMTNQERFDLLLFVTGS 1178
Cdd:pfam00632 160 AFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGS 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1061385183 1179 SSVPFEGFSALRgneeisKFCIEKWG--DATSFPRAHTCFNRLQLPSYNTKQQLKSKLQQAIVNG 1241
Cdd:pfam00632 240 SRLPVGGFKSLP------KFTIVRKGgdDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEG 298
|
|
| HUL4 |
COG5021 |
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones]; |
880-1241 |
6.70e-83 |
|
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227354 [Multi-domain] Cd Length: 872 Bit Score: 290.51 E-value: 6.70e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385183 880 DMKKEKLGKGPSRLCWKVSRDRLLDDAFRIILNVDPfVLKKSRLHIRFEGELALDYGGLSREFFILLSRELFHPKNGYFE 959
Cdd:COG5021 502 YSLKQKAKIFDPYLHIKVRRDRVFEDSYREIMDESG-DDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFE 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385183 960 YEGND-YHLQLRPRGCETEKEKKWLILCGRVLALAVIHRCYIDVFFTNVFYKSLQKRPVTLMDFKESDAEFYKSMNWLLE 1038
Cdd:COG5021 581 YITEDlYTLPINPLSSINPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLN 660
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385183 1039 N--DVVDLEMSFVYSSMVNGKLAEQELVPGGESQMVTEANKAEFIDLMCQKKAIRGVEKPLEILLTSFNQILNDNLLNSL 1116
Cdd:COG5021 661 NdiDETILDLTFTVEDDSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIF 740
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385183 1117 ESSDLKRILSGSLE-LDLNDWRTNTIYKGGYSDCHIVVeWFWEVIETMTNQERFDLLLFVTGSSSVPFEGFSALRGNEEI 1195
Cdd:COG5021 741 DESELELLIGGIPEdIDIDDWKSNTAYHGYTEDSPIIV-WFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGV 819
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1061385183 1196 SKFCIEKWGDAT-SFPRAHTCFNRLQLPSYNTKQQLKSKLQQAIVNG 1241
Cdd:COG5021 820 RKFTIEKGGTDDdRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEG 866
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
603-634 |
7.25e-08 |
|
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.
Pssm-ID: 197736 [Multi-domain] Cd Length: 33 Bit Score: 49.52 E-value: 7.25e-08
10 20 30
....*....|....*....|....*....|..
gi 1061385183 603 PPESHWKTYLDAKKRKFYVNHVTKETRWTKPD 634
Cdd:smart00456 1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPR 32
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
608-633 |
1.02e-07 |
|
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.
Pssm-ID: 459800 [Multi-domain] Cd Length: 30 Bit Score: 49.04 E-value: 1.02e-07
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
606-634 |
2.00e-07 |
|
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.
Pssm-ID: 238122 [Multi-domain] Cd Length: 31 Bit Score: 48.29 E-value: 2.00e-07
10 20
....*....|....*....|....*....
gi 1061385183 606 SHWKTYLDAKKRKFYVNHVTKETRWTKPD 634
Cdd:cd00201 2 PGWEERWDPDGRVYYYNHNTKETQWEDPR 30
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
746-777 |
1.26e-05 |
|
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.
Pssm-ID: 197736 [Multi-domain] Cd Length: 33 Bit Score: 42.97 E-value: 1.26e-05
10 20 30
....*....|....*....|....*....|...
gi 1061385183 746 PLPSGWECITM-NNRTVFLNHANKETSFYDPRI 777
Cdd:smart00456 1 PLPPGWEERKDpDGRPYYYNHETKETQWEKPRE 33
|
|
| FBA_2 |
pfam07735 |
F-box associated; Most of these proteins contain pfam00646 at the N terminus, suggesting that ... |
230-285 |
3.51e-05 |
|
F-box associated; Most of these proteins contain pfam00646 at the N terminus, suggesting that they are effectors linked with ubiquitination.
Pssm-ID: 429626 Cd Length: 67 Bit Score: 42.94 E-value: 3.51e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1061385183 230 DHIYLQH-ADWITSEDLLNLDVQTAMLIENNLTEQDLNAFIKQWLRSDSDKLWWLEV 285
Cdd:pfam07735 11 DELTIGDsSVWITLDDLLLINSKKIELDNSRLSLKDLNRFLKHWIKGSNPRLEYLEI 67
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
748-777 |
1.78e-04 |
|
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.
Pssm-ID: 238122 [Multi-domain] Cd Length: 31 Bit Score: 39.82 E-value: 1.78e-04
10 20 30
....*....|....*....|....*....|.
gi 1061385183 748 PSGWECITMNNRTV-FLNHANKETSFYDPRI 777
Cdd:cd00201 1 PPGWEERWDPDGRVyYYNHNTKETQWEDPRE 31
|
|
| HECW1_helix |
pfam18436 |
Helical box domain of E3 ubiquitin-protein ligase HECW1; This is a region of 109 amino acids ... |
679-741 |
5.62e-04 |
|
Helical box domain of E3 ubiquitin-protein ligase HECW1; This is a region of 109 amino acids found in HECW1 proteins in Eukaryotes.Polymorphisms in the same region in the C.elegans homolog affects C. elegans behavioural avoidance of a lawn of Pseudomonas aeruginosa.
Pssm-ID: 465766 Cd Length: 67 Bit Score: 39.40 E-value: 5.62e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1061385183 679 SDLIQFFQRDEFKTALYENQDAMQIYNECSVVRHAIHRIQKDLDPPSKFENQPLFVRFVNLFA 741
Cdd:pfam18436 5 SPAVKFITRPDFFSVLHNNYSAYRMFTNNTCLKHMISKVRRDPRHFERYQHNRDLVNFLNLFA 67
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| HECTc |
smart00119 |
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ... |
918-1244 |
2.60e-139 |
|
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to E2 enzymes.
Pssm-ID: 214523 Cd Length: 328 Bit Score: 426.26 E-value: 2.60e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385183 918 LKKSRLHIRFEGELALDYGGLSREFFILLSRELFHPKNGYFEYEGNDYHLQLRPRGCETEKEK-KWLILCGRVLALAVIH 996
Cdd:smart00119 2 LKKRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNPRSGFANEEHlSYFRFIGRVLGKALYD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385183 997 RCYIDVFFTNVFYKSLQKRPVTLMDFKESDAEFYKSMNWL-LENDVVD-LEMSFVYSSM-VNGKLAEQELVPGGESQMVT 1073
Cdd:smart00119 82 NRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEeLDLTFSIVLTsEFGQVKVVELKPGGSNIPVT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385183 1074 EANKAEFIDLMCQKKAIRGVEKPLEILLTSFNQILNDNLLNSLESSDLKRILSGSLELDLNDWRTNTIYKGGYSDCHIVV 1153
Cdd:smart00119 162 EENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGGYSANSQTI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385183 1154 EWFWEVIETMTNQERFDLLLFVTGSSSVPFEGFSALRGneeisKFCIEKWG-DATSFPRAHTCFNRLQLPSYNTKQQLKS 1232
Cdd:smart00119 242 KWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSP-----KFTIRKAGsDDERLPTAHTCFNRLKLPPYSSKEILRE 316
|
330
....*....|..
gi 1061385183 1233 KLQQAIVNGMSY 1244
Cdd:smart00119 317 KLLLAINEGKGF 328
|
|
| HECTc |
cd00078 |
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ... |
893-1245 |
4.55e-133 |
|
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It binds specific ubiquitin-conjugating enzymes (E2), accepts ubiquitin from E2, transfers ubiquitin to substrate lysine side chains, and transfers additional ubiquitin molecules to the end of growing ubiquitin chains.
Pssm-ID: 238033 [Multi-domain] Cd Length: 352 Bit Score: 410.80 E-value: 4.55e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385183 893 LCWKVSRDRLLDDAFRIILNVDPFVLKKsRLHIRFEGELALDYGGLSREFFILLSRELFHPKNGYFEY-EGNDYHLQLRP 971
Cdd:cd00078 1 LKITVRRDRILEDALRQLSKVSSSDLKK-VLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYtPDDSGLLYPNP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385183 972 RGCETEKEKKWLILCGRVLALAVIHRCYIDVFFTNVFYKSLQKRPVTLMDFKESDAEFYKSMNWLLENDVVDLEMSFVYS 1051
Cdd:cd00078 80 SSFADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385183 1052 SMVN---GKLAEQELVPGGESQMVTEANKAEFIDLMCQKKAIRGVEKPLEILLTSFNQILNDNLLNSLESSDLKRILSGS 1128
Cdd:cd00078 160 IELDssfGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385183 1129 LELDLNDWRTNTIYKGGYSDCHIVVEWFWEVIETMTNQERFDLLLFVTGSSSVPFEGFSALRgneeiSKFCIEKWGDATS 1208
Cdd:cd00078 240 EDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRVGSPDD 314
|
330 340 350
....*....|....*....|....*....|....*...
gi 1061385183 1209 F-PRAHTCFNRLQLPSYNTKQQLKSKLQQAIVNGMSYS 1245
Cdd:cd00078 315 RlPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
|
|
| HECT |
pfam00632 |
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ... |
945-1241 |
3.19e-87 |
|
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl Terminus.
Pssm-ID: 459880 Cd Length: 304 Bit Score: 285.27 E-value: 3.19e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385183 945 LLSRELFHPKNGYFEYE-GNDYHLQLRPRGCETEKEKKWLILC--GRVLALAVIHRCYIDVFFTNVFYKSLQKRPVTLMD 1021
Cdd:pfam00632 2 LLSKELFDPNYGLFEYEtEDDRTYWFNPSSSESPDLELLDYFKflGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLED 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385183 1022 FKESDAEFYKSMNWLL---ENDVVDLEMSFVYSsmVNGKLAEQELVPGGESQMVTEANKAEFIDLMCQKKAIRGVEKPLE 1098
Cdd:pfam00632 82 LESIDPELYKSLKSLLnmdNDDDEDLGLTFTIP--VFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385183 1099 ILLTSFNQILNDNLLNSLESSDLKRILSGSLELDLNDWRTNTIYKGGYSDCHIVVEWFWEVIETMTNQERFDLLLFVTGS 1178
Cdd:pfam00632 160 AFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGS 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1061385183 1179 SSVPFEGFSALRgneeisKFCIEKWG--DATSFPRAHTCFNRLQLPSYNTKQQLKSKLQQAIVNG 1241
Cdd:pfam00632 240 SRLPVGGFKSLP------KFTIVRKGgdDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEG 298
|
|
| HUL4 |
COG5021 |
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones]; |
880-1241 |
6.70e-83 |
|
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227354 [Multi-domain] Cd Length: 872 Bit Score: 290.51 E-value: 6.70e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385183 880 DMKKEKLGKGPSRLCWKVSRDRLLDDAFRIILNVDPfVLKKSRLHIRFEGELALDYGGLSREFFILLSRELFHPKNGYFE 959
Cdd:COG5021 502 YSLKQKAKIFDPYLHIKVRRDRVFEDSYREIMDESG-DDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFE 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385183 960 YEGND-YHLQLRPRGCETEKEKKWLILCGRVLALAVIHRCYIDVFFTNVFYKSLQKRPVTLMDFKESDAEFYKSMNWLLE 1038
Cdd:COG5021 581 YITEDlYTLPINPLSSINPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLN 660
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385183 1039 N--DVVDLEMSFVYSSMVNGKLAEQELVPGGESQMVTEANKAEFIDLMCQKKAIRGVEKPLEILLTSFNQILNDNLLNSL 1116
Cdd:COG5021 661 NdiDETILDLTFTVEDDSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIF 740
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385183 1117 ESSDLKRILSGSLE-LDLNDWRTNTIYKGGYSDCHIVVeWFWEVIETMTNQERFDLLLFVTGSSSVPFEGFSALRGNEEI 1195
Cdd:COG5021 741 DESELELLIGGIPEdIDIDDWKSNTAYHGYTEDSPIIV-WFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGV 819
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1061385183 1196 SKFCIEKWGDAT-SFPRAHTCFNRLQLPSYNTKQQLKSKLQQAIVNG 1241
Cdd:COG5021 820 RKFTIEKGGTDDdRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEG 866
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
603-634 |
7.25e-08 |
|
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.
Pssm-ID: 197736 [Multi-domain] Cd Length: 33 Bit Score: 49.52 E-value: 7.25e-08
10 20 30
....*....|....*....|....*....|..
gi 1061385183 603 PPESHWKTYLDAKKRKFYVNHVTKETRWTKPD 634
Cdd:smart00456 1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPR 32
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
608-633 |
1.02e-07 |
|
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.
Pssm-ID: 459800 [Multi-domain] Cd Length: 30 Bit Score: 49.04 E-value: 1.02e-07
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
606-634 |
2.00e-07 |
|
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.
Pssm-ID: 238122 [Multi-domain] Cd Length: 31 Bit Score: 48.29 E-value: 2.00e-07
10 20
....*....|....*....|....*....
gi 1061385183 606 SHWKTYLDAKKRKFYVNHVTKETRWTKPD 634
Cdd:cd00201 2 PGWEERWDPDGRVYYYNHNTKETQWEDPR 30
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
746-777 |
1.26e-05 |
|
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.
Pssm-ID: 197736 [Multi-domain] Cd Length: 33 Bit Score: 42.97 E-value: 1.26e-05
10 20 30
....*....|....*....|....*....|...
gi 1061385183 746 PLPSGWECITM-NNRTVFLNHANKETSFYDPRI 777
Cdd:smart00456 1 PLPPGWEERKDpDGRPYYYNHETKETQWEKPRE 33
|
|
| FBA_2 |
pfam07735 |
F-box associated; Most of these proteins contain pfam00646 at the N terminus, suggesting that ... |
230-285 |
3.51e-05 |
|
F-box associated; Most of these proteins contain pfam00646 at the N terminus, suggesting that they are effectors linked with ubiquitination.
Pssm-ID: 429626 Cd Length: 67 Bit Score: 42.94 E-value: 3.51e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1061385183 230 DHIYLQH-ADWITSEDLLNLDVQTAMLIENNLTEQDLNAFIKQWLRSDSDKLWWLEV 285
Cdd:pfam07735 11 DELTIGDsSVWITLDDLLLINSKKIELDNSRLSLKDLNRFLKHWIKGSNPRLEYLEI 67
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
748-777 |
1.78e-04 |
|
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.
Pssm-ID: 238122 [Multi-domain] Cd Length: 31 Bit Score: 39.82 E-value: 1.78e-04
10 20 30
....*....|....*....|....*....|.
gi 1061385183 748 PSGWECITMNNRTV-FLNHANKETSFYDPRI 777
Cdd:cd00201 1 PPGWEERWDPDGRVyYYNHNTKETQWEDPRE 31
|
|
| HECW1_helix |
pfam18436 |
Helical box domain of E3 ubiquitin-protein ligase HECW1; This is a region of 109 amino acids ... |
679-741 |
5.62e-04 |
|
Helical box domain of E3 ubiquitin-protein ligase HECW1; This is a region of 109 amino acids found in HECW1 proteins in Eukaryotes.Polymorphisms in the same region in the C.elegans homolog affects C. elegans behavioural avoidance of a lawn of Pseudomonas aeruginosa.
Pssm-ID: 465766 Cd Length: 67 Bit Score: 39.40 E-value: 5.62e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1061385183 679 SDLIQFFQRDEFKTALYENQDAMQIYNECSVVRHAIHRIQKDLDPPSKFENQPLFVRFVNLFA 741
Cdd:pfam18436 5 SPAVKFITRPDFFSVLHNNYSAYRMFTNNTCLKHMISKVRRDPRHFERYQHNRDLVNFLNLFA 67
|
|
| |
