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Conserved domains on  [gi|1831513283|ref|NP_001368363|]
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E3 ubiquitin-protein ligase [Caenorhabditis elegans]

Protein Classification

MIB_HERC2 and HECTc domain-containing protein( domain architecture ID 11043387)

protein containing domains F5_F8_type_C, MIB_HERC2, and HECTc

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
2178-2605 3.77e-123

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: 393.08  E-value: 3.77e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513283 2178 ERVKVTRaeETLLDQAIRLMKFHA--DRKAVLEIEYTNEEGTG-LGPTLEFYALVAAELQRKSLALWVCDDDDTHasksg 2254
Cdd:cd00078      1 LKITVRR--DRILEDALRQLSKVSssDLKKVLEVEFVGEEGIDaGGVTREFFTLVSKELFNPSYGLFRYTPDDSG----- 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513283 2255 eerevdlgegkkpigyyvrrvgGLFPAPLPPGTDETKraaDMFRVLGVFLAKVLLDGRLVDLPLSRPFLKLLvhpqigdd 2334
Cdd:cd00078     74 ----------------------LLYPNPSSFADEDHL---KLFRFLGRLLGKALYEGRLLDLPFSRAFYKKL-------- 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513283 2335 argpnLHKILSLDDFEEVNPVKGSFLKELRALAQRkrliendtsidsnskrrkiaelklhikgstcrVEDLALNFTVNPP 2414
Cdd:cd00078    121 -----LGKPLSLEDLEELDPELYKSLKELLDNDGD--------------------------------EDDLELTFTIELD 163
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513283 2415 SKVFQYAEMELVDGGSDIDVTIDNVEQYVEKCEEFYLNTGIAYQMRAFRDGFDRVFPLRTLRAYSPEEVQRLLSGEqcPE 2494
Cdd:cd00078    164 SSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGS--ED 241
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513283 2495 WSRDDILNYTEPKLGYTRESPGFLRFVDVMEALTAQERKNFLQFATGCSSLPPGGLANLHPRLTIvRKVESGDGSYPSVN 2574
Cdd:cd00078    242 IDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLNPKFTI-RRVGSPDDRLPTAH 320
                          410       420       430
                   ....*....|....*....|....*....|..
gi 1831513283 2575 TCVHYLKLPEYSSSAILRERLLTAINEK-GFH 2605
Cdd:cd00078    321 TCFNLLKLPPYSSKEILREKLLYAINEGaGFG 352
MIB_HERC2 pfam06701
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain ...
1409-1466 4.45e-24

Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain (either Ring or Hect).


:

Pssm-ID: 461991  Cd Length: 66  Bit Score: 97.29  E-value: 4.45e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1831513283 1409 SKVVRGKDWRWEDQDGGEGKFGRIT------SPPESGWVDVTWDNGNANSYRFGANGNFDIERV 1466
Cdd:pfam06701    2 ARVVRGPDWKWGDQDGGEGHVGTVVeirdwdSESPRSTVRVQWDNGSTNVYRVGYEGKYDLKVV 65
Sad1_UNC super family cl23730
Sad1 / UNC-like C-terminal; The C. elegans UNC-84 protein is a nuclear envelope protein that ...
1200-1322 8.98e-14

Sad1 / UNC-like C-terminal; The C. elegans UNC-84 protein is a nuclear envelope protein that is involved in nuclear anchoring and migration during development. The S. pombe Sad1 protein localizes at the spindle pole body. UNC-84 and and Sad1 share a common C-terminal region, that is often termed the SUN (Sad1 and UNC) domain. In mammals, the SUN domain is present in two proteins, Sun1 and Sun2. The SUN domain of Sun2 has been demonstrated to be in the periplasm.


The actual alignment was detected with superfamily member pfam07738:

Pssm-ID: 474037  Cd Length: 130  Bit Score: 70.40  E-value: 8.98e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513283 1200 PEDLLSRDQNPINCHTSDDKNAHFTIDLGLFVVPTSYSLRHSRGYGR-SALRNWMLQGSVDAKRWENVIVhtDDKGLGEP 1278
Cdd:pfam07738    8 PKVILQPDYMPGPCWSFKGSRGFVVIELSEFIIVEAITLEHVEKSVFsSAPKDFEVSGSDRYPTTKWVLL--GEFSYDLD 85
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1831513283 1279 GSTA-TWHVGEKGTTAFRF--FRIAQNGknssGQTHYLSCSGFEIYG 1322
Cdd:pfam07738   86 GKTIqTFQLENPPDIWVKYvkLRILSNY----GNEHYTCLYRFRVHG 128
ANKYR super family cl34000
Ankyrin repeat [Signal transduction mechanisms];
332-416 1.69e-07

Ankyrin repeat [Signal transduction mechanisms];


The actual alignment was detected with superfamily member COG0666:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 55.35  E-value: 1.69e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513283  332 YAAGSGAERVHRQLI------DAIRQKDLTALVDAIESGQV-----------DVNFADDVGQSLTNWASAFGSIEM---- 390
Cdd:COG0666    126 LAAYNGNLEIVKLLLeagadvNAQDNDGNTPLHLAAANGNLeivkllleagaDVNARDNDGETPLHLAAENGHLEIvkll 205
                           90       100
                   ....*....|....*....|....*...
gi 1831513283  391 --RGANPDLRDEDGKTALDKARERSDDD 416
Cdd:COG0666    206 leAGADVNAKDNDGKTALDLAAENGNLE 233
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
2178-2605 3.77e-123

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: 393.08  E-value: 3.77e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513283 2178 ERVKVTRaeETLLDQAIRLMKFHA--DRKAVLEIEYTNEEGTG-LGPTLEFYALVAAELQRKSLALWVCDDDDTHasksg 2254
Cdd:cd00078      1 LKITVRR--DRILEDALRQLSKVSssDLKKVLEVEFVGEEGIDaGGVTREFFTLVSKELFNPSYGLFRYTPDDSG----- 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513283 2255 eerevdlgegkkpigyyvrrvgGLFPAPLPPGTDETKraaDMFRVLGVFLAKVLLDGRLVDLPLSRPFLKLLvhpqigdd 2334
Cdd:cd00078     74 ----------------------LLYPNPSSFADEDHL---KLFRFLGRLLGKALYEGRLLDLPFSRAFYKKL-------- 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513283 2335 argpnLHKILSLDDFEEVNPVKGSFLKELRALAQRkrliendtsidsnskrrkiaelklhikgstcrVEDLALNFTVNPP 2414
Cdd:cd00078    121 -----LGKPLSLEDLEELDPELYKSLKELLDNDGD--------------------------------EDDLELTFTIELD 163
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513283 2415 SKVFQYAEMELVDGGSDIDVTIDNVEQYVEKCEEFYLNTGIAYQMRAFRDGFDRVFPLRTLRAYSPEEVQRLLSGEqcPE 2494
Cdd:cd00078    164 SSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGS--ED 241
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513283 2495 WSRDDILNYTEPKLGYTRESPGFLRFVDVMEALTAQERKNFLQFATGCSSLPPGGLANLHPRLTIvRKVESGDGSYPSVN 2574
Cdd:cd00078    242 IDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLNPKFTI-RRVGSPDDRLPTAH 320
                          410       420       430
                   ....*....|....*....|....*....|..
gi 1831513283 2575 TCVHYLKLPEYSSSAILRERLLTAINEK-GFH 2605
Cdd:cd00078    321 TCFNLLKLPPYSSKEILREKLLYAINEGaGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
2203-2604 4.01e-120

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: 383.12  E-value: 4.01e-120
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513283  2203 RKAVLEIEYTNEEG-TGLGPTLEFYALVAAELQRKSLALWVCDDDDTHasksgeerevdlgegkkpigyyvrrvggLFPA 2281
Cdd:smart00119    3 KKRVLEIEFEGEEGlDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYL----------------------------LYPN 54
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513283  2282 PLPPGTDETKRAadMFRVLGVFLAKVLLDGRLVDLPLSRPFLKLLvhpqigddargpnLHKILSLDDFEEVNPVKGSFLK 2361
Cdd:smart00119   55 PRSGFANEEHLS--YFRFIGRVLGKALYDNRLLDLFFARPFYKKL-------------LGKPVTLHDLESLDPELYKSLK 119
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513283  2362 ELralaqrkrLIENDTSidsnskrrkiaelklhikgstcrvEDLALNFTVNPPSKVFQYAEMELVDGGSDIDVTIDNVEQ 2441
Cdd:smart00119  120 WL--------LLNNDTS------------------------EELDLTFSIVLTSEFGQVKVVELKPGGSNIPVTEENKKE 167
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513283  2442 YVEKCEEFYLNTGIAYQMRAFRDGFDRVFPLRTLRAYSPEEVQRLLSGeqCPEWSRDDILNYTEPKLGYTRESPGFLRFV 2521
Cdd:smart00119  168 YVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICG--SPEIDVDDLKSNTEYKGGYSANSQTIKWFW 245
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513283  2522 DVMEALTAQERKNFLQFATGCSSLPPGGLANLHPRLTIVRKVESgDGSYPSVNTCVHYLKLPEYSSSAILRERLLTAINE 2601
Cdd:smart00119  246 EVVESFTNEERRKLLQFVTGSSRLPVGGFAALSPKFTIRKAGSD-DERLPTAHTCFNRLKLPPYSSKEILREKLLLAINE 324

                    ....
gi 1831513283  2602 -KGF 2604
Cdd:smart00119  325 gKGF 328
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
2228-2606 2.29e-84

HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl Terminus.


Pssm-ID: 459880  Cd Length: 304  Bit Score: 279.50  E-value: 2.29e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513283 2228 LVAAELQRKSLALWVCDDDDTHasksgeerevdlgegkkpigyyvrrvggLFPAPLPPGTDETKRAADMFRVLGVFLAKV 2307
Cdd:pfam00632    2 LLSKELFDPNYGLFEYETEDDR----------------------------TYWFNPSSSESPDLELLDYFKFLGKLLGKA 53
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513283 2308 LLDGRLVDLPLSRPFLKLLvhpqigddargpnLHKILSLDDFEEVNPVKGSFLKELRalaqrkrLIENDTsidsnskrrk 2387
Cdd:pfam00632   54 IYNGILLDLPFPPFFYKKL-------------LGEPLTLEDLESIDPELYKSLKSLL-------NMDNDD---------- 103
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513283 2388 iaelklhikgstcrVEDLALNFTVNppskVFQYAEM-ELVDGGSDIDVTIDNVEQYVEKCEEFYLNTGIAYQMRAFRDGF 2466
Cdd:pfam00632  104 --------------DEDLGLTFTIP----VFGESKTiELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQLEAFRKGF 165
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513283 2467 DRVFPLRTLRAYSPEEVQRLLSGEqcPEWSRDDILNYTEPKLGYTRESPGFLRFVDVMEALTAQERKNFLQFATGCSSLP 2546
Cdd:pfam00632  166 YSVIPKEALSLFTPEELELLICGS--PEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGSSRLP 243
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1831513283 2547 PGGLANLhPRLTIVRKVESGDGSYPSVNTCVHYLKLPEYSSSAILRERLLTAINE-KGFHL 2606
Cdd:pfam00632  244 VGGFKSL-PKFTIVRKGGDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEgEGFGL 303
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
2076-2604 3.01e-56

Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 213.09  E-value: 3.01e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513283 2076 FISDKLTLKVTQVLSDALVVAARSLPEWCSRlvyKYPCLFTVETRNMYMQATAFGVSRTIV--WLQQRRDAAVERargsa 2153
Cdd:COG5021    413 TYEDLRREQLGRESDESFYVASNVQQQRASR---EGPLLSGWKTRLNNLYRFYFVEHRKKTltKNDSRLGSFISL----- 484
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513283 2154 qagNSSAARQHDRYHEYRVGRLRHE---------RVKVTRaeETLLDQAIRLMKFHA--DRKAVLEIEYTNEEG-TGLGP 2221
Cdd:COG5021    485 ---NKLDIRRIKEDKRRKLFYSLKQkakifdpylHIKVRR--DRVFEDSYREIMDESgdDLKKTLEIEFVGEEGiDAGGL 559
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513283 2222 TLEFYALVAAELQrkslalwvcDDDDTHAsksgEEREVDLgegkkpigYYvrrvgglFPAPLPPGTDETKRaaDMFRVLG 2301
Cdd:COG5021    560 TREWLFLLSKEMF---------NPDYGLF----EYITEDL--------YT-------LPINPLSSINPEHL--SYFKFLG 609
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513283 2302 VFLAKVLLDGRLVDLPLSRPFLKLLvhpqigddargpnLHKILSLDDFEEVNPVKGSFLKELRalaqrkrlienDTSIDS 2381
Cdd:COG5021    610 RVIGKAIYDSRILDVQFSKAFYKKL-------------LGKPVSLVDLESLDPELYRSLVWLL-----------NNDIDE 665
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513283 2382 NskrrkiaelklhIKGSTCRVEDLALNFTVNppskvfqyaeMELVDGGSDIDVTIDNVEQYVEKCEEFYLNTGIAYQMRA 2461
Cdd:COG5021    666 T------------ILDLTFTVEDDSFGESRT----------VELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSA 723
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513283 2462 FRDGFDRVFPLRTLRAYSPEEVQRLLSGEqcPEWSR-DDILNYTEPKlGYTRESPGFLRFVDVMEALTAQERKNFLQFAT 2540
Cdd:COG5021    724 FKSGFSEIIPPDLLQIFDESELELLIGGI--PEDIDiDDWKSNTAYH-GYTEDSPIIVWFWEIISEFDFEERAKLLQFVT 800
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1831513283 2541 GCSSLPPGGLANLHPRLTIVRKV--ESGDGSY--PSVNTCVHYLKLPEYSSSAILRERLLTAINE-KGF 2604
Cdd:COG5021    801 GTSRIPINGFKDLQGSDGVRKFTieKGGTDDDrlPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEgAGF 869
MIB_HERC2 pfam06701
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain ...
1409-1466 4.45e-24

Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain (either Ring or Hect).


Pssm-ID: 461991  Cd Length: 66  Bit Score: 97.29  E-value: 4.45e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1831513283 1409 SKVVRGKDWRWEDQDGGEGKFGRIT------SPPESGWVDVTWDNGNANSYRFGANGNFDIERV 1466
Cdd:pfam06701    2 ARVVRGPDWKWGDQDGGEGHVGTVVeirdwdSESPRSTVRVQWDNGSTNVYRVGYEGKYDLKVV 65
Sad1_UNC pfam07738
Sad1 / UNC-like C-terminal; The C. elegans UNC-84 protein is a nuclear envelope protein that ...
1200-1322 8.98e-14

Sad1 / UNC-like C-terminal; The C. elegans UNC-84 protein is a nuclear envelope protein that is involved in nuclear anchoring and migration during development. The S. pombe Sad1 protein localizes at the spindle pole body. UNC-84 and and Sad1 share a common C-terminal region, that is often termed the SUN (Sad1 and UNC) domain. In mammals, the SUN domain is present in two proteins, Sun1 and Sun2. The SUN domain of Sun2 has been demonstrated to be in the periplasm.


Pssm-ID: 400199  Cd Length: 130  Bit Score: 70.40  E-value: 8.98e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513283 1200 PEDLLSRDQNPINCHTSDDKNAHFTIDLGLFVVPTSYSLRHSRGYGR-SALRNWMLQGSVDAKRWENVIVhtDDKGLGEP 1278
Cdd:pfam07738    8 PKVILQPDYMPGPCWSFKGSRGFVVIELSEFIIVEAITLEHVEKSVFsSAPKDFEVSGSDRYPTTKWVLL--GEFSYDLD 85
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1831513283 1279 GSTA-TWHVGEKGTTAFRF--FRIAQNGknssGQTHYLSCSGFEIYG 1322
Cdd:pfam07738   86 GKTIqTFQLENPPDIWVKYvkLRILSNY----GNEHYTCLYRFRVHG 128
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
332-416 1.69e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 55.35  E-value: 1.69e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513283  332 YAAGSGAERVHRQLI------DAIRQKDLTALVDAIESGQV-----------DVNFADDVGQSLTNWASAFGSIEM---- 390
Cdd:COG0666    126 LAAYNGNLEIVKLLLeagadvNAQDNDGNTPLHLAAANGNLeivkllleagaDVNARDNDGETPLHLAAENGHLEIvkll 205
                           90       100
                   ....*....|....*....|....*...
gi 1831513283  391 --RGANPDLRDEDGKTALDKARERSDDD 416
Cdd:COG0666    206 leAGADVNAKDNDGKTALDLAAENGNLE 233
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
2178-2605 3.77e-123

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: 393.08  E-value: 3.77e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513283 2178 ERVKVTRaeETLLDQAIRLMKFHA--DRKAVLEIEYTNEEGTG-LGPTLEFYALVAAELQRKSLALWVCDDDDTHasksg 2254
Cdd:cd00078      1 LKITVRR--DRILEDALRQLSKVSssDLKKVLEVEFVGEEGIDaGGVTREFFTLVSKELFNPSYGLFRYTPDDSG----- 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513283 2255 eerevdlgegkkpigyyvrrvgGLFPAPLPPGTDETKraaDMFRVLGVFLAKVLLDGRLVDLPLSRPFLKLLvhpqigdd 2334
Cdd:cd00078     74 ----------------------LLYPNPSSFADEDHL---KLFRFLGRLLGKALYEGRLLDLPFSRAFYKKL-------- 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513283 2335 argpnLHKILSLDDFEEVNPVKGSFLKELRALAQRkrliendtsidsnskrrkiaelklhikgstcrVEDLALNFTVNPP 2414
Cdd:cd00078    121 -----LGKPLSLEDLEELDPELYKSLKELLDNDGD--------------------------------EDDLELTFTIELD 163
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513283 2415 SKVFQYAEMELVDGGSDIDVTIDNVEQYVEKCEEFYLNTGIAYQMRAFRDGFDRVFPLRTLRAYSPEEVQRLLSGEqcPE 2494
Cdd:cd00078    164 SSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGS--ED 241
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513283 2495 WSRDDILNYTEPKLGYTRESPGFLRFVDVMEALTAQERKNFLQFATGCSSLPPGGLANLHPRLTIvRKVESGDGSYPSVN 2574
Cdd:cd00078    242 IDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLNPKFTI-RRVGSPDDRLPTAH 320
                          410       420       430
                   ....*....|....*....|....*....|..
gi 1831513283 2575 TCVHYLKLPEYSSSAILRERLLTAINEK-GFH 2605
Cdd:cd00078    321 TCFNLLKLPPYSSKEILREKLLYAINEGaGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
2203-2604 4.01e-120

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: 383.12  E-value: 4.01e-120
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513283  2203 RKAVLEIEYTNEEG-TGLGPTLEFYALVAAELQRKSLALWVCDDDDTHasksgeerevdlgegkkpigyyvrrvggLFPA 2281
Cdd:smart00119    3 KKRVLEIEFEGEEGlDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYL----------------------------LYPN 54
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513283  2282 PLPPGTDETKRAadMFRVLGVFLAKVLLDGRLVDLPLSRPFLKLLvhpqigddargpnLHKILSLDDFEEVNPVKGSFLK 2361
Cdd:smart00119   55 PRSGFANEEHLS--YFRFIGRVLGKALYDNRLLDLFFARPFYKKL-------------LGKPVTLHDLESLDPELYKSLK 119
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513283  2362 ELralaqrkrLIENDTSidsnskrrkiaelklhikgstcrvEDLALNFTVNPPSKVFQYAEMELVDGGSDIDVTIDNVEQ 2441
Cdd:smart00119  120 WL--------LLNNDTS------------------------EELDLTFSIVLTSEFGQVKVVELKPGGSNIPVTEENKKE 167
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513283  2442 YVEKCEEFYLNTGIAYQMRAFRDGFDRVFPLRTLRAYSPEEVQRLLSGeqCPEWSRDDILNYTEPKLGYTRESPGFLRFV 2521
Cdd:smart00119  168 YVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICG--SPEIDVDDLKSNTEYKGGYSANSQTIKWFW 245
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513283  2522 DVMEALTAQERKNFLQFATGCSSLPPGGLANLHPRLTIVRKVESgDGSYPSVNTCVHYLKLPEYSSSAILRERLLTAINE 2601
Cdd:smart00119  246 EVVESFTNEERRKLLQFVTGSSRLPVGGFAALSPKFTIRKAGSD-DERLPTAHTCFNRLKLPPYSSKEILREKLLLAINE 324

                    ....
gi 1831513283  2602 -KGF 2604
Cdd:smart00119  325 gKGF 328
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
2228-2606 2.29e-84

HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl Terminus.


Pssm-ID: 459880  Cd Length: 304  Bit Score: 279.50  E-value: 2.29e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513283 2228 LVAAELQRKSLALWVCDDDDTHasksgeerevdlgegkkpigyyvrrvggLFPAPLPPGTDETKRAADMFRVLGVFLAKV 2307
Cdd:pfam00632    2 LLSKELFDPNYGLFEYETEDDR----------------------------TYWFNPSSSESPDLELLDYFKFLGKLLGKA 53
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513283 2308 LLDGRLVDLPLSRPFLKLLvhpqigddargpnLHKILSLDDFEEVNPVKGSFLKELRalaqrkrLIENDTsidsnskrrk 2387
Cdd:pfam00632   54 IYNGILLDLPFPPFFYKKL-------------LGEPLTLEDLESIDPELYKSLKSLL-------NMDNDD---------- 103
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513283 2388 iaelklhikgstcrVEDLALNFTVNppskVFQYAEM-ELVDGGSDIDVTIDNVEQYVEKCEEFYLNTGIAYQMRAFRDGF 2466
Cdd:pfam00632  104 --------------DEDLGLTFTIP----VFGESKTiELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQLEAFRKGF 165
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513283 2467 DRVFPLRTLRAYSPEEVQRLLSGEqcPEWSRDDILNYTEPKLGYTRESPGFLRFVDVMEALTAQERKNFLQFATGCSSLP 2546
Cdd:pfam00632  166 YSVIPKEALSLFTPEELELLICGS--PEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGSSRLP 243
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1831513283 2547 PGGLANLhPRLTIVRKVESGDGSYPSVNTCVHYLKLPEYSSSAILRERLLTAINE-KGFHL 2606
Cdd:pfam00632  244 VGGFKSL-PKFTIVRKGGDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEgEGFGL 303
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
2076-2604 3.01e-56

Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 213.09  E-value: 3.01e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513283 2076 FISDKLTLKVTQVLSDALVVAARSLPEWCSRlvyKYPCLFTVETRNMYMQATAFGVSRTIV--WLQQRRDAAVERargsa 2153
Cdd:COG5021    413 TYEDLRREQLGRESDESFYVASNVQQQRASR---EGPLLSGWKTRLNNLYRFYFVEHRKKTltKNDSRLGSFISL----- 484
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513283 2154 qagNSSAARQHDRYHEYRVGRLRHE---------RVKVTRaeETLLDQAIRLMKFHA--DRKAVLEIEYTNEEG-TGLGP 2221
Cdd:COG5021    485 ---NKLDIRRIKEDKRRKLFYSLKQkakifdpylHIKVRR--DRVFEDSYREIMDESgdDLKKTLEIEFVGEEGiDAGGL 559
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513283 2222 TLEFYALVAAELQrkslalwvcDDDDTHAsksgEEREVDLgegkkpigYYvrrvgglFPAPLPPGTDETKRaaDMFRVLG 2301
Cdd:COG5021    560 TREWLFLLSKEMF---------NPDYGLF----EYITEDL--------YT-------LPINPLSSINPEHL--SYFKFLG 609
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513283 2302 VFLAKVLLDGRLVDLPLSRPFLKLLvhpqigddargpnLHKILSLDDFEEVNPVKGSFLKELRalaqrkrlienDTSIDS 2381
Cdd:COG5021    610 RVIGKAIYDSRILDVQFSKAFYKKL-------------LGKPVSLVDLESLDPELYRSLVWLL-----------NNDIDE 665
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513283 2382 NskrrkiaelklhIKGSTCRVEDLALNFTVNppskvfqyaeMELVDGGSDIDVTIDNVEQYVEKCEEFYLNTGIAYQMRA 2461
Cdd:COG5021    666 T------------ILDLTFTVEDDSFGESRT----------VELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSA 723
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513283 2462 FRDGFDRVFPLRTLRAYSPEEVQRLLSGEqcPEWSR-DDILNYTEPKlGYTRESPGFLRFVDVMEALTAQERKNFLQFAT 2540
Cdd:COG5021    724 FKSGFSEIIPPDLLQIFDESELELLIGGI--PEDIDiDDWKSNTAYH-GYTEDSPIIVWFWEIISEFDFEERAKLLQFVT 800
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1831513283 2541 GCSSLPPGGLANLHPRLTIVRKV--ESGDGSY--PSVNTCVHYLKLPEYSSSAILRERLLTAINE-KGF 2604
Cdd:COG5021    801 GTSRIPINGFKDLQGSDGVRKFTieKGGTDDDrlPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEgAGF 869
MIB_HERC2 pfam06701
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain ...
1409-1466 4.45e-24

Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain (either Ring or Hect).


Pssm-ID: 461991  Cd Length: 66  Bit Score: 97.29  E-value: 4.45e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1831513283 1409 SKVVRGKDWRWEDQDGGEGKFGRIT------SPPESGWVDVTWDNGNANSYRFGANGNFDIERV 1466
Cdd:pfam06701    2 ARVVRGPDWKWGDQDGGEGHVGTVVeirdwdSESPRSTVRVQWDNGSTNVYRVGYEGKYDLKVV 65
Sad1_UNC pfam07738
Sad1 / UNC-like C-terminal; The C. elegans UNC-84 protein is a nuclear envelope protein that ...
1200-1322 8.98e-14

Sad1 / UNC-like C-terminal; The C. elegans UNC-84 protein is a nuclear envelope protein that is involved in nuclear anchoring and migration during development. The S. pombe Sad1 protein localizes at the spindle pole body. UNC-84 and and Sad1 share a common C-terminal region, that is often termed the SUN (Sad1 and UNC) domain. In mammals, the SUN domain is present in two proteins, Sun1 and Sun2. The SUN domain of Sun2 has been demonstrated to be in the periplasm.


Pssm-ID: 400199  Cd Length: 130  Bit Score: 70.40  E-value: 8.98e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513283 1200 PEDLLSRDQNPINCHTSDDKNAHFTIDLGLFVVPTSYSLRHSRGYGR-SALRNWMLQGSVDAKRWENVIVhtDDKGLGEP 1278
Cdd:pfam07738    8 PKVILQPDYMPGPCWSFKGSRGFVVIELSEFIIVEAITLEHVEKSVFsSAPKDFEVSGSDRYPTTKWVLL--GEFSYDLD 85
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1831513283 1279 GSTA-TWHVGEKGTTAFRF--FRIAQNGknssGQTHYLSCSGFEIYG 1322
Cdd:pfam07738   86 GKTIqTFQLENPPDIWVKYvkLRILSNY----GNEHYTCLYRFRVHG 128
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
332-416 1.69e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 55.35  E-value: 1.69e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513283  332 YAAGSGAERVHRQLI------DAIRQKDLTALVDAIESGQV-----------DVNFADDVGQSLTNWASAFGSIEM---- 390
Cdd:COG0666    126 LAAYNGNLEIVKLLLeagadvNAQDNDGNTPLHLAAANGNLeivkllleagaDVNARDNDGETPLHLAAENGHLEIvkll 205
                           90       100
                   ....*....|....*....|....*...
gi 1831513283  391 --RGANPDLRDEDGKTALDKARERSDDD 416
Cdd:COG0666    206 leAGADVNAKDNDGKTALDLAAENGNLE 233
 
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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