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Conserved domains on  [gi|1831513289|ref|NP_001368366|]
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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 ...
2184-2611 3.78e-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: 3.78e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513289 2184 ERVKVTRaeETLLDQAIRLMKFHA--DRKAVLEIEYTNEEGTG-LGPTLEFYALVAAELQRKSLALWVCDDDDTHasksg 2260
Cdd:cd00078      1 LKITVRR--DRILEDALRQLSKVSssDLKKVLEVEFVGEEGIDaGGVTREFFTLVSKELFNPSYGLFRYTPDDSG----- 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513289 2261 eerevdlgegkkpigyyvrrvgGLFPAPLPPGTDETKraaDMFRVLGVFLAKVLLDGRLVDLPLSRPFLKLLvhpqigdd 2340
Cdd:cd00078     74 ----------------------LLYPNPSSFADEDHL---KLFRFLGRLLGKALYEGRLLDLPFSRAFYKKL-------- 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513289 2341 argpnLHKILSLDDFEEVNPVKGSFLKELRALAQRkrliendtsidsnskrrkiaelklhikgstcrVEDLALNFTVNPP 2420
Cdd:cd00078    121 -----LGKPLSLEDLEELDPELYKSLKELLDNDGD--------------------------------EDDLELTFTIELD 163
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513289 2421 SKVFQYAEMELVDGGSDIDVTIDNVEQYVEKCEEFYLNTGIAYQMRAFRDGFDRVFPLRTLRAYSPEEVQRLLSGEqcPE 2500
Cdd:cd00078    164 SSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGS--ED 241
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513289 2501 WSRDDILNYTEPKLGYTRESPGFLRFVDVMEALTAQERKNFLQFATGCSSLPPGGLANLHPRLTIvRKVESGDGSYPSVN 2580
Cdd:cd00078    242 IDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLNPKFTI-RRVGSPDDRLPTAH 320
                          410       420       430
                   ....*....|....*....|....*....|..
gi 1831513289 2581 TCVHYLKLPEYSSSAILRERLLTAINEK-GFH 2611
Cdd:cd00078    321 TCFNLLKLPPYSSKEILREKLLYAINEGaGFG 352
MIB_HERC2 pfam06701
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain ...
1415-1472 4.46e-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: 4.46e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1831513289 1415 SKVVRGKDWRWEDQDGGEGKFGRIT------SPPESGWVDVTWDNGNANSYRFGANGNFDIERV 1472
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 ...
1206-1328 9.00e-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: 9.00e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513289 1206 PEDLLSRDQNPINCHTSDDKNAHFTIDLGLFVVPTSYSLRHSRGYGR-SALRNWMLQGSVDAKRWENVIVhtDDKGLGEP 1284
Cdd:pfam07738    8 PKVILQPDYMPGPCWSFKGSRGFVVIELSEFIIVEAITLEHVEKSVFsSAPKDFEVSGSDRYPTTKWVLL--GEFSYDLD 85
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1831513289 1285 GSTA-TWHVGEKGTTAFRF--FRIAQNGknssGQTHYLSCSGFEIYG 1328
Cdd:pfam07738   86 GKTIqTFQLENPPDIWVKYvkLRILSNY----GNEHYTCLYRFRVHG 128
ANKYR super family cl34000
Ankyrin repeat [Signal transduction mechanisms];
332-416 1.70e-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: 1.70e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513289  332 YAAGSGAERVHRQLI------DAIRQKDLTALVDAIESGQV-----------DVNFADDVGQSLTNWASAFGSIEM---- 390
Cdd:COG0666    126 LAAYNGNLEIVKLLLeagadvNAQDNDGNTPLHLAAANGNLeivkllleagaDVNARDNDGETPLHLAAENGHLEIvkll 205
                           90       100
                   ....*....|....*....|....*...
gi 1831513289  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 ...
2184-2611 3.78e-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: 3.78e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513289 2184 ERVKVTRaeETLLDQAIRLMKFHA--DRKAVLEIEYTNEEGTG-LGPTLEFYALVAAELQRKSLALWVCDDDDTHasksg 2260
Cdd:cd00078      1 LKITVRR--DRILEDALRQLSKVSssDLKKVLEVEFVGEEGIDaGGVTREFFTLVSKELFNPSYGLFRYTPDDSG----- 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513289 2261 eerevdlgegkkpigyyvrrvgGLFPAPLPPGTDETKraaDMFRVLGVFLAKVLLDGRLVDLPLSRPFLKLLvhpqigdd 2340
Cdd:cd00078     74 ----------------------LLYPNPSSFADEDHL---KLFRFLGRLLGKALYEGRLLDLPFSRAFYKKL-------- 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513289 2341 argpnLHKILSLDDFEEVNPVKGSFLKELRALAQRkrliendtsidsnskrrkiaelklhikgstcrVEDLALNFTVNPP 2420
Cdd:cd00078    121 -----LGKPLSLEDLEELDPELYKSLKELLDNDGD--------------------------------EDDLELTFTIELD 163
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513289 2421 SKVFQYAEMELVDGGSDIDVTIDNVEQYVEKCEEFYLNTGIAYQMRAFRDGFDRVFPLRTLRAYSPEEVQRLLSGEqcPE 2500
Cdd:cd00078    164 SSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGS--ED 241
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513289 2501 WSRDDILNYTEPKLGYTRESPGFLRFVDVMEALTAQERKNFLQFATGCSSLPPGGLANLHPRLTIvRKVESGDGSYPSVN 2580
Cdd:cd00078    242 IDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLNPKFTI-RRVGSPDDRLPTAH 320
                          410       420       430
                   ....*....|....*....|....*....|..
gi 1831513289 2581 TCVHYLKLPEYSSSAILRERLLTAINEK-GFH 2611
Cdd:cd00078    321 TCFNLLKLPPYSSKEILREKLLYAINEGaGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
2209-2610 4.02e-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: 4.02e-120
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513289  2209 RKAVLEIEYTNEEG-TGLGPTLEFYALVAAELQRKSLALWVCDDDDTHasksgeerevdlgegkkpigyyvrrvggLFPA 2287
Cdd:smart00119    3 KKRVLEIEFEGEEGlDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYL----------------------------LYPN 54
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513289  2288 PLPPGTDETKRAadMFRVLGVFLAKVLLDGRLVDLPLSRPFLKLLvhpqigddargpnLHKILSLDDFEEVNPVKGSFLK 2367
Cdd:smart00119   55 PRSGFANEEHLS--YFRFIGRVLGKALYDNRLLDLFFARPFYKKL-------------LGKPVTLHDLESLDPELYKSLK 119
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513289  2368 ELralaqrkrLIENDTSidsnskrrkiaelklhikgstcrvEDLALNFTVNPPSKVFQYAEMELVDGGSDIDVTIDNVEQ 2447
Cdd:smart00119  120 WL--------LLNNDTS------------------------EELDLTFSIVLTSEFGQVKVVELKPGGSNIPVTEENKKE 167
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513289  2448 YVEKCEEFYLNTGIAYQMRAFRDGFDRVFPLRTLRAYSPEEVQRLLSGeqCPEWSRDDILNYTEPKLGYTRESPGFLRFV 2527
Cdd:smart00119  168 YVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICG--SPEIDVDDLKSNTEYKGGYSANSQTIKWFW 245
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513289  2528 DVMEALTAQERKNFLQFATGCSSLPPGGLANLHPRLTIVRKVESgDGSYPSVNTCVHYLKLPEYSSSAILRERLLTAINE 2607
Cdd:smart00119  246 EVVESFTNEERRKLLQFVTGSSRLPVGGFAALSPKFTIRKAGSD-DERLPTAHTCFNRLKLPPYSSKEILREKLLLAINE 324

                    ....
gi 1831513289  2608 -KGF 2610
Cdd:smart00119  325 gKGF 328
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
2234-2612 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 1831513289 2234 LVAAELQRKSLALWVCDDDDTHasksgeerevdlgegkkpigyyvrrvggLFPAPLPPGTDETKRAADMFRVLGVFLAKV 2313
Cdd:pfam00632    2 LLSKELFDPNYGLFEYETEDDR----------------------------TYWFNPSSSESPDLELLDYFKFLGKLLGKA 53
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513289 2314 LLDGRLVDLPLSRPFLKLLvhpqigddargpnLHKILSLDDFEEVNPVKGSFLKELRalaqrkrLIENDTsidsnskrrk 2393
Cdd:pfam00632   54 IYNGILLDLPFPPFFYKKL-------------LGEPLTLEDLESIDPELYKSLKSLL-------NMDNDD---------- 103
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513289 2394 iaelklhikgstcrVEDLALNFTVNppskVFQYAEM-ELVDGGSDIDVTIDNVEQYVEKCEEFYLNTGIAYQMRAFRDGF 2472
Cdd:pfam00632  104 --------------DEDLGLTFTIP----VFGESKTiELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQLEAFRKGF 165
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513289 2473 DRVFPLRTLRAYSPEEVQRLLSGEqcPEWSRDDILNYTEPKLGYTRESPGFLRFVDVMEALTAQERKNFLQFATGCSSLP 2552
Cdd:pfam00632  166 YSVIPKEALSLFTPEELELLICGS--PEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGSSRLP 243
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1831513289 2553 PGGLANLhPRLTIVRKVESGDGSYPSVNTCVHYLKLPEYSSSAILRERLLTAINE-KGFHL 2612
Cdd:pfam00632  244 VGGFKSL-PKFTIVRKGGDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEgEGFGL 303
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
2082-2610 3.02e-56

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 213.09  E-value: 3.02e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513289 2082 FISDKLTLKVTQVLSDALVVAARSLPEWCSRlvyKYPCLFTVETRNMYMQATAFGVSRTIV--WLQQRRDAAVERargsa 2159
Cdd:COG5021    413 TYEDLRREQLGRESDESFYVASNVQQQRASR---EGPLLSGWKTRLNNLYRFYFVEHRKKTltKNDSRLGSFISL----- 484
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513289 2160 qagNSSAARQHDRYHEYRVGRLRHE---------RVKVTRaeETLLDQAIRLMKFHA--DRKAVLEIEYTNEEG-TGLGP 2227
Cdd:COG5021    485 ---NKLDIRRIKEDKRRKLFYSLKQkakifdpylHIKVRR--DRVFEDSYREIMDESgdDLKKTLEIEFVGEEGiDAGGL 559
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513289 2228 TLEFYALVAAELQrkslalwvcDDDDTHAsksgEEREVDLgegkkpigYYvrrvgglFPAPLPPGTDETKRaaDMFRVLG 2307
Cdd:COG5021    560 TREWLFLLSKEMF---------NPDYGLF----EYITEDL--------YT-------LPINPLSSINPEHL--SYFKFLG 609
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513289 2308 VFLAKVLLDGRLVDLPLSRPFLKLLvhpqigddargpnLHKILSLDDFEEVNPVKGSFLKELRalaqrkrlienDTSIDS 2387
Cdd:COG5021    610 RVIGKAIYDSRILDVQFSKAFYKKL-------------LGKPVSLVDLESLDPELYRSLVWLL-----------NNDIDE 665
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513289 2388 NskrrkiaelklhIKGSTCRVEDLALNFTVNppskvfqyaeMELVDGGSDIDVTIDNVEQYVEKCEEFYLNTGIAYQMRA 2467
Cdd:COG5021    666 T------------ILDLTFTVEDDSFGESRT----------VELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSA 723
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513289 2468 FRDGFDRVFPLRTLRAYSPEEVQRLLSGEqcPEWSR-DDILNYTEPKlGYTRESPGFLRFVDVMEALTAQERKNFLQFAT 2546
Cdd:COG5021    724 FKSGFSEIIPPDLLQIFDESELELLIGGI--PEDIDiDDWKSNTAYH-GYTEDSPIIVWFWEIISEFDFEERAKLLQFVT 800
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1831513289 2547 GCSSLPPGGLANLHPRLTIVRKV--ESGDGSY--PSVNTCVHYLKLPEYSSSAILRERLLTAINE-KGF 2610
Cdd:COG5021    801 GTSRIPINGFKDLQGSDGVRKFTieKGGTDDDrlPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEgAGF 869
MIB_HERC2 pfam06701
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain ...
1415-1472 4.46e-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: 4.46e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1831513289 1415 SKVVRGKDWRWEDQDGGEGKFGRIT------SPPESGWVDVTWDNGNANSYRFGANGNFDIERV 1472
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 ...
1206-1328 9.00e-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: 9.00e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513289 1206 PEDLLSRDQNPINCHTSDDKNAHFTIDLGLFVVPTSYSLRHSRGYGR-SALRNWMLQGSVDAKRWENVIVhtDDKGLGEP 1284
Cdd:pfam07738    8 PKVILQPDYMPGPCWSFKGSRGFVVIELSEFIIVEAITLEHVEKSVFsSAPKDFEVSGSDRYPTTKWVLL--GEFSYDLD 85
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1831513289 1285 GSTA-TWHVGEKGTTAFRF--FRIAQNGknssGQTHYLSCSGFEIYG 1328
Cdd:pfam07738   86 GKTIqTFQLENPPDIWVKYvkLRILSNY----GNEHYTCLYRFRVHG 128
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
332-416 1.70e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 55.35  E-value: 1.70e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513289  332 YAAGSGAERVHRQLI------DAIRQKDLTALVDAIESGQV-----------DVNFADDVGQSLTNWASAFGSIEM---- 390
Cdd:COG0666    126 LAAYNGNLEIVKLLLeagadvNAQDNDGNTPLHLAAANGNLeivkllleagaDVNARDNDGETPLHLAAENGHLEIvkll 205
                           90       100
                   ....*....|....*....|....*...
gi 1831513289  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 ...
2184-2611 3.78e-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: 3.78e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513289 2184 ERVKVTRaeETLLDQAIRLMKFHA--DRKAVLEIEYTNEEGTG-LGPTLEFYALVAAELQRKSLALWVCDDDDTHasksg 2260
Cdd:cd00078      1 LKITVRR--DRILEDALRQLSKVSssDLKKVLEVEFVGEEGIDaGGVTREFFTLVSKELFNPSYGLFRYTPDDSG----- 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513289 2261 eerevdlgegkkpigyyvrrvgGLFPAPLPPGTDETKraaDMFRVLGVFLAKVLLDGRLVDLPLSRPFLKLLvhpqigdd 2340
Cdd:cd00078     74 ----------------------LLYPNPSSFADEDHL---KLFRFLGRLLGKALYEGRLLDLPFSRAFYKKL-------- 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513289 2341 argpnLHKILSLDDFEEVNPVKGSFLKELRALAQRkrliendtsidsnskrrkiaelklhikgstcrVEDLALNFTVNPP 2420
Cdd:cd00078    121 -----LGKPLSLEDLEELDPELYKSLKELLDNDGD--------------------------------EDDLELTFTIELD 163
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513289 2421 SKVFQYAEMELVDGGSDIDVTIDNVEQYVEKCEEFYLNTGIAYQMRAFRDGFDRVFPLRTLRAYSPEEVQRLLSGEqcPE 2500
Cdd:cd00078    164 SSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGS--ED 241
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513289 2501 WSRDDILNYTEPKLGYTRESPGFLRFVDVMEALTAQERKNFLQFATGCSSLPPGGLANLHPRLTIvRKVESGDGSYPSVN 2580
Cdd:cd00078    242 IDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLNPKFTI-RRVGSPDDRLPTAH 320
                          410       420       430
                   ....*....|....*....|....*....|..
gi 1831513289 2581 TCVHYLKLPEYSSSAILRERLLTAINEK-GFH 2611
Cdd:cd00078    321 TCFNLLKLPPYSSKEILREKLLYAINEGaGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
2209-2610 4.02e-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: 4.02e-120
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513289  2209 RKAVLEIEYTNEEG-TGLGPTLEFYALVAAELQRKSLALWVCDDDDTHasksgeerevdlgegkkpigyyvrrvggLFPA 2287
Cdd:smart00119    3 KKRVLEIEFEGEEGlDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYL----------------------------LYPN 54
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513289  2288 PLPPGTDETKRAadMFRVLGVFLAKVLLDGRLVDLPLSRPFLKLLvhpqigddargpnLHKILSLDDFEEVNPVKGSFLK 2367
Cdd:smart00119   55 PRSGFANEEHLS--YFRFIGRVLGKALYDNRLLDLFFARPFYKKL-------------LGKPVTLHDLESLDPELYKSLK 119
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513289  2368 ELralaqrkrLIENDTSidsnskrrkiaelklhikgstcrvEDLALNFTVNPPSKVFQYAEMELVDGGSDIDVTIDNVEQ 2447
Cdd:smart00119  120 WL--------LLNNDTS------------------------EELDLTFSIVLTSEFGQVKVVELKPGGSNIPVTEENKKE 167
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513289  2448 YVEKCEEFYLNTGIAYQMRAFRDGFDRVFPLRTLRAYSPEEVQRLLSGeqCPEWSRDDILNYTEPKLGYTRESPGFLRFV 2527
Cdd:smart00119  168 YVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICG--SPEIDVDDLKSNTEYKGGYSANSQTIKWFW 245
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513289  2528 DVMEALTAQERKNFLQFATGCSSLPPGGLANLHPRLTIVRKVESgDGSYPSVNTCVHYLKLPEYSSSAILRERLLTAINE 2607
Cdd:smart00119  246 EVVESFTNEERRKLLQFVTGSSRLPVGGFAALSPKFTIRKAGSD-DERLPTAHTCFNRLKLPPYSSKEILREKLLLAINE 324

                    ....
gi 1831513289  2608 -KGF 2610
Cdd:smart00119  325 gKGF 328
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
2234-2612 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 1831513289 2234 LVAAELQRKSLALWVCDDDDTHasksgeerevdlgegkkpigyyvrrvggLFPAPLPPGTDETKRAADMFRVLGVFLAKV 2313
Cdd:pfam00632    2 LLSKELFDPNYGLFEYETEDDR----------------------------TYWFNPSSSESPDLELLDYFKFLGKLLGKA 53
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513289 2314 LLDGRLVDLPLSRPFLKLLvhpqigddargpnLHKILSLDDFEEVNPVKGSFLKELRalaqrkrLIENDTsidsnskrrk 2393
Cdd:pfam00632   54 IYNGILLDLPFPPFFYKKL-------------LGEPLTLEDLESIDPELYKSLKSLL-------NMDNDD---------- 103
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513289 2394 iaelklhikgstcrVEDLALNFTVNppskVFQYAEM-ELVDGGSDIDVTIDNVEQYVEKCEEFYLNTGIAYQMRAFRDGF 2472
Cdd:pfam00632  104 --------------DEDLGLTFTIP----VFGESKTiELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQLEAFRKGF 165
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513289 2473 DRVFPLRTLRAYSPEEVQRLLSGEqcPEWSRDDILNYTEPKLGYTRESPGFLRFVDVMEALTAQERKNFLQFATGCSSLP 2552
Cdd:pfam00632  166 YSVIPKEALSLFTPEELELLICGS--PEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGSSRLP 243
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1831513289 2553 PGGLANLhPRLTIVRKVESGDGSYPSVNTCVHYLKLPEYSSSAILRERLLTAINE-KGFHL 2612
Cdd:pfam00632  244 VGGFKSL-PKFTIVRKGGDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEgEGFGL 303
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
2082-2610 3.02e-56

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 213.09  E-value: 3.02e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513289 2082 FISDKLTLKVTQVLSDALVVAARSLPEWCSRlvyKYPCLFTVETRNMYMQATAFGVSRTIV--WLQQRRDAAVERargsa 2159
Cdd:COG5021    413 TYEDLRREQLGRESDESFYVASNVQQQRASR---EGPLLSGWKTRLNNLYRFYFVEHRKKTltKNDSRLGSFISL----- 484
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513289 2160 qagNSSAARQHDRYHEYRVGRLRHE---------RVKVTRaeETLLDQAIRLMKFHA--DRKAVLEIEYTNEEG-TGLGP 2227
Cdd:COG5021    485 ---NKLDIRRIKEDKRRKLFYSLKQkakifdpylHIKVRR--DRVFEDSYREIMDESgdDLKKTLEIEFVGEEGiDAGGL 559
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513289 2228 TLEFYALVAAELQrkslalwvcDDDDTHAsksgEEREVDLgegkkpigYYvrrvgglFPAPLPPGTDETKRaaDMFRVLG 2307
Cdd:COG5021    560 TREWLFLLSKEMF---------NPDYGLF----EYITEDL--------YT-------LPINPLSSINPEHL--SYFKFLG 609
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513289 2308 VFLAKVLLDGRLVDLPLSRPFLKLLvhpqigddargpnLHKILSLDDFEEVNPVKGSFLKELRalaqrkrlienDTSIDS 2387
Cdd:COG5021    610 RVIGKAIYDSRILDVQFSKAFYKKL-------------LGKPVSLVDLESLDPELYRSLVWLL-----------NNDIDE 665
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513289 2388 NskrrkiaelklhIKGSTCRVEDLALNFTVNppskvfqyaeMELVDGGSDIDVTIDNVEQYVEKCEEFYLNTGIAYQMRA 2467
Cdd:COG5021    666 T------------ILDLTFTVEDDSFGESRT----------VELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSA 723
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513289 2468 FRDGFDRVFPLRTLRAYSPEEVQRLLSGEqcPEWSR-DDILNYTEPKlGYTRESPGFLRFVDVMEALTAQERKNFLQFAT 2546
Cdd:COG5021    724 FKSGFSEIIPPDLLQIFDESELELLIGGI--PEDIDiDDWKSNTAYH-GYTEDSPIIVWFWEIISEFDFEERAKLLQFVT 800
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1831513289 2547 GCSSLPPGGLANLHPRLTIVRKV--ESGDGSY--PSVNTCVHYLKLPEYSSSAILRERLLTAINE-KGF 2610
Cdd:COG5021    801 GTSRIPINGFKDLQGSDGVRKFTieKGGTDDDrlPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEgAGF 869
MIB_HERC2 pfam06701
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain ...
1415-1472 4.46e-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: 4.46e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1831513289 1415 SKVVRGKDWRWEDQDGGEGKFGRIT------SPPESGWVDVTWDNGNANSYRFGANGNFDIERV 1472
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 ...
1206-1328 9.00e-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: 9.00e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513289 1206 PEDLLSRDQNPINCHTSDDKNAHFTIDLGLFVVPTSYSLRHSRGYGR-SALRNWMLQGSVDAKRWENVIVhtDDKGLGEP 1284
Cdd:pfam07738    8 PKVILQPDYMPGPCWSFKGSRGFVVIELSEFIIVEAITLEHVEKSVFsSAPKDFEVSGSDRYPTTKWVLL--GEFSYDLD 85
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1831513289 1285 GSTA-TWHVGEKGTTAFRF--FRIAQNGknssGQTHYLSCSGFEIYG 1328
Cdd:pfam07738   86 GKTIqTFQLENPPDIWVKYvkLRILSNY----GNEHYTCLYRFRVHG 128
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
332-416 1.70e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 55.35  E-value: 1.70e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513289  332 YAAGSGAERVHRQLI------DAIRQKDLTALVDAIESGQV-----------DVNFADDVGQSLTNWASAFGSIEM---- 390
Cdd:COG0666    126 LAAYNGNLEIVKLLLeagadvNAQDNDGNTPLHLAAANGNLeivkllleagaDVNARDNDGETPLHLAAENGHLEIvkll 205
                           90       100
                   ....*....|....*....|....*...
gi 1831513289  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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