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Conserved domains on  [gi|1370464784|ref|XP_024305295|]
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E3 ubiquitin-protein ligase HECTD1 isoform X5 [Homo sapiens]

Protein Classification

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 ...
 2070-2547 3.84e-119

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: 381.53  E-value: 3.84e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784 2070 ERVKVPRGESLMEWAENVMQIH-ADRKSVLEVEFLGEEGTG-LGPTLEFYALVAAEFQRTDLGAWLCDDNFpddesrhvd 2147
Cdd:cd00078      1 LKITVRRDRILEDALRQLSKVSsSDLKKVLEVEFVGEEGIDaGGVTREFFTLVSKELFNPSYGLFRYTPDD--------- 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784 2148 lggglkppgyyvqRSCGLFTAPFPQDSDELeritKLFHFLGIFLAKCIQDNRLVDLPISKPFFKLMCmgdiksnmskliy 2227
Cdd:cd00078     72 -------------SGLLYPNPSSFADEDHL----KLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLL------------- 121

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784 2228 esrgdrdlhctesqseasteeghdslsvgsfeedsksefildppkpkppawfNGILTWEDFELVNPHRARFLKEIKDLAI 2307
Cdd:cd00078    122 ----------------------------------------------------GKPLSLEDLEELDPELYKSLKELLDNDG 149

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784 2308 krrqilsnkglsedekntklqelvlknpsgsgpplSIEDLGLNFQFCPSSRIYGFTAVDLKPSGEDEMITMDNAEEYVDL 2387
Cdd:cd00078    150 -----------------------------------DEDDLELTFTIELDSSFGGAVTVELKPGGRDIPVTNENKEEYVDL 194

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784 2388 MFDFCMHTGIQKQMEAFRDGFNKVFPMEKLSSFSHEEVQMILCGNqsPSWAAEDIINYTEPKLGYTRDSPGFLRFVRVLC 2467
Cdd:cd00078    195 YVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGS--EDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLE 272

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784 2468 GMSSDERKAFLQFTTGCSTLPPGGLANLHPRLTvVRKVDATDASYPSVNTCVHYLKLPEYSSEEIMRERLLAATMEK-GF 2546
Cdd:cd00078    273 SFTNEERKKFLQFVTGSSRLPVGGFADLNPKFT-IRRVGSPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGaGF 351


                   .
gi 1370464784 2547 H 2547
Cdd:cd00078    352 G 352
Sad1_UNC pfam07738
Sad1 / UNC-like C-terminal; The C. elegans UNC-84 protein is a nuclear envelope protein that ...
 1107-1240 9.13e-33

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: 124.71  E-value: 9.13e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784 1107 RNLPYGRLEDILSRDNSALNCHSNDDKNAWFAIDLGLWVIPSAYTLRHARGYGR-SALRNWVFQVSKDGQNWTslYTHVD 1185
Cdd:pfam07738    1 LNYEAKPPKVILQPDYMPGPCWSFKGSRGFVVIELSEFIIVEAITLEHVEKSVFsSAPKDFEVSGSDRYPTTK--WVLLG 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370464784 1186 DCSLNEPGSTA-TWPLDPPKDEkqGWRHVR--IKQMGknasGQTHYLSLSGFELYGTV 1240
Cdd:pfam07738   79 EFSYDLDGKTIqTFQLENPPDI--WVKYVKlrILSNY----GNEHYTCLYRFRVHGTV 130
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
366-479 8.25e-26

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 110.04  E-value: 8.25e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784  366 LIDCIRSKDTDALIDAIDTGAfEVNFMDDVGQTLLNWASAFGTQEMVEFLCERGADVNR--GQRSSSLHYAACFGRPQVA 443
Cdd:COG0666     91 LHAAARNGDLEIVKLLLEAGA-DVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAqdNDGNTPLHLAAANGNLEIV 169

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1370464784  444 KTLLRHGANPDLRDEDGKTPLDKARERGHSEVVAIL 479
Cdd:COG0666    170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
MIB_HERC2 pfam06701
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain ...
 1277-1335 1.23e-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: 98.83  E-value: 1.23e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370464784 1277 GARVIRGLDWKWRDQDGSPQGEGTVT------GELHNGWIDVTWDAGGSNSYRMGAEGKFDLKLA 1335
Cdd:pfam06701    1 GARVVRGPDWKWGDQDGGEGHVGTVVeirdwdSESPRSTVRVQWDNGSTNVYRVGYEGKYDLKVV 65
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
 2070-2547 3.84e-119

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: 381.53  E-value: 3.84e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784 2070 ERVKVPRGESLMEWAENVMQIH-ADRKSVLEVEFLGEEGTG-LGPTLEFYALVAAEFQRTDLGAWLCDDNFpddesrhvd 2147
Cdd:cd00078      1 LKITVRRDRILEDALRQLSKVSsSDLKKVLEVEFVGEEGIDaGGVTREFFTLVSKELFNPSYGLFRYTPDD--------- 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784 2148 lggglkppgyyvqRSCGLFTAPFPQDSDELeritKLFHFLGIFLAKCIQDNRLVDLPISKPFFKLMCmgdiksnmskliy 2227
Cdd:cd00078     72 -------------SGLLYPNPSSFADEDHL----KLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLL------------- 121

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784 2228 esrgdrdlhctesqseasteeghdslsvgsfeedsksefildppkpkppawfNGILTWEDFELVNPHRARFLKEIKDLAI 2307
Cdd:cd00078    122 ----------------------------------------------------GKPLSLEDLEELDPELYKSLKELLDNDG 149

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784 2308 krrqilsnkglsedekntklqelvlknpsgsgpplSIEDLGLNFQFCPSSRIYGFTAVDLKPSGEDEMITMDNAEEYVDL 2387
Cdd:cd00078    150 -----------------------------------DEDDLELTFTIELDSSFGGAVTVELKPGGRDIPVTNENKEEYVDL 194

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784 2388 MFDFCMHTGIQKQMEAFRDGFNKVFPMEKLSSFSHEEVQMILCGNqsPSWAAEDIINYTEPKLGYTRDSPGFLRFVRVLC 2467
Cdd:cd00078    195 YVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGS--EDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLE 272

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784 2468 GMSSDERKAFLQFTTGCSTLPPGGLANLHPRLTvVRKVDATDASYPSVNTCVHYLKLPEYSSEEIMRERLLAATMEK-GF 2546
Cdd:cd00078    273 SFTNEERKKFLQFVTGSSRLPVGGFADLNPKFT-IRRVGSPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGaGF 351


                   .
gi 1370464784 2547 H 2547
Cdd:cd00078    352 G 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
 2094-2546 2.43e-89

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: 294.91  E-value: 2.43e-89
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784  2094 RKSVLEVEFLGEEG-TGLGPTLEFYALVAAEFQRTDLGAWLCDDNfpddesrhvdlggglkppgyyvqrSCGLFTAPFPQ 2172
Cdd:smart00119    3 KKRVLEIEFEGEEGlDGGGVTREFFFLLSKELFNPDYGLFRYSPN------------------------DYLLYPNPRSG 58

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784  2173 DSDElERItKLFHFLGIFLAKCIQDNRLVDLPISKPFFKLMCmgdiksnmskliyesrgdrdlhctesqseasteeghds 2252
Cdd:smart00119   59 FANE-EHL-SYFRFIGRVLGKALYDNRLLDLFFARPFYKKLL-------------------------------------- 98

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784  2253 lsvgsfeedsksefildppkpkppawfNGILTWEDFELVNPHRARFLKEIKdlaikrrqilsnkgLSEDEkntklqelvl 2332
Cdd:smart00119   99 ---------------------------GKPVTLHDLESLDPELYKSLKWLL--------------LNNDT---------- 127

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784  2333 knpsgsgpplsIEDLGLNFQFCPSSRIYGFTAVDLKPSGEDEMITMDNAEEYVDLMFDFCMHTGIQKQMEAFRDGFNKVF 2412
Cdd:smart00119  128 -----------SEELDLTFSIVLTSEFGQVKVVELKPGGSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVI 196

                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784  2413 PMEKLSSFSHEEVQMILCGnqSPSWAAEDIINYTEPKLGYTRDSPGFLRFVRVLCGMSSDERKAFLQFTTGCSTLPPGGL 2492
Cdd:smart00119  197 PENLLKLFDPEELELLICG--SPEIDVDDLKSNTEYKGGYSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGF 274

                           410       420       430       440       450
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1370464784  2493 ANLHPRLTvVRKVDATDASYPSVNTCVHYLKLPEYSSEEIMRERLLAATME-KGF 2546
Cdd:smart00119  275 AALSPKFT-IRKAGSDDERLPTAHTCFNRLKLPPYSSKEILREKLLLAINEgKGF 328
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
 2161-2548 1.15e-72

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 245.98  E-value: 1.15e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784 2161 RSCGLFTAPFPQDSDELERItKLFHFLGIFLAKCIQDNRLVDLPISKPFFKLMCmgdiksnmskliyesrgdrdlhctes 2240
Cdd:pfam00632   21 DDRTYWFNPSSSESPDLELL-DYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLL-------------------------- 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784 2241 qseasteeghdslsvgsfeedsksefildppkpkppawfNGILTWEDFELVNPHRARFLKEIKDLaikrrqilsnkglSE 2320
Cdd:pfam00632   74 ---------------------------------------GEPLTLEDLESIDPELYKSLKSLLNM-------------DN 101

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784 2321 DEKntklqelvlknpsgsgpplsiEDLGLNFQFCpssrIYGFTA-VDLKPSGEDEMITMDNAEEYVDLMFDFCMHTGIQK 2399
Cdd:pfam00632  102 DDD---------------------EDLGLTFTIP----VFGESKtIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEP 156

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784 2400 QMEAFRDGFNKVFPMEKLSSFSHEEVQMILCGnqSPSWAAEDIINYTEPKLGYTRDSPGFLRFVRVLCGMSSDERKAFLQ 2479
Cdd:pfam00632  157 QLEAFRKGFYSVIPKEALSLFTPEELELLICG--SPEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLK 234

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784 2480 FTTGCSTLPPGGLANLhPRLTVVRKVDATDASYPSVNTCVHYLKLPEYSSEEIMRERLLAATME-KGFHL 2548
Cdd:pfam00632  235 FVTGSSRLPVGGFKSL-PKFTIVRKGGDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEgEGFGL 303
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
1987-2546 9.29e-55

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 208.47  E-value: 9.29e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784 1987 QIEEPLALASGALPDWCEQLTskcPFLIPFETRQLYFTCTAFgasraivWLQNRREATVERTRTTSSVRRDDPGEFRVGR 2066
Cdd:COG5021    425 ESDESFYVASNVQQQRASREG---PLLSGWKTRLNNLYRFYF-------VEHRKKTLTKNDSRLGSFISLNKLDIRRIKE 494

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784 2067 LKHERVKVprgeSLMEWAENVM---QIHADRKSVLEV---EFLGEEGTGLGPTLEFYALVAAEFQRTDLGAW----LCDD 2136
Cdd:COG5021    495 DKRRKLFY----SLKQKAKIFDpylHIKVRRDRVFEDsyrEIMDESGDDLKKTLEIEFVGEEGIDAGGLTREwlflLSKE 570

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784 2137 NFPDDesrhvdlggglkpPGYYVQRSCGLFTAPFPQDSDELERITKLFHFLGIFLAKCIQDNRLVDLPISKPFFKLMCmg 2216
Cdd:COG5021    571 MFNPD-------------YGLFEYITEDLYTLPINPLSSINPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLL-- 635

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784 2217 diksnmskliyesrgdrdlhctesqseasteeghdslsvgsfeedsksefildppkPKPpawfngiLTWEDFELVNPHRA 2296
Cdd:COG5021    636 --------------------------------------------------------GKP-------VSLVDLESLDPELY 652

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784 2297 RFLKEIKDLaikrrqilsnkglSEDEKNtklqelvlknpsgsgpplsiedLGLNFQFcpSSRIYGFTA-VDLKPSGEDEM 2375
Cdd:COG5021    653 RSLVWLLNN-------------DIDETI----------------------LDLTFTV--EDDSFGESRtVELIPNGRNIS 695

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784 2376 ITMDNAEEYVDLMFDFCMHTGIQKQMEAFRDGFNKVFPMEKLSSFSHEEVQMILCGNQSPSwAAEDIINYTEPKlGYTRD 2455
Cdd:COG5021    696 VTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEDI-DIDDWKSNTAYH-GYTED 773

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784 2456 SPGFLRFVRVLCGMSSDERKAFLQFTTGCSTLPPGGLANLHPRLTVVRKV--DATDASY--PSVNTCVHYLKLPEYSSEE 2531
Cdd:COG5021    774 SPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTieKGGTDDDrlPSAHTCFNRLKLPEYSSKE 853

                          570
                   ....*....|....*.
gi 1370464784 2532 IMRERLLAATME-KGF 2546
Cdd:COG5021    854 KLRSKLLTAINEgAGF 869
Sad1_UNC pfam07738
Sad1 / UNC-like C-terminal; The C. elegans UNC-84 protein is a nuclear envelope protein that ...
 1107-1240 9.13e-33

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: 124.71  E-value: 9.13e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784 1107 RNLPYGRLEDILSRDNSALNCHSNDDKNAWFAIDLGLWVIPSAYTLRHARGYGR-SALRNWVFQVSKDGQNWTslYTHVD 1185
Cdd:pfam07738    1 LNYEAKPPKVILQPDYMPGPCWSFKGSRGFVVIELSEFIIVEAITLEHVEKSVFsSAPKDFEVSGSDRYPTTK--WVLLG 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370464784 1186 DCSLNEPGSTA-TWPLDPPKDEkqGWRHVR--IKQMGknasGQTHYLSLSGFELYGTV 1240
Cdd:pfam07738   79 EFSYDLDGKTIqTFQLENPPDI--WVKYVKlrILSNY----GNEHYTCLYRFRVHGTV 130
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
366-479 8.25e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 110.04  E-value: 8.25e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784  366 LIDCIRSKDTDALIDAIDTGAfEVNFMDDVGQTLLNWASAFGTQEMVEFLCERGADVNR--GQRSSSLHYAACFGRPQVA 443
Cdd:COG0666     91 LHAAARNGDLEIVKLLLEAGA-DVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAqdNDGNTPLHLAAANGNLEIV 169

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1370464784  444 KTLLRHGANPDLRDEDGKTPLDKARERGHSEVVAIL 479
Cdd:COG0666    170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
MIB_HERC2 pfam06701
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain ...
 1277-1335 1.23e-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: 98.83  E-value: 1.23e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370464784 1277 GARVIRGLDWKWRDQDGSPQGEGTVT------GELHNGWIDVTWDAGGSNSYRMGAEGKFDLKLA 1335
Cdd:pfam06701    1 GARVVRGPDWKWGDQDGGEGHVGTVVeirdwdSESPRSTVRVQWDNGSTNVYRVGYEGKYDLKVV 65
Ank_2 pfam12796
Ankyrin repeats (3 copies);
366-457 1.44e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.52  E-value: 1.44e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784  366 LIDCIRSKDTDALIDAIDTGAfEVNFMDDVGQTLLNWASAFGTQEMVEFLCERGADVNRGQRSSSLHYAACFGRPQVAKT 445
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGA-DANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRTALHYAARSGHLEIVKL 79

                           90
                   ....*....|..
gi 1370464784  446 LLRHGANPDLRD 457
Cdd:pfam12796   80 LLEKGADINVKD 91
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 404-481 1.09e-07

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 57.60  E-value: 1.09e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784  404 SAFGTQEMVEFLCERGADVNRG--QRSSSLHYAACFGRPQVAKTLLRHGANPDLRDEDGKTPLDKARERGHSEVVAILQS 481
Cdd:PTZ00322    90 AASGDAVGARILLTGGADPNCRdyDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 396-464 1.49e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 43.85  E-value: 1.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784  396 GQTLLNWASAFGTQEMVEFLCERGADVN---------RGQRSSSLHY-------AACFGRPQVAKTLLRHGANPDLRDED 459
Cdd:cd22192     89 GETALHIAVVNQNLNLVRELIARGADVVspratgtffRPGPKNLIYYgehplsfAACVGNEEIVRLLIEHGADIRAQDSL 168


                   ....*
gi 1370464784  460 GKTPL 464
Cdd:cd22192    169 GNTVL 173
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 1127-1238 3.24e-03

Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached carbohydrate-binding domain, present in eukaryotes and assumed to have horizontally transferred to eubacterial genomes.


Pssm-ID: 238014 [Multi-domain]  Cd Length: 143  Bit Score: 40.41  E-value: 3.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784 1127 CHSNDDKNAWFAIDLGL--WVIPSAYTLRHaRGYGRSALRNWVFQVSKDGQNWTSLYTHVDDCSLN---EPGSTATWPLD 1201
Cdd:cd00057     38 TPAVNDPPQWLQVDLGKtrRVTGIQTQGRK-GGGSSEWVTSYKVQYSLDGETWTTYKDKGEEKVFTgnsDGSTPVTNDFP 116

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1370464784 1202 PPKDEkqgwRHVRIKQMGKNasgqtHYLSLsGFELYG 1238
Cdd:cd00057    117 PPIVA----RYIRILPTTWN-----GNISL-RLELYG 143
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 431-455 6.34e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.41  E-value: 6.34e-03
                            10        20
                    ....*....|....*....|....*
gi 1370464784   431 LHYAACFGRPQVAKTLLRHGANPDL 455
Cdd:smart00248    6 LHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
 2070-2547 3.84e-119

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: 381.53  E-value: 3.84e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784 2070 ERVKVPRGESLMEWAENVMQIH-ADRKSVLEVEFLGEEGTG-LGPTLEFYALVAAEFQRTDLGAWLCDDNFpddesrhvd 2147
Cdd:cd00078      1 LKITVRRDRILEDALRQLSKVSsSDLKKVLEVEFVGEEGIDaGGVTREFFTLVSKELFNPSYGLFRYTPDD--------- 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784 2148 lggglkppgyyvqRSCGLFTAPFPQDSDELeritKLFHFLGIFLAKCIQDNRLVDLPISKPFFKLMCmgdiksnmskliy 2227
Cdd:cd00078     72 -------------SGLLYPNPSSFADEDHL----KLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLL------------- 121

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784 2228 esrgdrdlhctesqseasteeghdslsvgsfeedsksefildppkpkppawfNGILTWEDFELVNPHRARFLKEIKDLAI 2307
Cdd:cd00078    122 ----------------------------------------------------GKPLSLEDLEELDPELYKSLKELLDNDG 149

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784 2308 krrqilsnkglsedekntklqelvlknpsgsgpplSIEDLGLNFQFCPSSRIYGFTAVDLKPSGEDEMITMDNAEEYVDL 2387
Cdd:cd00078    150 -----------------------------------DEDDLELTFTIELDSSFGGAVTVELKPGGRDIPVTNENKEEYVDL 194

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784 2388 MFDFCMHTGIQKQMEAFRDGFNKVFPMEKLSSFSHEEVQMILCGNqsPSWAAEDIINYTEPKLGYTRDSPGFLRFVRVLC 2467
Cdd:cd00078    195 YVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGS--EDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLE 272

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784 2468 GMSSDERKAFLQFTTGCSTLPPGGLANLHPRLTvVRKVDATDASYPSVNTCVHYLKLPEYSSEEIMRERLLAATMEK-GF 2546
Cdd:cd00078    273 SFTNEERKKFLQFVTGSSRLPVGGFADLNPKFT-IRRVGSPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGaGF 351


                   .
gi 1370464784 2547 H 2547
Cdd:cd00078    352 G 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
 2094-2546 2.43e-89

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: 294.91  E-value: 2.43e-89
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784  2094 RKSVLEVEFLGEEG-TGLGPTLEFYALVAAEFQRTDLGAWLCDDNfpddesrhvdlggglkppgyyvqrSCGLFTAPFPQ 2172
Cdd:smart00119    3 KKRVLEIEFEGEEGlDGGGVTREFFFLLSKELFNPDYGLFRYSPN------------------------DYLLYPNPRSG 58

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784  2173 DSDElERItKLFHFLGIFLAKCIQDNRLVDLPISKPFFKLMCmgdiksnmskliyesrgdrdlhctesqseasteeghds 2252
Cdd:smart00119   59 FANE-EHL-SYFRFIGRVLGKALYDNRLLDLFFARPFYKKLL-------------------------------------- 98

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784  2253 lsvgsfeedsksefildppkpkppawfNGILTWEDFELVNPHRARFLKEIKdlaikrrqilsnkgLSEDEkntklqelvl 2332
Cdd:smart00119   99 ---------------------------GKPVTLHDLESLDPELYKSLKWLL--------------LNNDT---------- 127

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784  2333 knpsgsgpplsIEDLGLNFQFCPSSRIYGFTAVDLKPSGEDEMITMDNAEEYVDLMFDFCMHTGIQKQMEAFRDGFNKVF 2412
Cdd:smart00119  128 -----------SEELDLTFSIVLTSEFGQVKVVELKPGGSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVI 196

                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784  2413 PMEKLSSFSHEEVQMILCGnqSPSWAAEDIINYTEPKLGYTRDSPGFLRFVRVLCGMSSDERKAFLQFTTGCSTLPPGGL 2492
Cdd:smart00119  197 PENLLKLFDPEELELLICG--SPEIDVDDLKSNTEYKGGYSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGF 274

                           410       420       430       440       450
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1370464784  2493 ANLHPRLTvVRKVDATDASYPSVNTCVHYLKLPEYSSEEIMRERLLAATME-KGF 2546
Cdd:smart00119  275 AALSPKFT-IRKAGSDDERLPTAHTCFNRLKLPPYSSKEILREKLLLAINEgKGF 328
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
 2161-2548 1.15e-72

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 245.98  E-value: 1.15e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784 2161 RSCGLFTAPFPQDSDELERItKLFHFLGIFLAKCIQDNRLVDLPISKPFFKLMCmgdiksnmskliyesrgdrdlhctes 2240
Cdd:pfam00632   21 DDRTYWFNPSSSESPDLELL-DYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLL-------------------------- 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784 2241 qseasteeghdslsvgsfeedsksefildppkpkppawfNGILTWEDFELVNPHRARFLKEIKDLaikrrqilsnkglSE 2320
Cdd:pfam00632   74 ---------------------------------------GEPLTLEDLESIDPELYKSLKSLLNM-------------DN 101

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784 2321 DEKntklqelvlknpsgsgpplsiEDLGLNFQFCpssrIYGFTA-VDLKPSGEDEMITMDNAEEYVDLMFDFCMHTGIQK 2399
Cdd:pfam00632  102 DDD---------------------EDLGLTFTIP----VFGESKtIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEP 156

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784 2400 QMEAFRDGFNKVFPMEKLSSFSHEEVQMILCGnqSPSWAAEDIINYTEPKLGYTRDSPGFLRFVRVLCGMSSDERKAFLQ 2479
Cdd:pfam00632  157 QLEAFRKGFYSVIPKEALSLFTPEELELLICG--SPEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLK 234

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784 2480 FTTGCSTLPPGGLANLhPRLTVVRKVDATDASYPSVNTCVHYLKLPEYSSEEIMRERLLAATME-KGFHL 2548
Cdd:pfam00632  235 FVTGSSRLPVGGFKSL-PKFTIVRKGGDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEgEGFGL 303
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
1987-2546 9.29e-55

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 208.47  E-value: 9.29e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784 1987 QIEEPLALASGALPDWCEQLTskcPFLIPFETRQLYFTCTAFgasraivWLQNRREATVERTRTTSSVRRDDPGEFRVGR 2066
Cdd:COG5021    425 ESDESFYVASNVQQQRASREG---PLLSGWKTRLNNLYRFYF-------VEHRKKTLTKNDSRLGSFISLNKLDIRRIKE 494

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784 2067 LKHERVKVprgeSLMEWAENVM---QIHADRKSVLEV---EFLGEEGTGLGPTLEFYALVAAEFQRTDLGAW----LCDD 2136
Cdd:COG5021    495 DKRRKLFY----SLKQKAKIFDpylHIKVRRDRVFEDsyrEIMDESGDDLKKTLEIEFVGEEGIDAGGLTREwlflLSKE 570

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784 2137 NFPDDesrhvdlggglkpPGYYVQRSCGLFTAPFPQDSDELERITKLFHFLGIFLAKCIQDNRLVDLPISKPFFKLMCmg 2216
Cdd:COG5021    571 MFNPD-------------YGLFEYITEDLYTLPINPLSSINPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLL-- 635

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784 2217 diksnmskliyesrgdrdlhctesqseasteeghdslsvgsfeedsksefildppkPKPpawfngiLTWEDFELVNPHRA 2296
Cdd:COG5021    636 --------------------------------------------------------GKP-------VSLVDLESLDPELY 652

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784 2297 RFLKEIKDLaikrrqilsnkglSEDEKNtklqelvlknpsgsgpplsiedLGLNFQFcpSSRIYGFTA-VDLKPSGEDEM 2375
Cdd:COG5021    653 RSLVWLLNN-------------DIDETI----------------------LDLTFTV--EDDSFGESRtVELIPNGRNIS 695

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784 2376 ITMDNAEEYVDLMFDFCMHTGIQKQMEAFRDGFNKVFPMEKLSSFSHEEVQMILCGNQSPSwAAEDIINYTEPKlGYTRD 2455
Cdd:COG5021    696 VTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEDI-DIDDWKSNTAYH-GYTED 773

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784 2456 SPGFLRFVRVLCGMSSDERKAFLQFTTGCSTLPPGGLANLHPRLTVVRKV--DATDASY--PSVNTCVHYLKLPEYSSEE 2531
Cdd:COG5021    774 SPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTieKGGTDDDrlPSAHTCFNRLKLPEYSSKE 853

                          570
                   ....*....|....*.
gi 1370464784 2532 IMRERLLAATME-KGF 2546
Cdd:COG5021    854 KLRSKLLTAINEgAGF 869
Sad1_UNC pfam07738
Sad1 / UNC-like C-terminal; The C. elegans UNC-84 protein is a nuclear envelope protein that ...
 1107-1240 9.13e-33

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: 124.71  E-value: 9.13e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784 1107 RNLPYGRLEDILSRDNSALNCHSNDDKNAWFAIDLGLWVIPSAYTLRHARGYGR-SALRNWVFQVSKDGQNWTslYTHVD 1185
Cdd:pfam07738    1 LNYEAKPPKVILQPDYMPGPCWSFKGSRGFVVIELSEFIIVEAITLEHVEKSVFsSAPKDFEVSGSDRYPTTK--WVLLG 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370464784 1186 DCSLNEPGSTA-TWPLDPPKDEkqGWRHVR--IKQMGknasGQTHYLSLSGFELYGTV 1240
Cdd:pfam07738   79 EFSYDLDGKTIqTFQLENPPDI--WVKYVKlrILSNY----GNEHYTCLYRFRVHGTV 130
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
366-479 8.25e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 110.04  E-value: 8.25e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784  366 LIDCIRSKDTDALIDAIDTGAfEVNFMDDVGQTLLNWASAFGTQEMVEFLCERGADVNR--GQRSSSLHYAACFGRPQVA 443
Cdd:COG0666     91 LHAAARNGDLEIVKLLLEAGA-DVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAqdNDGNTPLHLAAANGNLEIV 169

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1370464784  444 KTLLRHGANPDLRDEDGKTPLDKARERGHSEVVAIL 479
Cdd:COG0666    170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
MIB_HERC2 pfam06701
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain ...
 1277-1335 1.23e-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: 98.83  E-value: 1.23e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370464784 1277 GARVIRGLDWKWRDQDGSPQGEGTVT------GELHNGWIDVTWDAGGSNSYRMGAEGKFDLKLA 1335
Cdd:pfam06701    1 GARVVRGPDWKWGDQDGGEGHVGTVVeirdwdSESPRSTVRVQWDNGSTNVYRVGYEGKYDLKVV 65
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
366-480 8.30e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 104.27  E-value: 8.30e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784  366 LIDCIRSKDTDA---LIDAidtGAfEVNFMDDVGQTLLNWASAFGTQEMVEFLCERGADVNRGQRS--SSLHYAACFGRP 440
Cdd:COG0666    124 LHLAAYNGNLEIvklLLEA---GA-DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDgeTPLHLAAENGHL 199

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1370464784  441 QVAKTLLRHGANPDLRDEDGKTPLDKARERGHSEVVAILQ 480
Cdd:COG0666    200 EIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
366-479 3.70e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 93.48  E-value: 3.70e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784  366 LIDCIRSKDTDALIDAIDTGAFEVNFMDDVGQTLLNWASAFGTQEMVEFLCERGADVNR--GQRSSSLHYAACFGRPQVA 443
Cdd:COG0666     57 LLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNArdKDGETPLHLAAYNGNLEIV 136

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1370464784  444 KTLLRHGANPDLRDEDGKTPLDKARERGHSEVVAIL 479
Cdd:COG0666    137 KLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172
Ank_2 pfam12796
Ankyrin repeats (3 copies);
366-457 1.44e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.52  E-value: 1.44e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784  366 LIDCIRSKDTDALIDAIDTGAfEVNFMDDVGQTLLNWASAFGTQEMVEFLCERGADVNRGQRSSSLHYAACFGRPQVAKT 445
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGA-DANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRTALHYAARSGHLEIVKL 79

                           90
                   ....*....|..
gi 1370464784  446 LLRHGANPDLRD 457
Cdd:pfam12796   80 LLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
370-479 3.34e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 69.60  E-value: 3.34e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784  370 IRSKDTDALIDAIDTGAFEVNFMDDVGQTLLNWASAFGTQEMVEFLCERGADVNRG--QRSSSLHYAACFGRPQVAKTLL 447
Cdd:COG0666     28 AALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKddGGNTLLHAAARNGDLEIVKLLL 107

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1370464784  448 RHGANPDLRDEDGKTPLDKARERGHSEVVAIL 479
Cdd:COG0666    108 EAGADVNARDKDGETPLHLAAYNGNLEIVKLL 139
Ank_2 pfam12796
Ankyrin repeats (3 copies);
400-483 1.55e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 59.74  E-value: 1.55e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784  400 LNWASAFGTQEMVEFLCERGADVN--RGQRSSSLHYAACFGRPQVAKTLLRHgANPDLRDeDGKTPLDKARERGHSEVVA 477
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANlqDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78


                   ....*.
gi 1370464784  478 ILQSPG 483
Cdd:pfam12796   79 LLLEKG 84
Ank_4 pfam13637
Ankyrin repeats (many copies);
427-479 9.62e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.74  E-value: 9.62e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1370464784  427 RSSSLHYAACFGRPQVAKTLLRHGANPDLRDEDGKTPLDKARERGHSEVVAIL 479
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 404-481 1.09e-07

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 57.60  E-value: 1.09e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784  404 SAFGTQEMVEFLCERGADVNRG--QRSSSLHYAACFGRPQVAKTLLRHGANPDLRDEDGKTPLDKARERGHSEVVAILQS 481
Cdd:PTZ00322    90 AASGDAVGARILLTGGADPNCRdyDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 370-464 1.32e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 53.73  E-value: 1.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784  370 IRSKDTDALIDA------IDTGAfEVNFMD-DVGQTLLNWASAFGTQEMVEFLCERGADVNRGQR--SSSLHYAACFGRP 440
Cdd:PHA02878   136 IDKKSKDDIIEAeitkllLSYGA-DINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKtnNSPLHHAVKHYNK 214

                           90       100
                   ....*....|....*....|....
gi 1370464784  441 QVAKTLLRHGANPDLRDEDGKTPL 464
Cdd:PHA02878   215 PIVHILLENGASTDARDKCGNTPL 238
PHA03095 PHA03095
ankyrin-like protein; Provisional
 393-477 3.12e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 52.33  E-value: 3.12e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784  393 DDVGQTLLNWASAFGTQE--MVEFLCERGADVN----RGQrsSSLHYAACFGRPQVAKTLLRHGANPDLRDEDGKTPLDK 466
Cdd:PHA03095   219 DMLGNTPLHSMATGSSCKrsLVLPLLIAGISINarnrYGQ--TPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSL 296

                           90
                   ....*....|.
gi 1370464784  467 ARERGHSEVVA 477
Cdd:PHA03095   297 MVRNNNGRAVR 307
Ank_5 pfam13857
Ankyrin repeats (many copies);
418-467 6.80e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.42  E-value: 6.80e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1370464784  418 RGADVNR--GQRSSSLHYAACFGRPQVAKTLLRHGANPDLRDEDGKTPLDKA 467
Cdd:pfam13857    5 GPIDLNRldGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 410-484 1.50e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 50.05  E-value: 1.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784  410 EMVEFLCERGADVN--------------------RGqrSSSLHYAACFGRPQVAKTLLRHGANPDLRDEDGKTPLDKARE 469
Cdd:PHA03100   157 KILKLLIDKGVDINaknrvnyllsygvpinikdvYG--FTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAIL 234

                           90
                   ....*....|....*
gi 1370464784  470 RGHSEVVAILQSPGD 484
Cdd:PHA03100   235 NNNKEIFKLLLNNGP 249
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 391-483 2.57e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 49.22  E-value: 2.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784  391 FMDDV----GQTLLNWASAFGTQEMVEFLCERGAD--VNRGQRSSSLHYAACFGRPQVAKTLLRHGANPDLRDEDGKTPL 464
Cdd:PHA02875    93 FADDVfykdGMTPLHLATILKKLDIMKLLIARGADpdIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPL 172

                           90
                   ....*....|....*....
gi 1370464784  465 DKARERGHSEVVAILQSPG 483
Cdd:PHA02875   173 IIAMAKGDIAICKMLLDSG 191
F5_F8_type_C pfam00754
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.
 1127-1216 3.89e-05

F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.


Pssm-ID: 459925 [Multi-domain]  Cd Length: 127  Bit Score: 45.52  E-value: 3.89e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784 1127 CHSNDDKNAWFAIDLGlwvipSAYTLRHARGYGRSALRN-----WVFQVSKDGQNWTSLYTHVDDcSLNEPGSTATWPLD 1201
Cdd:pfam00754   27 SAWSGDDPQWIQVDLG-----KPKKITGVVTQGRQDGSNgyvtsYKIEYSLDGENWTTVKDEKIP-GNNDNNTPVTNTFD 100

                           90
                   ....*....|....*
gi 1370464784 1202 PPKDEkqgwRHVRIK 1216
Cdd:pfam00754  101 PPIKA----RYVRIV 111
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 410-464 9.94e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 45.97  E-value: 9.94e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370464784  410 EMVEFLCERGADVN---RGQRSSSLHYAACFGR---PQVAKTLLRHGANPDLRDEDGKTPL 464
Cdd:PHA02859    67 EILKFLIENGADVNfktRDNNLSALHHYLSFNKnvePEILKILIDSGSSITEEDEDGKNLL 127
PHA03095 PHA03095
ankyrin-like protein; Provisional
 408-465 1.91e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.56  E-value: 1.91e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370464784  408 TQEMVEFLCERGADVNR--GQRSSSLH-YAACFG-RPQVAKTLLRHGANPDLRDEDGKTPLD 465
Cdd:PHA03095    96 TLDVIKLLIKAGADVNAkdKVGRTPLHvYLSGFNiNPKVIRLLLRKGADVNALDLYGMTPLA 157
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 410-479 6.29e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 44.87  E-value: 6.29e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370464784  410 EMVEFLCERGADVNRGQR---SSSLHYAACFGRPQVAKTLLRHGANPDLRDEDGKTPLDKARERGHSEVVAIL 479
Cdd:PHA02878   148 EITKLLLSYGADINMKDRhkgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHIL 220
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 431-458 1.10e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.42  E-value: 1.10e-03
                           10        20
                   ....*....|....*....|....*....
gi 1370464784  431 LHYAAC-FGRPQVAKTLLRHGANPDLRDE 458
Cdd:pfam00023    6 LHLAAGrRGNLEIVKLLLSKGADVNARDK 34
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 396-464 1.49e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 43.85  E-value: 1.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784  396 GQTLLNWASAFGTQEMVEFLCERGADVN---------RGQRSSSLHY-------AACFGRPQVAKTLLRHGANPDLRDED 459
Cdd:cd22192     89 GETALHIAVVNQNLNLVRELIARGADVVspratgtffRPGPKNLIYYgehplsfAACVGNEEIVRLLIEHGADIRAQDSL 168


                   ....*
gi 1370464784  460 GKTPL 464
Cdd:cd22192    169 GNTVL 173
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 370-467 1.68e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 43.41  E-value: 1.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784  370 IRSKDTDALIDAIDTGAfEVNFMDDVGQTLLNWASAFGTQEMVEFLCERGA--DVNRGQRSSSLHYAACFGRPQVAKTLL 447
Cdd:PHA02874   132 IKKGDLESIKMLFEYGA-DVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAyaNVKDNNGESPLHNAAEYGDYACIKLLI 210

                           90       100
                   ....*....|....*....|
gi 1370464784  448 RHGANPDLRDEDGKTPLDKA 467
Cdd:PHA02874   211 DHGNHIMNKCKNGFTPLHNA 230
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 409-486 2.82e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 42.64  E-value: 2.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784  409 QEMVEFLCERGADVNRGQRSSS--LHYAACFGRPQVAKTLLRHGANPDLRDEDGKTPLDKARERGHSEVVAILQSPGDWM 486
Cdd:PHA02874   104 KDMIKTILDCGIDVNIKDAELKtfLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYA 183
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 1127-1238 3.24e-03

Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached carbohydrate-binding domain, present in eukaryotes and assumed to have horizontally transferred to eubacterial genomes.


Pssm-ID: 238014 [Multi-domain]  Cd Length: 143  Bit Score: 40.41  E-value: 3.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784 1127 CHSNDDKNAWFAIDLGL--WVIPSAYTLRHaRGYGRSALRNWVFQVSKDGQNWTSLYTHVDDCSLN---EPGSTATWPLD 1201
Cdd:cd00057     38 TPAVNDPPQWLQVDLGKtrRVTGIQTQGRK-GGGSSEWVTSYKVQYSLDGETWTTYKDKGEEKVFTgnsDGSTPVTNDFP 116

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1370464784 1202 PPKDEkqgwRHVRIKQMGKNasgqtHYLSLsGFELYG 1238
Cdd:cd00057    117 PPIVA----RYIRILPTTWN-----GNISL-RLELYG 143
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 431-455 6.34e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.41  E-value: 6.34e-03
                            10        20
                    ....*....|....*....|....*
gi 1370464784   431 LHYAACFGRPQVAKTLLRHGANPDL 455
Cdd:smart00248    6 LHLAAENGNLEVVKLLLDKGADINA 30
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 403-487 9.39e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.39  E-value: 9.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370464784  403 ASAFGTQEMVEFLCERG--ADVNRGQRSSSLHYAACFGRPQVAKTLLRHGANPDLRDEDGKTPLDKARERGHSEVVAIL- 479
Cdd:PLN03192   532 VASTGNAALLEELLKAKldPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILy 611

                           90
                   ....*....|....*.
gi 1370464784  480 --------QSPGDWMC 487
Cdd:PLN03192   612 hfasisdpHAAGDLLC 627
 
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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