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Conserved domains on  [gi|688594783|ref|XP_009291389|]
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E3 ubiquitin-protein ligase HECTD1 isoform X4 [Danio rerio]

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 ...
 2045-2522 7.43e-115

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: 369.20  E-value: 7.43e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783 2045 ERVKVPRGESMMEWAESVMQIH-ADRKSVLEVEFQGEEGTG-LGPTLEFYALVAAEFQRTSLGIWLCDDDFpddesrqvd 2122
Cdd:cd00078     1 LKITVRRDRILEDALRQLSKVSsSDLKKVLEVEFVGEEGIDaGGVTREFFTLVSKELFNPSYGLFRYTPDD--------- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783 2123 lggglkppgyyvqRSCGLFPAPFPQDSDELeritKLFLFLGIFLAKCIQDNRLVDLPISQPFFKLLCmgdiksnmsklly 2202
Cdd:cd00078    72 -------------SGLLYPNPSSFADEDHL----KLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLL------------- 121

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783 2203 qtrgesdchfseiqseasteegqdtysvgsfdedsksefildppkpkppawyHGILTWEDFELVNPHRALFLKELKALSV 2282
Cdd:cd00078   122 ----------------------------------------------------GKPLSLEDLEELDPELYKSLKELLDNDG 149

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783 2283 KrrqilgnkslsedekntrlqdlmlknpmgsgpplcVEDLGLNFQFCPSSKVHGFSSVDLKPNGEDEMVTMDNAEEYVEL 2362
Cdd:cd00078   150 D-----------------------------------EDDLELTFTIELDSSFGGAVTVELKPGGRDIPVTNENKEEYVDL 194

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783 2363 MFDFCMHTGIQKQMEAFREGFNKVFPMEKLSSFSHKEVQMILCGNqsPSWTAEDIVNYTEPKLGYTRDSPGFLRFVRVLC 2442
Cdd:cd00078   195 YVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGS--EDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLE 272

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783 2443 GMSSDERKAFLQFTTGCSTLPPGGLANLHPRLTIvRKVDATDASYPSVNTCVHYLKLPEYSSEEIMRERLLAATMEK-GF 2521
Cdd:cd00078   273 SFTNEERKKFLQFVTGSSRLPVGGFADLNPKFTI-RRVGSPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGaGF 351


                  .
gi 688594783 2522 H 2522
Cdd:cd00078   352 G 352
Sad1_UNC super family cl23730
Sad1 / UNC-like C-terminal; The C. elegans UNC-84 protein is a nuclear envelope protein that ...
 1107-1240 1.18e-26

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: 106.99  E-value: 1.18e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783  1107 RNLPYGRLEDILSRDSSALNCHTNDDKNAWFAIDLGLWFVPSAYTLRHARGYGR-SALRNWVFQVSKDGQNWmtLYTHVD 1185
Cdd:pfam07738    1 LNYEAKPPKVILQPDYMPGPCWSFKGSRGFVVIELSEFIIVEAITLEHVEKSVFsSAPKDFEVSGSDRYPTT--KWVLLG 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 688594783  1186 DSSLNEPGSTA-TWPLDPSKDEkqGWRH--IRIKQMGknasGQTHYLSLSGLEIYGTV 1240
Cdd:pfam07738   79 EFSYDLDGKTIqTFQLENPPDI--WVKYvkLRILSNY----GNEHYTCLYRFRVHGTV 130
MIB_HERC2 pfam06701
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain ...
 1277-1335 7.03e-26

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: 102.29  E-value: 7.03e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688594783  1277 GARVVRGIDWKWRDQDGNPAGEGTVT------GEAHNGWIDVTWDAGGSNSYRMGAEGKFDLKLA 1335
Cdd:pfam06701    1 GARVVRGPDWKWGDQDGGEGHVGTVVeirdwdSESPRSTVRVQWDNGSTNVYRVGYEGKYDLKVV 65
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
366-479 8.17e-26

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 110.04  E-value: 8.17e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783  366 LIDCIRSKDTDALIDAIDTGAfEVNFMDDVGQTLLNWASAFGTQEMVEFLCERGADVNR--GQRSSSLHYAACFGRPQVA 443
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGA-DVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAqdNDGNTPLHLAAANGNLEIV 169

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 688594783  444 KTLLRHGANPDLRDEDGKTPLDKARERGHSEVVAIL 479
Cdd:COG0666   170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
 2045-2522 7.43e-115

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: 369.20  E-value: 7.43e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783 2045 ERVKVPRGESMMEWAESVMQIH-ADRKSVLEVEFQGEEGTG-LGPTLEFYALVAAEFQRTSLGIWLCDDDFpddesrqvd 2122
Cdd:cd00078     1 LKITVRRDRILEDALRQLSKVSsSDLKKVLEVEFVGEEGIDaGGVTREFFTLVSKELFNPSYGLFRYTPDD--------- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783 2123 lggglkppgyyvqRSCGLFPAPFPQDSDELeritKLFLFLGIFLAKCIQDNRLVDLPISQPFFKLLCmgdiksnmsklly 2202
Cdd:cd00078    72 -------------SGLLYPNPSSFADEDHL----KLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLL------------- 121

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783 2203 qtrgesdchfseiqseasteegqdtysvgsfdedsksefildppkpkppawyHGILTWEDFELVNPHRALFLKELKALSV 2282
Cdd:cd00078   122 ----------------------------------------------------GKPLSLEDLEELDPELYKSLKELLDNDG 149

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783 2283 KrrqilgnkslsedekntrlqdlmlknpmgsgpplcVEDLGLNFQFCPSSKVHGFSSVDLKPNGEDEMVTMDNAEEYVEL 2362
Cdd:cd00078   150 D-----------------------------------EDDLELTFTIELDSSFGGAVTVELKPGGRDIPVTNENKEEYVDL 194

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783 2363 MFDFCMHTGIQKQMEAFREGFNKVFPMEKLSSFSHKEVQMILCGNqsPSWTAEDIVNYTEPKLGYTRDSPGFLRFVRVLC 2442
Cdd:cd00078   195 YVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGS--EDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLE 272

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783 2443 GMSSDERKAFLQFTTGCSTLPPGGLANLHPRLTIvRKVDATDASYPSVNTCVHYLKLPEYSSEEIMRERLLAATMEK-GF 2521
Cdd:cd00078   273 SFTNEERKKFLQFVTGSSRLPVGGFADLNPKFTI-RRVGSPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGaGF 351


                  .
gi 688594783 2522 H 2522
Cdd:cd00078   352 G 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
 2069-2521 1.29e-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: 295.68  E-value: 1.29e-89
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783   2069 RKSVLEVEFQGEEG-TGLGPTLEFYALVAAEFQRTSLGIWLCDDDfpddesrqvdlggglkppgyyvqrSCGLFPAPFPQ 2147
Cdd:smart00119    3 KKRVLEIEFEGEEGlDGGGVTREFFFLLSKELFNPDYGLFRYSPN------------------------DYLLYPNPRSG 58

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783   2148 DSDElERItKLFLFLGIFLAKCIQDNRLVDLPISQPFFKLLCmgdiksnmskllyqtrgesdchfseiqseasteegqdt 2227
Cdd:smart00119   59 FANE-EHL-SYFRFIGRVLGKALYDNRLLDLFFARPFYKKLL-------------------------------------- 98

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783   2228 ysvgsfdedsksefildppkpkppawyHGILTWEDFELVNPHRALFLKELKalsvkrrqilgnksLSEDEkntrlqdlml 2307
Cdd:smart00119   99 ---------------------------GKPVTLHDLESLDPELYKSLKWLL--------------LNNDT---------- 127

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783   2308 knpmgsgpplcVEDLGLNFQFCPSSKVHGFSSVDLKPNGEDEMVTMDNAEEYVELMFDFCMHTGIQKQMEAFREGFNKVF 2387
Cdd:smart00119  128 -----------SEELDLTFSIVLTSEFGQVKVVELKPGGSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVI 196

                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783   2388 PMEKLSSFSHKEVQMILCGnqSPSWTAEDIVNYTEPKLGYTRDSPGFLRFVRVLCGMSSDERKAFLQFTTGCSTLPPGGL 2467
Cdd:smart00119  197 PENLLKLFDPEELELLICG--SPEIDVDDLKSNTEYKGGYSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGF 274

                           410       420       430       440       450
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 688594783   2468 ANLHPRLTIvRKVDATDASYPSVNTCVHYLKLPEYSSEEIMRERLLAATME-KGF 2521
Cdd:smart00119  275 AALSPKFTI-RKAGSDDERLPTAHTCFNRLKLPPYSSKEILREKLLLAINEgKGF 328
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
 2094-2523 3.41e-75

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 253.30  E-value: 3.41e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783  2094 LVAAEFQRTSLGIWLCDDDfpddesrqvdlggglkppgyyvqRSCGLFPAPFPQDSDELERItKLFLFLGIFLAKCIQDN 2173
Cdd:pfam00632    2 LLSKELFDPNYGLFEYETE-----------------------DDRTYWFNPSSSESPDLELL-DYFKFLGKLLGKAIYNG 57

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783  2174 RLVDLPISQPFFKLLCmgdiksnmskllyqtrgesdchfseiqseasteegqdtysvgsfdedsksefildppkpkppaw 2253
Cdd:pfam00632   58 ILLDLPFPPFFYKKLL---------------------------------------------------------------- 73

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783  2254 yHGILTWEDFELVNPHRALFLKELKalsvkrrqilgnkSLSEDEkntrlqdlmlknpmgsgpplcVEDLGLNFQFCPSSK 2333
Cdd:pfam00632   74 -GEPLTLEDLESIDPELYKSLKSLL-------------NMDNDD---------------------DEDLGLTFTIPVFGE 118

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783  2334 VHgfsSVDLKPNGEDEMVTMDNAEEYVELMFDFCMHTGIQKQMEAFREGFNKVFPMEKLSSFSHKEVQMILCGnqSPSWT 2413
Cdd:pfam00632  119 SK---TIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQLEAFRKGFYSVIPKEALSLFTPEELELLICG--SPEID 193

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783  2414 AEDIVNYTEPKLGYTRDSPGFLRFVRVLCGMSSDERKAFLQFTTGCSTLPPGGLANLhPRLTIVRKVDATDASYPSVNTC 2493
Cdd:pfam00632  194 VEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGSSRLPVGGFKSL-PKFTIVRKGGDDDDRLPTAHTC 272

                          410       420       430
                   ....*....|....*....|....*....|.
gi 688594783  2494 VHYLKLPEYSSEEIMRERLLAATME-KGFHL 2523
Cdd:pfam00632  273 FNRLKLPDYSSKEILKEKLLIAIEEgEGFGL 303
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
1962-2521 1.72e-55

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 210.78  E-value: 1.72e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783 1962 QIEEPLALASGALPDWCEQLTskcPFLIPFETRQLYFTCTAFgasraivWLQNRREATMERSRPSTTVRRDDPGEFRVGR 2041
Cdd:COG5021   425 ESDESFYVASNVQQQRASREG---PLLSGWKTRLNNLYRFYF-------VEHRKKTLTKNDSRLGSFISLNKLDIRRIKE 494

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783 2042 LKHERVKVPRGESMMEwAESVMQIHADRKSVLEV---EFQGEEGTGLGPTLEFYALVAAEFQRTSLGIW----LCDDDFP 2114
Cdd:COG5021   495 DKRRKLFYSLKQKAKI-FDPYLHIKVRRDRVFEDsyrEIMDESGDDLKKTLEIEFVGEEGIDAGGLTREwlflLSKEMFN 573

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783 2115 DDesrqvdlggglkpPGYYVQRSCGLFPAPFPQDSDELERITKLFLFLGIFLAKCIQDNRLVDLPISQPFFKLLCmgdik 2194
Cdd:COG5021   574 PD-------------YGLFEYITEDLYTLPINPLSSINPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLL----- 635

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783 2195 snmskllyqtrgesdchfseiqseasteegqdtysvgsfdedsksefildppkPKPpawyhgiLTWEDFELVNPHRALFL 2274
Cdd:COG5021   636 -----------------------------------------------------GKP-------VSLVDLESLDPELYRSL 655

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783 2275 KELKALSVkrrqilgnkslseDEKNtrlqdlmlknpmgsgpplcvedLGLNFQFcpSSKVHGFS-SVDLKPNGEDEMVTM 2353
Cdd:COG5021   656 VWLLNNDI-------------DETI----------------------LDLTFTV--EDDSFGESrTVELIPNGRNISVTN 698

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783 2354 DNAEEYVELMFDFCMHTGIQKQMEAFREGFNKVFPMEKLSSFSHKEVQMILCGNQSPSwTAEDIVNYTEPKlGYTRDSPG 2433
Cdd:COG5021   699 ENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEDI-DIDDWKSNTAYH-GYTEDSPI 776

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783 2434 FLRFVRVLCGMSSDERKAFLQFTTGCSTLPPGGLANLHPRLTIVRKV--DATDASY--PSVNTCVHYLKLPEYSSEEIMR 2509
Cdd:COG5021   777 IVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTieKGGTDDDrlPSAHTCFNRLKLPEYSSKEKLR 856

                         570
                  ....*....|...
gi 688594783 2510 ERLLAATME-KGF 2521
Cdd:COG5021   857 SKLLTAINEgAGF 869
Sad1_UNC pfam07738
Sad1 / UNC-like C-terminal; The C. elegans UNC-84 protein is a nuclear envelope protein that ...
 1107-1240 1.18e-26

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: 106.99  E-value: 1.18e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783  1107 RNLPYGRLEDILSRDSSALNCHTNDDKNAWFAIDLGLWFVPSAYTLRHARGYGR-SALRNWVFQVSKDGQNWmtLYTHVD 1185
Cdd:pfam07738    1 LNYEAKPPKVILQPDYMPGPCWSFKGSRGFVVIELSEFIIVEAITLEHVEKSVFsSAPKDFEVSGSDRYPTT--KWVLLG 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 688594783  1186 DSSLNEPGSTA-TWPLDPSKDEkqGWRH--IRIKQMGknasGQTHYLSLSGLEIYGTV 1240
Cdd:pfam07738   79 EFSYDLDGKTIqTFQLENPPDI--WVKYvkLRILSNY----GNEHYTCLYRFRVHGTV 130
MIB_HERC2 pfam06701
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain ...
 1277-1335 7.03e-26

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: 102.29  E-value: 7.03e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688594783  1277 GARVVRGIDWKWRDQDGNPAGEGTVT------GEAHNGWIDVTWDAGGSNSYRMGAEGKFDLKLA 1335
Cdd:pfam06701    1 GARVVRGPDWKWGDQDGGEGHVGTVVeirdwdSESPRSTVRVQWDNGSTNVYRVGYEGKYDLKVV 65
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
366-479 8.17e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 110.04  E-value: 8.17e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783  366 LIDCIRSKDTDALIDAIDTGAfEVNFMDDVGQTLLNWASAFGTQEMVEFLCERGADVNR--GQRSSSLHYAACFGRPQVA 443
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGA-DVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAqdNDGNTPLHLAAANGNLEIV 169

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 688594783  444 KTLLRHGANPDLRDEDGKTPLDKARERGHSEVVAIL 479
Cdd:COG0666   170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
Ank_2 pfam12796
Ankyrin repeats (3 copies);
366-457 1.43e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.52  E-value: 1.43e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783   366 LIDCIRSKDTDALIDAIDTGAfEVNFMDDVGQTLLNWASAFGTQEMVEFLCERGADVNRGQRSSSLHYAACFGRPQVAKT 445
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGA-DANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRTALHYAARSGHLEIVKL 79

                           90
                   ....*....|..
gi 688594783   446 LLRHGANPDLRD 457
Cdd:pfam12796   80 LLEKGADINVKD 91
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 404-481 1.06e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 57.60  E-value: 1.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783  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 1.47e-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: 1.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783  396 GQTLLNWASAFGTQEMVEFLCERGADVN---------RGQRSSSLHY-------AACFGRPQVAKTLLRHGANPDLRDED 459
Cdd:cd22192    89 GETALHIAVVNQNLNLVRELIARGADVVspratgtffRPGPKNLIYYgehplsfAACVGNEEIVRLLIEHGADIRAQDSL 168


                  ....*
gi 688594783  460 GKTPL 464
Cdd:cd22192   169 GNTVL 173
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 431-455 6.28e-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: 6.28e-03
                            10        20
                    ....*....|....*....|....*
gi 688594783    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 ...
 2045-2522 7.43e-115

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: 369.20  E-value: 7.43e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783 2045 ERVKVPRGESMMEWAESVMQIH-ADRKSVLEVEFQGEEGTG-LGPTLEFYALVAAEFQRTSLGIWLCDDDFpddesrqvd 2122
Cdd:cd00078     1 LKITVRRDRILEDALRQLSKVSsSDLKKVLEVEFVGEEGIDaGGVTREFFTLVSKELFNPSYGLFRYTPDD--------- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783 2123 lggglkppgyyvqRSCGLFPAPFPQDSDELeritKLFLFLGIFLAKCIQDNRLVDLPISQPFFKLLCmgdiksnmsklly 2202
Cdd:cd00078    72 -------------SGLLYPNPSSFADEDHL----KLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLL------------- 121

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783 2203 qtrgesdchfseiqseasteegqdtysvgsfdedsksefildppkpkppawyHGILTWEDFELVNPHRALFLKELKALSV 2282
Cdd:cd00078   122 ----------------------------------------------------GKPLSLEDLEELDPELYKSLKELLDNDG 149

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783 2283 KrrqilgnkslsedekntrlqdlmlknpmgsgpplcVEDLGLNFQFCPSSKVHGFSSVDLKPNGEDEMVTMDNAEEYVEL 2362
Cdd:cd00078   150 D-----------------------------------EDDLELTFTIELDSSFGGAVTVELKPGGRDIPVTNENKEEYVDL 194

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783 2363 MFDFCMHTGIQKQMEAFREGFNKVFPMEKLSSFSHKEVQMILCGNqsPSWTAEDIVNYTEPKLGYTRDSPGFLRFVRVLC 2442
Cdd:cd00078   195 YVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGS--EDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLE 272

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783 2443 GMSSDERKAFLQFTTGCSTLPPGGLANLHPRLTIvRKVDATDASYPSVNTCVHYLKLPEYSSEEIMRERLLAATMEK-GF 2521
Cdd:cd00078   273 SFTNEERKKFLQFVTGSSRLPVGGFADLNPKFTI-RRVGSPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGaGF 351


                  .
gi 688594783 2522 H 2522
Cdd:cd00078   352 G 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
 2069-2521 1.29e-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: 295.68  E-value: 1.29e-89
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783   2069 RKSVLEVEFQGEEG-TGLGPTLEFYALVAAEFQRTSLGIWLCDDDfpddesrqvdlggglkppgyyvqrSCGLFPAPFPQ 2147
Cdd:smart00119    3 KKRVLEIEFEGEEGlDGGGVTREFFFLLSKELFNPDYGLFRYSPN------------------------DYLLYPNPRSG 58

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783   2148 DSDElERItKLFLFLGIFLAKCIQDNRLVDLPISQPFFKLLCmgdiksnmskllyqtrgesdchfseiqseasteegqdt 2227
Cdd:smart00119   59 FANE-EHL-SYFRFIGRVLGKALYDNRLLDLFFARPFYKKLL-------------------------------------- 98

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783   2228 ysvgsfdedsksefildppkpkppawyHGILTWEDFELVNPHRALFLKELKalsvkrrqilgnksLSEDEkntrlqdlml 2307
Cdd:smart00119   99 ---------------------------GKPVTLHDLESLDPELYKSLKWLL--------------LNNDT---------- 127

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783   2308 knpmgsgpplcVEDLGLNFQFCPSSKVHGFSSVDLKPNGEDEMVTMDNAEEYVELMFDFCMHTGIQKQMEAFREGFNKVF 2387
Cdd:smart00119  128 -----------SEELDLTFSIVLTSEFGQVKVVELKPGGSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVI 196

                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783   2388 PMEKLSSFSHKEVQMILCGnqSPSWTAEDIVNYTEPKLGYTRDSPGFLRFVRVLCGMSSDERKAFLQFTTGCSTLPPGGL 2467
Cdd:smart00119  197 PENLLKLFDPEELELLICG--SPEIDVDDLKSNTEYKGGYSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGF 274

                           410       420       430       440       450
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 688594783   2468 ANLHPRLTIvRKVDATDASYPSVNTCVHYLKLPEYSSEEIMRERLLAATME-KGF 2521
Cdd:smart00119  275 AALSPKFTI-RKAGSDDERLPTAHTCFNRLKLPPYSSKEILREKLLLAINEgKGF 328
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
 2094-2523 3.41e-75

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 253.30  E-value: 3.41e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783  2094 LVAAEFQRTSLGIWLCDDDfpddesrqvdlggglkppgyyvqRSCGLFPAPFPQDSDELERItKLFLFLGIFLAKCIQDN 2173
Cdd:pfam00632    2 LLSKELFDPNYGLFEYETE-----------------------DDRTYWFNPSSSESPDLELL-DYFKFLGKLLGKAIYNG 57

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783  2174 RLVDLPISQPFFKLLCmgdiksnmskllyqtrgesdchfseiqseasteegqdtysvgsfdedsksefildppkpkppaw 2253
Cdd:pfam00632   58 ILLDLPFPPFFYKKLL---------------------------------------------------------------- 73

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783  2254 yHGILTWEDFELVNPHRALFLKELKalsvkrrqilgnkSLSEDEkntrlqdlmlknpmgsgpplcVEDLGLNFQFCPSSK 2333
Cdd:pfam00632   74 -GEPLTLEDLESIDPELYKSLKSLL-------------NMDNDD---------------------DEDLGLTFTIPVFGE 118

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783  2334 VHgfsSVDLKPNGEDEMVTMDNAEEYVELMFDFCMHTGIQKQMEAFREGFNKVFPMEKLSSFSHKEVQMILCGnqSPSWT 2413
Cdd:pfam00632  119 SK---TIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQLEAFRKGFYSVIPKEALSLFTPEELELLICG--SPEID 193

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783  2414 AEDIVNYTEPKLGYTRDSPGFLRFVRVLCGMSSDERKAFLQFTTGCSTLPPGGLANLhPRLTIVRKVDATDASYPSVNTC 2493
Cdd:pfam00632  194 VEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGSSRLPVGGFKSL-PKFTIVRKGGDDDDRLPTAHTC 272

                          410       420       430
                   ....*....|....*....|....*....|.
gi 688594783  2494 VHYLKLPEYSSEEIMRERLLAATME-KGFHL 2523
Cdd:pfam00632  273 FNRLKLPDYSSKEILKEKLLIAIEEgEGFGL 303
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
1962-2521 1.72e-55

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 210.78  E-value: 1.72e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783 1962 QIEEPLALASGALPDWCEQLTskcPFLIPFETRQLYFTCTAFgasraivWLQNRREATMERSRPSTTVRRDDPGEFRVGR 2041
Cdd:COG5021   425 ESDESFYVASNVQQQRASREG---PLLSGWKTRLNNLYRFYF-------VEHRKKTLTKNDSRLGSFISLNKLDIRRIKE 494

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783 2042 LKHERVKVPRGESMMEwAESVMQIHADRKSVLEV---EFQGEEGTGLGPTLEFYALVAAEFQRTSLGIW----LCDDDFP 2114
Cdd:COG5021   495 DKRRKLFYSLKQKAKI-FDPYLHIKVRRDRVFEDsyrEIMDESGDDLKKTLEIEFVGEEGIDAGGLTREwlflLSKEMFN 573

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783 2115 DDesrqvdlggglkpPGYYVQRSCGLFPAPFPQDSDELERITKLFLFLGIFLAKCIQDNRLVDLPISQPFFKLLCmgdik 2194
Cdd:COG5021   574 PD-------------YGLFEYITEDLYTLPINPLSSINPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLL----- 635

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783 2195 snmskllyqtrgesdchfseiqseasteegqdtysvgsfdedsksefildppkPKPpawyhgiLTWEDFELVNPHRALFL 2274
Cdd:COG5021   636 -----------------------------------------------------GKP-------VSLVDLESLDPELYRSL 655

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783 2275 KELKALSVkrrqilgnkslseDEKNtrlqdlmlknpmgsgpplcvedLGLNFQFcpSSKVHGFS-SVDLKPNGEDEMVTM 2353
Cdd:COG5021   656 VWLLNNDI-------------DETI----------------------LDLTFTV--EDDSFGESrTVELIPNGRNISVTN 698

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783 2354 DNAEEYVELMFDFCMHTGIQKQMEAFREGFNKVFPMEKLSSFSHKEVQMILCGNQSPSwTAEDIVNYTEPKlGYTRDSPG 2433
Cdd:COG5021   699 ENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEDI-DIDDWKSNTAYH-GYTEDSPI 776

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783 2434 FLRFVRVLCGMSSDERKAFLQFTTGCSTLPPGGLANLHPRLTIVRKV--DATDASY--PSVNTCVHYLKLPEYSSEEIMR 2509
Cdd:COG5021   777 IVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTieKGGTDDDrlPSAHTCFNRLKLPEYSSKEKLR 856

                         570
                  ....*....|...
gi 688594783 2510 ERLLAATME-KGF 2521
Cdd:COG5021   857 SKLLTAINEgAGF 869
Sad1_UNC pfam07738
Sad1 / UNC-like C-terminal; The C. elegans UNC-84 protein is a nuclear envelope protein that ...
 1107-1240 1.18e-26

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: 106.99  E-value: 1.18e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783  1107 RNLPYGRLEDILSRDSSALNCHTNDDKNAWFAIDLGLWFVPSAYTLRHARGYGR-SALRNWVFQVSKDGQNWmtLYTHVD 1185
Cdd:pfam07738    1 LNYEAKPPKVILQPDYMPGPCWSFKGSRGFVVIELSEFIIVEAITLEHVEKSVFsSAPKDFEVSGSDRYPTT--KWVLLG 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 688594783  1186 DSSLNEPGSTA-TWPLDPSKDEkqGWRH--IRIKQMGknasGQTHYLSLSGLEIYGTV 1240
Cdd:pfam07738   79 EFSYDLDGKTIqTFQLENPPDI--WVKYvkLRILSNY----GNEHYTCLYRFRVHGTV 130
MIB_HERC2 pfam06701
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain ...
 1277-1335 7.03e-26

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: 102.29  E-value: 7.03e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688594783  1277 GARVVRGIDWKWRDQDGNPAGEGTVT------GEAHNGWIDVTWDAGGSNSYRMGAEGKFDLKLA 1335
Cdd:pfam06701    1 GARVVRGPDWKWGDQDGGEGHVGTVVeirdwdSESPRSTVRVQWDNGSTNVYRVGYEGKYDLKVV 65
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
366-479 8.17e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 110.04  E-value: 8.17e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783  366 LIDCIRSKDTDALIDAIDTGAfEVNFMDDVGQTLLNWASAFGTQEMVEFLCERGADVNR--GQRSSSLHYAACFGRPQVA 443
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGA-DVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAqdNDGNTPLHLAAANGNLEIV 169

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 688594783  444 KTLLRHGANPDLRDEDGKTPLDKARERGHSEVVAIL 479
Cdd:COG0666   170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
366-480 8.21e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 104.27  E-value: 8.21e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783  366 LIDCIRSKDTDA---LIDAidtGAfEVNFMDDVGQTLLNWASAFGTQEMVEFLCERGADVNRGQRS--SSLHYAACFGRP 440
Cdd:COG0666   124 LHLAAYNGNLEIvklLLEA---GA-DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDgeTPLHLAAENGHL 199

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 688594783  441 QVAKTLLRHGANPDLRDEDGKTPLDKARERGHSEVVAILQ 480
Cdd:COG0666   200 EIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
366-479 3.66e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 93.48  E-value: 3.66e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783  366 LIDCIRSKDTDALIDAIDTGAFEVNFMDDVGQTLLNWASAFGTQEMVEFLCERGADVNR--GQRSSSLHYAACFGRPQVA 443
Cdd:COG0666    57 LLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNArdKDGETPLHLAAYNGNLEIV 136

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 688594783  444 KTLLRHGANPDLRDEDGKTPLDKARERGHSEVVAIL 479
Cdd:COG0666   137 KLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172
Ank_2 pfam12796
Ankyrin repeats (3 copies);
366-457 1.43e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.52  E-value: 1.43e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783   366 LIDCIRSKDTDALIDAIDTGAfEVNFMDDVGQTLLNWASAFGTQEMVEFLCERGADVNRGQRSSSLHYAACFGRPQVAKT 445
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGA-DANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRTALHYAARSGHLEIVKL 79

                           90
                   ....*....|..
gi 688594783   446 LLRHGANPDLRD 457
Cdd:pfam12796   80 LLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
370-479 3.31e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 69.60  E-value: 3.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783  370 IRSKDTDALIDAIDTGAFEVNFMDDVGQTLLNWASAFGTQEMVEFLCERGADVNRG--QRSSSLHYAACFGRPQVAKTLL 447
Cdd:COG0666    28 AALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKddGGNTLLHAAARNGDLEIVKLLL 107

                          90       100       110
                  ....*....|....*....|....*....|..
gi 688594783  448 RHGANPDLRDEDGKTPLDKARERGHSEVVAIL 479
Cdd:COG0666   108 EAGADVNARDKDGETPLHLAAYNGNLEIVKLL 139
Ank_2 pfam12796
Ankyrin repeats (3 copies);
400-483 1.54e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 59.74  E-value: 1.54e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783   400 LNWASAFGTQEMVEFLCERGADVN--RGQRSSSLHYAACFGRPQVAKTLLRHgANPDLRDeDGKTPLDKARERGHSEVVA 477
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANlqDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78


                   ....*.
gi 688594783   478 ILQSPG 483
Cdd:pfam12796   79 LLLEKG 84
Ank_4 pfam13637
Ankyrin repeats (many copies);
427-479 9.53e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.74  E-value: 9.53e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 688594783   427 RSSSLHYAACFGRPQVAKTLLRHGANPDLRDEDGKTPLDKARERGHSEVVAIL 479
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 404-481 1.06e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 57.60  E-value: 1.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783  404 SAFGTQEMVEFLCERGADVNRG--QRSSSLHYAACFGRPQVAKTLLRHGANPDLRDEDGKTPLDKARERGHSEVVAILQS 481
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRdyDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 370-464 1.31e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 53.73  E-value: 1.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783  370 IRSKDTDALIDA------IDTGAfEVNFMD-DVGQTLLNWASAFGTQEMVEFLCERGADVNRGQR--SSSLHYAACFGRP 440
Cdd:PHA02878  136 IDKKSKDDIIEAeitkllLSYGA-DINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKtnNSPLHHAVKHYNK 214

                          90       100
                  ....*....|....*....|....
gi 688594783  441 QVAKTLLRHGANPDLRDEDGKTPL 464
Cdd:PHA02878  215 PIVHILLENGASTDARDKCGNTPL 238
PHA03095 PHA03095
ankyrin-like protein; Provisional
 393-477 3.09e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 52.33  E-value: 3.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783  393 DDVGQTLLNWASAFGTQE--MVEFLCERGADVN----RGQrsSSLHYAACFGRPQVAKTLLRHGANPDLRDEDGKTPLDK 466
Cdd:PHA03095  219 DMLGNTPLHSMATGSSCKrsLVLPLLIAGISINarnrYGQ--TPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSL 296

                          90
                  ....*....|.
gi 688594783  467 ARERGHSEVVA 477
Cdd:PHA03095  297 MVRNNNGRAVR 307
Ank_5 pfam13857
Ankyrin repeats (many copies);
418-467 6.74e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.42  E-value: 6.74e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 688594783   418 RGADVNR--GQRSSSLHYAACFGRPQVAKTLLRHGANPDLRDEDGKTPLDKA 467
Cdd:pfam13857    5 GPIDLNRldGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 410-484 1.48e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 50.05  E-value: 1.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783  410 EMVEFLCERGADVN--------------------RGqrSSSLHYAACFGRPQVAKTLLRHGANPDLRDEDGKTPLDKARE 469
Cdd:PHA03100  157 KILKLLIDKGVDINaknrvnyllsygvpinikdvYG--FTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAIL 234

                          90
                  ....*....|....*
gi 688594783  470 RGHSEVVAILQSPGD 484
Cdd:PHA03100  235 NNNKEIFKLLLNNGP 249
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 391-483 2.55e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 49.22  E-value: 2.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783  391 FMDDV----GQTLLNWASAFGTQEMVEFLCERGAD--VNRGQRSSSLHYAACFGRPQVAKTLLRHGANPDLRDEDGKTPL 464
Cdd:PHA02875   93 FADDVfykdGMTPLHLATILKKLDIMKLLIARGADpdIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPL 172

                          90
                  ....*....|....*....
gi 688594783  465 DKARERGHSEVVAILQSPG 483
Cdd:PHA02875  173 IIAMAKGDIAICKMLLDSG 191
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 410-464 9.84e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 45.97  E-value: 9.84e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688594783  410 EMVEFLCERGADVN---RGQRSSSLHYAACFGR---PQVAKTLLRHGANPDLRDEDGKTPL 464
Cdd:PHA02859   67 EILKFLIENGADVNfktRDNNLSALHHYLSFNKnvePEILKILIDSGSSITEEDEDGKNLL 127
PHA03095 PHA03095
ankyrin-like protein; Provisional
 408-465 1.89e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.56  E-value: 1.89e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688594783  408 TQEMVEFLCERGADVNR--GQRSSSLH-YAACFG-RPQVAKTLLRHGANPDLRDEDGKTPLD 465
Cdd:PHA03095   96 TLDVIKLLIKAGADVNAkdKVGRTPLHvYLSGFNiNPKVIRLLLRKGADVNALDLYGMTPLA 157
F5_F8_type_C pfam00754
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.
 1127-1216 1.98e-04

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: 43.59  E-value: 1.98e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783  1127 CHTNDDKNAWFAIDLGlwfvpSAYTLRHARGYGRSALRN-----WVFQVSKDGQNWMTLYTHVDDSSlNEPGSTATWPLD 1201
Cdd:pfam00754   27 SAWSGDDPQWIQVDLG-----KPKKITGVVTQGRQDGSNgyvtsYKIEYSLDGENWTTVKDEKIPGN-NDNNTPVTNTFD 100

                           90
                   ....*....|....*
gi 688594783  1202 PSKDEkqgwRHIRIK 1216
Cdd:pfam00754  101 PPIKA----RYVRIV 111
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 410-479 6.23e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 44.87  E-value: 6.23e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 688594783  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 1.09e-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: 1.09e-03
                           10        20
                   ....*....|....*....|....*....
gi 688594783   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 1.47e-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: 1.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783  396 GQTLLNWASAFGTQEMVEFLCERGADVN---------RGQRSSSLHY-------AACFGRPQVAKTLLRHGANPDLRDED 459
Cdd:cd22192    89 GETALHIAVVNQNLNLVRELIARGADVVspratgtffRPGPKNLIYYgehplsfAACVGNEEIVRLLIEHGADIRAQDSL 168


                  ....*
gi 688594783  460 GKTPL 464
Cdd:cd22192   169 GNTVL 173
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 370-467 1.67e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 43.41  E-value: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783  370 IRSKDTDALIDAIDTGAfEVNFMDDVGQTLLNWASAFGTQEMVEFLCERGA--DVNRGQRSSSLHYAACFGRPQVAKTLL 447
Cdd:PHA02874  132 IKKGDLESIKMLFEYGA-DVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAyaNVKDNNGESPLHNAAEYGDYACIKLLI 210

                          90       100
                  ....*....|....*....|
gi 688594783  448 RHGANPDLRDEDGKTPLDKA 467
Cdd:PHA02874  211 DHGNHIMNKCKNGFTPLHNA 230
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 409-486 2.79e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 42.64  E-value: 2.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783  409 QEMVEFLCERGADVNRGQRSSS--LHYAACFGRPQVAKTLLRHGANPDLRDEDGKTPLDKARERGHSEVVAILQSPGDWM 486
Cdd:PHA02874  104 KDMIKTILDCGIDVNIKDAELKtfLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYA 183
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 431-455 6.28e-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: 6.28e-03
                            10        20
                    ....*....|....*....|....*
gi 688594783    431 LHYAACFGRPQVAKTLLRHGANPDL 455
Cdd:smart00248    6 LHLAAENGNLEVVKLLLDKGADINA 30
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 403-487 9.13e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.39  E-value: 9.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688594783  403 ASAFGTQEMVEFLCERG--ADVNRGQRSSSLHYAACFGRPQVAKTLLRHGANPDLRDEDGKTPLDKARERGHSEVVAIL- 479
Cdd:PLN03192  532 VASTGNAALLEELLKAKldPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILy 611

                          90
                  ....*....|....*.
gi 688594783  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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