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Conserved domains on  [gi|767980210|ref|XP_011534923|]
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E3 ubiquitin-protein ligase HECTD1 isoform X9 [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 ...
 1852-2329 2.76e-118

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: 378.83  E-value: 2.76e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210 1852 ERVKVPRGESLMEWAENVMQIH-ADRKSVLEVEFLGEEGTG-LGPTLEFYALVAAEFQRTDLGAWLCDDNFpddesrhvd 1929
Cdd:cd00078     1 LKITVRRDRILEDALRQLSKVSsSDLKKVLEVEFVGEEGIDaGGVTREFFTLVSKELFNPSYGLFRYTPDD--------- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210 1930 lggglkppgyyvqRSCGLFTAPFPQDSDELeritKLFHFLGIFLAKCIQDNRLVDLPISKPFFKLMCmgdiksnmskliy 2009
Cdd:cd00078    72 -------------SGLLYPNPSSFADEDHL----KLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLL------------- 121

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210 2010 esrgdrdlhctesqseasteeghdslsvgsfeedsksefildppkpkppawfNGILTWEDFELVNPHRARFLKEIKDLAI 2089
Cdd:cd00078   122 ----------------------------------------------------GKPLSLEDLEELDPELYKSLKELLDNDG 149

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210 2090 krrqilsnkglsedekntklqelvlknpsgsgpplSIEDLGLNFQFCPSSRIYGFTAVDLKPSGEDEMITMDNAEEYVDL 2169
Cdd:cd00078   150 -----------------------------------DEDDLELTFTIELDSSFGGAVTVELKPGGRDIPVTNENKEEYVDL 194

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210 2170 MFDFCMHTGIQKQMEAFRDGFNKVFPMEKLSSFSHEEVQMILCGNqsPSWAAEDIINYTEPKLGYTRDSPGFLRFVRVLC 2249
Cdd:cd00078   195 YVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGS--EDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLE 272

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210 2250 GMSSDERKAFLQFTTGCSTLPPGGLANLHPRLTvVRKVDATDASYPSVNTCVHYLKLPEYSSEEIMRERLLAATMEK-GF 2328
Cdd:cd00078   273 SFTNEERKKFLQFVTGSSRLPVGGFADLNPKFT-IRRVGSPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGaGF 351


                  .
gi 767980210 2329 H 2329
Cdd:cd00078   352 G 352
BTHB_HectD1 cd21062
basic tilted helix bundle (BTHB) domain found in HECT domain-containing protein 1 (HectD1) and ...
 1614-1679 9.97e-38

basic tilted helix bundle (BTHB) domain found in HECT domain-containing protein 1 (HectD1) and similar proteins; HectD1, also called E3 ligase for inhibin receptor (EULIR), is a Hect-type E3 ubiquitin transferase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. HectD1 is required for development of head mesenchyme and neural tube closure.


:

Pssm-ID: 439138  Cd Length: 66  Bit Score: 136.26  E-value: 9.97e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767980210 1614 CWSIEHVEQYLGTDELPKNDLITYLQKNADAAFLRHWKLTGTNKSIRKNRNCSQLIAAYKDFCEHG 1679
Cdd:cd21062     1 EWTVEYVEQSLGTGELPKSDVITYLQKNADEAFLRRWKLTGTAKNIRKNRNCSQLIAAYKEFCEHG 66
Sad1_UNC pfam07738
Sad1 / UNC-like C-terminal; The C. elegans UNC-84 protein is a nuclear envelope protein that ...
 1107-1240 8.33e-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: 8.33e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210  1107 RNLPYGRLEDILSRDNSALNCHSNDDKNAWFAIDLGLWVIPSAYTLRHARGYGR-SALRNWVFQVSKDGQNWTslYTHVD 1185
Cdd:pfam07738    1 LNYEAKPPKVILQPDYMPGPCWSFKGSRGFVVIELSEFIIVEAITLEHVEKSVFsSAPKDFEVSGSDRYPTTK--WVLLG 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 767980210  1186 DCSLNEPGSTA-TWPLDPPKDEkqGWRHVR--IKQMGknasGQTHYLSLSGFELYGTV 1240
Cdd:pfam07738   79 EFSYDLDGKTIqTFQLENPPDI--WVKYVKlrILSNY----GNEHYTCLYRFRVHGTV 130
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
366-479 7.48e-26

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 110.04  E-value: 7.48e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210  366 LIDCIRSKDTDALIDAIDTGAfEVNFMDDVGQTLLNWASAFGTQEMVEFLCERGADVNR--GQRSSSLHYAACFGRPQVA 443
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGA-DVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAqdNDGNTPLHLAAANGNLEIV 169

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 767980210  444 KTLLRHGANPDLRDEDGKTPLDKARERGHSEVVAIL 479
Cdd:COG0666   170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
MIB_HERC2 super family cl05972
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain ...
 1277-1302 1.51e-08

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


The actual alignment was detected with superfamily member pfam06701:

Pssm-ID: 461991  Cd Length: 66  Bit Score: 52.99  E-value: 1.51e-08
                           10        20
                   ....*....|....*....|....*.
gi 767980210  1277 GARVIRGLDWKWRDQDGSPQGEGTVT 1302
Cdd:pfam06701    1 GARVVRGPDWKWGDQDGGEGHVGTVV 26
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
 1852-2329 2.76e-118

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: 378.83  E-value: 2.76e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210 1852 ERVKVPRGESLMEWAENVMQIH-ADRKSVLEVEFLGEEGTG-LGPTLEFYALVAAEFQRTDLGAWLCDDNFpddesrhvd 1929
Cdd:cd00078     1 LKITVRRDRILEDALRQLSKVSsSDLKKVLEVEFVGEEGIDaGGVTREFFTLVSKELFNPSYGLFRYTPDD--------- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210 1930 lggglkppgyyvqRSCGLFTAPFPQDSDELeritKLFHFLGIFLAKCIQDNRLVDLPISKPFFKLMCmgdiksnmskliy 2009
Cdd:cd00078    72 -------------SGLLYPNPSSFADEDHL----KLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLL------------- 121

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210 2010 esrgdrdlhctesqseasteeghdslsvgsfeedsksefildppkpkppawfNGILTWEDFELVNPHRARFLKEIKDLAI 2089
Cdd:cd00078   122 ----------------------------------------------------GKPLSLEDLEELDPELYKSLKELLDNDG 149

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210 2090 krrqilsnkglsedekntklqelvlknpsgsgpplSIEDLGLNFQFCPSSRIYGFTAVDLKPSGEDEMITMDNAEEYVDL 2169
Cdd:cd00078   150 -----------------------------------DEDDLELTFTIELDSSFGGAVTVELKPGGRDIPVTNENKEEYVDL 194

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210 2170 MFDFCMHTGIQKQMEAFRDGFNKVFPMEKLSSFSHEEVQMILCGNqsPSWAAEDIINYTEPKLGYTRDSPGFLRFVRVLC 2249
Cdd:cd00078   195 YVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGS--EDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLE 272

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210 2250 GMSSDERKAFLQFTTGCSTLPPGGLANLHPRLTvVRKVDATDASYPSVNTCVHYLKLPEYSSEEIMRERLLAATMEK-GF 2328
Cdd:cd00078   273 SFTNEERKKFLQFVTGSSRLPVGGFADLNPKFT-IRRVGSPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGaGF 351


                  .
gi 767980210 2329 H 2329
Cdd:cd00078   352 G 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
 1876-2328 2.20e-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: 2.20e-89
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210   1876 RKSVLEVEFLGEEG-TGLGPTLEFYALVAAEFQRTDLGAWLCDDNfpddesrhvdlggglkppgyyvqrSCGLFTAPFPQ 1954
Cdd:smart00119    3 KKRVLEIEFEGEEGlDGGGVTREFFFLLSKELFNPDYGLFRYSPN------------------------DYLLYPNPRSG 58

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210   1955 DSDElERItKLFHFLGIFLAKCIQDNRLVDLPISKPFFKLMCmgdiksnmskliyesrgdrdlhctesqseasteeghds 2034
Cdd:smart00119   59 FANE-EHL-SYFRFIGRVLGKALYDNRLLDLFFARPFYKKLL-------------------------------------- 98

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210   2035 lsvgsfeedsksefildppkpkppawfNGILTWEDFELVNPHRARFLKEIKdlaikrrqilsnkgLSEDEkntklqelvl 2114
Cdd:smart00119   99 ---------------------------GKPVTLHDLESLDPELYKSLKWLL--------------LNNDT---------- 127

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210   2115 knpsgsgpplsIEDLGLNFQFCPSSRIYGFTAVDLKPSGEDEMITMDNAEEYVDLMFDFCMHTGIQKQMEAFRDGFNKVF 2194
Cdd:smart00119  128 -----------SEELDLTFSIVLTSEFGQVKVVELKPGGSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVI 196

                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210   2195 PMEKLSSFSHEEVQMILCGnqSPSWAAEDIINYTEPKLGYTRDSPGFLRFVRVLCGMSSDERKAFLQFTTGCSTLPPGGL 2274
Cdd:smart00119  197 PENLLKLFDPEELELLICG--SPEIDVDDLKSNTEYKGGYSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGF 274

                           410       420       430       440       450
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 767980210   2275 ANLHPRLTvVRKVDATDASYPSVNTCVHYLKLPEYSSEEIMRERLLAATME-KGF 2328
Cdd:smart00119  275 AALSPKFT-IRKAGSDDERLPTAHTCFNRLKLPPYSSKEILREKLLLAINEgKGF 328
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
 1943-2330 1.18e-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: 245.60  E-value: 1.18e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210  1943 RSCGLFTAPFPQDSDELERItKLFHFLGIFLAKCIQDNRLVDLPISKPFFKLMCmgdiksnmskliyesrgdrdlhctes 2022
Cdd:pfam00632   21 DDRTYWFNPSSSESPDLELL-DYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLL-------------------------- 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210  2023 qseasteeghdslsvgsfeedsksefildppkpkppawfNGILTWEDFELVNPHRARFLKEIKDLaikrrqilsnkglSE 2102
Cdd:pfam00632   74 ---------------------------------------GEPLTLEDLESIDPELYKSLKSLLNM-------------DN 101

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210  2103 DEKntklqelvlknpsgsgpplsiEDLGLNFQFCpssrIYGFTA-VDLKPSGEDEMITMDNAEEYVDLMFDFCMHTGIQK 2181
Cdd:pfam00632  102 DDD---------------------EDLGLTFTIP----VFGESKtIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEP 156

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210  2182 QMEAFRDGFNKVFPMEKLSSFSHEEVQMILCGnqSPSWAAEDIINYTEPKLGYTRDSPGFLRFVRVLCGMSSDERKAFLQ 2261
Cdd:pfam00632  157 QLEAFRKGFYSVIPKEALSLFTPEELELLICG--SPEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLK 234

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210  2262 FTTGCSTLPPGGLANLhPRLTVVRKVDATDASYPSVNTCVHYLKLPEYSSEEIMRERLLAATME-KGFHL 2330
Cdd:pfam00632  235 FVTGSSRLPVGGFKSL-PKFTIVRKGGDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEgEGFGL 303
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
1769-2328 6.48e-55

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 208.85  E-value: 6.48e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210 1769 QIEEPLALASGALPDWCEQLTskcPFLIPFETRQLYFTCTAFgasraivWLQNRREATVERTRTTSSVRRDDPGEFRVGR 1848
Cdd:COG5021   425 ESDESFYVASNVQQQRASREG---PLLSGWKTRLNNLYRFYF-------VEHRKKTLTKNDSRLGSFISLNKLDIRRIKE 494

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210 1849 LKHERVKVprgeSLMEWAENVM---QIHADRKSVLEV---EFLGEEGTGLGPTLEFYALVAAEFQRTDLGAW----LCDD 1918
Cdd:COG5021   495 DKRRKLFY----SLKQKAKIFDpylHIKVRRDRVFEDsyrEIMDESGDDLKKTLEIEFVGEEGIDAGGLTREwlflLSKE 570

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210 1919 NFPDDesrhvdlggglkpPGYYVQRSCGLFTAPFPQDSDELERITKLFHFLGIFLAKCIQDNRLVDLPISKPFFKLMCmg 1998
Cdd:COG5021   571 MFNPD-------------YGLFEYITEDLYTLPINPLSSINPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLL-- 635

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210 1999 diksnmskliyesrgdrdlhctesqseasteeghdslsvgsfeedsksefildppkPKPpawfngiLTWEDFELVNPHRA 2078
Cdd:COG5021   636 --------------------------------------------------------GKP-------VSLVDLESLDPELY 652

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210 2079 RFLKEIKDLaikrrqilsnkglSEDEKNtklqelvlknpsgsgpplsiedLGLNFQFcpSSRIYGFTA-VDLKPSGEDEM 2157
Cdd:COG5021   653 RSLVWLLNN-------------DIDETI----------------------LDLTFTV--EDDSFGESRtVELIPNGRNIS 695

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210 2158 ITMDNAEEYVDLMFDFCMHTGIQKQMEAFRDGFNKVFPMEKLSSFSHEEVQMILCGNQSPSwAAEDIINYTEPKlGYTRD 2237
Cdd:COG5021   696 VTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEDI-DIDDWKSNTAYH-GYTED 773

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210 2238 SPGFLRFVRVLCGMSSDERKAFLQFTTGCSTLPPGGLANLHPRLTVVRKV--DATDASY--PSVNTCVHYLKLPEYSSEE 2313
Cdd:COG5021   774 SPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTieKGGTDDDrlPSAHTCFNRLKLPEYSSKE 853

                         570
                  ....*....|....*.
gi 767980210 2314 IMRERLLAATME-KGF 2328
Cdd:COG5021   854 KLRSKLLTAINEgAGF 869
BTHB_HectD1 cd21062
basic tilted helix bundle (BTHB) domain found in HECT domain-containing protein 1 (HectD1) and ...
 1614-1679 9.97e-38

basic tilted helix bundle (BTHB) domain found in HECT domain-containing protein 1 (HectD1) and similar proteins; HectD1, also called E3 ligase for inhibin receptor (EULIR), is a Hect-type E3 ubiquitin transferase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. HectD1 is required for development of head mesenchyme and neural tube closure.


Pssm-ID: 439138  Cd Length: 66  Bit Score: 136.26  E-value: 9.97e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767980210 1614 CWSIEHVEQYLGTDELPKNDLITYLQKNADAAFLRHWKLTGTNKSIRKNRNCSQLIAAYKDFCEHG 1679
Cdd:cd21062     1 EWTVEYVEQSLGTGELPKSDVITYLQKNADEAFLRRWKLTGTAKNIRKNRNCSQLIAAYKEFCEHG 66
Sad1_UNC pfam07738
Sad1 / UNC-like C-terminal; The C. elegans UNC-84 protein is a nuclear envelope protein that ...
 1107-1240 8.33e-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: 8.33e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210  1107 RNLPYGRLEDILSRDNSALNCHSNDDKNAWFAIDLGLWVIPSAYTLRHARGYGR-SALRNWVFQVSKDGQNWTslYTHVD 1185
Cdd:pfam07738    1 LNYEAKPPKVILQPDYMPGPCWSFKGSRGFVVIELSEFIIVEAITLEHVEKSVFsSAPKDFEVSGSDRYPTTK--WVLLG 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 767980210  1186 DCSLNEPGSTA-TWPLDPPKDEkqGWRHVR--IKQMGknasGQTHYLSLSGFELYGTV 1240
Cdd:pfam07738   79 EFSYDLDGKTIqTFQLENPPDI--WVKYVKlrILSNY----GNEHYTCLYRFRVHGTV 130
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
366-479 7.48e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 110.04  E-value: 7.48e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210  366 LIDCIRSKDTDALIDAIDTGAfEVNFMDDVGQTLLNWASAFGTQEMVEFLCERGADVNR--GQRSSSLHYAACFGRPQVA 443
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGA-DVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAqdNDGNTPLHLAAANGNLEIV 169

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 767980210  444 KTLLRHGANPDLRDEDGKTPLDKARERGHSEVVAIL 479
Cdd:COG0666   170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
BTHB pfam18410
Basic tilted helix bundle domain; This domain is found on the N-terminal region of FKBPs such ...
 1615-1680 3.85e-15

Basic tilted helix bundle domain; This domain is found on the N-terminal region of FKBPs such as FKBP25 and in the core region of E3 ubiquitin ligase HectD1. It adopts a compact 5-helix bundle, hence termed BTHB (Basic Tilted Helix Bundle) domain. In FKBP25, it has been suggested to have a role in regulating the association state of nucleosomes by interacting with nucleolin. Moreover, this basic domain in FKBP25 forms alternative complexes with other chromatin-related proteins, such as the HDAC1, HDAC2, and the transcriptional regulator YY1, the DNA binding activity of which is enhanced on binding FKBP25. Structural analysis of this fold suggests that the DNA binding properties of FKBP25 and HectD1 are presented by the conserved basic region.


Pssm-ID: 465755  Cd Length: 72  Bit Score: 72.02  E-value: 3.85e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767980210  1615 WSIEhveqYLGTDELPKNDLITYLQKNADAAFLRHWKLTGTNKSIRKNRNCSQLIAAYKDFCEHGT 1680
Cdd:pfam18410    5 WTEE----QLLSDALPKKDIIKFLQDNASLSFLKEHKLNGALKNVAKTAKKDQLAEAYNKLFESKR 66
Ank_2 pfam12796
Ankyrin repeats (3 copies);
366-457 1.32e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.52  E-value: 1.32e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210   366 LIDCIRSKDTDALIDAIDTGAfEVNFMDDVGQTLLNWASAFGTQEMVEFLCERGADVNRGQRSSSLHYAACFGRPQVAKT 445
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGA-DANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRTALHYAARSGHLEIVKL 79

                           90
                   ....*....|..
gi 767980210   446 LLRHGANPDLRD 457
Cdd:pfam12796   80 LLEKGADINVKD 91
MIB_HERC2 pfam06701
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain ...
 1277-1302 1.51e-08

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: 52.99  E-value: 1.51e-08
                           10        20
                   ....*....|....*....|....*.
gi 767980210  1277 GARVIRGLDWKWRDQDGSPQGEGTVT 1302
Cdd:pfam06701    1 GARVVRGPDWKWGDQDGGEGHVGTVV 26
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 404-481 8.51e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 57.60  E-value: 8.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210  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 1.35e-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: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210  396 GQTLLNWASAFGTQEMVEFLCERGADVN---------RGQRSSSLHY-------AACFGRPQVAKTLLRHGANPDLRDED 459
Cdd:cd22192    89 GETALHIAVVNQNLNLVRELIARGADVVspratgtffRPGPKNLIYYgehplsfAACVGNEEIVRLLIEHGADIRAQDSL 168


                  ....*
gi 767980210  460 GKTPL 464
Cdd:cd22192   169 GNTVL 173
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 1127-1238 2.95e-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: 2.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210 1127 CHSNDDKNAWFAIDLGL--WVIPSAYTLRHaRGYGRSALRNWVFQVSKDGQNWTSLYTHVDDCSLN---EPGSTATWPLD 1201
Cdd:cd00057    38 TPAVNDPPQWLQVDLGKtrRVTGIQTQGRK-GGGSSEWVTSYKVQYSLDGETWTTYKDKGEEKVFTgnsDGSTPVTNDFP 116

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 767980210 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 5.80e-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: 5.80e-03
                            10        20
                    ....*....|....*....|....*
gi 767980210    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 ...
 1852-2329 2.76e-118

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: 378.83  E-value: 2.76e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210 1852 ERVKVPRGESLMEWAENVMQIH-ADRKSVLEVEFLGEEGTG-LGPTLEFYALVAAEFQRTDLGAWLCDDNFpddesrhvd 1929
Cdd:cd00078     1 LKITVRRDRILEDALRQLSKVSsSDLKKVLEVEFVGEEGIDaGGVTREFFTLVSKELFNPSYGLFRYTPDD--------- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210 1930 lggglkppgyyvqRSCGLFTAPFPQDSDELeritKLFHFLGIFLAKCIQDNRLVDLPISKPFFKLMCmgdiksnmskliy 2009
Cdd:cd00078    72 -------------SGLLYPNPSSFADEDHL----KLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLL------------- 121

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210 2010 esrgdrdlhctesqseasteeghdslsvgsfeedsksefildppkpkppawfNGILTWEDFELVNPHRARFLKEIKDLAI 2089
Cdd:cd00078   122 ----------------------------------------------------GKPLSLEDLEELDPELYKSLKELLDNDG 149

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210 2090 krrqilsnkglsedekntklqelvlknpsgsgpplSIEDLGLNFQFCPSSRIYGFTAVDLKPSGEDEMITMDNAEEYVDL 2169
Cdd:cd00078   150 -----------------------------------DEDDLELTFTIELDSSFGGAVTVELKPGGRDIPVTNENKEEYVDL 194

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210 2170 MFDFCMHTGIQKQMEAFRDGFNKVFPMEKLSSFSHEEVQMILCGNqsPSWAAEDIINYTEPKLGYTRDSPGFLRFVRVLC 2249
Cdd:cd00078   195 YVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGS--EDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLE 272

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210 2250 GMSSDERKAFLQFTTGCSTLPPGGLANLHPRLTvVRKVDATDASYPSVNTCVHYLKLPEYSSEEIMRERLLAATMEK-GF 2328
Cdd:cd00078   273 SFTNEERKKFLQFVTGSSRLPVGGFADLNPKFT-IRRVGSPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGaGF 351


                  .
gi 767980210 2329 H 2329
Cdd:cd00078   352 G 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
 1876-2328 2.20e-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: 2.20e-89
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210   1876 RKSVLEVEFLGEEG-TGLGPTLEFYALVAAEFQRTDLGAWLCDDNfpddesrhvdlggglkppgyyvqrSCGLFTAPFPQ 1954
Cdd:smart00119    3 KKRVLEIEFEGEEGlDGGGVTREFFFLLSKELFNPDYGLFRYSPN------------------------DYLLYPNPRSG 58

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210   1955 DSDElERItKLFHFLGIFLAKCIQDNRLVDLPISKPFFKLMCmgdiksnmskliyesrgdrdlhctesqseasteeghds 2034
Cdd:smart00119   59 FANE-EHL-SYFRFIGRVLGKALYDNRLLDLFFARPFYKKLL-------------------------------------- 98

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210   2035 lsvgsfeedsksefildppkpkppawfNGILTWEDFELVNPHRARFLKEIKdlaikrrqilsnkgLSEDEkntklqelvl 2114
Cdd:smart00119   99 ---------------------------GKPVTLHDLESLDPELYKSLKWLL--------------LNNDT---------- 127

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210   2115 knpsgsgpplsIEDLGLNFQFCPSSRIYGFTAVDLKPSGEDEMITMDNAEEYVDLMFDFCMHTGIQKQMEAFRDGFNKVF 2194
Cdd:smart00119  128 -----------SEELDLTFSIVLTSEFGQVKVVELKPGGSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVI 196

                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210   2195 PMEKLSSFSHEEVQMILCGnqSPSWAAEDIINYTEPKLGYTRDSPGFLRFVRVLCGMSSDERKAFLQFTTGCSTLPPGGL 2274
Cdd:smart00119  197 PENLLKLFDPEELELLICG--SPEIDVDDLKSNTEYKGGYSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGF 274

                           410       420       430       440       450
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 767980210   2275 ANLHPRLTvVRKVDATDASYPSVNTCVHYLKLPEYSSEEIMRERLLAATME-KGF 2328
Cdd:smart00119  275 AALSPKFT-IRKAGSDDERLPTAHTCFNRLKLPPYSSKEILREKLLLAINEgKGF 328
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
 1943-2330 1.18e-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: 245.60  E-value: 1.18e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210  1943 RSCGLFTAPFPQDSDELERItKLFHFLGIFLAKCIQDNRLVDLPISKPFFKLMCmgdiksnmskliyesrgdrdlhctes 2022
Cdd:pfam00632   21 DDRTYWFNPSSSESPDLELL-DYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLL-------------------------- 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210  2023 qseasteeghdslsvgsfeedsksefildppkpkppawfNGILTWEDFELVNPHRARFLKEIKDLaikrrqilsnkglSE 2102
Cdd:pfam00632   74 ---------------------------------------GEPLTLEDLESIDPELYKSLKSLLNM-------------DN 101

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210  2103 DEKntklqelvlknpsgsgpplsiEDLGLNFQFCpssrIYGFTA-VDLKPSGEDEMITMDNAEEYVDLMFDFCMHTGIQK 2181
Cdd:pfam00632  102 DDD---------------------EDLGLTFTIP----VFGESKtIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEP 156

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210  2182 QMEAFRDGFNKVFPMEKLSSFSHEEVQMILCGnqSPSWAAEDIINYTEPKLGYTRDSPGFLRFVRVLCGMSSDERKAFLQ 2261
Cdd:pfam00632  157 QLEAFRKGFYSVIPKEALSLFTPEELELLICG--SPEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLK 234

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210  2262 FTTGCSTLPPGGLANLhPRLTVVRKVDATDASYPSVNTCVHYLKLPEYSSEEIMRERLLAATME-KGFHL 2330
Cdd:pfam00632  235 FVTGSSRLPVGGFKSL-PKFTIVRKGGDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEgEGFGL 303
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
1769-2328 6.48e-55

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 208.85  E-value: 6.48e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210 1769 QIEEPLALASGALPDWCEQLTskcPFLIPFETRQLYFTCTAFgasraivWLQNRREATVERTRTTSSVRRDDPGEFRVGR 1848
Cdd:COG5021   425 ESDESFYVASNVQQQRASREG---PLLSGWKTRLNNLYRFYF-------VEHRKKTLTKNDSRLGSFISLNKLDIRRIKE 494

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210 1849 LKHERVKVprgeSLMEWAENVM---QIHADRKSVLEV---EFLGEEGTGLGPTLEFYALVAAEFQRTDLGAW----LCDD 1918
Cdd:COG5021   495 DKRRKLFY----SLKQKAKIFDpylHIKVRRDRVFEDsyrEIMDESGDDLKKTLEIEFVGEEGIDAGGLTREwlflLSKE 570

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210 1919 NFPDDesrhvdlggglkpPGYYVQRSCGLFTAPFPQDSDELERITKLFHFLGIFLAKCIQDNRLVDLPISKPFFKLMCmg 1998
Cdd:COG5021   571 MFNPD-------------YGLFEYITEDLYTLPINPLSSINPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLL-- 635

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210 1999 diksnmskliyesrgdrdlhctesqseasteeghdslsvgsfeedsksefildppkPKPpawfngiLTWEDFELVNPHRA 2078
Cdd:COG5021   636 --------------------------------------------------------GKP-------VSLVDLESLDPELY 652

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210 2079 RFLKEIKDLaikrrqilsnkglSEDEKNtklqelvlknpsgsgpplsiedLGLNFQFcpSSRIYGFTA-VDLKPSGEDEM 2157
Cdd:COG5021   653 RSLVWLLNN-------------DIDETI----------------------LDLTFTV--EDDSFGESRtVELIPNGRNIS 695

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210 2158 ITMDNAEEYVDLMFDFCMHTGIQKQMEAFRDGFNKVFPMEKLSSFSHEEVQMILCGNQSPSwAAEDIINYTEPKlGYTRD 2237
Cdd:COG5021   696 VTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEDI-DIDDWKSNTAYH-GYTED 773

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210 2238 SPGFLRFVRVLCGMSSDERKAFLQFTTGCSTLPPGGLANLHPRLTVVRKV--DATDASY--PSVNTCVHYLKLPEYSSEE 2313
Cdd:COG5021   774 SPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTieKGGTDDDrlPSAHTCFNRLKLPEYSSKE 853

                         570
                  ....*....|....*.
gi 767980210 2314 IMRERLLAATME-KGF 2328
Cdd:COG5021   854 KLRSKLLTAINEgAGF 869
BTHB_HectD1 cd21062
basic tilted helix bundle (BTHB) domain found in HECT domain-containing protein 1 (HectD1) and ...
 1614-1679 9.97e-38

basic tilted helix bundle (BTHB) domain found in HECT domain-containing protein 1 (HectD1) and similar proteins; HectD1, also called E3 ligase for inhibin receptor (EULIR), is a Hect-type E3 ubiquitin transferase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. HectD1 is required for development of head mesenchyme and neural tube closure.


Pssm-ID: 439138  Cd Length: 66  Bit Score: 136.26  E-value: 9.97e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767980210 1614 CWSIEHVEQYLGTDELPKNDLITYLQKNADAAFLRHWKLTGTNKSIRKNRNCSQLIAAYKDFCEHG 1679
Cdd:cd21062     1 EWTVEYVEQSLGTGELPKSDVITYLQKNADEAFLRRWKLTGTAKNIRKNRNCSQLIAAYKEFCEHG 66
Sad1_UNC pfam07738
Sad1 / UNC-like C-terminal; The C. elegans UNC-84 protein is a nuclear envelope protein that ...
 1107-1240 8.33e-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: 8.33e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210  1107 RNLPYGRLEDILSRDNSALNCHSNDDKNAWFAIDLGLWVIPSAYTLRHARGYGR-SALRNWVFQVSKDGQNWTslYTHVD 1185
Cdd:pfam07738    1 LNYEAKPPKVILQPDYMPGPCWSFKGSRGFVVIELSEFIIVEAITLEHVEKSVFsSAPKDFEVSGSDRYPTTK--WVLLG 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 767980210  1186 DCSLNEPGSTA-TWPLDPPKDEkqGWRHVR--IKQMGknasGQTHYLSLSGFELYGTV 1240
Cdd:pfam07738   79 EFSYDLDGKTIqTFQLENPPDI--WVKYVKlrILSNY----GNEHYTCLYRFRVHGTV 130
BTHB cd21035
basic tilted helix bundle (BTHB) domain; BTHB domain is found in the N-terminal region of ...
 1614-1677 3.83e-31

basic tilted helix bundle (BTHB) domain; BTHB domain is found in the N-terminal region of FKBPs such as FKBP25 and in the core region of E3 ubiquitin ligase HectD1. It adopts a compact 5-helix bundle, hence termed BTHB (Basic Tilted Helix Bundle) domain. In FKBP25, it may have a role in regulating the association state of nucleosomes by interacting with nucleolin. This basic domain in FKBP25 also forms alternative complexes with other chromatin-related proteins, such as the HDAC1, HDAC2, and the transcriptional regulator YY1, the DNA binding activity of which is enhanced on binding FKBP25. Structural analysis of this fold suggests that the DNA binding properties of FKBP25 and HectD1 are presented by the conserved basic region.


Pssm-ID: 439137  Cd Length: 64  Bit Score: 117.22  E-value: 3.83e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767980210 1614 CWSIEHVEQYLGTDELPKNDLITYLQKNADAAFLRHWKLTGTNKSIRKNRNCSQLIAAYKDFCE 1677
Cdd:cd21035     1 VWTKQFDEAYTASDNLPKKDVVDFLQKYADNSFLREHKLNGSAKSVLKNRNKDQLVEAYNKVFE 64
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
366-479 7.48e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 110.04  E-value: 7.48e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210  366 LIDCIRSKDTDALIDAIDTGAfEVNFMDDVGQTLLNWASAFGTQEMVEFLCERGADVNR--GQRSSSLHYAACFGRPQVA 443
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGA-DVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAqdNDGNTPLHLAAANGNLEIV 169

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 767980210  444 KTLLRHGANPDLRDEDGKTPLDKARERGHSEVVAIL 479
Cdd:COG0666   170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
366-480 7.53e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 104.27  E-value: 7.53e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210  366 LIDCIRSKDTDA---LIDAidtGAfEVNFMDDVGQTLLNWASAFGTQEMVEFLCERGADVNRGQRS--SSLHYAACFGRP 440
Cdd:COG0666   124 LHLAAYNGNLEIvklLLEA---GA-DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDgeTPLHLAAENGHL 199

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 767980210  441 QVAKTLLRHGANPDLRDEDGKTPLDKARERGHSEVVAILQ 480
Cdd:COG0666   200 EIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
366-479 3.36e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 93.48  E-value: 3.36e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210  366 LIDCIRSKDTDALIDAIDTGAFEVNFMDDVGQTLLNWASAFGTQEMVEFLCERGADVNR--GQRSSSLHYAACFGRPQVA 443
Cdd:COG0666    57 LLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNArdKDGETPLHLAAYNGNLEIV 136

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 767980210  444 KTLLRHGANPDLRDEDGKTPLDKARERGHSEVVAIL 479
Cdd:COG0666   137 KLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172
BTHB pfam18410
Basic tilted helix bundle domain; This domain is found on the N-terminal region of FKBPs such ...
 1615-1680 3.85e-15

Basic tilted helix bundle domain; This domain is found on the N-terminal region of FKBPs such as FKBP25 and in the core region of E3 ubiquitin ligase HectD1. It adopts a compact 5-helix bundle, hence termed BTHB (Basic Tilted Helix Bundle) domain. In FKBP25, it has been suggested to have a role in regulating the association state of nucleosomes by interacting with nucleolin. Moreover, this basic domain in FKBP25 forms alternative complexes with other chromatin-related proteins, such as the HDAC1, HDAC2, and the transcriptional regulator YY1, the DNA binding activity of which is enhanced on binding FKBP25. Structural analysis of this fold suggests that the DNA binding properties of FKBP25 and HectD1 are presented by the conserved basic region.


Pssm-ID: 465755  Cd Length: 72  Bit Score: 72.02  E-value: 3.85e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767980210  1615 WSIEhveqYLGTDELPKNDLITYLQKNADAAFLRHWKLTGTNKSIRKNRNCSQLIAAYKDFCEHGT 1680
Cdd:pfam18410    5 WTEE----QLLSDALPKKDIIKFLQDNASLSFLKEHKLNGALKNVAKTAKKDQLAEAYNKLFESKR 66
Ank_2 pfam12796
Ankyrin repeats (3 copies);
366-457 1.32e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.52  E-value: 1.32e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210   366 LIDCIRSKDTDALIDAIDTGAfEVNFMDDVGQTLLNWASAFGTQEMVEFLCERGADVNRGQRSSSLHYAACFGRPQVAKT 445
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGA-DANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRTALHYAARSGHLEIVKL 79

                           90
                   ....*....|..
gi 767980210   446 LLRHGANPDLRD 457
Cdd:pfam12796   80 LLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
370-479 3.04e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 69.60  E-value: 3.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210  370 IRSKDTDALIDAIDTGAFEVNFMDDVGQTLLNWASAFGTQEMVEFLCERGADVNRG--QRSSSLHYAACFGRPQVAKTLL 447
Cdd:COG0666    28 AALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKddGGNTLLHAAARNGDLEIVKLLL 107

                          90       100       110
                  ....*....|....*....|....*....|..
gi 767980210  448 RHGANPDLRDEDGKTPLDKARERGHSEVVAIL 479
Cdd:COG0666   108 EAGADVNARDKDGETPLHLAAYNGNLEIVKLL 139
Ank_2 pfam12796
Ankyrin repeats (3 copies);
400-483 1.42e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 59.74  E-value: 1.42e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210   400 LNWASAFGTQEMVEFLCERGADVN--RGQRSSSLHYAACFGRPQVAKTLLRHgANPDLRDeDGKTPLDKARERGHSEVVA 477
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANlqDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78


                   ....*.
gi 767980210   478 ILQSPG 483
Cdd:pfam12796   79 LLLEKG 84
BTHB_FKBP25 cd21063
basic tilted helix bundle (BTHB) domain found in 25 kDa FK506-binding protein (FKBP25) and ...
 1620-1674 5.41e-09

basic tilted helix bundle (BTHB) domain found in 25 kDa FK506-binding protein (FKBP25) and similar proteins; FKBP25, also called 25 kDa FKBP, FK506-binding protein 3 (FKBP-3), immunophilin FKBP-25, rapamycin-selective 25 kDa immunophilin or rotamase, acts as a peptidyl-prolyl cis-trans isomerase (PPIase, EC 5.2.1.8) that interconverts the cis and trans isomers of peptide bonds with the amino acid proline. FKBP25 binds both FK506 and rapamycin, and thus belongs to a family of receptors for the two immunosuppressants which inhibit T-cell proliferation by arresting two distinct cytoplasmic signal transmission pathways.


Pssm-ID: 439139  Cd Length: 67  Bit Score: 54.53  E-value: 5.41e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767980210 1620 VEQyLGTDELPKNDLITYLQKNADAAFLRHWKLTGTNKSIRKNRNCSQLIAAYKD 1674
Cdd:cd21063     6 EEQ-LASDAVSKKDLIEFLQENASNSFLAEHKLLGKLKNVAKTAKKDQLVEAYNQ 59
MIB_HERC2 pfam06701
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain ...
 1277-1302 1.51e-08

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: 52.99  E-value: 1.51e-08
                           10        20
                   ....*....|....*....|....*.
gi 767980210  1277 GARVIRGLDWKWRDQDGSPQGEGTVT 1302
Cdd:pfam06701    1 GARVVRGPDWKWGDQDGGEGHVGTVV 26
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 404-481 8.51e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 57.60  E-value: 8.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210  404 SAFGTQEMVEFLCERGADVNRG--QRSSSLHYAACFGRPQVAKTLLRHGANPDLRDEDGKTPLDKARERGHSEVVAILQS 481
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRdyDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
Ank_4 pfam13637
Ankyrin repeats (many copies);
427-479 8.80e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.74  E-value: 8.80e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 767980210   427 RSSSLHYAACFGRPQVAKTLLRHGANPDLRDEDGKTPLDKARERGHSEVVAIL 479
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 370-464 1.20e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 53.73  E-value: 1.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210  370 IRSKDTDALIDA------IDTGAfEVNFMD-DVGQTLLNWASAFGTQEMVEFLCERGADVNRGQR--SSSLHYAACFGRP 440
Cdd:PHA02878  136 IDKKSKDDIIEAeitkllLSYGA-DINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKtnNSPLHHAVKHYNK 214

                          90       100
                  ....*....|....*....|....
gi 767980210  441 QVAKTLLRHGANPDLRDEDGKTPL 464
Cdd:PHA02878  215 PIVHILLENGASTDARDKCGNTPL 238
PHA03095 PHA03095
ankyrin-like protein; Provisional
 393-477 2.83e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 52.33  E-value: 2.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210  393 DDVGQTLLNWASAFGTQE--MVEFLCERGADVN----RGQrsSSLHYAACFGRPQVAKTLLRHGANPDLRDEDGKTPLDK 466
Cdd:PHA03095  219 DMLGNTPLHSMATGSSCKrsLVLPLLIAGISINarnrYGQ--TPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSL 296

                          90
                  ....*....|.
gi 767980210  467 ARERGHSEVVA 477
Cdd:PHA03095  297 MVRNNNGRAVR 307
Ank_5 pfam13857
Ankyrin repeats (many copies);
418-467 6.16e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.42  E-value: 6.16e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 767980210   418 RGADVNR--GQRSSSLHYAACFGRPQVAKTLLRHGANPDLRDEDGKTPLDKA 467
Cdd:pfam13857    5 GPIDLNRldGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 410-484 1.36e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 50.05  E-value: 1.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210  410 EMVEFLCERGADVN--------------------RGqrSSSLHYAACFGRPQVAKTLLRHGANPDLRDEDGKTPLDKARE 469
Cdd:PHA03100  157 KILKLLIDKGVDINaknrvnyllsygvpinikdvYG--FTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAIL 234

                          90
                  ....*....|....*
gi 767980210  470 RGHSEVVAILQSPGD 484
Cdd:PHA03100  235 NNNKEIFKLLLNNGP 249
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 391-483 2.34e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 49.22  E-value: 2.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210  391 FMDDV----GQTLLNWASAFGTQEMVEFLCERGAD--VNRGQRSSSLHYAACFGRPQVAKTLLRHGANPDLRDEDGKTPL 464
Cdd:PHA02875   93 FADDVfykdGMTPLHLATILKKLDIMKLLIARGADpdIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPL 172

                          90
                  ....*....|....*....
gi 767980210  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 3.55e-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: 3.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210  1127 CHSNDDKNAWFAIDLGlwvipSAYTLRHARGYGRSALRN-----WVFQVSKDGQNWTSLYTHVDDcSLNEPGSTATWPLD 1201
Cdd:pfam00754   27 SAWSGDDPQWIQVDLG-----KPKKITGVVTQGRQDGSNgyvtsYKIEYSLDGENWTTVKDEKIP-GNNDNNTPVTNTFD 100

                           90
                   ....*....|....*
gi 767980210  1202 PPKDEkqgwRHVRIK 1216
Cdd:pfam00754  101 PPIKA----RYVRIV 111
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 410-464 9.05e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 45.97  E-value: 9.05e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767980210  410 EMVEFLCERGADVN---RGQRSSSLHYAACFGR---PQVAKTLLRHGANPDLRDEDGKTPL 464
Cdd:PHA02859   67 EILKFLIENGADVNfktRDNNLSALHHYLSFNKnvePEILKILIDSGSSITEEDEDGKNLL 127
PHA03095 PHA03095
ankyrin-like protein; Provisional
 408-465 1.73e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.56  E-value: 1.73e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767980210  408 TQEMVEFLCERGADVNR--GQRSSSLH-YAACFG-RPQVAKTLLRHGANPDLRDEDGKTPLD 465
Cdd:PHA03095   96 TLDVIKLLIKAGADVNAkdKVGRTPLHvYLSGFNiNPKVIRLLLRKGADVNALDLYGMTPLA 157
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 410-479 5.72e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 44.87  E-value: 5.72e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767980210  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 1.00e-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: 1.00e-03
                           10        20
                   ....*....|....*....|....*....
gi 767980210   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 1.35e-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: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210  396 GQTLLNWASAFGTQEMVEFLCERGADVN---------RGQRSSSLHY-------AACFGRPQVAKTLLRHGANPDLRDED 459
Cdd:cd22192    89 GETALHIAVVNQNLNLVRELIARGADVVspratgtffRPGPKNLIYYgehplsfAACVGNEEIVRLLIEHGADIRAQDSL 168


                  ....*
gi 767980210  460 GKTPL 464
Cdd:cd22192   169 GNTVL 173
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 370-467 1.53e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 43.41  E-value: 1.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210  370 IRSKDTDALIDAIDTGAfEVNFMDDVGQTLLNWASAFGTQEMVEFLCERGA--DVNRGQRSSSLHYAACFGRPQVAKTLL 447
Cdd:PHA02874  132 IKKGDLESIKMLFEYGA-DVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAyaNVKDNNGESPLHNAAEYGDYACIKLLI 210

                          90       100
                  ....*....|....*....|
gi 767980210  448 RHGANPDLRDEDGKTPLDKA 467
Cdd:PHA02874  211 DHGNHIMNKCKNGFTPLHNA 230
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 409-486 2.56e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 42.64  E-value: 2.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210  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 2.95e-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: 2.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210 1127 CHSNDDKNAWFAIDLGL--WVIPSAYTLRHaRGYGRSALRNWVFQVSKDGQNWTSLYTHVDDCSLN---EPGSTATWPLD 1201
Cdd:cd00057    38 TPAVNDPPQWLQVDLGKtrRVTGIQTQGRK-GGGSSEWVTSYKVQYSLDGETWTTYKDKGEEKVFTgnsDGSTPVTNDFP 116

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 767980210 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 5.80e-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: 5.80e-03
                            10        20
                    ....*....|....*....|....*
gi 767980210    431 LHYAACFGRPQVAKTLLRHGANPDL 455
Cdd:smart00248    6 LHLAAENGNLEVVKLLLDKGADINA 30
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 403-487 8.53e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.39  E-value: 8.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980210  403 ASAFGTQEMVEFLCERG--ADVNRGQRSSSLHYAACFGRPQVAKTLLRHGANPDLRDEDGKTPLDKARERGHSEVVAIL- 479
Cdd:PLN03192  532 VASTGNAALLEELLKAKldPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILy 611

                          90
                  ....*....|....*.
gi 767980210  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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