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Conserved domains on  [gi|1622951571|ref|XP_028706381|]
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E3 ubiquitin-protein ligase HECTD1 isoform X3 [Macaca mulatta]

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 ...
 2091-2568 2.17e-119

HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It binds specific ubiquitin-conjugating enzymes (E2), accepts ubiquitin from E2, transfers ubiquitin to substrate lysine side chains, and transfers additional ubiquitin molecules to the end of growing ubiquitin chains.


:

Pssm-ID: 238033 [Multi-domain]  Cd Length: 352  Bit Score: 382.30  E-value: 2.17e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571 2091 ERVKVPRGESLMEWAENVMQIH-ADRKSVLEVEFLGEEGTG-LGPTLEFYALVAAEFQRTDLGAWLCDDNFpddesrhvd 2168
Cdd:cd00078      1 LKITVRRDRILEDALRQLSKVSsSDLKKVLEVEFVGEEGIDaGGVTREFFTLVSKELFNPSYGLFRYTPDD--------- 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571 2169 lggglkppgyyvqRSCGLFTAPFPQDSDELeritKLFHFLGIFLAKCIQDNRLVDLPISKPFFKLMCmgdiksnmskliy 2248
Cdd:cd00078     72 -------------SGLLYPNPSSFADEDHL----KLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLL------------- 121

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571 2249 esrgdrdlhctesqseasteeghdslsvgsfeedsksefildppkpkppawfNGILTWEDFELVNPHRARFLKEIKDLAI 2328
Cdd:cd00078    122 ----------------------------------------------------GKPLSLEDLEELDPELYKSLKELLDNDG 149

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571 2329 krrqilsnkglsedekntklqelvlknpsgsgpplSIEDLGLNFQFCPSSRIYGFTAVDLKPSGEDEMITMDNAEEYVDL 2408
Cdd:cd00078    150 -----------------------------------DEDDLELTFTIELDSSFGGAVTVELKPGGRDIPVTNENKEEYVDL 194

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571 2409 MFDFCMHTGIQKQMEAFRDGFNKVFPMEKLSSFSHEEVQMILCGNqsPSWAAEDIINYTEPKLGYTRDSPGFLRFVRVLC 2488
Cdd:cd00078    195 YVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGS--EDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLE 272

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571 2489 GMSSDERKAFLQFTTGCSTLPPGGLANLHPRLTvVRKVDATDASYPSVNTCVHYLKLPEYSSEEIMRERLLAATMEK-GF 2567
Cdd:cd00078    273 SFTNEERKKFLQFVTGSSRLPVGGFADLNPKFT-IRRVGSPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGaGF 351


                   .
gi 1622951571 2568 H 2568
Cdd:cd00078    352 G 352
BTHB_HectD1 cd21062
basic tilted helix bundle (BTHB) domain found in HECT domain-containing protein 1 (HectD1) and ...
 1853-1918 1.32e-37

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: 135.87  E-value: 1.32e-37
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622951571 1853 CWSIEHVEQYLGTDELPKNDLITYLQKNADAAFLRHWKLTGTNKSIRKNRNCSQLIAAYKDFCEHG 1918
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 ...
 1067-1200 9.21e-33

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


:

Pssm-ID: 400199  Cd Length: 130  Bit Score: 124.71  E-value: 9.21e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571 1067 RNLPYGRLEDILSRDNSALNCHSNDDKNAWFAIDLGLWVIPSAYTLRHARGYGR-SALRNWVFQVSKDGQNWTslYTHVD 1145
Cdd:pfam07738    1 LNYEAKPPKVILQPDYMPGPCWSFKGSRGFVVIELSEFIIVEAITLEHVEKSVFsSAPKDFEVSGSDRYPTTK--WVLLG 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622951571 1146 DCSLNEPGSTA-TWPLDPPKDEkqGWRHVR--IKQMGknasGQTHYLSLSGFELYGTV 1200
Cdd:pfam07738   79 EFSYDLDGKTIqTFQLENPPDI--WVKYVKlrILSNY----GNEHYTCLYRFRVHGTV 130
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
326-439 8.33e-26

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 110.04  E-value: 8.33e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571  326 LIDCIRSKDTDALIDAIDTGAfEVNFMDDVGQTLLNWASAFGTQEMVEFLCERGADVNR--GQRSSSLHYAACFGRPQVA 403
Cdd:COG0666     91 LHAAARNGDLEIVKLLLEAGA-DVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAqdNDGNTPLHLAAANGNLEIV 169

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1622951571  404 KTLLRHGANPDLRDEDGKTPLDKARERGHSEVVAIL 439
Cdd:COG0666    170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
MIB_HERC2 pfam06701
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain ...
 1237-1295 1.24e-24

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


:

Pssm-ID: 461991  Cd Length: 66  Bit Score: 98.83  E-value: 1.24e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622951571 1237 GARVIRGLDWKWRDQDGSPQGEGTVT------GELHNGWIDVTWDAGGSNSYRMGAEGKFDLKLA 1295
Cdd:pfam06701    1 GARVVRGPDWKWGDQDGGEGHVGTVVeirdwdSESPRSTVRVQWDNGSTNVYRVGYEGKYDLKVV 65
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
 2091-2568 2.17e-119

HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It binds specific ubiquitin-conjugating enzymes (E2), accepts ubiquitin from E2, transfers ubiquitin to substrate lysine side chains, and transfers additional ubiquitin molecules to the end of growing ubiquitin chains.


Pssm-ID: 238033 [Multi-domain]  Cd Length: 352  Bit Score: 382.30  E-value: 2.17e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571 2091 ERVKVPRGESLMEWAENVMQIH-ADRKSVLEVEFLGEEGTG-LGPTLEFYALVAAEFQRTDLGAWLCDDNFpddesrhvd 2168
Cdd:cd00078      1 LKITVRRDRILEDALRQLSKVSsSDLKKVLEVEFVGEEGIDaGGVTREFFTLVSKELFNPSYGLFRYTPDD--------- 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571 2169 lggglkppgyyvqRSCGLFTAPFPQDSDELeritKLFHFLGIFLAKCIQDNRLVDLPISKPFFKLMCmgdiksnmskliy 2248
Cdd:cd00078     72 -------------SGLLYPNPSSFADEDHL----KLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLL------------- 121

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571 2249 esrgdrdlhctesqseasteeghdslsvgsfeedsksefildppkpkppawfNGILTWEDFELVNPHRARFLKEIKDLAI 2328
Cdd:cd00078    122 ----------------------------------------------------GKPLSLEDLEELDPELYKSLKELLDNDG 149

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571 2329 krrqilsnkglsedekntklqelvlknpsgsgpplSIEDLGLNFQFCPSSRIYGFTAVDLKPSGEDEMITMDNAEEYVDL 2408
Cdd:cd00078    150 -----------------------------------DEDDLELTFTIELDSSFGGAVTVELKPGGRDIPVTNENKEEYVDL 194

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571 2409 MFDFCMHTGIQKQMEAFRDGFNKVFPMEKLSSFSHEEVQMILCGNqsPSWAAEDIINYTEPKLGYTRDSPGFLRFVRVLC 2488
Cdd:cd00078    195 YVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGS--EDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLE 272

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571 2489 GMSSDERKAFLQFTTGCSTLPPGGLANLHPRLTvVRKVDATDASYPSVNTCVHYLKLPEYSSEEIMRERLLAATMEK-GF 2567
Cdd:cd00078    273 SFTNEERKKFLQFVTGSSRLPVGGFADLNPKFT-IRRVGSPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGaGF 351


                   .
gi 1622951571 2568 H 2568
Cdd:cd00078    352 G 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
 2115-2567 2.46e-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: 2.46e-89
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571  2115 RKSVLEVEFLGEEG-TGLGPTLEFYALVAAEFQRTDLGAWLCDDNfpddesrhvdlggglkppgyyvqrSCGLFTAPFPQ 2193
Cdd:smart00119    3 KKRVLEIEFEGEEGlDGGGVTREFFFLLSKELFNPDYGLFRYSPN------------------------DYLLYPNPRSG 58

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571  2194 DSDElERItKLFHFLGIFLAKCIQDNRLVDLPISKPFFKLMCmgdiksnmskliyesrgdrdlhctesqseasteeghds 2273
Cdd:smart00119   59 FANE-EHL-SYFRFIGRVLGKALYDNRLLDLFFARPFYKKLL-------------------------------------- 98

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571  2274 lsvgsfeedsksefildppkpkppawfNGILTWEDFELVNPHRARFLKEIKdlaikrrqilsnkgLSEDEkntklqelvl 2353
Cdd:smart00119   99 ---------------------------GKPVTLHDLESLDPELYKSLKWLL--------------LNNDT---------- 127

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571  2354 knpsgsgpplsIEDLGLNFQFCPSSRIYGFTAVDLKPSGEDEMITMDNAEEYVDLMFDFCMHTGIQKQMEAFRDGFNKVF 2433
Cdd:smart00119  128 -----------SEELDLTFSIVLTSEFGQVKVVELKPGGSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVI 196

                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571  2434 PMEKLSSFSHEEVQMILCGnqSPSWAAEDIINYTEPKLGYTRDSPGFLRFVRVLCGMSSDERKAFLQFTTGCSTLPPGGL 2513
Cdd:smart00119  197 PENLLKLFDPEELELLICG--SPEIDVDDLKSNTEYKGGYSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGF 274

                           410       420       430       440       450
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1622951571  2514 ANLHPRLTvVRKVDATDASYPSVNTCVHYLKLPEYSSEEIMRERLLAATME-KGF 2567
Cdd:smart00119  275 AALSPKFT-IRKAGSDDERLPTAHTCFNRLKLPPYSSKEILREKLLLAINEgKGF 328
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
 2182-2569 1.16e-72

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 245.98  E-value: 1.16e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571 2182 RSCGLFTAPFPQDSDELERItKLFHFLGIFLAKCIQDNRLVDLPISKPFFKLMCmgdiksnmskliyesrgdrdlhctes 2261
Cdd:pfam00632   21 DDRTYWFNPSSSESPDLELL-DYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLL-------------------------- 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571 2262 qseasteeghdslsvgsfeedsksefildppkpkppawfNGILTWEDFELVNPHRARFLKEIKDLaikrrqilsnkglSE 2341
Cdd:pfam00632   74 ---------------------------------------GEPLTLEDLESIDPELYKSLKSLLNM-------------DN 101

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571 2342 DEKntklqelvlknpsgsgpplsiEDLGLNFQFCpssrIYGFTA-VDLKPSGEDEMITMDNAEEYVDLMFDFCMHTGIQK 2420
Cdd:pfam00632  102 DDD---------------------EDLGLTFTIP----VFGESKtIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEP 156

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571 2421 QMEAFRDGFNKVFPMEKLSSFSHEEVQMILCGnqSPSWAAEDIINYTEPKLGYTRDSPGFLRFVRVLCGMSSDERKAFLQ 2500
Cdd:pfam00632  157 QLEAFRKGFYSVIPKEALSLFTPEELELLICG--SPEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLK 234

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571 2501 FTTGCSTLPPGGLANLhPRLTVVRKVDATDASYPSVNTCVHYLKLPEYSSEEIMRERLLAATME-KGFHL 2569
Cdd:pfam00632  235 FVTGSSRLPVGGFKSL-PKFTIVRKGGDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEgEGFGL 303
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
2008-2567 9.39e-55

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 208.47  E-value: 9.39e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571 2008 QIEEPLALASGALPDWCEQLTskcPFLIPFETRQLYFTCTAFgasraivWLQNRREATVERTRTTSSVRRDDPGEFRVGR 2087
Cdd:COG5021    425 ESDESFYVASNVQQQRASREG---PLLSGWKTRLNNLYRFYF-------VEHRKKTLTKNDSRLGSFISLNKLDIRRIKE 494

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571 2088 LKHERVKVprgeSLMEWAENVM---QIHADRKSVLEV---EFLGEEGTGLGPTLEFYALVAAEFQRTDLGAW----LCDD 2157
Cdd:COG5021    495 DKRRKLFY----SLKQKAKIFDpylHIKVRRDRVFEDsyrEIMDESGDDLKKTLEIEFVGEEGIDAGGLTREwlflLSKE 570

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571 2158 NFPDDesrhvdlggglkpPGYYVQRSCGLFTAPFPQDSDELERITKLFHFLGIFLAKCIQDNRLVDLPISKPFFKLMCmg 2237
Cdd:COG5021    571 MFNPD-------------YGLFEYITEDLYTLPINPLSSINPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLL-- 635

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571 2238 diksnmskliyesrgdrdlhctesqseasteeghdslsvgsfeedsksefildppkPKPpawfngiLTWEDFELVNPHRA 2317
Cdd:COG5021    636 --------------------------------------------------------GKP-------VSLVDLESLDPELY 652

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571 2318 RFLKEIKDLaikrrqilsnkglSEDEKNtklqelvlknpsgsgpplsiedLGLNFQFcpSSRIYGFTA-VDLKPSGEDEM 2396
Cdd:COG5021    653 RSLVWLLNN-------------DIDETI----------------------LDLTFTV--EDDSFGESRtVELIPNGRNIS 695

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571 2397 ITMDNAEEYVDLMFDFCMHTGIQKQMEAFRDGFNKVFPMEKLSSFSHEEVQMILCGNQSPSwAAEDIINYTEPKlGYTRD 2476
Cdd:COG5021    696 VTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEDI-DIDDWKSNTAYH-GYTED 773

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571 2477 SPGFLRFVRVLCGMSSDERKAFLQFTTGCSTLPPGGLANLHPRLTVVRKV--DATDASY--PSVNTCVHYLKLPEYSSEE 2552
Cdd:COG5021    774 SPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTieKGGTDDDrlPSAHTCFNRLKLPEYSSKE 853

                          570
                   ....*....|....*.
gi 1622951571 2553 IMRERLLAATME-KGF 2567
Cdd:COG5021    854 KLRSKLLTAINEgAGF 869
BTHB_HectD1 cd21062
basic tilted helix bundle (BTHB) domain found in HECT domain-containing protein 1 (HectD1) and ...
 1853-1918 1.32e-37

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: 135.87  E-value: 1.32e-37
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622951571 1853 CWSIEHVEQYLGTDELPKNDLITYLQKNADAAFLRHWKLTGTNKSIRKNRNCSQLIAAYKDFCEHG 1918
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 ...
 1067-1200 9.21e-33

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


Pssm-ID: 400199  Cd Length: 130  Bit Score: 124.71  E-value: 9.21e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571 1067 RNLPYGRLEDILSRDNSALNCHSNDDKNAWFAIDLGLWVIPSAYTLRHARGYGR-SALRNWVFQVSKDGQNWTslYTHVD 1145
Cdd:pfam07738    1 LNYEAKPPKVILQPDYMPGPCWSFKGSRGFVVIELSEFIIVEAITLEHVEKSVFsSAPKDFEVSGSDRYPTTK--WVLLG 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622951571 1146 DCSLNEPGSTA-TWPLDPPKDEkqGWRHVR--IKQMGknasGQTHYLSLSGFELYGTV 1200
Cdd:pfam07738   79 EFSYDLDGKTIqTFQLENPPDI--WVKYVKlrILSNY----GNEHYTCLYRFRVHGTV 130
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
326-439 8.33e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 110.04  E-value: 8.33e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571  326 LIDCIRSKDTDALIDAIDTGAfEVNFMDDVGQTLLNWASAFGTQEMVEFLCERGADVNR--GQRSSSLHYAACFGRPQVA 403
Cdd:COG0666     91 LHAAARNGDLEIVKLLLEAGA-DVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAqdNDGNTPLHLAAANGNLEIV 169

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1622951571  404 KTLLRHGANPDLRDEDGKTPLDKARERGHSEVVAIL 439
Cdd:COG0666    170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
MIB_HERC2 pfam06701
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain ...
 1237-1295 1.24e-24

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


Pssm-ID: 461991  Cd Length: 66  Bit Score: 98.83  E-value: 1.24e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622951571 1237 GARVIRGLDWKWRDQDGSPQGEGTVT------GELHNGWIDVTWDAGGSNSYRMGAEGKFDLKLA 1295
Cdd:pfam06701    1 GARVVRGPDWKWGDQDGGEGHVGTVVeirdwdSESPRSTVRVQWDNGSTNVYRVGYEGKYDLKVV 65
BTHB pfam18410
Basic tilted helix bundle domain; This domain is found on the N-terminal region of FKBPs such ...
 1854-1919 4.25e-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: 4.25e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622951571 1854 WSIEhveqYLGTDELPKNDLITYLQKNADAAFLRHWKLTGTNKSIRKNRNCSQLIAAYKDFCEHGT 1919
Cdd:pfam18410    5 WTEE----QLLSDALPKKDIIKFLQDNASLSFLKEHKLNGALKNVAKTAKKDQLAEAYNKLFESKR 66
Ank_2 pfam12796
Ankyrin repeats (3 copies);
326-417 1.45e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.52  E-value: 1.45e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571  326 LIDCIRSKDTDALIDAIDTGAfEVNFMDDVGQTLLNWASAFGTQEMVEFLCERGADVNRGQRSSSLHYAACFGRPQVAKT 405
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGA-DANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRTALHYAARSGHLEIVKL 79

                           90
                   ....*....|..
gi 1622951571  406 LLRHGANPDLRD 417
Cdd:pfam12796   80 LLEKGADINVKD 91
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 364-441 1.04e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 57.60  E-value: 1.04e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571  364 SAFGTQEMVEFLCERGADVNRG--QRSSSLHYAACFGRPQVAKTLLRHGANPDLRDEDGKTPLDKARERGHSEVVAILQS 441
Cdd:PTZ00322    90 AASGDAVGARILLTGGADPNCRdyDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 356-424 1.50e-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: 1.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571  356 GQTLLNWASAFGTQEMVEFLCERGADVN---------RGQRSSSLHY-------AACFGRPQVAKTLLRHGANPDLRDED 419
Cdd:cd22192     89 GETALHIAVVNQNLNLVRELIARGADVVspratgtffRPGPKNLIYYgehplsfAACVGNEEIVRLLIEHGADIRAQDSL 168


                   ....*
gi 1622951571  420 GKTPL 424
Cdd:cd22192    169 GNTVL 173
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 1087-1198 3.27e-03

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


Pssm-ID: 238014 [Multi-domain]  Cd Length: 143  Bit Score: 40.41  E-value: 3.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571 1087 CHSNDDKNAWFAIDLGL--WVIPSAYTLRHaRGYGRSALRNWVFQVSKDGQNWTSLYTHVDDCSLN---EPGSTATWPLD 1161
Cdd:cd00057     38 TPAVNDPPQWLQVDLGKtrRVTGIQTQGRK-GGGSSEWVTSYKVQYSLDGETWTTYKDKGEEKVFTgnsDGSTPVTNDFP 116

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1622951571 1162 PPKDEkqgwRHVRIKQMGKNasgqtHYLSLsGFELYG 1198
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 ...
 391-415 6.39e-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: 6.39e-03
                            10        20
                    ....*....|....*....|....*
gi 1622951571   391 LHYAACFGRPQVAKTLLRHGANPDL 415
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 ...
 2091-2568 2.17e-119

HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It binds specific ubiquitin-conjugating enzymes (E2), accepts ubiquitin from E2, transfers ubiquitin to substrate lysine side chains, and transfers additional ubiquitin molecules to the end of growing ubiquitin chains.


Pssm-ID: 238033 [Multi-domain]  Cd Length: 352  Bit Score: 382.30  E-value: 2.17e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571 2091 ERVKVPRGESLMEWAENVMQIH-ADRKSVLEVEFLGEEGTG-LGPTLEFYALVAAEFQRTDLGAWLCDDNFpddesrhvd 2168
Cdd:cd00078      1 LKITVRRDRILEDALRQLSKVSsSDLKKVLEVEFVGEEGIDaGGVTREFFTLVSKELFNPSYGLFRYTPDD--------- 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571 2169 lggglkppgyyvqRSCGLFTAPFPQDSDELeritKLFHFLGIFLAKCIQDNRLVDLPISKPFFKLMCmgdiksnmskliy 2248
Cdd:cd00078     72 -------------SGLLYPNPSSFADEDHL----KLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLL------------- 121

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571 2249 esrgdrdlhctesqseasteeghdslsvgsfeedsksefildppkpkppawfNGILTWEDFELVNPHRARFLKEIKDLAI 2328
Cdd:cd00078    122 ----------------------------------------------------GKPLSLEDLEELDPELYKSLKELLDNDG 149

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571 2329 krrqilsnkglsedekntklqelvlknpsgsgpplSIEDLGLNFQFCPSSRIYGFTAVDLKPSGEDEMITMDNAEEYVDL 2408
Cdd:cd00078    150 -----------------------------------DEDDLELTFTIELDSSFGGAVTVELKPGGRDIPVTNENKEEYVDL 194

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571 2409 MFDFCMHTGIQKQMEAFRDGFNKVFPMEKLSSFSHEEVQMILCGNqsPSWAAEDIINYTEPKLGYTRDSPGFLRFVRVLC 2488
Cdd:cd00078    195 YVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGS--EDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLE 272

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571 2489 GMSSDERKAFLQFTTGCSTLPPGGLANLHPRLTvVRKVDATDASYPSVNTCVHYLKLPEYSSEEIMRERLLAATMEK-GF 2567
Cdd:cd00078    273 SFTNEERKKFLQFVTGSSRLPVGGFADLNPKFT-IRRVGSPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGaGF 351


                   .
gi 1622951571 2568 H 2568
Cdd:cd00078    352 G 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
 2115-2567 2.46e-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: 2.46e-89
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571  2115 RKSVLEVEFLGEEG-TGLGPTLEFYALVAAEFQRTDLGAWLCDDNfpddesrhvdlggglkppgyyvqrSCGLFTAPFPQ 2193
Cdd:smart00119    3 KKRVLEIEFEGEEGlDGGGVTREFFFLLSKELFNPDYGLFRYSPN------------------------DYLLYPNPRSG 58

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571  2194 DSDElERItKLFHFLGIFLAKCIQDNRLVDLPISKPFFKLMCmgdiksnmskliyesrgdrdlhctesqseasteeghds 2273
Cdd:smart00119   59 FANE-EHL-SYFRFIGRVLGKALYDNRLLDLFFARPFYKKLL-------------------------------------- 98

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571  2274 lsvgsfeedsksefildppkpkppawfNGILTWEDFELVNPHRARFLKEIKdlaikrrqilsnkgLSEDEkntklqelvl 2353
Cdd:smart00119   99 ---------------------------GKPVTLHDLESLDPELYKSLKWLL--------------LNNDT---------- 127

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571  2354 knpsgsgpplsIEDLGLNFQFCPSSRIYGFTAVDLKPSGEDEMITMDNAEEYVDLMFDFCMHTGIQKQMEAFRDGFNKVF 2433
Cdd:smart00119  128 -----------SEELDLTFSIVLTSEFGQVKVVELKPGGSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVI 196

                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571  2434 PMEKLSSFSHEEVQMILCGnqSPSWAAEDIINYTEPKLGYTRDSPGFLRFVRVLCGMSSDERKAFLQFTTGCSTLPPGGL 2513
Cdd:smart00119  197 PENLLKLFDPEELELLICG--SPEIDVDDLKSNTEYKGGYSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGF 274

                           410       420       430       440       450
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1622951571  2514 ANLHPRLTvVRKVDATDASYPSVNTCVHYLKLPEYSSEEIMRERLLAATME-KGF 2567
Cdd:smart00119  275 AALSPKFT-IRKAGSDDERLPTAHTCFNRLKLPPYSSKEILREKLLLAINEgKGF 328
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
 2182-2569 1.16e-72

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 245.98  E-value: 1.16e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571 2182 RSCGLFTAPFPQDSDELERItKLFHFLGIFLAKCIQDNRLVDLPISKPFFKLMCmgdiksnmskliyesrgdrdlhctes 2261
Cdd:pfam00632   21 DDRTYWFNPSSSESPDLELL-DYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLL-------------------------- 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571 2262 qseasteeghdslsvgsfeedsksefildppkpkppawfNGILTWEDFELVNPHRARFLKEIKDLaikrrqilsnkglSE 2341
Cdd:pfam00632   74 ---------------------------------------GEPLTLEDLESIDPELYKSLKSLLNM-------------DN 101

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571 2342 DEKntklqelvlknpsgsgpplsiEDLGLNFQFCpssrIYGFTA-VDLKPSGEDEMITMDNAEEYVDLMFDFCMHTGIQK 2420
Cdd:pfam00632  102 DDD---------------------EDLGLTFTIP----VFGESKtIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEP 156

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571 2421 QMEAFRDGFNKVFPMEKLSSFSHEEVQMILCGnqSPSWAAEDIINYTEPKLGYTRDSPGFLRFVRVLCGMSSDERKAFLQ 2500
Cdd:pfam00632  157 QLEAFRKGFYSVIPKEALSLFTPEELELLICG--SPEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLK 234

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571 2501 FTTGCSTLPPGGLANLhPRLTVVRKVDATDASYPSVNTCVHYLKLPEYSSEEIMRERLLAATME-KGFHL 2569
Cdd:pfam00632  235 FVTGSSRLPVGGFKSL-PKFTIVRKGGDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEgEGFGL 303
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
2008-2567 9.39e-55

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 208.47  E-value: 9.39e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571 2008 QIEEPLALASGALPDWCEQLTskcPFLIPFETRQLYFTCTAFgasraivWLQNRREATVERTRTTSSVRRDDPGEFRVGR 2087
Cdd:COG5021    425 ESDESFYVASNVQQQRASREG---PLLSGWKTRLNNLYRFYF-------VEHRKKTLTKNDSRLGSFISLNKLDIRRIKE 494

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571 2088 LKHERVKVprgeSLMEWAENVM---QIHADRKSVLEV---EFLGEEGTGLGPTLEFYALVAAEFQRTDLGAW----LCDD 2157
Cdd:COG5021    495 DKRRKLFY----SLKQKAKIFDpylHIKVRRDRVFEDsyrEIMDESGDDLKKTLEIEFVGEEGIDAGGLTREwlflLSKE 570

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571 2158 NFPDDesrhvdlggglkpPGYYVQRSCGLFTAPFPQDSDELERITKLFHFLGIFLAKCIQDNRLVDLPISKPFFKLMCmg 2237
Cdd:COG5021    571 MFNPD-------------YGLFEYITEDLYTLPINPLSSINPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLL-- 635

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571 2238 diksnmskliyesrgdrdlhctesqseasteeghdslsvgsfeedsksefildppkPKPpawfngiLTWEDFELVNPHRA 2317
Cdd:COG5021    636 --------------------------------------------------------GKP-------VSLVDLESLDPELY 652

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571 2318 RFLKEIKDLaikrrqilsnkglSEDEKNtklqelvlknpsgsgpplsiedLGLNFQFcpSSRIYGFTA-VDLKPSGEDEM 2396
Cdd:COG5021    653 RSLVWLLNN-------------DIDETI----------------------LDLTFTV--EDDSFGESRtVELIPNGRNIS 695

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571 2397 ITMDNAEEYVDLMFDFCMHTGIQKQMEAFRDGFNKVFPMEKLSSFSHEEVQMILCGNQSPSwAAEDIINYTEPKlGYTRD 2476
Cdd:COG5021    696 VTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEDI-DIDDWKSNTAYH-GYTED 773

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571 2477 SPGFLRFVRVLCGMSSDERKAFLQFTTGCSTLPPGGLANLHPRLTVVRKV--DATDASY--PSVNTCVHYLKLPEYSSEE 2552
Cdd:COG5021    774 SPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTieKGGTDDDrlPSAHTCFNRLKLPEYSSKE 853

                          570
                   ....*....|....*.
gi 1622951571 2553 IMRERLLAATME-KGF 2567
Cdd:COG5021    854 KLRSKLLTAINEgAGF 869
BTHB_HectD1 cd21062
basic tilted helix bundle (BTHB) domain found in HECT domain-containing protein 1 (HectD1) and ...
 1853-1918 1.32e-37

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: 135.87  E-value: 1.32e-37
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622951571 1853 CWSIEHVEQYLGTDELPKNDLITYLQKNADAAFLRHWKLTGTNKSIRKNRNCSQLIAAYKDFCEHG 1918
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 ...
 1067-1200 9.21e-33

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


Pssm-ID: 400199  Cd Length: 130  Bit Score: 124.71  E-value: 9.21e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571 1067 RNLPYGRLEDILSRDNSALNCHSNDDKNAWFAIDLGLWVIPSAYTLRHARGYGR-SALRNWVFQVSKDGQNWTslYTHVD 1145
Cdd:pfam07738    1 LNYEAKPPKVILQPDYMPGPCWSFKGSRGFVVIELSEFIIVEAITLEHVEKSVFsSAPKDFEVSGSDRYPTTK--WVLLG 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622951571 1146 DCSLNEPGSTA-TWPLDPPKDEkqGWRHVR--IKQMGknasGQTHYLSLSGFELYGTV 1200
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 ...
 1853-1916 4.22e-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: 4.22e-31
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622951571 1853 CWSIEHVEQYLGTDELPKNDLITYLQKNADAAFLRHWKLTGTNKSIRKNRNCSQLIAAYKDFCE 1916
Cdd:cd21035      1 VWTKQFDEAYTASDNLPKKDVVDFLQKYADNSFLREHKLNGSAKSVLKNRNKDQLVEAYNKVFE 64
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
326-439 8.33e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 110.04  E-value: 8.33e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571  326 LIDCIRSKDTDALIDAIDTGAfEVNFMDDVGQTLLNWASAFGTQEMVEFLCERGADVNR--GQRSSSLHYAACFGRPQVA 403
Cdd:COG0666     91 LHAAARNGDLEIVKLLLEAGA-DVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAqdNDGNTPLHLAAANGNLEIV 169

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1622951571  404 KTLLRHGANPDLRDEDGKTPLDKARERGHSEVVAIL 439
Cdd:COG0666    170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
MIB_HERC2 pfam06701
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain ...
 1237-1295 1.24e-24

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


Pssm-ID: 461991  Cd Length: 66  Bit Score: 98.83  E-value: 1.24e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622951571 1237 GARVIRGLDWKWRDQDGSPQGEGTVT------GELHNGWIDVTWDAGGSNSYRMGAEGKFDLKLA 1295
Cdd:pfam06701    1 GARVVRGPDWKWGDQDGGEGHVGTVVeirdwdSESPRSTVRVQWDNGSTNVYRVGYEGKYDLKVV 65
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
326-440 8.38e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 104.27  E-value: 8.38e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571  326 LIDCIRSKDTDA---LIDAidtGAfEVNFMDDVGQTLLNWASAFGTQEMVEFLCERGADVNRGQRS--SSLHYAACFGRP 400
Cdd:COG0666    124 LHLAAYNGNLEIvklLLEA---GA-DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDgeTPLHLAAENGHL 199

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1622951571  401 QVAKTLLRHGANPDLRDEDGKTPLDKARERGHSEVVAILQ 440
Cdd:COG0666    200 EIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
326-439 3.73e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 93.48  E-value: 3.73e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571  326 LIDCIRSKDTDALIDAIDTGAFEVNFMDDVGQTLLNWASAFGTQEMVEFLCERGADVNR--GQRSSSLHYAACFGRPQVA 403
Cdd:COG0666     57 LLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNArdKDGETPLHLAAYNGNLEIV 136

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1622951571  404 KTLLRHGANPDLRDEDGKTPLDKARERGHSEVVAIL 439
Cdd:COG0666    137 KLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172
BTHB pfam18410
Basic tilted helix bundle domain; This domain is found on the N-terminal region of FKBPs such ...
 1854-1919 4.25e-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: 4.25e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622951571 1854 WSIEhveqYLGTDELPKNDLITYLQKNADAAFLRHWKLTGTNKSIRKNRNCSQLIAAYKDFCEHGT 1919
Cdd:pfam18410    5 WTEE----QLLSDALPKKDIIKFLQDNASLSFLKEHKLNGALKNVAKTAKKDQLAEAYNKLFESKR 66
Ank_2 pfam12796
Ankyrin repeats (3 copies);
326-417 1.45e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.52  E-value: 1.45e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571  326 LIDCIRSKDTDALIDAIDTGAfEVNFMDDVGQTLLNWASAFGTQEMVEFLCERGADVNRGQRSSSLHYAACFGRPQVAKT 405
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGA-DANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRTALHYAARSGHLEIVKL 79

                           90
                   ....*....|..
gi 1622951571  406 LLRHGANPDLRD 417
Cdd:pfam12796   80 LLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
330-439 3.37e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 69.60  E-value: 3.37e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571  330 IRSKDTDALIDAIDTGAFEVNFMDDVGQTLLNWASAFGTQEMVEFLCERGADVNRG--QRSSSLHYAACFGRPQVAKTLL 407
Cdd:COG0666     28 AALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKddGGNTLLHAAARNGDLEIVKLLL 107

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1622951571  408 RHGANPDLRDEDGKTPLDKARERGHSEVVAIL 439
Cdd:COG0666    108 EAGADVNARDKDGETPLHLAAYNGNLEIVKLL 139
Ank_2 pfam12796
Ankyrin repeats (3 copies);
360-443 1.57e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 59.74  E-value: 1.57e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571  360 LNWASAFGTQEMVEFLCERGADVN--RGQRSSSLHYAACFGRPQVAKTLLRHgANPDLRDeDGKTPLDKARERGHSEVVA 437
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANlqDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78


                   ....*.
gi 1622951571  438 ILQSPG 443
Cdd:pfam12796   79 LLLEKG 84
BTHB_FKBP25 cd21063
basic tilted helix bundle (BTHB) domain found in 25 kDa FK506-binding protein (FKBP25) and ...
 1859-1913 5.97e-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: 5.97e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1622951571 1859 VEQyLGTDELPKNDLITYLQKNADAAFLRHWKLTGTNKSIRKNRNCSQLIAAYKD 1913
Cdd:cd21063      6 EEQ-LASDAVSKKDLIEFLQENASNSFLAEHKLLGKLKNVAKTAKKDQLVEAYNQ 59
Ank_4 pfam13637
Ankyrin repeats (many copies);
387-439 9.70e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.74  E-value: 9.70e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1622951571  387 RSSSLHYAACFGRPQVAKTLLRHGANPDLRDEDGKTPLDKARERGHSEVVAIL 439
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 364-441 1.04e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 57.60  E-value: 1.04e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571  364 SAFGTQEMVEFLCERGADVNRG--QRSSSLHYAACFGRPQVAKTLLRHGANPDLRDEDGKTPLDKARERGHSEVVAILQS 441
Cdd:PTZ00322    90 AASGDAVGARILLTGGADPNCRdyDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 330-424 1.33e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 53.73  E-value: 1.33e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571  330 IRSKDTDALIDA------IDTGAfEVNFMD-DVGQTLLNWASAFGTQEMVEFLCERGADVNRGQR--SSSLHYAACFGRP 400
Cdd:PHA02878   136 IDKKSKDDIIEAeitkllLSYGA-DINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKtnNSPLHHAVKHYNK 214

                           90       100
                   ....*....|....*....|....
gi 1622951571  401 QVAKTLLRHGANPDLRDEDGKTPL 424
Cdd:PHA02878   215 PIVHILLENGASTDARDKCGNTPL 238
PHA03095 PHA03095
ankyrin-like protein; Provisional
 353-437 3.15e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 52.33  E-value: 3.15e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571  353 DDVGQTLLNWASAFGTQE--MVEFLCERGADVN----RGQrsSSLHYAACFGRPQVAKTLLRHGANPDLRDEDGKTPLDK 426
Cdd:PHA03095   219 DMLGNTPLHSMATGSSCKrsLVLPLLIAGISINarnrYGQ--TPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSL 296

                           90
                   ....*....|.
gi 1622951571  427 ARERGHSEVVA 437
Cdd:PHA03095   297 MVRNNNGRAVR 307
Ank_5 pfam13857
Ankyrin repeats (many copies);
378-427 6.86e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.42  E-value: 6.86e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1622951571  378 RGADVNR--GQRSSSLHYAACFGRPQVAKTLLRHGANPDLRDEDGKTPLDKA 427
Cdd:pfam13857    5 GPIDLNRldGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 370-444 1.51e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 50.05  E-value: 1.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571  370 EMVEFLCERGADVN--------------------RGqrSSSLHYAACFGRPQVAKTLLRHGANPDLRDEDGKTPLDKARE 429
Cdd:PHA03100   157 KILKLLIDKGVDINaknrvnyllsygvpinikdvYG--FTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAIL 234

                           90
                   ....*....|....*
gi 1622951571  430 RGHSEVVAILQSPGD 444
Cdd:PHA03100   235 NNNKEIFKLLLNNGP 249
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 351-443 2.60e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 49.22  E-value: 2.60e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571  351 FMDDV----GQTLLNWASAFGTQEMVEFLCERGAD--VNRGQRSSSLHYAACFGRPQVAKTLLRHGANPDLRDEDGKTPL 424
Cdd:PHA02875    93 FADDVfykdGMTPLHLATILKKLDIMKLLIARGADpdIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPL 172

                           90
                   ....*....|....*....
gi 1622951571  425 DKARERGHSEVVAILQSPG 443
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.
 1087-1176 3.92e-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: 3.92e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571 1087 CHSNDDKNAWFAIDLGlwvipSAYTLRHARGYGRSALRN-----WVFQVSKDGQNWTSLYTHVDDcSLNEPGSTATWPLD 1161
Cdd:pfam00754   27 SAWSGDDPQWIQVDLG-----KPKKITGVVTQGRQDGSNgyvtsYKIEYSLDGENWTTVKDEKIP-GNNDNNTPVTNTFD 100

                           90
                   ....*....|....*
gi 1622951571 1162 PPKDEkqgwRHVRIK 1176
Cdd:pfam00754  101 PPIKA----RYVRIV 111
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 370-424 1.00e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 45.97  E-value: 1.00e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622951571  370 EMVEFLCERGADVN---RGQRSSSLHYAACFGR---PQVAKTLLRHGANPDLRDEDGKTPL 424
Cdd:PHA02859    67 EILKFLIENGADVNfktRDNNLSALHHYLSFNKnvePEILKILIDSGSSITEEDEDGKNLL 127
PHA03095 PHA03095
ankyrin-like protein; Provisional
 368-425 1.92e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.56  E-value: 1.92e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622951571  368 TQEMVEFLCERGADVNR--GQRSSSLH-YAACFG-RPQVAKTLLRHGANPDLRDEDGKTPLD 425
Cdd:PHA03095    96 TLDVIKLLIKAGADVNAkdKVGRTPLHvYLSGFNiNPKVIRLLLRKGADVNALDLYGMTPLA 157
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 370-439 6.35e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 44.87  E-value: 6.35e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622951571  370 EMVEFLCERGADVNRGQR---SSSLHYAACFGRPQVAKTLLRHGANPDLRDEDGKTPLDKARERGHSEVVAIL 439
Cdd:PHA02878   148 EITKLLLSYGADINMKDRhkgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHIL 220
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 391-418 1.11e-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: 1.11e-03
                           10        20
                   ....*....|....*....|....*....
gi 1622951571  391 LHYAAC-FGRPQVAKTLLRHGANPDLRDE 418
Cdd:pfam00023    6 LHLAAGrRGNLEIVKLLLSKGADVNARDK 34
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 356-424 1.50e-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: 1.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571  356 GQTLLNWASAFGTQEMVEFLCERGADVN---------RGQRSSSLHY-------AACFGRPQVAKTLLRHGANPDLRDED 419
Cdd:cd22192     89 GETALHIAVVNQNLNLVRELIARGADVVspratgtffRPGPKNLIYYgehplsfAACVGNEEIVRLLIEHGADIRAQDSL 168


                   ....*
gi 1622951571  420 GKTPL 424
Cdd:cd22192    169 GNTVL 173
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 330-427 1.70e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 43.41  E-value: 1.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571  330 IRSKDTDALIDAIDTGAfEVNFMDDVGQTLLNWASAFGTQEMVEFLCERGA--DVNRGQRSSSLHYAACFGRPQVAKTLL 407
Cdd:PHA02874   132 IKKGDLESIKMLFEYGA-DVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAyaNVKDNNGESPLHNAAEYGDYACIKLLI 210

                           90       100
                   ....*....|....*....|
gi 1622951571  408 RHGANPDLRDEDGKTPLDKA 427
Cdd:PHA02874   211 DHGNHIMNKCKNGFTPLHNA 230
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 369-446 2.84e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 42.64  E-value: 2.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571  369 QEMVEFLCERGADVNRGQRSSS--LHYAACFGRPQVAKTLLRHGANPDLRDEDGKTPLDKARERGHSEVVAILQSPGDWM 446
Cdd:PHA02874   104 KDMIKTILDCGIDVNIKDAELKtfLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYA 183
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 1087-1198 3.27e-03

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


Pssm-ID: 238014 [Multi-domain]  Cd Length: 143  Bit Score: 40.41  E-value: 3.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571 1087 CHSNDDKNAWFAIDLGL--WVIPSAYTLRHaRGYGRSALRNWVFQVSKDGQNWTSLYTHVDDCSLN---EPGSTATWPLD 1161
Cdd:cd00057     38 TPAVNDPPQWLQVDLGKtrRVTGIQTQGRK-GGGSSEWVTSYKVQYSLDGETWTTYKDKGEEKVFTgnsDGSTPVTNDFP 116

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1622951571 1162 PPKDEkqgwRHVRIKQMGKNasgqtHYLSLsGFELYG 1198
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 ...
 391-415 6.39e-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: 6.39e-03
                            10        20
                    ....*....|....*....|....*
gi 1622951571   391 LHYAACFGRPQVAKTLLRHGANPDL 415
Cdd:smart00248    6 LHLAAENGNLEVVKLLLDKGADINA 30
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 363-447 9.31e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.39  E-value: 9.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622951571  363 ASAFGTQEMVEFLCERG--ADVNRGQRSSSLHYAACFGRPQVAKTLLRHGANPDLRDEDGKTPLDKARERGHSEVVAIL- 439
Cdd:PLN03192   532 VASTGNAALLEELLKAKldPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILy 611

                           90
                   ....*....|....*.
gi 1622951571  440 --------QSPGDWMC 447
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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