|
Name |
Accession |
Description |
Interval |
E-value |
| HECTc |
cd00078 |
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ... |
2129-2606 |
2.48e-119 |
|
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It binds specific ubiquitin-conjugating enzymes (E2), accepts ubiquitin from E2, transfers ubiquitin to substrate lysine side chains, and transfers additional ubiquitin molecules to the end of growing ubiquitin chains.
Pssm-ID: 238033 [Multi-domain] Cd Length: 352 Bit Score: 381.91 E-value: 2.48e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355943 2129 ERVKVPRGESLMEWAENVMQIH-ADRKSVLEVEFLGEEGTG-LGPTLEFYALVAAEFQRTDLGTWLCDDNFpddesrhvd 2206
Cdd:cd00078 1 LKITVRRDRILEDALRQLSKVSsSDLKKVLEVEFVGEEGIDaGGVTREFFTLVSKELFNPSYGLFRYTPDD--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355943 2207 lggglkppgyyvqRSCGLFTAPFPQDSDELeritKLFHFLGIFLAKCIQDNRLVDLPISKPFFKLMCmgdiksnmskliy 2286
Cdd:cd00078 72 -------------SGLLYPNPSSFADEDHL----KLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLL------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355943 2287 esrgdrdlhctesqseasteeghdslsvgsfeedsksefildppkpkppawfNGILTWEDFELVNPHRARFLKEIKDLAI 2366
Cdd:cd00078 122 ----------------------------------------------------GKPLSLEDLEELDPELYKSLKELLDNDG 149
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355943 2367 krrqilgnkslsedekntklqelvlknpsgsgpplSIEDLGLNFQFCPSSRIYGFTAVDLKPSGEDEMITMDNAEEYVDL 2446
Cdd:cd00078 150 -----------------------------------DEDDLELTFTIELDSSFGGAVTVELKPGGRDIPVTNENKEEYVDL 194
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355943 2447 MFDFCMHTGIQKQMEAFRDGFNKVFPMEKLSSFSHEEVQMILCGNqsPSWAAEDIINYTEPKLGYTRDSPGFLRFVRVLC 2526
Cdd:cd00078 195 YVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGS--EDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLE 272
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355943 2527 GMSSDERKAFLQFTTGCSTLPPGGLANLHPRLTvVRKVDATDASYPSVNTCVHYLKLPEYSSEEIMRERLLAATMEK-GF 2605
Cdd:cd00078 273 SFTNEERKKFLQFVTGSSRLPVGGFADLNPKFT-IRRVGSPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGaGF 351
|
.
gi 564355943 2606 H 2606
Cdd:cd00078 352 G 352
|
|
| HECTc |
smart00119 |
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ... |
2153-2605 |
2.36e-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: 2.36e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355943 2153 RKSVLEVEFLGEEG-TGLGPTLEFYALVAAEFQRTDLGTWLCDDNfpddesrhvdlggglkppgyyvqrSCGLFTAPFPQ 2231
Cdd:smart00119 3 KKRVLEIEFEGEEGlDGGGVTREFFFLLSKELFNPDYGLFRYSPN------------------------DYLLYPNPRSG 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355943 2232 DSDElERItKLFHFLGIFLAKCIQDNRLVDLPISKPFFKLMCmgdiksnmskliyesrgdrdlhctesqseasteeghds 2311
Cdd:smart00119 59 FANE-EHL-SYFRFIGRVLGKALYDNRLLDLFFARPFYKKLL-------------------------------------- 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355943 2312 lsvgsfeedsksefildppkpkppawfNGILTWEDFELVNPHRARFLKEIKdlaikrrqilgnksLSEDEkntklqelvl 2391
Cdd:smart00119 99 ---------------------------GKPVTLHDLESLDPELYKSLKWLL--------------LNNDT---------- 127
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355943 2392 knpsgsgpplsIEDLGLNFQFCPSSRIYGFTAVDLKPSGEDEMITMDNAEEYVDLMFDFCMHTGIQKQMEAFRDGFNKVF 2471
Cdd:smart00119 128 -----------SEELDLTFSIVLTSEFGQVKVVELKPGGSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVI 196
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355943 2472 PMEKLSSFSHEEVQMILCGnqSPSWAAEDIINYTEPKLGYTRDSPGFLRFVRVLCGMSSDERKAFLQFTTGCSTLPPGGL 2551
Cdd:smart00119 197 PENLLKLFDPEELELLICG--SPEIDVDDLKSNTEYKGGYSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGF 274
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 564355943 2552 ANLHPRLTvVRKVDATDASYPSVNTCVHYLKLPEYSSEEIMRERLLAATME-KGF 2605
Cdd:smart00119 275 AALSPKFT-IRKAGSDDERLPTAHTCFNRLKLPPYSSKEILREKLLLAINEgKGF 328
|
|
| HECT |
pfam00632 |
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ... |
2178-2607 |
6.19e-73 |
|
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl Terminus.
Pssm-ID: 459880 Cd Length: 304 Bit Score: 246.75 E-value: 6.19e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355943 2178 LVAAEFQRTDLGTWLCDDNfpddesrhvdlggglkppgyyvqRSCGLFTAPFPQDSDELERItKLFHFLGIFLAKCIQDN 2257
Cdd:pfam00632 2 LLSKELFDPNYGLFEYETE-----------------------DDRTYWFNPSSSESPDLELL-DYFKFLGKLLGKAIYNG 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355943 2258 RLVDLPISKPFFKLMCmgdiksnmskliyesrgdrdlhctesqseasteeghdslsvgsfeedsksefildppkpkppaw 2337
Cdd:pfam00632 58 ILLDLPFPPFFYKKLL---------------------------------------------------------------- 73
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355943 2338 fNGILTWEDFELVNPHRARFLKEIKdlaikrrqilgnkSLSEDEKntklqelvlknpsgsgpplsiEDLGLNFQFCpssr 2417
Cdd:pfam00632 74 -GEPLTLEDLESIDPELYKSLKSLL-------------NMDNDDD---------------------EDLGLTFTIP---- 114
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355943 2418 IYGFTA-VDLKPSGEDEMITMDNAEEYVDLMFDFCMHTGIQKQMEAFRDGFNKVFPMEKLSSFSHEEVQMILCGnqSPSW 2496
Cdd:pfam00632 115 VFGESKtIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQLEAFRKGFYSVIPKEALSLFTPEELELLICG--SPEI 192
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355943 2497 AAEDIINYTEPKLGYTRDSPGFLRFVRVLCGMSSDERKAFLQFTTGCSTLPPGGLANLhPRLTVVRKVDATDASYPSVNT 2576
Cdd:pfam00632 193 DVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGSSRLPVGGFKSL-PKFTIVRKGGDDDDRLPTAHT 271
|
410 420 430
....*....|....*....|....*....|..
gi 564355943 2577 CVHYLKLPEYSSEEIMRERLLAATME-KGFHL 2607
Cdd:pfam00632 272 CFNRLKLPDYSSKEILKEKLLIAIEEgEGFGL 303
|
|
| HUL4 |
COG5021 |
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones]; |
2046-2605 |
7.59e-55 |
|
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227354 [Multi-domain] Cd Length: 872 Bit Score: 208.85 E-value: 7.59e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355943 2046 QIEEPLALASGALPDWCEQLTskcPFLIPFETRQLYFTCTAFgasraivWLQNRREATVERTRTTSSVRRDDPGEFRVGR 2125
Cdd:COG5021 425 ESDESFYVASNVQQQRASREG---PLLSGWKTRLNNLYRFYF-------VEHRKKTLTKNDSRLGSFISLNKLDIRRIKE 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355943 2126 LKHERVKVprgeSLMEWAENVM---QIHADRKSVLEV---EFLGEEGTGLGPTLEFYALVAAEFQRTDLGTW----LCDD 2195
Cdd:COG5021 495 DKRRKLFY----SLKQKAKIFDpylHIKVRRDRVFEDsyrEIMDESGDDLKKTLEIEFVGEEGIDAGGLTREwlflLSKE 570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355943 2196 NFPDDesrhvdlggglkpPGYYVQRSCGLFTAPFPQDSDELERITKLFHFLGIFLAKCIQDNRLVDLPISKPFFKLMCmg 2275
Cdd:COG5021 571 MFNPD-------------YGLFEYITEDLYTLPINPLSSINPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLL-- 635
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355943 2276 diksnmskliyesrgdrdlhctesqseasteeghdslsvgsfeedsksefildppkPKPpawfngiLTWEDFELVNPHRA 2355
Cdd:COG5021 636 --------------------------------------------------------GKP-------VSLVDLESLDPELY 652
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355943 2356 RFLKEIKDLaikrrqilgnkslSEDEKNtklqelvlknpsgsgpplsiedLGLNFQFcpSSRIYGFTA-VDLKPSGEDEM 2434
Cdd:COG5021 653 RSLVWLLNN-------------DIDETI----------------------LDLTFTV--EDDSFGESRtVELIPNGRNIS 695
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355943 2435 ITMDNAEEYVDLMFDFCMHTGIQKQMEAFRDGFNKVFPMEKLSSFSHEEVQMILCGNQSPSwAAEDIINYTEPKlGYTRD 2514
Cdd:COG5021 696 VTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEDI-DIDDWKSNTAYH-GYTED 773
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355943 2515 SPGFLRFVRVLCGMSSDERKAFLQFTTGCSTLPPGGLANLHPRLTVVRKV--DATDASY--PSVNTCVHYLKLPEYSSEE 2590
Cdd:COG5021 774 SPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTieKGGTDDDrlPSAHTCFNRLKLPEYSSKE 853
|
570
....*....|....*.
gi 564355943 2591 IMRERLLAATME-KGF 2605
Cdd:COG5021 854 KLRSKLLTAINEgAGF 869
|
|
| BTHB_HectD1 |
cd21062 |
basic tilted helix bundle (BTHB) domain found in HECT domain-containing protein 1 (HectD1) and ... |
1891-1956 |
1.17e-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: 136.26 E-value: 1.17e-37
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564355943 1891 CWSIEHVEQYLGTDELPKNDLITYLQKNADAAFLRHWKLTGTNKSIRKNRNCSQLIAAYKDFCEHG 1956
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 |
2.60e-31 |
|
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: 120.47 E-value: 2.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355943 1107 RNLPYGRLEDILSRDNSALNCHSNDDKNAWFAIDLGVWVIPSAYTLRHARGYGR-SALRNWVFQVSKDGQNWTslYTHVD 1185
Cdd:pfam07738 1 LNYEAKPPKVILQPDYMPGPCWSFKGSRGFVVIELSEFIIVEAITLEHVEKSVFsSAPKDFEVSGSDRYPTTK--WVLLG 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 564355943 1186 DCSLNEPGSTA-TWPLDPAKDEkqGWRHVRL--KQMGknasGQTHYLSLSGFELYGTV 1240
Cdd:pfam07738 79 EFSYDLDGKTIqTFQLENPPDI--WVKYVKLriLSNY----GNEHYTCLYRFRVHGTV 130
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
366-479 |
8.46e-26 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 110.04 E-value: 8.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355943 366 LIDCIRSKDTDALIDAIDTGAfEVNFMDDVGQTLLNWASAFGTQEMVEFLCERGADVNR--GQRSSSLHYAACFGRPQVA 443
Cdd:COG0666 91 LHAAARNGDLEIVKLLLEAGA-DVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAqdNDGNTPLHLAAANGNLEIV 169
|
90 100 110
....*....|....*....|....*....|....*.
gi 564355943 444 KTLLRHGANPDLRDEDGKTPLDKARERGHSEVVAIL 479
Cdd:COG0666 170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
|
|
| MIB_HERC2 |
pfam06701 |
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain ... |
1277-1335 |
1.26e-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: 1.26e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564355943 1277 GARVIRGLDWKWRDQDGSPQGEGTVT------GELHNGWIDVTWDAGGSNSYRMGAEGKFDLKLA 1335
Cdd:pfam06701 1 GARVVRGPDWKWGDQDGGEGHVGTVVeirdwdSESPRSTVRVQWDNGSTNVYRVGYEGKYDLKVV 65
|
|
| BTHB |
pfam18410 |
Basic tilted helix bundle domain; This domain is found on the N-terminal region of FKBPs such ... |
1892-1957 |
4.31e-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: 4.31e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564355943 1892 WSIEhveqYLGTDELPKNDLITYLQKNADAAFLRHWKLTGTNKSIRKNRNCSQLIAAYKDFCEHGT 1957
Cdd:pfam18410 5 WTEE----QLLSDALPKKDIIKFLQDNASLSFLKEHKLNGALKNVAKTAKKDQLAEAYNKLFESKR 66
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
366-457 |
1.48e-12 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 65.52 E-value: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355943 366 LIDCIRSKDTDALIDAIDTGAfEVNFMDDVGQTLLNWASAFGTQEMVEFLCERGADVNRGQRSSSLHYAACFGRPQVAKT 445
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGA-DANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRTALHYAARSGHLEIVKL 79
|
90
....*....|..
gi 564355943 446 LLRHGANPDLRD 457
Cdd:pfam12796 80 LLEKGADINVKD 91
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
404-481 |
1.10e-07 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 57.60 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355943 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 |
1.53e-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: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355943 396 GQTLLNWASAFGTQEMVEFLCERGADVN---------RGQRSSSLHY-------AACFGRPQVAKTLLRHGANPDLRDED 459
Cdd:cd22192 89 GETALHIAVVNQNLNLVRELIARGADVVspratgtffRPGPKNLIYYgehplsfAACVGNEEIVRLLIEHGADIRAQDSL 168
|
....*
gi 564355943 460 GKTPL 464
Cdd:cd22192 169 GNTVL 173
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
431-455 |
6.49e-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: 6.49e-03
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| HECTc |
cd00078 |
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ... |
2129-2606 |
2.48e-119 |
|
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It binds specific ubiquitin-conjugating enzymes (E2), accepts ubiquitin from E2, transfers ubiquitin to substrate lysine side chains, and transfers additional ubiquitin molecules to the end of growing ubiquitin chains.
Pssm-ID: 238033 [Multi-domain] Cd Length: 352 Bit Score: 381.91 E-value: 2.48e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355943 2129 ERVKVPRGESLMEWAENVMQIH-ADRKSVLEVEFLGEEGTG-LGPTLEFYALVAAEFQRTDLGTWLCDDNFpddesrhvd 2206
Cdd:cd00078 1 LKITVRRDRILEDALRQLSKVSsSDLKKVLEVEFVGEEGIDaGGVTREFFTLVSKELFNPSYGLFRYTPDD--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355943 2207 lggglkppgyyvqRSCGLFTAPFPQDSDELeritKLFHFLGIFLAKCIQDNRLVDLPISKPFFKLMCmgdiksnmskliy 2286
Cdd:cd00078 72 -------------SGLLYPNPSSFADEDHL----KLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLL------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355943 2287 esrgdrdlhctesqseasteeghdslsvgsfeedsksefildppkpkppawfNGILTWEDFELVNPHRARFLKEIKDLAI 2366
Cdd:cd00078 122 ----------------------------------------------------GKPLSLEDLEELDPELYKSLKELLDNDG 149
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355943 2367 krrqilgnkslsedekntklqelvlknpsgsgpplSIEDLGLNFQFCPSSRIYGFTAVDLKPSGEDEMITMDNAEEYVDL 2446
Cdd:cd00078 150 -----------------------------------DEDDLELTFTIELDSSFGGAVTVELKPGGRDIPVTNENKEEYVDL 194
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355943 2447 MFDFCMHTGIQKQMEAFRDGFNKVFPMEKLSSFSHEEVQMILCGNqsPSWAAEDIINYTEPKLGYTRDSPGFLRFVRVLC 2526
Cdd:cd00078 195 YVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGS--EDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLE 272
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355943 2527 GMSSDERKAFLQFTTGCSTLPPGGLANLHPRLTvVRKVDATDASYPSVNTCVHYLKLPEYSSEEIMRERLLAATMEK-GF 2605
Cdd:cd00078 273 SFTNEERKKFLQFVTGSSRLPVGGFADLNPKFT-IRRVGSPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGaGF 351
|
.
gi 564355943 2606 H 2606
Cdd:cd00078 352 G 352
|
|
| HECTc |
smart00119 |
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ... |
2153-2605 |
2.36e-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: 2.36e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355943 2153 RKSVLEVEFLGEEG-TGLGPTLEFYALVAAEFQRTDLGTWLCDDNfpddesrhvdlggglkppgyyvqrSCGLFTAPFPQ 2231
Cdd:smart00119 3 KKRVLEIEFEGEEGlDGGGVTREFFFLLSKELFNPDYGLFRYSPN------------------------DYLLYPNPRSG 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355943 2232 DSDElERItKLFHFLGIFLAKCIQDNRLVDLPISKPFFKLMCmgdiksnmskliyesrgdrdlhctesqseasteeghds 2311
Cdd:smart00119 59 FANE-EHL-SYFRFIGRVLGKALYDNRLLDLFFARPFYKKLL-------------------------------------- 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355943 2312 lsvgsfeedsksefildppkpkppawfNGILTWEDFELVNPHRARFLKEIKdlaikrrqilgnksLSEDEkntklqelvl 2391
Cdd:smart00119 99 ---------------------------GKPVTLHDLESLDPELYKSLKWLL--------------LNNDT---------- 127
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355943 2392 knpsgsgpplsIEDLGLNFQFCPSSRIYGFTAVDLKPSGEDEMITMDNAEEYVDLMFDFCMHTGIQKQMEAFRDGFNKVF 2471
Cdd:smart00119 128 -----------SEELDLTFSIVLTSEFGQVKVVELKPGGSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVI 196
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355943 2472 PMEKLSSFSHEEVQMILCGnqSPSWAAEDIINYTEPKLGYTRDSPGFLRFVRVLCGMSSDERKAFLQFTTGCSTLPPGGL 2551
Cdd:smart00119 197 PENLLKLFDPEELELLICG--SPEIDVDDLKSNTEYKGGYSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGF 274
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 564355943 2552 ANLHPRLTvVRKVDATDASYPSVNTCVHYLKLPEYSSEEIMRERLLAATME-KGF 2605
Cdd:smart00119 275 AALSPKFT-IRKAGSDDERLPTAHTCFNRLKLPPYSSKEILREKLLLAINEgKGF 328
|
|
| HECT |
pfam00632 |
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ... |
2178-2607 |
6.19e-73 |
|
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl Terminus.
Pssm-ID: 459880 Cd Length: 304 Bit Score: 246.75 E-value: 6.19e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355943 2178 LVAAEFQRTDLGTWLCDDNfpddesrhvdlggglkppgyyvqRSCGLFTAPFPQDSDELERItKLFHFLGIFLAKCIQDN 2257
Cdd:pfam00632 2 LLSKELFDPNYGLFEYETE-----------------------DDRTYWFNPSSSESPDLELL-DYFKFLGKLLGKAIYNG 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355943 2258 RLVDLPISKPFFKLMCmgdiksnmskliyesrgdrdlhctesqseasteeghdslsvgsfeedsksefildppkpkppaw 2337
Cdd:pfam00632 58 ILLDLPFPPFFYKKLL---------------------------------------------------------------- 73
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355943 2338 fNGILTWEDFELVNPHRARFLKEIKdlaikrrqilgnkSLSEDEKntklqelvlknpsgsgpplsiEDLGLNFQFCpssr 2417
Cdd:pfam00632 74 -GEPLTLEDLESIDPELYKSLKSLL-------------NMDNDDD---------------------EDLGLTFTIP---- 114
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355943 2418 IYGFTA-VDLKPSGEDEMITMDNAEEYVDLMFDFCMHTGIQKQMEAFRDGFNKVFPMEKLSSFSHEEVQMILCGnqSPSW 2496
Cdd:pfam00632 115 VFGESKtIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQLEAFRKGFYSVIPKEALSLFTPEELELLICG--SPEI 192
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355943 2497 AAEDIINYTEPKLGYTRDSPGFLRFVRVLCGMSSDERKAFLQFTTGCSTLPPGGLANLhPRLTVVRKVDATDASYPSVNT 2576
Cdd:pfam00632 193 DVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGSSRLPVGGFKSL-PKFTIVRKGGDDDDRLPTAHT 271
|
410 420 430
....*....|....*....|....*....|..
gi 564355943 2577 CVHYLKLPEYSSEEIMRERLLAATME-KGFHL 2607
Cdd:pfam00632 272 CFNRLKLPDYSSKEILKEKLLIAIEEgEGFGL 303
|
|
| HUL4 |
COG5021 |
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones]; |
2046-2605 |
7.59e-55 |
|
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227354 [Multi-domain] Cd Length: 872 Bit Score: 208.85 E-value: 7.59e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355943 2046 QIEEPLALASGALPDWCEQLTskcPFLIPFETRQLYFTCTAFgasraivWLQNRREATVERTRTTSSVRRDDPGEFRVGR 2125
Cdd:COG5021 425 ESDESFYVASNVQQQRASREG---PLLSGWKTRLNNLYRFYF-------VEHRKKTLTKNDSRLGSFISLNKLDIRRIKE 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355943 2126 LKHERVKVprgeSLMEWAENVM---QIHADRKSVLEV---EFLGEEGTGLGPTLEFYALVAAEFQRTDLGTW----LCDD 2195
Cdd:COG5021 495 DKRRKLFY----SLKQKAKIFDpylHIKVRRDRVFEDsyrEIMDESGDDLKKTLEIEFVGEEGIDAGGLTREwlflLSKE 570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355943 2196 NFPDDesrhvdlggglkpPGYYVQRSCGLFTAPFPQDSDELERITKLFHFLGIFLAKCIQDNRLVDLPISKPFFKLMCmg 2275
Cdd:COG5021 571 MFNPD-------------YGLFEYITEDLYTLPINPLSSINPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLL-- 635
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355943 2276 diksnmskliyesrgdrdlhctesqseasteeghdslsvgsfeedsksefildppkPKPpawfngiLTWEDFELVNPHRA 2355
Cdd:COG5021 636 --------------------------------------------------------GKP-------VSLVDLESLDPELY 652
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355943 2356 RFLKEIKDLaikrrqilgnkslSEDEKNtklqelvlknpsgsgpplsiedLGLNFQFcpSSRIYGFTA-VDLKPSGEDEM 2434
Cdd:COG5021 653 RSLVWLLNN-------------DIDETI----------------------LDLTFTV--EDDSFGESRtVELIPNGRNIS 695
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355943 2435 ITMDNAEEYVDLMFDFCMHTGIQKQMEAFRDGFNKVFPMEKLSSFSHEEVQMILCGNQSPSwAAEDIINYTEPKlGYTRD 2514
Cdd:COG5021 696 VTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEDI-DIDDWKSNTAYH-GYTED 773
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355943 2515 SPGFLRFVRVLCGMSSDERKAFLQFTTGCSTLPPGGLANLHPRLTVVRKV--DATDASY--PSVNTCVHYLKLPEYSSEE 2590
Cdd:COG5021 774 SPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTieKGGTDDDrlPSAHTCFNRLKLPEYSSKE 853
|
570
....*....|....*.
gi 564355943 2591 IMRERLLAATME-KGF 2605
Cdd:COG5021 854 KLRSKLLTAINEgAGF 869
|
|
| BTHB_HectD1 |
cd21062 |
basic tilted helix bundle (BTHB) domain found in HECT domain-containing protein 1 (HectD1) and ... |
1891-1956 |
1.17e-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: 136.26 E-value: 1.17e-37
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564355943 1891 CWSIEHVEQYLGTDELPKNDLITYLQKNADAAFLRHWKLTGTNKSIRKNRNCSQLIAAYKDFCEHG 1956
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 |
2.60e-31 |
|
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: 120.47 E-value: 2.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355943 1107 RNLPYGRLEDILSRDNSALNCHSNDDKNAWFAIDLGVWVIPSAYTLRHARGYGR-SALRNWVFQVSKDGQNWTslYTHVD 1185
Cdd:pfam07738 1 LNYEAKPPKVILQPDYMPGPCWSFKGSRGFVVIELSEFIIVEAITLEHVEKSVFsSAPKDFEVSGSDRYPTTK--WVLLG 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 564355943 1186 DCSLNEPGSTA-TWPLDPAKDEkqGWRHVRL--KQMGknasGQTHYLSLSGFELYGTV 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 ... |
1891-1954 |
4.29e-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: 4.29e-31
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564355943 1891 CWSIEHVEQYLGTDELPKNDLITYLQKNADAAFLRHWKLTGTNKSIRKNRNCSQLIAAYKDFCE 1954
Cdd:cd21035 1 VWTKQFDEAYTASDNLPKKDVVDFLQKYADNSFLREHKLNGSAKSVLKNRNKDQLVEAYNKVFE 64
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
366-479 |
8.46e-26 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 110.04 E-value: 8.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355943 366 LIDCIRSKDTDALIDAIDTGAfEVNFMDDVGQTLLNWASAFGTQEMVEFLCERGADVNR--GQRSSSLHYAACFGRPQVA 443
Cdd:COG0666 91 LHAAARNGDLEIVKLLLEAGA-DVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAqdNDGNTPLHLAAANGNLEIV 169
|
90 100 110
....*....|....*....|....*....|....*.
gi 564355943 444 KTLLRHGANPDLRDEDGKTPLDKARERGHSEVVAIL 479
Cdd:COG0666 170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
|
|
| MIB_HERC2 |
pfam06701 |
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain ... |
1277-1335 |
1.26e-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: 1.26e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564355943 1277 GARVIRGLDWKWRDQDGSPQGEGTVT------GELHNGWIDVTWDAGGSNSYRMGAEGKFDLKLA 1335
Cdd:pfam06701 1 GARVVRGPDWKWGDQDGGEGHVGTVVeirdwdSESPRSTVRVQWDNGSTNVYRVGYEGKYDLKVV 65
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
366-480 |
8.51e-24 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 104.27 E-value: 8.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355943 366 LIDCIRSKDTDA---LIDAidtGAfEVNFMDDVGQTLLNWASAFGTQEMVEFLCERGADVNRGQRS--SSLHYAACFGRP 440
Cdd:COG0666 124 LHLAAYNGNLEIvklLLEA---GA-DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDgeTPLHLAAENGHL 199
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 564355943 441 QVAKTLLRHGANPDLRDEDGKTPLDKARERGHSEVVAILQ 480
Cdd:COG0666 200 EIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
366-479 |
3.79e-20 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 93.48 E-value: 3.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355943 366 LIDCIRSKDTDALIDAIDTGAFEVNFMDDVGQTLLNWASAFGTQEMVEFLCERGADVNR--GQRSSSLHYAACFGRPQVA 443
Cdd:COG0666 57 LLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNArdKDGETPLHLAAYNGNLEIV 136
|
90 100 110
....*....|....*....|....*....|....*.
gi 564355943 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 ... |
1892-1957 |
4.31e-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: 4.31e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564355943 1892 WSIEhveqYLGTDELPKNDLITYLQKNADAAFLRHWKLTGTNKSIRKNRNCSQLIAAYKDFCEHGT 1957
Cdd:pfam18410 5 WTEE----QLLSDALPKKDIIKFLQDNASLSFLKEHKLNGALKNVAKTAKKDQLAEAYNKLFESKR 66
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
366-457 |
1.48e-12 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 65.52 E-value: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355943 366 LIDCIRSKDTDALIDAIDTGAfEVNFMDDVGQTLLNWASAFGTQEMVEFLCERGADVNRGQRSSSLHYAACFGRPQVAKT 445
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGA-DANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRTALHYAARSGHLEIVKL 79
|
90
....*....|..
gi 564355943 446 LLRHGANPDLRD 457
Cdd:pfam12796 80 LLEKGADINVKD 91
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
370-479 |
3.43e-12 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 69.60 E-value: 3.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355943 370 IRSKDTDALIDAIDTGAFEVNFMDDVGQTLLNWASAFGTQEMVEFLCERGADVNRG--QRSSSLHYAACFGRPQVAKTLL 447
Cdd:COG0666 28 AALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKddGGNTLLHAAARNGDLEIVKLLL 107
|
90 100 110
....*....|....*....|....*....|..
gi 564355943 448 RHGANPDLRDEDGKTPLDKARERGHSEVVAIL 479
Cdd:COG0666 108 EAGADVNARDKDGETPLHLAAYNGNLEIVKLL 139
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
400-483 |
1.59e-10 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 59.74 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355943 400 LNWASAFGTQEMVEFLCERGADVN--RGQRSSSLHYAACFGRPQVAKTLLRHgANPDLRDeDGKTPLDKARERGHSEVVA 477
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANlqDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
|
....*.
gi 564355943 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 ... |
1897-1951 |
6.06e-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: 6.06e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 564355943 1897 VEQyLGTDELPKNDLITYLQKNADAAFLRHWKLTGTNKSIRKNRNCSQLIAAYKD 1951
Cdd:cd21063 6 EEQ-LASDAVSKKDLIEFLQENASNSFLAEHKLLGKLKNVAKTAKKDQLVEAYNQ 59
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
427-479 |
9.85e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 50.74 E-value: 9.85e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 564355943 427 RSSSLHYAACFGRPQVAKTLLRHGANPDLRDEDGKTPLDKARERGHSEVVAIL 479
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
404-481 |
1.10e-07 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 57.60 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355943 404 SAFGTQEMVEFLCERGADVNRG--QRSSSLHYAACFGRPQVAKTLLRHGANPDLRDEDGKTPLDKARERGHSEVVAILQS 481
Cdd:PTZ00322 90 AASGDAVGARILLTGGADPNCRdyDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
370-464 |
1.35e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 53.73 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355943 370 IRSKDTDALIDA------IDTGAfEVNFMD-DVGQTLLNWASAFGTQEMVEFLCERGADVNRGQR--SSSLHYAACFGRP 440
Cdd:PHA02878 136 IDKKSKDDIIEAeitkllLSYGA-DINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKtnNSPLHHAVKHYNK 214
|
90 100
....*....|....*....|....
gi 564355943 441 QVAKTLLRHGANPDLRDEDGKTPL 464
Cdd:PHA02878 215 PIVHILLENGASTDARDKCGNTPL 238
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
393-477 |
3.20e-06 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 52.33 E-value: 3.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355943 393 DDVGQTLLNWASAFGTQE--MVEFLCERGADVN----RGQrsSSLHYAACFGRPQVAKTLLRHGANPDLRDEDGKTPLDK 466
Cdd:PHA03095 219 DMLGNTPLHSMATGSSCKrsLVLPLLIAGISINarnrYGQ--TPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSL 296
|
90
....*....|.
gi 564355943 467 ARERGHSEVVA 477
Cdd:PHA03095 297 MVRNNNGRAVR 307
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
418-467 |
6.96e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 45.42 E-value: 6.96e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 564355943 418 RGADVNR--GQRSSSLHYAACFGRPQVAKTLLRHGANPDLRDEDGKTPLDKA 467
Cdd:pfam13857 5 GPIDLNRldGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
410-484 |
1.54e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 50.05 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355943 410 EMVEFLCERGADVN--------------------RGqrSSSLHYAACFGRPQVAKTLLRHGANPDLRDEDGKTPLDKARE 469
Cdd:PHA03100 157 KILKLLIDKGVDINaknrvnyllsygvpinikdvYG--FTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAIL 234
|
90
....*....|....*
gi 564355943 470 RGHSEVVAILQSPGD 484
Cdd:PHA03100 235 NNNKEIFKLLLNNGP 249
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
391-483 |
2.64e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 49.22 E-value: 2.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355943 391 FMDDV----GQTLLNWASAFGTQEMVEFLCERGAD--VNRGQRSSSLHYAACFGRPQVAKTLLRHGANPDLRDEDGKTPL 464
Cdd:PHA02875 93 FADDVfykdGMTPLHLATILKKLDIMKLLIARGADpdIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPL 172
|
90
....*....|....*....
gi 564355943 465 DKARERGHSEVVAILQSPG 483
Cdd:PHA02875 173 IIAMAKGDIAICKMLLDSG 191
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
410-464 |
1.02e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 45.97 E-value: 1.02e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564355943 410 EMVEFLCERGADVN---RGQRSSSLHYAACFGR---PQVAKTLLRHGANPDLRDEDGKTPL 464
Cdd:PHA02859 67 EILKFLIENGADVNfktRDNNLSALHHYLSFNKnvePEILKILIDSGSSITEEDEDGKNLL 127
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
408-465 |
1.95e-04 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 46.56 E-value: 1.95e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564355943 408 TQEMVEFLCERGADVNR--GQRSSSLH-YAACFG-RPQVAKTLLRHGANPDLRDEDGKTPLD 465
Cdd:PHA03095 96 TLDVIKLLIKAGADVNAkdKVGRTPLHvYLSGFNiNPKVIRLLLRKGADVNALDLYGMTPLA 157
|
|
| F5_F8_type_C |
pfam00754 |
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family. |
1127-1216 |
3.84e-04 |
|
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.
Pssm-ID: 459925 [Multi-domain] Cd Length: 127 Bit Score: 42.43 E-value: 3.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355943 1127 CHSNDDKNAWFAIDLGvwvipSAYTLRHARGYGRSALRN-----WVFQVSKDGQNWTSLYTHVDDcSLNEPGSTATWPLD 1201
Cdd:pfam00754 27 SAWSGDDPQWIQVDLG-----KPKKITGVVTQGRQDGSNgyvtsYKIEYSLDGENWTTVKDEKIP-GNNDNNTPVTNTFD 100
|
90
....*....|....*
gi 564355943 1202 PAKDEkqgwRHVRLK 1216
Cdd:pfam00754 101 PPIKA----RYVRIV 111
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
410-479 |
6.45e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 44.87 E-value: 6.45e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564355943 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 |
1.12e-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: 1.12e-03
10 20
....*....|....*....|....*....
gi 564355943 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 |
1.53e-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: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355943 396 GQTLLNWASAFGTQEMVEFLCERGADVN---------RGQRSSSLHY-------AACFGRPQVAKTLLRHGANPDLRDED 459
Cdd:cd22192 89 GETALHIAVVNQNLNLVRELIARGADVVspratgtffRPGPKNLIYYgehplsfAACVGNEEIVRLLIEHGADIRAQDSL 168
|
....*
gi 564355943 460 GKTPL 464
Cdd:cd22192 169 GNTVL 173
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
370-467 |
1.72e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 43.41 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355943 370 IRSKDTDALIDAIDTGAfEVNFMDDVGQTLLNWASAFGTQEMVEFLCERGA--DVNRGQRSSSLHYAACFGRPQVAKTLL 447
Cdd:PHA02874 132 IKKGDLESIKMLFEYGA-DVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAyaNVKDNNGESPLHNAAEYGDYACIKLLI 210
|
90 100
....*....|....*....|
gi 564355943 448 RHGANPDLRDEDGKTPLDKA 467
Cdd:PHA02874 211 DHGNHIMNKCKNGFTPLHNA 230
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
409-486 |
2.89e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 42.64 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355943 409 QEMVEFLCERGADVNRGQRSSS--LHYAACFGRPQVAKTLLRHGANPDLRDEDGKTPLDKARERGHSEVVAILQSPGDWM 486
Cdd:PHA02874 104 KDMIKTILDCGIDVNIKDAELKtfLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYA 183
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
431-455 |
6.49e-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: 6.49e-03
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
403-487 |
9.70e-03 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 41.39 E-value: 9.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355943 403 ASAFGTQEMVEFLCERG--ADVNRGQRSSSLHYAACFGRPQVAKTLLRHGANPDLRDEDGKTPLDKARERGHSEVVAIL- 479
Cdd:PLN03192 532 VASTGNAALLEELLKAKldPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILy 611
|
90
....*....|....*.
gi 564355943 480 --------QSPGDWMC 487
Cdd:PLN03192 612 hfasisdpHAAGDLLC 627
|
|
| |
