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Conserved domains on  [gi|1831513287|ref|NP_001368365|]
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E3 ubiquitin-protein ligase [Caenorhabditis elegans]

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 ...
 2221-2648 3.84e-123

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: 393.08  E-value: 3.84e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513287 2221 ERVKVTRaeETLLDQAIRLMKFHA--DRKAVLEIEYTNEEGTG-LGPTLEFYALVAAELQRKSLALWVCDDDDTHasksg 2297
Cdd:cd00078      1 LKITVRR--DRILEDALRQLSKVSssDLKKVLEVEFVGEEGIDaGGVTREFFTLVSKELFNPSYGLFRYTPDDSG----- 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513287 2298 eerevdlgegkkpigyyvrrvgGLFPAPLPPGTDETKraaDMFRVLGVFLAKVLLDGRLVDLPLSRPFLKLLvhpqigdd 2377
Cdd:cd00078     74 ----------------------LLYPNPSSFADEDHL---KLFRFLGRLLGKALYEGRLLDLPFSRAFYKKL-------- 120

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513287 2378 argpnLHKILSLDDFEEVNPVKGSFLKELRALAQRkrliendtsidsnskrrkiaelklhikgstcrVEDLALNFTVNPP 2457
Cdd:cd00078    121 -----LGKPLSLEDLEELDPELYKSLKELLDNDGD--------------------------------EDDLELTFTIELD 163

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513287 2458 SKVFQYAEMELVDGGSDIDVTIDNVEQYVEKCEEFYLNTGIAYQMRAFRDGFDRVFPLRTLRAYSPEEVQRLLSGEqcPE 2537
Cdd:cd00078    164 SSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGS--ED 241

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513287 2538 WSRDDILNYTEPKLGYTRESPGFLRFVDVMEALTAQERKNFLQFATGCSSLPPGGLANLHPRLTIvRKVESGDGSYPSVN 2617
Cdd:cd00078    242 IDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLNPKFTI-RRVGSPDDRLPTAH 320

                          410       420       430
                   ....*....|....*....|....*....|..
gi 1831513287 2618 TCVHYLKLPEYSSSAILRERLLTAINEK-GFH 2648
Cdd:cd00078    321 TCFNLLKLPPYSSKEILREKLLYAINEGaGFG 352
MIB_HERC2 pfam06701
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain ...
 1452-1509 4.52e-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: 97.29  E-value: 4.52e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1831513287 1452 SKVVRGKDWRWEDQDGGEGKFGRIT------SPPESGWVDVTWDNGNANSYRFGANGNFDIERV 1509
Cdd:pfam06701    2 ARVVRGPDWKWGDQDGGEGHVGTVVeirdwdSESPRSTVRVQWDNGSTNVYRVGYEGKYDLKVV 65
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
237-453 8.06e-23

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 101.18  E-value: 8.06e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513287  237 LISIMVASNDENSPTTASANILSIVLSLIGNLCRGSSLITEKVLTSPNMITGLKATLTNKEERVVTDGLRFCDLLLVLLC 316
Cdd:COG0666      6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513287  317 EGRSALpltsvvsgDYAAGSGAERVHRQLIDA---IRQKDL---TALVDAIESGQV-----------DVNFADDVGQSLT 379
Cdd:COG0666     86 GGNTLL--------HAAARNGDLEIVKLLLEAgadVNARDKdgeTPLHLAAYNGNLeivkllleagaDVNAQDNDGNTPL 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1831513287  380 NWASAFGSIEMVQYLCDKGSDVNK--GHKSSSLHYAACFGRPDVVKLLLQRGANPDLRDEDGKTALDKARERSDDD 453
Cdd:COG0666    158 HLAAANGNLEIVKLLLEAGADVNArdNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLE 233
Sad1_UNC super family cl23730
Sad1 / UNC-like C-terminal; The C. elegans UNC-84 protein is a nuclear envelope protein that ...
 1243-1365 9.13e-14

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


The actual alignment was detected with superfamily member pfam07738:

Pssm-ID: 474037  Cd Length: 130  Bit Score: 70.40  E-value: 9.13e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513287 1243 PEDLLSRDQNPINCHTSDDKNAHFTIDLGLFVVPTSYSLRHSRGYGR-SALRNWMLQGSVDAKRWENVIVhtDDKGLGEP 1321
Cdd:pfam07738    8 PKVILQPDYMPGPCWSFKGSRGFVVIELSEFIIVEAITLEHVEKSVFsSAPKDFEVSGSDRYPTTKWVLL--GEFSYDLD 85

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1831513287 1322 GSTA-TWHVGEKGTTAFRF--FRIAQNGknssGQTHYLSCSGFEIYG 1365
Cdd:pfam07738   86 GKTIqTFQLENPPDIWVKYvkLRILSNY----GNEHYTCLYRFRVHG 128
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
 2221-2648 3.84e-123

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: 393.08  E-value: 3.84e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513287 2221 ERVKVTRaeETLLDQAIRLMKFHA--DRKAVLEIEYTNEEGTG-LGPTLEFYALVAAELQRKSLALWVCDDDDTHasksg 2297
Cdd:cd00078      1 LKITVRR--DRILEDALRQLSKVSssDLKKVLEVEFVGEEGIDaGGVTREFFTLVSKELFNPSYGLFRYTPDDSG----- 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513287 2298 eerevdlgegkkpigyyvrrvgGLFPAPLPPGTDETKraaDMFRVLGVFLAKVLLDGRLVDLPLSRPFLKLLvhpqigdd 2377
Cdd:cd00078     74 ----------------------LLYPNPSSFADEDHL---KLFRFLGRLLGKALYEGRLLDLPFSRAFYKKL-------- 120

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513287 2378 argpnLHKILSLDDFEEVNPVKGSFLKELRALAQRkrliendtsidsnskrrkiaelklhikgstcrVEDLALNFTVNPP 2457
Cdd:cd00078    121 -----LGKPLSLEDLEELDPELYKSLKELLDNDGD--------------------------------EDDLELTFTIELD 163

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513287 2458 SKVFQYAEMELVDGGSDIDVTIDNVEQYVEKCEEFYLNTGIAYQMRAFRDGFDRVFPLRTLRAYSPEEVQRLLSGEqcPE 2537
Cdd:cd00078    164 SSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGS--ED 241

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513287 2538 WSRDDILNYTEPKLGYTRESPGFLRFVDVMEALTAQERKNFLQFATGCSSLPPGGLANLHPRLTIvRKVESGDGSYPSVN 2617
Cdd:cd00078    242 IDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLNPKFTI-RRVGSPDDRLPTAH 320

                          410       420       430
                   ....*....|....*....|....*....|..
gi 1831513287 2618 TCVHYLKLPEYSSSAILRERLLTAINEK-GFH 2648
Cdd:cd00078    321 TCFNLLKLPPYSSKEILREKLLYAINEGaGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
 2246-2647 4.08e-120

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: 383.12  E-value: 4.08e-120
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513287  2246 RKAVLEIEYTNEEG-TGLGPTLEFYALVAAELQRKSLALWVCDDDDTHasksgeerevdlgegkkpigyyvrrvggLFPA 2324
Cdd:smart00119    3 KKRVLEIEFEGEEGlDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYL----------------------------LYPN 54

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513287  2325 PLPPGTDETKRAadMFRVLGVFLAKVLLDGRLVDLPLSRPFLKLLvhpqigddargpnLHKILSLDDFEEVNPVKGSFLK 2404
Cdd:smart00119   55 PRSGFANEEHLS--YFRFIGRVLGKALYDNRLLDLFFARPFYKKL-------------LGKPVTLHDLESLDPELYKSLK 119

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513287  2405 ELralaqrkrLIENDTSidsnskrrkiaelklhikgstcrvEDLALNFTVNPPSKVFQYAEMELVDGGSDIDVTIDNVEQ 2484
Cdd:smart00119  120 WL--------LLNNDTS------------------------EELDLTFSIVLTSEFGQVKVVELKPGGSNIPVTEENKKE 167

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513287  2485 YVEKCEEFYLNTGIAYQMRAFRDGFDRVFPLRTLRAYSPEEVQRLLSGeqCPEWSRDDILNYTEPKLGYTRESPGFLRFV 2564
Cdd:smart00119  168 YVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICG--SPEIDVDDLKSNTEYKGGYSANSQTIKWFW 245

                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513287  2565 DVMEALTAQERKNFLQFATGCSSLPPGGLANLHPRLTIVRKVESgDGSYPSVNTCVHYLKLPEYSSSAILRERLLTAINE 2644
Cdd:smart00119  246 EVVESFTNEERRKLLQFVTGSSRLPVGGFAALSPKFTIRKAGSD-DERLPTAHTCFNRLKLPPYSSKEILREKLLLAINE 324


                    ....
gi 1831513287  2645 -KGF 2647
Cdd:smart00119  325 gKGF 328
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
 2271-2649 2.33e-84

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 279.50  E-value: 2.33e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513287 2271 LVAAELQRKSLALWVCDDDDTHasksgeerevdlgegkkpigyyvrrvggLFPAPLPPGTDETKRAADMFRVLGVFLAKV 2350
Cdd:pfam00632    2 LLSKELFDPNYGLFEYETEDDR----------------------------TYWFNPSSSESPDLELLDYFKFLGKLLGKA 53

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513287 2351 LLDGRLVDLPLSRPFLKLLvhpqigddargpnLHKILSLDDFEEVNPVKGSFLKELRalaqrkrLIENDTsidsnskrrk 2430
Cdd:pfam00632   54 IYNGILLDLPFPPFFYKKL-------------LGEPLTLEDLESIDPELYKSLKSLL-------NMDNDD---------- 103

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513287 2431 iaelklhikgstcrVEDLALNFTVNppskVFQYAEM-ELVDGGSDIDVTIDNVEQYVEKCEEFYLNTGIAYQMRAFRDGF 2509
Cdd:pfam00632  104 --------------DEDLGLTFTIP----VFGESKTiELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQLEAFRKGF 165

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513287 2510 DRVFPLRTLRAYSPEEVQRLLSGEqcPEWSRDDILNYTEPKLGYTRESPGFLRFVDVMEALTAQERKNFLQFATGCSSLP 2589
Cdd:pfam00632  166 YSVIPKEALSLFTPEELELLICGS--PEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGSSRLP 243

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1831513287 2590 PGGLANLhPRLTIVRKVESGDGSYPSVNTCVHYLKLPEYSSSAILRERLLTAINE-KGFHL 2649
Cdd:pfam00632  244 VGGFKSL-PKFTIVRKGGDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEgEGFGL 303
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
2119-2647 2.92e-56

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 213.48  E-value: 2.92e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513287 2119 FISDKLTLKVTQVLSDALVVAARSLPEWCSRlvyKYPCLFTVETRNMYMQATAFGVSRTIV--WLQQRRDAAVERargsa 2196
Cdd:COG5021    413 TYEDLRREQLGRESDESFYVASNVQQQRASR---EGPLLSGWKTRLNNLYRFYFVEHRKKTltKNDSRLGSFISL----- 484

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513287 2197 qagNSSAARQHDRYHEYRVGRLRHE---------RVKVTRaeETLLDQAIRLMKFHA--DRKAVLEIEYTNEEG-TGLGP 2264
Cdd:COG5021    485 ---NKLDIRRIKEDKRRKLFYSLKQkakifdpylHIKVRR--DRVFEDSYREIMDESgdDLKKTLEIEFVGEEGiDAGGL 559

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513287 2265 TLEFYALVAAELQrkslalwvcDDDDTHAsksgEEREVDLgegkkpigYYvrrvgglFPAPLPPGTDETKRaaDMFRVLG 2344
Cdd:COG5021    560 TREWLFLLSKEMF---------NPDYGLF----EYITEDL--------YT-------LPINPLSSINPEHL--SYFKFLG 609

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513287 2345 VFLAKVLLDGRLVDLPLSRPFLKLLvhpqigddargpnLHKILSLDDFEEVNPVKGSFLKELRalaqrkrlienDTSIDS 2424
Cdd:COG5021    610 RVIGKAIYDSRILDVQFSKAFYKKL-------------LGKPVSLVDLESLDPELYRSLVWLL-----------NNDIDE 665

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513287 2425 NskrrkiaelklhIKGSTCRVEDLALNFTVNppskvfqyaeMELVDGGSDIDVTIDNVEQYVEKCEEFYLNTGIAYQMRA 2504
Cdd:COG5021    666 T------------ILDLTFTVEDDSFGESRT----------VELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSA 723

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513287 2505 FRDGFDRVFPLRTLRAYSPEEVQRLLSGEqcPEWSR-DDILNYTEPKlGYTRESPGFLRFVDVMEALTAQERKNFLQFAT 2583
Cdd:COG5021    724 FKSGFSEIIPPDLLQIFDESELELLIGGI--PEDIDiDDWKSNTAYH-GYTEDSPIIVWFWEIISEFDFEERAKLLQFVT 800

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1831513287 2584 GCSSLPPGGLANLHPRLTIVRKV--ESGDGSY--PSVNTCVHYLKLPEYSSSAILRERLLTAINE-KGF 2647
Cdd:COG5021    801 GTSRIPINGFKDLQGSDGVRKFTieKGGTDDDrlPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEgAGF 869
MIB_HERC2 pfam06701
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain ...
 1452-1509 4.52e-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: 97.29  E-value: 4.52e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1831513287 1452 SKVVRGKDWRWEDQDGGEGKFGRIT------SPPESGWVDVTWDNGNANSYRFGANGNFDIERV 1509
Cdd:pfam06701    2 ARVVRGPDWKWGDQDGGEGHVGTVVeirdwdSESPRSTVRVQWDNGSTNVYRVGYEGKYDLKVV 65
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
237-453 8.06e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 101.18  E-value: 8.06e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513287  237 LISIMVASNDENSPTTASANILSIVLSLIGNLCRGSSLITEKVLTSPNMITGLKATLTNKEERVVTDGLRFCDLLLVLLC 316
Cdd:COG0666      6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513287  317 EGRSALpltsvvsgDYAAGSGAERVHRQLIDA---IRQKDL---TALVDAIESGQV-----------DVNFADDVGQSLT 379
Cdd:COG0666     86 GGNTLL--------HAAARNGDLEIVKLLLEAgadVNARDKdgeTPLHLAAYNGNLeivkllleagaDVNAQDNDGNTPL 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1831513287  380 NWASAFGSIEMVQYLCDKGSDVNK--GHKSSSLHYAACFGRPDVVKLLLQRGANPDLRDEDGKTALDKARERSDDD 453
Cdd:COG0666    158 HLAAANGNLEIVKLLLEAGADVNArdNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLE 233
Ank_2 pfam12796
Ankyrin repeats (3 copies);
345-436 3.42e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.14  E-value: 3.42e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513287  345 LIDAIRQKDLTALVDAIESGqVDVNFADDVGQSLTNWASAFGSIEMVQYLCDKGSDVNKGHKSSSLHYAACFGRPDVVKL 424
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRTALHYAARSGHLEIVKL 79

                           90
                   ....*....|..
gi 1831513287  425 LLQRGANPDLRD 436
Cdd:pfam12796   80 LLEKGADINVKD 91
Sad1_UNC pfam07738
Sad1 / UNC-like C-terminal; The C. elegans UNC-84 protein is a nuclear envelope protein that ...
 1243-1365 9.13e-14

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: 70.40  E-value: 9.13e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513287 1243 PEDLLSRDQNPINCHTSDDKNAHFTIDLGLFVVPTSYSLRHSRGYGR-SALRNWMLQGSVDAKRWENVIVhtDDKGLGEP 1321
Cdd:pfam07738    8 PKVILQPDYMPGPCWSFKGSRGFVVIELSEFIIVEAITLEHVEKSVFsSAPKDFEVSGSDRYPTTKWVLL--GEFSYDLD 85

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1831513287 1322 GSTA-TWHVGEKGTTAFRF--FRIAQNGknssGQTHYLSCSGFEIYG 1365
Cdd:pfam07738   86 GKTIqTFQLENPPDIWVKYvkLRILSNY----GNEHYTCLYRFRVHG 128
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 391-443 1.47e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 50.05  E-value: 1.47e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1831513287  391 VQYLCDKGSDVN----KGhkSSSLHYAACFGRPDVVKLLLQRGANPDLRDEDGKTAL 443
Cdd:PHA03100   175 VNYLLSYGVPINikdvYG--FTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPL 229
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 405-434 1.36e-04

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: 41.03  E-value: 1.36e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 1831513287   405 HKSSSLHYAACFGRPDVVKLLLQRGANPDL 434
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 375-443 1.02e-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: 44.62  E-value: 1.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513287  375 GQSLTNWASAFGSIEMVQYLCDKGSDVNKG---------HKSSSLHY-------AACFGRPDVVKLLLQRGANPDLRDED 438
Cdd:cd22192     89 GETALHIAVVNQNLNLVRELIARGADVVSPratgtffrpGPKNLIYYgehplsfAACVGNEEIVRLLIEHGADIRAQDSL 168


                   ....*
gi 1831513287  439 GKTAL 443
Cdd:cd22192    169 GNTVL 173
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
 2221-2648 3.84e-123

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: 393.08  E-value: 3.84e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513287 2221 ERVKVTRaeETLLDQAIRLMKFHA--DRKAVLEIEYTNEEGTG-LGPTLEFYALVAAELQRKSLALWVCDDDDTHasksg 2297
Cdd:cd00078      1 LKITVRR--DRILEDALRQLSKVSssDLKKVLEVEFVGEEGIDaGGVTREFFTLVSKELFNPSYGLFRYTPDDSG----- 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513287 2298 eerevdlgegkkpigyyvrrvgGLFPAPLPPGTDETKraaDMFRVLGVFLAKVLLDGRLVDLPLSRPFLKLLvhpqigdd 2377
Cdd:cd00078     74 ----------------------LLYPNPSSFADEDHL---KLFRFLGRLLGKALYEGRLLDLPFSRAFYKKL-------- 120

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513287 2378 argpnLHKILSLDDFEEVNPVKGSFLKELRALAQRkrliendtsidsnskrrkiaelklhikgstcrVEDLALNFTVNPP 2457
Cdd:cd00078    121 -----LGKPLSLEDLEELDPELYKSLKELLDNDGD--------------------------------EDDLELTFTIELD 163

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513287 2458 SKVFQYAEMELVDGGSDIDVTIDNVEQYVEKCEEFYLNTGIAYQMRAFRDGFDRVFPLRTLRAYSPEEVQRLLSGEqcPE 2537
Cdd:cd00078    164 SSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGS--ED 241

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513287 2538 WSRDDILNYTEPKLGYTRESPGFLRFVDVMEALTAQERKNFLQFATGCSSLPPGGLANLHPRLTIvRKVESGDGSYPSVN 2617
Cdd:cd00078    242 IDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLNPKFTI-RRVGSPDDRLPTAH 320

                          410       420       430
                   ....*....|....*....|....*....|..
gi 1831513287 2618 TCVHYLKLPEYSSSAILRERLLTAINEK-GFH 2648
Cdd:cd00078    321 TCFNLLKLPPYSSKEILREKLLYAINEGaGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
 2246-2647 4.08e-120

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: 383.12  E-value: 4.08e-120
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513287  2246 RKAVLEIEYTNEEG-TGLGPTLEFYALVAAELQRKSLALWVCDDDDTHasksgeerevdlgegkkpigyyvrrvggLFPA 2324
Cdd:smart00119    3 KKRVLEIEFEGEEGlDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYL----------------------------LYPN 54

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513287  2325 PLPPGTDETKRAadMFRVLGVFLAKVLLDGRLVDLPLSRPFLKLLvhpqigddargpnLHKILSLDDFEEVNPVKGSFLK 2404
Cdd:smart00119   55 PRSGFANEEHLS--YFRFIGRVLGKALYDNRLLDLFFARPFYKKL-------------LGKPVTLHDLESLDPELYKSLK 119

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513287  2405 ELralaqrkrLIENDTSidsnskrrkiaelklhikgstcrvEDLALNFTVNPPSKVFQYAEMELVDGGSDIDVTIDNVEQ 2484
Cdd:smart00119  120 WL--------LLNNDTS------------------------EELDLTFSIVLTSEFGQVKVVELKPGGSNIPVTEENKKE 167

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513287  2485 YVEKCEEFYLNTGIAYQMRAFRDGFDRVFPLRTLRAYSPEEVQRLLSGeqCPEWSRDDILNYTEPKLGYTRESPGFLRFV 2564
Cdd:smart00119  168 YVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICG--SPEIDVDDLKSNTEYKGGYSANSQTIKWFW 245

                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513287  2565 DVMEALTAQERKNFLQFATGCSSLPPGGLANLHPRLTIVRKVESgDGSYPSVNTCVHYLKLPEYSSSAILRERLLTAINE 2644
Cdd:smart00119  246 EVVESFTNEERRKLLQFVTGSSRLPVGGFAALSPKFTIRKAGSD-DERLPTAHTCFNRLKLPPYSSKEILREKLLLAINE 324


                    ....
gi 1831513287  2645 -KGF 2647
Cdd:smart00119  325 gKGF 328
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
 2271-2649 2.33e-84

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 279.50  E-value: 2.33e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513287 2271 LVAAELQRKSLALWVCDDDDTHasksgeerevdlgegkkpigyyvrrvggLFPAPLPPGTDETKRAADMFRVLGVFLAKV 2350
Cdd:pfam00632    2 LLSKELFDPNYGLFEYETEDDR----------------------------TYWFNPSSSESPDLELLDYFKFLGKLLGKA 53

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513287 2351 LLDGRLVDLPLSRPFLKLLvhpqigddargpnLHKILSLDDFEEVNPVKGSFLKELRalaqrkrLIENDTsidsnskrrk 2430
Cdd:pfam00632   54 IYNGILLDLPFPPFFYKKL-------------LGEPLTLEDLESIDPELYKSLKSLL-------NMDNDD---------- 103

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513287 2431 iaelklhikgstcrVEDLALNFTVNppskVFQYAEM-ELVDGGSDIDVTIDNVEQYVEKCEEFYLNTGIAYQMRAFRDGF 2509
Cdd:pfam00632  104 --------------DEDLGLTFTIP----VFGESKTiELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQLEAFRKGF 165

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513287 2510 DRVFPLRTLRAYSPEEVQRLLSGEqcPEWSRDDILNYTEPKLGYTRESPGFLRFVDVMEALTAQERKNFLQFATGCSSLP 2589
Cdd:pfam00632  166 YSVIPKEALSLFTPEELELLICGS--PEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGSSRLP 243

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1831513287 2590 PGGLANLhPRLTIVRKVESGDGSYPSVNTCVHYLKLPEYSSSAILRERLLTAINE-KGFHL 2649
Cdd:pfam00632  244 VGGFKSL-PKFTIVRKGGDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEgEGFGL 303
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
2119-2647 2.92e-56

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 213.48  E-value: 2.92e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513287 2119 FISDKLTLKVTQVLSDALVVAARSLPEWCSRlvyKYPCLFTVETRNMYMQATAFGVSRTIV--WLQQRRDAAVERargsa 2196
Cdd:COG5021    413 TYEDLRREQLGRESDESFYVASNVQQQRASR---EGPLLSGWKTRLNNLYRFYFVEHRKKTltKNDSRLGSFISL----- 484

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513287 2197 qagNSSAARQHDRYHEYRVGRLRHE---------RVKVTRaeETLLDQAIRLMKFHA--DRKAVLEIEYTNEEG-TGLGP 2264
Cdd:COG5021    485 ---NKLDIRRIKEDKRRKLFYSLKQkakifdpylHIKVRR--DRVFEDSYREIMDESgdDLKKTLEIEFVGEEGiDAGGL 559

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513287 2265 TLEFYALVAAELQrkslalwvcDDDDTHAsksgEEREVDLgegkkpigYYvrrvgglFPAPLPPGTDETKRaaDMFRVLG 2344
Cdd:COG5021    560 TREWLFLLSKEMF---------NPDYGLF----EYITEDL--------YT-------LPINPLSSINPEHL--SYFKFLG 609

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513287 2345 VFLAKVLLDGRLVDLPLSRPFLKLLvhpqigddargpnLHKILSLDDFEEVNPVKGSFLKELRalaqrkrlienDTSIDS 2424
Cdd:COG5021    610 RVIGKAIYDSRILDVQFSKAFYKKL-------------LGKPVSLVDLESLDPELYRSLVWLL-----------NNDIDE 665

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513287 2425 NskrrkiaelklhIKGSTCRVEDLALNFTVNppskvfqyaeMELVDGGSDIDVTIDNVEQYVEKCEEFYLNTGIAYQMRA 2504
Cdd:COG5021    666 T------------ILDLTFTVEDDSFGESRT----------VELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSA 723

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513287 2505 FRDGFDRVFPLRTLRAYSPEEVQRLLSGEqcPEWSR-DDILNYTEPKlGYTRESPGFLRFVDVMEALTAQERKNFLQFAT 2583
Cdd:COG5021    724 FKSGFSEIIPPDLLQIFDESELELLIGGI--PEDIDiDDWKSNTAYH-GYTEDSPIIVWFWEIISEFDFEERAKLLQFVT 800

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1831513287 2584 GCSSLPPGGLANLHPRLTIVRKV--ESGDGSY--PSVNTCVHYLKLPEYSSSAILRERLLTAINE-KGF 2647
Cdd:COG5021    801 GTSRIPINGFKDLQGSDGVRKFTieKGGTDDDrlPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEgAGF 869
MIB_HERC2 pfam06701
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain ...
 1452-1509 4.52e-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: 97.29  E-value: 4.52e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1831513287 1452 SKVVRGKDWRWEDQDGGEGKFGRIT------SPPESGWVDVTWDNGNANSYRFGANGNFDIERV 1509
Cdd:pfam06701    2 ARVVRGPDWKWGDQDGGEGHVGTVVeirdwdSESPRSTVRVQWDNGSTNVYRVGYEGKYDLKVV 65
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
237-453 8.06e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 101.18  E-value: 8.06e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513287  237 LISIMVASNDENSPTTASANILSIVLSLIGNLCRGSSLITEKVLTSPNMITGLKATLTNKEERVVTDGLRFCDLLLVLLC 316
Cdd:COG0666      6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513287  317 EGRSALpltsvvsgDYAAGSGAERVHRQLIDA---IRQKDL---TALVDAIESGQV-----------DVNFADDVGQSLT 379
Cdd:COG0666     86 GGNTLL--------HAAARNGDLEIVKLLLEAgadVNARDKdgeTPLHLAAYNGNLeivkllleagaDVNAQDNDGNTPL 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1831513287  380 NWASAFGSIEMVQYLCDKGSDVNK--GHKSSSLHYAACFGRPDVVKLLLQRGANPDLRDEDGKTALDKARERSDDD 453
Cdd:COG0666    158 HLAAANGNLEIVKLLLEAGADVNArdNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLE 233
Ank_2 pfam12796
Ankyrin repeats (3 copies);
345-436 3.42e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.14  E-value: 3.42e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513287  345 LIDAIRQKDLTALVDAIESGqVDVNFADDVGQSLTNWASAFGSIEMVQYLCDKGSDVNKGHKSSSLHYAACFGRPDVVKL 424
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRTALHYAARSGHLEIVKL 79

                           90
                   ....*....|..
gi 1831513287  425 LLQRGANPDLRD 436
Cdd:pfam12796   80 LLEKGADINVKD 91
Sad1_UNC pfam07738
Sad1 / UNC-like C-terminal; The C. elegans UNC-84 protein is a nuclear envelope protein that ...
 1243-1365 9.13e-14

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: 70.40  E-value: 9.13e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513287 1243 PEDLLSRDQNPINCHTSDDKNAHFTIDLGLFVVPTSYSLRHSRGYGR-SALRNWMLQGSVDAKRWENVIVhtDDKGLGEP 1321
Cdd:pfam07738    8 PKVILQPDYMPGPCWSFKGSRGFVVIELSEFIIVEAITLEHVEKSVFsSAPKDFEVSGSDRYPTTKWVLL--GEFSYDLD 85

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1831513287 1322 GSTA-TWHVGEKGTTAFRF--FRIAQNGknssGQTHYLSCSGFEIYG 1365
Cdd:pfam07738   86 GKTIqTFQLENPPDIWVKYvkLRILSNY----GNEHYTCLYRFRVHG 128
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
332-461 7.77e-13

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 71.52  E-value: 7.77e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513287  332 YAAGSGAERVHRQLI------DAIRQKDLTALVDAIESGQV-----------DVNFADDVGQSLTNWASAFGSIEMVQYL 394
Cdd:COG0666    126 LAAYNGNLEIVKLLLeagadvNAQDNDGNTPLHLAAANGNLeivkllleagaDVNARDNDGETPLHLAAENGHLEIVKLL 205

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1831513287  395 CDKGSDVNK--GHKSSSLHYAACFGRPDVVKLLLQRGANPDLRDEDGKTALDKARERSDDDHNQVANIL 461
Cdd:COG0666    206 LEAGADVNAkdNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLA 274
Ank_2 pfam12796
Ankyrin repeats (3 copies);
410-443 1.07e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 48.96  E-value: 1.07e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1831513287  410 LHYAACFGRPDVVKLLLQRGANPDLRDEDGKTAL 443
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTAL 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
404-446 1.25e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.73  E-value: 1.25e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1831513287  404 GHKSSSLHYAACFGRPDVVKLLLQRGANPDLRDEDGKTALDKA 446
Cdd:pfam13857   14 GEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
407-446 3.28e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.11  E-value: 3.28e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1831513287  407 SSSLHYAACFGRPDVVKLLLQRGANPDLRDEDGKTALDKA 446
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFA 41
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 391-443 1.47e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 50.05  E-value: 1.47e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1831513287  391 VQYLCDKGSDVN----KGhkSSSLHYAACFGRPDVVKLLLQRGANPDLRDEDGKTAL 443
Cdd:PHA03100   175 VNYLLSYGVPINikdvYG--FTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPL 229
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 410-437 3.53e-05

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: 42.66  E-value: 3.53e-05
                           10        20
                   ....*....|....*....|....*....
gi 1831513287  410 LHYAAC-FGRPDVVKLLLQRGANPDLRDE 437
Cdd:pfam00023    6 LHLAAGrRGNLEIVKLLLSKGADVNARDK 34
PHA03095 PHA03095
ankyrin-like protein; Provisional
 352-446 4.95e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 48.48  E-value: 4.95e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513287  352 KDLTALVDAIESGQVDVNFADDVGQSLTNWASAFGS---IEMVQYLcDKGSDVNKGHKS--SSLHYAACFGRPDVVKLLL 426
Cdd:PHA03095   199 KPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSckrSLVLPLL-IAGISINARNRYgqTPLHYAAVFNNPRACRRLI 277

                           90       100
                   ....*....|....*....|
gi 1831513287  427 QRGANPDLRDEDGKTALDKA 446
Cdd:PHA03095   278 ALGADINAVSSDGNTPLSLM 297
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 383-497 5.79e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.74  E-value: 5.79e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513287  383 SAFGSIEMVQYLCDKGSDVN--KGHKSSSLHYAACFGRPDVVKLLLQRGANPDLRDEDGKTALDKARErsdDDHNQVANI 460
Cdd:PTZ00322    90 AASGDAVGARILLTGGADPNcrDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEE---NGFREVVQL 166

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1831513287  461 LESPSAFMRNKEDPKVKASTSKQPG-------TSTKPE---LPNPNL 497
Cdd:PTZ00322   167 LSRHSQCHFELGANAKPDSFTGKPPsledspiSSHHPDfsaVPQPMM 213
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 405-434 1.36e-04

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: 41.03  E-value: 1.36e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 1831513287   405 HKSSSLHYAACFGRPDVVKLLLQRGANPDL 434
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA03095 PHA03095
ankyrin-like protein; Provisional
 388-444 1.46e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.94  E-value: 1.46e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1831513287  388 IEMVQYLCDKGSDVNKGHKS--SSLH-YAACFG-RPDVVKLLLQRGANPDLRDEDGKTALD 444
Cdd:PHA03095    97 LDVIKLLIKAGADVNAKDKVgrTPLHvYLSGFNiNPKVIRLLLRKGADVNALDLYGMTPLA 157
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 387-443 2.91e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 44.42  E-value: 2.91e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1831513287  387 SIEMVQYLCDKGSDVN---KGHKSSSLHYAACFGR---PDVVKLLLQRGANPDLRDEDGKTAL 443
Cdd:PHA02859    65 NVEILKFLIENGADVNfktRDNNLSALHHYLSFNKnvePEILKILIDSGSSITEEDEDGKNLL 127
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 348-446 3.58e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 45.72  E-value: 3.58e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513287  348 AIRQKDLTALVDAIESGqVDVNFADDVGQSLTNWASAFGSIEMVQYLCDKGS--DVNKGHKSSSLHYAACFGRPDVVKLL 425
Cdd:PHA02874   131 AIKKGDLESIKMLFEYG-ADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAyaNVKDNNGESPLHNAAEYGDYACIKLL 209

                           90       100
                   ....*....|....*....|.
gi 1831513287  426 LQRGANPDLRDEDGKTALDKA 446
Cdd:PHA02874   210 IDHGNHIMNKCKNGFTPLHNA 230
Ank_4 pfam13637
Ankyrin repeats (many copies);
381-426 4.73e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.34  E-value: 4.73e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1831513287  381 WASAFGSIEMVQYLCDKGSDVNK--GHKSSSLHYAACFGRPDVVKLLL 426
Cdd:pfam13637    7 AAAASGHLELLRLLLEKGADINAvdGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 375-443 1.02e-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: 44.62  E-value: 1.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513287  375 GQSLTNWASAFGSIEMVQYLCDKGSDVNKG---------HKSSSLHY-------AACFGRPDVVKLLLQRGANPDLRDED 438
Cdd:cd22192     89 GETALHIAVVNQNLNLVRELIARGADVVSPratgtffrpGPKNLIYYgehplsfAACVGNEEIVRLLIEHGADIRAQDSL 168


                   ....*
gi 1831513287  439 GKTAL 443
Cdd:cd22192    169 GNTVL 173
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 408-433 2.86e-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.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.24  E-value: 2.86e-03
                           10        20
                   ....*....|....*....|....*.
gi 1831513287  408 SSLHYAACFGRPDVVKLLLQRGANPD 433
Cdd:pfam13606    4 TPLHLAARNGRLEIVKLLLENGADIN 29
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 367-443 3.96e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 42.56  E-value: 3.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513287  367 DVNFAD-DVGQSLTNWASAFGSIEMVQYLCDKGSDVNKGHK--SSSLHYAACFGRPDVVKLLLQRGANPDLRDEDGKTAL 443
Cdd:PHA02878   159 DINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKtnNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPL 238
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 375-483 4.33e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 42.44  E-value: 4.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513287  375 GQSLTNWASAFGSIEMVQYLCDKGSDVN---KG------HKSSSLHY-------AACFGRPDVVKLLLQRGANP-DLRDE 437
Cdd:cd22194    141 GQTALNIAIERRQGDIVKLLIAKGADVNahaKGvffnpkYKHEGFYFgetplalAACTNQPEIVQLLMEKESTDiTSQDS 220

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1831513287  438 DGKTALDKARERSDDDHNQVANILESPSAFMRNKEDPKVKASTSKQ 483
Cdd:cd22194    221 RGNTVLHALVTVAEDSKTQNDFVKRMYDMILLKSENKNLETIRNNE 266
 
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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