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Conserved domains on  [gi|1829727456|ref|XP_033178621|]
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E3 ubiquitin-protein ligase HECTD1 isoform X4 [Bombus impatiens]

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 ...
 2070-2526 1.38e-107

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: 348.40  E-value: 1.38e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456 2070 ERVSVPRGEKLLDWAEQVMKVHASR-KSILEVEFVGEEGTG-LGPTLEFFALVAAELQRKDLGLWLCDDENSpdtdqsrv 2147
Cdd:cd00078      1 LKITVRRDRILEDALRQLSKVSSSDlKKVLEVEFVGEEGIDaGGVTREFFTLVSKELFNPSYGLFRYTPDDS-------- 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456 2148 sgdqvrppgyyvtrpSGLFPAPLPQdsaACDRAIRYFWFLGVFLAKVLQDNRLVDLPLSRPFLKLMCHGDITnnvnekig 2227
Cdd:cd00078     73 ---------------GLLYPNPSSF---ADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLS-------- 126

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456 2228 lsgvtqesisssmsssfiseegeadtaysslepaswyaglldIEDLVLVDPVRGEFLKEVQtaiakrdrtlsdgRNSTDE 2307
Cdd:cd00078    127 ------------------------------------------LEDLEELDPELYKSLKELL-------------DNDGDE 151

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456 2308 ettlnithssgmsvpiEDLSLTMTYSPSSKIFAYNQVELIEGGAEISVTMENAREYAETTINFCLDGGISRQLESFKSGF 2387
Cdd:cd00078    152 ----------------DDLELTFTIELDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGF 215

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456 2388 SKVFPMEKLHAFSPEEVRAMLCGeqNPQWTREDLLNYTEPKLGYTRESPGFQRFVNVLLSLTGPERKAFLQFATGCSALP 2467
Cdd:cd00078    216 SEVIPEELLSLFTPEELELLICG--SEDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLP 293

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456 2468 PGGLCNLHPRLTvVRKVDAGSGGYPSVNTCVHYLKLPEYPTEEILKERLLAATRE-RGFH 2526
Cdd:cd00078    294 VGGFADLNPKFT-IRRVGSPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEgAGFG 352
MIB_HERC2 pfam06701
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain ...
 1331-1389 6.77e-26

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


:

Pssm-ID: 461991  Cd Length: 66  Bit Score: 102.68  E-value: 6.77e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1829727456 1331 GARVARGLDWKWRDQDGVPPGEGTVT------GELHNGWIDVTWDHGGSNSYRMGAEGKYDLRLV 1389
Cdd:pfam06701    1 GARVVRGPDWKWGDQDGGEGHVGTVVeirdwdSESPRSTVRVQWDNGSTNVYRVGYEGKYDLKVV 65
Sad1_UNC super family cl23730
Sad1 / UNC-like C-terminal; The C. elegans UNC-84 protein is a nuclear envelope protein that ...
 1162-1295 1.71e-24

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: 100.83  E-value: 1.71e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456 1162 RNLPYGHLEDILSRDPSALNCHTNDDRRAWFSIDLGVWIIPSAYTLRHARGYGR-SALRNWMFQASKDGIIWTtlYAHVD 1240
Cdd:pfam07738    1 LNYEAKPPKVILQPDYMPGPCWSFKGSRGFVVIELSEFIIVEAITLEHVEKSVFsSAPKDFEVSGSDRYPTTK--WVLLG 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1829727456 1241 DSSLNEPGSTA-SWTLEPPADETqgWRHLRLqQIGKNaSGQTHYLSVSGFEVYGEV 1295
Cdd:pfam07738   79 EFSYDLDGKTIqTFQLENPPDIW--VKYVKL-RILSN-YGNEHYTCLYRFRVHGTV 130
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
372-488 1.87e-23

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 103.11  E-value: 1.87e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456  372 LIDCIRSKDTDALIEAIDSGGIgVNFMDDVGQTLLNWASAFGTQEMVEFLCDRGADVNK--GQRSSSLHYAACFGRPAIA 449
Cdd:COG0666     91 LHAAARNGDLEIVKLLLEAGAD-VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAqdNDGNTPLHLAAANGNLEIV 169

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1829727456  450 KVLLRHGANPDLRDEDGKTPLDKArerVDEGHREVAAIL 488
Cdd:COG0666    170 KLLLEAGADVNARDNDGETPLHLA---AENGHLEIVKLL 205
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
 2070-2526 1.38e-107

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: 348.40  E-value: 1.38e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456 2070 ERVSVPRGEKLLDWAEQVMKVHASR-KSILEVEFVGEEGTG-LGPTLEFFALVAAELQRKDLGLWLCDDENSpdtdqsrv 2147
Cdd:cd00078      1 LKITVRRDRILEDALRQLSKVSSSDlKKVLEVEFVGEEGIDaGGVTREFFTLVSKELFNPSYGLFRYTPDDS-------- 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456 2148 sgdqvrppgyyvtrpSGLFPAPLPQdsaACDRAIRYFWFLGVFLAKVLQDNRLVDLPLSRPFLKLMCHGDITnnvnekig 2227
Cdd:cd00078     73 ---------------GLLYPNPSSF---ADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLS-------- 126

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456 2228 lsgvtqesisssmsssfiseegeadtaysslepaswyaglldIEDLVLVDPVRGEFLKEVQtaiakrdrtlsdgRNSTDE 2307
Cdd:cd00078    127 ------------------------------------------LEDLEELDPELYKSLKELL-------------DNDGDE 151

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456 2308 ettlnithssgmsvpiEDLSLTMTYSPSSKIFAYNQVELIEGGAEISVTMENAREYAETTINFCLDGGISRQLESFKSGF 2387
Cdd:cd00078    152 ----------------DDLELTFTIELDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGF 215

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456 2388 SKVFPMEKLHAFSPEEVRAMLCGeqNPQWTREDLLNYTEPKLGYTRESPGFQRFVNVLLSLTGPERKAFLQFATGCSALP 2467
Cdd:cd00078    216 SEVIPEELLSLFTPEELELLICG--SEDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLP 293

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456 2468 PGGLCNLHPRLTvVRKVDAGSGGYPSVNTCVHYLKLPEYPTEEILKERLLAATRE-RGFH 2526
Cdd:cd00078    294 VGGFADLNPKFT-IRRVGSPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEgAGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
 2094-2525 6.52e-88

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: 290.67  E-value: 6.52e-88
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456  2094 RKSILEVEFVGEEG-TGLGPTLEFFALVAAELQRKDLGLWLCDDENSpdtdqsrvsgdqvrppgyyvtrpsGLFPAPLPq 2172
Cdd:smart00119    3 KKRVLEIEFEGEEGlDGGGVTREFFFLLSKELFNPDYGLFRYSPNDY------------------------LLYPNPRS- 57

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456  2173 dSAACDRAIRYFWFLGVFLAKVLQDNRLVDLPLSRPFLKLMCHGDITnnvnekiglsgvtqesisssmsssfiseegead 2252
Cdd:smart00119   58 -GFANEEHLSYFRFIGRVLGKALYDNRLLDLFFARPFYKKLLGKPVT--------------------------------- 103

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456  2253 taysslepaswyaglldIEDLVLVDPVRGEFLKEVQtaiakrdrtlsdgrnstdeettLNithssgmSVPIEDLSLTMTY 2332
Cdd:smart00119  104 -----------------LHDLESLDPELYKSLKWLL----------------------LN-------NDTSEELDLTFSI 137

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456  2333 SPSSKIFAYNQVELIEGGAEISVTMENAREYAETTINFCLDGGISRQLESFKSGFSKVFPMEKLHAFSPEEVRAMLCGEQ 2412
Cdd:smart00119  138 VLTSEFGQVKVVELKPGGSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSP 217

                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456  2413 NpqWTREDLLNYTEPKLGYTRESPGFQRFVNVLLSLTGPERKAFLQFATGCSALPPGGLCNLHPRLTvVRKVDAGSGGYP 2492
Cdd:smart00119  218 E--IDVDDLKSNTEYKGGYSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSPKFT-IRKAGSDDERLP 294

                           410       420       430
                    ....*....|....*....|....*....|....
gi 1829727456  2493 SVNTCVHYLKLPEYPTEEILKERLLAATRE-RGF 2525
Cdd:smart00119  295 TAHTCFNRLKLPPYSSKEILREKLLLAINEgKGF 328
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
 2119-2527 3.13e-74

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 250.22  E-value: 3.13e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456 2119 LVAAELQRKDLGLWLCDDENSpdtdqsrvsgdqvrppGYYVTRPSGLFPAPLpqdsaacdRAIRYFWFLGVFLAKVLQDN 2198
Cdd:pfam00632    2 LLSKELFDPNYGLFEYETEDD----------------RTYWFNPSSSESPDL--------ELLDYFKFLGKLLGKAIYNG 57

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456 2199 RLVDLPLSRPFLKLMCHGDITnnvnekiglsgvtqesisssmsssfiseegeadtaysslepaswyaglldIEDLVLVDP 2278
Cdd:pfam00632   58 ILLDLPFPPFFYKKLLGEPLT--------------------------------------------------LEDLESIDP 87

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456 2279 VRGEFLKEVQTAIAKRDrtlsdgrnstdeettlnithssgmsvpiEDLSLTMTYSPSSKIFaynQVELIEGGAEISVTME 2358
Cdd:pfam00632   88 ELYKSLKSLLNMDNDDD----------------------------EDLGLTFTIPVFGESK---TIELIPNGRNIPVTNE 136

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456 2359 NAREYAETTINFCLDGGISRQLESFKSGFSKVFPMEKLHAFSPEEVRAMLCGeqNPQWTREDLLNYTEPKLGYTRESPGF 2438
Cdd:pfam00632  137 NKEEYIRLYVDYRLNKSIEPQLEAFRKGFYSVIPKEALSLFTPEELELLICG--SPEIDVEDLKKNTEYDGGYTKNSPTI 214

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456 2439 QRFVNVLLSLTGPERKAFLQFATGCSALPPGGLCNLhPRLTVVRKVDAGSGGYPSVNTCVHYLKLPEYPTEEILKERLLA 2518
Cdd:pfam00632  215 QWFWEILEEFSPEQRRLFLKFVTGSSRLPVGGFKSL-PKFTIVRKGGDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLI 293

                          410
                   ....*....|
gi 1829727456 2519 ATRE-RGFHL 2527
Cdd:pfam00632  294 AIEEgEGFGL 303
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
1933-2522 2.78e-52

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 200.76  E-value: 2.78e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456 1933 SVEDVLQLLRHVYVLSTTHddgkhidygeleestcWVHPDDftskkitNKIVQQIQDPLALAAGALPNWCEELArscPFL 2012
Cdd:COG5021    395 SIEDLGQFLFSDFLTSSST----------------YEDLRR-------EQLGRESDESFYVASNVQQQRASREG---PLL 448

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456 2013 LPFETRRLYFSCTAFGASRSIV--WLQTQRDAVLERQRAPGLSPRRDDIHEFR---------VGRLKHERVSvpRGEKLL 2081
Cdd:COG5021    449 SGWKTRLNNLYRFYFVEHRKKTltKNDSRLGSFISLNKLDIRRIKEDKRRKLFyslkqkakiFDPYLHIKVR--RDRVFE 526

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456 2082 DWAEQVMKVHAS-RKSILEVEFVGEEG-TGLGPTLEFFALVAAELQRKDLGLWLcddenspdtdqsrvsgdqvrppgyYV 2159
Cdd:COG5021    527 DSYREIMDESGDdLKKTLEIEFVGEEGiDAGGLTREWLFLLSKEMFNPDYGLFE------------------------YI 582

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456 2160 TrpSGLFPAPLPQDSAACDRAIRYFWFLGVFLAKVLQDNRLVDLPLSRPFLKLMCHGDITNnvnekiglsgvtqesisss 2239
Cdd:COG5021    583 T--EDLYTLPINPLSSINPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVSL------------------- 641

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456 2240 msssfiseegeadtaysslepaswyaglldiEDLVLVDPVRGEFLKEVQtaiakrdrtlsdgRNSTDEET-TLNIThssg 2318
Cdd:COG5021    642 -------------------------------VDLESLDPELYRSLVWLL-------------NNDIDETIlDLTFT---- 673

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456 2319 msvpIEDLSLTMTyspsskifayNQVELIEGGAEISVTMENAREYAETTINFCLDGGISRQLESFKSGFSKVFPMEKLHA 2398
Cdd:COG5021    674 ----VEDDSFGES----------RTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQI 739

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456 2399 FSPEEVRAMLCG-EQNPQWtrEDLLNYTEPKlGYTRESPGFQRFVNVLLSLTGPERKAFLQFATGCSALPPGGLCNLHPR 2477
Cdd:COG5021    740 FDESELELLIGGiPEDIDI--DDWKSNTAYH-GYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGS 816

                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*....
gi 1829727456 2478 LTVVRKVDAGSGG----YPSVNTCVHYLKLPEYPTEEILKERLLAATRE 2522
Cdd:COG5021    817 DGVRKFTIEKGGTdddrLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINE 865
MIB_HERC2 pfam06701
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain ...
 1331-1389 6.77e-26

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


Pssm-ID: 461991  Cd Length: 66  Bit Score: 102.68  E-value: 6.77e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1829727456 1331 GARVARGLDWKWRDQDGVPPGEGTVT------GELHNGWIDVTWDHGGSNSYRMGAEGKYDLRLV 1389
Cdd:pfam06701    1 GARVVRGPDWKWGDQDGGEGHVGTVVeirdwdSESPRSTVRVQWDNGSTNVYRVGYEGKYDLKVV 65
Sad1_UNC pfam07738
Sad1 / UNC-like C-terminal; The C. elegans UNC-84 protein is a nuclear envelope protein that ...
 1162-1295 1.71e-24

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: 100.83  E-value: 1.71e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456 1162 RNLPYGHLEDILSRDPSALNCHTNDDRRAWFSIDLGVWIIPSAYTLRHARGYGR-SALRNWMFQASKDGIIWTtlYAHVD 1240
Cdd:pfam07738    1 LNYEAKPPKVILQPDYMPGPCWSFKGSRGFVVIELSEFIIVEAITLEHVEKSVFsSAPKDFEVSGSDRYPTTK--WVLLG 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1829727456 1241 DSSLNEPGSTA-SWTLEPPADETqgWRHLRLqQIGKNaSGQTHYLSVSGFEVYGEV 1295
Cdd:pfam07738   79 EFSYDLDGKTIqTFQLENPPDIW--VKYVKL-RILSN-YGNEHYTCLYRFRVHGTV 130
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
372-488 1.87e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 103.11  E-value: 1.87e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456  372 LIDCIRSKDTDALIEAIDSGGIgVNFMDDVGQTLLNWASAFGTQEMVEFLCDRGADVNK--GQRSSSLHYAACFGRPAIA 449
Cdd:COG0666     91 LHAAARNGDLEIVKLLLEAGAD-VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAqdNDGNTPLHLAAANGNLEIV 169

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1829727456  450 KVLLRHGANPDLRDEDGKTPLDKArerVDEGHREVAAIL 488
Cdd:COG0666    170 KLLLEAGADVNARDNDGETPLHLA---AENGHLEIVKLL 205
Ank_2 pfam12796
Ankyrin repeats (3 copies);
372-463 3.84e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.06  E-value: 3.84e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456  372 LIDCIRSKDTDALIEAIDSGgIGVNFMDDVGQTLLNWASAFGTQEMVEFLCDRGADVNKGQRSSSLHYAACFGRPAIAKV 451
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRTALHYAARSGHLEIVKL 79

                           90
                   ....*....|..
gi 1829727456  452 LLRHGANPDLRD 463
Cdd:pfam12796   80 LLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 379-488 8.74e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 54.26  E-value: 8.74e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456  379 KDTDALIEAIDSGGIGVNFMDDVGQTLLNWASAFGTQE--MVEFLCDRGADVNKGQRS--SSLHYAACFGRPAIAKVLLR 454
Cdd:PHA03095   199 KPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYgqTPLHYAAVFNNPRACRRLIA 278

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1829727456  455 HGANPDLRDEDGKTPLDKAreRVDEGHREVAAIL 488
Cdd:PHA03095   279 LGADINAVSSDGNTPLSLM--VRNNNGRAVRAAL 310
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 402-470 3.95e-04

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: 45.77  E-value: 3.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456  402 GQTLLNWASAFGTQEMVEFLCDRGADVNKGQRSSS----------------LHYAACFGRPAIAKVLLRHGANPDLRDED 465
Cdd:cd22192     89 GETALHIAVVNQNLNLVRELIARGADVVSPRATGTffrpgpknliyygehpLSFAACVGNEEIVRLLIEHGADIRAQDSL 168


                   ....*
gi 1829727456  466 GKTPL 470
Cdd:cd22192    169 GNTVL 173
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 401-468 4.49e-03

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 42.38  E-value: 4.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456  401 VGQTLLNWASAFGTQEMVEFLCDRGADVN---------KGQRSSSLHY-------AACFGRPAIAKVLLRHGANPDLRDE 464
Cdd:TIGR00870  127 PGITALHLAAHRQNYEIVKLLLERGASVParacgdffvKSQGVDSFYHgesplnaAACLGSPSIVALLSEDPADILTADS 206


                   ....
gi 1829727456  465 DGKT 468
Cdd:TIGR00870  207 LGNT 210
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 437-461 7.81e-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: 36.03  E-value: 7.81e-03
                            10        20
                    ....*....|....*....|....*
gi 1829727456   437 LHYAACFGRPAIAKVLLRHGANPDL 461
Cdd:smart00248    6 LHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
 2070-2526 1.38e-107

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: 348.40  E-value: 1.38e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456 2070 ERVSVPRGEKLLDWAEQVMKVHASR-KSILEVEFVGEEGTG-LGPTLEFFALVAAELQRKDLGLWLCDDENSpdtdqsrv 2147
Cdd:cd00078      1 LKITVRRDRILEDALRQLSKVSSSDlKKVLEVEFVGEEGIDaGGVTREFFTLVSKELFNPSYGLFRYTPDDS-------- 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456 2148 sgdqvrppgyyvtrpSGLFPAPLPQdsaACDRAIRYFWFLGVFLAKVLQDNRLVDLPLSRPFLKLMCHGDITnnvnekig 2227
Cdd:cd00078     73 ---------------GLLYPNPSSF---ADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLS-------- 126

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456 2228 lsgvtqesisssmsssfiseegeadtaysslepaswyaglldIEDLVLVDPVRGEFLKEVQtaiakrdrtlsdgRNSTDE 2307
Cdd:cd00078    127 ------------------------------------------LEDLEELDPELYKSLKELL-------------DNDGDE 151

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456 2308 ettlnithssgmsvpiEDLSLTMTYSPSSKIFAYNQVELIEGGAEISVTMENAREYAETTINFCLDGGISRQLESFKSGF 2387
Cdd:cd00078    152 ----------------DDLELTFTIELDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGF 215

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456 2388 SKVFPMEKLHAFSPEEVRAMLCGeqNPQWTREDLLNYTEPKLGYTRESPGFQRFVNVLLSLTGPERKAFLQFATGCSALP 2467
Cdd:cd00078    216 SEVIPEELLSLFTPEELELLICG--SEDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLP 293

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456 2468 PGGLCNLHPRLTvVRKVDAGSGGYPSVNTCVHYLKLPEYPTEEILKERLLAATRE-RGFH 2526
Cdd:cd00078    294 VGGFADLNPKFT-IRRVGSPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEgAGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
 2094-2525 6.52e-88

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: 290.67  E-value: 6.52e-88
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456  2094 RKSILEVEFVGEEG-TGLGPTLEFFALVAAELQRKDLGLWLCDDENSpdtdqsrvsgdqvrppgyyvtrpsGLFPAPLPq 2172
Cdd:smart00119    3 KKRVLEIEFEGEEGlDGGGVTREFFFLLSKELFNPDYGLFRYSPNDY------------------------LLYPNPRS- 57

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456  2173 dSAACDRAIRYFWFLGVFLAKVLQDNRLVDLPLSRPFLKLMCHGDITnnvnekiglsgvtqesisssmsssfiseegead 2252
Cdd:smart00119   58 -GFANEEHLSYFRFIGRVLGKALYDNRLLDLFFARPFYKKLLGKPVT--------------------------------- 103

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456  2253 taysslepaswyaglldIEDLVLVDPVRGEFLKEVQtaiakrdrtlsdgrnstdeettLNithssgmSVPIEDLSLTMTY 2332
Cdd:smart00119  104 -----------------LHDLESLDPELYKSLKWLL----------------------LN-------NDTSEELDLTFSI 137

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456  2333 SPSSKIFAYNQVELIEGGAEISVTMENAREYAETTINFCLDGGISRQLESFKSGFSKVFPMEKLHAFSPEEVRAMLCGEQ 2412
Cdd:smart00119  138 VLTSEFGQVKVVELKPGGSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSP 217

                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456  2413 NpqWTREDLLNYTEPKLGYTRESPGFQRFVNVLLSLTGPERKAFLQFATGCSALPPGGLCNLHPRLTvVRKVDAGSGGYP 2492
Cdd:smart00119  218 E--IDVDDLKSNTEYKGGYSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSPKFT-IRKAGSDDERLP 294

                           410       420       430
                    ....*....|....*....|....*....|....
gi 1829727456  2493 SVNTCVHYLKLPEYPTEEILKERLLAATRE-RGF 2525
Cdd:smart00119  295 TAHTCFNRLKLPPYSSKEILREKLLLAINEgKGF 328
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
 2119-2527 3.13e-74

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 250.22  E-value: 3.13e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456 2119 LVAAELQRKDLGLWLCDDENSpdtdqsrvsgdqvrppGYYVTRPSGLFPAPLpqdsaacdRAIRYFWFLGVFLAKVLQDN 2198
Cdd:pfam00632    2 LLSKELFDPNYGLFEYETEDD----------------RTYWFNPSSSESPDL--------ELLDYFKFLGKLLGKAIYNG 57

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456 2199 RLVDLPLSRPFLKLMCHGDITnnvnekiglsgvtqesisssmsssfiseegeadtaysslepaswyaglldIEDLVLVDP 2278
Cdd:pfam00632   58 ILLDLPFPPFFYKKLLGEPLT--------------------------------------------------LEDLESIDP 87

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456 2279 VRGEFLKEVQTAIAKRDrtlsdgrnstdeettlnithssgmsvpiEDLSLTMTYSPSSKIFaynQVELIEGGAEISVTME 2358
Cdd:pfam00632   88 ELYKSLKSLLNMDNDDD----------------------------EDLGLTFTIPVFGESK---TIELIPNGRNIPVTNE 136

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456 2359 NAREYAETTINFCLDGGISRQLESFKSGFSKVFPMEKLHAFSPEEVRAMLCGeqNPQWTREDLLNYTEPKLGYTRESPGF 2438
Cdd:pfam00632  137 NKEEYIRLYVDYRLNKSIEPQLEAFRKGFYSVIPKEALSLFTPEELELLICG--SPEIDVEDLKKNTEYDGGYTKNSPTI 214

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456 2439 QRFVNVLLSLTGPERKAFLQFATGCSALPPGGLCNLhPRLTVVRKVDAGSGGYPSVNTCVHYLKLPEYPTEEILKERLLA 2518
Cdd:pfam00632  215 QWFWEILEEFSPEQRRLFLKFVTGSSRLPVGGFKSL-PKFTIVRKGGDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLI 293

                          410
                   ....*....|
gi 1829727456 2519 ATRE-RGFHL 2527
Cdd:pfam00632  294 AIEEgEGFGL 303
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
1933-2522 2.78e-52

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 200.76  E-value: 2.78e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456 1933 SVEDVLQLLRHVYVLSTTHddgkhidygeleestcWVHPDDftskkitNKIVQQIQDPLALAAGALPNWCEELArscPFL 2012
Cdd:COG5021    395 SIEDLGQFLFSDFLTSSST----------------YEDLRR-------EQLGRESDESFYVASNVQQQRASREG---PLL 448

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456 2013 LPFETRRLYFSCTAFGASRSIV--WLQTQRDAVLERQRAPGLSPRRDDIHEFR---------VGRLKHERVSvpRGEKLL 2081
Cdd:COG5021    449 SGWKTRLNNLYRFYFVEHRKKTltKNDSRLGSFISLNKLDIRRIKEDKRRKLFyslkqkakiFDPYLHIKVR--RDRVFE 526

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456 2082 DWAEQVMKVHAS-RKSILEVEFVGEEG-TGLGPTLEFFALVAAELQRKDLGLWLcddenspdtdqsrvsgdqvrppgyYV 2159
Cdd:COG5021    527 DSYREIMDESGDdLKKTLEIEFVGEEGiDAGGLTREWLFLLSKEMFNPDYGLFE------------------------YI 582

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456 2160 TrpSGLFPAPLPQDSAACDRAIRYFWFLGVFLAKVLQDNRLVDLPLSRPFLKLMCHGDITNnvnekiglsgvtqesisss 2239
Cdd:COG5021    583 T--EDLYTLPINPLSSINPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVSL------------------- 641

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456 2240 msssfiseegeadtaysslepaswyaglldiEDLVLVDPVRGEFLKEVQtaiakrdrtlsdgRNSTDEET-TLNIThssg 2318
Cdd:COG5021    642 -------------------------------VDLESLDPELYRSLVWLL-------------NNDIDETIlDLTFT---- 673

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456 2319 msvpIEDLSLTMTyspsskifayNQVELIEGGAEISVTMENAREYAETTINFCLDGGISRQLESFKSGFSKVFPMEKLHA 2398
Cdd:COG5021    674 ----VEDDSFGES----------RTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQI 739

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456 2399 FSPEEVRAMLCG-EQNPQWtrEDLLNYTEPKlGYTRESPGFQRFVNVLLSLTGPERKAFLQFATGCSALPPGGLCNLHPR 2477
Cdd:COG5021    740 FDESELELLIGGiPEDIDI--DDWKSNTAYH-GYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGS 816

                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*....
gi 1829727456 2478 LTVVRKVDAGSGG----YPSVNTCVHYLKLPEYPTEEILKERLLAATRE 2522
Cdd:COG5021    817 DGVRKFTIEKGGTdddrLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINE 865
MIB_HERC2 pfam06701
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain ...
 1331-1389 6.77e-26

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


Pssm-ID: 461991  Cd Length: 66  Bit Score: 102.68  E-value: 6.77e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1829727456 1331 GARVARGLDWKWRDQDGVPPGEGTVT------GELHNGWIDVTWDHGGSNSYRMGAEGKYDLRLV 1389
Cdd:pfam06701    1 GARVVRGPDWKWGDQDGGEGHVGTVVeirdwdSESPRSTVRVQWDNGSTNVYRVGYEGKYDLKVV 65
Sad1_UNC pfam07738
Sad1 / UNC-like C-terminal; The C. elegans UNC-84 protein is a nuclear envelope protein that ...
 1162-1295 1.71e-24

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: 100.83  E-value: 1.71e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456 1162 RNLPYGHLEDILSRDPSALNCHTNDDRRAWFSIDLGVWIIPSAYTLRHARGYGR-SALRNWMFQASKDGIIWTtlYAHVD 1240
Cdd:pfam07738    1 LNYEAKPPKVILQPDYMPGPCWSFKGSRGFVVIELSEFIIVEAITLEHVEKSVFsSAPKDFEVSGSDRYPTTK--WVLLG 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1829727456 1241 DSSLNEPGSTA-SWTLEPPADETqgWRHLRLqQIGKNaSGQTHYLSVSGFEVYGEV 1295
Cdd:pfam07738   79 EFSYDLDGKTIqTFQLENPPDIW--VKYVKL-RILSN-YGNEHYTCLYRFRVHGTV 130
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
372-488 1.87e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 103.11  E-value: 1.87e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456  372 LIDCIRSKDTDALIEAIDSGGIgVNFMDDVGQTLLNWASAFGTQEMVEFLCDRGADVNK--GQRSSSLHYAACFGRPAIA 449
Cdd:COG0666     91 LHAAARNGDLEIVKLLLEAGAD-VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAqdNDGNTPLHLAAANGNLEIV 169

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1829727456  450 KVLLRHGANPDLRDEDGKTPLDKArerVDEGHREVAAIL 488
Cdd:COG0666    170 KLLLEAGADVNARDNDGETPLHLA---AENGHLEIVKLL 205
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
372-489 2.56e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 99.64  E-value: 2.56e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456  372 LIDCIRSKDTDA---LIEAidsgGIGVNFMDDVGQTLLNWASAFGTQEMVEFLCDRGADVNKGQRS--SSLHYAACFGRP 446
Cdd:COG0666    124 LHLAAYNGNLEIvklLLEA----GADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDgeTPLHLAAENGHL 199

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1829727456  447 AIAKVLLRHGANPDLRDEDGKTPLDKARERvdeGHREVAAILQ 489
Cdd:COG0666    200 EIVKLLLEAGADVNAKDNDGKTALDLAAEN---GNLEIVKLLL 239
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
372-488 1.78e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 91.55  E-value: 1.78e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456  372 LIDCIRSKDTDALIEAIDSGGIGVNFMDDVGQTLLNWASAFGTQEMVEFLCDRGADVNK--GQRSSSLHYAACFGRPAIA 449
Cdd:COG0666     57 LLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNArdKDGETPLHLAAYNGNLEIV 136

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1829727456  450 KVLLRHGANPDLRDEDGKTPLDKArerVDEGHREVAAIL 488
Cdd:COG0666    137 KLLLEAGADVNAQDNDGNTPLHLA---AANGNLEIVKLL 172
Ank_2 pfam12796
Ankyrin repeats (3 copies);
372-463 3.84e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.06  E-value: 3.84e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456  372 LIDCIRSKDTDALIEAIDSGgIGVNFMDDVGQTLLNWASAFGTQEMVEFLCDRGADVNKGQRSSSLHYAACFGRPAIAKV 451
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRTALHYAARSGHLEIVKL 79

                           90
                   ....*....|..
gi 1829727456  452 LLRHGANPDLRD 463
Cdd:pfam12796   80 LLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
376-488 3.09e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 66.90  E-value: 3.09e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456  376 IRSKDTDALIEAIDSGGIGVNFMDDVGQTLLNWASAFGTQEMVEFLCDRGADVNKG--QRSSSLHYAACFGRPAIAKVLL 453
Cdd:COG0666     28 AALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKddGGNTLLHAAARNGDLEIVKLLL 107

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1829727456  454 RHGANPDLRDEDGKTPLDKArerVDEGHREVAAIL 488
Cdd:COG0666    108 EAGADVNARDKDGETPLHLA---AYNGNLEIVKLL 139
PHA03095 PHA03095
ankyrin-like protein; Provisional
 379-488 8.74e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 54.26  E-value: 8.74e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456  379 KDTDALIEAIDSGGIGVNFMDDVGQTLLNWASAFGTQE--MVEFLCDRGADVNKGQRS--SSLHYAACFGRPAIAKVLLR 454
Cdd:PHA03095   199 KPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYgqTPLHYAAVFNNPRACRRLIA 278

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1829727456  455 HGANPDLRDEDGKTPLDKAreRVDEGHREVAAIL 488
Cdd:PHA03095   279 LGADINAVSSDGNTPLSLM--VRNNNGRAVRAAL 310
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 376-477 8.89e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 54.12  E-value: 8.89e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456  376 IRSKDTDALIEA-----IDSGGIGVNFMD-DVGQTLLNWASAFGTQEMVEFLCDRGADVNKGQR--SSSLHYAACFGRPA 447
Cdd:PHA02878   136 IDKKSKDDIIEAeitklLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKtnNSPLHHAVKHYNKP 215

                           90       100       110
                   ....*....|....*....|....*....|
gi 1829727456  448 IAKVLLRHGANPDLRDEDGKTPLDKARERV 477
Cdd:PHA02878   216 IVHILLENGASTDARDKCGNTPLHISVGYC 245
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 410-522 1.58e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 53.75  E-value: 1.58e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456  410 SAFGTQEMVEFLCDRGADVN--KGQRSSSLHYAACFGRPAIAKVLLRHGANPDLRDEDGKTPLDKARErvdEGHREVAAI 487
Cdd:PTZ00322    90 AASGDAVGARILLTGGADPNcrDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEE---NGFREVVQL 166

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1829727456  488 LQSPGEWMLPNQEHRKPEteaEFTEPKGDPEMAPV 522
Cdd:PTZ00322   167 LSRHSQCHFELGANAKPD---SFTGKPPSLEDSPI 198
Ank_2 pfam12796
Ankyrin repeats (3 copies);
437-488 2.99e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 47.42  E-value: 2.99e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1829727456  437 LHYAACFGRPAIAKVLLRHGANPDLRDEDGKTPLDKArerVDEGHREVAAIL 488
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLA---AKNGHLEIVKLL 49
Ank_5 pfam13857
Ankyrin repeats (many copies);
431-473 7.30e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.42  E-value: 7.30e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1829727456  431 GQRSSSLHYAACFGRPAIAKVLLRHGANPDLRDEDGKTPLDKA 473
Cdd:pfam13857   14 GEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 371-526 3.57e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 48.83  E-value: 3.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456  371 QLIDCIRSKDTDALIEAIDSGgigvNFMDDV----GQTLLNWASAFGTQEMVEFLCDRGAD--VNKGQRSSSLHYAACFG 444
Cdd:PHA02875    71 ELHDAVEEGDVKAVEELLDLG----KFADDVfykdGMTPLHLATILKKLDIMKLLIARGADpdIPNTDKFSPLHLAVMMG 146

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456  445 RPAIAKVLLRHGANPDLRDEDGKTPLDKArerVDEGHREVAAILQSPGEwmLPNQEHRKPETEAE-FTEPKGDPEMAPVY 523
Cdd:PHA02875   147 DIKGIELLIDHKACLDIEDCCGCTPLIIA---MAKGDIAICKMLLDSGA--NIDYFGKNGCVAALcYAIENNKIDIVRLF 221


                   ...
gi 1829727456  524 LKR 526
Cdd:PHA02875   222 IKR 224
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 384-470 4.97e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 48.51  E-value: 4.97e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456  384 LIEAIDSGGIGVNFMDDVGQTLLNWASAFGTQ--EMVEFLCDRGADVNKGQR------------------SSSLHYAACF 443
Cdd:PHA03100   123 IVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKNRvnyllsygvpinikdvygFTPLHYAVYN 202

                           90       100
                   ....*....|....*....|....*..
gi 1829727456  444 GRPAIAKVLLRHGANPDLRDEDGKTPL 470
Cdd:PHA03100   203 NNPEFVKYLLDLGANPNLVNKYGDTPL 229
Ank_4 pfam13637
Ankyrin repeats (many copies);
433-488 6.01e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.65  E-value: 6.01e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1829727456  433 RSSSLHYAACFGRPAIAKVLLRHGANPDLRDEDGKTPLDKARERvdeGHREVAAIL 488
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASN---GNVEVLKLL 53
PHA03095 PHA03095
ankyrin-like protein; Provisional
 392-470 6.58e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 48.10  E-value: 6.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456  392 GIGVNFMDDVGQTLLNWASAFGTQ---EMVEFLCDRGADVNKGQRSSS--LHYAACFG-RPAIAKVLLRHGANPDLRDED 465
Cdd:PHA03095    37 GADVNFRGEYGKTPLHLYLHYSSEkvkDIVRLLLEAGADVNAPERCGFtpLHLYLYNAtTLDVIKLLIKAGADVNAKDKV 116


                   ....*
gi 1829727456  466 GKTPL 470
Cdd:PHA03095   117 GRTPL 121
PHA03095 PHA03095
ankyrin-like protein; Provisional
 382-471 8.66e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 47.71  E-value: 8.66e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456  382 DALIEAidsgGIGVNFMDDVGQTLLNWASAFG-TQEMVEFLCDRGADVNK--GQRSSSLH-YAACFG-RPAIAKVLLRHG 456
Cdd:PHA03095    67 RLLLEA----GADVNAPERCGFTPLHLYLYNAtTLDVIKLLIKAGADVNAkdKVGRTPLHvYLSGFNiNPKVIRLLLRKG 142

                           90
                   ....*....|....*
gi 1829727456  457 ANPDLRDEDGKTPLD 471
Cdd:PHA03095   143 ADVNALDLYGMTPLA 157
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 416-470 1.21e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 45.58  E-value: 1.21e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1829727456  416 EMVEFLCDRGADVN---KGQRSSSLHYAACFGR---PAIAKVLLRHGANPDLRDEDGKTPL 470
Cdd:PHA02859    67 EILKFLIENGADVNfktRDNNLSALHHYLSFNKnvePEILKILIDSGSSITEEDEDGKNLL 127
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 402-470 3.95e-04

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: 45.77  E-value: 3.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456  402 GQTLLNWASAFGTQEMVEFLCDRGADVNKGQRSSS----------------LHYAACFGRPAIAKVLLRHGANPDLRDED 465
Cdd:cd22192     89 GETALHIAVVNQNLNLVRELIARGADVVSPRATGTffrpgpknliyygehpLSFAACVGNEEIVRLLIEHGADIRAQDSL 168


                   ....*
gi 1829727456  466 GKTPL 470
Cdd:cd22192    169 GNTVL 173
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 437-464 1.20e-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: 1.20e-03
                           10        20
                   ....*....|....*....|....*....
gi 1829727456  437 LHYAAC-FGRPAIAKVLLRHGANPDLRDE 464
Cdd:pfam00023    6 LHLAAGrRGNLEIVKLLLSKGADVNARDK 34
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 392-473 2.63e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 43.03  E-value: 2.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456  392 GIGVNFMDDVGQTLLNWASAFGTQEMVEFLCDRGA--DVNKGQRSSSLHYAACFGRPAIAKVLLRHGANPDLRDEDGKTP 469
Cdd:PHA02874   147 GADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAyaNVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTP 226


                   ....
gi 1829727456  470 LDKA 473
Cdd:PHA02874   227 LHNA 230
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 373-478 4.00e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 42.26  E-value: 4.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456  373 IDCIrSKDTdalIEAIDSGGIGVNFMDDVGQTLLNWASAFGTQEMVEFLCDRGADVNKGQRSSS--LHYAACFGRPAIAK 450
Cdd:PHA02874    99 IPCI-EKDM---IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCypIHIAIKHNFFDIIK 174

                           90       100
                   ....*....|....*....|....*...
gi 1829727456  451 VLLRHGANPDLRDEDGKTPLDKARERVD 478
Cdd:PHA02874   175 LLLEKGAYANVKDNNGESPLHNAAEYGD 202
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 401-468 4.49e-03

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 42.38  E-value: 4.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829727456  401 VGQTLLNWASAFGTQEMVEFLCDRGADVN---------KGQRSSSLHY-------AACFGRPAIAKVLLRHGANPDLRDE 464
Cdd:TIGR00870  127 PGITALHLAAHRQNYEIVKLLLERGASVParacgdffvKSQGVDSFYHgesplnaAACLGSPSIVALLSEDPADILTADS 206


                   ....
gi 1829727456  465 DGKT 468
Cdd:TIGR00870  207 LGNT 210
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 437-461 7.81e-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: 36.03  E-value: 7.81e-03
                            10        20
                    ....*....|....*....|....*
gi 1829727456   437 LHYAACFGRPAIAKVLLRHGANPDL 461
Cdd:smart00248    6 LHLAAENGNLEVVKLLLDKGADINA 30
 
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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