|
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
|
|
|
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
|
|