|
Name |
Accession |
Description |
Interval |
E-value |
| HECTc |
cd00078 |
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ... |
2265-2725 |
5.11e-117 |
|
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: 375.36 E-value: 5.11e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583318 2265 ERVKVPRNEdLLMWAMQVMKTHCN--RKSVLEVEFLDEEGTG-LGPTLEFYALVAAEIQRSDLCMWLCDDDlgedtenst 2341
Cdd:cd00078 1 LKITVRRDR-ILEDALRQLSKVSSsdLKKVLEVEFVGEEGIDaGGVTREFFTLVSKELFNPSYGLFRYTPD--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583318 2342 qsaegnskpvgyyvnrREHGIFPAPLPQnseICENVLKYFWFFGVFVAKVLQDMRLVDIPLSTSFLQLLChnkvlsrnlq 2421
Cdd:cd00078 71 ----------------DSGLLYPNPSSF---ADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLL---------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583318 2422 kvisdrrngdlsvvsedsdivetctkllrtdsnksnafGGILSLENLKEIDPTRYQFLQEMQNLllrkqsiefddtisae 2501
Cdd:cd00078 122 --------------------------------------GKPLSLEDLEELDPELYKSLKELLDN---------------- 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583318 2502 kkhelinelklqtqnglEVSLEDLALTFTYLPSSSIYGYTQAELLPNGSSVNVTIDNLEAYCELLMNFILQDGIAQQMKA 2581
Cdd:cd00078 148 -----------------DGDEDDLELTFTIELDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEA 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583318 2582 FSDGFNEVFPLKKLAAFTPSEARMMICGEqfPHWSREDIISYTEPKLGYNKDSPGFQRFVNVLLSMSGDERKAFLQFTTG 2661
Cdd:cd00078 211 FRDGFSEVIPEELLSLFTPEELELLICGS--EDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTG 288
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24583318 2662 CSSLPPGGLANLHPRLTvVRKVDAGVGSYPSVNTCVHYLKLPDYPTEEIMKERLLTATKEK-GFH 2725
Cdd:cd00078 289 SSRLPVGGFADLNPKFT-IRRVGSPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGaGFG 352
|
|
| HECTc |
smart00119 |
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ... |
2289-2724 |
3.79e-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: 291.45 E-value: 3.79e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583318 2289 RKSVLEVEFLDEEG-TGLGPTLEFYALVAAEIQRSDLCMWLCDDDLgedtenstqsaegnskpvgyyvnrreHGIFPAPL 2367
Cdd:smart00119 3 KKRVLEIEFEGEEGlDGGGVTREFFFLLSKELFNPDYGLFRYSPND--------------------------YLLYPNPR 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583318 2368 pqNSEICENVLKYFWFFGVFVAKVLQDMRLVDIPLSTSFLQLLCHNKVlsrnlqkvisdrrngdlsvvsedsdivetctk 2447
Cdd:smart00119 57 --SGFANEEHLSYFRFIGRVLGKALYDNRLLDLFFARPFYKKLLGKPV-------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583318 2448 llrtdsnksnafggilSLENLKEIDPTRYQFLQEMQnlllrkqsIEFDDTisaekkhelinelklqtqnglevslEDLAL 2527
Cdd:smart00119 103 ----------------TLHDLESLDPELYKSLKWLL--------LNNDTS-------------------------EELDL 133
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583318 2528 TFTYLPSSSIYGYTQAELLPNGSSVNVTIDNLEAYCELLMNFILQDGIAQQMKAFSDGFNEVFPLKKLAAFTPSEARMMI 2607
Cdd:smart00119 134 TFSIVLTSEFGQVKVVELKPGGSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLI 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583318 2608 CGEqfPHWSREDIISYTEPKLGYNKDSPGFQRFVNVLLSMSGDERKAFLQFTTGCSSLPPGGLANLHPRLTvVRKVDAGV 2687
Cdd:smart00119 214 CGS--PEIDVDDLKSNTEYKGGYSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSPKFT-IRKAGSDD 290
|
410 420 430
....*....|....*....|....*....|....*...
gi 24583318 2688 GSYPSVNTCVHYLKLPDYPTEEIMKERLLTATKE-KGF 2724
Cdd:smart00119 291 ERLPTAHTCFNRLKLPPYSSKEILREKLLLAINEgKGF 328
|
|
| HECT |
pfam00632 |
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ... |
2314-2726 |
1.18e-80 |
|
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl Terminus.
Pssm-ID: 459880 Cd Length: 304 Bit Score: 269.09 E-value: 1.18e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583318 2314 LVAAEIQRSDLCMWLCDDDlgedtenstqsaegnskpvgyyvnrREHGIFPAPLPQNSEICENvLKYFWFFGVFVAKVLQ 2393
Cdd:pfam00632 2 LLSKELFDPNYGLFEYETE-------------------------DDRTYWFNPSSSESPDLEL-LDYFKFLGKLLGKAIY 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583318 2394 DMRLVDIPLSTSFLQLLCHNKVlsrnlqkvisdrrngdlsvvsedsdivetctkllrtdsnksnafggilSLENLKEIDP 2473
Cdd:pfam00632 56 NGILLDLPFPPFFYKKLLGEPL------------------------------------------------TLEDLESIDP 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583318 2474 TRYQFLQEMQNlllrkqsIEFDDtisaekkhelinelklqtqnglevsLEDLALTFTYlpssSIYGYT-QAELLPNGSSV 2552
Cdd:pfam00632 88 ELYKSLKSLLN-------MDNDD-------------------------DEDLGLTFTI----PVFGESkTIELIPNGRNI 131
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583318 2553 NVTIDNLEAYCELLMNFILQDGIAQQMKAFSDGFNEVFPLKKLAAFTPSEARMMICGEqfPHWSREDIISYTEPKLGYNK 2632
Cdd:pfam00632 132 PVTNENKEEYIRLYVDYRLNKSIEPQLEAFRKGFYSVIPKEALSLFTPEELELLICGS--PEIDVEDLKKNTEYDGGYTK 209
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583318 2633 DSPGFQRFVNVLLSMSGDERKAFLQFTTGCSSLPPGGLANLhPRLTVVRKVDAGVGSYPSVNTCVHYLKLPDYPTEEIMK 2712
Cdd:pfam00632 210 NSPTIQWFWEILEEFSPEQRRLFLKFVTGSSRLPVGGFKSL-PKFTIVRKGGDDDDRLPTAHTCFNRLKLPDYSSKEILK 288
|
410
....*....|....*
gi 24583318 2713 ERLLTATKE-KGFHL 2726
Cdd:pfam00632 289 EKLLIAIEEgEGFGL 303
|
|
| HUL4 |
COG5021 |
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones]; |
2105-2724 |
1.09e-53 |
|
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227354 [Multi-domain] Cd Length: 872 Bit Score: 205.39 E-value: 1.09e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583318 2105 DVSSKSGASTLSPNSPMhigFNVADNNLCSVDDVLELLTQING-----LNQSEIDSDVKEHGVSVLSEDLFISKKITNKL 2179
Cdd:COG5021 346 DDSSSIKDLPHQVGSNP---FLEAHPEFSELLKNQSRGTTRDFrnkptGWSSSIEDLGQFLFSDFLTSSSTYEDLRREQL 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583318 2180 QQQIQDPLVLASNALPNWCEnlnQSCPFLFPFETR---------------QLYFNCTSFGASRSIVCLQSQRDVTVERQR 2244
Cdd:COG5021 423 GRESDESFYVASNVQQQRAS---REGPLLSGWKTRlnnlyrfyfvehrkkTLTKNDSRLGSFISLNKLDIRRIKEDKRRK 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583318 2245 IPIMSPRRDDHEfriGRLKHERVKvprnedllmwamqvmkthcnRKSVLEV---EFLDEEGTGLGPTLEFYALVAAEIQR 2321
Cdd:COG5021 500 LFYSLKQKAKIF---DPYLHIKVR--------------------RDRVFEDsyrEIMDESGDDLKKTLEIEFVGEEGIDA 556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583318 2322 SDLCMWLCdddlgedtenSTQSAEGNSKPVGYYVNRREHgIFPAPLPQNSEICENVLKYFWFFGVFVAKVLQDMRLVDIP 2401
Cdd:COG5021 557 GGLTREWL----------FLLSKEMFNPDYGLFEYITED-LYTLPINPLSSINPEHLSYFKFLGRVIGKAIYDSRILDVQ 625
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583318 2402 LSTSFLQLLCHNKVlsrnlqkvisdrrngdlsvvsedsdivetctkllrtdsnksnafggilSLENLKEIDPTRYQFLQE 2481
Cdd:COG5021 626 FSKAFYKKLLGKPV------------------------------------------------SLVDLESLDPELYRSLVW 657
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583318 2482 MQNLLLRKQSIEfddtisaekkhelinelklqtqngLEVSLEDLALTFTylpsssiygyTQAELLPNGSSVNVTIDNLEA 2561
Cdd:COG5021 658 LLNNDIDETILD------------------------LTFTVEDDSFGES----------RTVELIPNGRNISVTNENKKE 703
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583318 2562 YCELLMNFILQDGIAQQMKAFSDGFNEVFPLKKLAAFTPSEARMMICG--EQFphwSREDIISYTEPKlGYNKDSPGFQR 2639
Cdd:COG5021 704 YVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGipEDI---DIDDWKSNTAYH-GYTEDSPIIVW 779
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583318 2640 FVNVLLSMSGDERKAFLQFTTGCSSLPPGGLANLHPRLTVVRKV--DAGVGSY--PSVNTCVHYLKLPDYPTEEIMKERL 2715
Cdd:COG5021 780 FWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTieKGGTDDDrlPSAHTCFNRLKLPEYSSKEKLRSKL 859
|
650
....*....|
gi 24583318 2716 LTATKE-KGF 2724
Cdd:COG5021 860 LTAINEgAGF 869
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
375-509 |
3.86e-25 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 108.12 E-value: 3.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583318 375 LAPRPRRNNTNTDRTHRQLIDCIRSKDSEALREAIESGgIDVNCMDDVGQTLLNWASAFGTLEMVEYLCEKGADVNK--G 452
Cdd:COG0666 73 LLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAG-ADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAqdN 151
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 24583318 453 QRSSSLHYAACFGRPAIAKILLKFGAYPDLRDEDGKTPLDKARERlddGHREVAAIL 509
Cdd:COG0666 152 DGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAEN---GHLEIVKLL 205
|
|
| MIB_HERC2 |
pfam06701 |
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain ... |
1333-1390 |
4.50e-23 |
|
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: 94.59 E-value: 4.50e-23
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24583318 1333 GARVIRGVDWRWEEQDGCAE--GTIT------GEIHNGWIDVKWDHGVRNSYRMGAEGKYDLKLAD 1390
Cdd:pfam06701 1 GARVVRGPDWKWGDQDGGEGhvGTVVeirdwdSESPRSTVRVQWDNGSTNVYRVGYEGKYDLKVVD 66
|
|
| Sad1_UNC |
pfam07738 |
Sad1 / UNC-like C-terminal; The C. elegans UNC-84 protein is a nuclear envelope protein that ... |
1173-1298 |
7.92e-20 |
|
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: 87.73 E-value: 7.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583318 1173 EDILSRDSISLNCHTKDNKKAWFAIDLGVYIIPTAYTLRHARGYGR-SALRNWLLQGSKDGSTWTtlSTHVDDKSLVEPG 1251
Cdd:pfam07738 9 KVILQPDYMPGPCWSFKGSRGFVVIELSEFIIVEAITLEHVEKSVFsSAPKDFEVSGSDRYPTTK--WVLLGEFSYDLDG 86
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 24583318 1252 STA-TWPINCATDDSVWYRHIRIQQNGrnasGQTHYLSLSGFEIYGRV 1298
Cdd:pfam07738 87 KTIqTFQLENPPDIWVKYVKLRILSNY----GNEHYTCLYRFRVHGTV 130
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
393-484 |
3.57e-15 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 72.84 E-value: 3.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583318 393 LIDCIRSKDSEALREAIESGgIDVNCMDDVGQTLLNWASAFGTLEMVEYLCEKGADVNKGQRSSSLHYAACFGRPAIAKI 472
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRTALHYAARSGHLEIVKL 79
|
90
....*....|..
gi 24583318 473 LLKFGAYPDLRD 484
Cdd:pfam12796 80 LLEKGADINVKD 91
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
431-511 |
1.09e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 54.13 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583318 431 SAFGTLEMVEYLCEKGADVN--KGQRSSSLHYAACFGRPAIAKILLKFGAYPDLRDEDGKTPLDKARErldDGHREVAAI 508
Cdd:PTZ00322 90 AASGDAVGARILLTGGADPNcrDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEE---NGFREVVQL 166
|
...
gi 24583318 509 LQS 511
Cdd:PTZ00322 167 LSR 169
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
423-491 |
2.81e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 43.08 E-value: 2.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583318 423 GQTLLNWASAFGTLEMVEYLCEKGADVNKGQRSSS----------------LHYAACFGRPAIAKILLKFGAYPDLRDED 486
Cdd:cd22192 89 GETALHIAVVNQNLNLVRELIARGADVVSPRATGTffrpgpknliyygehpLSFAACVGNEEIVRLLIEHGADIRAQDSL 168
|
....*
gi 24583318 487 GKTPL 491
Cdd:cd22192 169 GNTVL 173
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| HECTc |
cd00078 |
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ... |
2265-2725 |
5.11e-117 |
|
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: 375.36 E-value: 5.11e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583318 2265 ERVKVPRNEdLLMWAMQVMKTHCN--RKSVLEVEFLDEEGTG-LGPTLEFYALVAAEIQRSDLCMWLCDDDlgedtenst 2341
Cdd:cd00078 1 LKITVRRDR-ILEDALRQLSKVSSsdLKKVLEVEFVGEEGIDaGGVTREFFTLVSKELFNPSYGLFRYTPD--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583318 2342 qsaegnskpvgyyvnrREHGIFPAPLPQnseICENVLKYFWFFGVFVAKVLQDMRLVDIPLSTSFLQLLChnkvlsrnlq 2421
Cdd:cd00078 71 ----------------DSGLLYPNPSSF---ADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLL---------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583318 2422 kvisdrrngdlsvvsedsdivetctkllrtdsnksnafGGILSLENLKEIDPTRYQFLQEMQNLllrkqsiefddtisae 2501
Cdd:cd00078 122 --------------------------------------GKPLSLEDLEELDPELYKSLKELLDN---------------- 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583318 2502 kkhelinelklqtqnglEVSLEDLALTFTYLPSSSIYGYTQAELLPNGSSVNVTIDNLEAYCELLMNFILQDGIAQQMKA 2581
Cdd:cd00078 148 -----------------DGDEDDLELTFTIELDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEA 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583318 2582 FSDGFNEVFPLKKLAAFTPSEARMMICGEqfPHWSREDIISYTEPKLGYNKDSPGFQRFVNVLLSMSGDERKAFLQFTTG 2661
Cdd:cd00078 211 FRDGFSEVIPEELLSLFTPEELELLICGS--EDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTG 288
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24583318 2662 CSSLPPGGLANLHPRLTvVRKVDAGVGSYPSVNTCVHYLKLPDYPTEEIMKERLLTATKEK-GFH 2725
Cdd:cd00078 289 SSRLPVGGFADLNPKFT-IRRVGSPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGaGFG 352
|
|
| HECTc |
smart00119 |
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ... |
2289-2724 |
3.79e-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: 291.45 E-value: 3.79e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583318 2289 RKSVLEVEFLDEEG-TGLGPTLEFYALVAAEIQRSDLCMWLCDDDLgedtenstqsaegnskpvgyyvnrreHGIFPAPL 2367
Cdd:smart00119 3 KKRVLEIEFEGEEGlDGGGVTREFFFLLSKELFNPDYGLFRYSPND--------------------------YLLYPNPR 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583318 2368 pqNSEICENVLKYFWFFGVFVAKVLQDMRLVDIPLSTSFLQLLCHNKVlsrnlqkvisdrrngdlsvvsedsdivetctk 2447
Cdd:smart00119 57 --SGFANEEHLSYFRFIGRVLGKALYDNRLLDLFFARPFYKKLLGKPV-------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583318 2448 llrtdsnksnafggilSLENLKEIDPTRYQFLQEMQnlllrkqsIEFDDTisaekkhelinelklqtqnglevslEDLAL 2527
Cdd:smart00119 103 ----------------TLHDLESLDPELYKSLKWLL--------LNNDTS-------------------------EELDL 133
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583318 2528 TFTYLPSSSIYGYTQAELLPNGSSVNVTIDNLEAYCELLMNFILQDGIAQQMKAFSDGFNEVFPLKKLAAFTPSEARMMI 2607
Cdd:smart00119 134 TFSIVLTSEFGQVKVVELKPGGSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLI 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583318 2608 CGEqfPHWSREDIISYTEPKLGYNKDSPGFQRFVNVLLSMSGDERKAFLQFTTGCSSLPPGGLANLHPRLTvVRKVDAGV 2687
Cdd:smart00119 214 CGS--PEIDVDDLKSNTEYKGGYSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSPKFT-IRKAGSDD 290
|
410 420 430
....*....|....*....|....*....|....*...
gi 24583318 2688 GSYPSVNTCVHYLKLPDYPTEEIMKERLLTATKE-KGF 2724
Cdd:smart00119 291 ERLPTAHTCFNRLKLPPYSSKEILREKLLLAINEgKGF 328
|
|
| HECT |
pfam00632 |
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ... |
2314-2726 |
1.18e-80 |
|
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl Terminus.
Pssm-ID: 459880 Cd Length: 304 Bit Score: 269.09 E-value: 1.18e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583318 2314 LVAAEIQRSDLCMWLCDDDlgedtenstqsaegnskpvgyyvnrREHGIFPAPLPQNSEICENvLKYFWFFGVFVAKVLQ 2393
Cdd:pfam00632 2 LLSKELFDPNYGLFEYETE-------------------------DDRTYWFNPSSSESPDLEL-LDYFKFLGKLLGKAIY 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583318 2394 DMRLVDIPLSTSFLQLLCHNKVlsrnlqkvisdrrngdlsvvsedsdivetctkllrtdsnksnafggilSLENLKEIDP 2473
Cdd:pfam00632 56 NGILLDLPFPPFFYKKLLGEPL------------------------------------------------TLEDLESIDP 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583318 2474 TRYQFLQEMQNlllrkqsIEFDDtisaekkhelinelklqtqnglevsLEDLALTFTYlpssSIYGYT-QAELLPNGSSV 2552
Cdd:pfam00632 88 ELYKSLKSLLN-------MDNDD-------------------------DEDLGLTFTI----PVFGESkTIELIPNGRNI 131
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583318 2553 NVTIDNLEAYCELLMNFILQDGIAQQMKAFSDGFNEVFPLKKLAAFTPSEARMMICGEqfPHWSREDIISYTEPKLGYNK 2632
Cdd:pfam00632 132 PVTNENKEEYIRLYVDYRLNKSIEPQLEAFRKGFYSVIPKEALSLFTPEELELLICGS--PEIDVEDLKKNTEYDGGYTK 209
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583318 2633 DSPGFQRFVNVLLSMSGDERKAFLQFTTGCSSLPPGGLANLhPRLTVVRKVDAGVGSYPSVNTCVHYLKLPDYPTEEIMK 2712
Cdd:pfam00632 210 NSPTIQWFWEILEEFSPEQRRLFLKFVTGSSRLPVGGFKSL-PKFTIVRKGGDDDDRLPTAHTCFNRLKLPDYSSKEILK 288
|
410
....*....|....*
gi 24583318 2713 ERLLTATKE-KGFHL 2726
Cdd:pfam00632 289 EKLLIAIEEgEGFGL 303
|
|
| HUL4 |
COG5021 |
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones]; |
2105-2724 |
1.09e-53 |
|
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227354 [Multi-domain] Cd Length: 872 Bit Score: 205.39 E-value: 1.09e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583318 2105 DVSSKSGASTLSPNSPMhigFNVADNNLCSVDDVLELLTQING-----LNQSEIDSDVKEHGVSVLSEDLFISKKITNKL 2179
Cdd:COG5021 346 DDSSSIKDLPHQVGSNP---FLEAHPEFSELLKNQSRGTTRDFrnkptGWSSSIEDLGQFLFSDFLTSSSTYEDLRREQL 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583318 2180 QQQIQDPLVLASNALPNWCEnlnQSCPFLFPFETR---------------QLYFNCTSFGASRSIVCLQSQRDVTVERQR 2244
Cdd:COG5021 423 GRESDESFYVASNVQQQRAS---REGPLLSGWKTRlnnlyrfyfvehrkkTLTKNDSRLGSFISLNKLDIRRIKEDKRRK 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583318 2245 IPIMSPRRDDHEfriGRLKHERVKvprnedllmwamqvmkthcnRKSVLEV---EFLDEEGTGLGPTLEFYALVAAEIQR 2321
Cdd:COG5021 500 LFYSLKQKAKIF---DPYLHIKVR--------------------RDRVFEDsyrEIMDESGDDLKKTLEIEFVGEEGIDA 556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583318 2322 SDLCMWLCdddlgedtenSTQSAEGNSKPVGYYVNRREHgIFPAPLPQNSEICENVLKYFWFFGVFVAKVLQDMRLVDIP 2401
Cdd:COG5021 557 GGLTREWL----------FLLSKEMFNPDYGLFEYITED-LYTLPINPLSSINPEHLSYFKFLGRVIGKAIYDSRILDVQ 625
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583318 2402 LSTSFLQLLCHNKVlsrnlqkvisdrrngdlsvvsedsdivetctkllrtdsnksnafggilSLENLKEIDPTRYQFLQE 2481
Cdd:COG5021 626 FSKAFYKKLLGKPV------------------------------------------------SLVDLESLDPELYRSLVW 657
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583318 2482 MQNLLLRKQSIEfddtisaekkhelinelklqtqngLEVSLEDLALTFTylpsssiygyTQAELLPNGSSVNVTIDNLEA 2561
Cdd:COG5021 658 LLNNDIDETILD------------------------LTFTVEDDSFGES----------RTVELIPNGRNISVTNENKKE 703
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583318 2562 YCELLMNFILQDGIAQQMKAFSDGFNEVFPLKKLAAFTPSEARMMICG--EQFphwSREDIISYTEPKlGYNKDSPGFQR 2639
Cdd:COG5021 704 YVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGipEDI---DIDDWKSNTAYH-GYTEDSPIIVW 779
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583318 2640 FVNVLLSMSGDERKAFLQFTTGCSSLPPGGLANLHPRLTVVRKV--DAGVGSY--PSVNTCVHYLKLPDYPTEEIMKERL 2715
Cdd:COG5021 780 FWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTieKGGTDDDrlPSAHTCFNRLKLPEYSSKEKLRSKL 859
|
650
....*....|
gi 24583318 2716 LTATKE-KGF 2724
Cdd:COG5021 860 LTAINEgAGF 869
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
375-509 |
3.86e-25 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 108.12 E-value: 3.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583318 375 LAPRPRRNNTNTDRTHRQLIDCIRSKDSEALREAIESGgIDVNCMDDVGQTLLNWASAFGTLEMVEYLCEKGADVNK--G 452
Cdd:COG0666 73 LLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAG-ADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAqdN 151
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 24583318 453 QRSSSLHYAACFGRPAIAKILLKFGAYPDLRDEDGKTPLDKARERlddGHREVAAIL 509
Cdd:COG0666 152 DGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAEN---GHLEIVKLL 205
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
393-510 |
4.02e-23 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 102.34 E-value: 4.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583318 393 LIDCIRSKDSEALREAIESGgIDVNCMDDVGQTLLNWASAFGTLEMVEYLCEKGADVNKGQRS--SSLHYAACFGRPAIA 470
Cdd:COG0666 124 LHLAAYNGNLEIVKLLLEAG-ADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDgeTPLHLAAENGHLEIV 202
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 24583318 471 KILLKFGAYPDLRDEDGKTPLDKARERlddGHREVAAILQ 510
Cdd:COG0666 203 KLLLEAGADVNAKDNDGKTALDLAAEN---GNLEIVKLLL 239
|
|
| MIB_HERC2 |
pfam06701 |
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain ... |
1333-1390 |
4.50e-23 |
|
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: 94.59 E-value: 4.50e-23
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24583318 1333 GARVIRGVDWRWEEQDGCAE--GTIT------GEIHNGWIDVKWDHGVRNSYRMGAEGKYDLKLAD 1390
Cdd:pfam06701 1 GARVVRGPDWKWGDQDGGEGhvGTVVeirdwdSESPRSTVRVQWDNGSTNVYRVGYEGKYDLKVVD 66
|
|
| Sad1_UNC |
pfam07738 |
Sad1 / UNC-like C-terminal; The C. elegans UNC-84 protein is a nuclear envelope protein that ... |
1173-1298 |
7.92e-20 |
|
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: 87.73 E-value: 7.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583318 1173 EDILSRDSISLNCHTKDNKKAWFAIDLGVYIIPTAYTLRHARGYGR-SALRNWLLQGSKDGSTWTtlSTHVDDKSLVEPG 1251
Cdd:pfam07738 9 KVILQPDYMPGPCWSFKGSRGFVVIELSEFIIVEAITLEHVEKSVFsSAPKDFEVSGSDRYPTTK--WVLLGEFSYDLDG 86
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 24583318 1252 STA-TWPINCATDDSVWYRHIRIQQNGrnasGQTHYLSLSGFEIYGRV 1298
Cdd:pfam07738 87 KTIqTFQLENPPDIWVKYVKLRILSNY----GNEHYTCLYRFRVHGTV 130
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
393-509 |
4.30e-18 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 87.32 E-value: 4.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583318 393 LIDCIRSKDSEALREAIESGGIDVNCMDDVGQTLLNWASAFGTLEMVEYLCEKGADVNK--GQRSSSLHYAACFGRPAIA 470
Cdd:COG0666 57 LLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNArdKDGETPLHLAAYNGNLEIV 136
|
90 100 110
....*....|....*....|....*....|....*....
gi 24583318 471 KILLKFGAYPDLRDEDGKTPLDKARERlddGHREVAAIL 509
Cdd:COG0666 137 KLLLEAGADVNAQDNDGNTPLHLAAAN---GNLEIVKLL 172
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
393-484 |
3.57e-15 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 72.84 E-value: 3.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583318 393 LIDCIRSKDSEALREAIESGgIDVNCMDDVGQTLLNWASAFGTLEMVEYLCEKGADVNKGQRSSSLHYAACFGRPAIAKI 472
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRTALHYAARSGHLEIVKL 79
|
90
....*....|..
gi 24583318 473 LLKFGAYPDLRD 484
Cdd:pfam12796 80 LLEKGADINVKD 91
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
431-511 |
1.09e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 54.13 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583318 431 SAFGTLEMVEYLCEKGADVN--KGQRSSSLHYAACFGRPAIAKILLKFGAYPDLRDEDGKTPLDKARErldDGHREVAAI 508
Cdd:PTZ00322 90 AASGDAVGARILLTGGADPNcrDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEE---NGFREVVQL 166
|
...
gi 24583318 509 LQS 511
Cdd:PTZ00322 167 LSR 169
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
400-494 |
1.14e-06 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 53.88 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583318 400 KDSEALREAIESGGIDVNCMDDVGQTLLNWASAFGT---LEMVEYLcEKGADVNKGQRS--SSLHYAACFGRPAIAKILL 474
Cdd:PHA03095 199 KPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSckrSLVLPLL-IAGISINARNRYgqTPLHYAAVFNNPRACRRLI 277
|
90 100
....*....|....*....|
gi 24583318 475 KFGAYPDLRDEDGKTPLDKA 494
Cdd:PHA03095 278 ALGADINAVSSDGNTPLSLM 297
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
413-576 |
3.13e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 52.57 E-value: 3.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583318 413 GIDVNCMD-DVGQTLLNWASAFGTLEMVEYLCEKGADVNKGQR--SSSLHYAACFGRPAIAKILLKFGAYPDLRDEDGKT 489
Cdd:PHA02878 157 GADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKtnNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNT 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583318 490 PLDKARERLDDghREVAAIL---------QSPGEWMSPDHSLLNKDGKKYTLMEPRGDPEMAPIYLKVLLPIFCRTFLGS 560
Cdd:PHA02878 237 PLHISVGYCKD--YDILKLLlehgvdvnaKSYILGLTALHSSIKSERKLKLLLEYGADINSLNSYKLTPLSSAVKQYLCI 314
|
170
....*....|....*.
gi 24583318 561 MLGSVRRASLALIKKI 576
Cdd:PHA02878 315 NIGRILISNICLLKRI 330
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
458-509 |
1.03e-05 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 46.26 E-value: 1.03e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 24583318 458 LHYAACFGRPAIAKILLKFGAYPDLRDEDGKTPLDKARERlddGHREVAAIL 509
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKN---GHLEIVKLL 49
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
401-499 |
2.12e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 49.58 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583318 401 DSEALREAIESGgIDVNCMDDVGQTLLNWASAFGTLEMVEYLCEKGADVNKGQRSSS--LHYAACFGRPAIAKILLKFGA 478
Cdd:PHA02874 103 EKDMIKTILDCG-IDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCypIHIAIKHNFFDIIKLLLEKGA 181
|
90 100
....*....|....*....|.
gi 24583318 479 YPDLRDEDGKTPLDKARERLD 499
Cdd:PHA02874 182 YANVKDNNGESPLHNAAEYGD 202
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
382-491 |
2.52e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 49.28 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583318 382 NNTNTDRTHRQLIDCIRSKDSEALREAIESGGIDVNCMDDVGQTLLNWA--SAFGTLEMVEYLCEKGADVNKGQR----- 454
Cdd:PHA03100 100 NAPDNNGITPLLYAISKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYleSNKIDLKILKLLIDKGVDINAKNRvnyll 179
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 24583318 455 -------------SSSLHYAACFGRPAIAKILLKFGAYPDLRDEDGKTPL 491
Cdd:PHA03100 180 sygvpinikdvygFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPL 229
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
452-494 |
6.57e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 42.72 E-value: 6.57e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 24583318 452 GQRSSSLHYAACFGRPAIAKILLKFGAYPDLRDEDGKTPLDKA 494
Cdd:pfam13857 14 GEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
392-492 |
8.05e-05 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 48.10 E-value: 8.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583318 392 QLIDCIRSKDSEALREAIESGgIDVNCMDDVGQTLLNWASAFG-TLEMVEYLCEKGADVNK--GQRSSSLH-YAACFG-R 466
Cdd:PHA03095 53 LYLHYSSEKVKDIVRLLLEAG-ADVNAPERCGFTPLHLYLYNAtTLDVIKLLIKAGADVNAkdKVGRTPLHvYLSGFNiN 131
|
90 100
....*....|....*....|....*.
gi 24583318 467 PAIAKILLKFGAYPDLRDEDGKTPLD 492
Cdd:PHA03095 132 PKVIRLLLRKGADVNALDLYGMTPLA 157
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
436-491 |
2.81e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 44.81 E-value: 2.81e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24583318 436 LEMVEYLCEKGADVN---KGQRSSSLHYAACFGR---PAIAKILLKFGAYPDLRDEDGKTPL 491
Cdd:PHA02859 66 VEILKFLIENGADVNfktRDNNLSALHHYLSFNKnvePEILKILIDSGSSITEEDEDGKNLL 127
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
397-494 |
3.53e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 45.72 E-value: 3.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583318 397 IRSKDSEALREAIESGGiDVNCMDDVGQTLLNWASAFGTLEMVEYLCEKGA--DVNKGQRSSSLHYAACFGRPAIAKILL 474
Cdd:PHA02874 132 IKKGDLESIKMLFEYGA-DVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAyaNVKDNNGESPLHNAAEYGDYACIKLLI 210
|
90 100
....*....|....*....|
gi 24583318 475 KFGAYPDLRDEDGKTPLDKA 494
Cdd:PHA02874 211 DHGNHIMNKCKNGFTPLHNA 230
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
393-442 |
5.48e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 39.95 E-value: 5.48e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 24583318 393 LIDCIRSKDSEALREAIESGgIDVNCMDDVGQTLLNWASAFGTLEMVEYL 442
Cdd:pfam13637 5 LHAAAASGHLELLRLLLEKG-ADINAVDGNGETALHFAASNGNVEVLKLL 53
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
454-509 |
7.15e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 39.57 E-value: 7.15e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 24583318 454 RSSSLHYAACFGRPAIAKILLKFGAYPDLRDEDGKTPLDKARERlddGHREVAAIL 509
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASN---GNVEVLKLL 53
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
425-474 |
8.79e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 39.57 E-value: 8.79e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 24583318 425 TLLNWASAFGTLEMVEYLCEKGADVNK--GQRSSSLHYAACFGRPAIAKILL 474
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAvdGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
423-451 |
9.51e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 38.78 E-value: 9.51e-04
10 20
....*....|....*....|....*....
gi 24583318 423 GQTLLNWASAFGTLEMVEYLCEKGADVNK 451
Cdd:pfam13606 2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
393-491 |
2.35e-03 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 42.63 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583318 393 LIDCIRSKDSEALREAIESGgIDVNCMDDVGQTLLNWASAFGTLEMVEYLCEKGADVNKGQRSSS--LHYAACFGRPAIA 470
Cdd:COG0666 190 LHLAAENGHLEIVKLLLEAG-ADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLtaLLLAAAAGAALIV 268
|
90 100
....*....|....*....|.
gi 24583318 471 KILLKFGAYPDLRDEDGKTPL 491
Cdd:COG0666 269 KLLLLALLLLAAALLDLLTLL 289
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
423-491 |
2.81e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 43.08 E-value: 2.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583318 423 GQTLLNWASAFGTLEMVEYLCEKGADVNKGQRSSS----------------LHYAACFGRPAIAKILLKFGAYPDLRDED 486
Cdd:cd22192 89 GETALHIAVVNQNLNLVRELIARGADVVSPRATGTffrpgpknliyygehpLSFAACVGNEEIVRLLIEHGADIRAQDSL 168
|
....*
gi 24583318 487 GKTPL 491
Cdd:cd22192 169 GNTVL 173
|
|
| F5_F8_type_C |
pfam00754 |
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family. |
1185-1282 |
2.91e-03 |
|
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.
Pssm-ID: 459925 [Multi-domain] Cd Length: 127 Bit Score: 40.12 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583318 1185 CHTKDNKKAWFAIDLG-VYIIpTAYTLRHARGYGRSALRNWLLQGSKDGSTWTTLSTHvDDKSLVEPGSTATWPINCATD 1263
Cdd:pfam00754 27 SAWSGDDPQWIQVDLGkPKKI-TGVVTQGRQDGSNGYVTSYKIEYSLDGENWTTVKDE-KIPGNNDNNTPVTNTFDPPIK 104
|
90
....*....|....*....
gi 24583318 1264 dsvwYRHIRIQQNGRNASG 1282
Cdd:pfam00754 105 ----ARYVRIVPTSWNGGN 119
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
413-491 |
8.94e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 41.16 E-value: 8.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583318 413 GIDVNCMDDVGQT----LLNWASAfgTLEMVEYLCEKGADV--NKGQRSSSLHYAACFGRP--AIAKILLKFGAYPDLRD 484
Cdd:PHA03095 142 GADVNALDLYGMTplavLLKSRNA--NVELLRLLIDAGADVyaVDDRFRSLLHHHLQSFKPraRIVRELIRAGCDPAATD 219
|
....*..
gi 24583318 485 EDGKTPL 491
Cdd:PHA03095 220 MLGNTPL 226
|
|
| |
