|
Name |
Accession |
Description |
Interval |
E-value |
| HECTc |
cd00078 |
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ... |
2219-2646 |
3.83e-123 |
|
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It binds specific ubiquitin-conjugating enzymes (E2), accepts ubiquitin from E2, transfers ubiquitin to substrate lysine side chains, and transfers additional ubiquitin molecules to the end of growing ubiquitin chains.
Pssm-ID: 238033 [Multi-domain] Cd Length: 352 Bit Score: 393.08 E-value: 3.83e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356320 2219 ERVKVTRaeETLLDQAIRLMKFHA--DRKAVLEIEYTNEEGTG-LGPTLEFYALVAAELQRKSLALWVCDDDDTHasksg 2295
Cdd:cd00078 1 LKITVRR--DRILEDALRQLSKVSssDLKKVLEVEFVGEEGIDaGGVTREFFTLVSKELFNPSYGLFRYTPDDSG----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356320 2296 eerevdlgegkkpigyyvrrvgGLFPAPLPPGTDETKraaDMFRVLGVFLAKVLLDGRLVDLPLSRPFLKLLvhpqigdd 2375
Cdd:cd00078 74 ----------------------LLYPNPSSFADEDHL---KLFRFLGRLLGKALYEGRLLDLPFSRAFYKKL-------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356320 2376 argpnLHKILSLDDFEEVNPVKGSFLKELRALAQRkrliendtsidsnskrrkiaelklhikgstcrVEDLALNFTVNPP 2455
Cdd:cd00078 121 -----LGKPLSLEDLEELDPELYKSLKELLDNDGD--------------------------------EDDLELTFTIELD 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356320 2456 SKVFQYAEMELVDGGSDIDVTIDNVEQYVEKCEEFYLNTGIAYQMRAFRDGFDRVFPLRTLRAYSPEEVQRLLSGEqcPE 2535
Cdd:cd00078 164 SSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGS--ED 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356320 2536 WSRDDILNYTEPKLGYTRESPGFLRFVDVMEALTAQERKNFLQFATGCSSLPPGGLANLHPRLTIvRKVESGDGSYPSVN 2615
Cdd:cd00078 242 IDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLNPKFTI-RRVGSPDDRLPTAH 320
|
410 420 430
....*....|....*....|....*....|..
gi 808356320 2616 TCVHYLKLPEYSSSAILRERLLTAINEK-GFH 2646
Cdd:cd00078 321 TCFNLLKLPPYSSKEILREKLLYAINEGaGFG 352
|
|
| HECTc |
smart00119 |
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ... |
2244-2645 |
4.08e-120 |
|
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to E2 enzymes.
Pssm-ID: 214523 Cd Length: 328 Bit Score: 383.12 E-value: 4.08e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356320 2244 RKAVLEIEYTNEEG-TGLGPTLEFYALVAAELQRKSLALWVCDDDDTHasksgeerevdlgegkkpigyyvrrvggLFPA 2322
Cdd:smart00119 3 KKRVLEIEFEGEEGlDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYL----------------------------LYPN 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356320 2323 PLPPGTDETKRAadMFRVLGVFLAKVLLDGRLVDLPLSRPFLKLLvhpqigddargpnLHKILSLDDFEEVNPVKGSFLK 2402
Cdd:smart00119 55 PRSGFANEEHLS--YFRFIGRVLGKALYDNRLLDLFFARPFYKKL-------------LGKPVTLHDLESLDPELYKSLK 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356320 2403 ELralaqrkrLIENDTSidsnskrrkiaelklhikgstcrvEDLALNFTVNPPSKVFQYAEMELVDGGSDIDVTIDNVEQ 2482
Cdd:smart00119 120 WL--------LLNNDTS------------------------EELDLTFSIVLTSEFGQVKVVELKPGGSNIPVTEENKKE 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356320 2483 YVEKCEEFYLNTGIAYQMRAFRDGFDRVFPLRTLRAYSPEEVQRLLSGeqCPEWSRDDILNYTEPKLGYTRESPGFLRFV 2562
Cdd:smart00119 168 YVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICG--SPEIDVDDLKSNTEYKGGYSANSQTIKWFW 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356320 2563 DVMEALTAQERKNFLQFATGCSSLPPGGLANLHPRLTIVRKVESgDGSYPSVNTCVHYLKLPEYSSSAILRERLLTAINE 2642
Cdd:smart00119 246 EVVESFTNEERRKLLQFVTGSSRLPVGGFAALSPKFTIRKAGSD-DERLPTAHTCFNRLKLPPYSSKEILREKLLLAINE 324
|
....
gi 808356320 2643 -KGF 2645
Cdd:smart00119 325 gKGF 328
|
|
| HECT |
pfam00632 |
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ... |
2269-2647 |
2.33e-84 |
|
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl Terminus.
Pssm-ID: 459880 Cd Length: 304 Bit Score: 279.50 E-value: 2.33e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356320 2269 LVAAELQRKSLALWVCDDDDTHasksgeerevdlgegkkpigyyvrrvggLFPAPLPPGTDETKRAADMFRVLGVFLAKV 2348
Cdd:pfam00632 2 LLSKELFDPNYGLFEYETEDDR----------------------------TYWFNPSSSESPDLELLDYFKFLGKLLGKA 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356320 2349 LLDGRLVDLPLSRPFLKLLvhpqigddargpnLHKILSLDDFEEVNPVKGSFLKELRalaqrkrLIENDTsidsnskrrk 2428
Cdd:pfam00632 54 IYNGILLDLPFPPFFYKKL-------------LGEPLTLEDLESIDPELYKSLKSLL-------NMDNDD---------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356320 2429 iaelklhikgstcrVEDLALNFTVNppskVFQYAEM-ELVDGGSDIDVTIDNVEQYVEKCEEFYLNTGIAYQMRAFRDGF 2507
Cdd:pfam00632 104 --------------DEDLGLTFTIP----VFGESKTiELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQLEAFRKGF 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356320 2508 DRVFPLRTLRAYSPEEVQRLLSGEqcPEWSRDDILNYTEPKLGYTRESPGFLRFVDVMEALTAQERKNFLQFATGCSSLP 2587
Cdd:pfam00632 166 YSVIPKEALSLFTPEELELLICGS--PEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGSSRLP 243
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 808356320 2588 PGGLANLhPRLTIVRKVESGDGSYPSVNTCVHYLKLPEYSSSAILRERLLTAINE-KGFHL 2647
Cdd:pfam00632 244 VGGFKSL-PKFTIVRKGGDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEgEGFGL 303
|
|
| HUL4 |
COG5021 |
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones]; |
2117-2645 |
2.97e-56 |
|
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227354 [Multi-domain] Cd Length: 872 Bit Score: 213.09 E-value: 2.97e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356320 2117 FISDKLTLKVTQVLSDALVVAARSLPEWCSRlvyKYPCLFTVETRNMYMQATAFGVSRTIV--WLQQRRDAAVERargsa 2194
Cdd:COG5021 413 TYEDLRREQLGRESDESFYVASNVQQQRASR---EGPLLSGWKTRLNNLYRFYFVEHRKKTltKNDSRLGSFISL----- 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356320 2195 qagNSSAARQHDRYHEYRVGRLRHE---------RVKVTRaeETLLDQAIRLMKFHA--DRKAVLEIEYTNEEG-TGLGP 2262
Cdd:COG5021 485 ---NKLDIRRIKEDKRRKLFYSLKQkakifdpylHIKVRR--DRVFEDSYREIMDESgdDLKKTLEIEFVGEEGiDAGGL 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356320 2263 TLEFYALVAAELQrkslalwvcDDDDTHAsksgEEREVDLgegkkpigYYvrrvgglFPAPLPPGTDETKRaaDMFRVLG 2342
Cdd:COG5021 560 TREWLFLLSKEMF---------NPDYGLF----EYITEDL--------YT-------LPINPLSSINPEHL--SYFKFLG 609
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356320 2343 VFLAKVLLDGRLVDLPLSRPFLKLLvhpqigddargpnLHKILSLDDFEEVNPVKGSFLKELRalaqrkrlienDTSIDS 2422
Cdd:COG5021 610 RVIGKAIYDSRILDVQFSKAFYKKL-------------LGKPVSLVDLESLDPELYRSLVWLL-----------NNDIDE 665
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356320 2423 NskrrkiaelklhIKGSTCRVEDLALNFTVNppskvfqyaeMELVDGGSDIDVTIDNVEQYVEKCEEFYLNTGIAYQMRA 2502
Cdd:COG5021 666 T------------ILDLTFTVEDDSFGESRT----------VELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSA 723
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356320 2503 FRDGFDRVFPLRTLRAYSPEEVQRLLSGEqcPEWSR-DDILNYTEPKlGYTRESPGFLRFVDVMEALTAQERKNFLQFAT 2581
Cdd:COG5021 724 FKSGFSEIIPPDLLQIFDESELELLIGGI--PEDIDiDDWKSNTAYH-GYTEDSPIIVWFWEIISEFDFEERAKLLQFVT 800
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 808356320 2582 GCSSLPPGGLANLHPRLTIVRKV--ESGDGSY--PSVNTCVHYLKLPEYSSSAILRERLLTAINE-KGF 2645
Cdd:COG5021 801 GTSRIPINGFKDLQGSDGVRKFTieKGGTDDDrlPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEgAGF 869
|
|
| MIB_HERC2 |
pfam06701 |
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain ... |
1450-1507 |
4.52e-24 |
|
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain (either Ring or Hect).
Pssm-ID: 461991 Cd Length: 66 Bit Score: 97.29 E-value: 4.52e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 808356320 1450 SKVVRGKDWRWEDQDGGEGKFGRIT------SPPESGWVDVTWDNGNANSYRFGANGNFDIERV 1507
Cdd:pfam06701 2 ARVVRGPDWKWGDQDGGEGHVGTVVeirdwdSESPRSTVRVQWDNGSTNVYRVGYEGKYDLKVV 65
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
237-453 |
8.05e-23 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 101.18 E-value: 8.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356320 237 LISIMVASNDENSPTTASANILSIVLSLIGNLCRGSSLITEKVLTSPNMITGLKATLTNKEERVVTDGLRFCDLLLVLLC 316
Cdd:COG0666 6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356320 317 EGRSALpltsvvsgDYAAGSGAERVHRQLIDA---IRQKDL---TALVDAIESGQV-----------DVNFADDVGQSLT 379
Cdd:COG0666 86 GGNTLL--------HAAARNGDLEIVKLLLEAgadVNARDKdgeTPLHLAAYNGNLeivkllleagaDVNAQDNDGNTPL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 808356320 380 NWASAFGSIEMVQYLCDKGSDVNK--GHKSSSLHYAACFGRPDVVKLLLQRGANPDLRDEDGKTALDKARERSDDD 453
Cdd:COG0666 158 HLAAANGNLEIVKLLLEAGADVNArdNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLE 233
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
345-436 |
3.42e-14 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 70.14 E-value: 3.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356320 345 LIDAIRQKDLTALVDAIESGqVDVNFADDVGQSLTNWASAFGSIEMVQYLCDKGSDVNKGHKSSSLHYAACFGRPDVVKL 424
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRTALHYAARSGHLEIVKL 79
|
90
....*....|..
gi 808356320 425 LLQRGANPDLRD 436
Cdd:pfam12796 80 LLEKGADINVKD 91
|
|
| Sad1_UNC |
pfam07738 |
Sad1 / UNC-like C-terminal; The C. elegans UNC-84 protein is a nuclear envelope protein that ... |
1241-1363 |
9.13e-14 |
|
Sad1 / UNC-like C-terminal; The C. elegans UNC-84 protein is a nuclear envelope protein that is involved in nuclear anchoring and migration during development. The S. pombe Sad1 protein localizes at the spindle pole body. UNC-84 and and Sad1 share a common C-terminal region, that is often termed the SUN (Sad1 and UNC) domain. In mammals, the SUN domain is present in two proteins, Sun1 and Sun2. The SUN domain of Sun2 has been demonstrated to be in the periplasm.
Pssm-ID: 400199 Cd Length: 130 Bit Score: 70.40 E-value: 9.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356320 1241 PEDLLSRDQNPINCHTSDDKNAHFTIDLGLFVVPTSYSLRHSRGYGR-SALRNWMLQGSVDAKRWENVIVhtDDKGLGEP 1319
Cdd:pfam07738 8 PKVILQPDYMPGPCWSFKGSRGFVVIELSEFIIVEAITLEHVEKSVFsSAPKDFEVSGSDRYPTTKWVLL--GEFSYDLD 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 808356320 1320 GSTA-TWHVGEKGTTAFRF--FRIAQNGknssGQTHYLSCSGFEIYG 1363
Cdd:pfam07738 86 GKTIqTFQLENPPDIWVKYvkLRILSNY----GNEHYTCLYRFRVHG 128
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
391-443 |
1.47e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 50.05 E-value: 1.47e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 808356320 391 VQYLCDKGSDVN----KGhkSSSLHYAACFGRPDVVKLLLQRGANPDLRDEDGKTAL 443
Cdd:PHA03100 175 VNYLLSYGVPINikdvYG--FTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPL 229
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
405-434 |
1.36e-04 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 41.03 E-value: 1.36e-04
10 20 30
....*....|....*....|....*....|
gi 808356320 405 HKSSSLHYAACFGRPDVVKLLLQRGANPDL 434
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
375-443 |
1.01e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 44.62 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356320 375 GQSLTNWASAFGSIEMVQYLCDKGSDVNKG---------HKSSSLHY-------AACFGRPDVVKLLLQRGANPDLRDED 438
Cdd:cd22192 89 GETALHIAVVNQNLNLVRELIARGADVVSPratgtffrpGPKNLIYYgehplsfAACVGNEEIVRLLIEHGADIRAQDSL 168
|
....*
gi 808356320 439 GKTAL 443
Cdd:cd22192 169 GNTVL 173
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| HECTc |
cd00078 |
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ... |
2219-2646 |
3.83e-123 |
|
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It binds specific ubiquitin-conjugating enzymes (E2), accepts ubiquitin from E2, transfers ubiquitin to substrate lysine side chains, and transfers additional ubiquitin molecules to the end of growing ubiquitin chains.
Pssm-ID: 238033 [Multi-domain] Cd Length: 352 Bit Score: 393.08 E-value: 3.83e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356320 2219 ERVKVTRaeETLLDQAIRLMKFHA--DRKAVLEIEYTNEEGTG-LGPTLEFYALVAAELQRKSLALWVCDDDDTHasksg 2295
Cdd:cd00078 1 LKITVRR--DRILEDALRQLSKVSssDLKKVLEVEFVGEEGIDaGGVTREFFTLVSKELFNPSYGLFRYTPDDSG----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356320 2296 eerevdlgegkkpigyyvrrvgGLFPAPLPPGTDETKraaDMFRVLGVFLAKVLLDGRLVDLPLSRPFLKLLvhpqigdd 2375
Cdd:cd00078 74 ----------------------LLYPNPSSFADEDHL---KLFRFLGRLLGKALYEGRLLDLPFSRAFYKKL-------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356320 2376 argpnLHKILSLDDFEEVNPVKGSFLKELRALAQRkrliendtsidsnskrrkiaelklhikgstcrVEDLALNFTVNPP 2455
Cdd:cd00078 121 -----LGKPLSLEDLEELDPELYKSLKELLDNDGD--------------------------------EDDLELTFTIELD 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356320 2456 SKVFQYAEMELVDGGSDIDVTIDNVEQYVEKCEEFYLNTGIAYQMRAFRDGFDRVFPLRTLRAYSPEEVQRLLSGEqcPE 2535
Cdd:cd00078 164 SSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGS--ED 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356320 2536 WSRDDILNYTEPKLGYTRESPGFLRFVDVMEALTAQERKNFLQFATGCSSLPPGGLANLHPRLTIvRKVESGDGSYPSVN 2615
Cdd:cd00078 242 IDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLNPKFTI-RRVGSPDDRLPTAH 320
|
410 420 430
....*....|....*....|....*....|..
gi 808356320 2616 TCVHYLKLPEYSSSAILRERLLTAINEK-GFH 2646
Cdd:cd00078 321 TCFNLLKLPPYSSKEILREKLLYAINEGaGFG 352
|
|
| HECTc |
smart00119 |
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ... |
2244-2645 |
4.08e-120 |
|
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to E2 enzymes.
Pssm-ID: 214523 Cd Length: 328 Bit Score: 383.12 E-value: 4.08e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356320 2244 RKAVLEIEYTNEEG-TGLGPTLEFYALVAAELQRKSLALWVCDDDDTHasksgeerevdlgegkkpigyyvrrvggLFPA 2322
Cdd:smart00119 3 KKRVLEIEFEGEEGlDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYL----------------------------LYPN 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356320 2323 PLPPGTDETKRAadMFRVLGVFLAKVLLDGRLVDLPLSRPFLKLLvhpqigddargpnLHKILSLDDFEEVNPVKGSFLK 2402
Cdd:smart00119 55 PRSGFANEEHLS--YFRFIGRVLGKALYDNRLLDLFFARPFYKKL-------------LGKPVTLHDLESLDPELYKSLK 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356320 2403 ELralaqrkrLIENDTSidsnskrrkiaelklhikgstcrvEDLALNFTVNPPSKVFQYAEMELVDGGSDIDVTIDNVEQ 2482
Cdd:smart00119 120 WL--------LLNNDTS------------------------EELDLTFSIVLTSEFGQVKVVELKPGGSNIPVTEENKKE 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356320 2483 YVEKCEEFYLNTGIAYQMRAFRDGFDRVFPLRTLRAYSPEEVQRLLSGeqCPEWSRDDILNYTEPKLGYTRESPGFLRFV 2562
Cdd:smart00119 168 YVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICG--SPEIDVDDLKSNTEYKGGYSANSQTIKWFW 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356320 2563 DVMEALTAQERKNFLQFATGCSSLPPGGLANLHPRLTIVRKVESgDGSYPSVNTCVHYLKLPEYSSSAILRERLLTAINE 2642
Cdd:smart00119 246 EVVESFTNEERRKLLQFVTGSSRLPVGGFAALSPKFTIRKAGSD-DERLPTAHTCFNRLKLPPYSSKEILREKLLLAINE 324
|
....
gi 808356320 2643 -KGF 2645
Cdd:smart00119 325 gKGF 328
|
|
| HECT |
pfam00632 |
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ... |
2269-2647 |
2.33e-84 |
|
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl Terminus.
Pssm-ID: 459880 Cd Length: 304 Bit Score: 279.50 E-value: 2.33e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356320 2269 LVAAELQRKSLALWVCDDDDTHasksgeerevdlgegkkpigyyvrrvggLFPAPLPPGTDETKRAADMFRVLGVFLAKV 2348
Cdd:pfam00632 2 LLSKELFDPNYGLFEYETEDDR----------------------------TYWFNPSSSESPDLELLDYFKFLGKLLGKA 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356320 2349 LLDGRLVDLPLSRPFLKLLvhpqigddargpnLHKILSLDDFEEVNPVKGSFLKELRalaqrkrLIENDTsidsnskrrk 2428
Cdd:pfam00632 54 IYNGILLDLPFPPFFYKKL-------------LGEPLTLEDLESIDPELYKSLKSLL-------NMDNDD---------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356320 2429 iaelklhikgstcrVEDLALNFTVNppskVFQYAEM-ELVDGGSDIDVTIDNVEQYVEKCEEFYLNTGIAYQMRAFRDGF 2507
Cdd:pfam00632 104 --------------DEDLGLTFTIP----VFGESKTiELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQLEAFRKGF 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356320 2508 DRVFPLRTLRAYSPEEVQRLLSGEqcPEWSRDDILNYTEPKLGYTRESPGFLRFVDVMEALTAQERKNFLQFATGCSSLP 2587
Cdd:pfam00632 166 YSVIPKEALSLFTPEELELLICGS--PEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGSSRLP 243
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 808356320 2588 PGGLANLhPRLTIVRKVESGDGSYPSVNTCVHYLKLPEYSSSAILRERLLTAINE-KGFHL 2647
Cdd:pfam00632 244 VGGFKSL-PKFTIVRKGGDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEgEGFGL 303
|
|
| HUL4 |
COG5021 |
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones]; |
2117-2645 |
2.97e-56 |
|
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227354 [Multi-domain] Cd Length: 872 Bit Score: 213.09 E-value: 2.97e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356320 2117 FISDKLTLKVTQVLSDALVVAARSLPEWCSRlvyKYPCLFTVETRNMYMQATAFGVSRTIV--WLQQRRDAAVERargsa 2194
Cdd:COG5021 413 TYEDLRREQLGRESDESFYVASNVQQQRASR---EGPLLSGWKTRLNNLYRFYFVEHRKKTltKNDSRLGSFISL----- 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356320 2195 qagNSSAARQHDRYHEYRVGRLRHE---------RVKVTRaeETLLDQAIRLMKFHA--DRKAVLEIEYTNEEG-TGLGP 2262
Cdd:COG5021 485 ---NKLDIRRIKEDKRRKLFYSLKQkakifdpylHIKVRR--DRVFEDSYREIMDESgdDLKKTLEIEFVGEEGiDAGGL 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356320 2263 TLEFYALVAAELQrkslalwvcDDDDTHAsksgEEREVDLgegkkpigYYvrrvgglFPAPLPPGTDETKRaaDMFRVLG 2342
Cdd:COG5021 560 TREWLFLLSKEMF---------NPDYGLF----EYITEDL--------YT-------LPINPLSSINPEHL--SYFKFLG 609
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356320 2343 VFLAKVLLDGRLVDLPLSRPFLKLLvhpqigddargpnLHKILSLDDFEEVNPVKGSFLKELRalaqrkrlienDTSIDS 2422
Cdd:COG5021 610 RVIGKAIYDSRILDVQFSKAFYKKL-------------LGKPVSLVDLESLDPELYRSLVWLL-----------NNDIDE 665
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356320 2423 NskrrkiaelklhIKGSTCRVEDLALNFTVNppskvfqyaeMELVDGGSDIDVTIDNVEQYVEKCEEFYLNTGIAYQMRA 2502
Cdd:COG5021 666 T------------ILDLTFTVEDDSFGESRT----------VELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSA 723
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356320 2503 FRDGFDRVFPLRTLRAYSPEEVQRLLSGEqcPEWSR-DDILNYTEPKlGYTRESPGFLRFVDVMEALTAQERKNFLQFAT 2581
Cdd:COG5021 724 FKSGFSEIIPPDLLQIFDESELELLIGGI--PEDIDiDDWKSNTAYH-GYTEDSPIIVWFWEIISEFDFEERAKLLQFVT 800
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 808356320 2582 GCSSLPPGGLANLHPRLTIVRKV--ESGDGSY--PSVNTCVHYLKLPEYSSSAILRERLLTAINE-KGF 2645
Cdd:COG5021 801 GTSRIPINGFKDLQGSDGVRKFTieKGGTDDDrlPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEgAGF 869
|
|
| MIB_HERC2 |
pfam06701 |
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain ... |
1450-1507 |
4.52e-24 |
|
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain (either Ring or Hect).
Pssm-ID: 461991 Cd Length: 66 Bit Score: 97.29 E-value: 4.52e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 808356320 1450 SKVVRGKDWRWEDQDGGEGKFGRIT------SPPESGWVDVTWDNGNANSYRFGANGNFDIERV 1507
Cdd:pfam06701 2 ARVVRGPDWKWGDQDGGEGHVGTVVeirdwdSESPRSTVRVQWDNGSTNVYRVGYEGKYDLKVV 65
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
237-453 |
8.05e-23 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 101.18 E-value: 8.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356320 237 LISIMVASNDENSPTTASANILSIVLSLIGNLCRGSSLITEKVLTSPNMITGLKATLTNKEERVVTDGLRFCDLLLVLLC 316
Cdd:COG0666 6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356320 317 EGRSALpltsvvsgDYAAGSGAERVHRQLIDA---IRQKDL---TALVDAIESGQV-----------DVNFADDVGQSLT 379
Cdd:COG0666 86 GGNTLL--------HAAARNGDLEIVKLLLEAgadVNARDKdgeTPLHLAAYNGNLeivkllleagaDVNAQDNDGNTPL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 808356320 380 NWASAFGSIEMVQYLCDKGSDVNK--GHKSSSLHYAACFGRPDVVKLLLQRGANPDLRDEDGKTALDKARERSDDD 453
Cdd:COG0666 158 HLAAANGNLEIVKLLLEAGADVNArdNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLE 233
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
345-436 |
3.42e-14 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 70.14 E-value: 3.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356320 345 LIDAIRQKDLTALVDAIESGqVDVNFADDVGQSLTNWASAFGSIEMVQYLCDKGSDVNKGHKSSSLHYAACFGRPDVVKL 424
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRTALHYAARSGHLEIVKL 79
|
90
....*....|..
gi 808356320 425 LLQRGANPDLRD 436
Cdd:pfam12796 80 LLEKGADINVKD 91
|
|
| Sad1_UNC |
pfam07738 |
Sad1 / UNC-like C-terminal; The C. elegans UNC-84 protein is a nuclear envelope protein that ... |
1241-1363 |
9.13e-14 |
|
Sad1 / UNC-like C-terminal; The C. elegans UNC-84 protein is a nuclear envelope protein that is involved in nuclear anchoring and migration during development. The S. pombe Sad1 protein localizes at the spindle pole body. UNC-84 and and Sad1 share a common C-terminal region, that is often termed the SUN (Sad1 and UNC) domain. In mammals, the SUN domain is present in two proteins, Sun1 and Sun2. The SUN domain of Sun2 has been demonstrated to be in the periplasm.
Pssm-ID: 400199 Cd Length: 130 Bit Score: 70.40 E-value: 9.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356320 1241 PEDLLSRDQNPINCHTSDDKNAHFTIDLGLFVVPTSYSLRHSRGYGR-SALRNWMLQGSVDAKRWENVIVhtDDKGLGEP 1319
Cdd:pfam07738 8 PKVILQPDYMPGPCWSFKGSRGFVVIELSEFIIVEAITLEHVEKSVFsSAPKDFEVSGSDRYPTTKWVLL--GEFSYDLD 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 808356320 1320 GSTA-TWHVGEKGTTAFRF--FRIAQNGknssGQTHYLSCSGFEIYG 1363
Cdd:pfam07738 86 GKTIqTFQLENPPDIWVKYvkLRILSNY----GNEHYTCLYRFRVHG 128
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
332-461 |
7.76e-13 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 71.52 E-value: 7.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356320 332 YAAGSGAERVHRQLI------DAIRQKDLTALVDAIESGQV-----------DVNFADDVGQSLTNWASAFGSIEMVQYL 394
Cdd:COG0666 126 LAAYNGNLEIVKLLLeagadvNAQDNDGNTPLHLAAANGNLeivkllleagaDVNARDNDGETPLHLAAENGHLEIVKLL 205
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 808356320 395 CDKGSDVNK--GHKSSSLHYAACFGRPDVVKLLLQRGANPDLRDEDGKTALDKARERSDDDHNQVANIL 461
Cdd:COG0666 206 LEAGADVNAkdNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLA 274
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
410-443 |
1.07e-06 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 48.96 E-value: 1.07e-06
10 20 30
....*....|....*....|....*....|....
gi 808356320 410 LHYAACFGRPDVVKLLLQRGANPDLRDEDGKTAL 443
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTAL 34
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
404-446 |
1.26e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 47.34 E-value: 1.26e-06
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 808356320 404 GHKSSSLHYAACFGRPDVVKLLLQRGANPDLRDEDGKTALDKA 446
Cdd:pfam13857 14 GEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
407-446 |
3.28e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 46.11 E-value: 3.28e-06
10 20 30 40
....*....|....*....|....*....|....*....|
gi 808356320 407 SSSLHYAACFGRPDVVKLLLQRGANPDLRDEDGKTALDKA 446
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFA 41
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
391-443 |
1.47e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 50.05 E-value: 1.47e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 808356320 391 VQYLCDKGSDVN----KGhkSSSLHYAACFGRPDVVKLLLQRGANPDLRDEDGKTAL 443
Cdd:PHA03100 175 VNYLLSYGVPINikdvYG--FTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPL 229
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
410-437 |
3.52e-05 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 42.66 E-value: 3.52e-05
10 20
....*....|....*....|....*....
gi 808356320 410 LHYAAC-FGRPDVVKLLLQRGANPDLRDE 437
Cdd:pfam00023 6 LHLAAGrRGNLEIVKLLLSKGADVNARDK 34
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
352-446 |
4.95e-05 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 48.48 E-value: 4.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356320 352 KDLTALVDAIESGQVDVNFADDVGQSLTNWASAFGS---IEMVQYLcDKGSDVNKGHKS--SSLHYAACFGRPDVVKLLL 426
Cdd:PHA03095 199 KPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSckrSLVLPLL-IAGISINARNRYgqTPLHYAAVFNNPRACRRLI 277
|
90 100
....*....|....*....|
gi 808356320 427 QRGANPDLRDEDGKTALDKA 446
Cdd:PHA03095 278 ALGADINAVSSDGNTPLSLM 297
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
383-497 |
5.79e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 48.74 E-value: 5.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356320 383 SAFGSIEMVQYLCDKGSDVN--KGHKSSSLHYAACFGRPDVVKLLLQRGANPDLRDEDGKTALDKARErsdDDHNQVANI 460
Cdd:PTZ00322 90 AASGDAVGARILLTGGADPNcrDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEE---NGFREVVQL 166
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 808356320 461 LESPSAFMRNKEDPKVKASTSKQPG-------TSTKPE---LPNPNL 497
Cdd:PTZ00322 167 LSRHSQCHFELGANAKPDSFTGKPPsledspiSSHHPDfsaVPQPMM 213
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
405-434 |
1.36e-04 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 41.03 E-value: 1.36e-04
10 20 30
....*....|....*....|....*....|
gi 808356320 405 HKSSSLHYAACFGRPDVVKLLLQRGANPDL 434
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
388-444 |
1.46e-04 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 46.94 E-value: 1.46e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 808356320 388 IEMVQYLCDKGSDVNKGHKS--SSLH-YAACFG-RPDVVKLLLQRGANPDLRDEDGKTALD 444
Cdd:PHA03095 97 LDVIKLLIKAGADVNAKDKVgrTPLHvYLSGFNiNPKVIRLLLRKGADVNALDLYGMTPLA 157
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
387-443 |
2.91e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 44.42 E-value: 2.91e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 808356320 387 SIEMVQYLCDKGSDVN---KGHKSSSLHYAACFGR---PDVVKLLLQRGANPDLRDEDGKTAL 443
Cdd:PHA02859 65 NVEILKFLIENGADVNfktRDNNLSALHHYLSFNKnvePEILKILIDSGSSITEEDEDGKNLL 127
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
348-446 |
3.58e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 45.72 E-value: 3.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356320 348 AIRQKDLTALVDAIESGqVDVNFADDVGQSLTNWASAFGSIEMVQYLCDKGS--DVNKGHKSSSLHYAACFGRPDVVKLL 425
Cdd:PHA02874 131 AIKKGDLESIKMLFEYG-ADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAyaNVKDNNGESPLHNAAEYGDYACIKLL 209
|
90 100
....*....|....*....|.
gi 808356320 426 LQRGANPDLRDEDGKTALDKA 446
Cdd:PHA02874 210 IDHGNHIMNKCKNGFTPLHNA 230
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
381-426 |
4.73e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 40.34 E-value: 4.73e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 808356320 381 WASAFGSIEMVQYLCDKGSDVNK--GHKSSSLHYAACFGRPDVVKLLL 426
Cdd:pfam13637 7 AAAASGHLELLRLLLEKGADINAvdGNGETALHFAASNGNVEVLKLLL 54
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
375-443 |
1.01e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 44.62 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356320 375 GQSLTNWASAFGSIEMVQYLCDKGSDVNKG---------HKSSSLHY-------AACFGRPDVVKLLLQRGANPDLRDED 438
Cdd:cd22192 89 GETALHIAVVNQNLNLVRELIARGADVVSPratgtffrpGPKNLIYYgehplsfAACVGNEEIVRLLIEHGADIRAQDSL 168
|
....*
gi 808356320 439 GKTAL 443
Cdd:cd22192 169 GNTVL 173
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
408-433 |
2.86e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 37.24 E-value: 2.86e-03
10 20
....*....|....*....|....*.
gi 808356320 408 SSLHYAACFGRPDVVKLLLQRGANPD 433
Cdd:pfam13606 4 TPLHLAARNGRLEIVKLLLENGADIN 29
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| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
367-443 |
3.95e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 42.56 E-value: 3.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356320 367 DVNFAD-DVGQSLTNWASAFGSIEMVQYLCDKGSDVNKGHK--SSSLHYAACFGRPDVVKLLLQRGANPDLRDEDGKTAL 443
Cdd:PHA02878 159 DINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKtnNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPL 238
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| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
375-483 |
4.33e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411978 [Multi-domain] Cd Length: 680 Bit Score: 42.44 E-value: 4.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356320 375 GQSLTNWASAFGSIEMVQYLCDKGSDVN---KG------HKSSSLHY-------AACFGRPDVVKLLLQRGANP-DLRDE 437
Cdd:cd22194 141 GQTALNIAIERRQGDIVKLLIAKGADVNahaKGvffnpkYKHEGFYFgetplalAACTNQPEIVQLLMEKESTDiTSQDS 220
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90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 808356320 438 DGKTALDKARERSDDDHNQVANILESPSAFMRNKEDPKVKASTSKQ 483
Cdd:cd22194 221 RGNTVLHALVTVAEDSKTQNDFVKRMYDMILLKSENKNLETIRNNE 266
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