|
Name |
Accession |
Description |
Interval |
E-value |
| PGG |
pfam13962 |
Domain of unknown function; The PGG domain is named for the highly conserved sequence motif ... |
428-533 |
3.94e-36 |
|
Domain of unknown function; The PGG domain is named for the highly conserved sequence motif found at the startt of the domain. The function is not known.
Pssm-ID: 433609 Cd Length: 114 Bit Score: 131.14 E-value: 3.94e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 428 GINNATNSVTVVAVLFATVAFAAIFTVPGG---DDDH---GVAVMVHATSFKIFFIFNAIALFTSLAVVVVQITLVRGET 501
Cdd:pfam13962 3 WLKEARNTLLLVATLIATVTFAAGFTPPGGywqDDDGphaGKPILAKNPAFKAFVISNAIAFFASLVAVVLLLSIVSDFL 82
|
90 100 110
....*....|....*....|....*....|..
gi 240255309 502 KTERRVVEVINKLMWLASVCTTVAFISSSYIV 533
Cdd:pfam13962 83 RSLPRKLRIGLKLLWVALLSMLVAFAAGSYRV 114
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
91-383 |
3.07e-30 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 120.44 E-value: 3.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 91 ELHLAAQRGDLASVKQILSDIDSQITGTITGADFDDEVAQIMTSVVNEVNELGETPLFTAAEKGNIDVVKELLPYttIES 170
Cdd:COG0666 2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAA--GAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 171 LMQKNLSGFDALHIACSQGHRSIVQLLLEHEPQLsKTVAQSNATPLVSAATRGHSEVVNELLAKDSSLlEISRSNGKNAL 250
Cdd:COG0666 80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGADV-NARDKDGETPLHLAAYNGNLEIVKLLLEAGADV-NAQDNDGNTPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 251 HLAARQGHVDIVRTLLDKDPQLARRtDKKGQTSLHMAVKGVSSQVVRLLLRADpAIVMLPDKFGNTVLHIATRKKRAEIV 330
Cdd:COG0666 158 HLAAANGNLEIVKLLLEAGADVNAR-DNDGETPLHLAAENGHLEIVKLLLEAG-ADVNAKDNDGKTALDLAAENGNLEIV 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 240255309 331 NELLQLPDtNVNALTRDHKTAYDIAEGLTHSEETAEIKEILSRCGALKANELN 383
Cdd:COG0666 236 KLLLEAGA-DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
182-269 |
8.21e-17 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 75.92 E-value: 8.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 182 LHIACSQGHRSIVQLLLEHEPQLsKTVAQSNATPLVSAATRGHSEVVNELLAKDSSLLeisRSNGKNALHLAARQGHVDI 261
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADA-NLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL---KDNGRTALHYAARSGHLEI 76
|
....*...
gi 240255309 262 VRTLLDKD 269
Cdd:pfam12796 77 VKLLLEKG 84
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
145-335 |
3.42e-16 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 81.25 E-value: 3.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 145 TPLFTAAEKGNIDVVKELLpYTTIeSLMQKNLSGFDALHIACSQGH-----RSIVQLLLEHEPQLSKTVAQSNaTPLVSA 219
Cdd:PHA03100 37 LPLYLAKEARNIDVVKILL-DNGA-DINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGI-TPLLYA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 220 ATR--GHSEVVNELLAKDSSLlEISRSNGKNALHLAARQGHVD--IVRTLLDK--DPQLARR-------------TDKKG 280
Cdd:PHA03100 114 ISKksNSYSIVEYLLDNGANV-NIKNSDGENLLHLYLESNKIDlkILKLLIDKgvDINAKNRvnyllsygvpiniKDVYG 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 240255309 281 QTSLHMAVKGVSSQVVRLLLR--ADPAIVmlpDKFGNTVLHIATRKKRAEIVNELLQ 335
Cdd:PHA03100 193 FTPLHYAVYNNNPEFVKYLLDlgANPNLV---NKYGDTPLHIAILNNNKEIFKLLLN 246
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
144-359 |
1.54e-12 |
|
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: 70.43 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 144 ETPLFTAAEKGNIDVVKELLPYTTIEsLMQKNLSGFDALHIACSQGHRSIVQLLLEHEPQLsktvaqsnatplvsaatrg 223
Cdd:cd22192 18 ESPLLLAAKENDVQAIKKLLKCPSCD-LFQRGALGETALHVAALYDNLEAAVVLMEAAPEL------------------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 224 hsevVNEllAKDSSLLEisrsnGKNALHLAARQGHVDIVRTLLDK--DPQLARRTD---KKGQTSL-----HM----AVK 289
Cdd:cd22192 78 ----VNE--PMTSDLYQ-----GETALHIAVVNQNLNLVRELIARgaDVVSPRATGtffRPGPKNLiyygeHPlsfaACV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 240255309 290 GvSSQVVRLLLRADPAIVMlPDKFGNTVLHI----ATRKKRAEIVNELLQLpDTNVNALTRDHKTAYDiaeGLT 359
Cdd:cd22192 147 G-NEEIVRLLIEHGADIRA-QDSLGNTVLHIlvlqPNKTFACQMYDLILSY-DKEDDLQPLDLVPNNQ---GLT 214
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
95-321 |
6.01e-10 |
|
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: 62.41 E-value: 6.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 95 AAQRGDLASVKQILsdidsqitgtitgadfddevAQIMTSVVNEVNELGETPLFTAAEKGNIDVVKELLPYTTIESLMQK 174
Cdd:TIGR00870 24 AAERGDLASVYRDL--------------------EEPKKLNINCPDRLGRSALFVAAIENENLELTELLLNLSCRGAVGD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 175 NLsgfdaLHIAcSQGHRSIVQLLLEHEPQLsktvaqsnatplvsaatrgHSEVVNELLAKDSSLLEISRsnGKNALHLAA 254
Cdd:TIGR00870 84 TL-----LHAI-SLEYVDAVEAILLHLLAA-------------------FRKSGPLELANDQYTSEFTP--GITALHLAA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 255 RQGHVDIVRTLLDKDPQLARR------TDKKGQTSLHM------AVKGVSS-QVVRLLLRaDPAIVMLPDKFGNTVLHIA 321
Cdd:TIGR00870 137 HRQNYEIVKLLLERGASVPARacgdffVKSQGVDSFYHgesplnAAACLGSpSIVALLSE-DPADILTADSLGNTLLHLL 215
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
245-270 |
1.71e-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: 39.11 E-value: 1.71e-04
|
| NAM-associated |
pfam14303 |
No apical meristem-associated C-terminal domain; This domain is found in a number of different ... |
20-107 |
6.85e-03 |
|
No apical meristem-associated C-terminal domain; This domain is found in a number of different types of plant proteins including NAM-like proteins.
Pssm-ID: 464129 Cd Length: 142 Bit Score: 37.46 E-value: 6.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 20 ATDPTSPTGSTVADLSPTPTPRKTLVLSNSGKALMVSNSSKSLGLSNSGKRfdPTGKKKY---VKQVTGRHNDTELHLAA 96
Cdd:pfam14303 27 NKKPSSTASSSPAPTSLASTDPDTDSSDSSSAGSNESNSDDSSPSSKSPTR--PIGRKKAkekRQEELDAAKEEKKQNDI 104
|
90
....*....|.
gi 240255309 97 QRGDLASVKQI 107
Cdd:pfam14303 105 EEAQVAAELRL 115
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PGG |
pfam13962 |
Domain of unknown function; The PGG domain is named for the highly conserved sequence motif ... |
428-533 |
3.94e-36 |
|
Domain of unknown function; The PGG domain is named for the highly conserved sequence motif found at the startt of the domain. The function is not known.
Pssm-ID: 433609 Cd Length: 114 Bit Score: 131.14 E-value: 3.94e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 428 GINNATNSVTVVAVLFATVAFAAIFTVPGG---DDDH---GVAVMVHATSFKIFFIFNAIALFTSLAVVVVQITLVRGET 501
Cdd:pfam13962 3 WLKEARNTLLLVATLIATVTFAAGFTPPGGywqDDDGphaGKPILAKNPAFKAFVISNAIAFFASLVAVVLLLSIVSDFL 82
|
90 100 110
....*....|....*....|....*....|..
gi 240255309 502 KTERRVVEVINKLMWLASVCTTVAFISSSYIV 533
Cdd:pfam13962 83 RSLPRKLRIGLKLLWVALLSMLVAFAAGSYRV 114
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
91-383 |
3.07e-30 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 120.44 E-value: 3.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 91 ELHLAAQRGDLASVKQILSDIDSQITGTITGADFDDEVAQIMTSVVNEVNELGETPLFTAAEKGNIDVVKELLPYttIES 170
Cdd:COG0666 2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAA--GAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 171 LMQKNLSGFDALHIACSQGHRSIVQLLLEHEPQLsKTVAQSNATPLVSAATRGHSEVVNELLAKDSSLlEISRSNGKNAL 250
Cdd:COG0666 80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGADV-NARDKDGETPLHLAAYNGNLEIVKLLLEAGADV-NAQDNDGNTPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 251 HLAARQGHVDIVRTLLDKDPQLARRtDKKGQTSLHMAVKGVSSQVVRLLLRADpAIVMLPDKFGNTVLHIATRKKRAEIV 330
Cdd:COG0666 158 HLAAANGNLEIVKLLLEAGADVNAR-DNDGETPLHLAAENGHLEIVKLLLEAG-ADVNAKDNDGKTALDLAAENGNLEIV 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 240255309 331 NELLQLPDtNVNALTRDHKTAYDIAEGLTHSEETAEIKEILSRCGALKANELN 383
Cdd:COG0666 236 KLLLEAGA-DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
136-351 |
2.24e-28 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 115.05 E-value: 2.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 136 VNEVNELGETPLFTAAEKGNIDVVKELLPYttIESLMQKNLSGFDALHIACSQGHRSIVQLLLEHEPQLSKTVAQSNaTP 215
Cdd:COG0666 80 INAKDDGGNTLLHAAARNGDLEIVKLLLEA--GADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGN-TP 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 216 LVSAATRGHSEVVNELLAKDSSLlEISRSNGKNALHLAARQGHVDIVRTLLDK--DPQLarrTDKKGQTSLHMAVKGVSS 293
Cdd:COG0666 157 LHLAAANGNLEIVKLLLEAGADV-NARDNDGETPLHLAAENGHLEIVKLLLEAgaDVNA---KDNDGKTALDLAAENGNL 232
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 240255309 294 QVVRLLLRADpAIVMLPDKFGNTVLHIATRKKRAEIVNELLQLPDTNVNALTRDHKTA 351
Cdd:COG0666 233 EIVKLLLEAG-ADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
168-421 |
1.91e-25 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 106.58 E-value: 1.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 168 IESLMQKNLSGFDALHIACSQGHRSIVQLLLEHEPQLSKTVAQSNATPLVSAATRGHSEVVNELLAKDSSLlEISRSNGK 247
Cdd:COG0666 43 ALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADV-NARDKDGE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 248 NALHLAARQGHVDIVRTLLDK--DPQLarrTDKKGQTSLHMAVKGVSSQVVRLLLRADpAIVMLPDKFGNTVLHIATRKK 325
Cdd:COG0666 122 TPLHLAAYNGNLEIVKLLLEAgaDVNA---QDNDGNTPLHLAAANGNLEIVKLLLEAG-ADVNARDNDGETPLHLAAENG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 326 RAEIVNELLQLpDTNVNALTRDHKTAYDIAEGLTHseetAEIKEILSRCGALKANELNQPRDELRKTVTEIKKDVHTQLE 405
Cdd:COG0666 198 HLEIVKLLLEA-GADVNAKDNDGKTALDLAAENGN----LEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLL 272
|
250
....*....|....*.
gi 240255309 406 QTRKTNKNVDGIAKEL 421
Cdd:COG0666 273 LALLLLAAALLDLLTL 288
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
76-316 |
2.39e-24 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 103.50 E-value: 2.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 76 KKKYVKQVTGRHNDTELHLAAQRGDLASVKQILSDidsqitgtitGADfddevaqimtsvVNEVNELGETPLFTAAEKGN 155
Cdd:COG0666 75 AAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA----------GAD------------VNARDKDGETPLHLAAYNGN 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 156 IDVVKELL-----PYttieslmQKNLSGFDALHIACSQGHRSIVQLLLEHEPQLsKTVAQSNATPLVSAATRGHSEVVNE 230
Cdd:COG0666 133 LEIVKLLLeagadVN-------AQDNDGNTPLHLAAANGNLEIVKLLLEAGADV-NARDNDGETPLHLAAENGHLEIVKL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 231 LLAKDSSlLEISRSNGKNALHLAARQGHVDIVRTLLDKDPQLARRtDKKGQTSLHMAVKGVSSQVVRLLLRADPAIVMLP 310
Cdd:COG0666 205 LLEAGAD-VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAK-DKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
|
....*.
gi 240255309 311 DKFGNT 316
Cdd:COG0666 283 LDLLTL 288
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
159-355 |
2.80e-18 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 85.78 E-value: 2.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 159 VKELLPYTTIESLMQKNLSGFDALHIACSQGHRSIVQLLLEHEPQLSKTVAQSNATPLVSAATRGHSEVVNELLAKDSsL 238
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGA-D 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 239 LEISRSNGKNALHLAARQGHVDIVRTLLDKDPQLARRtDKKGQTSLHMAVKGVSSQVVRLLLRADpAIVMLPDKFGNTVL 318
Cdd:COG0666 80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNAR-DKDGETPLHLAAYNGNLEIVKLLLEAG-ADVNAQDNDGNTPL 157
|
170 180 190
....*....|....*....|....*....|....*..
gi 240255309 319 HIATRKKRAEIVNELLQLpDTNVNALTRDHKTAYDIA 355
Cdd:COG0666 158 HLAAANGNLEIVKLLLEA-GADVNARDNDGETPLHLA 193
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
182-269 |
8.21e-17 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 75.92 E-value: 8.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 182 LHIACSQGHRSIVQLLLEHEPQLsKTVAQSNATPLVSAATRGHSEVVNELLAKDSSLLeisRSNGKNALHLAARQGHVDI 261
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADA-NLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL---KDNGRTALHYAARSGHLEI 76
|
....*...
gi 240255309 262 VRTLLDKD 269
Cdd:pfam12796 77 VKLLLEKG 84
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
145-335 |
3.42e-16 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 81.25 E-value: 3.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 145 TPLFTAAEKGNIDVVKELLpYTTIeSLMQKNLSGFDALHIACSQGH-----RSIVQLLLEHEPQLSKTVAQSNaTPLVSA 219
Cdd:PHA03100 37 LPLYLAKEARNIDVVKILL-DNGA-DINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGI-TPLLYA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 220 ATR--GHSEVVNELLAKDSSLlEISRSNGKNALHLAARQGHVD--IVRTLLDK--DPQLARR-------------TDKKG 280
Cdd:PHA03100 114 ISKksNSYSIVEYLLDNGANV-NIKNSDGENLLHLYLESNKIDlkILKLLIDKgvDINAKNRvnyllsygvpiniKDVYG 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 240255309 281 QTSLHMAVKGVSSQVVRLLLR--ADPAIVmlpDKFGNTVLHIATRKKRAEIVNELLQ 335
Cdd:PHA03100 193 FTPLHYAVYNNNPEFVKYLLDlgANPNLV---NKYGDTPLHIAILNNNKEIFKLLLN 246
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
92-207 |
4.17e-16 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 73.61 E-value: 4.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 92 LHLAAQRGDLASVKQILSdidsqitgtiTGADfddevaqimtsvVNEVNELGETPLFTAAEKGNIDVVKELLPYTTIESl 171
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLE----------NGAD------------ANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL- 57
|
90 100 110
....*....|....*....|....*....|....*.
gi 240255309 172 mqkNLSGFDALHIACSQGHRSIVQLLLEHEPQLSKT 207
Cdd:pfam12796 58 ---KDNGRTALHYAARSGHLEIVKLLLEKGADINVK 90
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
147-238 |
1.79e-14 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 68.99 E-value: 1.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 147 LFTAAEKGNIDVVKELLPYttIESLMQKNLSGFDALHIACSQGHRSIVQLLLEHEPQLSKTvaqSNATPLVSAATRGHSE 226
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLEN--GADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD---NGRTALHYAARSGHLE 75
|
90
....*....|..
gi 240255309 227 VVNELLAKDSSL 238
Cdd:pfam12796 76 IVKLLLEKGADI 87
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
250-335 |
5.11e-13 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 65.14 E-value: 5.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 250 LHLAARQGHVDIVRTLLDKDPQlARRTDKKGQTSLHMAVKGVSSQVVRLLLRAdpAIVMLPDKfGNTVLHIATRKKRAEI 329
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGAD-ANLQDKNGRTALHLAAKNGHLEIVKLLLEH--ADVNLKDN-GRTALHYAARSGHLEI 76
|
....*.
gi 240255309 330 VNELLQ 335
Cdd:pfam12796 77 VKLLLE 82
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
144-359 |
1.54e-12 |
|
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: 70.43 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 144 ETPLFTAAEKGNIDVVKELLPYTTIEsLMQKNLSGFDALHIACSQGHRSIVQLLLEHEPQLsktvaqsnatplvsaatrg 223
Cdd:cd22192 18 ESPLLLAAKENDVQAIKKLLKCPSCD-LFQRGALGETALHVAALYDNLEAAVVLMEAAPEL------------------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 224 hsevVNEllAKDSSLLEisrsnGKNALHLAARQGHVDIVRTLLDK--DPQLARRTD---KKGQTSL-----HM----AVK 289
Cdd:cd22192 78 ----VNE--PMTSDLYQ-----GETALHIAVVNQNLNLVRELIARgaDVVSPRATGtffRPGPKNLiyygeHPlsfaACV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 240255309 290 GvSSQVVRLLLRADPAIVMlPDKFGNTVLHI----ATRKKRAEIVNELLQLpDTNVNALTRDHKTAYDiaeGLT 359
Cdd:cd22192 147 G-NEEIVRLLIEHGADIRA-QDSLGNTVLHIlvlqPNKTFACQMYDLILSY-DKEDDLQPLDLVPNNQ---GLT 214
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
95-321 |
6.01e-10 |
|
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: 62.41 E-value: 6.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 95 AAQRGDLASVKQILsdidsqitgtitgadfddevAQIMTSVVNEVNELGETPLFTAAEKGNIDVVKELLPYTTIESLMQK 174
Cdd:TIGR00870 24 AAERGDLASVYRDL--------------------EEPKKLNINCPDRLGRSALFVAAIENENLELTELLLNLSCRGAVGD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 175 NLsgfdaLHIAcSQGHRSIVQLLLEHEPQLsktvaqsnatplvsaatrgHSEVVNELLAKDSSLLEISRsnGKNALHLAA 254
Cdd:TIGR00870 84 TL-----LHAI-SLEYVDAVEAILLHLLAA-------------------FRKSGPLELANDQYTSEFTP--GITALHLAA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 255 RQGHVDIVRTLLDKDPQLARR------TDKKGQTSLHM------AVKGVSS-QVVRLLLRaDPAIVMLPDKFGNTVLHIA 321
Cdd:TIGR00870 137 HRQNYEIVKLLLERGASVPARacgdffVKSQGVDSFYHgesplnAAACLGSpSIVALLSE-DPADILTADSLGNTLLHLL 215
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
265-321 |
1.88e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 50.81 E-value: 1.88e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 240255309 265 LLDKDPQLARRTDKKGQTSLHMAVKGVSSQVVRLLLRADPAIvMLPDKFGNTVLHIA 321
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDL-NLKDEEGLTALDLA 56
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
248-300 |
2.41e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 47.65 E-value: 2.41e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 240255309 248 NALHLAARQGHVDIVRTLLDKDPQLArRTDKKGQTSLHMAVKGVSSQVVRLLL 300
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADIN-AVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
136-387 |
4.70e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 52.66 E-value: 4.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 136 VNEVNELGETPLFTAAEKGNIDVVKEL---------LPYTTIESLMQKNL--SGFDA----------LHIACSQGHRSIV 194
Cdd:PHA02874 61 INHINTKIPHPLLTAIKIGAHDIIKLLidngvdtsiLPIPCIEKDMIKTIldCGIDVnikdaelktfLHYAIKKGDLESI 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 195 QLLLEHEPQLSktVAQSNATPLVSAATRGHSEVVNELLAKDSSLLEISRSNGKNALHLAARQGHVDIVRTLLDKDPQLAR 274
Cdd:PHA02874 141 KMLFEYGADVN--IEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMN 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 275 RTdKKGQTSLHMAVKGVSSqVVRLLLraDPAIVMLPDKFGNTVLHIATRKK-RAEIVNELLQlpdTNVNALTRDHKTAYD 353
Cdd:PHA02874 219 KC-KNGFTPLHNAIIHNRS-AIELLI--NNASINDQDIDGSTPLHHAINPPcDIDIIDILLY---HKADISIKDNKGENP 291
|
250 260 270
....*....|....*....|....*....|....
gi 240255309 354 IAEGLTHSEETAEIKEILSrcGALKANELNQPRD 387
Cdd:PHA02874 292 IDTAFKYINKDPVIKDIIA--NAVLIKEADKLKD 323
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
145-198 |
7.01e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 46.50 E-value: 7.01e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 240255309 145 TPLFTAAEKGNIDVVKELLPYTTieSLMQKNLSGFDALHIACSQGHRSIVQLLL 198
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGA--DINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02741 |
PHA02741 |
hypothetical protein; Provisional |
228-356 |
7.78e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 165108 [Multi-domain] Cd Length: 169 Bit Score: 49.27 E-value: 7.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 228 VNELLAKDSSLLEISRSNGKNALHLAARQGHVDIVRTLL-----DKDPQLARRTDKKGQTSLHMAV----KGVSSQVVRL 298
Cdd:PHA02741 3 SPHFMTCLEEMIAEKNSEGENFFHEAARCGCFDIIARFTpfirgDCHAAALNATDDAGQMCIHIAAekheAQLAAEIIDH 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 240255309 299 LLRADPAIVMLPDKFGNTVLHIATRKKRAEIVNELLQLPDTNVNALTRDHKTAYDIAE 356
Cdd:PHA02741 83 LIELGADINAQEMLEGDTALHLAAHRRDHDLAEWLCCQPGIDLHFCNADNKSPFELAI 140
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
299-355 |
8.12e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 46.19 E-value: 8.12e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 240255309 299 LLRADPAIVMLPDKFGNTVLHIATRKKRAEIVNELLQLPdTNVNALTRDHKTAYDIA 355
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYG-VDLNLKDEEGLTALDLA 56
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
154-334 |
8.20e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 51.53 E-value: 8.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 154 GNIDVVKELLpyttiESLMQKNLS---GFDALHIACSQGHRSIVQLLLEHE--PQLSKTVAQSnatPLVSAATRGHSEVV 228
Cdd:PHA02875 13 GELDIARRLL-----DIGINPNFEiydGISPIKLAMKFRDSEAIKLLMKHGaiPDVKYPDIES---ELHDAVEEGDVKAV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 229 NELLAKDSSLLEISRSNGKNALHLAARQGHVDIVRTLLDK--DPQLArRTDKKgqTSLHMAVKGVSSQVVRLLLRaDPAI 306
Cdd:PHA02875 85 EELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARgaDPDIP-NTDKF--SPLHLAVMMGDIKGIELLID-HKAC 160
|
170 180
....*....|....*....|....*...
gi 240255309 307 VMLPDKFGNTVLHIATRKKRAEIVNELL 334
Cdd:PHA02875 161 LDIEDCCGCTPLIIAMAKGDIAICKMLL 188
|
|
| PHA02736 |
PHA02736 |
Viral ankyrin protein; Provisional |
246-355 |
9.97e-07 |
|
Viral ankyrin protein; Provisional
Pssm-ID: 165103 [Multi-domain] Cd Length: 154 Bit Score: 48.72 E-value: 9.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 246 GKNALHLAARQGHV-DIV---RTLLDKDPQLARRTDKKGQTSLHMAV---KGVSSQVVRLLLRADPAIVMLPDKFGNTVL 318
Cdd:PHA02736 17 GENILHYLCRNGGVtDLLafkNAISDENRYLVLEYNRHGKQCVHIVSnpdKADPQEKLKLLMEWGADINGKERVFGNTPL 96
|
90 100 110
....*....|....*....|....*....|....*..
gi 240255309 319 HIATRKKRAEIVNELLQLPDTNVNALTRDHKTAYDIA 355
Cdd:PHA02736 97 HIAVYTQNYELATWLCNQPGVNMEILNYAFKTPYYVA 133
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
89-268 |
1.22e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 51.15 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 89 DTELHLAAQRGDLASVKQILsdidsqITGTitgadFDDEVaqimtsvvneVNELGETPLFTAAEKGNIDVVKELLPYTTI 168
Cdd:PHA02875 69 ESELHDAVEEGDVKAVEELL------DLGK-----FADDV----------FYKDGMTPLHLATILKKLDIMKLLIARGAD 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 169 ESLmqKNLSGFDALHIACSQGHRSIVQLLLEHEPQLSKTVAqSNATPLVSAATRGHSEVVNELLAKDSSLLEISRSNGKN 248
Cdd:PHA02875 128 PDI--PNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDC-CGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVA 204
|
170 180
....*....|....*....|
gi 240255309 249 ALHLAARQGHVDIVRTLLDK 268
Cdd:PHA02875 205 ALCYAIENNKIDIVRLFIKR 224
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
231-287 |
1.91e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 45.03 E-value: 1.91e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 240255309 231 LLAKDSSLLEISRSNGKNALHLAARQGHVDIVRTLLDKdPQLARRTDKKGQTSLHMA 287
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAY-GVDLNLKDEEGLTALDLA 56
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
104-355 |
1.96e-06 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 51.02 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 104 VKQILSD-IDSQITGTITGADFDDEVAQI---------MTSVVNEVNELGETPLFTAAE---KGNIDVVKELLPYtties 170
Cdd:PLN03192 426 VEIIDSEgEKERVVGTLGCGDIFGEVGALccrpqsftfRTKTLSQLLRLKTSTLIEAMQtrqEDNVVILKNFLQH----- 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 171 lmQKNLSGFDalhiacsqghrsIVQLLLEHEPQLSKTVAQSNatpLVSAATRGHSEVVNELL-AKDSSllEISRSNGKNA 249
Cdd:PLN03192 501 --HKELHDLN------------VGDLLGDNGGEHDDPNMASN---LLTVASTGNAALLEELLkAKLDP--DIGDSKGRTP 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 250 LHLAARQGHVDIVRTLLDKDPQLARRtDKKGQTSLHMAVKGVSSQVVRLLLR----ADPAIvmlpdkfGNTVLHIATRKK 325
Cdd:PLN03192 562 LHIAASKGYEDCVLVLLKHACNVHIR-DANGNTALWNAISAKHHKIFRILYHfasiSDPHA-------AGDLLCTAAKRN 633
|
250 260 270
....*....|....*....|....*....|
gi 240255309 326 RAEIVNELLQLpDTNVNALTRDHKTAYDIA 355
Cdd:PLN03192 634 DLTAMKELLKQ-GLNVDSEDHQGATALQVA 662
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
214-266 |
3.57e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 44.19 E-value: 3.57e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 240255309 214 TPLVSAATRGHSEVVNELLAKDSSLLEISRsNGKNALHLAARQGHVDIVRTLL 266
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDG-NGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
284-355 |
3.95e-06 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 45.49 E-value: 3.95e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 240255309 284 LHMAVKGVSSQVVRLLLRADPAIvMLPDKFGNTVLHIATRKKRAEIVNELLQLPDTNVNAltrDHKTAYDIA 355
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADA-NLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD---NGRTALHYA 68
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
86-268 |
6.22e-06 |
|
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: 49.24 E-value: 6.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 86 RHNDTELHLAAQRGDLASVKQIL--SDIDSQITGTI------TGADFD-DEVAQIMTSVVNE-VNE-------LGETPLF 148
Cdd:cd22192 15 RISESPLLLAAKENDVQAIKKLLkcPSCDLFQRGALgetalhVAALYDnLEAAVVLMEAAPElVNEpmtsdlyQGETALH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 149 TAAEKGNIDVVKELLPYT----------TIESLMQKNLS--GFDALHIACSQGHRSIVQLLLEH------EPQLSKTV-- 208
Cdd:cd22192 95 IAVVNQNLNLVRELIARGadvvspratgTFFRPGPKNLIyyGEHPLSFAACVGNEEIVRLLIEHgadiraQDSLGNTVlh 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 240255309 209 ---AQSNATPLvsaatrghSEVVNELLAKDSSLLEISRSNGKN-----ALHLAARQGHVDIVRTLLDK 268
Cdd:cd22192 175 ilvLQPNKTFA--------CQMYDLILSYDKEDDLQPLDLVPNnqgltPFKLAAKEGNIVMFQHLVQK 234
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
146-343 |
7.07e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 48.72 E-value: 7.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 146 PLFTAAEKGNIDVVKELLpyTTIESLMQKNLSGFDALHIACSQGH--------RSIVQLLLEHEPQLSKTVAQSN----- 212
Cdd:PHA02878 40 PLHQAVEARNLDVVKSLL--TRGHNVNQPDHRDLTPLHIICKEPNklgmkemiRSINKCSVFYTLVAIKDAFNNRnveif 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 213 ------------ATPLVSAATRGH-----SEVVNELLAKDSSLLEISRSNGKNALHLAARQGHVDIVRTLLDK--DPQLA 273
Cdd:PHA02878 118 kiiltnrykniqTIDLVYIDKKSKddiieAEITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYgaNVNIP 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 240255309 274 RRTDKkgqTSLHMAVKGVSSQVVRLLLRaDPAIVMLPDKFGNTVLHIAT-RKKRAEIVNELLQlPDTNVNA 343
Cdd:PHA02878 198 DKTNN---SPLHHAVKHYNKPIVHILLE-NGASTDARDKCGNTPLHISVgYCKDYDILKLLLE-HGVDVNA 263
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
180-232 |
1.33e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 42.65 E-value: 1.33e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 240255309 180 DALHIACSQGHRSIVQLLLEHEPQLSKTVAQSNaTPLVSAATRGHSEVVNELL 232
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGE-TALHFAASNGNVEVLKLLL 54
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
143-266 |
3.04e-05 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 47.17 E-value: 3.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 143 GETPLFTAAEKGNIDVVKELLPYTTieSLMQKNLSGFDALHIACSQGHRSIVQLLLeHEPQLSKTVAQSNAtpLVSAATR 222
Cdd:PLN03192 558 GRTPLHIAASKGYEDCVLVLLKHAC--NVHIRDANGNTALWNAISAKHHKIFRILY-HFASISDPHAAGDL--LCTAAKR 632
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 240255309 223 GHSEVVNELLaKDSSLLEISRSNGKNALHLAARQGHVDIVRTLL 266
Cdd:PLN03192 633 NDLTAMKELL-KQGLNVDSEDHQGATALQVAMAEDHVDMVRLLI 675
|
|
| PHA02743 |
PHA02743 |
Viral ankyrin protein; Provisional |
247-376 |
3.57e-05 |
|
Viral ankyrin protein; Provisional
Pssm-ID: 222925 [Multi-domain] Cd Length: 166 Bit Score: 44.42 E-value: 3.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 247 KNALHLAARQGHVDI---VRTLLDKDPQLARRTDKKGQTSLHMAVK-GVSSQVVR--LLLRADPAIVMLPDKFGNTVLHI 320
Cdd:PHA02743 21 QNTFLRICRTGNIYElmeVAPFISGDGHLLHRYDHHGRQCTHMVAWyDRANAVMKieLLVNMGADINARELGTGNTLLHI 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 240255309 321 ATRKKRAEIVNELLQLPDTNVNALTRDHKTAYDIAegltHSEETAEIKEILSRCGA 376
Cdd:PHA02743 101 AASTKNYELAEWLCRQLGVNLGAINYQHETAYHIA----YKMRDRRMMEILRANGA 152
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
86-341 |
4.03e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 46.50 E-value: 4.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 86 RHNDTELHLAAQRGDLASVKQILSdidsqitgtiTGADfddevaqimtsvVNEVNELGETPLFTAAEKGNIDVVKELLPY 165
Cdd:PHA02874 122 AELKTFLHYAIKKGDLESIKMLFE----------YGAD------------VNIEDDNGCYPIHIAIKHNFFDIIKLLLEK 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 166 TTIESLmqKNLSGFDALHIACSQGHRSIVQLLLEHEPQLSKTvAQSNATPLVSAATrgHSEVVNELLAKDSSlLEISRSN 245
Cdd:PHA02874 180 GAYANV--KDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNK-CKNGFTPLHNAII--HNRSAIELLINNAS-INDQDID 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 246 GKNALHLAARQG-HVDIVRTLLDKDPQLARRtDKKGQTSLHMAVKGVSSQVVrlllradpaivmLPDKFGNTVLhiatrk 324
Cdd:PHA02874 254 GSTPLHHAINPPcDIDIIDILLYHKADISIK-DNKGENPIDTAFKYINKDPV------------IKDIIANAVL------ 314
|
250
....*....|....*..
gi 240255309 325 kraeiVNELLQLPDTNV 341
Cdd:PHA02874 315 -----IKEADKLKDSDF 326
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
245-270 |
1.71e-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: 39.11 E-value: 1.71e-04
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
245-301 |
1.93e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 44.50 E-value: 1.93e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 240255309 245 NGKNALHLAARQGHVDIVRTLLD--KDPQLarrTDKKGQTSLHMAVKGVSSQVVRLLLR 301
Cdd:PTZ00322 114 DGRTPLHIACANGHVQVVRVLLEfgADPTL---LDKDGKTPLELAEENGFREVVQLLSR 169
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
197-253 |
4.54e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 38.48 E-value: 4.54e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 240255309 197 LLEHEPQLSKTVAQSNATPLVSAATRGHSEVVNELLAKDSSLLeISRSNGKNALHLA 253
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLN-LKDEEGLTALDLA 56
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
160-320 |
7.86e-04 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (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. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).
Pssm-ID: 411975 [Multi-domain] Cd Length: 600 Bit Score: 42.56 E-value: 7.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 160 KELLPY------TTIESLMQKNLSGFDALHIAcsqghrsivqLLLEHEPQLSKtvaqsnATPLVSAA--TRGHSEVVNEL 231
Cdd:cd21882 2 EELLGLleclrwYLTDSAYQRGATGKTCLHKA----------ALNLNDGVNEA------IMLLLEAApdSGNPKELVNAP 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 232 LAkdSSLLEisrsnGKNALHLAARQGHVDIVRTLLDK--DPQLA------RRTDKK----GQTSLHMAVKGVSSQVVRLL 299
Cdd:cd21882 66 CT--DEFYQ-----GQTALHIAIENRNLNLVRLLVENgaDVSARatgrffRKSPGNlfyfGELPLSLAACTNQEEIVRLL 138
|
170 180
....*....|....*....|...
gi 240255309 300 LR--ADPAIVMLPDKFGNTVLHI 320
Cdd:cd21882 139 LEngAQPAALEAQDSLGNTVLHA 161
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
136-202 |
8.19e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 41.96 E-value: 8.19e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 240255309 136 VNEVNELGETPLFTAAEKGNIDVVKELLPYTTieSLMQKNLSGFDALHIACSQGHRSIVQLLLEHEP 202
Cdd:PHA03100 185 INIKDVYGFTPLHYAVYNNNPEFVKYLLDLGA--NPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
136-348 |
9.09e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 42.36 E-value: 9.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 136 VNEVNELGETPLFTAAEKGNIDVVKELLPYTTIESLMqkNLSGFDALHIACSQGHRSIVQLLLEHEPQLSKtvaqsNATP 215
Cdd:PHA02876 171 VNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNII--ALDDLSVLECAVDSKNIDTIKAIIDNRSNINK-----NDLS 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 216 LVSAATrgHSEVVNELLAKDSSLLEISRSNGKNA-LHLAARQGHVD-IVRTLLDKDPQLARRtDKKGQTSLH-MAVKGVS 292
Cdd:PHA02876 244 LLKAIR--NEDLETSLLLYDAGFSVNSIDDCKNTpLHHASQAPSLSrLVPKLLERGADVNAK-NIKGETPLYlMAKNGYD 320
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 240255309 293 SQVVRLLLRADpAIVMLPDKFGNTVLHIA-TRKKRAEIVNELLQLpDTNVNAltRDH 348
Cdd:PHA02876 321 TENIRTLIMLG-ADVNAADRLYITPLHQAsTLDRNKDIVITLLEL-GANVNA--RDY 373
|
|
| PRK11207 |
PRK11207 |
tellurite resistance methyltransferase TehB; |
221-307 |
9.22e-04 |
|
tellurite resistance methyltransferase TehB;
Pssm-ID: 183040 Cd Length: 197 Bit Score: 40.87 E-value: 9.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 221 TRGHSEVVNEL-LAKDSSLLEISRSNGKNALHLAARQGHVdivrTLLDKDP----QLARRTDKKGQTSLHMAVKG----- 290
Cdd:PRK11207 16 TRTHSEVLEAVkVVKPGKTLDLGCGNGRNSLYLAANGFDV----TAWDKNPmsiaNLERIKAAENLDNLHTAVVDlnnlt 91
|
90 100
....*....|....*....|....*.
gi 240255309 291 -------VSSQVVRLLLRAD--PAIV 307
Cdd:PRK11207 92 fdgeydfILSTVVLMFLEAKtiPGLI 117
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
88-163 |
9.23e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 37.64 E-value: 9.23e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 240255309 88 NDTELHLAAQRGDLASVKQILSdidsqitgtiTGADfddevaqimtsvVNEVNELGETPLFTAAEKGNIDVVKELL 163
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLE----------KGAD------------INAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
251-334 |
2.36e-03 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 41.04 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 251 HLAARQGHVDIvRTLLDKDPQLARRtDKKGQTSLHMAVKGVSSQVVRLLLR--ADPAivmLPDKFGNTVLHIATRKKRAE 328
Cdd:PTZ00322 88 QLAASGDAVGA-RILLTGGADPNCR-DYDGRTPLHIACANGHVQVVRVLLEfgADPT---LLDKDGKTPLELAEENGFRE 162
|
....*.
gi 240255309 329 IVNELL 334
Cdd:PTZ00322 163 VVQLLS 168
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
296-389 |
3.17e-03 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 40.65 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 296 VRLLLR--ADPAIVmlpDKFGNTVLHIATRKKRAEIVNELLQLpDTNVNALTRDHKTAYDIAEglthSEETAEIKEILSR 373
Cdd:PTZ00322 98 ARILLTggADPNCR---DYDGRTPLHIACANGHVQVVRVLLEF-GADPTLLDKDGKTPLELAE----ENGFREVVQLLSR 169
|
90
....*....|....*..
gi 240255309 374 CGALKAN-ELNQPRDEL 389
Cdd:PTZ00322 170 HSQCHFElGANAKPDSF 186
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
245-272 |
3.20e-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.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 35.31 E-value: 3.20e-03
10 20
....*....|....*....|....*...
gi 240255309 245 NGKNALHLAARQGHVDIVRTLLDKDPQL 272
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADI 28
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
245-277 |
3.79e-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: 35.34 E-value: 3.79e-03
10 20 30
....*....|....*....|....*....|....
gi 240255309 245 NGKNALHLAA-RQGHVDIVRTLLDKDPQLARRTD 277
Cdd:pfam00023 1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
226-354 |
3.81e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 40.01 E-value: 3.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 226 EVVNELLAKDSSLlEISRSNGKNALHLAARQGH---VDIVRTLLDKDPQLARRtDKKGQTSLHMAVK-GVSSQVVRLLLR 301
Cdd:PHA03095 28 EEVRRLLAAGADV-NFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAP-ERCGFTPLHLYLYnATTLDVIKLLIK 105
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 240255309 302 ADpAIVMLPDKFGNTVLHIATRKK--RAEIVNELLQLpDTNVNALTRDHKTAYDI 354
Cdd:PHA03095 106 AG-ADVNAKDKVGRTPLHVYLSGFniNPKVIRLLLRK-GADVNALDLYGMTPLAV 158
|
|
| NAM-associated |
pfam14303 |
No apical meristem-associated C-terminal domain; This domain is found in a number of different ... |
20-107 |
6.85e-03 |
|
No apical meristem-associated C-terminal domain; This domain is found in a number of different types of plant proteins including NAM-like proteins.
Pssm-ID: 464129 Cd Length: 142 Bit Score: 37.46 E-value: 6.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255309 20 ATDPTSPTGSTVADLSPTPTPRKTLVLSNSGKALMVSNSSKSLGLSNSGKRfdPTGKKKY---VKQVTGRHNDTELHLAA 96
Cdd:pfam14303 27 NKKPSSTASSSPAPTSLASTDPDTDSSDSSSAGSNESNSDDSSPSSKSPTR--PIGRKKAkekRQEELDAAKEEKKQNDI 104
|
90
....*....|.
gi 240255309 97 QRGDLASVKQI 107
Cdd:pfam14303 105 EEAQVAAELRL 115
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
178-200 |
9.05e-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: 34.10 E-value: 9.05e-03
|
|