|
Name |
Accession |
Description |
Interval |
E-value |
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
56-343 |
7.83e-47 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 169.75 E-value: 7.83e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 56 ILQLLLMSGANVNAKDTLWLTPLHRAAASRNEKVLGLLLAHSADVNARDKLWQTPLHVAAANRATKCAEALAPLLSSLNV 135
Cdd:COG0666 3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 136 ADRSGRSALHHAVHSGHLETVNLLLNKGASLNVCDKKERQPLHWAAFLGHLEVLKLLVARGADLSCKDRKGYGLLHTAAA 215
Cdd:COG0666 83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 216 SGQIEVVKHLLRMGAEIDEPNAFGNTALHIACYLGQDAVAIELVNAGANVNQPNDKGFTPLHVAAVSTNGALcLELLVNN 295
Cdd:COG0666 163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI-VKLLLEA 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 27370168 296 GADVNYQSKEGKSPLHMAAIHGRFTRSQILIQNGSEIDCADKFGNTPL 343
Cdd:COG0666 242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
87-366 |
1.52e-45 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 165.90 E-value: 1.52e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 87 EKVLGLLLAHSADVNARDKLWQTPLHVAAANRATKCAEALAPLLSSLNVADRSGRSALHHAVHSGHLETVNLLLNKGASL 166
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 167 NVCDKKERQPLHWAAFLGHLEVLKLLVARGADLSCKDRKGYGLLHTAAASGQIEVVKHLLRMGAEIDEPNAFGNTALHIA 246
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 247 CYLGQDAVAIELVNAGANVNQPNDKGFTPLHVAAVSTNGALcLELLVNNGADVNYQSKEGKSPLHMAAIHGRFTRSQILI 326
Cdd:COG0666 161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEI-VKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 27370168 327 QNGSEIDCADKFGNTPLHVAARYGHELLISTLMTNGADTA 366
Cdd:COG0666 240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLA 279
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
21-301 |
1.75e-44 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 162.82 E-value: 1.75e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 21 VEEVRSLLSQKENINVLDQERRTPLHAAAYVGDVPILQLLLMSGANVNAKDTLWLTPLHRAAASRNEKVLGLLLAHSADV 100
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 101 NARDKLWQTPLHVAAANRATKCAEALAPLLSSLNVADRSGRSALHHAVHSGHLETVNLLLNKGASLNVCDKKERQPLHWA 180
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 181 AFLGHLEVLKLLVARGADLSCKDRKGYGLLHTAAASGQIEVVKHLLRMGAEIDEPNAFGNTALHIACYLGQDAVAIELVN 260
Cdd:COG0666 161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 27370168 261 AGANVNQPNDKGFTPLHVAAVSTNGALCLELLVNNGADVNY 301
Cdd:COG0666 241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAA 281
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
11-276 |
2.96e-44 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 162.43 E-value: 2.96e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 11 PLVQAIFSRDVEEVRSLLSQKENINVLDQERRTPLHAAAYVGDVPILQLLLMSGANVNAKDTLWLTPLHRAAASRNEKVL 90
Cdd:COG0666 24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 91 GLLLAHSADVNARDKLWQTPLHVAAANRATKCAEALAPLLSSLNVADRSGRSALHHAVHSGHLETVNLLLNKGASLNVCD 170
Cdd:COG0666 104 KLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARD 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 171 KKERQPLHWAAFLGHLEVLKLLVARGADLSCKDRKGYGLLHTAAASGQIEVVKHLLRMGAEIDEPNAFGNTALHIACYLG 250
Cdd:COG0666 184 NDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAG 263
|
250 260
....*....|....*....|....*.
gi 27370168 251 QDAVAIELVNAGANVNQPNDKGFTPL 276
Cdd:COG0666 264 AALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
8-243 |
3.36e-38 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 144.71 E-value: 3.36e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 8 DQPPLVQAIFSRDVEEVRSLLSQKENINVLDQERRTPLHAAAYVGDVPILQLLLMSGANVNAKDTLWLTPLHRAAASRNE 87
Cdd:COG0666 87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 88 KVLGLLLAHSADVNARDKlwqtplhvaaanratkcaealapllsslnvadrSGRSALHHAVHSGHLETVNLLLNKGASLN 167
Cdd:COG0666 167 EIVKLLLEAGADVNARDN---------------------------------DGETPLHLAAENGHLEIVKLLLEAGADVN 213
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27370168 168 VCDKKERQPLHWAAFLGHLEVLKLLVARGADLSCKDRKGYGLLHTAAASGQIEVVKHLLRMGAEIDEPNAFGNTAL 243
Cdd:COG0666 214 AKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
20-317 |
8.08e-38 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 148.63 E-value: 8.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 20 DVEEVRSLLSQKENINVLDQERRTPLHA--AAYVGDVP-ILQLLLMSGANVNAKDTLWLTPLHRAAASRN-EKVLGLLLA 95
Cdd:PHA03095 26 TVEEVRRLLAAGADVNFRGEYGKTPLHLylHYSSEKVKdIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 96 HSADVNARDKLWQTPLHVAaanratkcaealaplLSSLNVadrsgrsalhhavhsgHLETVNLLLNKGASLNVCDKKERQ 175
Cdd:PHA03095 106 AGADVNAKDKVGRTPLHVY---------------LSGFNI----------------NPKVIRLLLRKGADVNALDLYGMT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 176 PLHwaAFLGH----LEVLKLLVARGADLSCKDRKGYGLLHTAAASGQI--EVVKHLLRMGAEIDEPNAFGNTALHIACYL 249
Cdd:PHA03095 155 PLA--VLLKSrnanVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPraRIVRELIRAGCDPAATDMLGNTPLHSMATG 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 250 G--QDAVAIELVNAGANVNQPNDKGFTPLHVAAVSTNGALCLELLvNNGADVNYQSKEGKSPLHMAAIHG 317
Cdd:PHA03095 233 SscKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLI-ALGADINAVSSDGNTPLSLMVRNN 301
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
56-417 |
5.16e-37 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 149.44 E-value: 5.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 56 ILQLLLMSGANVNAKDTLWLTPLHRAAASRNEKVLGLLLAHSADVN--ARDKLwqTPLHVAAANRATKCAEALAPLLSSL 133
Cdd:PHA02876 160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNiiALDDL--SVLECAVDSKNIDTIKAIIDNRSNI 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 134 NVADRSgrsaLHHAVHSGHLETVNLLLNKGASLNVCDKKERQPLHWAAFLGHLEVL-KLLVARGADLSCKDRKGYGLLHT 212
Cdd:PHA02876 238 NKNDLS----LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLvPKLLERGADVNAKNIKGETPLYL 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 213 AAASG-QIEVVKHLLRMGAEIDEPNAFGNTALHIACYLGQDA-VAIELVNAGANVNQPNDKGFTPLHVAAVStNGALCLE 290
Cdd:PHA02876 314 MAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKdIVITLLELGANVNARDYCDKTPIHYAAVR-NNVVIIN 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 291 LLVNNGADVNYQSKEGKSPLHMaAIHGR--FTRSQILIQNGSEIDCADKFGNTPLHVAARYGHEL-LISTLMTNGADTAR 367
Cdd:PHA02876 393 TLLDYGADIEALSQKIGTALHF-ALCGTnpYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKLdVIEMLLDNGADVNA 471
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 27370168 368 RGIHDMFPLHLAVlfGFSDCCRKLLSSGqlysivSSLSNEHVLSAGFDIN 417
Cdd:PHA02876 472 INIQNQYPLLIAL--EYHGIVNILLHYG------AELRDSRVLHKSLNDN 513
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
186-489 |
2.28e-36 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 139.32 E-value: 2.28e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 186 LEVLKLLVARGADLSCKDRKGYGLLHTAAASGQIEVVKHLLRMGAEIDEPNAFGNTALHIACYLGQDAVAIELVNAGANV 265
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 266 NQPNDKGFTPLHvAAVSTNGALCLELLVNNGADVNYQSKEGKSPLHMAAIHGRFTRSQILIQNGSEIDCADKFGNTPLHV 345
Cdd:COG0666 81 NAKDDGGNTLLH-AAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 346 AARYGHELLISTLMTNGADTARRGIHDMFPLHLAVLFGFSDCCRKLlssgqlysivsslsnehvLSAGFDINTPDSLGRT 425
Cdd:COG0666 160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL------------------LEAGADVNAKDNDGKT 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27370168 426 CLHAAASGGNVECLNLLLSSGADLRRRDKFGRTPLHYAAANGSYQCAVTLVTAGAGVNEADCKG 489
Cdd:COG0666 222 ALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
16-373 |
8.38e-33 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 132.78 E-value: 8.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 16 IFSRDVEEVRSLLSQKEN-INVLDQERRTPLHAAAYVGDVPILQLLLMSGANVNAKDTLWLTPLHRAAASRNEKVLGLLL 94
Cdd:PHA02874 9 IYSGDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 95 AHSADVNArdklwqtpLHVAAANRatkcaEALAPLLSS---LNVADRSGRSALHHAVHSGHLETVNLLLNKGASLNVCDK 171
Cdd:PHA02874 89 DNGVDTSI--------LPIPCIEK-----DMIKTILDCgidVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 172 KERQPLHWAAFLGHLEVLKLLVARGADLSCKDRKGYGLLHTAAASGQIEVVKHLLRMGAEIDEPNAFGNTALHIACYLGQ 251
Cdd:PHA02874 156 NGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 252 DAVAIELVNAGANVNQPNdkGFTPLHVAAVSTNGALCLELLVNNGADVNYQSKEGKSPLHMAAIH-GRFTRSQILIQNGS 330
Cdd:PHA02874 236 SAIELLINNASINDQDID--GSTPLHHAINPPCDIDIIDILLYHKADISIKDNKGENPIDTAFKYiNKDPVIKDIIANAV 313
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 27370168 331 EIDCADKFGNTPL--HVaaryghELLISTLMTNGADTARRGIHDM 373
Cdd:PHA02874 314 LIKEADKLKDSDFleHI------EIKDNKEFSDFIKECNEEIEDM 352
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
289-622 |
9.80e-33 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 128.92 E-value: 9.80e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 289 LELLVNNGADVNYQSKEGKSPLHMAAIHGRFTRSQILIQNGSEIDCADKFGNTPLHVAARYGHELLISTLMTNGADTARR 368
Cdd:COG0666 4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 369 GIHDMFPLHLAVLFGFSDCCRKLLSsgqlysivsslsnehvlsAGFDINTPDSLGRTCLHAAASGGNVECLNLLLSSGAD 448
Cdd:COG0666 84 DDGGNTLLHAAARNGDLEIVKLLLE------------------AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGAD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 449 LRRRDKFGRTPLHYAAANGSYQCAVTLVTAGAGVNEADCKGCSPLHYAAASDtyrraephtasshdaeedellkesrRKE 528
Cdd:COG0666 146 VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENG-------------------------HLE 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 529 AffcLEFLLDNGADPSLRDRQGYTAVHYAAAYGNRQNLELLLEMSFNclEDVESTVPVSPLHLAAYNGHCEALKTLAETL 608
Cdd:COG0666 201 I---VKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD--LNAKDKDGLTALLLAAAAGAALIVKLLLLAL 275
|
330
....*....|....
gi 27370168 609 VNLDVRDHKGRTAL 622
Cdd:COG0666 276 LLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
668-998 |
2.40e-32 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 127.76 E-value: 2.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 668 LHLLIDSGERADITDVMDAYGQTPLMLAIMNGHVDCVHLLLEKGSTADAADLRGRTALHRGAVTGCEDCLAALLDHDAFV 747
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 748 LCRDFKGRTPIHLASACGHTAVLRTLLQAALSTDpldaGVDYSGYSPMHWASYTGHEDCLELLLEHspfsylegnpftpl 827
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVN----ARDKDGETPLHLAAYNGNLEIVKLLLEA-------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 828 hcavinnqdsttemllgalGAKiVNSRDAKGRTPLHAAAFADNVSGLRMLLQHQAEVNATDHTGRTALMTAAESGQTAAV 907
Cdd:COG0666 143 -------------------GAD-VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 908 EFLLYRGkADLTVLDENKNTALHLACSKGHEKCALMILAEtqdLGLINATNSALQMPLHIAARNGLASVVQALLSRGATV 987
Cdd:COG0666 203 KLLLEAG-ADVNAKDNDGKTALDLAAENGNLEIVKLLLEA---GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLL 278
|
330
....*....|.
gi 27370168 988 LAVDEEGHTPA 998
Cdd:COG0666 279 AAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
773-1015 |
1.83e-29 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 119.29 E-value: 1.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 773 LLQAALSTDPLDAGVDYSGYSPMHWASYTGHEDCLELLLEHSPFSYLEGNPFTPLHCAVINNQDSTTEMLLGALGAKIvN 852
Cdd:COG0666 3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI-N 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 853 SRDAKGRTPLHAAAFADNVSGLRMLLQHQAEVNATDHTGRTALMTAAESGQTAAVEFLLYRGkADLTVLDENKNTALHLA 932
Cdd:COG0666 82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAG-ADVNAQDNDGNTPLHLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 933 CSKGHEKCALMILAETQDlglINATNSALQMPLHIAARNGLASVVQALLSRGATVLAVDEEGHTPALACAPNKDVADCLA 1012
Cdd:COG0666 161 AANGNLEIVKLLLEAGAD---VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKL 237
|
...
gi 27370168 1013 LIL 1015
Cdd:COG0666 238 LLE 240
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
588-860 |
2.30e-29 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 119.29 E-value: 2.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 588 PLHLAAYNGHCEALKTLAETLVNLDVRDHKGRTALFLATERGSTECVEVLTAHGAsALIKERKRKWTPLHAAAASGHTDS 667
Cdd:COG0666 24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGA-DINAKDDGGNTLLHAAARNGDLEI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 668 LHLLIDSGerADItDVMDAYGQTPLMLAIMNGHVDCVHLLLEKGSTADAADLRGRTALHRGAVTGCEDCLAALLDHDAFV 747
Cdd:COG0666 103 VKLLLEAG--ADV-NARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 748 LCRDFKGRTPIHLASACGHTAVLRTLLQAALSTDPLDAgvdySGYSPMHWASYTGHEDCLELLLEHSPFSYLEGNPFTPL 827
Cdd:COG0666 180 NARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN----DGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTA 255
|
250 260 270
....*....|....*....|....*....|...
gi 27370168 828 HCAVINNQDSTTEMLLGALGAKIVNSRDAKGRT 860
Cdd:COG0666 256 LLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
706-1015 |
3.85e-29 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 118.52 E-value: 3.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 706 LLLEKGSTADAADLRGRTALHRGAVTGCEDCLAALLDHDAFVLCRDFKGRTPIHLASACGHTAVLRTLLQAALSTDPLDA 785
Cdd:COG0666 6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 786 GvdysGYSPMHWASYTGHEDCLELLLEHspfsylegnpftplhcavinnqdsttemllgalGAKiVNSRDAKGRTPLHAA 865
Cdd:COG0666 86 G----GNTLLHAAARNGDLEIVKLLLEA---------------------------------GAD-VNARDKDGETPLHLA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 866 AFADNVSGLRMLLQHQAEVNATDHTGRTALMTAAESGQTAAVEFLLYRGkADLTVLDENKNTALHLACSKGHEKCALMIL 945
Cdd:COG0666 128 AYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAG-ADVNARDNDGETPLHLAAENGHLEIVKLLL 206
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 946 AETQDlglINATNSALQMPLHIAARNGLASVVQALLSRGATVLAVDEEGHTPALACAPNKDVADCLALIL 1015
Cdd:COG0666 207 EAGAD---VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLL 273
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
512-758 |
1.05e-28 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 117.36 E-value: 1.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 512 SHDAEEDELLKESRRKEAFFCLEFLLDNGADPSLRDRQGYTAVHYAAAYGNRQNLELLLEMSFNCleDVESTVPVSPLHL 591
Cdd:COG0666 49 LADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADV--NARDKDGETPLHL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 592 AAYNGHCEALKTLAETLVNLDVRDHKGRTALFLATERGSTECVEVLTAHGASALIKERKrKWTPLHAAAASGHTDSLHLL 671
Cdd:COG0666 127 AAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDND-GETPLHLAAENGHLEIVKLL 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 672 IDSGerADITDVmDAYGQTPLMLAIMNGHVDCVHLLLEKGSTADAADLRGRTALHRGAVTGCEDCLAALLDHDAFVLCRD 751
Cdd:COG0666 206 LEAG--ADVNAK-DNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
|
....*..
gi 27370168 752 FKGRTPI 758
Cdd:COG0666 283 LDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
656-956 |
7.76e-28 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 114.67 E-value: 7.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 656 LHAAAASGHTDSLHLLIDSGERADITDVMDAYGQTPLMLAIMNGHVDCVHLLLEKGSTADAADLRGRTALHRGAVTGCED 735
Cdd:COG0666 22 ALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 736 CLAALLDHDAFVLCRDFKGRTPIHLASACGHTAVLRTLLQAALSTDPLDAgvdySGYSPMHWASYTGHEDCLELLLEHsp 815
Cdd:COG0666 102 IVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN----DGNTPLHLAAANGNLEIVKLLLEA-- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 816 fsylegnpftplhcavinnqdsttemllgalGAKiVNSRDAKGRTPLHAAAFADNVSGLRMLLQHQAEVNATDHTGRTAL 895
Cdd:COG0666 176 -------------------------------GAD-VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTAL 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27370168 896 MTAAESGQTAAVEFLLYRGkADLTVLDENKNTALHLACSKGHEKCALMILAETQDLGLINA 956
Cdd:COG0666 224 DLAAENGNLEIVKLLLEAG-ADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
21-301 |
1.54e-27 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 116.69 E-value: 1.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 21 VEEVRSLLSQKENINVLDQERRTPLHAAAYVGDVPILQLLLMSGANVNAKDTLWLTPLH-----RAAASRNEKVLGLLLA 95
Cdd:PHA03100 15 VKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 96 HSADVNARDKLWQTPLHVAAANratkcaealapllsslnvadrsgrsalhhavHSGHLETVNLLLNKGASLNVCDKKERQ 175
Cdd:PHA03100 95 YGANVNAPDNNGITPLLYAISK-------------------------------KSNSYSIVEYLLDNGANVNIKNSDGEN 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 176 PLHWAAFLGH--LEVLKLLVARGADLSCKDRkgygllhtaaasgqievVKHLLRMGAEIDEPNAFGNTALHIACYlgqdA 253
Cdd:PHA03100 144 LLHLYLESNKidLKILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVY----N 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 27370168 254 VAIELVNA----GANVNQPNDKGFTPLHVAAVSTNGALcLELLVNNGADVNY 301
Cdd:PHA03100 203 NNPEFVKYlldlGANPNLVNKYGDTPLHIAILNNNKEI-FKLLLNNGPSIKT 253
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
410-725 |
1.66e-27 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 113.90 E-value: 1.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 410 LSAGFDINTPDSLGRTCLHAAASGGNVECLNLLLSSGADLRRRDKFGRTPLHYAAANGSYQCAVTLVTAGAGVNEADCKG 489
Cdd:COG0666 41 LLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDG 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 490 CSPLHYAAASDtyrraepHTAsshdaeedellkesrrkeaffCLEFLLDNGADPSLRDRQGYTavhyaaaygnrqnlell 569
Cdd:COG0666 121 ETPLHLAAYNG-------NLE---------------------IVKLLLEAGADVNAQDNDGNT----------------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 570 lemsfncledvestvpvsPLHLAAYNGHCEALKTLAETLVNLDVRDHKGRTALFLATERGSTECVEVLTAHGASALIKEr 649
Cdd:COG0666 156 ------------------PLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKD- 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27370168 650 KRKWTPLHAAAASGHTDSLHLLIDSGERADITdvmDAYGQTPLMLAIMNGHVDCVHLLLEKGSTADAADLRGRTAL 725
Cdd:COG0666 217 NDGKTALDLAAENGNLEIVKLLLEAGADLNAK---DKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
148-493 |
2.11e-27 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 119.40 E-value: 2.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 148 VHSGHLETVNLLLNKGASLNVCDKKERQPLHWAAFLGHLEVLKLLVARGADLSCKDRKGYGLLHTAAASGQIEVVKHLLR 227
Cdd:PHA02876 153 IQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIID 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 228 MGAEIDEP-----NAFGNTALHiacylgqdaVAIELVNAGANVNQPNDKGFTPLHVAAVSTNGALCLELLVNNGADVNYQ 302
Cdd:PHA02876 233 NRSNINKNdlsllKAIRNEDLE---------TSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLVPKLLERGADVNAK 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 303 SKEGKSPLHMAAIHGRFTRS-QILIQNGSEIDCADKFGNTPLHVAARYG-HELLISTLMTNGADTARRGIHDMFPLHLAV 380
Cdd:PHA02876 304 NIKGETPLYLMAKNGYDTENiRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAA 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 381 LfgfsdccrkllssGQLYSIVSSLsnehvLSAGFDINTPDSLGRTCLHAAASGGN-VECLNLLLSSGADLRRRDKFGRTP 459
Cdd:PHA02876 384 V-------------RNNVVIINTL-----LDYGADIEALSQKIGTALHFALCGTNpYMSVKTLIDRGANVNSKNKDLSTP 445
|
330 340 350
....*....|....*....|....*....|....*
gi 27370168 460 LHYAAANG-SYQCAVTLVTAGAGVNEADCKGCSPL 493
Cdd:PHA02876 446 LHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPL 480
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
219-660 |
3.28e-26 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 113.58 E-value: 3.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 219 IEVVKHLLRMGAEIDEPNAFGNTALH--IACYLGQDAVAIE-LVNAGANVNQPNDKGFTPLHVAAVSTNGALCLELLVNN 295
Cdd:PHA03095 27 VEEVRRLLAAGADVNFRGEYGKTPLHlyLHYSSEKVKDIVRlLLEAGADVNAPERCGFTPLHLYLYNATTLDVIKLLIKA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 296 GADVNYQskegksplhmaaihgrftrsqiliqngseidcaDKFGNTPLHVaaryghellistlmtngadtarrgihdmfp 375
Cdd:PHA03095 107 GADVNAK---------------------------------DKVGRTPLHV------------------------------ 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 376 lHLAvlfgfSDCCRkllssgqlYSIVSSLsnehvLSAGFDINTPDSLGRTCLHA--AASGGNVECLNLLLSSGADLRRRD 453
Cdd:PHA03095 124 -YLS-----GFNIN--------PKVIRLL-----LRKGADVNALDLYGMTPLAVllKSRNANVELLRLLIDAGADVYAVD 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 454 KFGRTPLHYAAAN--GSYQCAVTLVTAGAGVNEADCKGCSPLHYAAASDTYRRAEphtasshdaeedellkesrrkeaff 531
Cdd:PHA03095 185 DRFRSLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSL------------------------- 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 532 cLEFLLDNGADPSLRDRQGYTAVHYAAAYGNRQNLELLLEMSFNCleDVESTVPVSPLHLAAYNGH----------CEAL 601
Cdd:PHA03095 240 -VLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADI--NAVSSDGNTPLSLMVRNNNgravraalakNPSA 316
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 27370168 602 KTLAETLVNLDVRDHKGRTAlflaterGSTECVEVLTAHGASALIKERKRKwtpLHAAA 660
Cdd:PHA03095 317 ETVAATLNTASVAGGDIPSD-------ATRLCVAKVVLRGAFSLLPEPIRA---YHADF 365
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
148-463 |
3.34e-24 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 106.97 E-value: 3.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 148 VHSGHLETV-NLLLNKGASLNVCDKKERQPLHWAAFLGHLEVLKLLVARGADLSCKDRKGYGLLHTAAASGQIEVVKHLL 226
Cdd:PHA02874 9 IYSGDIEAIeKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 227 RMGAEidepnafgNTALHIACyLGQDAVAIeLVNAGANVNQPNDKGFTPLHVAaVSTNGALCLELLVNNGADVNYQSKEG 306
Cdd:PHA02874 89 DNGVD--------TSILPIPC-IEKDMIKT-ILDCGIDVNIKDAELKTFLHYA-IKKGDLESIKMLFEYGADVNIEDDNG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 307 KSPLHMAAIHGRFTRSQILIQNGSEIDCADKFGNTPLHVAARYGHELLISTLMTNGADTARRGIHDMFPLHLAVLFGfsd 386
Cdd:PHA02874 158 CYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHN--- 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27370168 387 ccrkllssgqlYSIVSSLSNEHvlsagfDINTPDSLGRTCLHAAAS-GGNVECLNLLLSSGADLRRRDKFGRTPLHYA 463
Cdd:PHA02874 235 -----------RSAIELLINNA------SINDQDIDGSTPLHHAINpPCDIDIIDILLYHKADISIKDNKGENPIDTA 295
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
15-204 |
3.41e-23 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 103.59 E-value: 3.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 15 AIFSRDVEEVRSLLSQKENINVLDQERRTPLHAAAY--VGDVPILQLLLMSGANVNAKDTLWLTPLHRAAAS--RNEKVL 90
Cdd:PHA03100 80 YNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISkkSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESnkIDLKIL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 91 GLLLAHSADVNARDKLwqtplhvaaanratkcaEALAPLLSSLNVADRSGRSALHHAVHSGHLETVNLLLNKGASLNVCD 170
Cdd:PHA03100 160 KLLIDKGVDINAKNRV-----------------NYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVN 222
|
170 180 190
....*....|....*....|....*....|....
gi 27370168 171 KKERQPLHWAAFLGHLEVLKLLVARGADLSCKDR 204
Cdd:PHA03100 223 KYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
341-625 |
9.59e-23 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 102.73 E-value: 9.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 341 TPLHVAARYGHELLISTLMTNGADTARRGIHDMFPLHLAVLFGFSDCCRKLLSSGQLYSI--VSSLSNEHV---LSAGFD 415
Cdd:PHA02874 37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSIlpIPCIEKDMIktiLDCGID 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 416 INTPDSLGRTCLHAAASGGNVECLNLLLSSGADLRRRDKFGRTPLHYAAANGSYQCAVTLVTAGAGVNEADCKGCSPLHY 495
Cdd:PHA02874 117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHN 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 496 AAASDTYRraephtasshdaeedellkesrrkeaffCLEFLLDNGADPSLRDRQGYTAVHYAAAYgNRQNLELLLEMSFN 575
Cdd:PHA02874 197 AAEYGDYA----------------------------CIKLLIDHGNHIMNKCKNGFTPLHNAIIH-NRSAIELLINNASI 247
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 27370168 576 CLEDVESTvpvSPLHLA-AYNGHCEALKTLAETLVNLDVRDHKGRTALFLA 625
Cdd:PHA02874 248 NDQDIDGS---TPLHHAiNPPCDIDIIDILLYHKADISIKDNKGENPIDTA 295
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
11-246 |
1.59e-22 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 102.27 E-value: 1.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 11 PLVQAIFSRDVEEVRSLLSQKENINVLDQERRTPLH-------------------------------AAAYVGDVPILQL 59
Cdd:PHA02878 40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHiickepnklgmkemirsinkcsvfytlvaikDAFNNRNVEIFKI 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 60 LLMSGANVNAKDTLWLTPLHRAAASRNEKVLGLLLAHSADVNARDK-LWQTPLHVAAANRATKCAEALAPLLSSLNVADR 138
Cdd:PHA02878 120 ILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDK 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 139 SGRSALHHAVHSGHLETVNLLLNKGASLNVCDKKERQPLHWA-AFLGHLEVLKLLVARGADLSCKDR-KGYGLLHTAAAS 216
Cdd:PHA02878 200 TNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKS 279
|
250 260 270
....*....|....*....|....*....|
gi 27370168 217 GQieVVKHLLRMGAEIDEPNAFGNTALHIA 246
Cdd:PHA02878 280 ER--KLKLLLEYGADINSLNSYKLTPLSSA 307
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
24-332 |
7.35e-22 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 101.68 E-value: 7.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 24 VRSLLSQKENINVLDQERRTPLHAAAYVGDVPILQLLLMSGANVNAKDtlwltpLHRAAASRNEKVLGLLLAHSA--DVN 101
Cdd:PHA02876 194 VNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKND------LSLLKAIRNEDLETSLLLYDAgfSVN 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 102 ARDKLWQTPLHVAAanrATKCAEALAPLL----SSLNVADRSGRSALHHAVHSGH-LETVNLLLNKGASLNVCDKKERQP 176
Cdd:PHA02876 268 SIDDCKNTPLHHAS---QAPSLSRLVPKLlergADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITP 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 177 LHWAAFLG-HLEVLKLLVARGADLSCKDRKGYGLLHTAAASGQIEVVKHLLRMGAEIDEPNAFGNTALHIACYLGQDAVA 255
Cdd:PHA02876 345 LHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMS 424
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27370168 256 IE-LVNAGANVNQPNDKGFTPLHVAAVSTNGALCLELLVNNGADVNYQSKEGKSPLHMAAihGRFTRSQILIQNGSEI 332
Cdd:PHA02876 425 VKtLIDRGANVNSKNKDLSTPLHYACKKNCKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILLHYGAEL 500
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
75-358 |
1.15e-21 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 99.95 E-value: 1.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 75 LTPLHRAAASRNEKVLGLLLAHSADVNARDKLWQTPLHVAaanratkCAE----ALAPLLSSLNVADRS-GRSALHHAVH 149
Cdd:PHA02878 38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHII-------CKEpnklGMKEMIRSINKCSVFyTLVAIKDAFN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 150 SGHLETVN-LLLNKGASLNVCDKKERQPLHWAAFLgHLEVLKLLVARGADLSCKDR-KGYGLLHTAAASGQIEVVKHLLR 227
Cdd:PHA02878 111 NRNVEIFKiILTNRYKNIQTIDLVYIDKKSKDDII-EAEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 228 MGAEIDEPNAFGNTALHIACYLGQDAVAIELVNAGANVNQPNDKGFTPLHVAAVSTNGALCLELLVNNGADVNYQSK-EG 306
Cdd:PHA02878 190 YGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDYDILKLLLEHGVDVNAKSYiLG 269
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 27370168 307 KSPLHMaAIHGRfTRSQILIQNGSEIDCADKFGNTPLHVAA--RYGHE---LLISTL 358
Cdd:PHA02878 270 LTALHS-SIKSE-RKLKLLLEYGADINSLNSYKLTPLSSAVkqYLCINigrILISNI 324
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
604-985 |
6.84e-20 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 95.52 E-value: 6.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 604 LAETLVNLDVRDHKGRTALFLATERGSTECVEVLTAHGASALIKERKrKWTPLHAAAASGHTDSLHLLIDSGERADITDV 683
Cdd:PHA02876 164 LLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALD-DLSVLECAVDSKNIDTIKAIIDNRSNINKNDL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 684 mdaygqtPLMLAIMNGHVDCVHLLLEKGSTADAADLRGRTALHRGAVT-GCEDCLAALLDHDAFVLCRDFKGRTPIHLAS 762
Cdd:PHA02876 243 -------SLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQApSLSRLVPKLLERGADVNAKNIKGETPLYLMA 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 763 ACGH-TAVLRTLLQAalstdpldaGVDYSGYSPMHwasytghedclelllehspfsylegnpFTPLHCAVINNQDSTTEM 841
Cdd:PHA02876 316 KNGYdTENIRTLIML---------GADVNAADRLY---------------------------ITPLHQASTLDRNKDIVI 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 842 LLGALGAKiVNSRDAKGRTPLHAAAFADNVSGLRMLLQHQAEVNATDHTGRTALMTA-AESGQTAAVEFLLYRGkADLTV 920
Cdd:PHA02876 360 TLLELGAN-VNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRG-ANVNS 437
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27370168 921 LDENKNTALHLACSKgheKCALMILAETQDLGL-INATNSALQMPLHIAArnGLASVVQALLSRGA 985
Cdd:PHA02876 438 KNKDLSTPLHYACKK---NCKLDVIEMLLDNGAdVNAINIQNQYPLLIAL--EYHGIVNILLHYGA 498
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
10-233 |
9.63e-20 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 93.19 E-value: 9.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 10 PPLVQAIFSRDVEEVRSLLSQKENINVLDQERRTPLHAAAYVG-----DVPILQLLLMSGANVNAKDTLWLTPLHRAAA- 83
Cdd:PHA03100 37 LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKynltdVKEIVKLLLEYGANVNAPDNNGITPLLYAISk 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 84 -SRNEKVLGLLLAHSADVNARDKLWQTPLHVAAANRATKcAEALAPLLSS---LNVADRsgrsalhhavhsghletVNLL 159
Cdd:PHA03100 117 kSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKID-LKILKLLIDKgvdINAKNR-----------------VNYL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27370168 160 LNKGASLNVCDKKERQPLHWAAFLGHLEVLKLLVARGADLSCKDRKGYGLLHTAAASGQIEVVKHLLRMGAEID 233
Cdd:PHA03100 179 LSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
186-466 |
9.90e-20 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 93.19 E-value: 9.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 186 LEVLKLLVARGADLSCKDRKGYGLLHTAAASGQIEVVKHLLRMGAEIDEPNAFGNTALHIAC---YLGQDAVAIE--LVN 260
Cdd:PHA03100 15 VKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSnikYNLTDVKEIVklLLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 261 AGANVNQPNDKGFTPLHVAAVSTNGALCL-ELLVNNGADVNYQSKEGKSPLHMAA--IHGRFTRSQILIQNGSEIDCADK 337
Cdd:PHA03100 95 YGANVNAPDNNGITPLLYAISKKSNSYSIvEYLLDNGANVNIKNSDGENLLHLYLesNKIDLKILKLLIDKGVDINAKNR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 338 FgntplhvaaryghellistlmtngadtarrgihDMFplhlavlfgfsdccrkllssgqlysivsslsnehvLSAGFDIN 417
Cdd:PHA03100 175 V---------------------------------NYL-----------------------------------LSYGVPIN 186
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 27370168 418 TPDSLGRTCLHAAASGGNVECLNLLLSSGADLRRRDKFGRTPLHYAAAN 466
Cdd:PHA03100 187 IKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILN 235
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
589-898 |
2.01e-19 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 92.33 E-value: 2.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 589 LHLAAYNGHCEALKTLAETLVN-LDVRDHKGRTALFLATERGSTECVEVLTAHGASalIKERKRKW-TPLHAAAASGHTD 666
Cdd:PHA02874 5 LRMCIYSGDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGAD--INHINTKIpHPLLTAIKIGAHD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 667 SLHLLIDSGERADITDVMDAYGQTplmlaimnghvdcVHLLLEKGSTADAADLRGRTALHRGAVTGCEDCLAALLDHDAF 746
Cdd:PHA02874 83 IIKLLIDNGVDTSILPIPCIEKDM-------------IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGAD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 747 VLCRDFKGRTPIHLASACGHTAVLRTLLQ--AALSTDpldagvDYSGYSPMHWASYTGHEDCLELLLEH-SPFSYLEGNP 823
Cdd:PHA02874 150 VNIEDDNGCYPIHIAIKHNFFDIIKLLLEkgAYANVK------DNNGESPLHNAAEYGDYACIKLLIDHgNHIMNKCKNG 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27370168 824 FTPLHCAVINNQdSTTEMLlgaLGAKIVNSRDAKGRTPLH-AAAFADNVSGLRMLLQHQAEVNATDHTGRTALMTA 898
Cdd:PHA02874 224 FTPLHNAIIHNR-SAIELL---INNASINDQDIDGSTPLHhAINPPCDIDIIDILLYHKADISIKDNKGENPIDTA 295
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
144-462 |
1.11e-18 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 90.71 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 144 LHHAVHSGHLETVNLLLNKGASLNVCDKKERQPLHWAAFLGHLEVLKLLVArgadLSCKDRKGYGL--LHTAAASGQIEV 221
Cdd:PHA02878 41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIR----SINKCSVFYTLvaIKDAFNNRNVEI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 222 VKHLLrmgaeIDEPNAFGNTALHIACYLGQDAVaIE------LVNAGANVNQPN-DKGFTPLHVAAVSTNGALcLELLVN 294
Cdd:PHA02878 117 FKIIL-----TNRYKNIQTIDLVYIDKKSKDDI-IEaeitklLLSYGADINMKDrHKGNTALHYATENKDQRL-TELLLS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 295 NGADVNYQSKEGKSPLHMAAIHGRFTRSQILIQNGSEIDCADKFGNTPLHVAARYGHEL-LISTLMTNGAD-TARRGIHD 372
Cdd:PHA02878 190 YGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDYdILKLLLEHGVDvNAKSYILG 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 373 MFPLHLAVlfgFSDCCRKLLssgqlysivsslsnehvLSAGFDINTPDSLGRTCLHAAA-SGGNVECLNLLLSSGADLRR 451
Cdd:PHA02878 270 LTALHSSI---KSERKLKLL-----------------LEYGADINSLNSYKLTPLSSAVkQYLCINIGRILISNICLLKR 329
|
330
....*....|.
gi 27370168 452 RDKFGRTPLHY 462
Cdd:PHA02878 330 IKPDIKNSEGF 340
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
654-985 |
1.17e-18 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 90.47 E-value: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 654 TPLHAAAASGHTDSLHLLIDSGERADITDVM------------DAYGQTPLMLAIMNGHVDC---VHLLLEKGSTADAAD 718
Cdd:PHA03095 1 DEEDESVDIIMEAALYDYLLNASNVTVEEVRrllaagadvnfrGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 719 LRGRTALH---RGAVTgcEDCLAALLDHDAFVLCRDFKGRTPIH--LASACGHTAVLRTLLQAALSTDPLDAgvdySGYS 793
Cdd:PHA03095 81 RCGFTPLHlylYNATT--LDVIKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDL----YGMT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 794 PMHwaSYTGHEDC----LELLLEH-SPFSYLEGNPFTPLHCAVINNQDSTTEM-LLGALGAKiVNSRDAKGRTPLHAAAF 867
Cdd:PHA03095 155 PLA--VLLKSRNAnvelLRLLIDAgADVYAVDDRFRSLLHHHLQSFKPRARIVrELIRAGCD-PAATDMLGNTPLHSMAT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 868 ADNVSGLRM--LLQHQAEVNATDHTGRTALMTAAESGQTAAVEFLLYRGkADLTVLDENKNTALHLACSKGHEKCALMIL 945
Cdd:PHA03095 232 GSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALG-ADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 27370168 946 AETQDLGLINATNSALQMPLHIAARNGLASVVQALLSRGA 985
Cdd:PHA03095 311 AKNPSAETVAATLNTASVAGGDIPSDATRLCVAKVVLRGA 350
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
42-300 |
2.73e-18 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 88.51 E-value: 2.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 42 RTPLHAAAYVGDVPILQLLLMSGANVNAKDTLWLTPLHRAAASRNEKVLGLLLAHSA--DVNARDKlwqtplhvaaanra 119
Cdd:PHA02875 3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAipDVKYPDI-------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 120 tkcaealapllsslnvadrsgRSALHHAVHSGHLETVNLLLNKGASLN-VCDKKERQPLHWAAFLGHLEVLKLLVARGAD 198
Cdd:PHA02875 69 ---------------------ESELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGAD 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 199 LSCKDRKGYGLLHTAAASGQIEVVKHLLRMGAEIDEPNAFGNTALHIACYLGQDAVAIELVNAGANVNQPNDKGFTPLHV 278
Cdd:PHA02875 128 PDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALC 207
|
250 260
....*....|....*....|..
gi 27370168 279 AAVSTNGALCLELLVNNGADVN 300
Cdd:PHA02875 208 YAIENNKIDIVRLFIKRGADCN 229
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
589-682 |
3.08e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 80.55 E-value: 3.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 589 LHLAAYNGHCEALKTLAETLVNLDVRDHKGRTALFLATERGSTECVEVLTAHgasALIKERKRKWTPLHAAAASGHTDSL 668
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH---ADVNLKDNGRTALHYAARSGHLEIV 77
|
90
....*....|....
gi 27370168 669 HLLIDSGERADITD 682
Cdd:pfam12796 78 KLLLEKGADINVKD 91
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
247-563 |
3.77e-18 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 88.48 E-value: 3.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 247 CYLGQDAVAIE--LVNAGANVNQPNDKGFTPLhVAAVSTNGALCLELLVNNGADVNYQSKEGKSPLHMAAIHGRFTRSQI 324
Cdd:PHA02874 8 CIYSGDIEAIEkiIKNKGNCINISVDETTTPL-IDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 325 LIQNGSE-----------------IDCA------DKFGNTPLHVAARYGHELLISTLMTNGADTARRGIHDMFPLHLAVL 381
Cdd:PHA02874 87 LIDNGVDtsilpipciekdmiktiLDCGidvnikDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 382 FGFSDCCRKLLSSGQLysivsslsnehvlsagfdINTPDSLGRTCLHAAASGGNVECLNLLLSSGADLRRRDKFGRTPLH 461
Cdd:PHA02874 167 HNFFDIIKLLLEKGAY------------------ANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLH 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 462 YAAANGsyQCAVTLVTAGAGVNEADCKGCSPLHYAAasdtyrraepHTASSHDAeedellkesrrkeaffcLEFLLDNGA 541
Cdd:PHA02874 229 NAIIHN--RSAIELLINNASINDQDIDGSTPLHHAI----------NPPCDIDI-----------------IDILLYHKA 279
|
330 340
....*....|....*....|..
gi 27370168 542 DPSLRDRQGYTAVHYAAAYGNR 563
Cdd:PHA02874 280 DISIKDNKGENPIDTAFKYINK 301
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
519-929 |
6.57e-18 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 88.97 E-value: 6.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 519 ELLKESRRKEAFFCLEFLLDNGADPSLRDRQGYTAVHYAAAYGNRQNLELLLemSFNCLEDVESTVPVSPLHLAAYNGHC 598
Cdd:PHA02876 147 KLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLL--SYGADVNIIALDDLSVLECAVDSKNI 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 599 EALKTLAETLVNLDVRDhkgrTALFLATERGSTECVEVLTAHGASA-LIKERKRkwTPLHAAAasgHTDSLHLLIDS-GE 676
Cdd:PHA02876 225 DTIKAIIDNRSNINKND----LSLLKAIRNEDLETSLLLYDAGFSVnSIDDCKN--TPLHHAS---QAPSLSRLVPKlLE 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 677 RADITDVMDAYGQTPLMLAIMNGH-VDCVHLLLEKGSTADAADLRGRTALHRGA-VTGCEDCLAALLDHDAFVLCRDFKG 754
Cdd:PHA02876 296 RGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQAStLDRNKDIVITLLELGANVNARDYCD 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 755 RTPIHLASACGHTAVLRTLLQAALSTDPLDAGVDysgySPMHWASYTghedclelllehspfsyleGNPFTPLHCAVINN 834
Cdd:PHA02876 376 KTPIHYAAVRNNVVIINTLLDYGADIEALSQKIG----TALHFALCG-------------------TNPYMSVKTLIDRG 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 835 QDsttemllgalgakiVNSRDAKGRTPLHAAAFAD-NVSGLRMLLQHQAEVNATDHTGRTALMTAAesGQTAAVEFLLYR 913
Cdd:PHA02876 433 AN--------------VNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILLHY 496
|
410
....*....|....*...
gi 27370168 914 GKA--DLTVLDENKNTAL 929
Cdd:PHA02876 497 GAElrDSRVLHKSLNDNM 514
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
111-203 |
3.68e-17 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 77.46 E-value: 3.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 111 LHVAAANRATKCAEALAPLLSSLNVADRSGRSALHHAVHSGHLETVNLLLNKgASLNVCDKKeRQPLHWAAFLGHLEVLK 190
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNG-RTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 27370168 191 LLVARGADLSCKD 203
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
11-198 |
4.26e-17 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 85.04 E-value: 4.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 11 PLVQAIFSRDVEEVRSLLSQKENINVLDQERRTPLHAAAYVGDVPILQLLLMSGANVNakDTLW---LTPLHRAAASRNE 87
Cdd:PHA02875 38 PIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAD--DVFYkdgMTPLHLATILKKL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 88 KVLGLLLAHSADVNARDKLWQTPLHVAAANRATKCAEALAPLLSSLNVADRSGRSALHHAVHSGHLETVNLLLNKGASLN 167
Cdd:PHA02875 116 DIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANID 195
|
170 180 190
....*....|....*....|....*....|..
gi 27370168 168 VCDKK-ERQPLHWAAFLGHLEVLKLLVARGAD 198
Cdd:PHA02875 196 YFGKNgCVAALCYAIENNKIDIVRLFIKRGAD 227
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
144-236 |
5.18e-17 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 77.08 E-value: 5.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 144 LHHAVHSGHLETVNLLLNKGASLNVCDKKERQPLHWAAFLGHLEVLKLLVARgADLSCKDrKGYGLLHTAAASGQIEVVK 223
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 27370168 224 HLLRMGAEIDEPN 236
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
656-751 |
6.23e-17 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 76.69 E-value: 6.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 656 LHAAAASGHTDSLHLLIDSGERADitdVMDAYGQTPLMLAIMNGHVDCVHLLLEKGSTADaaDLRGRTALHRGAVTGCED 735
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADAN---LQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLE 75
|
90
....*....|....*.
gi 27370168 736 CLAALLDHDAFVLCRD 751
Cdd:pfam12796 76 IVKLLLEKGADINVKD 91
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
533-730 |
6.27e-17 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 84.66 E-value: 6.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 533 LEFLLDNGADPSLRDRQGYTAVHYAAAYGNRQNLELLleMSFNCLEDVESTVPVSPLHLAAYNGHCEALKTL--AETLVN 610
Cdd:PHA02875 18 ARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLL--MKHGAIPDVKYPDIESELHDAVEEGDVKAVEELldLGKFAD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 611 lDVRDHKGRTALFLATERGSTECVEVLTAHGASALIKERKRkWTPLHAAAASGHTDSLHLLIDsgERAdITDVMDAYGQT 690
Cdd:PHA02875 96 -DVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDK-FSPLHLAVMMGDIKGIELLID--HKA-CLDIEDCCGCT 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 27370168 691 PLMLAIMNGHVDCVHLLLEKGSTADAADLRGRTALHRGAV 730
Cdd:PHA02875 171 PLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAI 210
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
599-895 |
1.04e-16 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 84.31 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 599 EALKTLAETLVNLDVRDHKGRTALFLATERGSTECVEV---LTAHGASALIKERKrKWTPLHAAAASGHT-DSLHLLIDS 674
Cdd:PHA03095 28 EEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERC-GFTPLHLYLYNATTlDVIKLLIKA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 675 GerADITDVmDAYGQTPL--MLAIMNGHVDCVHLLLEKGSTADAADLRGRTALH-----RGAvtgCEDCLAALLDHDAFV 747
Cdd:PHA03095 107 G--ADVNAK-DKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAvllksRNA---NVELLRLLIDAGADV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 748 LCRDFKGRTP--IHLASACGHTAVLRTLLqaALSTDPldAGVDYSGYSPMHwaSYTGHEDCLELLLehSPFsylegnpft 825
Cdd:PHA03095 181 YAVDDRFRSLlhHHLQSFKPRARIVRELI--RAGCDP--AATDMLGNTPLH--SMATGSSCKRSLV--LPL--------- 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 826 plhcaVINNQDsttemllgalgakiVNSRDAKGRTPLHAAAFADNVSGLRMLLQHQAEVNATDHTGRTAL 895
Cdd:PHA03095 244 -----LIAGIS--------------INARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL 294
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
436-789 |
1.86e-16 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 83.54 E-value: 1.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 436 VECLNLLLSSGADLRRRDKFGRTPLHYAAANGSYQCA---VTLVTAGAGVNEADCKGCSPLHYAAasdtyrraephtasS 512
Cdd:PHA03095 27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKdivRLLLEAGADVNAPERCGFTPLHLYL--------------Y 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 513 HDAEEDellkesrrkeaffCLEFLLDNGADPSLRDRQGYTAVHyaaaygnrqnlelllemsfncledvestvpvspLHLA 592
Cdd:PHA03095 93 NATTLD-------------VIKLLIKAGADVNAKDKVGRTPLH---------------------------------VYLS 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 593 AYNGHCEALKTLAETLVNLDVRDHKGRTAL--FLATERGSTECVEVLTAHGASALIKERKRKwTPLHAAAASGHTDS--L 668
Cdd:PHA03095 127 GFNINPKVIRLLLRKGADVNALDLYGMTPLavLLKSRNANVELLRLLIDAGADVYAVDDRFR-SLLHHHLQSFKPRAriV 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 669 HLLIDSGERADITDVmdaYGQTPLMLAIMngHVDCVHL----LLEKGSTADAADLRGRTALHRGAVTG----CEDCLAAL 740
Cdd:PHA03095 206 RELIRAGCDPAATDM---LGNTPLHSMAT--GSSCKRSlvlpLLIAGISINARNRYGQTPLHYAAVFNnpraCRRLIALG 280
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 27370168 741 LDhdafVLCRDFKGRTPIHLASACGHTAVLRTLLQAALSTDPLDAGVDY 789
Cdd:PHA03095 281 AD----INAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAATLNT 325
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
210-302 |
3.39e-16 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 74.77 E-value: 3.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 210 LHTAAASGQIEVVKHLLRMGAEIDEPNAFGNTALHIACYLGQDAVAIELVNaGANVNqPNDKGFTPLHVAAVSTNGAlCL 289
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVN-LKDNGRTALHYAARSGHLE-IV 77
|
90
....*....|...
gi 27370168 290 ELLVNNGADVNYQ 302
Cdd:pfam12796 78 KLLLEKGADINVK 90
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
177-269 |
4.20e-16 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 74.38 E-value: 4.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 177 LHWAAFLGHLEVLKLLVARGADLSCKDRKGYGLLHTAAASGQIEVVKHLLRmGAEIDEPNaFGNTALHIACYLGQDAVAI 256
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 27370168 257 ELVNAGANVNQPN 269
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
862-955 |
1.20e-15 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 73.23 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 862 LHAAAFADNVSGLRMLLQHQAEVNATDHTGRTALMTAAESGQTAAVEFLLYRGKADltvLDENKNTALHLACSKGHEKCA 941
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN---LKDNGRTALHYAARSGHLEIV 77
|
90
....*....|....
gi 27370168 942 LMILAETQDLGLIN 955
Cdd:pfam12796 78 KLLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
622-718 |
1.42e-15 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 72.84 E-value: 1.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 622 LFLATERGSTECVEVLTAHGASALIKErKRKWTPLHAAAASGHTDSLHLLIDSGeRADITDvmdaYGQTPLMLAIMNGHV 701
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQD-KNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKD----NGRTALHYAARSGHL 74
|
90
....*....|....*..
gi 27370168 702 DCVHLLLEKGSTADAAD 718
Cdd:pfam12796 75 EIVKLLLEKGADINVKD 91
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
12-194 |
1.55e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 80.39 E-value: 1.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 12 LVQAIFSRDVEEVRSLLSQKENINVLDQERRTPLHAAAYVGDVPILQLLLMSGANVNAKDTLWLTPLHRAAASRNEKVLG 91
Cdd:PHA02874 128 LHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIK 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 92 LLLAHSADVNARDKLWQTPLHVAAA-NRATkcaealAPLL---SSLNVADRSGRSALHHAVH-SGHLETVNLLLNKGASL 166
Cdd:PHA02874 208 LLIDHGNHIMNKCKNGFTPLHNAIIhNRSA------IELLinnASINDQDIDGSTPLHHAINpPCDIDIIDILLYHKADI 281
|
170 180
....*....|....*....|....*....
gi 27370168 167 NVCDKKERQPLHWA-AFLGHLEVLKLLVA 194
Cdd:PHA02874 282 SIKDNKGENPIDTAfKYINKDPVIKDIIA 310
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
12-104 |
3.25e-15 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 72.07 E-value: 3.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 12 LVQAIFSRDVEEVRSLLSQKENINVLDQERRTPLHAAAYVGDVPILQLLLmSGANVNAKDTLWlTPLHRAAASRNEKVLG 91
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKDNGR-TALHYAARSGHLEIVK 78
|
90
....*....|...
gi 27370168 92 LLLAHSADVNARD 104
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
8-199 |
9.74e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 78.95 E-value: 9.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 8 DQPPLVQAIFSRDVEEVRSLLSQKENINVLDQERRTPLHAAAYVG-DVPILQLLLMSGANVNAKDTLWLTPLHRAAASRN 86
Cdd:PHA02876 308 ETPLYLMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNN 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 87 EKVLGLLLAHSADVNARDKLWQTPLHVA-AANRATKCAEALAPLLSSLNVADRSGRSALHHAVHSG-HLETVNLLLNKGA 164
Cdd:PHA02876 388 VVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGA 467
|
170 180 190
....*....|....*....|....*....|....*
gi 27370168 165 SLNVCDKKERQPLHWAafLGHLEVLKLLVARGADL 199
Cdd:PHA02876 468 DVNAINIQNQYPLLIA--LEYHGIVNILLHYGAEL 500
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
397-718 |
1.34e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 77.40 E-value: 1.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 397 LYSIVS-------SLSNEHVLSAGFDINTPDSLGRT-CLHAAASGGNVECLNLLLSSGADLRRRDKFGRTPLHYAAANGS 468
Cdd:PHA03100 1 LYSYIVltksriiKVKNIKYIIMEDDLNDYSYKKPVlPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 469 YQCAVT-----LVTAGAGVNEADCKGCSPLHYAAasdtyrraephtasshdaeedellkeSRRKEAFFCLEFLLDNGADP 543
Cdd:PHA03100 81 NLTDVKeivklLLEYGANVNAPDNNGITPLLYAI--------------------------SKKSNSYSIVEYLLDNGANV 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 544 SLRDRQGYTAVHYAAAYgNRQNLELllemsfncledvestvpvsplhlaaynghceaLKTLAETLVNLDVRDHkgrtalf 623
Cdd:PHA03100 135 NIKNSDGENLLHLYLES-NKIDLKI--------------------------------LKLLIDKGVDINAKNR------- 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 624 latergstecVEVLTAHGASALIKErKRKWTPLHAAAASGHTDSLHLLIDSGerADITDVMDaYGQTPLMLAIMNGHVDC 703
Cdd:PHA03100 175 ----------VNYLLSYGVPINIKD-VYGFTPLHYAVYNNNPEFVKYLLDLG--ANPNLVNK-YGDTPLHIAILNNNKEI 240
|
330
....*....|....*
gi 27370168 704 VHLLLEKGSTADAAD 718
Cdd:PHA03100 241 FKLLLNNGPSIKTII 255
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
376-486 |
1.37e-14 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 70.14 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 376 LHLAVLFGFSDCCRKLLSSGqlysivsslsnehvlsagFDINTPDSLGRTCLHAAASGGNVECLNLLLSSgADLRRRDKf 455
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENG------------------ADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN- 60
|
90 100 110
....*....|....*....|....*....|.
gi 27370168 456 GRTPLHYAAANGSYQCAVTLVTAGAGVNEAD 486
Cdd:pfam12796 61 GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
427-547 |
1.59e-14 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 70.14 E-value: 1.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 427 LHAAASGGNVECLNLLLSSGADLRRRDKFGRTPLHYAAANGSYQCAVTLVTAGAGvnEADCKGCSPLHYAAasdtyrrae 506
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAA--------- 69
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 27370168 507 phtasshdaeedellkESRRKEaffCLEFLLDNGADPSLRD 547
Cdd:pfam12796 70 ----------------RSGHLE---IVKLLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
692-775 |
1.64e-14 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 70.14 E-value: 1.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 692 LMLAIMNGHVDCVHLLLEKGSTADAADLRGRTALHRGAVTGCEDCLAALLDHdaFVLCRDFKGRTPIHLASACGHTAVLR 771
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH--ADVNLKDNGRTALHYAARSGHLEIVK 78
|
....
gi 27370168 772 TLLQ 775
Cdd:pfam12796 79 LLLE 82
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
74-284 |
1.65e-14 |
|
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: 78.13 E-value: 1.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 74 WLTPLHRAAASRN-EKVLGLLLAHSADVNARDKLWQTPLHVAAANRATKCAEAL---APLLssLNVADRS----GRSALH 145
Cdd:cd22192 17 SESPLLLAAKENDvQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLmeaAPEL--VNEPMTSdlyqGETALH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 146 HAVHSGHLETVNLLLNKGASL---------------NVCDKKErQPLHWAAFLGHLEVLKLLVARGADLSCKDRKGYGLL 210
Cdd:cd22192 95 IAVVNQNLNLVRELIARGADVvspratgtffrpgpkNLIYYGE-HPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27370168 211 HTAAASGQIEVVKHLLRMGAEIDEPnafgntalhiacylgQDAVAIELVnaganvnqPNDKGFTPLHVAAVSTN 284
Cdd:cd22192 174 HILVLQPNKTFACQMYDLILSYDKE---------------DDLQPLDLV--------PNNQGLTPFKLAAKEGN 224
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
740-993 |
1.92e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 77.80 E-value: 1.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 740 LLDHDAFVLCRDFKGRTPIHLASACGHTAVLRTLLQ--AALSTDPLDagvdysGYSPMHWASYTGHEDCLELLLEHSpfS 817
Cdd:PHA02876 164 LLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSygADVNIIALD------DLSVLECAVDSKNIDTIKAIIDNR--S 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 818 YLEGNPFTPLHcaVINNQDSTTEMLLGALGAKiVNSRDAKGRTPLHAAAFADNVSGL-RMLLQHQAEVNATDHTGRTALM 896
Cdd:PHA02876 236 NINKNDLSLLK--AIRNEDLETSLLLYDAGFS-VNSIDDCKNTPLHHASQAPSLSRLvPKLLERGADVNAKNIKGETPLY 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 897 TAAESG-QTAAVEFLLYRGkADLTVLDENKNTALHLACSKGHEKCALMILAEtqdLGL-INATNSALQMPLHIAARNGLA 974
Cdd:PHA02876 313 LMAKNGyDTENIRTLIMLG-ADVNAADRLYITPLHQASTLDRNKDIVITLLE---LGAnVNARDYCDKTPIHYAAVRNNV 388
|
250
....*....|....*....
gi 27370168 975 SVVQALLSRGATVLAVDEE 993
Cdd:PHA02876 389 VIINTLLDYGADIEALSQK 407
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
3-118 |
1.92e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 77.23 E-value: 1.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 3 ILSITDQPPLVQAIFSRDVEEVRSLLSQKENINVLDQERRTPLH-AAAYVGDVPILQLLLMSGANVNAKDT-LWLTPLHr 80
Cdd:PHA02878 196 IPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHiSVGYCKDYDILKLLLEHGVDVNAKSYiLGLTALH- 274
|
90 100 110
....*....|....*....|....*....|....*...
gi 27370168 81 aAASRNEKVLGLLLAHSADVNARDKLWQTPLHVAAANR 118
Cdd:PHA02878 275 -SSIKSERKLKLLLEYGADINSLNSYKLTPLSSAVKQY 311
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
45-137 |
2.56e-14 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 69.37 E-value: 2.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 45 LHAAAYVGDVPILQLLLMSGANVNAKDTLWLTPLHRAAASRNEKVLGLLLAHsADVNARDKLWqTPLHVAAANRATKCAE 124
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGR-TALHYAARSGHLEIVK 78
|
90
....*....|...
gi 27370168 125 ALAPLLSSLNVAD 137
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
895-991 |
5.37e-14 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 68.60 E-value: 5.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 895 LMTAAESGQTAAVEFLLYRGkADLTVLDENKNTALHLACSKGHEKCAlMILAETQDLGLINATNSalqmPLHIAARNGLA 974
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKNGHLEIV-KLLLEHADVNLKDNGRT----ALHYAARSGHL 74
|
90
....*....|....*..
gi 27370168 975 SVVQALLSRGATVLAVD 991
Cdd:pfam12796 75 EIVKLLLEKGADINVKD 91
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
48-284 |
8.31e-14 |
|
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: 75.89 E-value: 8.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 48 AAYVGDVPILQLLLMSGA--NVNAKDTLWLTPLHRAAA-SRNEKVLGLLLAHSADVNARDKLwqtpLHVAAANRATKCAE 124
Cdd:TIGR00870 24 AAERGDLASVYRDLEEPKklNINCPDRLGRSALFVAAIeNENLELTELLLNLSCRGAVGDTL----LHAISLEYVDAVEA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 125 ALAPLL-------SSLNVADRS------GRSALHHAVHSGHLETVNLLLNKGASLNV------CDKKERQ--------PL 177
Cdd:TIGR00870 100 ILLHLLaafrksgPLELANDQYtseftpGITALHLAAHRQNYEIVKLLLERGASVPAracgdfFVKSQGVdsfyhgesPL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 178 HWAAFLGHLEVLKLLVARGADLSCKDRKGYGLLhtaaasgqievvkHLLRMGAEidepNAFGNTALHIACY------LGQ 251
Cdd:TIGR00870 180 NAAACLGSPSIVALLSEDPADILTADSLGNTLL-------------HLLVMENE----FKAEYEELSCQMYnfalslLDK 242
|
250 260 270
....*....|....*....|....*....|....*
gi 27370168 252 --DAVAIELVnaganvnqPNDKGFTPLHVAAVSTN 284
Cdd:TIGR00870 243 lrDSKELEVI--------LNHQGLTPLKLAAKEGR 269
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
141-408 |
1.10e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 74.26 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 141 RSALHHAVHSGHLETVNLLLNKGASLNVCDKKERQPLHWAAFLGHLEVLKLLVARGADLSCKDRKGYGLLHTAAASGQIE 220
Cdd:PHA02875 3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 221 VVKHLLRMGAEIDEpnafgntalhiACYlgqdavaielvnaganvnqpnDKGFTPLHVAAVSTNGALcLELLVNNGADVN 300
Cdd:PHA02875 83 AVEELLDLGKFADD-----------VFY---------------------KDGMTPLHLATILKKLDI-MKLLIARGADPD 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 301 YQSKEGKSPLHMAAIHGRFTRSQILIQNGSEIDCADKFGNTPLHVAARYGHELLISTLMTNGADT---ARRGihDMFPLH 377
Cdd:PHA02875 130 IPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIdyfGKNG--CVAALC 207
|
250 260 270
....*....|....*....|....*....|.
gi 27370168 378 LAVLFGFSDCCRKLLSSGQLYSIVSSLSNEH 408
Cdd:PHA02875 208 YAIENNKIDIVRLFIKRGADCNIMFMIEGEE 238
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
596-872 |
1.22e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 74.26 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 596 GHCEALKTLAETLVNLDVRDHKGRTALFLATERGSTECVEVLTAHGASALIKERKRKwTPLHAAAASGHTDSLHLLIDSG 675
Cdd:PHA02875 13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIE-SELHDAVEEGDVKAVEELLDLG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 676 ERADitDVMDAYGQTPLMLAIMNGHVDCVHLLLEKGSTADAADLRGRTALHRGAVTGCEDCLAALLDHDAFVLCRDFKGR 755
Cdd:PHA02875 92 KFAD--DVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGC 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 756 TPIHLASACGHTAVLRTLLQAAlstdpldAGVDYSGYSP----MHWASYTGHEDCLELLLEHSP----FSYLEGNPFTPL 827
Cdd:PHA02875 170 TPLIIAMAKGDIAICKMLLDSG-------ANIDYFGKNGcvaaLCYAIENNKIDIVRLFIKRGAdcniMFMIEGEECTIL 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 27370168 828 HcaVINNQDSTTEM-LLGALGAKIVNSRDAKgrTPLHAAAFADNVS 872
Cdd:PHA02875 243 D--MICNMCTNLESeAIDALIADIAIRIHKK--TIRRDEGFKNNMS 284
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
441-761 |
4.83e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 73.56 E-value: 4.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 441 LLLSSGADLRRRDKFGRTPLHYAAANGSYQCAVTLVTAGAGVNEADCKGCSPLHYAAAS---DTYrRAEPHTASSHDAEE 517
Cdd:PHA02876 163 MLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSkniDTI-KAIIDNRSNINKND 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 518 DELLKESRRKEAFFCLeFLLDNGadpslrdrqgytavhyaaaygnrqnlellleMSFNCLEDVESTvpvsPLHLAAYNGH 597
Cdd:PHA02876 242 LSLLKAIRNEDLETSL-LLYDAG-------------------------------FSVNSIDDCKNT----PLHHASQAPS 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 598 CEAL-KTLAETLVNLDVRDHKGRTALFLATERG-STECVEVLTAHGASALIKERKRKwTPLHAAAA-SGHTDSLHLLIDS 674
Cdd:PHA02876 286 LSRLvPKLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYI-TPLHQASTlDRNKDIVITLLEL 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 675 GERadiTDVMDAYGQTPLMLAIMNGHVDCVHLLLEKGSTADAADLRGRTALHRgAVTGCEDCLA--ALLDHDAFVLCRDF 752
Cdd:PHA02876 365 GAN---VNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHF-ALCGTNPYMSvkTLIDRGANVNSKNK 440
|
....*....
gi 27370168 753 KGRTPIHLA 761
Cdd:PHA02876 441 DLSTPLHYA 449
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
233-477 |
5.13e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 72.61 E-value: 5.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 233 DEPNAFGNTALHIACYLGQDAVAIELVNAGANVNQPNDKGFTPLHVAAVSTN---------------------------- 284
Cdd:PHA02878 31 TSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNklgmkemirsinkcsvfytlvaikdafn 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 285 -----------------------------------GALCLELLVNNGADVNYQSKE-GKSPLHMAAIHGRFTRSQILIQN 328
Cdd:PHA02878 111 nrnveifkiiltnrykniqtidlvyidkkskddiiEAEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSY 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 329 GSEIDCADKFGNTPLHVAARYGHELLISTLMTNGADTARRGIHDMFPLHLAVlfgfsdccrkllSSGQLYSIVSSLsneh 408
Cdd:PHA02878 191 GANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISV------------GYCKDYDILKLL---- 254
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27370168 409 vLSAGFDINTPDS-LGRTCLHAAASGGNVecLNLLLSSGADLRRRDKFGRTPLHYAAANGS-YQCAVTLVT 477
Cdd:PHA02878 255 -LEHGVDVNAKSYiLGLTALHSSIKSERK--LKLLLEYGADINSLNSYKLTPLSSAVKQYLcINIGRILIS 322
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
209-345 |
6.48e-13 |
|
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: 72.74 E-value: 6.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 209 LLHTAAASGQIEVVKHLLRM-GAEIDEPNAFGNTALHIACYLGQDAVAIELVNAGAN-VNQPND----KGFTPLHVAAVS 282
Cdd:cd22192 20 PLLLAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEPMTsdlyQGETALHIAVVN 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27370168 283 TNGALcLELLVNNGADVN-------YQSKEGKS-------PLHMAAIHGRFTRSQILIQNGSEIDCADKFGNTPLHV 345
Cdd:cd22192 100 QNLNL-VRELIARGADVVspratgtFFRPGPKNliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
9-168 |
1.01e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 71.56 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 9 QPPLVQAIFSRDVEEVRSLLSQKENIN-VLDQERRTPLHAAAYVGDVPILQLLLMSGANVNAKDTLWLTPLHRAAASRNE 87
Cdd:PHA02875 69 ESELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 88 KVLGLLLAHSADVNARDKLWQTPLHVAAANRATKCAEALAPLLSSLNVADRSGR-SALHHAVHSGHLETVNLLLNKGASL 166
Cdd:PHA02875 149 KGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADC 228
|
..
gi 27370168 167 NV 168
Cdd:PHA02875 229 NI 230
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
536-761 |
1.44e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 71.15 E-value: 1.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 536 LLDNGADPSLRDRQGYTAVHYAAAYGNRQNLELLLEMSFNC-LEDVESTVPVsplHLAAYNGHCEALKTLAETLVNLDVR 614
Cdd:PHA02874 110 ILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVnIEDDNGCYPI---HIAIKHNFFDIIKLLLEKGAYANVK 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 615 DHKGRTALFLATERGSTECVEVLTAHGASALIKeRKRKWTPLHAAAasghtdslhllidsgeraditdvmdAYGQTPLML 694
Cdd:PHA02874 187 DNNGESPLHNAAEYGDYACIKLLIDHGNHIMNK-CKNGFTPLHNAI-------------------------IHNRSAIEL 240
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27370168 695 AIMNghvdcvhlllekgSTADAADLRGRTALHRGAVTGCE-DCLAALLDHDAFVLCRDFKGRTPIHLA 761
Cdd:PHA02874 241 LINN-------------ASINDQDIDGSTPLHHAINPPCDiDIIDILLYHKADISIKDNKGENPIDTA 295
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
310-395 |
1.64e-12 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 64.37 E-value: 1.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 310 LHMAAIHGRFTRSQILIQNGSEIDCADKFGNTPLHVAARYGHELLISTLMTNGAdtARRGIHDMFPLHLAVLFGFSDCCR 389
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78
|
....*.
gi 27370168 390 KLLSSG 395
Cdd:pfam12796 79 LLLEKG 84
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
276-364 |
1.94e-12 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 63.98 E-value: 1.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 276 LHVAAVStNGALCLELLVNNGADVNYQSKEGKSPLHMAAIHGRFTRSQILIQNGsEIDCADKfGNTPLHVAARYGHELLI 355
Cdd:pfam12796 1 LHLAAKN-GNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKDN-GRTALHYAARSGHLEIV 77
|
....*....
gi 27370168 356 STLMTNGAD 364
Cdd:pfam12796 78 KLLLEKGAD 86
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
265-571 |
2.14e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 70.46 E-value: 2.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 265 VNQPNDKGFTPLHVAAVSTNGALCLELLVNNGADVNYQSKEGKSPLHMAA-IHGRFTR----SQILIQNGSEIDCADKFG 339
Cdd:PHA03100 27 LNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSnIKYNLTDvkeiVKLLLEYGANVNAPDNNG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 340 NTPLHVAA--RYGHELLISTLMTNGADT---ARRGIHdmfPLHLAVlfgfSDCCRKLlssgqlySIVSSLsnehvLSAGF 414
Cdd:PHA03100 107 ITPLLYAIskKSNSYSIVEYLLDNGANVnikNSDGEN---LLHLYL----ESNKIDL-------KILKLL-----IDKGV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 415 DINTPDSLgrtclhaaasggnveclNLLLSSGADlrrrdkfgrtplhyaaangsyqcavtlvtagagVNEADCKGCSPLH 494
Cdd:PHA03100 168 DINAKNRV-----------------NYLLSYGVP---------------------------------INIKDVYGFTPLH 197
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27370168 495 YAAasdtyrraephtasSHDAEEdellkesrrkeaFFclEFLLDNGADPSLRDRQGYTAVHYAAAYGNRQNLELLLE 571
Cdd:PHA03100 198 YAV--------------YNNNPE------------FV--KYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLN 246
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
555-647 |
2.50e-12 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 63.60 E-value: 2.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 555 HYAAAYGNRQNLELLLEMSFNCleDVESTVPVSPLHLAAYNGHCEALKTLAETlVNLDVRDHkGRTALFLATERGSTECV 634
Cdd:pfam12796 2 HLAAKNGNLELVKLLLENGADA--NLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIV 77
|
90
....*....|...
gi 27370168 635 EVLTAHGASALIK 647
Cdd:pfam12796 78 KLLLEKGADINVK 90
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
343-453 |
2.92e-12 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 63.60 E-value: 2.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 343 LHVAARYGHELLISTLMTNGADTARRGIHDMFPLHLAVLFGFSDCCRKLLSSgqlysivsslsnehvlsagFDINTPDSl 422
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-------------------ADVNLKDN- 60
|
90 100 110
....*....|....*....|....*....|.
gi 27370168 423 GRTCLHAAASGGNVECLNLLLSSGADLRRRD 453
Cdd:pfam12796 61 GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
522-789 |
3.13e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 70.08 E-value: 3.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 522 KESRRKEAffcLEFLLDNGADPSLRDRQGYTAVHYAAAYGNrqnlelllemsfncledVESTVPvsplhlaaynghcEAL 601
Cdd:PHA03100 43 KEARNIDV---VKILLDNGADINSSTKNNSTPLHYLSNIKY-----------------NLTDVK-------------EIV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 602 KTLAETLVNLDVRDHKGRTALFLA--TERGSTECVEVLTAHGASALIKeRKRKWTPLHAAAASGHTDS--LHLLIDSGer 677
Cdd:PHA03100 90 KLLLEYGANVNAPDNNGITPLLYAisKKSNSYSIVEYLLDNGANVNIK-NSDGENLLHLYLESNKIDLkiLKLLIDKG-- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 678 ADItDVMDAygqtplmlaimnghvdcVHLLLEKGSTADAADLRGRTALHRGAVTGCEDCLAALLDHDAFVLCRDFKGRTP 757
Cdd:PHA03100 167 VDI-NAKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTP 228
|
250 260 270
....*....|....*....|....*....|..
gi 27370168 758 IHLASACGHTAVLRTLLQAALSTDPLDAGVDY 789
Cdd:PHA03100 229 LHIAILNNNKEIFKLLLNNGPSIKTIIETLLY 260
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
459-761 |
3.72e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 69.91 E-value: 3.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 459 PLHYAAANGSYQCAVTLVTAGAGVNEADCKGCSPLHYAAAsdtyrraEPHTASShdaeeDELLKESrrkeaffcleflld 538
Cdd:PHA02878 40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICK-------EPNKLGM-----KEMIRSI-------------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 539 ngadpsLRDRQGYTAVHYAAAYGNRqNLELLLEMSFNCLeDVESTVPVSPLHLAAYNGHCEA--LKTLAETLVNLDVRD- 615
Cdd:PHA02878 94 ------NKCSVFYTLVAIKDAFNNR-NVEIFKIILTNRY-KNIQTIDLVYIDKKSKDDIIEAeiTKLLLSYGADINMKDr 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 616 HKGRTALFLATERGSTECVEVLTAHGASALIKERKRKwTPLHAAAASGHTDSLHLLIDSGERadiTDVMDAYGQTPLMLA 695
Cdd:PHA02878 166 HKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNN-SPLHHAVKHYNKPIVHILLENGAS---TDARDKCGNTPLHIS 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 696 ImnGHV---DCVHLLLEKGSTADA-ADLRGRTALHRGAVTgcEDCLAALLDHDAFVLCRDFKGRTPIHLA 761
Cdd:PHA02878 242 V--GYCkdyDILKLLLEHGVDVNAkSYILGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSA 307
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
342-592 |
8.97e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 68.75 E-value: 8.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 342 PLHVAARYGHELLISTLMTNGADTARRGIHDMFPLHLAV----LFGFSDCCRKLLS---SGQLYSIVSSLSNEHV----- 409
Cdd:PHA02878 40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICkepnKLGMKEMIRSINKcsvFYTLVAIKDAFNNRNVeifki 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 410 -LSAGFDINTPDSLGRTCLHAAASGGNVECLNLLLSSGADLRRRDK-FGRTPLHYAAANGSYQCAVTLVTAGAGVNEADC 487
Cdd:PHA02878 120 iLTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDK 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 488 KGCSPLHYAaasdtyrraephtasshdaeedelLKESRRKeaffCLEFLLDNGADPSLRDRQGYTAVHYAAAY-GNRQNL 566
Cdd:PHA02878 200 TNNSPLHHA------------------------VKHYNKP----IVHILLENGASTDARDKCGNTPLHISVGYcKDYDIL 251
|
250 260
....*....|....*....|....*.
gi 27370168 567 ELLLEMSfNCLEDVESTVPVSPLHLA 592
Cdd:PHA02878 252 KLLLEHG-VDVNAKSYILGLTALHSS 276
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
795-888 |
9.40e-12 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 62.06 E-value: 9.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 795 MHWASYTGHEDCLELLLE-HSPFSYLEGNPFTPLHCAVINNQDSTTEMLLGALGAKIVNsrdaKGRTPLHAAAFADNVSG 873
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLEnGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD----NGRTALHYAARSGHLEI 76
|
90
....*....|....*
gi 27370168 874 LRMLLQHQAEVNATD 888
Cdd:pfam12796 77 VKLLLEKGADINVKD 91
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
246-490 |
1.36e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 67.71 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 246 ACYLGQDAVAIELVNAGANVNQPNDKGFTPLHVAaVSTNGALCLELLVNNGADVNYQSKEGKSPLHMAAIHGRFTRSQIL 325
Cdd:PHA02875 9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLA-MKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 326 IQNGSEI-DCADKFGNTPLHVAARYGHELLISTLMTNGADTARRGIHDMFPLHLAVLFGfsdccrkllssgqlysivssl 404
Cdd:PHA02875 88 LDLGKFAdDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMG--------------------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 405 snehvlsagfDINTpdslgrtclhaaasggnvecLNLLLSSGADLRRRDKFGRTPLHYAAANGSYQCAVTLVTAGAGVNE 484
Cdd:PHA02875 147 ----------DIKG--------------------IELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDY 196
|
....*.
gi 27370168 485 ADCKGC 490
Cdd:PHA02875 197 FGKNGC 202
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
81-236 |
1.43e-11 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 68.74 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 81 AAASRNEKVLGLLLAHSADVNARDKLWQTPLHVAAANRATKCAEALAPLLSSLNVADRSGRSALHHAVHSGHLETVNLLL 160
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILY 611
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27370168 161 NKGASLNvcDKKERQPLHWAAFLGHLEVLKLLVARGADLSCKDRKGYGLLHTAAASGQIEVVKHLLRMGAEIDEPN 236
Cdd:PLN03192 612 HFASISD--PHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
532-615 |
2.77e-11 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 60.90 E-value: 2.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 532 CLEFLLDNGADPSLRDRQGYTAVHYAAAYGNRQNLELLLEMSFNCLEDVESTvpvsPLHLAAYNGHCEALKTLAETLVNL 611
Cdd:pfam12796 12 LVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRT----ALHYAARSGHLEIVKLLLEKGADI 87
|
....
gi 27370168 612 DVRD 615
Cdd:pfam12796 88 NVKD 91
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
113-276 |
3.62e-11 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 67.59 E-value: 3.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 113 VAAANRATKCAEALAPLLSSL-------NVADRSGRSALHHAVHSGHLETVNLLLNKGASLNVCDKKERQPLHWAAFLGH 185
Cdd:PLN03192 524 NMASNLLTVASTGNAALLEELlkakldpDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKH 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 186 LEVLKLL--VARGADlsckDRKGYGLLHTAAASGQIEVVKHLLRMGAEIDEPNAFGNTALHIACYLGQDAVAIELVNAGA 263
Cdd:PLN03192 604 HKIFRILyhFASISD----PHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGA 679
|
170
....*....|....
gi 27370168 264 NVNQPN-DKGFTPL 276
Cdd:PLN03192 680 DVDKANtDDDFSPT 693
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
20-168 |
3.85e-11 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 66.59 E-value: 3.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 20 DVEEVRSLLSQKENINVLDQERRTPLHA-AAYVGDVP-ILQLLLMSGANVNAKDTLWLTPLHRAAASRNEK--VLGLLLA 95
Cdd:PHA03095 166 NVELLRLLIDAGADVYAVDDRFRSLLHHhLQSFKPRArIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLI 245
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27370168 96 HSADVNARDKLWQTPLHVAAANRATKCAEALAPLLSSLNVADRSGRSALHHAVHSGHLETVNLLLNKGASLNV 168
Cdd:PHA03095 246 AGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAET 318
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
670-919 |
3.91e-11 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 67.20 E-value: 3.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 670 LLIDSGERADitdvmDAYGQTPLMLAIMNGHVDCVHLLLEKGSTADAADLRGRTALHRGAVTGCEDCLAALLDHDAFVLC 749
Cdd:PLN03192 512 LLGDNGGEHD-----DPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHI 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 750 RDFKGRTPIHLASACGHTAVLRTLLQAALSTDPLDAGvdysgyspmhwasytghedclELLLEhspfsylegnpftplhc 829
Cdd:PLN03192 587 RDANGNTALWNAISAKHHKIFRILYHFASISDPHAAG---------------------DLLCT----------------- 628
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 830 avinnqdsttemllgalgakivnsrdakgrtplhaAAFADNVSGLRMLLQHQAEVNATDHTGRTALMTAAESGQTAAVEF 909
Cdd:PLN03192 629 -----------------------------------AAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRL 673
|
250
....*....|
gi 27370168 910 LLYRGkADLT 919
Cdd:PLN03192 674 LIMNG-ADVD 682
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
423-476 |
6.78e-11 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 58.44 E-value: 6.78e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 27370168 423 GRTCLHAAASGGNVECLNLLLSSGADLRRRDKFGRTPLHYAAANGSYQCAVTLV 476
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
274-461 |
1.03e-10 |
|
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: 65.80 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 274 TPLHVAAvSTNGALCLE-LLVNNGADVNYQSKEGKSPLHMAAIHGRFTRSQILIQNGSE-----IDCADKFGNTPLHVAA 347
Cdd:cd22192 19 SPLLLAA-KENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElvnepMTSDLYQGETALHIAV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 348 RYGHELLISTLMTNGADTA---------RRGIHDMFplhlavLFGfsdccrkllssgqlysivsslsnEHVLSagFdint 418
Cdd:cd22192 98 VNQNLNLVRELIARGADVVspratgtffRPGPKNLI------YYG-----------------------EHPLS--F---- 142
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 27370168 419 pdslgrtclhaAASGGNVECLNLLLSSGADLRRRDKFGRTPLH 461
Cdd:cd22192 143 -----------AACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
257-460 |
1.60e-10 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 64.69 E-value: 1.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 257 ELVNAGANVNQPNDKGFTPLHVAAVSTNGALcLELLVNNGADVNYQSKEGKSPLHMAAIHGR--FTRSQILIQNGSEID- 333
Cdd:PHA02946 57 ELLHRGYSPNETDDDGNYPLHIASKINNNRI-VAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAKINn 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 334 CADKFGNTPLhVAARYGHELLISTLMTNGadtarrgihdmFPLHLAVLFGFSDCCRKLLSSGQLYSIVSSLsnehvLSAG 413
Cdd:PHA02946 136 SVDEEGCGPL-LACTDPSERVFKKIMSIG-----------FEARIVDKFGKNHIHRHLMSDNPKASTISWM-----MKLG 198
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 27370168 414 FDINTPDSLGRTCLHAAASG--GNVECLNLLLSSgADLRRRDKFGRTPL 460
Cdd:PHA02946 199 ISPSKPDHDGNTPLHIVCSKtvKNVDIINLLLPS-TDVNKQNKFGDSPL 246
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
140-193 |
2.24e-10 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 56.90 E-value: 2.24e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 27370168 140 GRSALHHAVHSGHLETVNLLLNKGASLNVCDKKERQPLHWAAFLGHLEVLKLLV 193
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
429-570 |
3.10e-10 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 64.50 E-value: 3.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 429 AAASGGNVECLNLLLSSGADLRRRDKFGRTPLHYAAANGSYQCAVTLVTAGAGVNEADCKGCSPL--------------- 493
Cdd:PLN03192 531 TVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnaisakhhkifril 610
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27370168 494 -HYAAASDtyrraePHTASshdaeedELLKESRRKEAFFCLEFLLDNGADPSLRDRQGYTAVHYAAAYGNRQNLELLL 570
Cdd:PLN03192 611 yHFASISD------PHAAG-------DLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLI 675
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
851-1011 |
4.12e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 63.44 E-value: 4.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 851 VNSRDAKGRTPLHAAAFADNVSGLRMLLQHQAEVNATDHTGRTALMTAAESGQTAAVEFLLYRGkADLTVLDENKNTALH 930
Cdd:PHA02874 117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKG-AYANVKDNNGESPLH 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 931 LACSKGHEKCALMILAETQDlgLINATNSALqMPLHIAARNGLASVvqALLSRGATVLAVDEEGHTP---ALACAPNKDV 1007
Cdd:PHA02874 196 NAAEYGDYACIKLLIDHGNH--IMNKCKNGF-TPLHNAIIHNRSAI--ELLINNASINDQDIDGSTPlhhAINPPCDIDI 270
|
....
gi 27370168 1008 ADCL 1011
Cdd:PHA02874 271 IDIL 274
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
132-312 |
6.55e-10 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 62.76 E-value: 6.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 132 SLNVADRSGRSALHHAVHSGHLETVNLLLNKGASLNVCDKKERQPLHWAAFLGH--LEVLKLLVARGADLSCK-DRKGYG 208
Cdd:PHA02946 64 SPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAKINNSvDEEGCG 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 209 LLhTAAASGQIEVVKHLLRMGAEIDEPNAFGNTalHIACYLGQD---AVAIE-LVNAGANVNQPNDKGFTPLHVAAVSTN 284
Cdd:PHA02946 144 PL-LACTDPSERVFKKIMSIGFEARIVDKFGKN--HIHRHLMSDnpkASTISwMMKLGISPSKPDHDGNTPLHIVCSKTV 220
|
170 180
....*....|....*....|....*...
gi 27370168 285 GALCLELLVNNGADVNYQSKEGKSPLHM 312
Cdd:PHA02946 221 KNVDIINLLLPSTDVNKQNKFGDSPLTL 248
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
51-346 |
8.16e-10 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 62.54 E-value: 8.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 51 VGDVPILQL--LLMSGANVN---AKDTLWLTPLHRAAASRneKVLGLLLAHSADVNARDKLWQTPLhvaaanratkCAea 125
Cdd:PHA02798 12 FSDNVKLSTvkLLIKSCNPNeivNEYSIFQKYLQRDSPST--DIVKLFINLGANVNGLDNEYSTPL----------CT-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 126 lapLLSslNVADrsgrsalhhavHSGHLETVNLLLNKGASLNVCDKKERQPLHWA---AFLGHLEVLKLLVARGADLSCK 202
Cdd:PHA02798 78 ---ILS--NIKD-----------YKHMLDIVKILIENGADINKKNSDGETPLYCLlsnGYINNLEILLFMIENGADTTLL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 203 DRKGYGLLHTAAASG---QIEVVKHLLRMGAEIDE-PNAFGNTALHiaCYLGQDAVAIE------LVNAGANVNQPND-- 270
Cdd:PHA02798 142 DKDGFTMLQVYLQSNhhiDIEIIKLLLEKGVDINThNNKEKYDTLH--CYFKYNIDRIDadilklFVDNGFIINKENKsh 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27370168 271 -KGFTPLHVAAVSTNGALCLELL--VNNGADVNYQSKEGKSPLHMAAIHGRFTRSQILIQNGSEIDCADKFGNTPLHVA 346
Cdd:PHA02798 220 kKKFMEYLNSLLYDNKRFKKNILdfIFSYIDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTA 298
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
659-934 |
2.04e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 61.16 E-value: 2.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 659 AAASGHTDSLHLLIDSGERADITdVMDAYgqTPLMLAIMNGHVDCVHLLLEKGSTADAADLRGRTALHRGAVTGCEDCLA 738
Cdd:PHA02875 9 AILFGELDIARRLLDIGINPNFE-IYDGI--SPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 739 ALLDHDAF---VLCRDfkGRTPIHLASACGHTAVLRTLLqaALSTDPLDAGVDYsgYSPMHWASYTGHEDCLELLLEHSP 815
Cdd:PHA02875 86 ELLDLGKFaddVFYKD--GMTPLHLATILKKLDIMKLLI--ARGADPDIPNTDK--FSPLHLAVMMGDIKGIELLIDHKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 816 FSYLEgnpftplhcavinnqdsttemllgalgakivnsrDAKGRTPLHAAAFADNVSGLRMLLQHQAEVNATDHTGRTAL 895
Cdd:PHA02875 160 CLDIE----------------------------------DCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAA 205
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 27370168 896 M-TAAESGQTAAVEFLLYRGkAD---LTVLDENKNTALHLACS 934
Cdd:PHA02875 206 LcYAIENNKIDIVRLFIKRG-ADcniMFMIEGEECTILDMICN 247
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
653-708 |
3.17e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 53.82 E-value: 3.17e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 27370168 653 WTPLHAAAASGHTDSLHLLIDSGerADItDVMDAYGQTPLMLAIMNGHVDCVHLLL 708
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKG--ADI-NAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
339-576 |
6.75e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 59.23 E-value: 6.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 339 GNTPLHVAARYGHELLISTLMTNGA--DTARRGIHDmfPLHLAVLFGFSDCCRKLLSSGqlysivsSLSNEHVLSAGfdi 416
Cdd:PHA02875 35 GISPIKLAMKFRDSEAIKLLMKHGAipDVKYPDIES--ELHDAVEEGDVKAVEELLDLG-------KFADDVFYKDG--- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 417 NTPdslgrtcLHAAASGGNVECLNLLLSSGAD--LRRRDKFgrTPLHYAAANGSYQCAVTLVTAGAGVNEADCKGCSPLH 494
Cdd:PHA02875 103 MTP-------LHLATILKKLDIMKLLIARGADpdIPNTDKF--SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLI 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 495 YAAAsdtyrraephtasshdaeedellkesrRKEAFFClEFLLDNGADPSLRDRQGYTAVHYAAAYGNRQNL-ELLLEMS 573
Cdd:PHA02875 174 IAMA---------------------------KGDIAIC-KMLLDSGANIDYFGKNGCVAALCYAIENNKIDIvRLFIKRG 225
|
...
gi 27370168 574 FNC 576
Cdd:PHA02875 226 ADC 228
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
851-1007 |
8.10e-09 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 59.27 E-value: 8.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 851 VNSRDAKGRTPLHA---AAFADNVSGLRMLLQHQAEVNATDHTGRTALMTAAESGQTAAV-EFLLYRGkADLTVLDENKN 926
Cdd:PHA03095 40 VNFRGEYGKTPLHLylhYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDViKLLIKAG-ADVNAKDKVGR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 927 TALHlACSKG---HEKCALMILAETQDlglINATNSALQMPLHIAARNGLASV--VQALLSRGATVLAVDEEG----HTP 997
Cdd:PHA03095 119 TPLH-VYLSGfniNPKVIRLLLRKGAD---VNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADVYAVDDRFrsllHHH 194
|
170
....*....|
gi 27370168 998 ALACAPNKDV 1007
Cdd:PHA03095 195 LQSFKPRARI 204
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
592-719 |
1.00e-08 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 59.50 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 592 AAYNGHCEALKTLAETLVNLDVRDHKGRTALFLATERGSTECVEVLTAHGASALIKE---------------RKRKWTPL 656
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDangntalwnaisakhHKIFRILY 611
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27370168 657 HAAAASGHTDSLHLLIDSGERADIT------------DVMDAYGQTPLMLAIMNGHVDCVHLLLEKGSTADAADL 719
Cdd:PLN03192 612 HFASISDPHAAGDLLCTAAKRNDLTamkellkqglnvDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANT 686
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
173-226 |
1.43e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 51.89 E-value: 1.43e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 27370168 173 ERQPLHWAAFLGHLEVLKLLVARGADLSCKDRKGYGLLHTAAASGQIEVVKHLL 226
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
722-914 |
1.79e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 58.08 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 722 RTALHRGAVTGCEDCLAALLD---HDAFVLcrdFKGRTPIHLASACGHTAVLRTLLQAALSTDPLDAGVDysgySPMHWA 798
Cdd:PHA02875 3 QVALCDAILFGELDIARRLLDigiNPNFEI---YDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIE----SELHDA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 799 SYTGHEDCLELLLEHSPFS----YLEGNpfTPLHCAVINNQDSTTEMLLGALGAKIVNSRDAKgrTPLHAAAFADNVSGL 874
Cdd:PHA02875 76 VEEGDVKAVEELLDLGKFAddvfYKDGM--TPLHLATILKKLDIMKLLIARGADPDIPNTDKF--SPLHLAVMMGDIKGI 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 27370168 875 RMLLQHQAEVNATDHTGRTALMTAAESGQTAAVEFLLYRG 914
Cdd:PHA02875 152 ELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSG 191
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
766-992 |
2.80e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 57.37 E-value: 2.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 766 HTAVLRTLLQAALSTDPLDAGVDYSGYSPMHWASYTGHEDCLELLLEHS--PFSYLEGNpFTPLH-----CAVINNQDST 838
Cdd:PHA03100 10 SRIIKVKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGadINSSTKNN-STPLHylsniKYNLTDVKEI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 839 TEMLLgALGAkIVNSRDAKGRTPLHAAAFA--DNVSGLRMLLQHQAEVNATDHTGRTALMTAAESGQ--TAAVEFLLYRG 914
Cdd:PHA03100 89 VKLLL-EYGA-NVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 915 ---------------KADLTVLDENKNTALHLACSKGHEKCALMILaetqDLGL-INATNSALQMPLHIAARNGLASVVQ 978
Cdd:PHA03100 167 vdinaknrvnyllsyGVPINIKDVYGFTPLHYAVYNNNPEFVKYLL----DLGAnPNLVNKYGDTPLHIAILNNNKEIFK 242
|
250
....*....|....
gi 27370168 979 ALLSRGATVLAVDE 992
Cdd:PHA03100 243 LLLNNGPSIKTIIE 256
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
858-911 |
2.93e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 51.12 E-value: 2.93e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 27370168 858 GRTPLHAAAFADNVSGLRMLLQHQAEVNATDHTGRTALMTAAESGQTAAVEFLL 911
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
49-276 |
4.60e-08 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 56.99 E-value: 4.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 49 AYVG----DVPILQLLLMSGANVNAKDTLWLTPLHRAAASRNEKVLGLLLAHSADVNARDKLWQTPLHVAAANRATKcae 124
Cdd:PHA02946 43 AYCGikglDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEV--- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 125 alapllsslnvadrsgrsalhhavhsghLETVNLLLNKGASL-NVCDKKERQPLhWAAFLGHLEVLKLLVARGADLSCKD 203
Cdd:PHA02946 120 ----------------------------IERINLLVQYGAKInNSVDEEGCGPL-LACTDPSERVFKKIMSIGFEARIVD 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27370168 204 RKGYGLLHTAAASG--QIEVVKHLLRMGAEIDEPNAFGNTALHIACYLGQDAV-AIELVNAGANVNQPNDKGFTPL 276
Cdd:PHA02946 171 KFGKNHIHRHLMSDnpKASTISWMMKLGISPSKPDHDGNTPLHIVCSKTVKNVdIINLLLPSTDVNKQNKFGDSPL 246
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
55-237 |
4.92e-08 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 57.22 E-value: 4.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 55 PILQLLLMSGANVNAKDTLWLTPLHRAAASRNEkvLGLLLAHSADVNARDKLWQTPLHVAAANratkcaEALAP-LLSSL 133
Cdd:PTZ00322 11 SAFAAQLFFGTEGSRKRRAKPISFERMAAIQEE--IARIDTHLEALEATENKDATPDHNLTTE------EVIDPvVAHML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 134 NVAdrsgrsaLHHAVHSGHLETVNLLLNKGASLNVCDKKERQPLHWAAFLGHLEVLKLLVARGADLSCKDRKGYGLLHTA 213
Cdd:PTZ00322 83 TVE-------LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELA 155
|
170 180
....*....|....*....|....
gi 27370168 214 AASGQIEVVKHLLRMGAEIDEPNA 237
Cdd:PTZ00322 156 EENGFREVVQLLSRHSQCHFELGA 179
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
840-997 |
5.41e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 57.00 E-value: 5.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 840 EMLLGalGAKIVNSRDAKGRTPLHAAAFADNVSGLRMLLQHQAEVNATDHTGRTALMTAAESGQTAAVE----------- 908
Cdd:PHA02876 162 EMLLE--GGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKaiidnrsnink 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 909 -----------------FLLYRGKADLTVLDENKNTALHLAC-SKGHEKCALMILAETQDlglINATNSALQMPLHIAAR 970
Cdd:PHA02876 240 ndlsllkairnedletsLLLYDAGFSVNSIDDCKNTPLHHASqAPSLSRLVPKLLERGAD---VNAKNIKGETPLYLMAK 316
|
170 180
....*....|....*....|....*...
gi 27370168 971 NGLASV-VQALLSRGATVLAVDEEGHTP 997
Cdd:PHA02876 317 NGYDTEnIRTLIMLGADVNAADRLYITP 344
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
858-1020 |
6.14e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 56.15 E-value: 6.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 858 GRTPLHAAAFADNVSGLRMLLQHQAEVNATDHTGRTALMTAAESGQTAAVEFLLYRGKADLTVLDENKNTALHLACSKGH 937
Cdd:PHA02875 35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKK 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 938 EKCALMILAETQDLGLINATNSAlqmPLHIAARNGLASVVQALLSRGATVLAVDEEGHTPALACAPNKDVADCLALILST 1017
Cdd:PHA02875 115 LDIMKLLIARGADPDIPNTDKFS---PLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSG 191
|
...
gi 27370168 1018 MKP 1020
Cdd:PHA02875 192 ANI 194
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
200-347 |
6.57e-08 |
|
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: 56.63 E-value: 6.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 200 SCKDRKGYGLLHTAAASGQ-IEVVKHLLRMGAEIDEpnafGNTALHIACYLGQDAV----AIELVNAGANVNQP--ND-- 270
Cdd:TIGR00870 46 NCPDRLGRSALFVAAIENEnLELTELLLNLSCRGAV----GDTLLHAISLEYVDAVeailLHLLAAFRKSGPLElaNDqy 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 271 -----KGFTPLHVAAVsTNGALCLELLVNNGADVNYQSK--------------EGKSPLHMAAIHGRFTRSQILIQNGSE 331
Cdd:TIGR00870 122 tseftPGITALHLAAH-RQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPAD 200
|
170
....*....|....*.
gi 27370168 332 IDCADKFGNTPLHVAA 347
Cdd:TIGR00870 201 ILTADSLGNTLLHLLV 216
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
337-494 |
7.00e-08 |
|
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: 56.56 E-value: 7.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 337 KFGNTPLHVAARYGHELLISTLMT-NGADTARRGIHDMFPLHLAVLFGFSDCCRKLLSSgqlysiVSSLSNEHVLSAGFd 415
Cdd:cd22192 15 RISESPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEA------APELVNEPMTSDLY- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 416 intpdsLGRTCLHAAASGGNVECLNLLLSSGADL----------RRRDK----FGRTPLHYAAANGSYQCAVTLVTAGAG 481
Cdd:cd22192 88 ------QGETALHIAVVNQNLNLVRELIARGADVvspratgtffRPGPKnliyYGEHPLSFAACVGNEEIVRLLIEHGAD 161
|
170
....*....|...
gi 27370168 482 VNEADCKGCSPLH 494
Cdd:cd22192 162 IRAQDSLGNTVLH 174
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
41-94 |
8.52e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 49.58 E-value: 8.52e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 27370168 41 RRTPLHAAAYVGDVPILQLLLMSGANVNAKDTLWLTPLHRAAASRNEKVLGLLL 94
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
27-166 |
1.07e-07 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 56.03 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 27 LLSQKENINVLDQERRTPLHAAAYVGDVPILQLLLMSGANVNAKDTLWLTPLHRAAASRNEKVLGLL--LAHSADVNARD 104
Cdd:PLN03192 544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILyhFASISDPHAAG 623
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27370168 105 KLWQTplhvaAANRATkcAEALAPLLS-SLNV--ADRSGRSALHHAVHSGHLETVNLLLNKGASL 166
Cdd:PLN03192 624 DLLCT-----AAKRND--LTAMKELLKqGLNVdsEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
74-126 |
1.71e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 48.81 E-value: 1.71e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 27370168 74 WLTPLHRAAASRNEKVLGLLLAHSADVNARDKLWQTPLHVAAANRATKCAEAL 126
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
428-501 |
1.87e-07 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 55.29 E-value: 1.87e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27370168 428 HAAASGGNVEcLNLLLSSGADLRRRDKFGRTPLHYAAANGSYQCAVTLVTAGAGVNEADCKGCSPLHYAAASDT 501
Cdd:PTZ00322 88 QLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGF 160
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
153-448 |
2.15e-07 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 54.84 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 153 LETVNLLLNKGASLNVCDKKERQPL-----HWAAFLGHLEVLKLLVARGADLSCKDRKG----YGLLHTAAASgQIEVVK 223
Cdd:PHA02798 51 TDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGetplYCLLSNGYIN-NLEILL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 224 HLLRMGAEIDEPNAFGNTALHI----ACYLGQDAVAIeLVNAGANVNQPNDK-GFTPLHV---AAVSTNGALCLELLVNN 295
Cdd:PHA02798 130 FMIENGADTTLLDKDGFTMLQVylqsNHHIDIEIIKL-LLEKGVDINTHNNKeKYDTLHCyfkYNIDRIDADILKLFVDN 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 296 GADVNYQSKegksplhmaaihgrFTRSQILiqngseidcadkfgntplhvaaryghELLISTLMTNgadtaRRGIHDMFP 375
Cdd:PHA02798 209 GFIINKENK--------------SHKKKFM--------------------------EYLNSLLYDN-----KRFKKNILD 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27370168 376 LhlavLFGFSDCCRK-LLSSGQLYSIVSSLSN---EHVLSAGFDINTPDSLGRTCLHAAASGGNVECLNLLLSSGAD 448
Cdd:PHA02798 244 F----IFSYIDINQVdELGFNPLYYSVSHNNRkifEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNKKPN 316
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
587-760 |
2.53e-07 |
|
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: 54.63 E-value: 2.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 587 SPLHLAAYNGHCEALKTLAETlvnldvrdhkGRTALFlatERGstecvevltAHGASALikerkrkwtplHAAAASGHTD 666
Cdd:cd22192 19 SPLLLAAKENDVQAIKKLLKC----------PSCDLF---QRG---------ALGETAL-----------HVAALYDNLE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 667 SLHLLIDSGERAdITDVM--DAY-GQTPLMLAIMNGHVDCVHLLLEKGstADAADLR----------------GRTALHR 727
Cdd:cd22192 66 AAVVLMEAAPEL-VNEPMtsDLYqGETALHIAVVNQNLNLVRELIARG--ADVVSPRatgtffrpgpknliyyGEHPLSF 142
|
170 180 190
....*....|....*....|....*....|...
gi 27370168 728 GAVTGCEDCLAALLDHDAFVLCRDFKGRTPIHL 760
Cdd:cd22192 143 AACVGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
723-814 |
3.17e-07 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 54.52 E-value: 3.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 723 TALHRGAVTGCEdcLAA---------LLDHDAFVLCRDFKGRTPIHLASACGHTAVLRTLLQaaLSTDPldAGVDYSGYS 793
Cdd:PTZ00322 77 VVAHMLTVELCQ--LAAsgdavgariLLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLE--FGADP--TLLDKDGKT 150
|
90 100
....*....|....*....|.
gi 27370168 794 PMHWASYTGHEDCLELLLEHS 814
Cdd:PTZ00322 151 PLELAEENGFREVVQLLSRHS 171
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
842-997 |
3.23e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 54.12 E-value: 3.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 842 LLGALGAKIVNSRDAKGRTPLHAAAFADNVSGLRMLLQHQAEVNATDHTGRTALMTAAESGQTAAVEFLLYRGkADLTVL 921
Cdd:PHA02878 152 LLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENG-ASTDAR 230
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27370168 922 DENKNTALHLACSKGHEKCALMILAETQdlGLINATNSALQM-PLHIAARNglASVVQALLSRGATVLAVDEEGHTP 997
Cdd:PHA02878 231 DKCGNTPLHISVGYCKDYDILKLLLEHG--VDVNAKSYILGLtALHSSIKS--ERKLKLLLEYGADINSLNSYKLTP 303
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
682-879 |
3.61e-07 |
|
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: 54.32 E-value: 3.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 682 DVMDAYGQTPLM-LAIMNGHVDCVHLLLEKGSTADAadlrGRTALH---RGAVTGCEDCLAALLDHD----------AFV 747
Cdd:TIGR00870 46 NCPDRLGRSALFvAAIENENLELTELLLNLSCRGAV----GDTLLHaisLEYVDAVEAILLHLLAAFrksgplelanDQY 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 748 LCRDFKGRTPIHLASACGHTAVLRTLLQAALSTdPLDAGVD-----------YSGYSPMHWASYTGHEDCLELLLEHsPF 816
Cdd:TIGR00870 122 TSEFTPGITALHLAAHRQNYEIVKLLLERGASV-PARACGDffvksqgvdsfYHGESPLNAAACLGSPSIVALLSED-PA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 817 SYLE----GNpfTPLHCAVINNQDST--TEM------LLGALGAKIVNSRDA------KGRTPLHAAAFADNVSGLRMLL 878
Cdd:TIGR00870 200 DILTadslGN--TLLHLLVMENEFKAeyEELscqmynFALSLLDKLRDSKELevilnhQGLTPLKLAAKEGRIVLFRLKL 277
|
.
gi 27370168 879 Q 879
Cdd:TIGR00870 278 A 278
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
658-790 |
3.75e-07 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 54.49 E-value: 3.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 658 AAAASGHTDSLHLLIDSGERADITDvmdAYGQTPLMLAIMNGHVDCVHLLLEKGSTADAADLRGRTAL------------ 725
Cdd:PLN03192 531 TVASTGNAALLEELLKAKLDPDIGD---SKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnaisakhhkif 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 726 ------------HRGAVTGCE-------DCLAALLDHDAFVLCRDFKGRTPIHLASACGHTAVLRTLLQAALSTDPLDAG 786
Cdd:PLN03192 608 rilyhfasisdpHAAGDLLCTaakrndlTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTD 687
|
....
gi 27370168 787 VDYS 790
Cdd:PLN03192 688 DDFS 691
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
721-774 |
4.13e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 47.65 E-value: 4.13e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 27370168 721 GRTALHRGAVTGCEDCLAALLDHDAFVLCRDFKGRTPIHLASACGHTAVLRTLL 774
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
660-743 |
4.16e-07 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 54.13 E-value: 4.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 660 AASGHTDSLHLLIDSGerADiTDVMDAYGQTPLMLAIMNGHVDCVHLLLEKGSTADAADLRGRTALHRGAVTGCEDCLAA 739
Cdd:PTZ00322 90 AASGDAVGARILLTGG--AD-PNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166
|
....
gi 27370168 740 LLDH 743
Cdd:PTZ00322 167 LSRH 170
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
869-1015 |
4.61e-07 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 54.10 E-value: 4.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 869 DNVSGLRMLLQHQAEVNA--------------TDHTGRTALMTAAESGQTAAVEFLLyRGKADLTVLDENKNTALHLACS 934
Cdd:PLN03192 489 DNVVILKNFLQHHKELHDlnvgdllgdnggehDDPNMASNLLTVASTGNAALLEELL-KAKLDPDIGDSKGRTPLHIAAS 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 935 KGHEKCALMILAETQDLGLINAT-NSAL---------------------QMP------LHIAARNGLASVVQALLSRGAT 986
Cdd:PLN03192 568 KGYEDCVLVLLKHACNVHIRDANgNTALwnaisakhhkifrilyhfasiSDPhaagdlLCTAAKRNDLTAMKELLKQGLN 647
|
170 180
....*....|....*....|....*....
gi 27370168 987 VLAVDEEGHTpALACAPNKDVADCLALIL 1015
Cdd:PLN03192 648 VDSEDHQGAT-ALQVAMAEDHVDMVRLLI 675
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
783-1016 |
5.70e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 53.07 E-value: 5.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 783 LDAGVD-----YSGYSPMHWASYTGHEDCLELLLEHSPF-SYLEGNPFTPLHCAVINNQDSTTEMLLgALGAKIVNSRDA 856
Cdd:PHA02875 22 LDIGINpnfeiYDGISPIKLAMKFRDSEAIKLLMKHGAIpDVKYPDIESELHDAVEEGDVKAVEELL-DLGKFADDVFYK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 857 KGRTPLHAAAFADNVSGLRMLLQHQAE--VNATDHTgrTALMTAAESGQTAAVEFLLYrgkadltvldenkntalHLACS 934
Cdd:PHA02875 101 DGMTPLHLATILKKLDIMKLLIARGADpdIPNTDKF--SPLHLAVMMGDIKGIELLID-----------------HKACL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 935 KGHEKCALMilaetqdlglinatnsalqmPLHIAARNGLASVVQALLSRGATVLAVDEEGHTPALACAPNKDVADCLALI 1014
Cdd:PHA02875 162 DIEDCCGCT--------------------PLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLF 221
|
..
gi 27370168 1015 LS 1016
Cdd:PHA02875 222 IK 223
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
308-358 |
6.23e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 47.27 E-value: 6.23e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 27370168 308 SPLHMAAIHGRFTRSQILIQNGSEIDCADKFGNTPLHVAARYGHELLISTL 358
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
615-774 |
6.26e-07 |
|
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: 53.61 E-value: 6.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 615 DHKGRTALFLATERGSTECVEVLTAHGASALIKERKRKWTPlhaaaasghtdslhllidsgeradiTDVMDAY--GQTPL 692
Cdd:cd22194 138 AYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVFFNP-------------------------KYKHEGFyfGETPL 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 693 MLAIMNGHVDCVHLLLEKGSTADAA-DLRGRTALHrGAVTGCEDclaaLLDHDAFVL-----------------CRDFKG 754
Cdd:cd22194 193 ALAACTNQPEIVQLLMEKESTDITSqDSRGNTVLH-ALVTVAED----SKTQNDFVKrmydmillksenknletIRNNEG 267
|
170 180
....*....|....*....|
gi 27370168 755 RTPIHLASACGHTAVLRTLL 774
Cdd:cd22194 268 LTPLQLAAKMGKAEILKYIL 287
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
587-637 |
6.67e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 47.27 E-value: 6.67e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 27370168 587 SPLHLAAYNGHCEALKTLAETLVNLDVRDHKGRTALFLATERGSTECVEVL 637
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
227-359 |
9.87e-07 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 52.98 E-value: 9.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 227 RMGAeIDEPNAFGNTALHiACYLGQDAVAielvnaGANVNQPNDKGFTP--LHVAAV------STNGALCLELLVNNGAD 298
Cdd:PTZ00322 36 RMAA-IQEEIARIDTHLE-ALEATENKDA------TPDHNLTTEEVIDPvvAHMLTVelcqlaASGDAVGARILLTGGAD 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27370168 299 VNYQSKEGKSPLHMAAIHGRFTRSQILIQNGSEIDCADKFGNTPLHVAARYGHELLISTLM 359
Cdd:PTZ00322 108 PNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
180-343 |
1.03e-06 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 52.95 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 180 AAFLGHLEVLKLLVARGADLSCKDRKGYGLLHTAAASGQIEVVKHLLRMGAEIDEPNAFGNTALHIACYLGQDAVaIELV 259
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKI-FRIL 610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 260 NAGANVNQPNDKGftPLHVAAVSTNGALCLELLVNNGADVNYQSKEGKSPLHMAAIHGRFTRSQILIQNGSEIDCA---D 336
Cdd:PLN03192 611 YHFASISDPHAAG--DLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAntdD 688
|
....*..
gi 27370168 337 KFGNTPL 343
Cdd:PLN03192 689 DFSPTEL 695
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
825-997 |
1.07e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 52.27 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 825 TPLHCAVINNQDSTTEMLLgALGAKiVNSRDAKGRTPLHAAAFADNVSGLRMLLQHQAEVNATDHTGRTALMTAAESGQT 904
Cdd:PHA02874 126 TFLHYAIKKGDLESIKMLF-EYGAD-VNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDY 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 905 AAVEFLLYRGkADLTVLDENKNTALHLACSKGHEKCALMILAETqdlglINATNSALQMPLHIAARNGLA-SVVQALLSR 983
Cdd:PHA02874 204 ACIKLLIDHG-NHIMNKCKNGFTPLHNAIIHNRSAIELLINNAS-----INDQDIDGSTPLHHAINPPCDiDIIDILLYH 277
|
170
....*....|....
gi 27370168 984 GATVLAVDEEGHTP 997
Cdd:PHA02874 278 KADISIKDNKGENP 291
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
309-499 |
1.32e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 52.19 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 309 PLHMAAIHGRFTRSQILIQNGSEIDCADKFGNTPLHVAARY----GHELLISTLMTNGADTARRGIHDMFPLHLAVLF-- 382
Cdd:PHA02878 40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEpnklGMKEMIRSINKCSVFYTLVAIKDAFNNRNVEIFki 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 383 -------GFSDCCRKLLSSGQLYSIVSSLSNEHVLSAGFDINTPD-SLGRTCLHAAASGGNVECLNLLLSSGADLRRRDK 454
Cdd:PHA02878 120 iltnrykNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDK 199
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 27370168 455 FGRTPLHYAAANGSYQCAVTLVTAGAGVNEADCKGCSPLHYAAAS 499
Cdd:PHA02878 200 TNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGY 244
|
|
| PHA02791 |
PHA02791 |
ankyrin-like protein; Provisional |
123-227 |
1.55e-06 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165154 [Multi-domain] Cd Length: 284 Bit Score: 51.20 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 123 AEALAPLLSSLNV--ADRSGRSALHHAVHSGHLETVNLLLNKGASLNVCDKKErqPLHWAAFLGHLEVLKLLVARGADLS 200
Cdd:PHA02791 11 SKQLKSFLSSKDAfkADVHGHSALYYAIADNNVRLVCTLLNAGALKNLLENEF--PLHQAATLEDTKIVKILLFSGMDDS 88
|
90 100
....*....|....*....|....*..
gi 27370168 201 CKDRKGYGLLHTAAASGQIEVVKHLLR 227
Cdd:PHA02791 89 QFDDKGNTALYYAVDSGNMQTVKLFVK 115
|
|
| PHA02716 |
PHA02716 |
CPXV016; CPX019; EVM010; Provisional |
289-493 |
1.71e-06 |
|
CPXV016; CPX019; EVM010; Provisional
Pssm-ID: 165089 [Multi-domain] Cd Length: 764 Bit Score: 52.22 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 289 LELLVNNGADVNYQSKEGKSPLHMAAIHGRFTRSQI--LIQNGSEIDCADKFGNTPlhvaaryghellISTLMTNgADTA 366
Cdd:PHA02716 195 LEWLCNNGVNVNLQNNHLITPLHTYLITGNVCASVIkkIIELGGDMDMKCVNGMSP------------IMTYIIN-IDNI 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 367 RRGIHDMFPLHLavlfgfsDCCRKLLSSGQLYSIVSSLSN------EHVLSAGFDINTPDSLGRTCLHA--AASGGNVEC 438
Cdd:PHA02716 262 NPEITNIYIESL-------DGNKVKNIPMILHSYITLARNidisvvYSFLQPGVKLHYKDSAGRTCLHQyiLRHNISTDI 334
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27370168 439 LNLLLSSGADLRRRDKFGRTPLHY------------AAANGSYQCAVT--LVTAGAGVNEADCKGCSPL 493
Cdd:PHA02716 335 IKLLHEYGNDLNEPDNIGNTVLHTylsmlsvvnildPETDNDIRLDVIqcLISLGADITAVNCLGYTPL 403
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
325-486 |
1.84e-06 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 52.18 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 325 LIQNGSEIDCADKFGNTPLHVAARYGHELLISTLMTNGADTARRGIHDMFPLHLAVLFGFSDCCRKLLSsgqlysiVSSL 404
Cdd:PLN03192 544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYH-------FASI 616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 405 SNEHvlsAGFDIntpdslgrtcLHAAASGGNVECLNLLLSSGADLRRRDKFGRTPLHYAAANGSYQCAVTLVTAGAGVNE 484
Cdd:PLN03192 617 SDPH---AAGDL----------LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDK 683
|
..
gi 27370168 485 AD 486
Cdd:PLN03192 684 AN 685
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
415-463 |
1.95e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 45.80 E-value: 1.95e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 27370168 415 DINTPDSLGRTCLHAAASGGNVECLNLLLSSGADLRRRDKFGRTPLHYA 463
Cdd:pfam13857 8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
87-284 |
2.20e-06 |
|
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: 51.80 E-value: 2.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 87 EKVLGLL----LAHSADVNARDKLWQTPLHVAAANRATKCAEALAPLLSSLNVADRS--------------GRSALHHAV 148
Cdd:cd21882 2 EELLGLLeclrWYLTDSAYQRGATGKTCLHKAALNLNDGVNEAIMLLLEAAPDSGNPkelvnapctdefyqGQTALHIAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 149 HSGHLETVNLLLNKGASLNV--CDKKERQPLHWAAFLGHLEvlkllvargadlsckdrkgyglLHTAAASGQIEVVKHLL 226
Cdd:cd21882 82 ENRNLNLVRLLVENGADVSAraTGRFFRKSPGNLFYFGELP----------------------LSLAACTNQEEIVRLLL 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27370168 227 RMGAEIDEPNA---FGNTALHIACYLGQDAVAI---------ELVNAGANVNQ-------PNDKGFTPLHVAAVSTN 284
Cdd:cd21882 140 ENGAQPAALEAqdsLGNTVLHALVLQADNTPENsafvcqmynLLLSYGAHLDPtqqleeiPNHQGLTPLKLAAVEGK 216
|
|
| TRPV1-4 |
cd22193 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ... |
608-814 |
2.67e-06 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong 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: 411977 [Multi-domain] Cd Length: 607 Bit Score: 51.33 E-value: 2.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 608 LVNLDVRD--HKGRTALFLATERGSTECVEVLTAHGASALIKERKRKWTPlhaaaASGHTDSLhllidsgeraditdvmd 685
Cdd:cd22193 64 FINAEYTDeyYEGQTALHIAIERRQGDIVALLVENGADVHAHAKGRFFQP-----KYQGEGFY----------------- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 686 aYGQTPLMLAIMNGHVDCVHLLLE---KGSTADAADLRGRTALHrGAVTGCEDclaaLLDHDAFV-------------LC 749
Cdd:cd22193 122 -FGELPLSLAACTNQPDIVQYLLEnehQPADIEAQDSRGNTVLH-ALVTVADN----TKENTKFVtrmydmilirgakLC 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 750 --------RDFKGRTPIHLASACGHTAVLRTLLQAALSTDP---LDAGVDYSGYSPMHWASY-------TGHEDCLELLL 811
Cdd:cd22193 196 ptveleeiRNNDGLTPLQLAAKMGKIEILKYILQREIKEPElrhLSRKFTDWAYGPVSSSLYdlsnvdtCEKNSVLEIIV 275
|
...
gi 27370168 812 EHS 814
Cdd:cd22193 276 YNS 278
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
430-604 |
3.50e-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: 51.17 E-value: 3.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 430 AASGGNVECLN-LLLSSGADLRRRDKFGRTPLHYAAANGSYQCAVTLVTAGAG-VNEADC----KGCSPLHYAAASDTY- 502
Cdd:cd22192 24 AAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEPMTsdlyQGETALHIAVVNQNLn 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 503 -------RRAEPHTASSHDAeedeLLKESRRKEAFF---------C------LEFLLDNGADPSLRDRQGYTAVHYAAAY 560
Cdd:cd22192 104 lvreliaRGADVVSPRATGT----FFRPGPKNLIYYgehplsfaaCvgneeiVRLLIEHGADIRAQDSLGNTVLHILVLQ 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 27370168 561 GNR----QNLELLLEMSFN----CLEDVESTVPVSPLHLAAYNGHCEALKTL 604
Cdd:cd22192 180 PNKtfacQMYDLILSYDKEddlqPLDLVPNNQGLTPFKLAAKEGNIVMFQHL 231
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
421-692 |
4.14e-06 |
|
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: 50.65 E-value: 4.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 421 SLGRTCLHAAA---SGGNVECLNLLLSSGADLRRRDKF-----------GRTPLHYAAANGSYQCAVTLVTAGAGVNead 486
Cdd:cd21882 24 ATGKTCLHKAAlnlNDGVNEAIMLLLEAAPDSGNPKELvnapctdefyqGQTALHIAIENRNLNLVRLLVENGADVS--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 487 ckgcsplhyAAASDTYRRAEPHTASsHDAEEDELLKESRRKEAFfcLEFLLDNGADP---SLRDRQGYTAVHyaaaygnr 563
Cdd:cd21882 101 ---------ARATGRFFRKSPGNLF-YFGELPLSLAACTNQEEI--VRLLLENGAQPaalEAQDSLGNTVLH-------- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 564 qnleLLLEMSFNcledvesTVPVSPLHLAAYNGHCEALKTLAETLVNLDVRDHKGRTALFLATERGSTECVEVLTAHGAS 643
Cdd:cd21882 161 ----ALVLQADN-------TPENSAFVCQMYNLLLSYGAHLDPTQQLEEIPNHQGLTPLKLAAVEGKIVMFQHILQREFS 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27370168 644 ALIKERKRK---WT--PLHAAA-------ASGHTDSLHLLIDSGERADITDVMDaygQTPL 692
Cdd:cd21882 230 GPYQPLSRKfteWTygPVTSSLydlseidSWEKNSVLELIAFSKKREARHQMLV---QEPL 287
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
845-911 |
4.28e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 50.67 E-value: 4.28e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27370168 845 ALGAKIV-------NSRDAKGRTPLHAAAFADNVSGLRMLLQHQAEVNATDHTGRTALMTAAESGQTAAVEFLL 911
Cdd:PTZ00322 95 AVGARILltggadpNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
|
|
| PHA02716 |
PHA02716 |
CPXV016; CPX019; EVM010; Provisional |
218-471 |
4.64e-06 |
|
CPXV016; CPX019; EVM010; Provisional
Pssm-ID: 165089 [Multi-domain] Cd Length: 764 Bit Score: 50.68 E-value: 4.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 218 QIEVVKHLLRMG-AEID-EPNAFGNTALHiaCYLGQDAVAIE----LVNAGANVNQPNDKGFTPLHVAAVSTN-GALCLE 290
Cdd:PHA02716 154 DLDLIKYMVDVGiVNLNyVCKKTGYGILH--AYLGNMYVDIDilewLCNNGVNVNLQNNHLITPLHTYLITGNvCASVIK 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 291 LLVNNGADVNYQSKEGKSPLHMAAIHGRFTRSQILIQNGSEIDcADKFGNTP--LHV---AARYGHELLISTLMTNGA-- 363
Cdd:PHA02716 232 KIIELGGDMDMKCVNGMSPIMTYIINIDNINPEITNIYIESLD-GNKVKNIPmiLHSyitLARNIDISVVYSFLQPGVkl 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 364 ---DTARRGIhdmfpLHLAVLfgfsdccRKLLSSgqlySIVsSLSNEHvlsaGFDINTPDSLGRTCLHAAAS-------- 432
Cdd:PHA02716 311 hykDSAGRTC-----LHQYIL-------RHNIST----DII-KLLHEY----GNDLNEPDNIGNTVLHTYLSmlsvvnil 369
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 27370168 433 ------GGNVECLNLLLSSGADLRRRDKFGRTPLhyaaanGSYQC 471
Cdd:PHA02716 370 dpetdnDIRLDVIQCLISLGADITAVNCLGYTPL------TSYIC 408
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
533-697 |
6.89e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 49.60 E-value: 6.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 533 LEFLLDNG--ADPSLRdRQGYTAVHYAAAYGNRQNLELLLEMSFNclEDVESTVPVSPLHLAAYNGHCEALKTLAETLVN 610
Cdd:PHA02875 84 VEELLDLGkfADDVFY-KDGMTPLHLATILKKLDIMKLLIARGAD--PDIPNTDKFSPLHLAVMMGDIKGIELLIDHKAC 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 611 LDVRDHKGRTALFLATERGSTECVEVLTAHGASALIKERKRKWTPLHAAAASGHTDSLHLLIDSGERADI-TDVMDAYGQ 689
Cdd:PHA02875 161 LDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIKRGADCNImFMIEGEECT 240
|
....*...
gi 27370168 690 TPLMLAIM 697
Cdd:PHA02875 241 ILDMICNM 248
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
216-360 |
8.12e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 47.89 E-value: 8.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 216 SGQIEVVKHLLRMgaeIDEPNAFGNTALHiACyLGQDAVAIE----LVNAGANVN-QPNDKGFTPLHvAAVSTNGAL--- 287
Cdd:PHA02859 31 KDDIEGVKKWIKF---VNDCNDLYETPIF-SC-LEKDKVNVEilkfLIENGADVNfKTRDNNLSALH-HYLSFNKNVepe 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27370168 288 CLELLVNNGADVNYQSKEGKSPLH--MAAIHGRFTRSQILIQNGSEIDCADKFGNTPLHVAARYGHELLISTLMT 360
Cdd:PHA02859 105 ILKILIDSGSSITEEDEDGKNLLHmyMCNFNVRINVIKLLIDSGVSFLNKDFDNNNILYSYILFHSDKKIFDFLT 179
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
740-898 |
1.04e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 49.49 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 740 LLDHDAFVLCRD-FKGRTPIHLASACGHTAVLRTLLQAALSTDPLDAGVDYsgysPMHWASYTGHEDCLELLLEHSPFS- 817
Cdd:PHA02878 153 LLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNS----PLHHAVKHYNKPIVHILLENGASTd 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 818 --YLEGNpfTPLHCAVINNQDSTTEMLLGALGAKIVNSRDAKGRTPLHAAAFADNVsgLRMLLQHQAEVNATDHTGRTAL 895
Cdd:PHA02878 229 arDKCGN--TPLHISVGYCKDYDILKLLLEHGVDVNAKSYILGLTALHSSIKSERK--LKLLLEYGADINSLNSYKLTPL 304
|
...
gi 27370168 896 MTA 898
Cdd:PHA02878 305 SSA 307
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
109-160 |
1.22e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 43.42 E-value: 1.22e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 27370168 109 TPLHVAAANRATKCAEALAPLLSSLNVADRSGRSALHHAVHSGHLETVNLLL 160
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
206-259 |
1.31e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 43.42 E-value: 1.31e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 27370168 206 GYGLLHTAAASGQIEVVKHLLRMGAEIDEPNAFGNTALHIACYLGQDAVAIELV 259
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
258-313 |
1.32e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 43.49 E-value: 1.32e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 27370168 258 LVNAG-ANVNQPNDKGFTPLHVAAvSTNGALCLELLVNNGADVNYQSKEGKSPLHMA 313
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAA-KYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
547-775 |
1.33e-05 |
|
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: 49.31 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 547 DRQGYTAVHYAAAYGNRQNLELLLEmSFNCLEDVESTVpvspLHLAA--YNGHCEAL---------KTLAETLVNLDVRD 615
Cdd:TIGR00870 49 DRLGRSALFVAAIENENLELTELLL-NLSCRGAVGDTL----LHAISleYVDAVEAIllhllaafrKSGPLELANDQYTS 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 616 --HKGRTALFLATERGSTECVEVLTAHGASalikerkrkwtpLHAAA------ASGHTDSLHllidsgeraditdvmdaY 687
Cdd:TIGR00870 124 efTPGITALHLAAHRQNYEIVKLLLERGAS------------VPARAcgdffvKSQGVDSFY-----------------H 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 688 GQTPLMLAIMNGHVDCVHLLLEKGSTADAADLRGRTALH------------RGAVTGCEDCLAALLDHdafvlCRD---- 751
Cdd:TIGR00870 175 GESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHllvmenefkaeyEELSCQMYNFALSLLDK-----LRDskel 249
|
250 260
....*....|....*....|....*....
gi 27370168 752 -----FKGRTPIHLASACGHTAVLRTLLQ 775
Cdd:TIGR00870 250 evilnHQGLTPLKLAAKEGRIVLFRLKLA 278
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
291-346 |
1.33e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 43.49 E-value: 1.33e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 27370168 291 LLVNNGADVNYQSKEGKSPLHMAAIHGRFTRSQILIQNGSEIDCADKFGNTPLHVA 346
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
274-326 |
1.45e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 43.42 E-value: 1.45e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 27370168 274 TPLHVAAVSTNGAlCLELLVNNGADVNYQSKEGKSPLHMAAIHGRFTRSQILI 326
Cdd:pfam13637 3 TALHAAAASGHLE-LLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
230-350 |
1.46e-05 |
|
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: 48.99 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 230 AEIDEPNAFGNTALHIACYLGQDAVAIELVNAGANVN--------QPNDK--GF----TPLHVAAVsTNGALCLELLVNN 295
Cdd:cd22194 132 AEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNahakgvffNPKYKheGFyfgeTPLALAAC-TNQPEIVQLLMEK 210
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27370168 296 GAD-VNYQSKEGKSPLHMAAIHGRFTRSQI--LIQNGSEI--DCADKF--------GNTPLHVAARYG 350
Cdd:cd22194 211 ESTdITSQDSRGNTVLHALVTVAEDSKTQNdfVKRMYDMIllKSENKNletirnneGLTPLQLAAKMG 278
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
891-945 |
1.72e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 43.03 E-value: 1.72e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 27370168 891 GRTALMTAAESGQTAAVEFLLYRGkADLTVLDENKNTALHLACSKGHEKCALMIL 945
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKG-ADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
409-467 |
2.26e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 48.36 E-value: 2.26e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 27370168 409 VLSAGFDINTPDSLGRTCLHAAASGGNVECLNLLLSSGADLRRRDKFGRTPLHYAAANG 467
Cdd:PTZ00322 101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENG 159
|
|
| PHA02716 |
PHA02716 |
CPXV016; CPX019; EVM010; Provisional |
45-243 |
2.40e-05 |
|
CPXV016; CPX019; EVM010; Provisional
Pssm-ID: 165089 [Multi-domain] Cd Length: 764 Bit Score: 48.37 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 45 LHAaaYVG----DVPILQLLLMSGANVNAKDTLWLTPLHRAAASRN--EKVLGLLLAHSADVNARDKLWQTPLHVAAANr 118
Cdd:PHA02716 181 LHA--YLGnmyvDIDILEWLCNNGVNVNLQNNHLITPLHTYLITGNvcASVIKKIIELGGDMDMKCVNGMSPIMTYIIN- 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 119 atkcAEALAPLLSSLNVADRSGRSA------LHHAVHSGH---LETVNLLLNKGASLNVCDKKERQPLHwAAFLGH---L 186
Cdd:PHA02716 258 ----IDNINPEITNIYIESLDGNKVknipmiLHSYITLARnidISVVYSFLQPGVKLHYKDSAGRTCLH-QYILRHnisT 332
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27370168 187 EVLKLLVARGADLSCKDRKGYGLLHTAAA--------------SGQIEVVKHLLRMGAEIDEPNAFGNTAL 243
Cdd:PHA02716 333 DIIKLLHEYGNDLNEPDNIGNTVLHTYLSmlsvvnildpetdnDIRLDVIQCLISLGADITAVNCLGYTPL 403
|
|
| PHA02989 |
PHA02989 |
ankyrin repeat protein; Provisional |
57-355 |
2.42e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222954 [Multi-domain] Cd Length: 494 Bit Score: 48.20 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 57 LQLLLMSGANVNAK---DTLWLTPLHRAAASrnEKVLGLLLAHSADVNARDkLWQTPLhvaaanratkCAealapLLSSL 133
Cdd:PHA02989 19 LEFLLRTGFDVNEEyrgNSILLLYLKRKDVK--IKIVKLLIDNGADVNYKG-YIETPL----------CA-----VLRNR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 134 NVADRSGRSALHHAVHSG---HLETVNlllnkGASLNVCdkkerqpLHWAAFLGHLEVLKLLVARGADL-SCKDRKGYGL 209
Cdd:PHA02989 81 EITSNKIKKIVKLLLKFGadiNLKTFN-----GVSPIVC-------FIYNSNINNCDMLRFLLSKGINVnDVKNSRGYNL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 210 LHT--AAASGQIEVVKHLLRMGAEIDEP-NAFGNTALHIacYLGQDAVAIE------LVNAGANVNQPNDKGFTPLHvAA 280
Cdd:PHA02989 149 LHMylESFSVKKDVIKILLSFGVNLFEKtSLYGLTPMNI--YLRNDIDVISikvikyLIKKGVNIETNNNGSESVLE-SF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 281 VSTNGAL---CLELL--VNNGADVNYQSKEGKSPLHMAAIHGRFTRSQILIQNGSEIDCADKFGNTPLHVAARYGHELLI 355
Cdd:PHA02989 226 LDNNKILskkEFKVLnfILKYIKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDML 305
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
10-61 |
2.81e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 42.65 E-value: 2.81e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 27370168 10 PPLVQAIFSRDVEEVRSLLSQKENINVLDQERRTPLHAAAYVGDVPILQLLL 61
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
533-692 |
2.82e-05 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 48.33 E-value: 2.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 533 LEFLLDNGADPSLRDRQGYTAVHYAAAYGNRQNLELLLEMSFNC-LEDVESTvpvSPLHLAAYNGHCEALKTLAETLVNL 611
Cdd:PLN03192 541 LEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVhIRDANGN---TALWNAISAKHHKIFRILYHFASIS 617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 612 DvrDHKGRTALFLATERGSTECVEVLTAHGASALIKERKRKwTPLHAAAASGHTDSLHLLIDSGERADITDVMDAYGQTP 691
Cdd:PLN03192 618 D--PHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGA-TALQVAMAEDHVDMVRLLIMNGADVDKANTDDDFSPTE 694
|
.
gi 27370168 692 L 692
Cdd:PLN03192 695 L 695
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
237-345 |
3.20e-05 |
|
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: 47.95 E-value: 3.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 237 AFGNTALHIAC-YL--GQDAVAIELVNAGANVNQPND-----------KGFTPLHVAAVSTNgALCLELLVNNGADVNYQ 302
Cdd:cd21882 24 ATGKTCLHKAAlNLndGVNEAIMLLLEAAPDSGNPKElvnapctdefyQGQTALHIAIENRN-LNLVRLLVENGADVSAR 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 27370168 303 SKE-------------GKSPLHMAAIHGRFTRSQILIQNGSEI---DCADKFGNTPLHV 345
Cdd:cd21882 103 ATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPaalEAQDSLGNTVLHA 161
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
609-775 |
3.53e-05 |
|
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: 47.77 E-value: 3.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 609 VNLDVRDHKGRTALFLATERGST-ECVEVLTAHGASALIKErkrkwTPLHAAAASGHTD----SLHLLIDSGERADITDV 683
Cdd:TIGR00870 43 LNINCPDRLGRSALFVAAIENENlELTELLLNLSCRGAVGD-----TLLHAISLEYVDAveaiLLHLLAAFRKSGPLELA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 684 MDAY------GQTPLMLAIMNGHVDCVHLLLEKGSTADAAdlrgrtalhrgavTGCEDCLAAlLDHDAFvlcrdFKGRTP 757
Cdd:TIGR00870 118 NDQYtseftpGITALHLAAHRQNYEIVKLLLERGASVPAR-------------ACGDFFVKS-QGVDSF-----YHGESP 178
|
170
....*....|....*...
gi 27370168 758 IHLASACGHTAVLRTLLQ 775
Cdd:TIGR00870 179 LNAAACLGSPSIVALLSE 196
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
330-594 |
3.75e-05 |
|
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: 47.77 E-value: 3.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 330 SEIDCADKFGNTPLHVAARYG-HELLISTLMTNGA-----DTArrgihdmfpLHLAVLfGFSDCCRKLLSSgQLYSIVSS 403
Cdd:TIGR00870 43 LNINCPDRLGRSALFVAAIENeNLELTELLLNLSCrgavgDTL---------LHAISL-EYVDAVEAILLH-LLAAFRKS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 404 LSNEHVLSAGFDINTPDslgRTCLHAAASGGNVECLNLLLSSGADLRRRDK--------------FGRTPLHYAAANGSY 469
Cdd:TIGR00870 112 GPLELANDQYTSEFTPG---ITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSP 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 470 QCAVTLVTAGAGVNEADCKGCSPLHyAAASDTYRRAEPHTASSHdaeedellkesrrkeaffCLEFLLDNGA--DPSL-- 545
Cdd:TIGR00870 189 SIVALLSEDPADILTADSLGNTLLH-LLVMENEFKAEYEELSCQ------------------MYNFALSLLDklRDSKel 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 27370168 546 ---RDRQGYTAVHYAAAYGNRQNLELLLEMSFNCLEDVEStvPVSPLHLAAY 594
Cdd:TIGR00870 250 eviLNHQGLTPLKLAAKEGRIVLFRLKLAIKYKQKKFVAW--PNGQQLLSLY 299
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
690-741 |
3.77e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 42.26 E-value: 3.77e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 27370168 690 TPLMLAIMNGHVDCVHLLLEKGSTADAADLRGRTALHRGAVTGCEDCLAALL 741
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
13-178 |
4.09e-05 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 47.36 E-value: 4.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 13 VQAIFSRDVEEvrsLLSQKENINVLDQERRTPLHAAAYVGDVPILQLLLMSGANVNAKDTLWLTPLHRAAASRNEKV--L 90
Cdd:PHA02946 47 IKGLDERFVEE---LLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIerI 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 91 GLLLAHSADV-NARDKLWQTPLhVAAANRATKCAEALAPLLSSLNVADRSGRSALHHAVHSGH--LETVNLLLNKGASLN 167
Cdd:PHA02946 124 NLLVQYGAKInNSVDEEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDNpkASTISWMMKLGISPS 202
|
170
....*....|.
gi 27370168 168 VCDKKERQPLH 178
Cdd:PHA02946 203 KPDHDGNTPLH 213
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
43-115 |
4.15e-05 |
|
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: 47.77 E-value: 4.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 43 TPLHAAAYVGDVPILQLLLMSGANVNAK------------DTLWLT--PLHRAAASRNEKVLGLLLAHSADVNARDKLWQ 108
Cdd:TIGR00870 130 TALHLAAHRQNYEIVKLLLERGASVPARacgdffvksqgvDSFYHGesPLNAAACLGSPSIVALLSEDPADILTADSLGN 209
|
....*..
gi 27370168 109 TPLHVAA 115
Cdd:TIGR00870 210 TLLHLLV 216
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
530-570 |
4.33e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 41.88 E-value: 4.33e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 27370168 530 FFCLEFLLDNGADPSLRDRQGYTAVHYAAAYGNRQNLELLL 570
Cdd:pfam13637 14 LELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
32-81 |
4.46e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 41.95 E-value: 4.46e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 27370168 32 ENINVLDQERRTPLHAAAYVGDVPILQLLLMSGANVNAKDTLWLTPLHRA 81
Cdd:pfam13857 7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
566-814 |
4.50e-05 |
|
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: 47.57 E-value: 4.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 566 LELLLEMSFNCLEDVESTVPV---SPLHLAAYNGHCEALKTLA------------ETLVNLDVRD--HKGRTALFLATER 628
Cdd:cd21882 4 LLGLLECLRWYLTDSAYQRGAtgkTCLHKAALNLNDGVNEAIMllleaapdsgnpKELVNAPCTDefYQGQTALHIAIEN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 629 GSTECVEVLTAHGASAlikerkrkwtplhAAAASGH--TDSLHLLIdsgeraditdvmdAYGQTPLMLAIMNGHVDCVHL 706
Cdd:cd21882 84 RNLNLVRLLVENGADV-------------SARATGRffRKSPGNLF-------------YFGELPLSLAACTNQEEIVRL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 707 LLEKG---STADAADLRGRTALH------------RGAVTGCEDCLAAL---LDH-DAFVLCRDFKGRTPIHLASACGHT 767
Cdd:cd21882 138 LLENGaqpAALEAQDSLGNTVLHalvlqadntpenSAFVCQMYNLLLSYgahLDPtQQLEEIPNHQGLTPLKLAAVEGKI 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 27370168 768 AVLRTLLQAALST--DPLDAGVDYSGYSPMHWASY-------TGHEDCLELLLEHS 814
Cdd:cd21882 218 VMFQHILQREFSGpyQPLSRKFTEWTYGPVTSSLYdlseidsWEKNSVLELIAFSK 273
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
52-126 |
4.55e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 47.59 E-value: 4.55e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27370168 52 GDVPILQLLLMSGANVNAKDTLWLTPLHRAAASRNEKVLGLLLAHSADVNARDKLWQTPLHVAAANRATKCAEAL 126
Cdd:PTZ00322 93 GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
12-97 |
4.83e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 47.59 E-value: 4.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 12 LVQAIFSRDVEEVRSLLSQKENINVLDQERRTPLHAAAYVGDVPILQLLLMSGANVNAKDTLWLTPLHRAAASRNEKVLG 91
Cdd:PTZ00322 86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165
|
....*.
gi 27370168 92 LLLAHS 97
Cdd:PTZ00322 166 LLSRHS 171
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
791-843 |
5.22e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 41.88 E-value: 5.22e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 27370168 791 GYSPMHWASYTGHEDCLELLLEHS-PFSYLEGNPFTPLHCAVINNQDSTTEMLL 843
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGaDINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
191-246 |
5.33e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 41.95 E-value: 5.33e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 27370168 191 LLVARGADLSCKDRKGYGLLHTAAASGQIEVVKHLLRMGAEIDEPNAFGNTALHIA 246
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
407-637 |
5.49e-05 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 46.97 E-value: 5.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 407 EHVLSAGFDINTPDSLGRTCLHAAASGGNVECLNLLLSSGADLRRRDKFGRTPLHYAAANGS--YQCAVTLVTAGAGVNE 484
Cdd:PHA02946 56 EELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAKINN 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 485 A-DCKGCSPLhyAAASDTYRRAEPHTAS-----------SHDAEEDELLKESRRKEAffcLEFLLDNGADPSLRDRQGYT 552
Cdd:PHA02946 136 SvDEEGCGPL--LACTDPSERVFKKIMSigfearivdkfGKNHIHRHLMSDNPKAST---ISWMMKLGISPSKPDHDGNT 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 553 AVHYAAA--YGNRQNLELLLEMS----FNCLEDVESTV---PVSPLHLaaYNGHCEALKTLAETLVN----------LDV 613
Cdd:PHA02946 211 PLHIVCSktVKNVDIINLLLPSTdvnkQNKFGDSPLTLlikTLSPAHL--INKLLSTSNVITDQTVNicifydrddvLEI 288
|
250 260
....*....|....*....|....*...
gi 27370168 614 RDHKGR----TALFLATERGSTECVEVL 637
Cdd:PHA02946 289 INDKGKqydsTDFKMAVEVGSIRCVKYL 316
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
754-811 |
5.64e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 41.49 E-value: 5.64e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 27370168 754 GRTPIHLASACGHTAVLRTLLQAALSTDPldagVDYSGYSPMHWASYTGHEDCLELLL 811
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINA----VDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
92-147 |
6.36e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 41.56 E-value: 6.36e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 27370168 92 LLLAHSADVNARDKLWQTPLHVAAANRATKCAEALAPLLSSLNVADRSGRSALHHA 147
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
140-168 |
6.37e-05 |
|
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: 6.37e-05
10 20
....*....|....*....|....*....
gi 27370168 140 GRSALHHAVHSGHLETVNLLLNKGASLNV 168
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
863-932 |
6.41e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 47.20 E-value: 6.41e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 863 HAAAFADNVsGLRMLLQHQAEVNATDHTGRTALMTAAESGQTAAVEFLLYRGkADLTVLDENKNTALHLA 932
Cdd:PTZ00322 88 QLAASGDAV-GARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFG-ADPTLLDKDGKTPLELA 155
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
899-982 |
6.52e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 46.82 E-value: 6.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 899 AESGQTAAVEFLLyRGKADLTVLDENKNTALHLACSKGHEKCALMILAETQDLGLINATNsalQMPLHIAARNGLASVVQ 978
Cdd:PTZ00322 90 AASGDAVGARILL-TGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDG---KTPLELAEENGFREVVQ 165
|
....
gi 27370168 979 ALLS 982
Cdd:PTZ00322 166 LLSR 169
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
354-575 |
8.29e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 46.14 E-value: 8.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 354 LISTLMTNGADTARR----GIHDMF-------PLHLAVLFGFSDCCRKLLSSGQLYsivsslsnehvlsagfDINTPDSl 422
Cdd:PHA02875 6 LCDAILFGELDIARRlldiGINPNFeiydgisPIKLAMKFRDSEAIKLLMKHGAIP----------------DVKYPDI- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 423 gRTCLHAAASGGNVECLNLLLSSGA---DLRRRDkfGRTPLHYAAANGSYQCAVTLVTAGAGVNEADCKGCSPLHYAAAS 499
Cdd:PHA02875 69 -ESELHDAVEEGDVKAVEELLDLGKfadDVFYKD--GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMM 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27370168 500 DTYRRaephtasshdaeedellkesrrkeaffcLEFLLDNGADPSLRDRQGYTAVHYAAAYGNRQNLELLLEMSFN 575
Cdd:PHA02875 146 GDIKG----------------------------IELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGAN 193
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
271-304 |
8.84e-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: 40.74 E-value: 8.84e-05
10 20 30
....*....|....*....|....*....|....
gi 27370168 271 KGFTPLHVAAVSTNGALCLELLVNNGADVNYQSK 304
Cdd:pfam00023 1 DGNTPLHLAAGRRGNLEIVKLLLSKGADVNARDK 34
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
339-392 |
1.03e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 41.11 E-value: 1.03e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 27370168 339 GNTPLHVAARYGHELLISTLMTNGADTARRGIHDMFPLHLAVLFGFSDCCRKLL 392
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
153-275 |
1.27e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 44.42 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 153 LETVNLLLNKGASLNVCDKKER-QPLHWaaFLGH-----LEVLKLLVARGADLSCKDRKGYGLLHT--AAASGQIEVVKH 224
Cdd:PHA02859 66 VEILKFLIENGADVNFKTRDNNlSALHH--YLSFnknvePEILKILIDSGSSITEEDEDGKNLLHMymCNFNVRINVIKL 143
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 27370168 225 LLRMGAEIDEPNAFGNTALH-IACYLGQDAVAIELVNAGANVNQPNDKGFTP 275
Cdd:PHA02859 144 LIDSGVSFLNKDFDNNNILYsYILFHSDKKIFDFLTSLGIDINETNKSGYNC 195
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
375-443 |
1.30e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 40.72 E-value: 1.30e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27370168 375 PLHLAVLFGFSDCCRKLLSSGqlysivsslsnehvlsagFDINTPDSLGRTCLHAAASGGNVECLNLLL 443
Cdd:pfam13637 4 ALHAAAASGHLELLRLLLEKG------------------ADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| TRPV1 |
cd22196 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ... |
271-344 |
1.32e-04 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. 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.
Pssm-ID: 411980 [Multi-domain] Cd Length: 649 Bit Score: 45.95 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 271 KGFTPLHVAAVSTNGALcLELLVNNGADVN-------YQSKEGKS-------PLHMAAIHGRFTRSQILIQN---GSEID 333
Cdd:cd22196 93 KGQTALHIAIERRNMHL-VELLVQNGADVHarasgefFKKKKGGPgfyfgelPLSLAACTNQLDIVKFLLENphsPADIS 171
|
90
....*....|.
gi 27370168 334 CADKFGNTPLH 344
Cdd:cd22196 172 ARDSMGNTVLH 182
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
447-496 |
1.44e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 40.79 E-value: 1.44e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 27370168 447 ADLRRRDKFGRTPLHYAAANGSYQCAVTLVTAGAGVNEADCKGCSPLHYA 496
Cdd:pfam13857 7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
311-399 |
1.74e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 45.66 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 311 HMAAiHGRFTRSQILIQNGSEIDCADKFGNTPLHVAARYGHELLISTLMTNGADTARRGIHDMFPLHLAVLFGFSDCCRK 390
Cdd:PTZ00322 88 QLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166
|
....*....
gi 27370168 391 LLSSGQLYS 399
Cdd:PTZ00322 167 LSRHSQCHF 175
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
687-716 |
1.77e-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: 39.49 E-value: 1.77e-04
10 20 30
....*....|....*....|....*....|
gi 27370168 687 YGQTPLMLAIMNGHVDCVHLLLEKGSTADA 716
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
893-987 |
2.14e-04 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 45.39 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 893 TALMTAAESGQTAAVEFLLYRGKADL---TVLDEnknTALHLACSKGHEKCALMILAEtqDLGLIN-ATNSAL---QMPL 965
Cdd:cd22192 19 SPLLLAAKENDVQAIKKLLKCPSCDLfqrGALGE---TALHVAALYDNLEAAVVLMEA--APELVNePMTSDLyqgETAL 93
|
90 100
....*....|....*....|..
gi 27370168 966 HIAARNGLASVVQALLSRGATV 987
Cdd:cd22192 94 HIAVVNQNLNLVRELIARGADV 115
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
140-171 |
2.14e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. 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: 39.58 E-value: 2.14e-04
10 20 30
....*....|....*....|....*....|...
gi 27370168 140 GRSALHHAV-HSGHLETVNLLLNKGASLNVCDK 171
Cdd:pfam00023 2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
852-1017 |
2.52e-04 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 44.66 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 852 NSRDAKGRTPLHAAAFADNVSGLRMLLQHQAEVNATDHTGRTAL--MTAAESGQTAAVEFLLYRGKADLTVLDENKNTAL 929
Cdd:PHA02946 66 NETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLyyLSGTDDEVIERINLLVQYGAKINNSVDEEGCGPL 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 930 hLACSKGHEKCALMILAETQDLGLINATNSAlQMPLHIAARNGLASVVQALLSRGATVLAVDEEGHTPA-LACAPNKDVA 1008
Cdd:PHA02946 146 -LACTDPSERVFKKIMSIGFEARIVDKFGKN-HIHRHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLhIVCSKTVKNV 223
|
....*....
gi 27370168 1009 DCLALILST 1017
Cdd:PHA02946 224 DIINLLLPS 232
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
214-314 |
2.82e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 44.89 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 214 AASGQIEVVKHLLRMGAEIDEPNAFGNTALHIACYLGQDAVAIELVNAGANVNQPNDKGFTPLHVAAVSTNGALcLELLV 293
Cdd:PTZ00322 90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREV-VQLLS 168
|
90 100 110
....*....|....*....|....*....|....
gi 27370168 294 -------NNGADVNYQSKEGK------SPLHMAA 314
Cdd:PTZ00322 169 rhsqchfELGANAKPDSFTGKppsledSPISSHH 202
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
43-162 |
2.88e-04 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 45.00 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 43 TPLHAAAYVGDVPILQLLLMSGANVN---AKDTLWLT-----------PLHRAAASRNEKVLGLLLAHSADVNARDKLWQ 108
Cdd:cd22192 91 TALHIAVVNQNLNLVRELIARGADVVsprATGTFFRPgpknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGN 170
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27370168 109 TPLHVAAANRATKCAEALAPLLSSLNVADRS----------GRSALHHAVHSGHLETVNLLLNK 162
Cdd:cd22192 171 TVLHILVLQPNKTFACQMYDLILSYDKEDDLqpldlvpnnqGLTPFKLAAKEGNIVMFQHLVQK 234
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
926-981 |
3.00e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 39.57 E-value: 3.00e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 27370168 926 NTALHLACSKGHEKCALMILAETQDlglINATNSALQMPLHIAARNGLASVVQALL 981
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGAD---INAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
190-246 |
3.10e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 44.89 E-value: 3.10e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 27370168 190 KLLVARGADLSCKDRKGYGLLHTAAASGQIEVVKHLLRMGAEIDEPNAFGNTALHIA 246
Cdd:PTZ00322 99 RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELA 155
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
42-71 |
3.30e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 38.81 E-value: 3.30e-04
10 20 30
....*....|....*....|....*....|.
gi 27370168 42 RTPLHAAAY-VGDVPILQLLLMSGANVNAKD 71
Cdd:pfam00023 3 NTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
|
|
| PHA02791 |
PHA02791 |
ankyrin-like protein; Provisional |
12-167 |
4.08e-04 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165154 [Multi-domain] Cd Length: 284 Bit Score: 43.49 E-value: 4.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 12 LVQAIFSRDVEEVRSLLSQKENINVLDQErrTPLHAAAYVGDVPILQLLLMSGANVNAKDTLWLTPLHRAAASRNEKVLG 91
Cdd:PHA02791 34 LYYAIADNNVRLVCTLLNAGALKNLLENE--FPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGNMQTVK 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27370168 92 LLLAHSADVNARDKL-WQTPL-HVAAANRATKCAEALAPLLSSLNVADRsgRSALHHAVHSGHLETVNLLLNKGASLN 167
Cdd:PHA02791 112 LFVKKNWRLMFYGKTgWKTSFyHAVMLNDVSIVSYFLSEIPSTFDLAIL--LSCIHITIKNGHVDMMILLLDYMTSTN 187
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
423-449 |
4.68e-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: 38.34 E-value: 4.68e-04
10 20
....*....|....*....|....*..
gi 27370168 423 GRTCLHAAASGGNVECLNLLLSSGADL 449
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADI 28
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
156-358 |
4.90e-04 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 43.89 E-value: 4.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 156 VNLLLNKGASLNVCDKKERQPLHWAAFLGHLEVLKLLVARGADLSCKDRKGYGLLHTAAASGQ--IEVVKHLLRMGAEID 233
Cdd:PHA02946 55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAKIN 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 234 EPNAFGNTALHIACYLGQDAVAIELVNAGANVNQPNDKGFTPLHVAAVSTN-GALCLELLVNNGADVNYQSKEGKSPLHM 312
Cdd:PHA02946 135 NSVDEEGCGPLLACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDNpKASTISWMMKLGISPSKPDHDGNTPLHI 214
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 27370168 313 AAIHGRFTRSQI-LIQNGSEIDCADKFGNTPLhvaaryghELLISTL 358
Cdd:PHA02946 215 VCSKTVKNVDIInLLLPSTDVNKQNKFGDSPL--------TLLIKTL 253
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
158-213 |
5.87e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 38.87 E-value: 5.87e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 27370168 158 LLLNKGASLNVCDKKERQPLHWAAFLGHLEVLKLLVARGADLSCKDRKGYGLLHTA 213
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
618-672 |
5.98e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 38.79 E-value: 5.98e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 27370168 618 GRTALFLATERGSTECVEVLTAHGASALIKERkRKWTPLHAAAASGHTDSLHLLI 672
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDG-NGETALHFAASNGNVEVLKLLL 54
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
423-454 |
8.47e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. 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: 37.65 E-value: 8.47e-04
10 20 30
....*....|....*....|....*....|...
gi 27370168 423 GRTCLHAAA-SGGNVECLNLLLSSGADLRRRDK 454
Cdd:pfam00023 2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
950-997 |
9.99e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 38.10 E-value: 9.99e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 27370168 950 DLGLINATNSALQMPLHIAARNGLASVVQALLSRGATVLAVDEEGHTP 997
Cdd:pfam13857 5 GPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTA 52
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
486-640 |
1.09e-03 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 42.96 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 486 DCKGCSPLHYAAASDTY--------RRAEPHTASSHDAEEDELLKESRRKEAFFCLEFLL---------DNGADPSLRDR 548
Cdd:PTZ00322 2 SFLVCSVASSAFAAQLFfgtegsrkRRAKPISFERMAAIQEEIARIDTHLEALEATENKDatpdhnlttEEVIDPVVAHM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 549 QGYTAVHYAAAyGNRQNLELLLE--MSFNCLEDVESTvpvsPLHLAAYNGHCEALKTLAETLVNLDVRDHKGRTALFLAT 626
Cdd:PTZ00322 82 LTVELCQLAAS-GDAVGARILLTggADPNCRDYDGRT----PLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAE 156
|
170
....*....|....
gi 27370168 627 ERGSTECVEVLTAH 640
Cdd:PTZ00322 157 ENGFREVVQLLSRH 170
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
687-716 |
1.17e-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: 1.17e-03
10 20 30
....*....|....*....|....*....|
gi 27370168 687 YGQTPLMLAIMNGHVDCVHLLLEKGSTADA 716
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
825-878 |
1.31e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 37.64 E-value: 1.31e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 27370168 825 TPLHCAVINNQDSTTEMLLgALGAKIvNSRDAKGRTPLHAAAFADNVSGLRMLL 878
Cdd:pfam13637 3 TALHAAAASGHLELLRLLL-EKGADI-NAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
803-932 |
1.55e-03 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 42.76 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 803 HEDCLELLLEHSPFSYLEGnpfTPLHCAVINNQDSTTEMLL-------GALGAKIVNSRDA----KGRTPLHAAAFADNV 871
Cdd:TIGR00870 65 NLELTELLLNLSCRGAVGD---TLLHAISLEYVDAVEAILLhllaafrKSGPLELANDQYTseftPGITALHLAAHRQNY 141
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27370168 872 SGLRMLLQHQAEVNA---------TDHT-----GRTALMTAAESGQTAAVEFLLYRGkADLTVLDENKNTALHLA 932
Cdd:TIGR00870 142 EIVKLLLERGASVPAracgdffvkSQGVdsfyhGESPLNAAACLGSPSIVALLSEDP-ADILTADSLGNTLLHLL 215
|
|
| TRPV1-4 |
cd22193 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ... |
271-344 |
1.72e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong 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: 411977 [Multi-domain] Cd Length: 607 Bit Score: 42.48 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 271 KGFTPLHVAAVSTNGAlCLELLVNNGADVNYQSKE--------------GKSPLHMAAIHGRFTRSQILIQNG---SEID 333
Cdd:cd22193 75 EGQTALHIAIERRQGD-IVALLVENGADVHAHAKGrffqpkyqgegfyfGELPLSLAACTNQPDIVQYLLENEhqpADIE 153
|
90
....*....|.
gi 27370168 334 CADKFGNTPLH 344
Cdd:cd22193 154 AQDSRGNTVLH 164
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
140-168 |
2.00e-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: 36.47 E-value: 2.00e-03
10 20
....*....|....*....|....*....
gi 27370168 140 GRSALHHAVHSGHLETVNLLLNKGASLNV 168
Cdd:pfam13606 2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
687-718 |
2.07e-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: 36.88 E-value: 2.07e-03
10 20 30
....*....|....*....|....*....|...
gi 27370168 687 YGQTPLMLAI-MNGHVDCVHLLLEKGSTADAAD 718
Cdd:pfam00023 1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
877-932 |
2.31e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 37.33 E-value: 2.31e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 27370168 877 LLQH-QAEVNATDHTGRTALMTAAESGQTAAVEFLLYRGkADLTVLDENKNTALHLA 932
Cdd:pfam13857 1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYG-VDLNLKDEEGLTALDLA 56
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
910-968 |
2.31e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 37.33 E-value: 2.31e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 27370168 910 LLYRGKADLTVLDENKNTALHLACSKGHEKCALMILAETQDlglINATNSALQMPLHIA 968
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVD---LNLKDEEGLTALDLA 56
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
239-293 |
2.45e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 37.25 E-value: 2.45e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 27370168 239 GNTALHIACYLGQDAVAIELVNAGANVNQPNDKGFTPLHVAAVSTNGAlCLELLV 293
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVE-VLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
456-506 |
2.52e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 36.87 E-value: 2.52e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 27370168 456 GRTPLHYAAANGSYQCAVTLVTAGAGVNEADCKGCSPLHYAAASDTYRRAE 506
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLK 51
|
|
| TRPV2 |
cd22197 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ... |
334-467 |
3.16e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 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 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.
Pssm-ID: 411981 [Multi-domain] Cd Length: 640 Bit Score: 41.38 E-value: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 334 CADKF--GNTPLHVAARYGHELLISTLMTNGADTARRGIHDMFPLHLAVLFGFSDCCRKLLSSGQLYSIVSS-LSNEHVL 410
Cdd:cd22197 87 CTDEYyrGHSALHIAIEKRSLQCVKLLVENGADVHARACGRFFQKKQGTCFYFGELPLSLAACTKQWDVVNYlLENPHQP 166
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27370168 411 SAgfdINTPDSLGRTCLHAAA-----SGGNVECL----NLLLSSGADLRRRDKF-------GRTPLHYAAANG 467
Cdd:cd22197 167 AS---LQAQDSLGNTVLHALVmiadnSPENSALVikmyDGLLQAGARLCPTVQLeeisnheGLTPLKLAAKEG 236
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
306-467 |
3.28e-03 |
|
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: 41.40 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 306 GKSPLHMAAIH---GRFTRSQILIQNGSEID---------CADKF--GNTPLHVAARYGHELLISTLMTNGADTARRGIH 371
Cdd:cd21882 26 GKTCLHKAALNlndGVNEAIMLLLEAAPDSGnpkelvnapCTDEFyqGQTALHIAIENRNLNLVRLLVENGADVSARATG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 372 DMFPLHLAVLFGFSDCCRKLLSSGQLYSIVSSL-SNEHVLSagfDINTPDSLGRTCLHAAASGGN---------VECLNL 441
Cdd:cd21882 106 RFFRKSPGNLFYFGELPLSLAACTNQEEIVRLLlENGAQPA---ALEAQDSLGNTVLHALVLQADntpensafvCQMYNL 182
|
170 180 190
....*....|....*....|....*....|...
gi 27370168 442 LLSSGADLRRRDKF-------GRTPLHYAAANG 467
Cdd:cd21882 183 LLSYGAHLDPTQQLeeipnhqGLTPLKLAAVEG 215
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
962-1029 |
3.32e-03 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 41.42 E-value: 3.32e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27370168 962 QMPLHIAARNGLASVVQALLSRGATVLAVDEEGHTPaLACAPNKDVADCLALILSTMKPFPPKDAVSP 1029
Cdd:PTZ00322 116 RTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTP-LELAEENGFREVVQLLSRHSQCHFELGANAK 182
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
176-204 |
3.78e-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: 36.11 E-value: 3.78e-03
10 20 30
....*....|....*....|....*....|
gi 27370168 176 PLHWAA-FLGHLEVLKLLVARGADLSCKDR 204
Cdd:pfam00023 5 PLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
860-1031 |
3.93e-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: 41.15 E-value: 3.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 860 TPLHAAAFADNVSGL-RMLLQHQAEVNATDHTGRTALMTAAESGQTAAVEFL---------------LYRGKadltvlde 923
Cdd:cd22192 19 SPLLLAAKENDVQAIkKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLmeaapelvnepmtsdLYQGE-------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 924 nknTALHLACSKGHEKCALMILAETQDLGLINATNSAL-----------QMPLHIAARNGLASVVQALLSRGATVLAVDE 992
Cdd:cd22192 91 ---TALHIAVVNQNLNLVRELIARGADVVSPRATGTFFrpgpknliyygEHPLSFAACVGNEEIVRLLIEHGADIRAQDS 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 27370168 993 EGHTP--ALACAPNKDVAdCLA--LILSTMKP--------FPPKDAVSPFS 1031
Cdd:cd22192 168 LGNTVlhILVLQPNKTFA-CQMydLILSYDKEddlqpldlVPNNQGLTPFK 217
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
456-484 |
3.95e-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: 35.64 E-value: 3.95e-03
10 20
....*....|....*....|....*....
gi 27370168 456 GRTPLHYAAANGSYQCAVTLVTAGAGVNE 484
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
857-889 |
4.05e-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: 35.73 E-value: 4.05e-03
10 20 30
....*....|....*....|....*....|....
gi 27370168 857 KGRTPLHAAA-FADNVSGLRMLLQHQAEVNATDH 889
Cdd:pfam00023 1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
|
|
| TRPV1 |
cd22196 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ... |
609-726 |
4.38e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. 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.
Pssm-ID: 411980 [Multi-domain] Cd Length: 649 Bit Score: 40.94 E-value: 4.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 609 VNLDVRD--HKGRTALFLATERGSTECVEVLTAHGASalikerkrkwtpLHAAAasghtdslhllidSGERADITDVMDA 686
Cdd:cd22196 83 VNAAYTDsyYKGQTALHIAIERRNMHLVELLVQNGAD------------VHARA-------------SGEFFKKKKGGPG 137
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 27370168 687 --YGQTPLMLAIMNGHVDCVHLLLE---KGSTADAADLRGRTALH 726
Cdd:cd22196 138 fyFGELPLSLAACTNQLDIVKFLLEnphSPADISARDSMGNTVLH 182
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
654-708 |
4.59e-03 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 41.04 E-value: 4.59e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 27370168 654 TPLHAAAASGHTDSLHLLIDSGerADITdVMDAYGQTPLMLAIMNGHVDCVHLLL 708
Cdd:PTZ00322 117 TPLHIACANGHVQVVRVLLEFG--ADPT-LLDKDGKTPLELAEENGFREVVQLLS 168
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
550-604 |
4.64e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 36.10 E-value: 4.64e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 27370168 550 GYTAVHYAAAYGNRQNLELLLEMSFNCLEDVESTVPvsPLHLAAYNGHCEALKTL 604
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGET--ALHFAASNGNVEVLKLL 53
|
|
| PHA02741 |
PHA02741 |
hypothetical protein; Provisional |
186-325 |
4.86e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 165108 [Multi-domain] Cd Length: 169 Bit Score: 39.26 E-value: 4.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 186 LEVLKLLVARGADLSCKDRKGYGLLHTAAASGQIEVVKHLL------RMGAEIDEPNAFGNTALHIACYLGQDAVAIE-- 257
Cdd:PHA02741 1 MESPHFMTCLEEMIAEKNSEGENFFHEAARCGCFDIIARFTpfirgdCHAAALNATDDAGQMCIHIAAEKHEAQLAAEii 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27370168 258 --LVNAGANVN-QPNDKGFTPLHVAAVSTNGALCLELLVNNGADVNYQSKEGKSPLHMAAIHGRFTRSQIL 325
Cdd:PHA02741 81 dhLIELGADINaQEMLEGDTALHLAAHRRDHDLAEWLCCQPGIDLHFCNADNKSPFELAIDNEDVAMMQIL 151
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
791-815 |
5.05e-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: 35.64 E-value: 5.05e-03
|
| PHA02884 |
PHA02884 |
ankyrin repeat protein; Provisional |
209-313 |
5.08e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165212 [Multi-domain] Cd Length: 300 Bit Score: 40.35 E-value: 5.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 209 LLHTAAASGQIEVVKHLLRMGAEIDEP-----NAFGNTALHIACYLGQDAvAIELVNAGANVNQ-PNDKGFTPLHVAAVS 282
Cdd:PHA02884 36 ILYSSIKFHYTDIIDAILKLGADPEAPfplseNSKTNPLIYAIDCDNDDA-AKLLIRYGADVNRyAEEAKITPLYISVLH 114
|
90 100 110
....*....|....*....|....*....|.
gi 27370168 283 TNGAlCLELLVNNGADVNYQSKEGKSPLHMA 313
Cdd:PHA02884 115 GCLK-CLEILLSYGADINIQTNDMVTPIELA 144
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
132-180 |
5.18e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 36.17 E-value: 5.18e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 27370168 132 SLNVADRSGRSALHHAVHSGHLETVNLLLNKGASLNVCDKKERQPLHWA 180
Cdd:pfam13857 8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
42-69 |
5.30e-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: 35.26 E-value: 5.30e-03
10 20
....*....|....*....|....*...
gi 27370168 42 RTPLHAAAYVGDVPILQLLLMSGANVNA 69
Cdd:smart00248 3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PHA02989 |
PHA02989 |
ankyrin repeat protein; Provisional |
219-496 |
5.59e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222954 [Multi-domain] Cd Length: 494 Bit Score: 40.49 E-value: 5.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 219 IEVVKHLLRMGAEIDEPNAfGNTALHIacYLGQDAVAIE----LVNAGANVNQpndKGF--TPLhvAAVSTNGALC---- 288
Cdd:PHA02989 16 KNALEFLLRTGFDVNEEYR-GNSILLL--YLKRKDVKIKivklLIDNGADVNY---KGYieTPL--CAVLRNREITsnki 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 289 ---LELLVNNGADVNYQSKEGKSPLhMAAIHGrftrsqiliqngSEIDCADkfgntplhvaaryghelLISTLMTNGADT 365
Cdd:PHA02989 88 kkiVKLLLKFGADINLKTFNGVSPI-VCFIYN------------SNINNCD-----------------MLRFLLSKGINV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 366 ARRGIHDMFPLHLAVLFGFS---DCCRKLLSSG-------QLY-------------SIVSSLSNEHVLSAGFDINTPDSL 422
Cdd:PHA02989 138 NDVKNSRGYNLLHMYLESFSvkkDVIKILLSFGvnlfektSLYgltpmniylrndiDVISIKVIKYLIKKGVNIETNNNG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 423 GRTCL------HAAASGGNVECLNLLLSSgADLRRRDKFGRTPLHYAAANGSYQCAVTLVTAGAGVNEADCKGCSPLHYA 496
Cdd:PHA02989 218 SESVLesfldnNKILSKKEFKVLNFILKY-IKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYA 296
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
721-913 |
5.86e-03 |
|
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: 40.63 E-value: 5.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 721 GRTALHRGAV---TGCEDCLAALLDHD-----------AFVLCRDFKGRTPIHLASACGHTAVLRTLLQAALSTDPLDAG 786
Cdd:cd21882 26 GKTCLHKAALnlnDGVNEAIMLLLEAApdsgnpkelvnAPCTDEFYQGQTALHIAIENRNLNLVRLLVENGADVSARATG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 787 ---------VDYSGYSPMHWASYTGHEDCLELLLEHspfsylegnpftPLHCAVINNQDSTTEMLLGALGAKIVNSRDak 857
Cdd:cd21882 106 rffrkspgnLFYFGELPLSLAACTNQEEIVRLLLEN------------GAQPAALEAQDSLGNTVLHALVLQADNTPE-- 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27370168 858 grtplhAAAFAdnVSGLRMLLQHQAEVNAT-------DHTGRTALMTAAESGQTAAVEFLLYR 913
Cdd:cd21882 172 ------NSAFV--CQMYNLLLSYGAHLDPTqqleeipNHQGLTPLKLAAVEGKIVMFQHILQR 226
|
|
| TRPV1-4 |
cd22193 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ... |
765-913 |
6.29e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong 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: 411977 [Multi-domain] Cd Length: 607 Bit Score: 40.55 E-value: 6.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 765 GHTAVLRTLLQAALSTDPLDAGVD-------YSGYSPMHWASYTGHEDCLELLLE-------------------HSPFSY 818
Cdd:cd22193 43 GTNDTIRILLDIAEKTDNLKRFINaeytdeyYEGQTALHIAIERRQGDIVALLVEngadvhahakgrffqpkyqGEGFYF 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 819 LEgnpfTPLHCAVINNQDSTTEMLLGALGAKI-VNSRDAKGRTPLHA-AAFADN--------VSGLRMLLQHQAEVNAT- 887
Cdd:cd22193 123 GE----LPLSLAACTNQPDIVQYLLENEHQPAdIEAQDSRGNTVLHAlVTVADNtkentkfvTRMYDMILIRGAKLCPTv 198
|
170 180 190
....*....|....*....|....*....|..
gi 27370168 888 ------DHTGRTALMTAAESGQTAAVEFLLYR 913
Cdd:cd22193 199 eleeirNNDGLTPLQLAAKMGKIEILKYILQR 230
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
76-105 |
6.63e-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: 6.63e-03
10 20 30
....*....|....*....|....*....|.
gi 27370168 76 TPLHRAAASR-NEKVLGLLLAHSADVNARDK 105
Cdd:pfam00023 4 TPLHLAAGRRgNLEIVKLLLSKGADVNARDK 34
|
|
| TRPV1 |
cd22196 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ... |
857-930 |
6.66e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. 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.
Pssm-ID: 411980 [Multi-domain] Cd Length: 649 Bit Score: 40.56 E-value: 6.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 857 KGRTPLHAAAFADNVSGLRMLLQHQAEVNATD--------------HTGRTALMTAAESGQTAAVEFLLYR--GKADLTV 920
Cdd:cd22196 93 KGQTALHIAIERRNMHLVELLVQNGADVHARAsgeffkkkkggpgfYFGELPLSLAACTNQLDIVKFLLENphSPADISA 172
|
90
....*....|
gi 27370168 921 LDENKNTALH 930
Cdd:cd22196 173 RDSMGNTVLH 182
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
11-171 |
6.71e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 39.03 E-value: 6.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 11 PLVQAIFSRDVEEVRSLLSQKENINVLDQerrTPLHAA---AYVgDVPILQLLLMSGANVNAKDTLW-LTPLHRAAA--- 83
Cdd:PHA02859 24 PLFYYVEKDDIEGVKKWIKFVNDCNDLYE---TPIFSClekDKV-NVEILKFLIENGADVNFKTRDNnLSALHHYLSfnk 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 84 SRNEKVLGLLLAHSADVNARDKLWQTPLHVAAANRATK--CAEALAPLLSSLNVADRSGRSALHHAV--HSGHlETVNLL 159
Cdd:PHA02859 100 NVEPEILKILIDSGSSITEEDEDGKNLLHMYMCNFNVRinVIKLLIDSGVSFLNKDFDNNNILYSYIlfHSDK-KIFDFL 178
|
170
....*....|..
gi 27370168 160 LNKGASLNVCDK 171
Cdd:PHA02859 179 TSLGIDINETNK 190
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
235-279 |
7.24e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 35.79 E-value: 7.24e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 27370168 235 PNAFGNTALHIACYLGQDAVAIELVNAGANVNQPNDKGFTPLHVA 279
Cdd:pfam13857 12 LDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
239-270 |
8.48e-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: 34.96 E-value: 8.48e-03
10 20 30
....*....|....*....|....*....|...
gi 27370168 239 GNTALHIACY-LGQDAVAIELVNAGANVNQPND 270
Cdd:pfam00023 2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
205-234 |
9.21e-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: 34.93 E-value: 9.21e-03
10 20 30
....*....|....*....|....*....|
gi 27370168 205 KGYGLLHTAAASGQIEVVKHLLRMGAEIDE 234
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
793-931 |
9.22e-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: 40.00 E-value: 9.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370168 793 SPMHWASYTGHEDCLELLLEHSPFSYLEGNPF--TPLHCAVINNQDSTTEMLLGAlGAKIVN----SRDAKGRTPLHAAA 866
Cdd:cd22192 19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALgeTALHVAALYDNLEAAVVLMEA-APELVNepmtSDLYQGETALHIAV 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27370168 867 FADNVSGLRMLLQHQAEVN---ATD-----------HTGRTALMTAAESGQTAAVEFLLYRGkADLTVLDENKNTALHL 931
Cdd:cd22192 98 VNQNLNLVRELIARGADVVsprATGtffrpgpknliYYGEHPLSFAACVGNEEIVRLLIEHG-ADIRAQDSLGNTVLHI 175
|
|
| PHA02736 |
PHA02736 |
Viral ankyrin protein; Provisional |
423-472 |
9.23e-03 |
|
Viral ankyrin protein; Provisional
Pssm-ID: 165103 [Multi-domain] Cd Length: 154 Bit Score: 37.93 E-value: 9.23e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 27370168 423 GRTCLHAAASGGNV---ECLNLLLSSGADLRRRD-KFGRTPLHYAAANGSYQCA 472
Cdd:PHA02736 55 GKQCVHIVSNPDKAdpqEKLKLLMEWGADINGKErVFGNTPLHIAVYTQNYELA 108
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
339-364 |
9.29e-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: 34.87 E-value: 9.29e-03
10 20
....*....|....*....|....*.
gi 27370168 339 GNTPLHVAARYGHELLISTLMTNGAD 364
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGAD 27
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
176-201 |
9.85e-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: 34.87 E-value: 9.85e-03
10 20
....*....|....*....|....*.
gi 27370168 176 PLHWAAFLGHLEVLKLLVARGADLSC 201
Cdd:smart00248 5 PLHLAAENGNLEVVKLLLDKGADINA 30
|
|
|