|
Name |
Accession |
Description |
Interval |
E-value |
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
56-343 |
1.70e-51 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 183.23 E-value: 1.70e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 56 IMDLLISAGANVNAKDHVWLTPLHRAAASRNERAVGLLLRKGADVTARDKYWQTPLHIAAANRATRCVETLLPHVSSLNM 135
Cdd:COG0666 3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 136 ADRTGRAPLHHAAQSGYQEMVKLLLNKGANLSASDKKDRQPIHWAAYLGHLEVVKLLVSQGSDKSCKDKRGYTPLHAAAA 215
Cdd:COG0666 83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 216 SGHVDVVKYLLRNGAEIDEPNAFGNTALHVACYTGQEAVANELVNRGANVNQPNHRGYTPLHLAAVSTNGALcLELLVNN 295
Cdd:COG0666 163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI-VKLLLEA 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 66392221 296 GADVNMQSKEGKSPLHMAAIHGRFTRSQILIQNGGEIDCVDRYGNTPL 343
Cdd:COG0666 242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
21-300 |
4.74e-49 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 176.30 E-value: 4.74e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 21 ADEVKLFLHKKDEVNALDQERRTPLHAAAWLGDVHIMDLLISAGANVNAKDHVWLTPLHRAAASRNERAVGLLLRKGADV 100
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 101 TARDKYWQTPLHIAAANRATRCVETLLPHVSSLNMADRTGRAPLHHAAQSGYQEMVKLLLNKGANLSASDKKDRQPIHWA 180
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 181 AYLGHLEVVKLLVSQGSDKSCKDKRGYTPLHAAAASGHVDVVKYLLRNGAEIDEPNAFGNTALHVACYTGQEAVANELVN 260
Cdd:COG0666 161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 66392221 261 RGANVNQPNHRGYTPLHLAAVSTNGALCLELLVNNGADVN 300
Cdd:COG0666 241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAA 280
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
5-276 |
3.48e-48 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 173.60 E-value: 3.48e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 5 NISDQPPLVQAIFNRNADEVKLFLHKKDEVNALDQERRTPLHAAAWLGDVHIMDLLISAGANVNAKDHVWLTPLHRAAAS 84
Cdd:COG0666 18 LLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 85 RNERAVGLLLRKGADVTARDKYWQTPLHIAAANRATRCVETLLPHVSSLNMADRTGRAPLHHAAQSGYQEMVKLLLNKGA 164
Cdd:COG0666 98 GDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 165 NLSASDKKDRQPIHWAAYLGHLEVVKLLVSQGSDKSCKDKRGYTPLHAAAASGHVDVVKYLLRNGAEIDEPNAFGNTALH 244
Cdd:COG0666 178 DVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALL 257
|
250 260 270
....*....|....*....|....*....|..
gi 66392221 245 VACYTGQEAVANELVNRGANVNQPNHRGYTPL 276
Cdd:COG0666 258 LAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
186-493 |
1.33e-39 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 148.95 E-value: 1.33e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 186 LEVVKLLVSQGSDKSCKDKRGYTPLHAAAASGHVDVVKYLLRNGAEIDEPNAFGNTALHVACYTGQEAVANELVNRGANV 265
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 266 NQPNHRGYTPLHLAAVSTNGALcLELLVNNGADVNMQSKEGKSPLHMAAIHGRFTRSQILIQNGGEIDCVDRYGNTPLHV 345
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEI-VKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 346 AAKYGHELLISTLMTNGADTARQGIHGMFPLHLAVLYGSSDCCRKLlssgqlysivlsmskehvLSAGFDINTPDNFGRT 425
Cdd:COG0666 160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL------------------LEAGADVNAKDNDGKT 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66392221 426 CLHAAASGGNIECLNLLLSSGADMNKKDKFGRTPLHYAAANGRYQCVVVLVGAGAEVNERDRSGCTPL 493
Cdd:COG0666 222 ALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
53-317 |
7.63e-37 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 145.55 E-value: 7.63e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 53 DVHIMDLLISAGANVNAKDHVWLTPLHRAAASRNE---RAVGLLLRKGADVTARDKYWQTPLHIAAANRAT-RCVETLLP 128
Cdd:PHA03095 26 TVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEkvkDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 129 HVSSLNMADRTGRAPLH-HAA-QSGYQEMVKLLLNKGANLSASDKKDRQPIHwaAYLGH----LEVVKLLVSQGSDKSCK 202
Cdd:PHA03095 106 AGADVNAKDKVGRTPLHvYLSgFNINPKVIRLLLRKGADVNALDLYGMTPLA--VLLKSrnanVELLRLLIDAGADVYAV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 203 DKRGYTPLHAAAASGHVD--VVKYLLRNGAEIDEPNAFGNTALHV-ACYTGQEA--VANeLVNRGANVNQPNHRGYTPLH 277
Cdd:PHA03095 184 DDRFRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSmATGSSCKRslVLP-LLIAGISINARNRYGQTPLH 262
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 66392221 278 LAAVSTNGALCLELLvNNGADVNMQSKEGKSPLHMAAIHG 317
Cdd:PHA03095 263 YAAVFNNPRACRRLI-ALGADINAVSSDGNTPLSLMVRNN 301
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
289-602 |
1.62e-36 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 140.09 E-value: 1.62e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 289 LELLVNNGADVNMQSKEGKSPLHMAAIHGRFTRSQILIQNGGEIDCVDRYGNTPLHVAAKYGHELLISTLMTNGADTARQ 368
Cdd:COG0666 4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 369 GIHGMFPLHLAVLYGSSDCCRKLLSsgqlysivlsmskehvlsAGFDINTPDNFGRTCLHAAASGGNIECLNLLLSSGAD 448
Cdd:COG0666 84 DDGGNTLLHAAARNGDLEIVKLLLE------------------AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGAD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 449 MNKKDKFGRTPLHYAAANGRYQCVVVLVGAGAEVNERDRSGCTPLHYsaastafcrtdrphASTHQNQEdgekesflCVE 528
Cdd:COG0666 146 VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHL--------------AAENGHLE--------IVK 203
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66392221 529 HLLDNGADPCLCNTKGYSAVHYAAAHGNKQNLELLLEMcfNTLGDKESNGSISPLHLAVESGHWECVTVLIESG 602
Cdd:COG0666 204 LLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA--GADLNAKDKDGLTALLLAAAAGAALIVKLLLLAL 275
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
530-771 |
1.89e-33 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 130.84 E-value: 1.89e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 530 LLDNGADPCLCNTKGYSAVHYAAAHGNKQNLELLLEMCFNTlgDKESNGSISPLHLAVESGHWECVTVLIESGVCVDVCD 609
Cdd:COG0666 40 LLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI--NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARD 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 610 PVGRSVLYLASQRGHSRCVELLLSQSAScLLAEHRSKWGPLHVAAANGHSECLRMLLcsEGGADlVNVTDAEGQTPLMLA 689
Cdd:COG0666 118 KDGETPLHLAAYNGNLEIVKLLLEAGAD-VNAQDNDGNTPLHLAAANGNLEIVKLLL--EAGAD-VNARDNDGETPLHLA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 690 VLGGHTDCVHLLLERGACPDMKDRRGRTALHRGAVMGREDCLTALLSHNVSVLSRDFQGRSALHLAASCGHADILSNLLS 769
Cdd:COG0666 194 AENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLL 273
|
..
gi 66392221 770 AA 771
Cdd:COG0666 274 AL 275
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
541-808 |
6.16e-33 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 129.69 E-value: 6.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 541 NTKGYSAVHYAAAHGNKQNLELLLEMCFNTLGDKESNGSISPLHLAVESGHWECVTVLIESGVCVDVCDPVGRSVLYLAS 620
Cdd:COG0666 16 LLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 621 QRGHSRCVELLLSQSAScLLAEHRSKWGPLHVAAANGHSECLRMLLcsEGGADlVNVTDAEGQTPLMLAVLGGHTDCVHL 700
Cdd:COG0666 96 RNGDLEIVKLLLEAGAD-VNARDKDGETPLHLAAYNGNLEIVKLLL--EAGAD-VNAQDNDGNTPLHLAAANGNLEIVKL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 701 LLERGACPDMKDRRGRTALHRGAVMGREDCLTALLSHNVSVLSRDFQGRSALHLAASCGHADILSNLLSAADhsqpQDPL 780
Cdd:COG0666 172 LLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA----DLNA 247
|
250 260
....*....|....*....|....*...
gi 66392221 781 TDRHGYTPAHWAAYHGHEDCLEVLLELK 808
Cdd:COG0666 248 KDKDGLTALLLAAAAGAALIVKLLLLAL 275
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
53-384 |
1.67e-32 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 135.58 E-value: 1.67e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 53 DVHIMDLLISAGANVNAKDHVWLTPLHRAAASRNERAVGLLLRKGADVTARDKYWQTPLHIAAANRATRCVETLLPHVSS 132
Cdd:PHA02876 157 ELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSN 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 133 LNMADRTgrapLHHAAQSGYQEMVKLLLNKGANLSASDKKDRQPIHWAAYLGHL-EVVKLLVSQGSDKSCKDKRGYTPLH 211
Cdd:PHA02876 237 INKNDLS----LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLY 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 212 AAAASGH-VDVVKYLLRNGAEIDEPNAFGNTALHVACYTGQ-EAVANELVNRGANVNQPNHRGYTPLHLAAVStNGALCL 289
Cdd:PHA02876 313 LMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDRnKDIVITLLELGANVNARDYCDKTPIHYAAVR-NNVVII 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 290 ELLVNNGADVNMQSKEGKSPLHMaAIHGR--FTRSQILIQNGGEIDCVDRYGNTPLHVAAKYGHEL-LISTLMTNGADTA 366
Cdd:PHA02876 392 NTLLDYGADIEALSQKIGTALHF-ALCGTnpYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKLdVIEMLLDNGADVN 470
|
330
....*....|....*...
gi 66392221 367 RQGIHGMFPLHLAVLYGS 384
Cdd:PHA02876 471 AINIQNQYPLLIALEYHG 488
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
25-364 |
2.31e-32 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 134.81 E-value: 2.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 25 KLFLHKKDEVNALDQERRTPLHAAAWLGDVHIMDLLISAGANVNAKDHVWLTPLHRAAASRNERAVGLLLRKGADVTARD 104
Cdd:PHA02876 162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKND 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 105 kywqtpLHIAAANRATRCVETLLPHVS--SLNMADRTGRAPLHHAAQS-GYQEMVKLLLNKGANLSASDKKDRQPIHWAA 181
Cdd:PHA02876 242 ------LSLLKAIRNEDLETSLLLYDAgfSVNSIDDCKNTPLHHASQApSLSRLVPKLLERGADVNAKNIKGETPLYLMA 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 182 YLGH-LEVVKLLVSQGSDKSCKDKRGYTPLHAAAA-SGHVDVVKYLLRNGAEIDEPNAFGNTALHVACYTGQEAVANELV 259
Cdd:PHA02876 316 KNGYdTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLL 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 260 NRGANVNQPNHRGYTPLHLAAVSTNGALCLELLVNNGADVNMQSKEGKSPLHMAAIHG-RFTRSQILIQNGGEIDCVDRY 338
Cdd:PHA02876 396 DYGADIEALSQKIGTALHFALCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQ 475
|
330 340
....*....|....*....|....*.
gi 66392221 339 GNTPLHVAAKYghELLISTLMTNGAD 364
Cdd:PHA02876 476 NQYPLLIALEY--HGIVNILLHYGAE 499
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
66-301 |
4.65e-32 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 130.17 E-value: 4.65e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 66 NVNAKDHVwlTPLHRAAASRNERAVGLLLRKGADVTARDKYWQTPLHIAAANRA--TRCVET---LLPHVSSLNMADRTG 140
Cdd:PHA03100 29 DYSYKKPV--LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnlTDVKEIvklLLEYGANVNAPDNNG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 141 RAPLHHAAQ--SGYQEMVKLLLNKGANLSASDKKDRQPIHWAAYLGH--LEVVKLLVSQGSDKSCKDKrgytplhaaaas 216
Cdd:PHA03100 107 ITPLLYAISkkSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKNR------------ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 217 ghvdvVKYLLRNGAEIDEPNAFGNTALHVACYTGQEAVANELVNRGANVNQPNHRGYTPLHLAAVSTNGALcLELLVNNG 296
Cdd:PHA03100 175 -----VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEI-FKLLLNNG 248
|
....*
gi 66392221 297 ADVNM 301
Cdd:PHA03100 249 PSIKT 253
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
580-853 |
4.90e-31 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 123.91 E-value: 4.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 580 ISPLHLAVESGHWECVTVLIESGVCVDVCDPVGRSVLYLASQRGHSRCVELLLSQSAScLLAEHRSKWGPLHVAAANGHS 659
Cdd:COG0666 22 ALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGAD-INAKDDGGNTLLHAAARNGDL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 660 ECLRMLLcsEGGADlVNVTDAEGQTPLMLAVLGGHTDCVHLLLERGACPDMKDRRGRTALHRGAVMGREDCLTALLSHNV 739
Cdd:COG0666 101 EIVKLLL--EAGAD-VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 740 SVLSRDFQGRSALHLAASCGHADILSNLLSA-ADHSqpqdpLTDRHGYTPAHWAAYHGHEDCLEVLLE-LKPCSIQEGNP 817
Cdd:COG0666 178 DVNARDNDGETPLHLAAENGHLEIVKLLLEAgADVN-----AKDNDGKTALDLAAENGNLEIVKLLLEaGADLNAKDKDG 252
|
250 260 270
....*....|....*....|....*....|....*.
gi 66392221 818 FTPLHCALINGHSGSAELLLESSVCNSLVNIRDAKG 853
Cdd:COG0666 253 LTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
186-472 |
8.78e-31 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 127.45 E-value: 8.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 186 LEVVKLLVSQGSDKSCKDKRGYTPLHAAAASGH---VDVVKYLLRNGAEIDEPNAFGNTALHV-ACYTGQEAVANELVNR 261
Cdd:PHA03095 27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLyLYNATTLDVIKLLIKA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 262 GANVNQPNHRGYTPLH--LAAVSTNgALCLELLVNNGADVNMQSKEGKSPLHmaaIHGRFTRSQI-----LIQNGGEIDC 334
Cdd:PHA03095 107 GADVNAKDKVGRTPLHvyLSGFNIN-PKVIRLLLRKGADVNALDLYGMTPLA---VLLKSRNANVellrlLIDAGADVYA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 335 VDRYGNTPLHVAAKYGH--ELLISTLMTNGADTARQGIHGMFPLHLAVLYGSsdcCRKllssgqlySIVLSmskehVLSA 412
Cdd:PHA03095 183 VDDRFRSLLHHHLQSFKprARIVRELIRAGCDPAATDMLGNTPLHSMATGSS---CKR--------SLVLP-----LLIA 246
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 413 GFDINTPDNFGRTCLHAAASGGNIECLNLLLSSGADMNKKDKFGRTPLHYAAANGRYQCV 472
Cdd:PHA03095 247 GISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAV 306
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
25-364 |
1.11e-30 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 126.62 E-value: 1.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 25 KLFLHKKDEVNALDQERRTPLHAAAWLGDVHIMDLLISAGANVNAKDHVWLTPLHRAAASRNERAVGLLLRKGADVTard 104
Cdd:PHA02874 19 KIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTS--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 105 kywqtplhiaaanratrcvetLLPhVSSLNmadrtgraplhhaaqsgyQEMVKLLLNKGANLSASDKKDRQPIHWAAYLG 184
Cdd:PHA02874 96 ---------------------ILP-IPCIE------------------KDMIKTILDCGIDVNIKDAELKTFLHYAIKKG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 185 HLEVVKLLVSQGSDKSCKDKRGYTPLHAAAASGHVDVVKYLLRNGAEIDEPNAFGNTALHVACYTGQEAVANELVNRGAN 264
Cdd:PHA02874 136 DLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNH 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 265 VNQPNHRGYTPLHLAAVSTNGAlcLELLVNNgADVNMQSKEGKSPLHMaAIHGRFTRS--QILIQNGGEIDCVDRYGNTP 342
Cdd:PHA02874 216 IMNKCKNGFTPLHNAIIHNRSA--IELLINN-ASINDQDIDGSTPLHH-AINPPCDIDiiDILLYHKADISIKDNKGENP 291
|
330 340
....*....|....*....|....*...
gi 66392221 343 LHVAAKYGH------ELLISTLMTNGAD 364
Cdd:PHA02874 292 IDTAFKYINkdpvikDIIANAVLIKEAD 319
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
19-266 |
2.15e-30 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 125.16 E-value: 2.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 19 RNADEVKLFLHKKDEVN-ALDQERRTPLHAAAWLGDVHIMDLLISAGANVNAKDHVWLTPLH-----RAAASRNERAVGL 92
Cdd:PHA03100 12 IIKVKNIKYIIMEDDLNdYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHylsniKYNLTDVKEIVKL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 93 LLRKGADVTARDKYWQTPLHIAAANRA--TRCVETLLPHVSSLNMADRTGRAPLHHAAQSGYQ--EMVKLLLNKGANLsa 168
Cdd:PHA03100 92 LLEYGANVNAPDNNGITPLLYAISKKSnsYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDI-- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 169 sDKKDRqpihwaaylghlevVKLLVSQGSDKSCKDKRGYTPLHAAAASGHVDVVKYLLRNGAEIDEPNAFGNTALHVACY 248
Cdd:PHA03100 170 -NAKNR--------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAIL 234
|
250
....*....|....*...
gi 66392221 249 TGQEAVANELVNRGANVN 266
Cdd:PHA03100 235 NNNKEIFKLLLNNGPSIK 252
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
219-555 |
3.72e-30 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 125.52 E-value: 3.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 219 VDVVKYLLRNGAEIDEPNAFGNTALHVACYTGQEAVA---NELVNRGANVNQPNHRGYTPLHLAAVSTNGALCLELLVNN 295
Cdd:PHA03095 27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKdivRLLLEAGADVNAPERCGFTPLHLYLYNATTLDVIKLLIKA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 296 GADVNMQSKEGKSPLHmAAIHGRFTRS---QILIQNGGEIDCVDRYGNTPLHVaakygheLLISTLMTngADTARqgihg 372
Cdd:PHA03095 107 GADVNAKDKVGRTPLH-VYLSGFNINPkviRLLLRKGADVNALDLYGMTPLAV-------LLKSRNAN--VELLR----- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 373 MFPLHLAVLYGSSDCCRKLLSSGQLY-----SIVlsmskEHVLSAGFDINTPDNFGRTCLHAAASGGNIECLNL--LLSS 445
Cdd:PHA03095 172 LLIDAGADVYAVDDRFRSLLHHHLQSfkpraRIV-----RELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 446 GADMNKKDKFGRTPLHYAAANGRYQCVVVLVGAGAEVNERDRSGCTPL------HYSAASTAFCRTdRPHASTHQNQedg 519
Cdd:PHA03095 247 GISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLslmvrnNNGRAVRAALAK-NPSAETVAAT--- 322
|
330 340 350
....*....|....*....|....*....|....*.
gi 66392221 520 ekesflcVEHLLDNGADPCLCNTKgySAVHYAAAHG 555
Cdd:PHA03095 323 -------LNTASVAGGDIPSDATR--LCVAKVVLRG 349
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
672-951 |
1.14e-29 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 120.06 E-value: 1.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 672 ADLVNVTDAEGQTPLMLAVLGGHTDCVHLLLERGACPDMKDRRGRTALHRGAVMGREDCLTALLSHNVSVLSRDFQGRSA 751
Cdd:COG0666 11 LLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 752 LHLAASCGHADILSNLLSAADhsqpqDP-LTDRHGYTPAHWAAYHGHEDCLEVLLELK-PCSIQEGNPFTPLHCALINGH 829
Cdd:COG0666 91 LHAAARNGDLEIVKLLLEAGA-----DVnARDKDGETPLHLAAYNGNLEIVKLLLEAGaDVNAQDNDGNTPLHLAAANGN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 830 SGSAELLLESsvcNSLVNIRDAKGRTPLHAAAVAEDVAGLQLVLRQGADIDAVDHSGRSALMVAADYGQSGAVALLLhRA 909
Cdd:COG0666 166 LEIVKLLLEA---GADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL-EA 241
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 66392221 910 KADLSLLDVNKNTALHLACSKAHEMCAMLILKEIHNPILINA 951
Cdd:COG0666 242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
155-536 |
1.80e-29 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 125.95 E-value: 1.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 155 MVKLLLNKGANLSASDKKDRQPIHWAAYLGHLEVVKLLVSQGSDKSCKDKRGYTPLHAAAASGHVDVVKYLLRNGAEIDE 234
Cdd:PHA02876 160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINK 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 235 P-----NAFGNTALHVACYtgqeavaneLVNRGANVNQPNHRGYTPLHLAAVSTNGALCLELLVNNGADVNMQSKEGKSP 309
Cdd:PHA02876 240 NdlsllKAIRNEDLETSLL---------LYDAGFSVNSIDDCKNTPLHHASQAPSLSRLVPKLLERGADVNAKNIKGETP 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 310 LHMAAIHGRFTRS-QILIQNGGEIDCVDRYGNTPLHVAakyghelliSTLMTNGadtarqgihgmfplhlavlygssdcc 388
Cdd:PHA02876 311 LYLMAKNGYDTENiRTLIMLGADVNAADRLYITPLHQA---------STLDRNK-------------------------- 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 389 rkllssgqlySIVLSMskehvLSAGFDINTPDNFGRTCLHAAASGGNIECLNLLLSSGADMNKKDKFGRTPLHYA-AANG 467
Cdd:PHA02876 356 ----------DIVITL-----LELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTN 420
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66392221 468 RYQCVVVLVGAGAEVNERDRSGCTPLHYSAASTafCRTDrphasthqnqedgekesflCVEHLLDNGAD 536
Cdd:PHA02876 421 PYMSVKTLIDRGANVNSKNKDLSTPLHYACKKN--CKLD-------------------VIEMLLDNGAD 468
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
700-993 |
5.14e-29 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 118.13 E-value: 5.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 700 LLLERGACPDMKDRRGRTALHRGAVMGREDCLTALLSHNVSVLSRDFQGRSALHLAASCGHADILSNLLSAADHsqpqDP 779
Cdd:COG0666 6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGAD----IN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 780 LTDRHGYTPAHWAAYHGHEDCLEVLLELKP-CSIQEGNPFTPLHCALINGHSGSAELLLESsvcNSLVNIRDAKGRTPLH 858
Cdd:COG0666 82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGAdVNARDKDGETPLHLAAYNGNLEIVKLLLEA---GADVNAQDNDGNTPLH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 859 AAAVAEDVAGLQLVLRQGADIDAVDHSGRSALMVAADYGQSGAVALLLhRAKADLSLLDVNKNTALHLACSKAHEMCAML 938
Cdd:COG0666 159 LAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLL-EAGADVNAKDNDGKTALDLAAENGNLEIVKL 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 66392221 939 ILKEIHNpilINATNSMLQMPLHIAARNGLATVVQALLNRGATVLAVDEEGHTPA 993
Cdd:COG0666 238 LLEAGAD---LNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
4-313 |
2.28e-27 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 116.60 E-value: 2.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 4 LNISDQ---PPLVQAIFNRNADEVKLFLHKKDEVNALDQERRTPLHAAAWLGDVHIMDLLISAGANVNakdhvwLTPLhr 80
Cdd:PHA02874 28 INISVDettTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTS------ILPI-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 81 aaASRNERAVGLLLRKGADVTARDKYWQTPLHIAAANRATRCVETLLPHVSSLNMADRTGRAPLHHAAQSGYQEMVKLLL 160
Cdd:PHA02874 100 --PCIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 161 NKGANLSASDKKDRQPIHWAAYLGHLEVVKLLVSQGSDKSCKDKRGYTPLHAAaasghvdvvkyLLRNGAEIdepnafgn 240
Cdd:PHA02874 178 EKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA-----------IIHNRSAI-------- 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66392221 241 talhvacytgqeavanELVNRGANVNQPNHRGYTPLHLAAVSTNGALCLELLVNNGADVNMQSKEGKSPLHMA 313
Cdd:PHA02874 239 ----------------ELLINNASINDQDIDGSTPLHHAINPPCDIDIIDILLYHKADISIKDNKGENPIDTA 295
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
778-1010 |
2.60e-27 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 113.13 E-value: 2.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 778 DPLTDRHGYTPAHWAAYHGHEDCLEVLLELKPCSIQEGNPFTPLHCALINGHSGSAELLLESSVCNslVNIRDAKGRTPL 857
Cdd:COG0666 14 ALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGAD--INAKDDGGNTLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 858 HAAAVAEDVAGLQLVLRQGADIDAVDHSGRSALMVAADYGQSGAVALLLhRAKADLSLLDVNKNTALHLACSKAH-EMCA 936
Cdd:COG0666 92 HAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLL-EAGADVNAQDNDGNTPLHLAAANGNlEIVK 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66392221 937 MLilkeIHNPILINATNSMLQMPLHIAARNGLATVVQALLNRGATVLAVDEEGHTPALACASNKAVADCLALIL 1010
Cdd:COG0666 171 LL----LEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
23-313 |
8.62e-27 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 115.36 E-value: 8.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 23 EVKLFLHKKDEVNALDQERRTPLHAAAWLGDVHIMDLLISAGANVNAKDHVWLTPLHRAAASRNERAVGLLLRkgaDVTA 102
Cdd:PHA02878 19 YIEYIDHTENYSTSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIR---SINK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 103 RD-KYWQTPLHIAAANRATRCVETLLphvssLNMADRTGRAPLHHAAQSGYQ-----EMVKLLLNKGANLSASDK-KDRQ 175
Cdd:PHA02878 96 CSvFYTLVAIKDAFNNRNVEIFKIIL-----TNRYKNIQTIDLVYIDKKSKDdiieaEITKLLLSYGADINMKDRhKGNT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 176 PIHWAAYLGHLEVVKLLVSQGSDKSCKDKRGYTPLHAAAASGHVDVVKYLLRNGAEIDEPNAFGNTALHVAC-YTGQEAV 254
Cdd:PHA02878 171 ALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVgYCKDYDI 250
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 255 ANELVNRGANVN-QPNHRGYTPLHLAAVSTNGalcLELLVNNGADVNMQSKEGKSPLHMA 313
Cdd:PHA02878 251 LKLLLEHGVDVNaKSYILGLTALHSSIKSERK---LKLLLEYGADINSLNSYKLTPLSSA 307
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
157-463 |
3.97e-26 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 112.75 E-value: 3.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 157 KLLLNKGANLSASDKKDRQPIHWAAYLGHLEVVKLLVSQGSDKSCKDKRGYTPLHAAAASGHVDVVKYLLRNGAEidepn 236
Cdd:PHA02874 19 KIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVD----- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 237 afgNTALHVACYtgQEAVANELVNRGANVNQPNHRGYTPLHLAaVSTNGALCLELLVNNGADVNMQSKEGKSPLHMAAIH 316
Cdd:PHA02874 94 ---TSILPIPCI--EKDMIKTILDCGIDVNIKDAELKTFLHYA-IKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKH 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 317 GRFTRSQILIQNGGEIDCVDRYGNTPLHVAAKYGHELLISTLMTNGADTARQGIHGMFPLHLAVLYGSSdccrkllssgq 396
Cdd:PHA02874 168 NFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRS----------- 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66392221 397 lySIVLSMSKEhvlsagfDINTPDNFGRTCLHAAAS-GGNIECLNLLLSSGADMNKKDKFGRTPLHYA 463
Cdd:PHA02874 237 --AIELLINNA-------SINDQDIDGSTPLHHAINpPCDIDIIDILLYHKADISIKDNKGENPIDTA 295
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
761-1010 |
6.24e-26 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 109.27 E-value: 6.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 761 ADILSNLLSAADHSQPQDPLTDRHGYTPAHWAAYHGHEDCLEVLLELKPCSIQEGNP--FTPLHCALINGHSGSAELLLE 838
Cdd:COG0666 29 ALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDggNTLLHAAARNGDLEIVKLLLE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 839 SsvcNSLVNIRDAKGRTPLHAAAVAEDVAGLQLVLRQGADIDAVDHSGRSALMVAADYGQSGAVALLLHrAKADLSLLDV 918
Cdd:COG0666 109 A---GADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLE-AGADVNARDN 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 919 NKNTALHLACSKAH-EMCAMLILKEIHnpilINATNSMLQMPLHIAARNGLATVVQALLNRGATVLAVDEEGHTPALACA 997
Cdd:COG0666 185 DGETPLHLAAENGHlEIVKLLLEAGAD----VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAA 260
|
250
....*....|...
gi 66392221 998 SNKAVADCLALIL 1010
Cdd:COG0666 261 AAGAALIVKLLLL 273
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
258-557 |
1.25e-25 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 111.66 E-value: 1.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 258 LVNRGANVNQPNHRGYTPLHLAaVSTNGALCLE---LLVNNGADVNMQSKEGKSPLHMAAIHGRFTR-SQILIQNGGEID 333
Cdd:PHA03095 33 LLAAGADVNFRGEYGKTPLHLY-LHYSSEKVKDivrLLLEAGADVNAPERCGFTPLHLYLYNATTLDvIKLLIKAGADVN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 334 CVDRYGNTPLHVaakyghellistlmtngadtarqgihgmfplhlavlYGSSDCCRkllssgqlYSIVLSMskehvLSAG 413
Cdd:PHA03095 112 AKDKVGRTPLHV------------------------------------YLSGFNIN--------PKVIRLL-----LRKG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 414 FDINTPDNFGRTCLHA--AASGGNIECLNLLLSSGADMNKKDKFGRTPLHYAAAN--GRYQCVVVLVGAGAEVNERDRSG 489
Cdd:PHA03095 143 ADVNALDLYGMTPLAVllKSRNANVELLRLLIDAGADVYAVDDRFRSLLHHHLQSfkPRARIVRELIRAGCDPAATDMLG 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66392221 490 CTPLHYSAASTAFCRTDrphasthqnqedgekesflcVEHLLDNGADPCLCNTKGYSAVHYAAAHGNK 557
Cdd:PHA03095 223 NTPLHSMATGSSCKRSL--------------------VLPLLIAGISINARNRYGQTPLHYAAVFNNP 270
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
143-455 |
2.23e-24 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 107.44 E-value: 2.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 143 PLHHAAQSGYQEMVKLLLNKGANLSASDKKDRQPIHWAAYLGH-----LEVVKLLVSQGSDKSCKDKRGYTPLHAAAA-- 215
Cdd:PHA03100 38 PLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGITPLLYAISkk 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 216 SGHVDVVKYLLrngaeidepnafgntalhvacytgqeavanelvNRGANVNQPNHRGYTPLHLAAVSTNGAL-CLELLVN 294
Cdd:PHA03100 118 SNSYSIVEYLL---------------------------------DNGANVNIKNSDGENLLHLYLESNKIDLkILKLLID 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 295 NGADVNMQskegksplhmaaihgrfTRSQILIQNGGEIDCVDRYGNTPLHVAAKYGHELLISTLMTNGADtarqgihgmf 374
Cdd:PHA03100 165 KGVDINAK-----------------NRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGAN---------- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 375 plhlavlygssdccrkllssgqlysivlsmskehvlsagfdINTPDNFGRTCLHAAASGGNIECLNLLLSSGADMNKKDK 454
Cdd:PHA03100 218 -----------------------------------------PNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
|
.
gi 66392221 455 F 455
Cdd:PHA03100 257 T 257
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
186-466 |
2.56e-24 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 107.06 E-value: 2.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 186 LEVVKLLVSQGSDKSCKDKRGYTPLHAAAASGHVDVVKYLLRNGAEIDEPNAFGNTALHVAcyTGQEAVANE-------L 258
Cdd:PHA03100 15 VKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYL--SNIKYNLTDvkeivklL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 259 VNRGANVNQPNHRGYTPLHLAAVSTNGALCL-ELLVNNGADVNMQSKEGKSPLHMAA--IHGRFTRSQILIQNGGEIDCV 335
Cdd:PHA03100 93 LEYGANVNAPDNNGITPLLYAISKKSNSYSIvEYLLDNGANVNIKNSDGENLLHLYLesNKIDLKILKLLIDKGVDINAK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 336 DRYgntplhvaakyghELLISTlmtngadtarqgihgmfplhlavlygssdccrkllssgqlysivlsmskehvlsaGFD 415
Cdd:PHA03100 173 NRV-------------NYLLSY-------------------------------------------------------GVP 184
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 66392221 416 INTPDNFGRTCLHAAASGGNIECLNLLLSSGADMNKKDKFGRTPLHYAAAN 466
Cdd:PHA03100 185 INIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILN 235
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
12-332 |
9.51e-24 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 107.84 E-value: 9.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 12 LVQAIFNRNADEVKLFLHKKDEVNALDQERRTPLHaaawlgdvhimdllisaganvnakdhvwltplHRAAASRNERAVG 91
Cdd:PHA02876 244 LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLH--------------------------------HASQAPSLSRLVP 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 92 LLLRKGADVTARDKYWQTPLHIAAAN-RATRCVETLLPHVSSLNMADRTGRAPLHHAAQ-SGYQEMVKLLLNKGANLSAS 169
Cdd:PHA02876 292 KLLERGADVNAKNIKGETPLYLMAKNgYDTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNAR 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 170 DKKDRQPIHWaaylghlevvkllvsqgsdksckdkrgytplhaAAASGHVDVVKYLLRNGAEIDEPNAFGNTALHVA-CY 248
Cdd:PHA02876 372 DYCDKTPIHY---------------------------------AAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCG 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 249 TGQEAVANELVNRGANVNQPNHRGYTPLHLAAVSTNGALCLELLVNNGADVNMQSKEGKSPLHMAAihGRFTRSQILIQN 328
Cdd:PHA02876 419 TNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILLHY 496
|
....
gi 66392221 329 GGEI 332
Cdd:PHA02876 497 GAEL 500
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
290-619 |
1.26e-22 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 102.35 E-value: 1.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 290 ELLVNNGADVNMQSKEGKSPLHMAAIHGRFTRSQILIQNGGEIDCVDRYGNTPLHVAAKYGHELLISTLMTNGADTArqg 369
Cdd:PHA02874 19 KIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTS--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 370 ihgMFPlhlavlygssdccrkllssgqlysiVLSMSKEHV---LSAGFDINTPDNFGRTCLHAAASGGNIECLNLLLSSG 446
Cdd:PHA02874 96 ---ILP-------------------------IPCIEKDMIktiLDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 447 ADMNKKDKFGRTPLHYAAANGRYQCVVVLVGAGAEVNERDRSGCTPLHYSAastafcrtdrphasthqnqedgEKESFLC 526
Cdd:PHA02874 148 ADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAA----------------------EYGDYAC 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 527 VEHLLDNGADPCLCNTKGYSAVHYAAAHgNKQNLELLLEMcfNTLGDKESNGSiSPLHLAVEsghWEC----VTVLIESG 602
Cdd:PHA02874 206 IKLLIDHGNHIMNKCKNGFTPLHNAIIH-NRSAIELLINN--ASINDQDIDGS-TPLHHAIN---PPCdidiIDILLYHK 278
|
330
....*....|....*..
gi 66392221 603 VCVDVCDPVGRSVLYLA 619
Cdd:PHA02874 279 ADISIKDNKGENPIDTA 295
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
177-269 |
7.69e-22 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 90.95 E-value: 7.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 177 IHWAAYLGHLEVVKLLVSQGSDKSCKDKRGYTPLHAAAASGHVDVVKYLLRNgAEIDEPNaFGNTALHVACYTGQEAVAN 256
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 66392221 257 ELVNRGANVNQPN 269
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
144-236 |
1.03e-21 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 90.56 E-value: 1.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 144 LHHAAQSGYQEMVKLLLNKGANLSASDKKDRQPIHWAAYLGHLEVVKLLVSQGsDKSCKDKrGYTPLHAAAASGHVDVVK 223
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKDN-GRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 66392221 224 YLLRNGAEIDEPN 236
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
143-380 |
9.37e-21 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 96.87 E-value: 9.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 143 PLHHAAQSGYQEMVKLLLNKGANLSASDKKDRQPIHWAAYLGHLEVVKLLVSQGSdkscKDKRGYT--PLHAAAASGHVD 220
Cdd:PHA02878 40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSIN----KCSVFYTlvAIKDAFNNRNVE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 221 VVKYLLRNG---------AEIDEPNAFGNTalhvacytgQEAVANELVNRGANVNQPN-HRGYTPLHLAAVSTNGALcLE 290
Cdd:PHA02878 116 IFKIILTNRykniqtidlVYIDKKSKDDII---------EAEITKLLLSYGADINMKDrHKGNTALHYATENKDQRL-TE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 291 LLVNNGADVNMQSKEGKSPLHMAAIHGRFTRSQILIQNGGEIDCVDRYGNTPLHVAAKYGHEL-LISTLMTNGAD-TARQ 368
Cdd:PHA02878 186 LLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDYdILKLLLEHGVDvNAKS 265
|
250
....*....|..
gi 66392221 369 GIHGMFPLHLAV 380
Cdd:PHA02878 266 YILGLTALHSSI 277
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
24-227 |
3.31e-19 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 92.01 E-value: 3.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 24 VKLFLHKKDEVNALDQERRTPLHAaaWLG----DVHIMDLLISAGANVNAKDHVWLTPLHRAAASRN--ERAVGLLLRKG 97
Cdd:PHA03095 100 IKLLIKAGADVNAKDKVGRTPLHV--YLSgfniNPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanVELLRLLIDAG 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 98 ADVTARDKYWQTPLHIAAANRATR--CVETLLPHVSSLNMADRTGRAPLHHAAQSGYQEMVKL--LLNKGANLSASDKKD 173
Cdd:PHA03095 178 ADVYAVDDRFRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYG 257
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 66392221 174 RQPIHWAAYLGHLEVVKLLVSQGSDKSCKDKRGYTPLHAAAASGHVDVVKYLLR 227
Cdd:PHA03095 258 QTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALA 311
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
24-194 |
3.82e-18 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 88.78 E-value: 3.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 24 VKLFLHKKDEVNALDQER-RTPLHAAAWLGDVHIMDLLISAGANVNAKDHVWLTPLHRAAASRNERAVGLLLRKGADVTA 102
Cdd:PHA02878 150 TKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 103 RDKYWQTPLHIAAAN-RATRCVETLLPHVSSLNMADRT-GRAPLHHAAQSgyQEMVKLLLNKGANLSASDKKDRQPIHWA 180
Cdd:PHA02878 230 RDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYIlGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSA 307
|
170
....*....|....*.
gi 66392221 181 A--YLGhLEVVKLLVS 194
Cdd:PHA02878 308 VkqYLC-INIGRILIS 322
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
78-170 |
3.87e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 80.16 E-value: 3.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 78 LHRAAASRNERAVGLLLRKGADVTARDKYWQTPLHIAAANRATRCVETLLPHVsSLNMADRtGRAPLHHAAQSGYQEMVK 157
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKDN-GRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 66392221 158 LLLNKGANLSASD 170
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
111-203 |
6.36e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 79.77 E-value: 6.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 111 LHIAAANRATRCVETLLPHVSSLNMADRTGRAPLHHAAQSGYQEMVKLLLNKGAnlSASDKKDRQPIHWAAYLGHLEVVK 190
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 66392221 191 LLVSQGSDKSCKD 203
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
650-745 |
8.85e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 79.39 E-value: 8.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 650 LHVAAANGHSECLRMLLcsEGGADlVNVTDAEGQTPLMLAVLGGHTDCVHLLLERgACPDMKDRrGRTALHRGAVMGRED 729
Cdd:pfam12796 1 LHLAAKNGNLELVKLLL--ENGAD-ANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLE 75
|
90
....*....|....*.
gi 66392221 730 CLTALLSHNVSVLSRD 745
Cdd:pfam12796 76 IVKLLLEKGADINVKD 91
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
109-301 |
1.36e-17 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 86.58 E-value: 1.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 109 TPLHIAAANRATRCVETLLPHVSSLNMADRTGRAPLHHAAQSGYQEMVKLLLNkgANLSASD---KKDRQPIHWAAYLGH 185
Cdd:PHA02875 37 SPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLD--LGKFADDvfyKDGMTPLHLATILKK 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 186 LEVVKLLVSQGSDKSCKDKRGYTPLHAAAASGHVDVVKYLLRNGAEIDEPNAFGNTALHVACYTGQEAVANELVNRGANV 265
Cdd:PHA02875 115 LDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANI 194
|
170 180 190
....*....|....*....|....*....|....*.
gi 66392221 266 NQPNHRGYTPLHLAAVSTNGALCLELLVNNGADVNM 301
Cdd:PHA02875 195 DYFGKNGCVAALCYAIENNKIDIVRLFIKRGADCNI 230
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
376-486 |
2.90e-17 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 77.85 E-value: 2.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 376 LHLAVLYGSSDCCRKLLSSGqlysivlsmskehvlsagFDINTPDNFGRTCLHAAASGGNIECLNLLLSSgADMNKKDKf 455
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENG------------------ADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN- 60
|
90 100 110
....*....|....*....|....*....|.
gi 66392221 456 GRTPLHYAAANGRYQCVVVLVGAGAEVNERD 486
Cdd:pfam12796 61 GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
233-463 |
3.32e-17 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 86.09 E-value: 3.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 233 DEPNAFGNTALHVACYTGQEAVANELVNRGANVNQPNHRGYTPLHLAAVSTN---------------------------- 284
Cdd:PHA02878 31 TSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNklgmkemirsinkcsvfytlvaikdafn 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 285 -----------------------------------GALCLELLVNNGADVNMQSKE-GKSPLHMAAIHGRFTRSQILIQN 328
Cdd:PHA02878 111 nrnveifkiiltnrykniqtidlvyidkkskddiiEAEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSY 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 329 GGEIDCVDRYGNTPLHVAAKYGHELLISTLMTNGADTARQGIHGMFPLHLAVlygssdccrkllssGQLYSI-VLSMSKE 407
Cdd:PHA02878 191 GANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISV--------------GYCKDYdILKLLLE 256
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 66392221 408 HvlsaGFDINTPDNF-GRTCLHAAASGGNIecLNLLLSSGADMNKKDKFGRTPLHYA 463
Cdd:PHA02878 257 H----GVDVNAKSYIlGLTALHSSIKSERK--LKLLLEYGADINSLNSYKLTPLSSA 307
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
51-236 |
7.90e-17 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 85.69 E-value: 7.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 51 LGDVHIMDLLISAGANvnAKDHVWLTPLHRAAASRNERAVGLLLRKGADVTARDKYWQTPLHIAAANRATRCVETLLPHV 130
Cdd:PLN03192 504 LHDLNVGDLLGDNGGE--HDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHA 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 131 SSLNMADRTGRAPLHHAAQSGYQEMVKLLLNKGanlSASDKKDRQPIH-WAAYLGHLEVVKLLVSQGSDKSCKDKRGYTP 209
Cdd:PLN03192 582 CNVHIRDANGNTALWNAISAKHHKIFRILYHFA---SISDPHAAGDLLcTAAKRNDLTAMKELLKQGLNVDSEDHQGATA 658
|
170 180
....*....|....*....|....*..
gi 66392221 210 LHAAAASGHVDVVKYLLRNGAEIDEPN 236
Cdd:PLN03192 659 LQVAMAEDHVDMVRLLIMNGADVDKAN 685
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
11-198 |
1.25e-16 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 83.50 E-value: 1.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 11 PLVQAIFNRNADEVKLFLHKKDEVNALDQERRTPLHAAAWLGDVHIMDLLISAGANVNakDHVW---LTPLHRAAASRNE 87
Cdd:PHA02875 38 PIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAD--DVFYkdgMTPLHLATILKKL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 88 RAVGLLLRKGA--DVTARDKYwqTPLHIAAANRATRCVETLLPHVSSLNMADRTGRAPLHHAAQSGYQEMVKLLLNKGAN 165
Cdd:PHA02875 116 DIMKLLIARGAdpDIPNTDKF--SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGAN 193
|
170 180 190
....*....|....*....|....*....|....
gi 66392221 166 LS-ASDKKDRQPIHWAAYLGHLEVVKLLVSQGSD 198
Cdd:PHA02875 194 IDyFGKNGCVAALCYAIENNKIDIVRLFIKRGAD 227
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
516-907 |
2.95e-16 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 83.57 E-value: 2.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 516 QEDGEKESFLCVEHLLDNGADPCLCNTKGYSAVHYAAAHGNKQNLELLL----EMCFNTLGDkesngsISPLHLAVESGH 591
Cdd:PHA02876 150 KERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLsygaDVNIIALDD------LSVLECAVDSKN 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 592 WECVTVLIESGVCVDVCDpvgrsVLYLASQRGHSRCVELLLSQSASCLLAEHRSKWGPLHVAA-ANGHSECLRMLLcsEG 670
Cdd:PHA02876 224 IDTIKAIIDNRSNINKND-----LSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASqAPSLSRLVPKLL--ER 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 671 GADlVNVTDAEGQTPLMLAVLGGH-TDCVHLLLERGACPDMKDRRGRTALHRGAVMGR-EDCLTALLSHNVSVLSRDFQG 748
Cdd:PHA02876 297 GAD-VNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDRnKDIVITLLELGANVNARDYCD 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 749 RSALHLAASCGHADILSNLLsaaDHSQPQDPLTDRHGyTPAHWAAYHghedclevllelkpcsiqeGNPFTPLHCALING 828
Cdd:PHA02876 376 KTPIHYAAVRNNVVIINTLL---DYGADIEALSQKIG-TALHFALCG-------------------TNPYMSVKTLIDRG 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 829 HSgsaelllessvcnslVNIRDAKGRTPLHAAA---VAEDVagLQLVLRQGADIDAVDHSGRSALMVAADYgqSGAVALL 905
Cdd:PHA02876 433 AN---------------VNSKNKDLSTPLHYACkknCKLDV--IEMLLDNGADVNAINIQNQYPLLIALEY--HGIVNIL 493
|
..
gi 66392221 906 LH 907
Cdd:PHA02876 494 LH 495
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
425-706 |
1.76e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 80.09 E-value: 1.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 425 TCLHAAASGGNIECLNLLLSSGADMNKKDKFGRTPLHYAAaNGRY------QCVVVLVGAGAEVNERDRSGCTPLHYsAA 498
Cdd:PHA03100 37 LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLS-NIKYnltdvkEIVKLLLEYGANVNAPDNNGITPLLY-AI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 499 STafcrtdrphasthqnqedgEKESFLCVEHLLDNGADPCLCNTKGYSAVHYAaahgnkqnlellLEMCFNTLgdkesng 578
Cdd:PHA03100 115 SK-------------------KSNSYSIVEYLLDNGANVNIKNSDGENLLHLY------------LESNKIDL------- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 579 sisplhlavesghwECVTVLIESGVCVDVCDPvgrsvlylasqrghsrcVELLLSQSASCLLAEHRSkWGPLHVAAANGH 658
Cdd:PHA03100 157 --------------KILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIKDVYG-FTPLHYAVYNNN 204
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 66392221 659 SECLRMLLcsEGGADlVNVTDAEGQTPLMLAVLGGHTDCVHLLLERGA 706
Cdd:PHA03100 205 PEFVKYLL--DLGAN-PNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
141-365 |
2.40e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 79.65 E-value: 2.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 141 RAPLHHAAQSGYQEMVKLLLNKGANLSASDKKDRQPIHWAAYLGHLEVVKLLVSQGSDKSCKDKRGYTPLHAAAASGHVD 220
Cdd:PHA02875 3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 221 VVKYLLRNGAEIDEpnAF---GNTALHVACYTGQEAVANELVNRGANVNQPNHRGYTPLHLAAVSTNGALcLELLVNNGA 297
Cdd:PHA02875 83 AVEELLDLGKFADD--VFykdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKG-IELLIDHKA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66392221 298 DVNMQSKEGKSPLHMAAIHGRFTRSQILIQNGGEIDCVDRYGNTPLHVAAKYGHEL-LISTLMTNGADT 365
Cdd:PHA02875 160 CLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIdIVRLFIKRGADC 228
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
427-537 |
2.44e-15 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 72.46 E-value: 2.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 427 LHAAASGGNIECLNLLLSSGADMNKKDKFGRTPLHYAAANGRYQCVVVLVgAGAEVNERDrSGCTPLHYSAAStafcrtd 506
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARS------- 71
|
90 100 110
....*....|....*....|....*....|.
gi 66392221 507 rphasthqNQEDgekesflCVEHLLDNGADP 537
Cdd:pfam12796 72 --------GHLE-------IVKLLLEKGADI 87
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
583-679 |
2.69e-15 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 72.07 E-value: 2.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 583 LHLAVESGHWECVTVLIESGVCVDVCDPVGRSVLYLASQRGHSRCVELLLSQSASCLLAEHRSkwgPLHVAAANGHSECL 662
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRT---ALHYAARSGHLEIV 77
|
90
....*....|....*..
gi 66392221 663 RMLLCSegGADlVNVTD 679
Cdd:pfam12796 78 KLLLEK--GAD-INVKD 91
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
246-493 |
3.05e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 79.26 E-value: 3.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 246 ACYTGQEAVANELVNRGANVNQPNHRGYTPLHLAaVSTNGALCLELLVNNGADVNMQSKEGKSPLHMAAIHGRFTRSQIL 325
Cdd:PHA02875 9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLA-MKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 326 IQNGGEI-DCVDRYGNTPLHVAAKYGHELLISTLMTNGADTarqgihgmfplhlavlygssdccrkllssgqlysivlsm 404
Cdd:PHA02875 88 LDLGKFAdDVFYKDGMTPLHLATILKKLDIMKLLIARGADP--------------------------------------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 405 skehvlsagfDINTPDNFgrTCLHAAASGGNIECLNLLLSSGADMNKKDKFGRTPLHYAAANGRYQCVVVLVGAGAEVNE 484
Cdd:PHA02875 129 ----------DIPNTDKF--SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDY 196
|
....*....
gi 66392221 485 RDRSGCTPL 493
Cdd:PHA02875 197 FGKNGCVAA 205
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
140-335 |
3.13e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 79.26 E-value: 3.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 140 GRAPLHHAAQSGYQEMVKLLLNKGANLSASDKKDRQPIHWAAYLGHLEVVKLLVSQGsdKSCKD---KRGYTPLHAAAAS 216
Cdd:PHA02875 35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLG--KFADDvfyKDGMTPLHLATIL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 217 GHVDVVKYLLRNGAEIDEPNAFGNTALHVACYTGQEAVANELVNRGANVNQPNHRGYTPLHLAAVSTNGALClELLVNNG 296
Cdd:PHA02875 113 KKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAIC-KMLLDSG 191
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 66392221 297 ADVNMQSKEGKSPLHMAAI-HGRFTRSQILIQNGGEIDCV 335
Cdd:PHA02875 192 ANIDYFGKNGCVAALCYAIeNNKIDIVRLFIKRGADCNIM 231
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
662-1010 |
3.65e-15 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 79.30 E-value: 3.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 662 LRMLLcsEGGADlVNVTDAEGQTPLMLAVLGGHTDC---VHLLLERGACPDMKDRRGRTALHRGAVMG-REDCLTALLSH 737
Cdd:PHA03095 30 VRRLL--AAGAD-VNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLHLYLYNAtTLDVIKLLIKA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 738 NVSVLSRDFQGRSALH--LAASCGHADILSNLLSA-ADhsqPQDplTDRHGYTPAHwaAYHGHEDC-LEVL--LELKPCS 811
Cdd:PHA03095 107 GADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKgAD---VNA--LDLYGMTPLA--VLLKSRNAnVELLrlLIDAGAD 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 812 I--QEGNPFTPLHCALINGHSgSAELLLESSVCNSLVNIRDAKGRTPLHAAAVAEDVAGLQLV--LRQGADIDAVDHSGR 887
Cdd:PHA03095 180 VyaVDDRFRSLLHHHLQSFKP-RARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVLplLIAGISINARNRYGQ 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 888 SALMVAADYGQSGAVALLLhRAKADLSLLDVNKNTALHLACSKAHEMCAMLILKEIHNPILINATnsmlqmpLHIAARNG 967
Cdd:PHA03095 259 TPLHYAAVFNNPRACRRLI-ALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAAT-------LNTASVAG 330
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 66392221 968 LATVVQALLNRGATVLAVDEEGHTPALACASNKA-VADCLALIL 1010
Cdd:PHA03095 331 GDIPSDATRLCVAKVVLRGAFSLLPEPIRAYHADfIRECEAEIA 374
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
616-712 |
4.50e-15 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 71.69 E-value: 4.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 616 LYLASQRGHSRCVELLLSQSASCLLAEHRsKWGPLHVAAANGHSECLRmLLCSEGGADLVNvtdaEGQTPLMLAVLGGHT 695
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKN-GRTALHLAAKNGHLEIVK-LLLEHADVNLKD----NGRTALHYAARSGHL 74
|
90
....*....|....*..
gi 66392221 696 DCVHLLLERGACPDMKD 712
Cdd:pfam12796 75 EIVKLLLEKGADINVKD 91
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
628-896 |
5.81e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 78.47 E-value: 5.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 628 VELLLSQSASCLLAEHRSKWGPLHVAAANGHSECLRMLLCSegGADlVNVTDAEGQTPLMLAVLGGHTDCVHLLLERGA- 706
Cdd:PHA02874 17 IEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKH--GAD-INHINTKIPHPLLTAIKIGAHDIIKLLIDNGVd 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 707 -----CPDM-----------------KDRRGRTALHRGAVMGREDCLTALLSHNVSVLSRDFQGRSALHLAASCGHADIL 764
Cdd:PHA02874 94 tsilpIPCIekdmiktildcgidvniKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDII 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 765 SNLLSAADHSQpqdpLTDRHGYTPAHWAAYHGHEDCLEVLLE-LKPCSIQEGNPFTPLHCALINGHSgSAELLLEssvcN 843
Cdd:PHA02874 174 KLLLEKGAYAN----VKDNNGESPLHNAAEYGDYACIKLLIDhGNHIMNKCKNGFTPLHNAIIHNRS-AIELLIN----N 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 66392221 844 SLVNIRDAKGRTPLHAA---AVAEDVagLQLVLRQGADIDAVDHSGRSALMVAADY 896
Cdd:PHA02874 245 ASINDQDIDGSTPLHHAinpPCDIDI--IDILLYHKADISIKDNKGENPIDTAFKY 298
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
201-445 |
7.41e-15 |
|
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: 78.90 E-value: 7.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 201 CKDKRGY-TPLHAAAASGHVDVVKYLLR-NGAEIDEPNAFGNTALHVACYTGQEAVANELVNRGAN-VNQPN----HRGY 273
Cdd:cd22192 11 LQQKRISeSPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEPMtsdlYQGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 274 TPLHLAAVSTNGALcLELLVNNGADVNMQSKEGKSplhmaaihgrFTRSQiliqnggeiDCVDRYGNTPLHVAAKYGHEL 353
Cdd:cd22192 91 TALHIAVVNQNLNL-VRELIARGADVVSPRATGTF----------FRPGP---------KNLIYYGEHPLSFAACVGNEE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 354 LISTLMTNGADTARQGIHGMFPLHLAVLYGSSDccrkllSSGQLYSIVLSMSKE---HVLSagfdiNTPDNFGRTCLHAA 430
Cdd:cd22192 151 IVRLLIEHGADIRAQDSLGNTVLHILVLQPNKT------FACQMYDLILSYDKEddlQPLD-----LVPNNQGLTPFKLA 219
|
250
....*....|....*
gi 66392221 431 ASGGNIECLNLLLSS 445
Cdd:cd22192 220 AKEGNIVMFQHLVQK 234
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
436-796 |
7.65e-15 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 78.53 E-value: 7.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 436 IECLNLLLSSGADMNKKDKFGRTPLHYAAANGRYQC---VVVLVGAGAEVNERDRSGCTPLHYsaastafcrtdrphast 512
Cdd:PHA03095 27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLHL----------------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 513 hqnqedgekesflcvehlldngadpclcntkgysavhYaaahgnkqnlellleMCFNTLgdkesngsisplhlavesghW 592
Cdd:PHA03095 90 -------------------------------------Y---------------LYNATT--------------------L 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 593 ECVTVLIESGVCVDVCDPVGRSVL--YLASQRGHSRCVELLLsqsascllaehrskwgplhvaaanghseclrmllcsEG 670
Cdd:PHA03095 98 DVIKLLIKAGADVNAKDKVGRTPLhvYLSGFNINPKVIRLLL------------------------------------RK 141
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 671 GADlVNVTDAEGQTPlmLAVLGGHTDC----VHLLLERGACPDMKDRRGRTALHRGA--VMGREDCLTALLSHNVSVLSR 744
Cdd:PHA03095 142 GAD-VNALDLYGMTP--LAVLLKSRNAnvelLRLLIDAGADVYAVDDRFRSLLHHHLqsFKPRARIVRELIRAGCDPAAT 218
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 66392221 745 DFQGRSALHLAA---SCGHADILSNLLSAADhsqpqDPLTDRHGYTPAHWAAYHG 796
Cdd:PHA03095 219 DMLGNTPLHSMAtgsSCKRSLVLPLLIAGIS-----INARNRYGQTPLHYAAVFN 268
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
343-453 |
1.03e-14 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 70.53 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 343 LHVAAKYGHELLISTLMTNGADTARQGIHGMFPLHLAVLYGSSDCCRKLLSSgqlysivlsmskehvlsagFDINTPDNf 422
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-------------------ADVNLKDN- 60
|
90 100 110
....*....|....*....|....*....|.
gi 66392221 423 GRTCLHAAASGGNIECLNLLLSSGADMNKKD 453
Cdd:pfam12796 61 GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
12-104 |
3.19e-14 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 68.99 E-value: 3.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 12 LVQAIFNRNADEVKLFLHKKDEVNALDQERRTPLHAAAWLGDVHIMDLLISaGANVNAKDHVWlTPLHRAAASRNERAVG 91
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNGR-TALHYAARSGHLEIVK 78
|
90
....*....|...
gi 66392221 92 LLLRKGADVTARD 104
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
686-769 |
5.89e-14 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 68.22 E-value: 5.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 686 LMLAVLGGHTDCVHLLLERGACPDMKDRRGRTALHRGAVMGREDCLTALLSHNvsVLSRDFQGRSALHLAASCGHADILS 765
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA--DVNLKDNGRTALHYAARSGHLEIVK 78
|
....
gi 66392221 766 NLLS 769
Cdd:pfam12796 79 LLLE 82
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
207-460 |
1.10e-13 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 74.70 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 207 YTPLHAAAASGHVDVvkylLRNGAEIDEPNafGNT-ALHVACYTG--QEAVANELVNRGANVNQPNHRGYTPLHLAAVST 283
Cdd:PHA02946 10 YLSLYAKYNSKNLDV----FRNMLQAIEPS--GNYhILHAYCGIKglDERFVEELLHRGYSPNETDDDGNYPLHIASKIN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 284 NGALcLELLVNNGADVNMQSKEGKSPLHMAAIHGR--FTRSQILIQNGGEI-DCVDRYGNTPLhVAAKYGHELLISTLMT 360
Cdd:PHA02946 84 NNRI-VAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAKInNSVDEEGCGPL-LACTDPSERVFKKIMS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 361 NGadtarqgihgmFPLHLAVLYGSSDCCRKLLSSGQLYSIVLSMSKehvlsAGFDINTPDNFGRTCLHAAASG--GNIEC 438
Cdd:PHA02946 162 IG-----------FEARIVDKFGKNHIHRHLMSDNPKASTISWMMK-----LGISPSKPDHDGNTPLHIVCSKtvKNVDI 225
|
250 260
....*....|....*....|..
gi 66392221 439 LNLLLSSgADMNKKDKFGRTPL 460
Cdd:PHA02946 226 INLLLPS-TDVNKQNKFGDSPL 246
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
529-736 |
1.26e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 74.26 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 529 HLLDNGADPCLCNTKGYSAVHYAAAHGNKQNLELLleMCFNTLGDKESNGSISPLHLAVESGHWECVTVLIESGVCV-DV 607
Cdd:PHA02875 20 RLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLL--MKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAdDV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 608 CDPVGRSVLYLASQRGHSRCVELLLSQSASCLLAeHRSKWGPLHVAAANGHSECLRMLLCSEGgadLVNVTDAEGQTPLM 687
Cdd:PHA02875 98 FYKDGMTPLHLATILKKLDIMKLLIARGADPDIP-NTDKFSPLHLAVMMGDIKGIELLIDHKA---CLDIEDCCGCTPLI 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 66392221 688 LAVLGGHTDCVHLLLERGACPDMKDRRGRTALHRGAVM-GREDCLTALLS 736
Cdd:PHA02875 174 IAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIEnNKIDIVRLFIK 223
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
64-284 |
1.38e-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: 75.05 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 64 GANVNAKDHVWLTPLHRAAASRNERAVG-LLLRKGADVTARDKYWQTPLHIAAANRATRCVETLLPHVSSL-NMADRT-- 139
Cdd:cd22192 7 ELHLLQQKRISESPLLLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELvNEPMTSdl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 140 --GRAPLHHAAQSGYQEMVKLLLNKGANLSasdkKDRqpihwaaylghleVVKLLVSQGSDKSCKdkRGYTPLHAAAASG 217
Cdd:cd22192 87 yqGETALHIAVVNQNLNLVRELIARGADVV----SPR-------------ATGTFFRPGPKNLIY--YGEHPLSFAACVG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66392221 218 HVDVVKYLLRNGAEIDEPNAFGNTALHVACYTGQEAVANE----LVNRGANVNQ------PNHRGYTPLHLAAVSTN 284
Cdd:cd22192 148 NEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFACQmydlILSYDKEDDLqpldlvPNNQGLTPFKLAAKEGN 224
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
10-139 |
1.46e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 73.93 E-value: 1.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 10 PPLVQAIFNR--NADEVKLFLHKKDEVNALDQERRTPLHAAAW--LGDVHIMDLLISAGANVNAKDHVWL---------- 75
Cdd:PHA03100 108 TPLLYAISKKsnSYSIVEYLLDNGANVNIKNSDGENLLHLYLEsnKIDLKILKLLIDKGVDINAKNRVNYllsygvpini 187
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 76 ------TPLHRAAASRNERAVGLLLRKGADVTARDKYWQTPLHIAAANRATRCVETLLPHVSSLNMADRT 139
Cdd:PHA03100 188 kdvygfTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
11-169 |
2.11e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 74.71 E-value: 2.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 11 PLVQA-IFNRNADEVKLFLHKKDEVNALDQERRTPLHAAAWLGDVHIMDLLISAGANVNAKDHVWLTPLHRAAASRNE-R 88
Cdd:PHA02876 344 PLHQAsTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPyM 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 89 AVGLLLRKGADVTARDKYWQTPLHIAAANRAT-RCVETLLPHVSSLNMADRTGRAPLHHAAqsGYQEMVKLLLNKGANLS 167
Cdd:PHA02876 424 SVKTLIDRGANVNSKNKDLSTPLHYACKKNCKlDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILLHYGAELR 501
|
..
gi 66392221 168 AS 169
Cdd:PHA02876 502 DS 503
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
407-714 |
2.30e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 74.33 E-value: 2.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 407 EHVLSAGFDINTPDNFGRTCLHAAASGGNIECLNLLLSSGADMNKKDKFGRTPLHYAA---------------------- 464
Cdd:PHA02876 162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVdsknidtikaiidnrsninknd 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 465 -------ANGRYQCVVVLVGAGAEVNERDRSGCTPLHYSAASTAFCRTdrphasthqnqedgekesflcVEHLLDNGADP 537
Cdd:PHA02876 242 lsllkaiRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRL---------------------VPKLLERGADV 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 538 CLCNTKGYSAVHYAAAHG-NKQNLELLLEMCFNTlgDKESNGSISPLHLAVESGHW-ECVTVLIESGVCVDVCDPVGRSV 615
Cdd:PHA02876 301 NAKNIKGETPLYLMAKNGyDTENIRTLIMLGADV--NAADRLYITPLHQASTLDRNkDIVITLLELGANVNARDYCDKTP 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 616 LYLASQRGHSRCVELL---------LSQSASCLL------------------------AEHRSKWGPLHVAAANG-HSEC 661
Cdd:PHA02876 379 IHYAAVRNNVVIINTLldygadieaLSQKIGTALhfalcgtnpymsvktlidrganvnSKNKDLSTPLHYACKKNcKLDV 458
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 66392221 662 LRMLLcsEGGADlVNVTDAEGQTPLMLAVlgGHTDCVHLLLERGAcpDMKDRR 714
Cdd:PHA02876 459 IEMLL--DNGAD-VNAINIQNQYPLLIAL--EYHGIVNILLHYGA--ELRDSR 504
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
310-395 |
4.34e-13 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 65.91 E-value: 4.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 310 LHMAAIHGRFTRSQILIQNGGEIDCVDRYGNTPLHVAAKYGH----ELLISTLMTNGADtarqgiHGMFPLHLAVLYGSS 385
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHleivKLLLEHADVNLKD------NGRTALHYAARSGHL 74
|
90
....*....|
gi 66392221 386 DCCRKLLSSG 395
Cdd:pfam12796 75 EIVKLLLEKG 84
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
276-364 |
5.76e-13 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 65.52 E-value: 5.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 276 LHLAAVStNGALCLELLVNNGADVNMQSKEGKSPLHMAAIHGRFTRSQILIQNGgEIDCVDrYGNTPLHVAAKYGHELLI 355
Cdd:pfam12796 1 LHLAAKN-GNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKD-NGRTALHYAARSGHLEIV 77
|
....*....
gi 66392221 356 STLMTNGAD 364
Cdd:pfam12796 78 KLLLEKGAD 86
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
8-266 |
7.13e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 71.95 E-value: 7.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 8 DQPPLVQAIFNRNADEVKLFLHKKDEVNALDQERRTPLHAAAWLGDVHIMDLLISAGANVNAKDHVWLTPLHRAAASRNE 87
Cdd:PHA02875 2 DQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 88 RAVGLLLRKGA---DVTARDkywqtplhiaaanratrcvetllphvsslnmadrtGRAPLHHAAQSGYQEMVKLLLNKGA 164
Cdd:PHA02875 82 KAVEELLDLGKfadDVFYKD-----------------------------------GMTPLHLATILKKLDIMKLLIARGA 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 165 NLSASDKKDRQPIHWAAYLGHLEVVKLLVSQGSDKSCKDKRGYTPLHAAAASGHVDVVKYLLRNGAEIDEPNAFGNTALh 244
Cdd:PHA02875 127 DPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAA- 205
|
250 260
....*....|....*....|....*
gi 66392221 245 vACYTGQEA---VANELVNRGANVN 266
Cdd:PHA02875 206 -LCYAIENNkidIVRLFIKRGADCN 229
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
3-118 |
7.75e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 72.22 E-value: 7.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 3 VLNISDQPPLVQAIFNRNADEVKLFLHKKDEVNALDQERRTPLH-AAAWLGDVHIMDLLISAGANVNAKDHVW-LTPLHr 80
Cdd:PHA02878 196 IPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHiSVGYCKDYDILKLLLEHGVDVNAKSYILgLTALH- 274
|
90 100 110
....*....|....*....|....*....|....*...
gi 66392221 81 aAASRNERAVGLLLRKGADVTARDKYWQTPLHIAAANR 118
Cdd:PHA02878 275 -SSIKSERKLKLLLEYGADINSLNSYKLTPLSSAVKQY 311
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
45-137 |
9.28e-13 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 65.14 E-value: 9.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 45 LHAAAWLGDVHIMDLLISAGANVNAKDHVWLTPLHRAAASRNERAVGLLLRKgADVTARDKYWqTPLHIAAANRATRCVE 124
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGR-TALHYAARSGHLEIVK 78
|
90
....*....|...
gi 66392221 125 TLLPHVSSLNMAD 137
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
424-719 |
1.16e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 71.53 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 424 RTCLHAaasgGNIECL-NLLLSSGADMNKKDKFGRTPLHYAAANGRYQCVVVLVGAGAEVNERDRSGCTPLhysaaSTAF 502
Cdd:PHA02874 6 RMCIYS----GDIEAIeKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPL-----LTAI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 503 crTDRPHASTHQNQEDGEKESFL---CVEH-----LLDNGADPCLCNTKGYSAVHYAAAHGNKQNLELLLEMCFNtLGDK 574
Cdd:PHA02874 77 --KIGAHDIIKLLIDNGVDTSILpipCIEKdmiktILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGAD-VNIE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 575 ESNGSIsPLHLAVESGHWECVTVLIESGVCVDVCDPVGRSVLYLASQRGHSRCVELLLSQSaSCLLAEHRSKWGPLHVAA 654
Cdd:PHA02874 154 DDNGCY-PIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHG-NHIMNKCKNGFTPLHNAI 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66392221 655 ANGHSeCLRMLLCSEGgadlVNVTDAEGQTPLMLAV-LGGHTDCVHLLLERGACPDMKDRRGRTAL 719
Cdd:PHA02874 232 IHNRS-AIELLINNAS----INDQDIDGSTPLHHAInPPCDIDIIDILLYHKADISIKDNKGENPI 292
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
121-312 |
1.29e-12 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 71.24 E-value: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 121 RCVETLLPHVSSLNMADRTGRAPLHHAAQSGYQEMVKLLLNKGANLSASDKKDRQPIHWAAYLGH--LEVVKLLVSQGSD 198
Cdd:PHA02946 53 RFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAK 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 199 -KSCKDKRGYTPLHAAAASGHvDVVKYLLRNGAEIDEPNAFGNTAL--HVACYTGQEAVANELVNRGANVNQPNHRGYTP 275
Cdd:PHA02946 133 iNNSVDEEGCGPLLACTDPSE-RVFKKIMSIGFEARIVDKFGKNHIhrHLMSDNPKASTISWMMKLGISPSKPDHDGNTP 211
|
170 180 190
....*....|....*....|....*....|....*..
gi 66392221 276 LHLAAVSTNGALCLELLVNNGADVNMQSKEGKSPLHM 312
Cdd:PHA02946 212 LHIVCSKTVKNVDIINLLLPSTDVNKQNKFGDSPLTL 248
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
594-980 |
2.24e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 71.25 E-value: 2.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 594 CVTVLIESGVCVDVC-DPVGRSVLYLAS-----QRGHSRCVELLLSQSASCLLAEHRSKwGPLHVAAANGHSECLRMLLC 667
Cdd:PHA02876 121 CIHILKEAISGNDIHyDKINESIEYMKLikeriQQDELLIAEMLLEGGADVNAKDIYCI-TPIHYAAERGNAKMVNLLLS 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 668 SegGADlVNVTDAEGQTPLMLAVLGGHTDCVHLLLergacpDMKDRRGRTALHRGAVMGREDCLTALLSHNV--SVLSRD 745
Cdd:PHA02876 200 Y--GAD-VNIIALDDLSVLECAVDSKNIDTIKAII------DNRSNINKNDLSLLKAIRNEDLETSLLLYDAgfSVNSID 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 746 FQGRSALHLAAscgHADILSNLLSAADHSQPQDPLTDRHGYTPAHWAAYHGH--EDCLEVLLELKPCSIQEGNPFTPLHC 823
Cdd:PHA02876 271 DCKNTPLHHAS---QAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdtENIRTLIMLGADVNAADRLYITPLHQ 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 824 A-LINGHSGSAELLLEssvCNSLVNIRDAKGRTPLHAAAVAEDVAGLQLVLRQGADIDAVDHSGRSALMVAAdYGQS--G 900
Cdd:PHA02876 348 AsTLDRNKDIVITLLE---LGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAL-CGTNpyM 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 901 AVALLLHRAkADLSLLDVNKNTALHLACSKAhemCAMLILKE-IHNPILINATNSMLQMPLHIAArnGLATVVQALLNRG 979
Cdd:PHA02876 424 SVKTLIDRG-ANVNSKNKDLSTPLHYACKKN---CKLDVIEMlLDNGADVNAINIQNQYPLLIAL--EYHGIVNILLHYG 497
|
.
gi 66392221 980 A 980
Cdd:PHA02876 498 A 498
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
243-336 |
2.82e-12 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 63.60 E-value: 2.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 243 LHVACYTGQEAVANELVNRGANVNQPNHRGYTPLHLAAvSTNGALCLELLVNNgADVNMQSkEGKSPLHMAAIHGRFTRS 322
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAA-KNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77
|
90
....*....|....
gi 66392221 323 QILIQNGGEIDCVD 336
Cdd:pfam12796 78 KLLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
790-883 |
3.11e-12 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 63.60 E-value: 3.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 790 HWAAYHGHEDCLEVLLELKP-CSIQEGNPFTPLHCALINGHSGSAELLLESSVCNSlvnirDAKGRTPLHAAAVAEDVAG 868
Cdd:pfam12796 2 HLAAKNGNLELVKLLLENGAdANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL-----KDNGRTALHYAARSGHLEI 76
|
90
....*....|....*
gi 66392221 869 LQLVLRQGADIDAVD 883
Cdd:pfam12796 77 VKLLLEKGADINVKD 91
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
154-346 |
7.28e-12 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 69.09 E-value: 7.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 154 EMVKLLLNKGANLSASDKKDRQPI-----HWAAYLGHLEVVKLLVSQGSDKSCKDKRGYTPLHAAAASGHV---DVVKYL 225
Cdd:PHA02798 52 DIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYInnlEILLFM 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 226 LRNGAEIDEPNAFGNTALHVACYTG---QEAVANELVNRGANVNQPNHR-GYTPLHL---AAVSTNGALCLELLVNNGAD 298
Cdd:PHA02798 132 IENGADTTLLDKDGFTMLQVYLQSNhhiDIEIIKLLLEKGVDINTHNNKeKYDTLHCyfkYNIDRIDADILKLFVDNGFI 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 299 VNMQSKEGKS---------------------------------------PLHMAAIHGRFTRSQILIQNGGEIDCVDRYG 339
Cdd:PHA02798 212 INKENKSHKKkfmeylnsllydnkrfkknildfifsyidinqvdelgfnPLYYSVSHNNRKIFEYLLQLGGDINIITELG 291
|
....*..
gi 66392221 340 NTPLHVA 346
Cdd:PHA02798 292 NTCLFTA 298
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
213-450 |
8.40e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 68.48 E-value: 8.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 213 AAASGHVDVVKYLLRNGAEIDEPNAFGNTALHVACYTGQEAVANELVNRGA--NVNQPNHRgyTPLHLAAVSTNGALCLE 290
Cdd:PHA02875 9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAipDVKYPDIE--SELHDAVEEGDVKAVEE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 291 LLVNNGADVNMQSKEGKSPLHMAAIHGRFTRSQILIQNGGEIDCVDRYGNTPLHVAAKYGHELLISTLMTNGADTARQGI 370
Cdd:PHA02875 87 LLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDC 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 371 HGMFPLHLAVLYGSSDCCRKLLSSGQlysivlsmskehvlsagfdinTPDNFGR----TCLHAAASGGNIECLNLLLSSG 446
Cdd:PHA02875 167 CGCTPLIIAMAKGDIAICKMLLDSGA---------------------NIDYFGKngcvAALCYAIENNKIDIVRLFIKRG 225
|
....
gi 66392221 447 ADMN 450
Cdd:PHA02875 226 ADCN 229
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
719-806 |
8.40e-12 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 62.06 E-value: 8.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 719 LHRGAVMGREDCLTALLSHNVSVLSRDFQGRSALHLAASCGHADILSNLLSAAdhsqpqDPLTDRHGYTPAHWAAYHGHE 798
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA------DVNLKDNGRTALHYAARSGHL 74
|
....*...
gi 66392221 799 DCLEVLLE 806
Cdd:pfam12796 75 EIVKLLLE 82
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
526-607 |
9.92e-12 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 62.06 E-value: 9.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 526 CVEHLLDNGADPCLCNTKGYSAVHYAAAHGNKQNLELLLEMCFntlGDKESNGSiSPLHLAVESGHWECVTVLIESGVCV 605
Cdd:pfam12796 12 LVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD---VNLKDNGR-TALHYAARSGHLEIVKLLLEKGADI 87
|
..
gi 66392221 606 DV 607
Cdd:pfam12796 88 NV 89
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
676-929 |
1.06e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 68.09 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 676 NVTDAEGQTPLMLAVLGGHTDCVHLLLERGACPDMKDRRGRTALHRGAVMGREDCLTALLSHNV---SVLSRDfqGRSAL 752
Cdd:PHA02875 29 NFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKfadDVFYKD--GMTPL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 753 HLAASCGHADILSNLLsaADHSQPQDPLTDRhgytpahwaayhghedclevllelkpcsiqegnpFTPLHCALINGHSGS 832
Cdd:PHA02875 107 HLATILKKLDIMKLLI--ARGADPDIPNTDK----------------------------------FSPLHLAVMMGDIKG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 833 AELLLESSVCnslVNIRDAKGRTPLHAAAVAEDVAGLQLVLRQGADIDAVDHSGRSALM-VAADYGQSGAVALLLHRAkA 911
Cdd:PHA02875 151 IELLIDHKAC---LDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALcYAIENNKIDIVRLFIKRG-A 226
|
250 260
....*....|....*....|.
gi 66392221 912 DLSLLDVNKN---TALHLACS 929
Cdd:PHA02875 227 DCNIMFMIEGeecTILDMICN 247
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
423-476 |
1.32e-11 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 60.37 E-value: 1.32e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 66392221 423 GRTCLHAAASGGNIECLNLLLSSGADMNKKDKFGRTPLHYAAANGRYQCVVVLV 476
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
180-338 |
1.44e-11 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 68.74 E-value: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 180 AAYLGHLEVVKLLVSQGSDKSCKDKRGYTPLHAAAASGHVDVVKYLLRNGAEIDEPNAFGNTALHVACYTGQEAVANeLV 259
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFR-IL 610
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66392221 260 NRGANVNQPnHRGYTPLHLAAVSTNGALCLELLvNNGADVNMQSKEGKSPLHMAAIHGRFTRSQILIQNGGEIDCVDRY 338
Cdd:PLN03192 611 YHFASISDP-HAAGDLLCTAAKRNDLTAMKELL-KQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTD 687
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
579-860 |
1.77e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 67.68 E-value: 1.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 579 SISPLHLAVESGHWECVTVLIESGVCVDVCDPVGRSVLYLASQRGHSRCVELLLSQSAS-------CLLAE--------- 642
Cdd:PHA02874 35 TTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDtsilpipCIEKDmiktildcg 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 643 ------HRSKWGPLHVAAANGHSECLRMLLcsEGGADlVNVTDAEGQTPLMLAVLGGHTDCVHLLLERGACPDMKDRRGR 716
Cdd:PHA02874 115 idvnikDAELKTFLHYAIKKGDLESIKMLF--EYGAD-VNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 717 TALHRGAVMGREDCLTALLSHNVsvlsrdfqgrsalHLAASCghadilsnllsaadhsqpqdpltdRHGYTPAHWAAYHg 796
Cdd:PHA02874 192 SPLHNAAEYGDYACIKLLIDHGN-------------HIMNKC------------------------KNGFTPLHNAIIH- 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66392221 797 HEDCLEVLLELKPCSIQEGNPFTPLHCALinGHSGSAELLLESSVCNSLVNIRDAKGRTPLHAA 860
Cdd:PHA02874 234 NRSAIELLINNASINDQDIDGSTPLHHAI--NPPCDIDIIDILLYHKADISIKDNKGENPIDTA 295
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
174-226 |
1.82e-11 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 59.98 E-value: 1.82e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 66392221 174 RQPIHWAAYLGHLEVVKLLVSQGSDKSCKDKRGYTPLHAAAASGHVDVVKYLL 226
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
342-691 |
3.65e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 66.83 E-value: 3.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 342 PLHVAAKYGHELLISTLMTNGADTARQGIHGMFPLHLAVLYGSSDCCRKLLSSGQLYSIVLSMSK-------------EH 408
Cdd:PHA02878 40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFYTLVAikdafnnrnveifKI 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 409 VLSAGFDINTPDNFGRTCLHAAASGGNIECLNLLLSSGADMNKKDK-FGRTPLHYAAANGRYQCVVVLVGAGAEVNERDR 487
Cdd:PHA02878 120 ILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDK 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 488 SGCTPLHysaastafcrtdrpHASTHQNqEDGekesflcVEHLLDNGAdpclcNTKgysavhyaaaHGNKqnlelllemC 567
Cdd:PHA02878 200 TNNSPLH--------------HAVKHYN-KPI-------VHILLENGA-----STD----------ARDK---------C 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 568 FNTlgdkesngsisPLHLAVES-GHWECVTVLIESGVCVDVcdpvgrsvlyLASQRGHSrcvelllsqsascllaehrsk 646
Cdd:PHA02878 234 GNT-----------PLHISVGYcKDYDILKLLLEHGVDVNA----------KSYILGLT--------------------- 271
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 66392221 647 wgPLHVAAangHSE-CLRMLLcsEGGADlVNVTDAEGQTPLMLAVL 691
Cdd:PHA02878 272 --ALHSSI---KSErKLKLLL--EYGAD-INSLNSYKLTPLSSAVK 309
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
755-906 |
5.32e-11 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 66.82 E-value: 5.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 755 AASCGHADILSNLLSAAdhsqpQDP-LTDRHGYTPAHWAAYHGHEDCLEVLLElKPCS--IQEGNPFTPLHCALINGHSG 831
Cdd:PLN03192 532 VASTGNAALLEELLKAK-----LDPdIGDSKGRTPLHIAASKGYEDCVLVLLK-HACNvhIRDANGNTALWNAISAKHHK 605
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66392221 832 SAELLLEssvCNSLVNIRdaKGRTPLHAAAVAEDVAGLQLVLRQGADIDAVDHSGRSALMVAADYGQSGAVALLL 906
Cdd:PLN03192 606 IFRILYH---FASISDPH--AAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLI 675
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
206-259 |
5.83e-11 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 58.44 E-value: 5.83e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 66392221 206 GYTPLHAAAASGHVDVVKYLLRNGAEIDEPNAFGNTALHVACYTGQEAVANELV 259
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
18-168 |
1.40e-10 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 65.05 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 18 NRNADEVKLFLHKKDEVNALDQERRTPLHaaawlgdVH---------IMDLLISAGANVNAKDHVWLTPLHRAAASRNER 88
Cdd:PHA03095 164 NANVELLRLLIDAGADVYAVDDRFRSLLH-------HHlqsfkprarIVRELIRAGCDPAATDMLGNTPLHSMATGSSCK 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 89 A--VGLLLRKGADVTARDKYWQTPLHIAAANRATRCVETLLPHVSSLNMADRTGRAPLHHAAQSGYQEMVKLLLNKGANL 166
Cdd:PHA03095 237 RslVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSA 316
|
..
gi 66392221 167 SA 168
Cdd:PHA03095 317 ET 318
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
31-228 |
2.15e-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: 64.65 E-value: 2.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 31 KDEVNALDQER--RTPLHAAAWLGDVH-IMDLLISAGANVNAKDHVWLTPLHRAAASRNERAVGLLLRKGAD-----VTA 102
Cdd:cd22192 5 LDELHLLQQKRisESPLLLAAKENDVQaIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElvnepMTS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 103 RDKYWQTPLHIAAANRATRCVETLLPHVSSLNMADRTGRA--------------PLHHAAQSGYQEMVKLLLNKGANLSA 168
Cdd:cd22192 85 DLYQGETALHIAVVNQNLNLVRELIARGADVVSPRATGTFfrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADIRA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 169 SDkkdrqpihwaaYLGHlEVVKLLVSQGS-DKSCK---------------------DKRGYTPLHAAAASGHVDVVKYLL 226
Cdd:cd22192 165 QD-----------SLGN-TVLHILVLQPNkTFACQmydlilsydkeddlqpldlvpNNQGLTPFKLAAKEGNIVMFQHLV 232
|
..
gi 66392221 227 RN 228
Cdd:cd22192 233 QK 234
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
144-237 |
2.72e-10 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 64.53 E-value: 2.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 144 LHHAAQSGYQEMVKLLLNKGANLSASDKKDRQPIHWAAYLGHLEVVKLLVSQGSDKSCKDKRGYTPLHAAAASGHVDVVK 223
Cdd:PTZ00322 86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165
|
90
....*....|....
gi 66392221 224 YLLRNGAEIDEPNA 237
Cdd:PTZ00322 166 LLSRHSQCHFELGA 179
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
140-193 |
5.58e-10 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 55.74 E-value: 5.58e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 66392221 140 GRAPLHHAAQSGYQEMVKLLLNKGANLSASDKKDRQPIHWAAYLGHLEVVKLLV 193
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
890-986 |
6.19e-10 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 57.05 E-value: 6.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 890 LMVAADYGQSGAVALLLhRAKADLSLLDVNKNTALHLACSKAHEMCAMLILKEIH-NPILINATnsmlqmPLHIAARNGL 968
Cdd:pfam12796 1 LHLAAKNGNLELVKLLL-ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADvNLKDNGRT------ALHYAARSGH 73
|
90
....*....|....*...
gi 66392221 969 ATVVQALLNRGATVLAVD 986
Cdd:pfam12796 74 LEIVKLLLEKGADINVKD 91
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
428-493 |
6.91e-10 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 62.99 E-value: 6.91e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66392221 428 HAAASGGNIEcLNLLLSSGADMNKKDKFGRTPLHYAAANGRYQCVVVLVGAGAEVNERDRSGCTPL 493
Cdd:PTZ00322 88 QLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPL 152
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
549-638 |
7.67e-10 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 56.66 E-value: 7.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 549 HYAAAHGNKQNLELLLEMCFNtLGDKESNGsISPLHLAVESGHWECVTVLIESgVCVDVCDPvGRSVLYLASQRGHSRCV 628
Cdd:pfam12796 2 HLAAKNGNLELVKLLLENGAD-ANLQDKNG-RTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIV 77
|
90
....*....|
gi 66392221 629 ELLLSQSASC 638
Cdd:pfam12796 78 KLLLEKGADI 87
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
857-944 |
8.80e-10 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 56.66 E-value: 8.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 857 LHAAAVAEDVAGLQLVLRQGADIDAVDHSGRSALMVAADYGQSGAVALLLHRAKADlslLDVNKNTALHLACSKAH-EMC 935
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN---LKDNGRTALHYAARSGHlEIV 77
|
....*....
gi 66392221 936 AMLILKEIH 944
Cdd:pfam12796 78 KLLLEKGAD 86
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
274-461 |
1.06e-09 |
|
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: 62.34 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 274 TPLHLAAvSTNGALCLE-LLVNNGADVNMQSKEGKSPLHMAAIHGRFTRSQILIQNGGEIDCV----DRY-GNTPLHVAA 347
Cdd:cd22192 19 SPLLLAA-KENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEpmtsDLYqGETALHIAV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 348 KYGHELLISTLMTNGADTA---------RQGIHGMFplhlavLYGssdccrkllssgqlysivlsmskEHVLSagfdint 418
Cdd:cd22192 98 VNQNLNLVRELIARGADVVspratgtffRPGPKNLI------YYG-----------------------EHPLS------- 141
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 66392221 419 pdnFgrtclhaAASGGNIECLNLLLSSGADMNKKDKFGRTPLH 461
Cdd:cd22192 142 ---F-------AACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
|
|
| PHA02989 |
PHA02989 |
ankyrin repeat protein; Provisional |
90-317 |
1.27e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222954 [Multi-domain] Cd Length: 494 Bit Score: 62.07 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 90 VGLLLRKGADVTARDkYWQTPLHIAAANRA------TRCVETLLPHVSSLNMADRTGRAPLH---HAAQSGYQEMVKLLL 160
Cdd:PHA02989 53 VKLLIDNGADVNYKG-YIETPLCAVLRNREitsnkiKKIVKLLLKFGADINLKTFNGVSPIVcfiYNSNINNCDMLRFLL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 161 NKGANL-SASDKKDRQPIHwaAYLG----HLEVVKLLVSQGSDK-SCKDKRGYTP----LHAAAASGHVDVVKYLLRNGA 230
Cdd:PHA02989 132 SKGINVnDVKNSRGYNLLH--MYLEsfsvKKDVIKILLSFGVNLfEKTSLYGLTPmniyLRNDIDVISIKVIKYLIKKGV 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 231 EIDEPNAFGNTAL------HVACYTGQEAVANELVNRgANVNQPNHRGYTPLHLAAVSTNGALCLELLvNNGADVNMQSK 304
Cdd:PHA02989 210 NIETNNNGSESVLesfldnNKILSKKEFKVLNFILKY-IKINKKDKKGFNPLLISAKVDNYEAFNYLL-KLGDDIYNVSK 287
|
250
....*....|...
gi 66392221 305 EGKSPLHMAAIHG 317
Cdd:PHA02989 288 DGDTVLTYAIKHG 300
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
605-826 |
1.32e-09 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 62.41 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 605 VDVCDPVGRSVLYLASQRG-HSRCVELLLSQSasCLLAEHRSKwgpLHVAAANGH---SECLRMLLCSEGGAD---LVNV 677
Cdd:TIGR00870 45 INCPDRLGRSALFVAAIENeNLELTELLLNLS--CRGAVGDTL---LHAISLEYVdavEAILLHLLAAFRKSGpleLAND 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 678 TDA----EGQTPLMLAVLGGHTDCVHLLLERGA-------CPDMKDRRGRTALHRG-------AVMGREDCLTALLSHNV 739
Cdd:TIGR00870 120 QYTseftPGITALHLAAHRQNYEIVKLLLERGAsvparacGDFFVKSQGVDSFYHGesplnaaACLGSPSIVALLSEDPA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 740 SVLSRDFQGRSALHLAA------------SCGHADILSNLLSAADHSQPQDPLTDRHGYTPAHWAAYHGHEDCLEVLLEL 807
Cdd:TIGR00870 200 DILTADSLGNTLLHLLVmenefkaeyeelSCQMYNFALSLLDKLRDSKELEVILNHQGLTPLKLAAKEGRIVLFRLKLAI 279
|
250 260
....*....|....*....|
gi 66392221 808 KPCSIQ-EGNPFTPLHCALI 826
Cdd:TIGR00870 280 KYKQKKfVAWPNGQQLLSLY 299
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
35-152 |
1.36e-09 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 61.58 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 35 NALDQERRTPLHAAAWLGDVH--IMDLLISAGANVNAKDHVWLTPLHRAAASRNERAVGLLLRKGADVTARDKYWQTPLH 112
Cdd:PHA03095 216 AATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLS 295
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 66392221 113 IAAANRATRCVETLLPHVSSLNMADRTgrapLHHAAQSGY 152
Cdd:PHA03095 296 LMVRNNNGRAVRAALAKNPSAETVAAT----LNTASVAGG 331
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
339-564 |
1.60e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 61.16 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 339 GNTPLHVAAKYGHELLISTLMTNGA--DTARQGIHGmfPLHLAVLYGSSDCCRKLLSSGQLYSIVLSMskehvlsagfDI 416
Cdd:PHA02875 35 GISPIKLAMKFRDSEAIKLLMKHGAipDVKYPDIES--ELHDAVEEGDVKAVEELLDLGKFADDVFYK----------DG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 417 NTPdnfgrtcLHAAASGGNIECLNLLLSSGAD--MNKKDKFgrTPLHYAAANGRYQCVVVLVGAGAEVNERDRSGCTPLH 494
Cdd:PHA02875 103 MTP-------LHLATILKKLDIMKLLIARGADpdIPNTDKF--SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLI 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66392221 495 YSAA--STAFCRTdrphasthqnqedgekesflcvehLLDNGADPCLCNTKGYSAVHYAAAHGNKQNLELLL 564
Cdd:PHA02875 174 IAMAkgDIAICKM------------------------LLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLF 221
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
662-883 |
1.62e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 61.22 E-value: 1.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 662 LRMLLcsEGGADLVNVTDAEgQTPLMLAVLGGHT-----DCVHLLLERGACPDMKDRRGRTALHRGAV--MGREDCLTAL 734
Cdd:PHA03100 51 VKILL--DNGADINSSTKNN-STPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISkkSNSYSIVEYL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 735 LSHNVSVLSRDFQGRSALHLAASCGHAD--ILSNLLSaadhsqpqdpltdrHGYtpahwaaYHGHEDCLEVLLELK-PCS 811
Cdd:PHA03100 128 LDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLID--------------KGV-------DINAKNRVNYLLSYGvPIN 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66392221 812 IQEGNPFTPLHCALINGHSGSAELLLESSvCNslVNIRDAKGRTPLHAAAVAEDVAGLQLVLRQGADIDAVD 883
Cdd:PHA03100 187 IKDVYGFTPLHYAVYNNNPEFVKYLLDLG-AN--PNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTII 255
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
54-313 |
2.31e-09 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 61.00 E-value: 2.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 54 VHIMDLLISAGANVNAKDHVWLTPLhraaasrneravglllrkgADVTARDKYWQTPLHIaaanratrcVETLLPHVSSL 133
Cdd:PHA02798 51 TDIVKLFINLGANVNGLDNEYSTPL-------------------CTILSNIKDYKHMLDI---------VKILIENGADI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 134 NMADRTGRAPLHHAAQSGY---QEMVKLLLNKGANLSASDKKDRQPIHWAAYLGH---LEVVKLLVSQGSD-KSCKDKRG 206
Cdd:PHA02798 103 NKKNSDGETPLYCLLSNGYinnLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDiNTHNNKEK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 207 YTPLHAAAASG----HVDVVKYLLRNGAEIDEPNAFGNTALhvACYTGQEAVANELVNRGA--------NVNQPNHRGYT 274
Cdd:PHA02798 183 YDTLHCYFKYNidriDADILKLFVDNGFIINKENKSHKKKF--MEYLNSLLYDNKRFKKNIldfifsyiDINQVDELGFN 260
|
250 260 270
....*....|....*....|....*....|....*....
gi 66392221 275 PLHLaAVSTNGALCLELLVNNGADVNMQSKEGKSPLHMA 313
Cdd:PHA02798 261 PLYY-SVSHNNRKIFEYLLQLGGDINIITELGNTCLFTA 298
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
337-494 |
2.57e-09 |
|
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: 61.18 E-value: 2.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 337 RYGNTPLHVAAKYGHELLISTLMT-NGADTARQGIHGMFPLHLAVLYGSSDCCRKLLSSgqlysiVLSMSKEHVLSAGFD 415
Cdd:cd22192 15 RISESPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEA------APELVNEPMTSDLYQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 416 intpdnfGRTCLHAAASGGNIECLNLLLSSGADM------------NKKDK--FGRTPLHYAAANGRYQCVVVLVGAGAE 481
Cdd:cd22192 89 -------GETALHIAVVNQNLNLVRELIARGADVvspratgtffrpGPKNLiyYGEHPLSFAACVGNEEIVRLLIEHGAD 161
|
170
....*....|...
gi 66392221 482 VNERDRSGCTPLH 494
Cdd:cd22192 162 IRAQDSLGNTVLH 174
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
429-606 |
3.40e-09 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 61.04 E-value: 3.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 429 AAASGGNIECLNLLLSSGADMNKKDKFGRTPLHYAAANGRYQCVVVLVGAGAEVNERDRSGCTPLHYSAAST-------- 500
Cdd:PLN03192 531 TVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKhhkifril 610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 501 -AFCRTDRPHAsthqnqedgekesflcvehlldnGADpCLCntkgysavhYAAAHGNKQNLELLLEMCFNTlgDKESNGS 579
Cdd:PLN03192 611 yHFASISDPHA-----------------------AGD-LLC---------TAAKRNDLTAMKELLKQGLNV--DSEDHQG 655
|
170 180
....*....|....*....|....*..
gi 66392221 580 ISPLHLAVESGHWECVTVLIESGVCVD 606
Cdd:PLN03192 656 ATALQVAMAEDHVDMVRLLIMNGADVD 682
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
66-284 |
3.88e-09 |
|
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: 60.87 E-value: 3.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 66 NVNAKDHVWLTPLHRAAA-SRNERAVGLLLRKGADVTARDkywqTPLHiAAANRATRCVETLLPHV-------SSLNMA- 136
Cdd:TIGR00870 44 NINCPDRLGRSALFVAAIeNENLELTELLLNLSCRGAVGD----TLLH-AISLEYVDAVEAILLHLlaafrksGPLELAn 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 137 DRT------GRAPLHHAAQSGYQEMVKLLLNKGANLSA---------SDKKD-----RQPIHWAAYLGHLEVVKLLVSQG 196
Cdd:TIGR00870 119 DQYtseftpGITALHLAAHRQNYEIVKLLLERGASVPAracgdffvkSQGVDsfyhgESPLNAAACLGSPSIVALLSEDP 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 197 SDKSCKDKRGYTPLHAAAasghvdvvkyllrngaeIDEPNAFGNTALHVACYtgqeavaNELVNRGANVNQ-------PN 269
Cdd:TIGR00870 199 ADILTADSLGNTLLHLLV-----------------MENEFKAEYEELSCQMY-------NFALSLLDKLRDskeleviLN 254
|
250
....*....|....*
gi 66392221 270 HRGYTPLHLAAVSTN 284
Cdd:TIGR00870 255 HQGLTPLKLAAKEGR 269
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
654-737 |
4.74e-09 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 60.30 E-value: 4.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 654 AANGHSECLRMLLcsEGGADlVNVTDAEGQTPLMLAVLGGHTDCVHLLLERGACPDMKDRRGRTALHRGAVMGREDCLTA 733
Cdd:PTZ00322 90 AASGDAVGARILL--TGGAD-PNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166
|
....
gi 66392221 734 LLSH 737
Cdd:PTZ00322 167 LSRH 170
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
582-893 |
1.24e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 58.74 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 582 PLHLAVESGHWECVTVLIESGVCVDVCDPVGRSVLYLASQRGHSRCVELLLSQSASCLLAEHRSKwgpLHVAAANGHSEC 661
Cdd:PHA02878 40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFYTLVA---IKDAFNNRNVEI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 662 LRMLLCS----EGGADLVNVTDAEGQTPLmlavlggHTDCVHLLLERGACPDMKDR-RGRTALHRGAVMGREDCLTALLS 736
Cdd:PHA02878 117 FKIILTNryknIQTIDLVYIDKKSKDDII-------EAEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 737 HNVSVLSRDFQGRSALHLAASCGHADILSNLL---SAADHSqpqdpltDRHGYTPAHWAAyhGHEDCLEVLlelkpcsiq 813
Cdd:PHA02878 190 YGANVNIPDKTNNSPLHHAVKHYNKPIVHILLengASTDAR-------DKCGNTPLHISV--GYCKDYDIL--------- 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 814 egnpftplhcalinghsgsaELLLESSVCnslVNIRDA-KGRTPLHAAAVAEDVagLQLVLRQGADIDAVDHSGRSALMV 892
Cdd:PHA02878 252 --------------------KLLLEHGVD---VNAKSYiLGLTALHSSIKSERK--LKLLLEYGADINSLNSYKLTPLSS 306
|
.
gi 66392221 893 A 893
Cdd:PHA02878 307 A 307
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
139-284 |
1.37e-08 |
|
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: 58.74 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 139 TGRAPLHHAA---QSGYQEMVKLLLNKG---------ANLSASDK--KDRQPIHWAAYLGHLEVVKLLVSQGSD---KSC 201
Cdd:cd21882 25 TGKTCLHKAAlnlNDGVNEAIMLLLEAApdsgnpkelVNAPCTDEfyQGQTALHIAIENRNLNLVRLLVENGADvsaRAT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 202 KD--KR--------GYTPLHAAAASGHVDVVKYLLRNGAEIDEPNA---FGNTALHVACYTGQEAVA---------NELV 259
Cdd:cd21882 105 GRffRKspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPAALEAqdsLGNTVLHALVLQADNTPEnsafvcqmyNLLL 184
|
170 180 190
....*....|....*....|....*....|..
gi 66392221 260 NRGANVNQ-------PNHRGYTPLHLAAVSTN 284
Cdd:cd21882 185 SYGAHLDPtqqleeiPNHQGLTPLKLAAVEGK 216
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
7-152 |
1.39e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 58.74 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 7 SDQPPLVQAIFNRNADEVKLFLHKKDEVNALDQERRTPLHAAAWLGDVHIMDLLISAGANVNAKDHVWLTPLHRAAAS-R 85
Cdd:PHA02878 167 KGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcK 246
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66392221 86 NERAVGLLLRKGADVTARDKYWQ-TPLHIAAanRATRCVETLLPHVSSLNMADRTGRAPLHHAAQSGY 152
Cdd:PHA02878 247 DYDILKLLLEHGVDVNAKSYILGlTALHSSI--KSERKLKLLLEYGADINSLNSYKLTPLSSAVKQYL 312
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
833-999 |
1.68e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 58.54 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 833 AELLLESSVCnslVNIRDAKGRTPLHAAAVAEDVAGLQLVLRQGADIDAVDHSGRSALMVAADYGQSGAV-ALLLHRA-- 909
Cdd:PHA02876 161 AEMLLEGGAD---VNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIkAIIDNRSni 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 910 -KADLSLLDVNKNTALHLAcskahemcamLILKEihNPILINATNSMLQMPLHIAARN-GLATVVQALLNRGATVLAVDE 987
Cdd:PHA02876 238 nKNDLSLLKAIRNEDLETS----------LLLYD--AGFSVNSIDDCKNTPLHHASQApSLSRLVPKLLERGADVNAKNI 305
|
170
....*....|..
gi 66392221 988 EGHTPALACASN 999
Cdd:PHA02876 306 KGETPLYLMAKN 317
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
821-917 |
2.20e-08 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 52.43 E-value: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 821 LHCALINGHSGSAELLLEssvCNSLVNIRDAKGRTPLHAAAVAEDVAGLQLVLRQgADIDAVDHsGRSALMVAADYGQSG 900
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLE---NGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLE 75
|
90
....*....|....*..
gi 66392221 901 AVALLLHRaKADLSLLD 917
Cdd:pfam12796 76 IVKLLLEK-GADINVKD 91
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
74-127 |
3.58e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 50.74 E-value: 3.58e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 66392221 74 WLTPLHRAAASRNERAVGLLLRKGADVTARDKYWQTPLHIAAANRATRCVETLL 127
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
183-374 |
3.69e-08 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 57.57 E-value: 3.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 183 LGHLEVVKLLVSQGSDKSckDKRGYTPLHAAAASGHVDVVKYLLRNGAEIDEPNAFGNTALHVACYTGQEAVANELVNRG 262
Cdd:PLN03192 504 LHDLNVGDLLGDNGGEHD--DPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHA 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 263 ANVNQPNHRGYTPLhLAAVSTNGALCLELLVNNGADVNMQSkeGKSPLHMAAIHGRFTRSQILIQNGGEIDCVDRYGNTP 342
Cdd:PLN03192 582 CNVHIRDANGNTAL-WNAISAKHHKIFRILYHFASISDPHA--AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATA 658
|
170 180 190
....*....|....*....|....*....|..
gi 66392221 343 LHVAAKYGHELLISTLMTNGADTARQGIHGMF 374
Cdd:PLN03192 659 LQVAMAEDHVDMVRLLIMNGADVDKANTDDDF 690
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
72-176 |
3.78e-08 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 57.60 E-value: 3.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 72 HVWLTPLHRAAASRNERAVGLLLRKGADVTARDKYWQTPLHIAAANRATRCVETLLPHVSSLNMADRTGRAPLHHAAQSG 151
Cdd:PTZ00322 80 HMLTVELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENG 159
|
90 100 110
....*....|....*....|....*....|..
gi 66392221 152 YQEMVKLLL-------NKGANlSASDKKDRQP 176
Cdd:PTZ00322 160 FREVVQLLSrhsqchfELGAN-AKPDSFTGKP 190
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
647-702 |
5.19e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 50.35 E-value: 5.19e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 66392221 647 WGPLHVAAANGHSECLRMLLCSegGADlVNVTDAEGQTPLMLAVLGGHTDCVHLLL 702
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEK--GAD-INAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
551-706 |
5.74e-08 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 57.19 E-value: 5.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 551 AAAHGNKQNLELLLEMCFNT-LGDkeSNGSiSPLHLAVESGHWECVTVLIESGVCVDVCDPVGRSVLYLASQRGHSRCVE 629
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPdIGD--SKGR-TPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFR 608
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66392221 630 LLLSQSAsclLAEHRSKWGPLHVAAANGHSECLRMLLcsEGGADlVNVTDAEGQTPLMLAVLGGHTDCVHLLLERGA 706
Cdd:PLN03192 609 ILYHFAS---ISDPHAAGDLLCTAAKRNDLTAMKELL--KQGLN-VDSEDHQGATALQVAMAEDHVDMVRLLIMNGA 679
|
|
| PHA02716 |
PHA02716 |
CPXV016; CPX019; EVM010; Provisional |
289-493 |
7.22e-08 |
|
CPXV016; CPX019; EVM010; Provisional
Pssm-ID: 165089 [Multi-domain] Cd Length: 764 Bit Score: 56.84 E-value: 7.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 289 LELLVNNGADVNMQSKEGKSPLHMAAIHGRFTRSQI--LIQNGGEID--CVDryGNTPlhvaakyghellISTLMTNGAD 364
Cdd:PHA02716 195 LEWLCNNGVNVNLQNNHLITPLHTYLITGNVCASVIkkIIELGGDMDmkCVN--GMSP------------IMTYIINIDN 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 365 TARQGIHgmfplhlavLYGSSDCCRKLLSSGQLYSIVLSMSK-------EHVLSAGFDINTPDNFGRTCLHAAASGGNI- 436
Cdd:PHA02716 261 INPEITN---------IYIESLDGNKVKNIPMILHSYITLARnidisvvYSFLQPGVKLHYKDSAGRTCLHQYILRHNIs 331
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66392221 437 -ECLNLLLSSGADMNKKDKFGRTPLHYAAA--------------NGRYQCVVVLVGAGAEVNERDRSGCTPL 493
Cdd:PHA02716 332 tDIIKLLHEYGNDLNEPDNIGNTVLHTYLSmlsvvnildpetdnDIRLDVIQCLISLGADITAVNCLGYTPL 403
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
143-278 |
8.56e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 54.05 E-value: 8.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 143 PLHHAAQSGY--QEMVKLLLNKGANLSASDKKDR-QPIHWaaYLGH-----LEVVKLLVSQGSDKSCKDKRGYTPLHA-- 212
Cdd:PHA02859 54 PIFSCLEKDKvnVEILKFLIENGADVNFKTRDNNlSALHH--YLSFnknvePEILKILIDSGSSITEEDEDGKNLLHMym 131
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66392221 213 AAASGHVDVVKYLLRNGAEIDEPNAFGNTALHV-ACYTGQEAVANELVNRGANVNQPNHRGYTPLHL 278
Cdd:PHA02859 132 CNFNVRINVIKLLIDSGVSFLNKDFDNNNILYSyILFHSDKKIFDFLTSLGIDINETNKSGYNCYDL 198
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
53-278 |
1.19e-07 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 55.45 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 53 DVHIMDLLISAGANVNAKDHVWLTPLHRAAASRNERAVGLLLRKGADVTARDKYWQTPLHIAAA--NRATRCVETLLPHV 130
Cdd:PHA02946 51 DERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGtdDEVIERINLLVQYG 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 131 SSLNMA-DRTGRAPLhhaaqsgyqemvklllnkganLSASDKKDRqpihwaaylghleVVKLLVSQGSDKSCKDKRGYTP 209
Cdd:PHA02946 131 AKINNSvDEEGCGPL---------------------LACTDPSER-------------VFKKIMSIGFEARIVDKFGKNH 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66392221 210 LHAAAASGH--VDVVKYLLRNGAEIDEPNAFGNTALHVACytgQEAVAN----ELVNRGANVNQPNHRGYTPLHL 278
Cdd:PHA02946 177 IHRHLMSDNpkASTISWMMKLGISPSKPDHDGNTPLHIVC---SKTVKNvdiiNLLLPSTDVNKQNKFGDSPLTL 248
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
785-837 |
1.80e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 48.81 E-value: 1.80e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 66392221 785 GYTPAHWAAYHGHEDCLEVLLELK-PCSIQEGNPFTPLHCALINGHSGSAELLL 837
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGaDINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
834-999 |
1.89e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 54.67 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 834 ELLLESSVCnslVNIRDAKGRTPLHAAAVAEDVAG-----LQLVLRQGADIDAVDHSGRSALMVAADY--GQSGAVALLL 906
Cdd:PHA03100 52 KILLDNGAD---INSSTKNNSTPLHYLSNIKYNLTdvkeiVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 907 HRAkADLSLLDVNKNTALHLA---CSKAHEMCAMLILKEIH------------NPILINATNSMLQMPLHIAARNGLATV 971
Cdd:PHA03100 129 DNG-ANVNIKNSDGENLLHLYlesNKIDLKILKLLIDKGVDinaknrvnyllsYGVPINIKDVYGFTPLHYAVYNNNPEF 207
|
170 180
....*....|....*....|....*....
gi 66392221 972 VQALLNRGATVLAVDEEGHTPA-LACASN 999
Cdd:PHA03100 208 VKYLLDLGANPNLVNKYGDTPLhIAILNN 236
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
396-719 |
2.58e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 54.50 E-value: 2.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 396 QLYSIVLSMSKEHVLSAGFDINTPDNF--GRTC-----LHAAASGGNIECLNLLLSSGADMNKKDKFGRTPLHYAAANGR 468
Cdd:PHA02878 3 KLYKSMYTDNYETILKYIEYIDHTENYstSASLipfipLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 469 YQCVVVLVgagAEVNERDRSgctpLHYSAASTAFCRTDRPHA-STHQNQEDGEKES---FLCvEHLLDNGADPCLcntkg 544
Cdd:PHA02878 83 KLGMKEMI---RSINKCSVF----YTLVAIKDAFNNRNVEIFkIILTNRYKNIQTIdlvYID-KKSKDDIIEAEI----- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 545 ysaVHYAAAHGNKQNLelllemcfntlgdKESNGSISPLHLAVESGHWECVTVLIESGVCVDVCDPVGRSVLYLASQRGH 624
Cdd:PHA02878 150 ---TKLLLSYGADINM-------------KDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYN 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 625 SRCVELLLSQSAScllAEHRSKWG--PLHVAAANGHS-ECLRMLLcsEGGADLVNVTDAEGQTPLMLAVlgGHTDCVHLL 701
Cdd:PHA02878 214 KPIVHILLENGAS---TDARDKCGntPLHISVGYCKDyDILKLLL--EHGVDVNAKSYILGLTALHSSI--KSERKLKLL 286
|
330
....*....|....*...
gi 66392221 702 LERGACPDMKDRRGRTAL 719
Cdd:PHA02878 287 LEYGADINSLNSYKLTPL 304
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
581-720 |
2.60e-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: 2.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 581 SPLHLAVESGHWECVTVLIESGVCvDVCD--PVGRSVLYLASQRGH-------SRCVELLLSQSASCLLAEHRSkwgPLH 651
Cdd:cd22192 19 SPLLLAAKENDVQAIKKLLKCPSC-DLFQrgALGETALHVAALYDNleaavvlMEAAPELVNEPMTSDLYQGET---ALH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 652 VAAANGHSECLRMLLcsEGGADLVN--VTDA-----------EGQTPLMLAVLGGHTDCVHLLLERGACPDMKDRRGRTA 718
Cdd:cd22192 95 IAVVNQNLNLVRELI--ARGADVVSprATGTffrpgpknliyYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTV 172
|
..
gi 66392221 719 LH 720
Cdd:cd22192 173 LH 174
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
787-978 |
3.06e-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: 3.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 787 TPAHWAAYHGHEDCLEVLLELKPCSIQEGNPF--TPLHCALINGHSGSAELLLESSvcNSLVNIRDA----KGRTPLHAA 860
Cdd:cd22192 19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALgeTALHVAALYDNLEAAVVLMEAA--PELVNEPMTsdlyQGETALHIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 861 AVAEDVAGLQLVLRQGADI--------------DAVDHSGRSALMVAADYGQSGAVALLLHRAkADLSLLDVNKNTALHL 926
Cdd:cd22192 97 VVNQNLNLVRELIARGADVvspratgtffrpgpKNLIYYGEHPLSFAACVGNEEIVRLLIEHG-ADIRAQDSLGNTVLHI 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 66392221 927 ACSKAHE--MCAM--LIL---KEIHNPILINATNSMLQMPLHIAARNGLATVVQALLNR 978
Cdd:cd22192 176 LVLQPNKtfACQMydLILsydKEDDLQPLDLVPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
325-493 |
3.82e-07 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 53.90 E-value: 3.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 325 LIQNGGEIDCVDRYGNTPLHVAAKYGHELLISTLMTNGADTARQGIHGMFPLH--------------LAVLYGS------ 384
Cdd:PHA02946 58 LLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYylsgtddevierinLLVQYGAkinnsv 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 385 -SDCCRKLLSSGQLYSIVLsmskEHVLSAGFDINTPDNFGRTCLHAAASGGN--IECLNLLLSSGADMNKKDKFGRTPLH 461
Cdd:PHA02946 138 dEEGCGPLLACTDPSERVF----KKIMSIGFEARIVDKFGKNHIHRHLMSDNpkASTISWMMKLGISPSKPDHDGNTPLH 213
|
170 180 190
....*....|....*....|....*....|...
gi 66392221 462 YAAANGRYQC-VVVLVGAGAEVNERDRSGCTPL 493
Cdd:PHA02946 214 IVCSKTVKNVdIINLLLPSTDVNKQNKFGDSPL 246
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
189-258 |
3.83e-07 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 54.13 E-value: 3.83e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 189 VKLLVSQGSDKSCKDKRGYTPLHAAAASGHVDVVKYLLRNGAEIDEPNAFGNTALHVACYTGQEAVANEL 258
Cdd:PTZ00322 98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
277-359 |
4.14e-07 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 54.13 E-value: 4.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 277 HLAAvsTNGALCLELLVNNGADVNMQSKEGKSPLHMAAIHGRFTRSQILIQNGGEIDCVDRYGNTPLHVAAKYGHELLIS 356
Cdd:PTZ00322 88 QLAA--SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165
|
...
gi 66392221 357 TLM 359
Cdd:PTZ00322 166 LLS 168
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
186-450 |
5.15e-07 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 53.69 E-value: 5.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 186 LEVVKLLVSQGSDKSCKDKRGYTPLHAAAAS-----GHVDVVKYLLRNGAEIDEPNAFGNTALHvaCYTGQEAVANE--- 257
Cdd:PHA02798 51 TDIVKLFINLGANVNGLDNEYSTPLCTILSNikdykHMLDIVKILIENGADINKKNSDGETPLY--CLLSNGYINNLeil 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 258 --LVNRGANVNQPNHRGYTPLHLAAVSTNGAL--CLELLVNNGADVNMQS-KEGKSPLHmAAIHGRFTR-----SQILIQ 327
Cdd:PHA02798 129 lfMIENGADTTLLDKDGFTMLQVYLQSNHHIDieIIKLLLEKGVDINTHNnKEKYDTLH-CYFKYNIDRidadiLKLFVD 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 328 NGGEIDCVDRYGNTPLhvaakygHELLISTLMTNGA-------------DTARQGIHGMFPLHLAVLYGSSDCCrkllss 394
Cdd:PHA02798 208 NGFIINKENKSHKKKF-------MEYLNSLLYDNKRfkknildfifsyiDINQVDELGFNPLYYSVSHNNRKIF------ 274
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 66392221 395 gqlysivlsmskEHVLSAGFDINTPDNFGRTCLHAAASGGNIECLNLLLSSGADMN 450
Cdd:PHA02798 275 ------------EYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNKKPNKN 318
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
41-94 |
5.20e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 47.27 E-value: 5.20e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 66392221 41 RRTPLHAAAWLGDVHIMDLLISAGANVNAKDHVWLTPLHRAAASRNERAVGLLL 94
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
456-498 |
6.14e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 47.27 E-value: 6.14e-07
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 66392221 456 GRTPLHYAAANGRYQCVVVLVGAGAEVNERDRSGCTPLHYSAA 498
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAAS 43
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
230-350 |
6.55e-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: 6.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 230 AEIDEPNAFGNTALHVACYTGQEAVANELVNRGANVN--------QPNHR------GYTPLHLAAVsTNGALCLELLVNN 295
Cdd:cd22194 132 AEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNahakgvffNPKYKhegfyfGETPLALAAC-TNQPEIVQLLMEK 210
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66392221 296 GAD-VNMQSKEGKSPLH---MAA----IHGRFTR---SQILIQNGGE-IDCV-DRYGNTPLHVAAKYG 350
Cdd:cd22194 211 ESTdITSQDSRGNTVLHalvTVAedskTQNDFVKrmyDMILLKSENKnLETIrNNEGLTPLQLAAKMG 278
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
684-735 |
7.25e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 46.88 E-value: 7.25e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 66392221 684 TPLMLAVLGGHTDCVHLLLERGACPDMKDRRGRTALHRGAVMGREDCLTALL 735
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
842-1006 |
7.41e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 53.04 E-value: 7.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 842 CNSLVNIRDAKGRTPLHAAAVAEDVAGLQLVLRQGADIDAVDHSGRSALMVAADYGQSGAVALLLHRAkADLSLLDVNKN 921
Cdd:PHA02874 113 CGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKG-AYANVKDNNGE 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 922 TALHLACSKAHEMCAMLILKEIHNpILINATNSMlqMPLHIAARNGlATVVQALLNrGATVLAVDEEGHTP---ALACAS 998
Cdd:PHA02874 192 SPLHNAAEYGDYACIKLLIDHGNH-IMNKCKNGF--TPLHNAIIHN-RSAIELLIN-NASINDQDIDGSTPlhhAINPPC 266
|
....*...
gi 66392221 999 NKAVADCL 1006
Cdd:PHA02874 267 DIDIIDIL 274
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
323-488 |
7.86e-07 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 52.91 E-value: 7.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 323 QILIQNGGEIDCVDRYGNTPLHVA----AKYGHEL-LISTLMTNGADTARQGIHGMFPLhlavlygssdCCrkLLSSGQL 397
Cdd:PHA02798 55 KLFINLGANVNGLDNEYSTPLCTIlsniKDYKHMLdIVKILIENGADINKKNSDGETPL----------YC--LLSNGYI 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 398 YS--IVLSMskehvLSAGFDINTPDNFGRTCLHAAASGGN---IECLNLLLSSGADMNK-KDKFGRTPLH-YAAANgrYQ 470
Cdd:PHA02798 123 NNleILLFM-----IENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINThNNKEKYDTLHcYFKYN--ID 195
|
170 180
....*....|....*....|...
gi 66392221 471 CVVV-----LVGAGAEVNERDRS 488
Cdd:PHA02798 196 RIDAdilklFVDNGFIINKENKS 218
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
308-358 |
8.57e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 46.88 E-value: 8.57e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 66392221 308 SPLHMAAIHGRFTRSQILIQNGGEIDCVDRYGNTPLHVAAKYGHELLISTL 358
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
447-495 |
9.01e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 46.96 E-value: 9.01e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 66392221 447 ADMNKKDKFGRTPLHYAAANGRYQCVVVLVGAGAEVNERDRSGCTPLHY 495
Cdd:pfam13857 7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
650-806 |
1.10e-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: 52.57 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 650 LHVAAAN---GHSECLRMLL----CSEGGADLVN--VTDA--EGQTPLMLAVLGGHTDCVHLLLERG------ACPDMKD 712
Cdd:cd21882 30 LHKAALNlndGVNEAIMLLLeaapDSGNPKELVNapCTDEfyQGQTALHIAIENRNLNLVRLLVENGadvsarATGRFFR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 713 RRGRTALHRG-------AVMGREDCLTALLSHN---VSVLSRDFQGRSALHL------------AASCGHADILSNLLSA 770
Cdd:cd21882 110 KSPGNLFYFGelplslaACTNQEEIVRLLLENGaqpAALEAQDSLGNTVLHAlvlqadntpensAFVCQMYNLLLSYGAH 189
|
170 180 190
....*....|....*....|....*....|....*.
gi 66392221 771 ADHSQPQDPLTDRHGYTPAHWAAYHGHEDCLEVLLE 806
Cdd:cd21882 190 LDPTQQLEEIPNHQGLTPLKLAAVEGKIVMFQHILQ 225
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
52-129 |
1.29e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 52.59 E-value: 1.29e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66392221 52 GDVHIMDLLISAGANVNAKDHVWLTPLHRAAASRNERAVGLLLRKGADVTARDKYWQTPLHIAAANRATRCVETLLPH 129
Cdd:PTZ00322 93 GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
606-707 |
1.49e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 52.21 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 606 DVCDPVGRSVLYLA----SQRGHSRCVELLLSQSASCLLAEHRSKwGPLHVAAANGHSECLRMLLcsEGGADlVNVTDAE 681
Cdd:PTZ00322 72 EVIDPVVAHMLTVElcqlAASGDAVGARILLTGGADPNCRDYDGR-TPLHIACANGHVQVVRVLL--EFGAD-PTLLDKD 147
|
90 100
....*....|....*....|....*.
gi 66392221 682 GQTPLMLAVLGGHTDCVHLLLERGAC 707
Cdd:PTZ00322 148 GKTPLELAEENGFREVVQLLSRHSQC 173
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
816-987 |
1.55e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 51.97 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 816 NPFTPLHCALINgHSGSAEL--LLESSVCNslVNIRDAKGRTPLHAAA--VAEDVAGLQLVLRQGADIDAVDHsgrsalm 891
Cdd:PHA03100 105 NGITPLLYAISK-KSNSYSIveYLLDNGAN--VNIKNSDGENLLHLYLesNKIDLKILKLLIDKGVDINAKNR------- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 892 vaadygqsgaVALLLhRAKADLSLLDVNKNTALHLACSKAHEMCAMLILKEIHNPiliNATNSMLQMPLHIAARNGLATV 971
Cdd:PHA03100 175 ----------VNYLL-SYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANP---NLVNKYGDTPLHIAILNNNKEI 240
|
170
....*....|....*.
gi 66392221 972 VQALLNRGATVLAVDE 987
Cdd:PHA03100 241 FKLLLNNGPSIKTIIE 256
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
581-632 |
1.70e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 46.11 E-value: 1.70e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 66392221 581 SPLHLAVESGHWECVTVLIESGVCVDVCDPVGRSVLYLASQRGHSRCVELLL 632
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
332-568 |
1.71e-06 |
|
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: 52.01 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 332 IDCVDRYGNTPLHVAAKYG-HELLISTLMTNGadtaRQGIHGMFPLHLAVLyGSSDCCRKLLSSgQLYSIVLSMSKEHVL 410
Cdd:TIGR00870 45 INCPDRLGRSALFVAAIENeNLELTELLLNLS----CRGAVGDTLLHAISL-EYVDAVEAILLH-LLAAFRKSGPLELAN 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 411 SAGFDINTPDnfgRTCLHAAASGGNIECLNLLLSSGADMNKKDK--------------FGRTPLHYAAANGRYQCVVVLV 476
Cdd:TIGR00870 119 DQYTSEFTPG---ITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLS 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 477 GAGAEVNERDRSGCTPLHYSAASTAFcrtdrphasthqnQEDGEKESFLCVEHLLDNGADPC-------LCNTKGYSAVH 549
Cdd:TIGR00870 196 EDPADILTADSLGNTLLHLLVMENEF-------------KAEYEELSCQMYNFALSLLDKLRdskelevILNHQGLTPLK 262
|
250
....*....|....*....
gi 66392221 550 YAAAHGNKQNLELLLEMCF 568
Cdd:TIGR00870 263 LAAKEGRIVLFRLKLAIKY 281
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
586-770 |
1.79e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 51.53 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 586 AVESGHWECVTVLIESGVCVDVCDPVGRSVLYLASQRGHSRCVELLLSQSA--SCLLAEHRSkwgPLHVAAANGHSECLR 663
Cdd:PHA02875 9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAipDVKYPDIES---ELHDAVEEGDVKAVE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 664 MLLCSEGGADlvNVTDAEGQTPLMLAVLGGHTDCVHLLLERGACPDMKDRRGRTALHRGAVMGREDCLTALLSHNVSVLS 743
Cdd:PHA02875 86 ELLDLGKFAD--DVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDI 163
|
170 180
....*....|....*....|....*..
gi 66392221 744 RDFQGRSALHLAASCGHADILSNLLSA 770
Cdd:PHA02875 164 EDCCGCTPLIIAMAKGDIAICKMLLDS 190
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
415-463 |
2.04e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 45.80 E-value: 2.04e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 66392221 415 DINTPDNFGRTCLHAAASGGNIECLNLLLSSGADMNKKDKFGRTPLHYA 463
Cdd:pfam13857 8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
409-489 |
2.19e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 51.82 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 409 VLSAGFDINTPDNFGRTCLHAAASGGNIECLNLLLSSGADMNKKDKFGRTPLHYAAANGRYQCVVVLVGAGAEVNERDRS 488
Cdd:PTZ00322 101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGAN 180
|
.
gi 66392221 489 G 489
Cdd:PTZ00322 181 A 181
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
527-688 |
2.51e-06 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 51.79 E-value: 2.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 527 VEHLLDNGADPCLCNTKGYSAVHYAAAHGNKQNLELLLEMCFNtLGDKESNGSiSPLHLAVESGHWECVTVLIEsgvCVD 606
Cdd:PLN03192 541 LEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACN-VHIRDANGN-TALWNAISAKHHKIFRILYH---FAS 615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 607 VCDP-VGRSVLYLASQRGHSRCVELLLSQSAScLLAEHRSKWGPLHVAAANGHSECLRMLLCSegGADLVNVTDAEGQTP 685
Cdd:PLN03192 616 ISDPhAAGDLLCTAAKRNDLTAMKELLKQGLN-VDSEDHQGATALQVAMAEDHVDMVRLLIMN--GADVDKANTDDDFSP 692
|
...
gi 66392221 686 LML 688
Cdd:PLN03192 693 TEL 695
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
92-147 |
2.55e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 45.42 E-value: 2.55e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 66392221 92 LLLRKGADVTARDKYWQTPLHIAAANRATRCVETLLPHVSSLNMADRTGRAPLHHA 147
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
407-493 |
2.73e-06 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 51.21 E-value: 2.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 407 EHVLSAGFDINTPDNFGRTCLHAAASGGNIECLNLLLSSGADMNKKDKFGRTPLHYAAANGR--YQCVVVLVGAGAEVNE 484
Cdd:PHA02946 56 EELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAKINN 135
|
90
....*....|
gi 66392221 485 R-DRSGCTPL 493
Cdd:PHA02946 136 SvDEEGCGPL 145
|
|
| TRPV1 |
cd22196 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ... |
172-280 |
2.96e-06 |
|
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: 51.35 E-value: 2.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 172 KDRQPIHWAAYLGHLEVVKLLVSQGSD----------KSCKDKRGY----TPLHAAAASGHVDVVKYLLRN---GAEIDE 234
Cdd:cd22196 93 KGQTALHIAIERRNMHLVELLVQNGADvharasgeffKKKKGGPGFyfgeLPLSLAACTNQLDIVKFLLENphsPADISA 172
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66392221 235 PNAFGNTALH----VACYTGQEA-----VANELVNRGANVNQ-------PNHRGYTPLHLAA 280
Cdd:cd22196 173 RDSMGNTVLHalveVADNTPENTkfvtkMYNEILILGAKIRPllkleeiTNKKGLTPLKLAA 234
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
43-186 |
3.36e-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: 3.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 43 TPLHAAAWLGDVHIMDLLISAGANVNAK------------------DHvwltPLHRAAASRNERAVGLLLRKGADVTARD 104
Cdd:cd22192 91 TALHIAVVNQNLNLVRELIARGADVVSPratgtffrpgpknliyygEH----PLSFAACVGNEEIVRLLIEHGADIRAQD 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 105 KYWQTPLHI----AAANRATRCVETLLPHVSSLN------MADRTGRAPLHHAAQSGYQEMVKLLLNKganlsasdkkdR 174
Cdd:cd22192 167 SLGNTVLHIlvlqPNKTFACQMYDLILSYDKEDDlqpldlVPNNQGLTPFKLAAKEGNIVMFQHLVQK-----------R 235
|
170
....*....|..
gi 66392221 175 QPIHWAayLGHL 186
Cdd:cd22192 236 RHIQWT--YGPL 245
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
202-246 |
3.89e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 45.03 E-value: 3.89e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 66392221 202 KDKRGYTPLHAAAASGHVDVVKYLLRNGAEIDEPNAFGNTALHVA 246
Cdd:pfam13857 12 LDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
258-313 |
4.08e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 45.03 E-value: 4.08e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 66392221 258 LVNRGANVNQPNHRGYTPLHLAAvSTNGALCLELLVNNGADVNMQSKEGKSPLHMA 313
Cdd:pfam13857 2 LEHGPIDLNRLDGEGYTPLHVAA-KYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| TRPV2 |
cd22197 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ... |
140-280 |
4.17e-06 |
|
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: 51.01 E-value: 4.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 140 GRAPLHHAAQSGYQEMVKLLLNKGANLSASDKKD--RQPIHWAAYLGHLevvkllvsqgsdksckdkrgytPLHAAAASG 217
Cdd:cd22197 94 GHSALHIAIEKRSLQCVKLLVENGADVHARACGRffQKKQGTCFYFGEL----------------------PLSLAACTK 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 218 HVDVVKYLLRNG---AEIDEPNAFGNTALHVACYTGQEAVAN---------ELVNRGANVNQ-------PNHRGYTPLHL 278
Cdd:cd22197 152 QWDVVNYLLENPhqpASLQAQDSLGNTVLHALVMIADNSPENsalvikmydGLLQAGARLCPtvqleeiSNHEGLTPLKL 231
|
..
gi 66392221 279 AA 280
Cdd:cd22197 232 AA 233
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
715-768 |
4.46e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 44.96 E-value: 4.46e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 66392221 715 GRTALHRGAVMGREDCLTALLSHNVSVLSRDFQGRSALHLAASCGHADILSNLL 768
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02884 |
PHA02884 |
ankyrin repeat protein; Provisional |
56-195 |
5.87e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165212 [Multi-domain] Cd Length: 300 Bit Score: 49.60 E-value: 5.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 56 IMDLLISAGANVNAK----DHVWLTPLHRAAASRNERAVGLLLRKGADVTARDKYWQ-TPLHIAAANRATRCVETLLPHV 130
Cdd:PHA02884 48 IIDAILKLGADPEAPfplsENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKiTPLYISVLHGCLKCLEILLSYG 127
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66392221 131 SSLNMADRTGRAPLHHAAQSGYQEMVKLLlnKGANLSASDKkdrqpiHWAAYLGHLEVVKLLVSQ 195
Cdd:PHA02884 128 ADINIQTNDMVTPIELALMICNNFLAFMI--CDNEISNFYK------HPKKILINFDILKILVSH 184
|
|
| PHA02716 |
PHA02716 |
CPXV016; CPX019; EVM010; Provisional |
45-276 |
6.48e-06 |
|
CPXV016; CPX019; EVM010; Provisional
Pssm-ID: 165089 [Multi-domain] Cd Length: 764 Bit Score: 50.30 E-value: 6.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 45 LHAaaWLG----DVHIMDLLISAGANVNAKDHVWLTPLHRAAASRNERAVGL--LLRKGADVTARDKYWQTPLHIAAANR 118
Cdd:PHA02716 181 LHA--YLGnmyvDIDILEWLCNNGVNVNLQNNHLITPLHTYLITGNVCASVIkkIIELGGDMDMKCVNGMSPIMTYIINI 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 119 ATRCVETLLPHVSSLNmADRTGRAPlhhaaqsgyqEMVKLLLNKGANLSASdkkdrqpihwaaylghleVVKLLVSQGSD 198
Cdd:PHA02716 259 DNINPEITNIYIESLD-GNKVKNIP----------MILHSYITLARNIDIS------------------VVYSFLQPGVK 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 199 KSCKDKRGYTPLHAAAASGHV--DVVKYLLRNGAEIDEPNAFGNTALHVacYTGQEAVANE----------------LVN 260
Cdd:PHA02716 310 LHYKDSAGRTCLHQYILRHNIstDIIKLLHEYGNDLNEPDNIGNTVLHT--YLSMLSVVNIldpetdndirldviqcLIS 387
|
250
....*....|....*.
gi 66392221 261 RGANVNQPNHRGYTPL 276
Cdd:PHA02716 388 LGADITAVNCLGYTPL 403
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
734-988 |
6.75e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 50.06 E-value: 6.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 734 LLSHNVSVLSRDFQGRSALHLAASCGHADILSNLLS-AADHSqpqdpLTDRHGYTPAHWAAYHGHEDCLEVLLELKpcSI 812
Cdd:PHA02876 164 LLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSyGADVN-----IIALDDLSVLECAVDSKNIDTIKAIIDNR--SN 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 813 QEGNPFTPLHcALINGHSGSAELLLESSVCnslVNIRDAKGRTPLHAAAVAEDVAGL-QLVLRQGADIDAVDHSGRSALM 891
Cdd:PHA02876 237 INKNDLSLLK-AIRNEDLETSLLLYDAGFS---VNSIDDCKNTPLHHASQAPSLSRLvPKLLERGADVNAKNIKGETPLY 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 892 VAADYGQSGAVALLLHRAKADLSLLDVNKNTALHLACSKAHEMCAMLILKEIHNPIliNATNSMLQMPLHIAARNGLATV 971
Cdd:PHA02876 313 LMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKDIVITLLELGANV--NARDYCDKTPIHYAAVRNNVVI 390
|
250
....*....|....*..
gi 66392221 972 VQALLNRGATVLAVDEE 988
Cdd:PHA02876 391 INTLLDYGADIEALSQK 407
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
669-720 |
6.81e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 44.26 E-value: 6.81e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 66392221 669 EGGADLVNVTDAEGQTPLMLAVLGGHTDCVHLLLERGACPDMKDRRGRTALH 720
Cdd:pfam13857 3 EHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
278-451 |
7.33e-06 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 50.25 E-value: 7.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 278 LAAVSTNGALCLELLVNNGADVNMQSKEGKSPLHMAAIHGRFTRSQILIQNGGEIDCVDRYGNTPLHVAAKYGHELLIST 357
Cdd:PLN03192 530 LTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRI 609
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 358 LMtngadtarqgihgmfplHLAVL---YGSSDCCRKLLSSGQLysivlSMSKEhVLSAGFDINTPDNFGRTCLHAAASGG 434
Cdd:PLN03192 610 LY-----------------HFASIsdpHAAGDLLCTAAKRNDL-----TAMKE-LLKQGLNVDSEDHQGATALQVAMAED 666
|
170
....*....|....*..
gi 66392221 435 NIECLNLLLSSGADMNK 451
Cdd:PLN03192 667 HVDMVRLLIMNGADVDK 683
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
205-234 |
9.55e-06 |
|
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: 43.35 E-value: 9.55e-06
10 20 30
....*....|....*....|....*....|
gi 66392221 205 RGYTPLHAAAASGHVDVVKYLLRNGAEIDE 234
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
272-326 |
9.77e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 43.80 E-value: 9.77e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 66392221 272 GYTPLHLAAVSTNGAlCLELLVNNGADVNMQSKEGKSPLHMAAIHGRFTRSQILI 326
Cdd:pfam13637 1 ELTALHAAAASGHLE-LLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
846-992 |
1.26e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 49.11 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 846 VNIRDA-KGRTPLHAAAVAEDVAGLQLVLRQGADIDAVDHSGRSALMVAADYGQSGAVALLLhRAKADLSLLDVNKNTAL 924
Cdd:PHA02878 160 INMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILL-ENGASTDARDKCGNTPL 238
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66392221 925 HLACSKAHEMCAMLILKEihNPILINATNSMLQM-PLHIAARNglATVVQALLNRGATVLAVDEEGHTP 992
Cdd:PHA02878 239 HISVGYCKDYDILKLLLE--HGVDVNAKSYILGLtALHSSIKS--ERKLKLLLEYGADINSLNSYKLTP 303
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
291-346 |
1.44e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 43.49 E-value: 1.44e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 66392221 291 LLVNNGADVNMQSKEGKSPLHMAAIHGRFTRSQILIQNGGEIDCVDRYGNTPLHVA 346
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| TRPV1-4 |
cd22193 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ... |
186-280 |
1.70e-05 |
|
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: 49.02 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 186 LEVVKLLVSQGSD---KSC------KDKRGY-----TPLHAAAASGHVDVVKYLLRNG---AEIDEPNAFGNTALHVACY 248
Cdd:cd22193 89 GDIVALLVENGADvhaHAKgrffqpKYQGEGfyfgeLPLSLAACTNQPDIVQYLLENEhqpADIEAQDSRGNTVLHALVT 168
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 66392221 249 TGQEAVAN---------ELVNRGANVNQP-------NHRGYTPLHLAA 280
Cdd:cd22193 169 VADNTKENtkfvtrmydMILIRGAKLCPTveleeirNNDGLTPLQLAA 216
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
24-243 |
1.75e-05 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 48.51 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 24 VKLFLHKKDEVNALDQERRTPLHAAAWLGDVHIMDLLISAGANVNAKDHVWLTPLHRAAASRNE--RAVGLLLRKGADV- 100
Cdd:PHA02946 55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEviERINLLVQYGAKIn 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 101 TARDKYWQTPLhIAAANRATRCVETLLPHVSSLNMADRTGRAPLHHAAQsgyqemvklllnkganlsaSDKKDRQPIHWa 180
Cdd:PHA02946 135 NSVDEEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLM-------------------SDNPKASTISW- 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66392221 181 aylghlevvklLVSQGSDKSCKDKRGYTPLHAAAAS--GHVDVVKYLLRNgAEIDEPNAFGNTAL 243
Cdd:PHA02946 194 -----------MMKLGISPSKPDHDGNTPLHIVCSKtvKNVDIINLLLPS-TDVNKQNKFGDSPL 246
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
375-443 |
1.80e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 43.03 E-value: 1.80e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66392221 375 PLHLAVLYGSSDCCRKLLSSGqlysivlsmskehvlsagFDINTPDNFGRTCLHAAASGGNIECLNLLL 443
Cdd:pfam13637 4 ALHAAAASGHLELLRLLLEKG------------------ADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
944-992 |
1.89e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 43.10 E-value: 1.89e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 66392221 944 HNPILINATNSMLQMPLHIAARNGLATVVQALLNRGATVLAVDEEGHTP 992
Cdd:pfam13857 4 HGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTA 52
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
859-1010 |
2.07e-05 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 48.71 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 859 AAAVAEDVAGLQLVLRQGADIDAVDHSGRSALMVAADYGQSGAVALLLHRAkADLSLLDVNKNTALHLACSKAHEMCAML 938
Cdd:PLN03192 531 TVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHA-CNVHIRDANGNTALWNAISAKHHKIFRI 609
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66392221 939 I--LKEIHNPiliNATNSMLQMplhiAARNGLATVVQALLNRGATVLAVDEEGHTpALACASNKAVADCLALIL 1010
Cdd:PLN03192 610 LyhFASISDP---HAAGDLLCT----AAKRNDLTAMKELLKQGLNVDSEDHQGAT-ALQVAMAEDHVDMVRLLI 675
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
109-160 |
2.44e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 42.65 E-value: 2.44e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 66392221 109 TPLHIAAANRATRCVETLLPHVSSLNMADRTGRAPLHHAAQSGYQEMVKLLL 160
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
158-213 |
2.59e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 42.72 E-value: 2.59e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 66392221 158 LLLNKGANLSASDKKDRQPIHWAAYLGHLEVVKLLVSQGSDKSCKDKRGYTPLHAA 213
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
205-236 |
2.90e-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: 41.89 E-value: 2.90e-05
10 20 30
....*....|....*....|....*....|...
gi 66392221 205 RGYTPLHAAAAS-GHVDVVKYLLRNGAEIDEPN 236
Cdd:pfam00023 1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
339-392 |
3.15e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 42.26 E-value: 3.15e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 66392221 339 GNTPLHVAAKYGHELLISTLMTNGADTARQGIHGMFPLHLAVLYGSSDCCRKLL 392
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
819-992 |
3.22e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 47.65 E-value: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 819 TPLHCALINGHSGSAELLLESsvcNSLVNIRDAKGRTPLHAAAVAEDVAGLQLVLRQGADIDAVDHSGRSALMVAADYGQ 898
Cdd:PHA02874 126 TFLHYAIKKGDLESIKMLFEY---GADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGD 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 899 SGAVALLLHRAkADLSLLDVNKNTALHLACSKAHEMCAMLIlkeihNPILINATNSMLQMPLHIAARNGLAT-VVQALLN 977
Cdd:PHA02874 203 YACIKLLIDHG-NHIMNKCKNGFTPLHNAIIHNRSAIELLI-----NNASINDQDIDGSTPLHHAINPPCDIdIIDILLY 276
|
170
....*....|....*
gi 66392221 978 RGATVLAVDEEGHTP 992
Cdd:PHA02874 277 HKADISIKDNKGENP 291
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
173-443 |
3.31e-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: 48.15 E-value: 3.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 173 DRQPIHWAAYlGHLEVVK--LLVSQGSDKSCKDKRGYTPLHAAAASG-HVDVVKYLLRNGAEIDEpnafGNTALHVACYT 249
Cdd:TIGR00870 18 EKAFLPAAER-GDLASVYrdLEEPKKLNINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGAV----GDTLLHAISLE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 250 GQEAVaNELvnrgANVNQPNHRGYTPLHLAavstngalclellvnngadvNMQSK----EGKSPLHMAAIHGRFTRSQIL 325
Cdd:TIGR00870 93 YVDAV-EAI----LLHLLAAFRKSGPLELA--------------------NDQYTseftPGITALHLAAHRQNYEIVKLL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 326 IQNGGEI-------DCVD-------RYGNTPLHVAAKYGHELLISTLMTNGADTARQGIHGMFPLHLAVLYGSSDCCRKL 391
Cdd:TIGR00870 148 LERGASVparacgdFFVKsqgvdsfYHGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVMENEFKAEYEE 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66392221 392 LSSgQLYSIVL--------SMSKEHVLsagfdintpdNF-GRTCLHAAASGGNIECLNLLL 443
Cdd:TIGR00870 228 LSC-QMYNFALslldklrdSKELEVIL----------NHqGLTPLKLAAKEGRIVLFRLKL 277
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
205-234 |
3.60e-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.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 41.47 E-value: 3.60e-05
10 20 30
....*....|....*....|....*....|
gi 66392221 205 RGYTPLHAAAASGHVDVVKYLLRNGAEIDE 234
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
888-982 |
3.88e-05 |
|
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: 47.70 E-value: 3.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 888 SALMVAADYGQSGAVALLLHRAKADLSLLDVNKNTALHLACSKAHEMCAMLILKEIhnPILIN--ATNSMLQ--MPLHIA 963
Cdd:cd22192 19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAA--PELVNepMTSDLYQgeTALHIA 96
|
90
....*....|....*....
gi 66392221 964 ARNGLATVVQALLNRGATV 982
Cdd:cd22192 97 VVNQNLNLVRELIARGADV 115
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
861-927 |
5.56e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 47.20 E-value: 5.56e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66392221 861 AVAEDVAGLQLVLRQGADIDAVDHSGRSALMVAADYGQSGAVALLLHRAkADLSLLDVNKNTALHLA 927
Cdd:PTZ00322 90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFG-ADPTLLDKDGKTPLELA 155
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
271-304 |
6.62e-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: 6.62e-05
10 20 30
....*....|....*....|....*....|....
gi 66392221 271 RGYTPLHLAAVSTNGALCLELLVNNGADVNMQSK 304
Cdd:pfam00023 1 DGNTPLHLAAGRRGNLEIVKLLLSKGADVNARDK 34
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
112-206 |
7.43e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 46.82 E-value: 7.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 112 HIAAANRATRcVETLLPHVSSLNMADRTGRAPLHHAAQSGYQEMVKLLLNKGANLSASDKKDRQPIHWAAYLGHLEVVKL 191
Cdd:PTZ00322 88 QLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166
|
90
....*....|....*
gi 66392221 192 LVSQGSDKSCKDKRG 206
Cdd:PTZ00322 167 LSRHSQCHFELGANA 181
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
423-451 |
7.72e-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: 40.65 E-value: 7.72e-05
10 20
....*....|....*....|....*....
gi 66392221 423 GRTCLHAAASGGNIECLNLLLSSGADMNK 451
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
311-399 |
8.37e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 46.82 E-value: 8.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 311 HMAAiHGRFTRSQILIQNGGEIDCVDRYGNTPLHVAAKYGHELLISTLMTNGADTARQGIHGMFPLHLAVLYGSSDCCRK 390
Cdd:PTZ00322 88 QLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166
|
....*....
gi 66392221 391 LLSSGQLYS 399
Cdd:PTZ00322 167 LSRHSQCHF 175
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
237-443 |
1.17e-04 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).
Pssm-ID: 411975 [Multi-domain] Cd Length: 600 Bit Score: 46.03 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 237 AFGNTALHVACYTGQEA----------VANELVNRGANVNQPN----HRGYTPLHLAAVSTNgALCLELLVNNGADVnmq 302
Cdd:cd21882 24 ATGKTCLHKAALNLNDGvneaimllleAAPDSGNPKELVNAPCtdefYQGQTALHIAIENRN-LNLVRLLVENGADV--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 303 skegksplHMAAIHGRFTRSQIliqnggeiDCVdRYGNTPLHVAAKYGHELLISTLMTNGADTA---RQGIHGMFPLHLA 379
Cdd:cd21882 100 --------SARATGRFFRKSPG--------NLF-YFGELPLSLAACTNQEEIVRLLLENGAQPAaleAQDSLGNTVLHAL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66392221 380 VLYGSSDCCRKLLSSgQLYSIVLSMSKEHVLSAGFDInTPDNFGRTCLHAAASGGNIECLNLLL 443
Cdd:cd21882 163 VLQADNTPENSAFVC-QMYNLLLSYGAHLDPTQQLEE-IPNHQGLTPLKLAAVEGKIVMFQHIL 224
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
430-565 |
1.24e-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: 46.16 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 430 AASGGNIECLN-LLLSSGADMNKKDKFGRTPLHYAAANGRYQCVVVLVGAGAE-VNERDRS----GCTPLHYSAAstafc 503
Cdd:cd22192 24 AAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEPMTSdlyqGETALHIAVV----- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 504 rtdrphasthqnqedgeKESFLCVEHLLDNGADP---------------CLCntkgYSAVH---YAAAHGNKQNLELLLE 565
Cdd:cd22192 99 -----------------NQNLNLVRELIARGADVvspratgtffrpgpkNLI----YYGEHplsFAACVGNEEIVRLLIE 157
|
|
| PHA02791 |
PHA02791 |
ankyrin-like protein; Provisional |
136-227 |
1.36e-04 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165154 [Multi-domain] Cd Length: 284 Bit Score: 45.03 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 136 ADRTGRAPLHHAAQSGYQEMVKLLLNKGA--NLSasdkKDRQPIHWAAYLGHLEVVKLLVSQGSDKSCKDKRGYTPLHAA 213
Cdd:PHA02791 26 ADVHGHSALYYAIADNNVRLVCTLLNAGAlkNLL----ENEFPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYA 101
|
90
....*....|....
gi 66392221 214 AASGHVDVVKYLLR 227
Cdd:PHA02791 102 VDSGNMQTVKLFVK 115
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
664-999 |
1.40e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 45.82 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 664 MLLcsEGGADlVNVTDAEGQTPLMLAVLGGHTDCVHLLLERGACPDMKDRRGRTALHRGAVMGREDCLTALLSHNVSVLS 743
Cdd:PHA02876 163 MLL--EGGAD-VNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINK 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 744 RDfqgrsaLHLAASCGHADILSNLLsAADHSQPQDPLtDRHGYTPAHWAAYhghedclevllelkpcsiqegnpfTPLHC 823
Cdd:PHA02876 240 ND------LSLLKAIRNEDLETSLL-LYDAGFSVNSI-DDCKNTPLHHASQ------------------------APSLS 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 824 ALINGhsgsaelLLESSVCnslVNIRDAKGRTPLH-AAAVAEDVAGLQLVLRQGADIDAVDHSGRSALMVAADYGQSGAV 902
Cdd:PHA02876 288 RLVPK-------LLERGAD---VNAKNIKGETPLYlMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKDI 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 903 ALLLHRAKADLSLLDVNKNTALHLACSKAHEMcamlilkeIHNPIL-----INATNSMLQMPLHIA-ARNGLATVVQALL 976
Cdd:PHA02876 358 VITLLELGANVNARDYCDKTPIHYAAVRNNVV--------IINTLLdygadIEALSQKIGTALHFAlCGTNPYMSVKTLI 429
|
330 340
....*....|....*....|....
gi 66392221 977 NRGATVLAVDEEGHTPA-LACASN 999
Cdd:PHA02876 430 DRGANVNSKNKDLSTPLhYACKKN 453
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
609-741 |
1.51e-04 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 46.01 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 609 DPVGRSVLYLASQRGHSRCVELLLSQSASCLLAEHRSKwGPLHVAAANGHSECLRMLL---CSeggadlVNVTDAEGQTP 685
Cdd:PLN03192 522 DPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGR-TPLHIAASKGYEDCVLVLLkhaCN------VHIRDANGNTA 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 686 LMLAVLGGHTD-------CVHL------------------------LLERGACPDMKDRRGRTALHRGAVMGREDCLTAL 734
Cdd:PLN03192 595 LWNAISAKHHKifrilyhFASIsdphaagdllctaakrndltamkeLLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLL 674
|
....*..
gi 66392221 735 LSHNVSV 741
Cdd:PLN03192 675 IMNGADV 681
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
816-1011 |
1.66e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 45.37 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 816 NPFTPLHCALINGHSGSAELLLESsvcNSLVNIRDAKGRTPLHAAAVAEDVAGLQLVLRQGADIDAVDHS-GRSALMVAA 894
Cdd:PHA02875 34 DGISPIKLAMKFRDSEAIKLLMKH---GAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKdGMTPLHLAT 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 895 DYGQSGAVALLLHRaKADLSLLDVNKNTALHLAC-SKAHEMCAMLIlkeIHNPILiNATNSMLQMPLHIAARNGLATVVQ 973
Cdd:PHA02875 111 ILKKLDIMKLLIAR-GADPDIPNTDKFSPLHLAVmMGDIKGIELLI---DHKACL-DIEDCCGCTPLIIAMAKGDIAICK 185
|
170 180 190
....*....|....*....|....*....|....*...
gi 66392221 974 ALLNRGATVLAVDEEGHTPALACASNKAVADCLALILS 1011
Cdd:PHA02875 186 MLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIK 223
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
56-248 |
1.81e-04 |
|
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: 45.52 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 56 IMDLLISAgaNVNAKDHVWLTPLHRAAASRNERAVGLLLRKGADVTARDK--------------YWQTPLHIAAANRATR 121
Cdd:cd22194 125 ILDRFINA--EYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKgvffnpkykhegfyFGETPLALAACTNQPE 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 122 CVETLLPHVSS-LNMADRTGRAPLHH----AAQSGYQ--------EMVkLLLNKGANLSA-SDKKDRQPIHWAAYLGHLE 187
Cdd:cd22194 203 IVQLLMEKESTdITSQDSRGNTVLHAlvtvAEDSKTQndfvkrmyDMI-LLKSENKNLETiRNNEGLTPLQLAAKMGKAE 281
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66392221 188 VVKLLVSQgsDKSCKDKRGYTPLHAAAASGHVDVVKYLLrNGAEIDEPnafgNTALHVACY 248
Cdd:cd22194 282 ILKYILSR--EIKEKPNRSLSRKFTDWAYGPVSSSLYDL-TNVDTTTD----NSVLEIIVY 335
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
681-713 |
1.86e-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: 1.86e-04
10 20 30
....*....|....*....|....*....|....
gi 66392221 681 EGQTPLMLAVL-GGHTDCVHLLLERGACPDMKDR 713
Cdd:pfam00023 1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
423-537 |
1.96e-04 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).
Pssm-ID: 411975 [Multi-domain] Cd Length: 600 Bit Score: 45.26 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 423 GRTCLHAAA---SGGNIECLNLLLSSGADMNKKDKF-----------GRTPLHYAAANGRYQCVVVLVGAGAEVNER--- 485
Cdd:cd21882 26 GKTCLHKAAlnlNDGVNEAIMLLLEAAPDSGNPKELvnapctdefyqGQTALHIAIENRNLNLVRLLVENGADVSARatg 105
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 66392221 486 ---DRSGCTPLHYSAASTAFCrtdrphASThqNQEDgekesflCVEHLLDNGADP 537
Cdd:cd21882 106 rffRKSPGNLFYFGELPLSLA------ACT--NQEE-------IVRLLLENGAQP 145
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
423-454 |
2.40e-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: 39.19 E-value: 2.40e-04
10 20 30
....*....|....*....|....*....|...
gi 66392221 423 GRTCLHAAA-SGGNIECLNLLLSSGADMNKKDK 454
Cdd:pfam00023 2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
42-72 |
2.52e-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: 39.19 E-value: 2.52e-04
10 20 30
....*....|....*....|....*....|..
gi 66392221 42 RTPLHAAAW-LGDVHIMDLLISAGANVNAKDH 72
Cdd:pfam00023 3 NTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
827-915 |
2.60e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 44.89 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 827 NGHSGSAELLLESSV-CNSlvniRDAKGRTPLHAAAVAEDVAGLQLVLRQGADIDAVDHSGRSALMVAADYGQSGAVALL 905
Cdd:PTZ00322 92 SGDAVGARILLTGGAdPNC----RDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
|
90
....*....|
gi 66392221 906 LHRAKADLSL 915
Cdd:PTZ00322 168 SRHSQCHFEL 177
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
214-314 |
2.76e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 44.89 E-value: 2.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 214 AASGHVDVVKYLLRNGAEIDEPNAFGNTALHVACYTGQEAVANELVNRGANVNQPNHRGYTPLHLAAVSTNGALcLELLV 293
Cdd:PTZ00322 90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREV-VQLLS 168
|
90 100 110
....*....|....*....|....*....|....
gi 66392221 294 -------NNGADVNMQSKEGK------SPLHMAA 314
Cdd:PTZ00322 169 rhsqchfELGANAKPDSFTGKppsledSPISSHH 202
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
265-426 |
3.05e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 43.27 E-value: 3.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 265 VNQPNHRGYTPLHLAAVSTNGAL-CLELLVNNGADVNMQSK-EGKSPLHMAAIHGRFTRS---QILIQNGGEIDCVDRYG 339
Cdd:PHA02859 44 VNDCNDLYETPIFSCLEKDKVNVeILKFLIENGADVNFKTRdNNLSALHHYLSFNKNVEPeilKILIDSGSSITEEDEDG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 340 NTPLHVaakYGHEL-----LISTLMTNGADTARQGIHGMFPLHLAVLYGSSDccrkllssgqlySIVlsmskEHVLSAGF 414
Cdd:PHA02859 124 KNLLHM---YMCNFnvrinVIKLLIDSGVSFLNKDFDNNNILYSYILFHSDK------------KIF-----DFLTSLGI 183
|
170
....*....|..
gi 66392221 415 DINTPDNFGRTC 426
Cdd:PHA02859 184 DINETNKSGYNC 195
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
547-691 |
3.91e-04 |
|
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: 44.69 E-value: 3.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 547 AVHYAAAHGNKQNLELLLEMCFNTlgdkESNGsISPLHLAVESGHWECVTVLIESGVCVDVcdpvgrsvlylasqRGHsr 626
Cdd:TIGR00870 101 LLHLLAAFRKSGPLELANDQYTSE----FTPG-ITALHLAAHRQNYEIVKLLLERGASVPA--------------RAC-- 159
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66392221 627 CVELLLSQSASCL-LAEHrskwgPLHVAAANGHSECLRMLlcSEGGADlVNVTDAEGQTPLMLAVL 691
Cdd:TIGR00870 160 GDFFVKSQGVDSFyHGES-----PLNAAACLGSPSIVALL--SEDPAD-ILTADSLGNTLLHLLVM 217
|
|
| PHA02791 |
PHA02791 |
ankyrin-like protein; Provisional |
99-247 |
3.92e-04 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165154 [Multi-domain] Cd Length: 284 Bit Score: 43.49 E-value: 3.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 99 DVTARDKYWQTPLHIAAANRATRCVETLLPHVSSLNMADrtGRAPLHHAAQSGYQEMVKLLLNKGANLSASDKKDRQPIH 178
Cdd:PHA02791 22 DAFKADVHGHSALYYAIADNNVRLVCTLLNAGALKNLLE--NEFPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALY 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 179 WAAYLGHLEVVKLLVSQGSDKSCKDKRGY-TPLHAAAASGHVDVVKYLLrngAEIdePNAFgNTALHVAC 247
Cdd:PHA02791 100 YAVDSGNMQTVKLFVKKNWRLMFYGKTGWkTSFYHAVMLNDVSIVSYFL---SEI--PSTF-DLAILLSC 163
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
853-906 |
4.18e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 39.18 E-value: 4.18e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 66392221 853 GRTPLHAAAVAEDVAGLQLVLRQGADIDAVDHSGRSALMVAADYGQSGAVALLL 906
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02743 |
PHA02743 |
Viral ankyrin protein; Provisional |
233-363 |
4.70e-04 |
|
Viral ankyrin protein; Provisional
Pssm-ID: 222925 [Multi-domain] Cd Length: 166 Bit Score: 42.11 E-value: 4.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 233 DEPNAFgntalHVACYTGQeavANELV-------NRGANVNQPNHRGYTPLHLAAV--STNGALCLELLVNNGADVNM-Q 302
Cdd:PHA02743 19 DEQNTF-----LRICRTGN---IYELMevapfisGDGHLLHRYDHHGRQCTHMVAWydRANAVMKIELLVNMGADINArE 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66392221 303 SKEGKSPLHMAAIHGRFTRSQILIQN-GGEIDCVDRYGNTPLHVAAKYGHELLISTLMTNGA 363
Cdd:PHA02743 91 LGTGNTLLHIAASTKNYELAEWLCRQlGVNLGAINYQHETAYHIAYKMRDRRMMEILRANGA 152
|
|
| TRPV1 |
cd22196 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ... |
270-344 |
5.35e-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: 44.03 E-value: 5.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 270 HRGYTPLHLAAVSTNGALcLELLVNNGADVNM--------QSKE------GKSPLHMAAIHGRFTRSQILIQN---GGEI 332
Cdd:cd22196 92 YKGQTALHIAIERRNMHL-VELLVQNGADVHArasgeffkKKKGgpgfyfGELPLSLAACTNQLDIVKFLLENphsPADI 170
|
90
....*....|..
gi 66392221 333 DCVDRYGNTPLH 344
Cdd:cd22196 171 SARDSMGNTVLH 182
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
225-279 |
5.56e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 38.87 E-value: 5.56e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 66392221 225 LLRNG-AEIDEPNAFGNTALHVACYTGQEAVANELVNRGANVNQPNHRGYTPLHLA 279
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
239-293 |
5.61e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 38.79 E-value: 5.61e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 66392221 239 GNTALHVACYTGQEAVANELVNRGANVNQPNHRGYTPLHLAAVSTNGAlCLELLV 293
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVE-VLKLLL 54
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
9-173 |
6.46e-04 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 43.70 E-value: 6.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 9 QPPLVQAIFNRNADEV---KLFLHKKDEVNALD---------QERRTPLHAA-----AWLGDVHIMDLLISAGANVNAKD 71
Cdd:PLN03192 476 TSTLIEAMQTRQEDNVvilKNFLQHHKELHDLNvgdllgdngGEHDDPNMASnlltvASTGNAALLEELLKAKLDPDIGD 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 72 HVWLTPLHRAAASRNERAVGLLLRKGADVTARDKYWQTPL----------------HIAAANR-----------ATR--- 121
Cdd:PLN03192 556 SKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnaisakhhkifrilyHFASISDphaagdllctaAKRndl 635
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 66392221 122 -CVETLLPHVSSLNMADRTGRAPLHHAAQSGYQEMVKLLLNKGANLSASDKKD 173
Cdd:PLN03192 636 tAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDD 688
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
239-266 |
6.83e-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: 37.95 E-value: 6.83e-04
10 20
....*....|....*....|....*...
gi 66392221 239 GNTALHVACYTGQEAVANELVNRGANVN 266
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
258-444 |
7.44e-04 |
|
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: 43.59 E-value: 7.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 258 LVNrgANVNQPNHRGYTPLHLAAVSTNGALcLELLVNNGADVNMQSKegksplhmaaihGRFtrsqilIQNGGEIDCVdR 337
Cdd:cd22194 129 FIN--AEYTEEAYEGQTALNIAIERRQGDI-VKLLIAKGADVNAHAK------------GVF------FNPKYKHEGF-Y 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 338 YGNTPLHVAAKYGHELLISTLMTNGADT-ARQGIHGMFPLHlAVLYGSSDCCRKLLSSGQLYSIVLSMSKEHVLSAgfdi 416
Cdd:cd22194 187 FGETPLALAACTNQPEIVQLLMEKESTDiTSQDSRGNTVLH-ALVTVAEDSKTQNDFVKRMYDMILLKSENKNLET---- 261
|
170 180
....*....|....*....|....*...
gi 66392221 417 nTPDNFGRTCLHAAASGGNIECLNLLLS 444
Cdd:cd22194 262 -IRNNEGLTPLQLAAKMGKAEILKYILS 288
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
687-769 |
8.22e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 43.35 E-value: 8.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 687 MLAV----LGGHTDCV--HLLLERGACPDMKDRRGRTALHRGAVMGREDCLTALLSHNVSVLSRDFQGRSALHLAASCGH 760
Cdd:PTZ00322 81 MLTVelcqLAASGDAVgaRILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGF 160
|
....*....
gi 66392221 761 ADILSNLLS 769
Cdd:PTZ00322 161 REVVQLLSR 169
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
456-484 |
8.47e-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: 37.57 E-value: 8.47e-04
10 20
....*....|....*....|....*....
gi 66392221 456 GRTPLHYAAANGRYQCVVVLVGAGAEVNE 484
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
232-344 |
8.93e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 41.73 E-value: 8.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 232 IDEPNAFGNTALHvACYTgQEAVANE----LVNRGANVN-QPNHRGYTPLHlAAVSTNGAL---CLELLVNNGADVNMQS 303
Cdd:PHA02859 44 VNDCNDLYETPIF-SCLE-KDKVNVEilkfLIENGADVNfKTRDNNLSALH-HYLSFNKNVepeILKILIDSGSSITEED 120
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 66392221 304 KEGKSPLH--MAAIHGRFTRSQILIQNGGEIDCVDRYGNTPLH 344
Cdd:PHA02859 121 EDGKNLLHmyMCNFNVRINVIKLLIDSGVSFLNKDFDNNNILY 163
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
140-171 |
9.30e-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: 37.65 E-value: 9.30e-04
10 20 30
....*....|....*....|....*....|...
gi 66392221 140 GRAPLHHAA-QSGYQEMVKLLLNKGANLSASDK 171
Cdd:pfam00023 2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
|
|
| TRPV1-4 |
cd22193 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ... |
270-344 |
9.73e-04 |
|
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: 43.25 E-value: 9.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 270 HRGYTPLHLAAVSTNGAlCLELLVNNGADVNMQSKE--------------GKSPLHMAAIHGRFTRSQILIQNG---GEI 332
Cdd:cd22193 74 YEGQTALHIAIERRQGD-IVALLVENGADVHAHAKGrffqpkyqgegfyfGELPLSLAACTNQPDIVQYLLENEhqpADI 152
|
90
....*....|..
gi 66392221 333 DCVDRYGNTPLH 344
Cdd:cd22193 153 EAQDSRGNTVLH 164
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
878-982 |
1.10e-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: 43.15 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 878 DIDAVDHSGRSALMVAADYGQSGAVA--LLLHRAKADLSlldvnkNTALHLACSKAHEMCAMLIL------KEIHNPILI 949
Cdd:TIGR00870 44 NINCPDRLGRSALFVAAIENENLELTelLLNLSCRGAVG------DTLLHAISLEYVDAVEAILLhllaafRKSGPLELA 117
|
90 100 110
....*....|....*....|....*....|....*..
gi 66392221 950 NA----TNSMLQMPLHIAARNGLATVVQALLNRGATV 982
Cdd:TIGR00870 118 NDqytsEFTPGITALHLAAHRQNYEIVKLLLERGASV 154
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
104-239 |
1.21e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 41.34 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 104 DKYWQTPLH--IAAANRATRCVETLLPHVSSLNMADR-TGRAPLHHAA---QSGYQEMVKLLLNKGANLSASDKKDRQPI 177
Cdd:PHA02859 48 NDLYETPIFscLEKDKVNVEILKFLIENGADVNFKTRdNNLSALHHYLsfnKNVEPEILKILIDSGSSITEEDEDGKNLL 127
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66392221 178 HwaAYLGH----LEVVKLLVSQGSDKSCKDKRGYTPLHAAAASgHVD--VVKYLLRNGAEIDEPNAFG 239
Cdd:PHA02859 128 H--MYMCNfnvrINVIKLLIDSGVSFLNKDFDNNNILYSYILF-HSDkkIFDFLTSLGIDINETNKSG 192
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
416-494 |
1.28e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 41.34 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 416 INTPDNFGRTCLHAAASG--GNIECLNLLLSSGADMNKKDK-FGRTPLHYAAA---NGRYQCVVVLVGAGAEVNERDRSG 489
Cdd:PHA02859 44 VNDCNDLYETPIFSCLEKdkVNVEILKFLIENGADVNFKTRdNNLSALHHYLSfnkNVEPEILKILIDSGSSITEEDEDG 123
|
....*
gi 66392221 490 CTPLH 494
Cdd:PHA02859 124 KNLLH 128
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
456-487 |
1.55e-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: 1.55e-03
10 20 30
....*....|....*....|....*....|...
gi 66392221 456 GRTPLHYAAA-NGRYQCVVVLVGAGAEVNERDR 487
Cdd:pfam00023 2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
|
|
| TRPV1-4 |
cd22193 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ... |
76-237 |
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 66392221 76 TPLHRAAASRNERAVGLLLRKGADVTARDK--------------YWQTPLHIAAANRATRCVETLL--PHV-SSLNMADR 138
Cdd:cd22193 78 TALHIAIERRQGDIVALLVENGADVHAHAKgrffqpkyqgegfyFGELPLSLAACTNQPDIVQYLLenEHQpADIEAQDS 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 139 TGRAPLH--------HAAQSGY-QEMVKLLLNKGANLSASDKkdrqpihwaaylghLEVVKllvsqgsdksckDKRGYTP 209
Cdd:cd22193 158 RGNTVLHalvtvadnTKENTKFvTRMYDMILIRGAKLCPTVE--------------LEEIR------------NNDGLTP 211
|
170 180
....*....|....*....|....*...
gi 66392221 210 LHAAAASGHVDVVKYLLRNgaEIDEPNA 237
Cdd:cd22193 212 LQLAAKMGKIEILKYILQR--EIKEPEL 237
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
748-805 |
1.76e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 37.64 E-value: 1.76e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 66392221 748 GRSALHLAASCGHADILSNLLSaadhSQPQDPLTDRHGYTPAHWAAYHGHEDCLEVLL 805
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLE----KGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
612-666 |
1.78e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 37.64 E-value: 1.78e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 66392221 612 GRSVLYLASQRGHSRCVELLLSQSASCLLAEhRSKWGPLHVAAANGHSECLRMLL 666
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVD-GNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02736 |
PHA02736 |
Viral ankyrin protein; Provisional |
423-470 |
1.90e-03 |
|
Viral ankyrin protein; Provisional
Pssm-ID: 165103 [Multi-domain] Cd Length: 154 Bit Score: 39.86 E-value: 1.90e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 66392221 423 GRTCLHAAASGGNI---ECLNLLLSSGADMNKKD-KFGRTPLHYAAANGRYQ 470
Cdd:PHA02736 55 GKQCVHIVSNPDKAdpqEKLKLLMEWGADINGKErVFGNTPLHIAVYTQNYE 106
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
546-772 |
1.93e-03 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 41.96 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 546 SAVHYAAAHG--NKQNLELLLEMcfntLGDKESNGSISPLH--LAVESGHWECVTVLIESGVCVDVCDPVGRSVLYLASQ 621
Cdd:PHA02946 6 SAEYYLSLYAkyNSKNLDVFRNM----LQAIEPSGNYHILHayCGIKGLDERFVEELLHRGYSPNETDDDGNYPLHIASK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 622 RGHSRCVELLLSQSASCLLAEHRSKwGPLHVAAANGHSECLRMLLCSEGGADLVNVTDAEGQTPLmLAVLGGHTDCVHLL 701
Cdd:PHA02946 82 INNNRIVAMLLTHGADPNACDKQHK-TPLYYLSGTDDEVIERINLLVQYGAKINNSVDEEGCGPL-LACTDPSERVFKKI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66392221 702 LERGACPDMKDRRGRTALHRGAVMG--REDCLTALLSHNVSVLSRDFQGRSALHLAAS--CGHADILSNLLSAAD 772
Cdd:PHA02946 160 MSIGFEARIVDKFGKNHIHRHLMSDnpKASTISWMMKLGISPSKPDHDGNTPLHIVCSktVKNVDIINLLLPSTD 234
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
649-689 |
2.06e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 37.33 E-value: 2.06e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 66392221 649 PLHVAAANGHSECLRMLLcsEGGADLvNVTDAEGQTPLMLA 689
Cdd:pfam13857 19 PLHVAAKYGALEIVRVLL--AYGVDL-NLKDEEGLTALDLA 56
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
520-564 |
2.10e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 37.25 E-value: 2.10e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 66392221 520 EKESFLCVEHLLDNGADPCLCNTKGYSAVHYAAAHGNKQNLELLL 564
Cdd:pfam13637 10 ASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02741 |
PHA02741 |
hypothetical protein; Provisional |
202-325 |
2.27e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 165108 [Multi-domain] Cd Length: 169 Bit Score: 40.03 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 202 KDKRGYTPLHAAAASGHVDVVK----YLLRN--GAEIDEPNAFGNTALHVACYTGQEAVANE----LVNRGANVN-QPNH 270
Cdd:PHA02741 17 KNSEGENFFHEAARCGCFDIIArftpFIRGDchAAALNATDDAGQMCIHIAAEKHEAQLAAEiidhLIELGADINaQEML 96
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 66392221 271 RGYTPLHLAAVSTNGALCLELLVNNGADVNMQSKEGKSPLHMAAIHGRFTRSQIL 325
Cdd:PHA02741 97 EGDTALHLAAHRRDHDLAEWLCCQPGIDLHFCNADNKSPFELAIDNEDVAMMQIL 151
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
681-710 |
2.57e-03 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 36.41 E-value: 2.57e-03
10 20 30
....*....|....*....|....*....|
gi 66392221 681 EGQTPLMLAVLGGHTDCVHLLLERGACPDM 710
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
682-769 |
2.67e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411978 [Multi-domain] Cd Length: 680 Bit Score: 41.67 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 682 GQTPLMLAVLGGHTDCVHLLLERGACP-DMKDRRGRTALHrGAVMGREDCLTA-----------LLSHNVSVLS--RDFQ 747
Cdd:cd22194 188 GETPLALAACTNQPEIVQLLMEKESTDiTSQDSRGNTVLH-ALVTVAEDSKTQndfvkrmydmiLLKSENKNLEtiRNNE 266
|
90 100
....*....|....*....|..
gi 66392221 748 GRSALHLAASCGHADILSNLLS 769
Cdd:cd22194 267 GLTPLQLAAKMGKAEILKYILS 288
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
140-168 |
2.68e-03 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 36.41 E-value: 2.68e-03
10 20
....*....|....*....|....*....
gi 66392221 140 GRAPLHHAAQSGYQEMVKLLLNKGANLSA 168
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
42-69 |
2.92e-03 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 36.03 E-value: 2.92e-03
10 20
....*....|....*....|....*...
gi 66392221 42 RTPLHAAAWLGDVHIMDLLISAGANVNA 69
Cdd:smart00248 3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
819-873 |
3.83e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 36.48 E-value: 3.83e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 66392221 819 TPLHCALINGHSGSAELLLESSVCnslVNIRDAKGRTPLHAAAVAEDVAGLQLVL 873
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGAD---INAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
957-992 |
4.52e-03 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 41.04 E-value: 4.52e-03
10 20 30
....*....|....*....|....*....|....*.
gi 66392221 957 QMPLHIAARNGLATVVQALLNRGATVLAVDEEGHTP 992
Cdd:PTZ00322 116 RTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTP 151
|
|
| PHA02736 |
PHA02736 |
Viral ankyrin protein; Provisional |
203-297 |
4.53e-03 |
|
Viral ankyrin protein; Provisional
Pssm-ID: 165103 [Multi-domain] Cd Length: 154 Bit Score: 39.09 E-value: 4.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 203 DKRGYTPLHAAAASGHVD---VVKYLLRNGAEID-EPNAFGNTALHVACYTGQEAVANELVNR-GANVNQPNHRGYTPLH 277
Cdd:PHA02736 52 NRHGKQCVHIVSNPDKADpqeKLKLLMEWGADINgKERVFGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYY 131
|
90 100
....*....|....*....|
gi 66392221 278 LAAvSTNGALCLELLVNNGA 297
Cdd:PHA02736 132 VAC-ERHDAKMMNILRAKGA 150
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
846-992 |
4.60e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 40.72 E-value: 4.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 846 VNIRDAKGRTPLHAAAVAEDVAGLQLVLRQGADIDAVDHSGRSALMVAADYGQSGAVALLLHRAkADLSLL---DVNKNT 922
Cdd:PHA02874 28 INISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG-VDTSILpipCIEKDM 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 923 alhlacskahemcamlILKEIHNPILINATNSMLQMPLHIAARNGLATVVQALLNRGATVLAVDEEGHTP 992
Cdd:PHA02874 107 ----------------IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYP 160
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
852-978 |
4.81e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411978 [Multi-domain] Cd Length: 680 Bit Score: 40.90 E-value: 4.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 852 KGRTPLHAAAVAEDVAGLQLVLRQGADIDAVD--------------HSGRSALMVAADYGQSGAVALLLHRAKADLSLLD 917
Cdd:cd22194 140 EGQTALNIAIERRQGDIVKLLIAKGADVNAHAkgvffnpkykhegfYFGETPLALAACTNQPEIVQLLMEKESTDITSQD 219
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 918 VNKNTALHLACSKAHEMCAML-ILKEIHNPILINATNSMLQ--------MPLHIAARNGLATVVQALLNR 978
Cdd:cd22194 220 SRGNTVLHALVTVAEDSKTQNdFVKRMYDMILLKSENKNLEtirnneglTPLQLAAKMGKAEILKYILSR 289
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
239-270 |
4.91e-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: 4.91e-03
10 20 30
....*....|....*....|....*....|...
gi 66392221 239 GNTALHVACY-TGQEAVANELVNRGANVNQPNH 270
Cdd:pfam00023 2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
43-160 |
5.19e-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: 40.83 E-value: 5.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 43 TPLHAAAWLGDVHIMDLLISAGANVNAK---------DHVWL-----TPLHRAAASRNERAVGLLLRKGADVTARDKYWQ 108
Cdd:TIGR00870 130 TALHLAAHRQNYEIVKLLLERGASVPARacgdffvksQGVDSfyhgeSPLNAAACLGSPSIVALLSEDPADILTADSLGN 209
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66392221 109 TPLHIA-------AANRATRC-----VETLLPHVSSLN----MADRTGRAPLHHAAQSGYQEMVKLLL 160
Cdd:TIGR00870 210 TLLHLLvmenefkAEYEELSCqmynfALSLLDKLRDSKelevILNHQGLTPLKLAAKEGRIVLFRLKL 277
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
24-95 |
5.32e-03 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 40.65 E-value: 5.32e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66392221 24 VKLFLHKKDEVNALDQERRTPLHAAAWLGDVHIMDLLISAGANVNAKDHVWLTPLHRAAASRNERAVGLLLR 95
Cdd:PTZ00322 98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
960-1013 |
5.62e-03 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 37.02 E-value: 5.62e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 66392221 960 LHIAARNGLATVVQALLNRGATVLAVDEEGHTPALACASNKaVADCLALILSTM 1013
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNG-HLEIVKLLLEHA 53
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
921-976 |
6.59e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 35.71 E-value: 6.59e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 66392221 921 NTALHLACSKAHEMCAMLILKeihNPILINATNSMLQMPLHIAARNGLATVVQALL 976
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLE---KGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
784-809 |
6.62e-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: 6.62e-03
10 20
....*....|....*....|....*.
gi 66392221 784 HGYTPAHWAAYHGHEDCLEVLLELKP 809
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
10-61 |
7.13e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 35.71 E-value: 7.13e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 66392221 10 PPLVQAIFNRNADEVKLFLHKKDEVNALDQERRTPLHAAAWLGDVHIMDLLI 61
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
781-927 |
7.48e-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: 40.45 E-value: 7.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 781 TDRHGYTPAHWAAYHGHEDCLEVLLELKPCSIQEGNpfTPLHCALINGHSGSAELLL------ESSVCNSLVNIRDA--- 851
Cdd:TIGR00870 48 PDRLGRSALFVAAIENENLELTELLLNLSCRGAVGD--TLLHAISLEYVDAVEAILLhllaafRKSGPLELANDQYTsef 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392221 852 -KGRTPLHAAAVAEDVAGLQLVLRQGADIDA-------VDHS-------GRSALMVAADYGQSGAVALLLhRAKADLSLL 916
Cdd:TIGR00870 126 tPGITALHLAAHRQNYEIVKLLLERGASVPAracgdffVKSQgvdsfyhGESPLNAAACLGSPSIVALLS-EDPADILTA 204
|
170
....*....|.
gi 66392221 917 DVNKNTALHLA 927
Cdd:TIGR00870 205 DSLGNTLLHLL 215
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
338-364 |
7.59e-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: 7.59e-03
10 20
....*....|....*....|....*..
gi 66392221 338 YGNTPLHVAAKYGHELLISTLMTNGAD 364
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
530-604 |
8.14e-03 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 40.27 E-value: 8.14e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66392221 530 LLDNGADPCLCNTKGYSAVHYAAAHGNKQNLELLLEMCFN-TLGDKESNgsiSPLHLAVESGHWECVTVLIESGVC 604
Cdd:PTZ00322 101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADpTLLDKDGK---TPLELAEENGFREVVQLLSRHSQC 173
|
|
|